path: root/plip/test/pdb/1xdn.pdb

HEADER    LIGASE                                  07-SEP-04   1XDN              
TITLE     HIGH RESOLUTION CRYSTAL STRUCTURE OF AN EDITOSOME ENZYME FROM         
TITLE    2 TRYPANOSOMA BRUCEI: RNA EDITING LIGASE 1                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RNA EDITING LIGASE MP52;                                   
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: ADENYLATION DOMAIN;                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: TRYPANOSOMA BRUCEI;                             
SOURCE   3 ORGANISM_TAXID: 5691;                                                
SOURCE   4 GENE: MP52;                                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21GOLD DE3;                              
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PSKB3                                     
KEYWDS    RNA EDITING, LIGASE, TRYPANOSOMA BRUCEI,                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.DENG,A.SCHNAUFER,R.SALAVATI,K.D.STUART,W.G.HOL                      
REVDAT   3   10-SEP-14 1XDN    1       JRNL   VERSN                             
REVDAT   2   24-FEB-09 1XDN    1       VERSN                                    
REVDAT   1   07-DEC-04 1XDN    0                                                
JRNL        AUTH   J.DENG,A.SCHNAUFER,R.SALAVATI,K.D.STUART,W.G.HOL             
JRNL        TITL   HIGH RESOLUTION CRYSTAL STRUCTURE OF A KEY EDITOSOME ENZYME  
JRNL        TITL 2 FROM TRYPANOSOMA BRUCEI: RNA EDITING LIGASE 1.               
JRNL        REF    J.MOL.BIOL.                   V. 343   601 2004              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   15465048                                                     
JRNL        DOI    10.1016/J.JMB.2004.08.041                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1.24                                        
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 78835                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.129                           
REMARK   3   R VALUE            (WORKING SET) : 0.128                           
REMARK   3   FREE R VALUE                     : 0.148                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4149                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.23                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4798                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1170                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 260                          
REMARK   3   BIN FREE R VALUE                    : 0.1310                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2119                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 32                                      
REMARK   3   SOLVENT ATOMS            : 440                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 7.29                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 9.40                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.22000                                             
REMARK   3    B22 (A**2) : -0.02000                                             
REMARK   3    B33 (A**2) : 0.28000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.12000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.034         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.033         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.017         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.349         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.975                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.972                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2206 ; 0.010 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  1976 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2993 ; 1.420 ; 1.978       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  4606 ; 0.784 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   264 ; 5.763 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   320 ; 0.084 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2428 ; 0.011 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   457 ; 0.017 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   423 ; 0.220 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  2349 ; 0.250 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  1304 ; 0.084 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   304 ; 0.169 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    11 ; 0.119 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    38 ; 0.217 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    36 ; 0.177 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1319 ; 1.192 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2128 ; 1.915 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   887 ; 2.829 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   865 ; 4.258 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 1XDN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-SEP-04.                  
REMARK 100 THE RCSB ID CODE IS RCSB030242.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-DEC-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97885, 0.97899, 0.96112          
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 95711                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 86.8                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.06400                            
REMARK 200  R SYM                      (I) : 0.06400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 33.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 86.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.06400                            
REMARK 200  R SYM FOR SHELL            (I) : 0.06400                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 33.800                             
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.80                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 3350, MAGNESIUM CHLORIDE, TRIS,      
REMARK 280  ATP, PH 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       29.28950            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    48                                                      
REMARK 465     HIS A    49                                                      
REMARK 465     MET A    50                                                      
REMARK 465     ASP A    51                                                      
REMARK 465     LYS A   317                                                      
REMARK 465     HIS A   318                                                      
REMARK 465     PRO A   319                                                      
REMARK 465     GLY A   320                                                      
REMARK 465     LYS A   321                                                      
REMARK 465     GLN A   322                                                      
REMARK 465     LYS A   323                                                      
REMARK 465     GLU A   324                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     GLU A  278   CD   OE1  OE2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OE1  GLU A   278     O    HOH A   677              2.08            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    TYR A 165       96.21   -160.96                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 502  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ATP A 501   O1G                                                    
REMARK 620 2 ATP A 501   O2B  86.6                                              
REMARK 620 3 HOH A 528   O   177.6  94.7                                        
REMARK 620 4 HOH A 514   O    89.5 173.3  89.4                                  
REMARK 620 5 HOH A 530   O    90.8  95.6  87.1  89.9                            
REMARK 620 6 HOH A 520   O    96.9  90.2  85.1  84.9 170.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP A 501                 
DBREF  1XDN A   51   324  GB     11067037 AAG27062        51    324             
SEQADV 1XDN GLY A   48  GB   11067037            CLONING ARTIFACT               
SEQADV 1XDN HIS A   49  GB   11067037            CLONING ARTIFACT               
SEQADV 1XDN MET A   50  GB   11067037            CLONING ARTIFACT               
SEQADV 1XDN MSE A  115  GB   11067037  MET   115 MODIFIED RESIDUE               
SEQADV 1XDN MSE A  263  GB   11067037  MET   263 MODIFIED RESIDUE               
SEQADV 1XDN MSE A  314  GB   11067037  MET   314 MODIFIED RESIDUE               
SEQRES   1 A  277  GLY HIS MET ASP GLN SER ASP PHE SER PRO TYR ILE GLU          
SEQRES   2 A  277  ILE ASP LEU PRO SER GLU SER ARG ILE GLN SER LEU HIS          
SEQRES   3 A  277  LYS SER GLY LEU ALA ALA GLN GLU TRP VAL ALA CYS GLU          
SEQRES   4 A  277  LYS VAL HIS GLY THR ASN PHE GLY ILE TYR LEU ILE ASN          
SEQRES   5 A  277  GLN GLY ASP HIS GLU VAL VAL ARG PHE ALA LYS ARG SER          
SEQRES   6 A  277  GLY ILE MSE ASP PRO ASN GLU ASN PHE PHE GLY TYR HIS          
SEQRES   7 A  277  ILE LEU ILE ASP GLU PHE THR ALA GLN ILE ARG ILE LEU          
SEQRES   8 A  277  ASN ASP LEU LEU LYS GLN LYS TYR GLY LEU SER ARG VAL          
SEQRES   9 A  277  GLY ARG LEU VAL LEU ASN GLY GLU LEU PHE GLY ALA LYS          
SEQRES  10 A  277  TYR LYS HIS PRO LEU VAL PRO LYS SER GLU LYS TRP CYS          
SEQRES  11 A  277  THR LEU PRO ASN GLY LYS LYS PHE PRO ILE ALA GLY VAL          
SEQRES  12 A  277  GLN ILE GLN ARG GLU PRO PHE PRO GLN TYR SER PRO GLU          
SEQRES  13 A  277  LEU HIS PHE PHE ALA PHE ASP ILE LYS TYR SER VAL SER          
SEQRES  14 A  277  GLY ALA GLU GLU ASP PHE VAL LEU LEU GLY TYR ASP GLU          
SEQRES  15 A  277  PHE VAL GLU PHE SER SER LYS VAL PRO ASN LEU LEU TYR          
SEQRES  16 A  277  ALA ARG ALA LEU VAL ARG GLY THR LEU ASP GLU CYS LEU          
SEQRES  17 A  277  ALA PHE ASP VAL GLU ASN PHE MSE THR PRO LEU PRO ALA          
SEQRES  18 A  277  LEU LEU GLY LEU GLY ASN TYR PRO LEU GLU GLY ASN LEU          
SEQRES  19 A  277  ALA GLU GLY VAL VAL ILE ARG HIS VAL ARG ARG GLY ASP          
SEQRES  20 A  277  PRO ALA VAL GLU LYS HIS ASN VAL SER THR ILE ILE LYS          
SEQRES  21 A  277  LEU ARG CYS SER SER PHE MSE GLU LEU LYS HIS PRO GLY          
SEQRES  22 A  277  LYS GLN LYS GLU                                              
MODRES 1XDN MSE A  115  MET  SELENOMETHIONINE                                   
MODRES 1XDN MSE A  263  MET  SELENOMETHIONINE                                   
MODRES 1XDN MSE A  314  MET  SELENOMETHIONINE                                   
HET    MSE  A 115       8                                                       
HET    MSE  A 263       8                                                       
HET    MSE  A 314      10                                                       
HET     MG  A 502       1                                                       
HET    ATP  A 501      31                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     ATP ADENOSINE-5'-TRIPHOSPHATE                                        
FORMUL   1  MSE    3(C5 H11 N O2 SE)                                            
FORMUL   2   MG    MG 2+                                                        
FORMUL   3  ATP    C10 H16 N5 O13 P3                                            
FORMUL   4  HOH   *440(H2 O)                                                    
HELIX    1   1 SER A   65  SER A   75  1                                  11    
HELIX    2   2 GLY A   76  GLN A   80  5                                   5    
HELIX    3   3 GLY A  123  ILE A  126  5                                   4    
HELIX    4   4 LEU A  127  GLY A  147  1                                  21    
HELIX    5   5 ALA A  188  VAL A  190  5                                   3    
HELIX    6   6 ALA A  218  GLU A  220  5                                   3    
HELIX    7   7 GLY A  226  LYS A  236  1                                  11    
HELIX    8   8 THR A  250  ALA A  256  1                                   7    
HELIX    9   9 ASP A  258  PHE A  262  5                                   5    
HELIX   10  10 PRO A  265  LEU A  270  1                                   6    
HELIX   11  11 ASP A  294  LYS A  299  1                                   6    
HELIX   12  12 CYS A  310  LEU A  316  1                                   7    
SHEET    1   A 4 VAL A 247  GLY A 249  0                                        
SHEET    2   A 4 TRP A  82  LYS A  87 -1  N  TRP A  82   O  GLY A 249           
SHEET    3   A 4 GLY A 284  HIS A 289 -1  O  VAL A 286   N  CYS A  85           
SHEET    4   A 4 ILE A 305  ARG A 309 -1  O  ILE A 306   N  ILE A 287           
SHEET    1   B 6 GLY A 113  ILE A 114  0                                        
SHEET    2   B 6 HIS A 103  LYS A 110 -1  N  LYS A 110   O  GLY A 113           
SHEET    3   B 6 THR A  91  GLN A 100 -1  N  GLN A 100   O  HIS A 103           
SHEET    4   B 6 ARG A 153  LYS A 164 -1  O  LEU A 160   N  THR A  91           
SHEET    5   B 6 SER A 201  SER A 214 -1  O  LYS A 212   N  VAL A 155           
SHEET    6   B 6 PHE A 222  LEU A 224 -1  O  VAL A 223   N  TYR A 213           
SHEET    1   C 6 GLY A 113  ILE A 114  0                                        
SHEET    2   C 6 HIS A 103  LYS A 110 -1  N  LYS A 110   O  GLY A 113           
SHEET    3   C 6 THR A  91  GLN A 100 -1  N  GLN A 100   O  HIS A 103           
SHEET    4   C 6 ARG A 153  LYS A 164 -1  O  LEU A 160   N  THR A  91           
SHEET    5   C 6 SER A 201  SER A 214 -1  O  LYS A 212   N  VAL A 155           
SHEET    6   C 6 LEU A 241  TYR A 242  1  O  LEU A 241   N  ALA A 208           
SHEET    1   D 2 TRP A 176  THR A 178  0                                        
SHEET    2   D 2 LYS A 184  PRO A 186 -1  O  PHE A 185   N  CYS A 177           
LINK         C   ILE A 114                 N   MSE A 115     1555   1555  1.33  
LINK         C   MSE A 115                 N   ASP A 116     1555   1555  1.33  
LINK         C   PHE A 262                 N   MSE A 263     1555   1555  1.33  
LINK         C   MSE A 263                 N   THR A 264     1555   1555  1.32  
LINK         C   PHE A 313                 N   MSE A 314     1555   1555  1.33  
LINK         C   MSE A 314                 N   GLU A 315     1555   1555  1.33  
LINK        MG    MG A 502                 O1G ATP A 501     1555   1555  2.09  
LINK        MG    MG A 502                 O2B ATP A 501     1555   1555  2.06  
LINK        MG    MG A 502                 O   HOH A 528     1555   1555  2.13  
LINK        MG    MG A 502                 O   HOH A 514     1555   1555  2.07  
LINK        MG    MG A 502                 O   HOH A 530     1555   1555  2.04  
LINK        MG    MG A 502                 O   HOH A 520     1555   1555  2.11  
CISPEP   1 PHE A  197    PRO A  198          0        -7.28                     
SITE     1 AC1  5 ATP A 501  HOH A 514  HOH A 520  HOH A 528                    
SITE     2 AC1  5 HOH A 530                                                     
SITE     1 AC2 27 TYR A  58  ILE A  59  GLU A  60  ILE A  61                    
SITE     2 AC2 27 GLU A  86  LYS A  87  VAL A  88  ASN A  92                    
SITE     3 AC2 27 ARG A 111  GLU A 159  PHE A 209  VAL A 286                    
SITE     4 AC2 27 LYS A 307  ARG A 309   MG A 502  HOH A 514                    
SITE     5 AC2 27 HOH A 520  HOH A 528  HOH A 530  HOH A 536                    
SITE     6 AC2 27 HOH A 587  HOH A 634  HOH A 650  HOH A 777                    
SITE     7 AC2 27 HOH A 829  HOH A 871  HOH A 886                               
CRYST1   44.911   58.579   52.984  90.00 100.23  90.00 P 1 21 1      2          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.022266  0.000000  0.004018        0.00000                         
SCALE2      0.000000  0.017071  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.019179        0.00000                         
ATOM      1  N   GLN A  52      42.237  16.800  35.823  1.00 12.04           N  
ANISOU    1  N   GLN A  52     1764   1519   1290    -51     85      8       N  
ATOM      2  CA  GLN A  52      41.667  17.015  34.477  1.00 10.21           C  
ANISOU    2  CA  GLN A  52     1684   1030   1163     45     63    174       C  
ATOM      3  C   GLN A  52      40.148  17.010  34.446  1.00 10.33           C  
ANISOU    3  C   GLN A  52     1788   1017   1117    104    129    163       C  
ATOM      4  O   GLN A  52      39.564  17.006  33.382  1.00  9.88           O  
ANISOU    4  O   GLN A  52     1826    876   1049    292    181    182       O  
ATOM      5  CB  GLN A  52      42.228  15.967  33.522  1.00  9.36           C  
ANISOU    5  CB  GLN A  52     1554    833   1170     72     15    146       C  
ATOM      6  CG  GLN A  52      43.734  16.095  33.352  1.00  9.40           C  
ANISOU    6  CG  GLN A  52     1581    771   1218     86   -200    237       C  
ATOM      7  CD  GLN A  52      44.170  17.346  32.622  1.00  8.47           C  
ANISOU    7  CD  GLN A  52     1399    689   1130     22   -142    158       C  
ATOM      8  OE1 GLN A  52      45.312  17.791  32.785  1.00 12.47           O  
ANISOU    8  OE1 GLN A  52     1745   1079   1911    -88   -491    288       O  
ATOM      9  NE2 GLN A  52      43.296  17.915  31.849  1.00  8.79           N  
ANISOU    9  NE2 GLN A  52     1234   1041   1063     15    -69    506       N  
ATOM     10  N   SER A  53      39.488  17.025  35.604  1.00 11.01           N  
ANISOU   10  N   SER A  53     1803   1212   1166    179    187    226       N  
ATOM     11  CA  SER A  53      38.026  16.949  35.611  1.00 12.75           C  
ANISOU   11  CA  SER A  53     1863   1569   1413    117    173    171       C  
ATOM     12  C   SER A  53      37.340  18.091  34.862  1.00 12.38           C  
ANISOU   12  C   SER A  53     1797   1573   1333    176    171    119       C  
ATOM     13  O   SER A  53      36.209  17.937  34.426  1.00 14.69           O  
ANISOU   13  O   SER A  53     2013   1898   1670    142    240    202       O  
ATOM     14  CB  SER A  53      37.462  16.890  37.026  1.00 13.59           C  
ANISOU   14  CB  SER A  53     1919   1711   1532    147    222    282       C  
ATOM     15  OG  SER A  53      37.854  18.006  37.781  1.00 17.90           O  
ANISOU   15  OG  SER A  53     2616   2299   1887    226    311    383       O  
ATOM     16  N   ASP A  54      38.012  19.228  34.730  1.00 11.65           N  
ANISOU   16  N   ASP A  54     1724   1454   1246    264    152    134       N  
ATOM     17  CA  ASP A  54      37.455  20.341  33.968  1.00 11.85           C  
ANISOU   17  CA  ASP A  54     1767   1455   1278    249    117    178       C  
ATOM     18  C   ASP A  54      37.742  20.271  32.474  1.00 10.23           C  
ANISOU   18  C   ASP A  54     1562   1275   1050    292    187    237       C  
ATOM     19  O   ASP A  54      37.168  21.045  31.722  1.00 11.10           O  
ANISOU   19  O   ASP A  54     1719   1326   1173    448    195    446       O  
ATOM     20  CB  ASP A  54      37.947  21.667  34.531  1.00 13.04           C  
ANISOU   20  CB  ASP A  54     1995   1543   1413    294     64    201       C  
ATOM     21  CG  ASP A  54      37.464  21.907  35.937  1.00 16.08           C  
ANISOU   21  CG  ASP A  54     2341   1811   1956    415     -6    115       C  
ATOM     22  OD1 ASP A  54      36.280  21.638  36.211  1.00 19.99           O  
ANISOU   22  OD1 ASP A  54     3244   2206   2145    740    396    -50       O  
ATOM     23  OD2 ASP A  54      38.207  22.360  36.811  1.00 21.76           O  
ANISOU   23  OD2 ASP A  54     3388   2268   2612    735      2   -249       O  
ATOM     24  N   PHE A  55      38.617  19.367  32.044  1.00  9.13           N  
ANISOU   24  N   PHE A  55     1451   1102    915    233    164    264       N  
ATOM     25  CA  PHE A  55      38.972  19.219  30.642  1.00  8.35           C  
ANISOU   25  CA  PHE A  55     1276    990    906    119    108    255       C  
ATOM     26  C   PHE A  55      37.915  18.485  29.848  1.00  8.87           C  
ANISOU   26  C   PHE A  55     1313    994   1061     61    120    286       C  
ATOM     27  O   PHE A  55      37.392  17.475  30.303  1.00 10.67           O  
ANISOU   27  O   PHE A  55     1623   1170   1260   -158    142    415       O  
ATOM     28  CB  PHE A  55      40.300  18.470  30.543  1.00  8.52           C  
ANISOU   28  CB  PHE A  55     1252   1126    858    129     47    237       C  
ATOM     29  CG  PHE A  55      40.730  18.127  29.138  1.00  7.26           C  
ANISOU   29  CG  PHE A  55     1080    883    793    155     55    228       C  
ATOM     30  CD1 PHE A  55      41.050  19.110  28.229  1.00  7.47           C  
ANISOU   30  CD1 PHE A  55     1050    928    859    -63    -52    233       C  
ATOM     31  CD2 PHE A  55      40.847  16.803  28.753  1.00  8.45           C  
ANISOU   31  CD2 PHE A  55     1262    862   1085     80    -70    130       C  
ATOM     32  CE1 PHE A  55      41.470  18.763  26.957  1.00  8.40           C  
ANISOU   32  CE1 PHE A  55     1229   1056    906    -61     20    249       C  
ATOM     33  CE2 PHE A  55      41.266  16.455  27.495  1.00  8.90           C  
ANISOU   33  CE2 PHE A  55     1324    977   1079     50    -63    -24       C  
ATOM     34  CZ  PHE A  55      41.584  17.426  26.589  1.00  9.37           C  
ANISOU   34  CZ  PHE A  55     1038   1362   1158    -23   -149     95       C  
ATOM     35  N   SER A  56      37.615  18.984  28.653  1.00  8.47           N  
ANISOU   35  N   SER A  56     1233    979   1006     32    116    228       N  
ATOM     36  CA  SER A  56      36.702  18.341  27.727  1.00  8.75           C  
ANISOU   36  CA  SER A  56     1231   1019   1072     38     57    197       C  
ATOM     37  C   SER A  56      37.409  18.135  26.390  1.00  8.22           C  
ANISOU   37  C   SER A  56     1168    944   1009     47     69    195       C  
ATOM     38  O   SER A  56      37.676  19.116  25.681  1.00  8.56           O  
ANISOU   38  O   SER A  56     1332    879   1041     91    107    301       O  
ATOM     39  CB  SER A  56      35.476  19.231  27.540  1.00  9.47           C  
ANISOU   39  CB  SER A  56     1297   1149   1149     85     42    121       C  
ATOM     40  OG  SER A  56      34.454  18.554  26.839  1.00 11.56           O  
ANISOU   40  OG  SER A  56     1305   1468   1617    -23    -67    121       O  
ATOM     41  N   PRO A  57      37.729  16.888  26.033  1.00  8.33           N  
ANISOU   41  N   PRO A  57     1272    890   1002     32    116    228       N  
ATOM     42  CA  PRO A  57      38.409  16.649  24.754  1.00  8.76           C  
ANISOU   42  CA  PRO A  57     1200   1016   1111     46     70    126       C  
ATOM     43  C   PRO A  57      37.622  17.191  23.585  1.00  8.53           C  
ANISOU   43  C   PRO A  57     1115   1087   1037     -2     90    120       C  
ATOM     44  O   PRO A  57      36.400  17.105  23.551  1.00 10.15           O  
ANISOU   44  O   PRO A  57     1192   1471   1192   -149     81    282       O  
ATOM     45  CB  PRO A  57      38.525  15.124  24.677  1.00  9.69           C  
ANISOU   45  CB  PRO A  57     1335   1102   1242     80    109    130       C  
ATOM     46  CG  PRO A  57      38.403  14.640  26.059  1.00 11.00           C  
ANISOU   46  CG  PRO A  57     1529   1180   1471    -88    159    137       C  
ATOM     47  CD  PRO A  57      37.508  15.628  26.772  1.00  9.30           C  
ANISOU   47  CD  PRO A  57     1414    924   1193    -51    111    240       C  
ATOM     48  N   TYR A  58      38.339  17.747  22.619  1.00  7.67           N  
ANISOU   48  N   TYR A  58     1033    891    988     31     36    154       N  
ATOM     49  CA  TYR A  58      37.722  18.174  21.383  1.00  8.58           C  
ANISOU   49  CA  TYR A  58     1188    996   1074     55     -4     48       C  
ATOM     50  C   TYR A  58      37.720  16.916  20.539  1.00 10.08           C  
ANISOU   50  C   TYR A  58     1394   1110   1326     65    -88     72       C  
ATOM     51  O   TYR A  58      37.954  15.802  21.051  1.00 12.68           O  
ANISOU   51  O   TYR A  58     1913   1264   1641     93    -65     79       O  
ATOM     52  CB  TYR A  58      38.459  19.389  20.783  1.00  7.74           C  
ANISOU   52  CB  TYR A  58     1048    922    971      4     19    108       C  
ATOM     53  CG  TYR A  58      37.649  20.058  19.693  1.00  7.14           C  
ANISOU   53  CG  TYR A  58      861    917    932     -6     51    201       C  
ATOM     54  CD1 TYR A  58      36.490  20.749  19.989  1.00  7.63           C  
ANISOU   54  CD1 TYR A  58      917   1131    849     48    144     55       C  
ATOM     55  CD2 TYR A  58      38.011  19.951  18.354  1.00  7.35           C  
ANISOU   55  CD2 TYR A  58      888    932    972    137    181    246       C  
ATOM     56  CE1 TYR A  58      35.725  21.321  18.986  1.00  6.97           C  
ANISOU   56  CE1 TYR A  58      857    814    975    105     84    107       C  
ATOM     57  CE2 TYR A  58      37.237  20.520  17.348  1.00  7.25           C  
ANISOU   57  CE2 TYR A  58      889    973    892    200    133    157       C  
ATOM     58  CZ  TYR A  58      36.095  21.188  17.671  1.00  6.13           C  
ANISOU   58  CZ  TYR A  58      822    864    641     39    -21    125       C  
ATOM     59  OH  TYR A  58      35.360  21.745  16.658  1.00  7.63           O  
ANISOU   59  OH  TYR A  58      905   1039    954    192    126    112       O  
ATOM     60  N   ILE A  59      37.333  17.049  19.295  1.00 12.35           N  
ANISOU   60  N   ILE A  59     1858   1391   1442     67    -54     19       N  
ATOM     61  CA  ILE A  59      37.115  15.901  18.448  1.00 12.48           C  
ANISOU   61  CA  ILE A  59     1815   1511   1414    -18      3     -5       C  
ATOM     62  C   ILE A  59      38.089  15.820  17.302  1.00 11.76           C  
ANISOU   62  C   ILE A  59     1818   1340   1310   -112     39    106       C  
ATOM     63  O   ILE A  59      38.750  16.803  16.917  1.00 13.39           O  
ANISOU   63  O   ILE A  59     2188   1365   1534   -381     75    175       O  
ATOM     64  CB  ILE A  59      35.694  15.926  17.889  1.00 13.52           C  
ANISOU   64  CB  ILE A  59     1835   1762   1541    -39    108     14       C  
ATOM     65  CG1 ILE A  59      35.445  17.222  17.112  1.00 15.44           C  
ANISOU   65  CG1 ILE A  59     1949   2069   1846     73      0   -114       C  
ATOM     66  CG2 ILE A  59      34.704  15.759  19.016  1.00 15.64           C  
ANISOU   66  CG2 ILE A  59     2034   2173   1734    -60    181     -9       C  
ATOM     67  CD1 ILE A  59      34.256  17.154  16.212  1.00 17.64           C  
ANISOU   67  CD1 ILE A  59     2133   2466   2102    160    -11    -39       C  
ATOM     68  N   GLU A  60      38.180  14.611  16.777  1.00 10.67           N  
ANISOU   68  N   GLU A  60     1639   1280   1133    -23    -37     88       N  
ATOM     69  CA  GLU A  60      38.661  14.409  15.428  1.00 10.55           C  
ANISOU   69  CA  GLU A  60     1532   1315   1163     56    -49     68       C  
ATOM     70  C   GLU A  60      37.481  14.459  14.452  1.00  8.69           C  
ANISOU   70  C   GLU A  60     1216   1143    942     52     12    -16       C  
ATOM     71  O   GLU A  60      36.332  14.278  14.839  1.00 10.07           O  
ANISOU   71  O   GLU A  60     1502   1442    879    -96     30    -26       O  
ATOM     72  CB  GLU A  60      39.495  13.129  15.350  1.00 12.80           C  
ANISOU   72  CB  GLU A  60     1738   1695   1428    183     12     58       C  
ATOM     73  CG  GLU A  60      40.798  13.316  16.137  1.00 17.70           C  
ANISOU   73  CG  GLU A  60     2231   2365   2126    151     23    142       C  
ATOM     74  CD  GLU A  60      41.613  12.057  16.350  1.00 21.64           C  
ANISOU   74  CD  GLU A  60     2708   3021   2493    302   -110    170       C  
ATOM     75  OE1 GLU A  60      41.570  11.155  15.484  1.00 23.57           O  
ANISOU   75  OE1 GLU A  60     3086   2940   2929    615    207     -9       O  
ATOM     76  OE2 GLU A  60      42.308  11.976  17.395  1.00 25.13           O  
ANISOU   76  OE2 GLU A  60     3159   3620   2769    347    -86    501       O  
ATOM     77  N   ILE A  61      37.793  14.733  13.206  1.00  6.90           N  
ANISOU   77  N   ILE A  61      935    872    813      2    -41    -38       N  
ATOM     78  CA  ILE A  61      36.779  14.950  12.200  1.00  7.13           C  
ANISOU   78  CA  ILE A  61      905    956    846     47    -10    -79       C  
ATOM     79  C   ILE A  61      37.084  14.056  11.030  1.00  7.33           C  
ANISOU   79  C   ILE A  61      914    895    976     45     11   -111       C  
ATOM     80  O   ILE A  61      38.219  13.998  10.572  1.00  8.79           O  
ANISOU   80  O   ILE A  61      909   1355   1074     35     25   -277       O  
ATOM     81  CB  ILE A  61      36.757  16.443  11.793  1.00  6.83           C  
ANISOU   81  CB  ILE A  61      872    907    815     11      2    -39       C  
ATOM     82  CG1 ILE A  61      36.419  17.333  12.993  1.00  6.74           C  
ANISOU   82  CG1 ILE A  61      894    785    881    -42    -61     65       C  
ATOM     83  CG2 ILE A  61      35.749  16.663  10.695  1.00  6.97           C  
ANISOU   83  CG2 ILE A  61      825   1030    791     13     -1   -137       C  
ATOM     84  CD1 ILE A  61      36.548  18.813  12.744  1.00  7.60           C  
ANISOU   84  CD1 ILE A  61      801    979   1105     37   -192     19       C  
ATOM     85  N   ASP A  62      36.066  13.372  10.530  1.00  6.96           N  
ANISOU   85  N   ASP A  62      879    847    917     63     -2   -113       N  
ATOM     86  CA  ASP A  62      36.254  12.425   9.448  1.00  7.34           C  
ANISOU   86  CA  ASP A  62     1021    854    911     87     -4   -129       C  
ATOM     87  C   ASP A  62      36.040  13.011   8.060  1.00  6.96           C  
ANISOU   87  C   ASP A  62      928    814    901     54    -13   -187       C  
ATOM     88  O   ASP A  62      35.232  13.916   7.872  1.00  6.52           O  
ANISOU   88  O   ASP A  62      908    660    910    138      9    -84       O  
ATOM     89  CB  ASP A  62      35.294  11.244   9.583  1.00  8.39           C  
ANISOU   89  CB  ASP A  62     1213    924   1048     72    -53    -65       C  
ATOM     90  CG  ASP A  62      35.411  10.521  10.881  1.00 11.97           C  
ANISOU   90  CG  ASP A  62     1683   1327   1535     27     30     -2       C  
ATOM     91  OD1 ASP A  62      36.506  10.494  11.474  1.00 15.65           O  
ANISOU   91  OD1 ASP A  62     2210   1886   1848    225   -149    466       O  
ATOM     92  OD2 ASP A  62      34.418   9.952  11.370  1.00 17.75           O  
ANISOU   92  OD2 ASP A  62     2414   2056   2271    -23     11    498       O  
ATOM     93  N   LEU A  63      36.758  12.454   7.084  1.00  6.71           N  
ANISOU   93  N   LEU A  63      874    717    956    136    -25   -252       N  
ATOM     94  CA  LEU A  63      36.396  12.571   5.682  1.00  6.81           C  
ANISOU   94  CA  LEU A  63      904    778    905     69     43   -222       C  
ATOM     95  C   LEU A  63      35.017  11.951   5.504  1.00  7.10           C  
ANISOU   95  C   LEU A  63      931    775    990     53     -5   -271       C  
ATOM     96  O   LEU A  63      34.647  11.040   6.252  1.00  7.91           O  
ANISOU   96  O   LEU A  63     1014    903   1085     -4    -28   -172       O  
ATOM     97  CB  LEU A  63      37.396  11.824   4.813  1.00  7.22           C  
ANISOU   97  CB  LEU A  63      943    739   1059    109     54   -290       C  
ATOM     98  CG  LEU A  63      38.828  12.357   4.856  1.00  7.73           C  
ANISOU   98  CG  LEU A  63      976    923   1038    116     32   -262       C  
ATOM     99  CD1 LEU A  63      39.771  11.385   4.148  1.00  8.36           C  
ANISOU   99  CD1 LEU A  63      942   1034   1198    124    181   -250       C  
ATOM    100  CD2 LEU A  63      38.933  13.737   4.253  1.00  8.58           C  
ANISOU  100  CD2 LEU A  63     1048   1104   1109    136    157   -380       C  
ATOM    101  N   PRO A  64      34.242  12.400   4.526  1.00  7.30           N  
ANISOU  101  N   PRO A  64      878    898    996     37     15   -243       N  
ATOM    102  CA  PRO A  64      32.886  11.862   4.349  1.00  7.38           C  
ANISOU  102  CA  PRO A  64      910    874   1018      0     44   -191       C  
ATOM    103  C   PRO A  64      32.877  10.416   3.868  1.00  7.74           C  
ANISOU  103  C   PRO A  64      968    851   1122     11     81   -205       C  
ATOM    104  O   PRO A  64      33.404  10.094   2.797  1.00  8.70           O  
ANISOU  104  O   PRO A  64     1187    984   1135    -21     85   -296       O  
ATOM    105  CB  PRO A  64      32.270  12.793   3.299  1.00  8.12           C  
ANISOU  105  CB  PRO A  64     1011    975   1099     38      3   -211       C  
ATOM    106  CG  PRO A  64      33.462  13.342   2.535  1.00  7.13           C  
ANISOU  106  CG  PRO A  64      901    882    923    108    -19   -170       C  
ATOM    107  CD  PRO A  64      34.540  13.481   3.572  1.00  7.55           C  
ANISOU  107  CD  PRO A  64      975    909    984     19     39   -240       C  
ATOM    108  N   SER A  65      32.257   9.546   4.658  1.00  8.35           N  
ANISOU  108  N   SER A  65     1040    960   1170    -13    147   -170       N  
ATOM    109  CA  SER A  65      32.130   8.131   4.315  1.00  8.84           C  
ANISOU  109  CA  SER A  65     1063    976   1317     41    117   -168       C  
ATOM    110  C   SER A  65      30.817   7.862   3.590  1.00  8.60           C  
ANISOU  110  C   SER A  65     1095    888   1282     56    135   -174       C  
ATOM    111  O   SER A  65      29.878   8.664   3.639  1.00  8.27           O  
ANISOU  111  O   SER A  65     1084    748   1309     52    143   -317       O  
ATOM    112  CB  SER A  65      32.191   7.250   5.568  1.00  9.54           C  
ANISOU  112  CB  SER A  65     1118   1109   1394     36    100   -117       C  
ATOM    113  OG  SER A  65      31.018   7.423   6.342  1.00 10.43           O  
ANISOU  113  OG  SER A  65     1032   1304   1625    177    169    -41       O  
ATOM    114  N   GLU A  66      30.748   6.713   2.924  1.00  9.13           N  
ANISOU  114  N   GLU A  66     1150    896   1421    100    219   -236       N  
ATOM    115  CA  GLU A  66      29.508   6.316   2.271  1.00 10.14           C  
ANISOU  115  CA  GLU A  66     1322   1114   1416     20    180   -273       C  
ATOM    116  C   GLU A  66      28.356   6.255   3.260  1.00  9.39           C  
ANISOU  116  C   GLU A  66     1243    968   1354    -10    174   -287       C  
ATOM    117  O   GLU A  66      27.277   6.760   2.981  1.00  9.78           O  
ANISOU  117  O   GLU A  66     1233   1039   1443    -76    161   -393       O  
ATOM    118  CB  GLU A  66      29.642   4.957   1.552  1.00 11.33           C  
ANISOU  118  CB  GLU A  66     1516   1287   1500     47    250   -342       C  
ATOM    119  CG  GLU A  66      28.306   4.414   1.019  1.00 15.93           C  
ANISOU  119  CG  GLU A  66     2181   1857   2012    -25    131   -304       C  
ATOM    120  CD  GLU A  66      28.433   3.123   0.242  1.00 20.49           C  
ANISOU  120  CD  GLU A  66     2698   2536   2548     23     78   -291       C  
ATOM    121  OE1 GLU A  66      28.933   2.141   0.821  1.00 23.61           O  
ANISOU  121  OE1 GLU A  66     3389   2405   3173     62    213   -304       O  
ATOM    122  OE2 GLU A  66      28.019   3.089  -0.939  1.00 25.25           O  
ANISOU  122  OE2 GLU A  66     3394   3150   3050    -68    119   -533       O  
ATOM    123  N   SER A  67      28.585   5.632   4.407  1.00  9.14           N  
ANISOU  123  N   SER A  67     1199    902   1370     32    172   -273       N  
ATOM    124  CA  SER A  67      27.500   5.447   5.369  1.00 10.01           C  
ANISOU  124  CA  SER A  67     1291   1065   1444     45    173   -145       C  
ATOM    125  C   SER A  67      27.067   6.771   5.976  1.00  8.81           C  
ANISOU  125  C   SER A  67     1186    902   1256     79    189   -212       C  
ATOM    126  O   SER A  67      25.882   6.991   6.211  1.00  9.60           O  
ANISOU  126  O   SER A  67     1155    969   1524     19    204   -237       O  
ATOM    127  CB  SER A  67      27.874   4.458   6.473  1.00 11.61           C  
ANISOU  127  CB  SER A  67     1512   1255   1643     68    210    -99       C  
ATOM    128  OG  SER A  67      28.977   4.872   7.232  1.00 14.26           O  
ANISOU  128  OG  SER A  67     1889   1507   2023    157    282    -11       O  
ATOM    129  N   ARG A  68      28.017   7.667   6.221  1.00  8.58           N  
ANISOU  129  N   ARG A  68     1052    960   1244     56    157   -229       N  
ATOM    130  CA  ARG A  68      27.693   8.974   6.785  1.00  8.32           C  
ANISOU  130  CA  ARG A  68     1039    947   1175     48    105   -202       C  
ATOM    131  C   ARG A  68      26.824   9.757   5.813  1.00  8.01           C  
ANISOU  131  C   ARG A  68     1022    890   1132     28    105   -216       C  
ATOM    132  O   ARG A  68      25.796  10.325   6.203  1.00  7.98           O  
ANISOU  132  O   ARG A  68      872    844   1316     15    198   -303       O  
ATOM    133  CB  ARG A  68      28.955   9.785   7.107  1.00  8.65           C  
ANISOU  133  CB  ARG A  68     1069   1018   1196     81     30   -168       C  
ATOM    134  CG  ARG A  68      28.649  11.128   7.782  1.00  8.97           C  
ANISOU  134  CG  ARG A  68     1110    907   1392     50    -97   -146       C  
ATOM    135  CD  ARG A  68      28.366  10.995   9.266  1.00  9.86           C  
ANISOU  135  CD  ARG A  68     1105   1188   1452    -60    226   -276       C  
ATOM    136  NE  ARG A  68      29.617  10.789   9.969  1.00  9.23           N  
ANISOU  136  NE  ARG A  68     1213   1036   1255   -109    225   -175       N  
ATOM    137  CZ  ARG A  68      30.474  11.757  10.265  1.00  8.88           C  
ANISOU  137  CZ  ARG A  68     1105   1141   1126   -174    125   -158       C  
ATOM    138  NH1 ARG A  68      30.148  13.034  10.076  1.00  9.14           N  
ANISOU  138  NH1 ARG A  68     1127   1073   1272   -131     62   -183       N  
ATOM    139  NH2 ARG A  68      31.642  11.441  10.803  1.00  9.93           N  
ANISOU  139  NH2 ARG A  68     1215   1068   1488    -27     36   -227       N  
ATOM    140  N   ILE A  69      27.229   9.824   4.555  1.00  7.72           N  
ANISOU  140  N   ILE A  69      885    910   1135      4    115   -207       N  
ATOM    141  CA  ILE A  69      26.494  10.586   3.566  1.00  7.90           C  
ANISOU  141  CA  ILE A  69      959    925   1115     37     72   -232       C  
ATOM    142  C   ILE A  69      25.093  10.004   3.380  1.00  8.35           C  
ANISOU  142  C   ILE A  69     1007    994   1170     19     23   -233       C  
ATOM    143  O   ILE A  69      24.116  10.740   3.335  1.00  8.77           O  
ANISOU  143  O   ILE A  69      989   1068   1272     37    -30   -256       O  
ATOM    144  CB  ILE A  69      27.280  10.669   2.238  1.00  8.29           C  
ANISOU  144  CB  ILE A  69     1035    986   1127     77    115   -182       C  
ATOM    145  CG1 ILE A  69      28.568  11.485   2.415  1.00  8.01           C  
ANISOU  145  CG1 ILE A  69      952    904   1187    184    213   -180       C  
ATOM    146  CG2 ILE A  69      26.414  11.244   1.119  1.00  9.03           C  
ANISOU  146  CG2 ILE A  69     1110   1183   1137     45    155   -331       C  
ATOM    147  CD1 ILE A  69      28.371  12.938   2.863  1.00  8.71           C  
ANISOU  147  CD1 ILE A  69     1037   1033   1238     55    266   -114       C  
ATOM    148  N   GLN A  70      24.978   8.687   3.301  1.00  9.03           N  
ANISOU  148  N   GLN A  70     1023   1088   1319    -11     57   -267       N  
ATOM    149  CA  GLN A  70      23.663   8.065   3.154  1.00  9.97           C  
ANISOU  149  CA  GLN A  70     1134   1229   1422    -84     36   -257       C  
ATOM    150  C   GLN A  70      22.760   8.408   4.337  1.00  9.86           C  
ANISOU  150  C   GLN A  70     1054   1190   1500    -57     46   -275       C  
ATOM    151  O   GLN A  70      21.590   8.713   4.159  1.00 10.39           O  
ANISOU  151  O   GLN A  70      953   1295   1697    -79    -36   -383       O  
ATOM    152  CB  GLN A  70      23.802   6.548   3.000  1.00 11.39           C  
ANISOU  152  CB  GLN A  70     1280   1362   1685    -84     87   -323       C  
ATOM    153  CG  GLN A  70      24.345   6.122   1.634  1.00 15.15           C  
ANISOU  153  CG  GLN A  70     1770   1919   2066    -29     81   -381       C  
ATOM    154  CD  GLN A  70      24.586   4.613   1.506  1.00 19.50           C  
ANISOU  154  CD  GLN A  70     2491   2463   2452     25    124   -470       C  
ATOM    155  OE1 GLN A  70      24.649   4.085   0.390  1.00 25.55           O  
ANISOU  155  OE1 GLN A  70     3245   3184   3279     -6    196   -531       O  
ATOM    156  NE2 GLN A  70      24.751   3.927   2.639  1.00 21.99           N  
ANISOU  156  NE2 GLN A  70     2791   2398   3164    107    233   -469       N  
ATOM    157  N   SER A  71      23.313   8.370   5.539  1.00  9.16           N  
ANISOU  157  N   SER A  71     1011   1038   1428    -29    128   -209       N  
ATOM    158  CA  SER A  71      22.538   8.672   6.737  1.00  9.41           C  
ANISOU  158  CA  SER A  71     1085   1087   1401   -121    143   -168       C  
ATOM    159  C   SER A  71      22.139  10.142   6.811  1.00  8.82           C  
ANISOU  159  C   SER A  71      972   1048   1328    -68    153   -190       C  
ATOM    160  O   SER A  71      21.038  10.469   7.249  1.00  9.42           O  
ANISOU  160  O   SER A  71      864   1183   1533   -135    238   -254       O  
ATOM    161  CB  SER A  71      23.330   8.303   7.980  1.00 10.04           C  
ANISOU  161  CB  SER A  71     1320   1116   1378    -43    252   -113       C  
ATOM    162  OG  SER A  71      23.470   6.912   8.117  1.00 14.22           O  
ANISOU  162  OG  SER A  71     1888   1464   2049    -85    255    -11       O  
ATOM    163  N   LEU A  72      23.025  11.035   6.393  1.00  7.98           N  
ANISOU  163  N   LEU A  72      853    960   1218    -38    152   -203       N  
ATOM    164  CA  LEU A  72      22.700  12.454   6.385  1.00  7.91           C  
ANISOU  164  CA  LEU A  72      876    981   1146     13    111   -173       C  
ATOM    165  C   LEU A  72      21.559  12.750   5.425  1.00  8.47           C  
ANISOU  165  C   LEU A  72      940   1035   1241     20     65   -209       C  
ATOM    166  O   LEU A  72      20.677  13.537   5.738  1.00  9.08           O  
ANISOU  166  O   LEU A  72      859   1217   1372    134     55   -196       O  
ATOM    167  CB  LEU A  72      23.937  13.291   6.066  1.00  7.31           C  
ANISOU  167  CB  LEU A  72      877    883   1017     -7    164   -205       C  
ATOM    168  CG  LEU A  72      24.961  13.356   7.203  1.00  7.27           C  
ANISOU  168  CG  LEU A  72      782    970   1010     81    147   -122       C  
ATOM    169  CD1 LEU A  72      26.247  13.996   6.730  1.00  7.32           C  
ANISOU  169  CD1 LEU A  72      919    833   1030     -2     79   -179       C  
ATOM    170  CD2 LEU A  72      24.421  14.102   8.419  1.00  7.53           C  
ANISOU  170  CD2 LEU A  72      963    910    985     26    119    -72       C  
ATOM    171  N   HIS A  73      21.531  12.080   4.287  1.00  9.11           N  
ANISOU  171  N   HIS A  73      936   1192   1333     26     18   -163       N  
ATOM    172  CA  HIS A  73      20.392  12.239   3.387  1.00 10.66           C  
ANISOU  172  CA  HIS A  73     1139   1424   1487     -5    -56   -122       C  
ATOM    173  C   HIS A  73      19.112  11.631   3.938  1.00 11.06           C  
ANISOU  173  C   HIS A  73     1124   1461   1617    -29    -60   -150       C  
ATOM    174  O   HIS A  73      18.081  12.290   3.955  1.00 11.72           O  
ANISOU  174  O   HIS A  73     1038   1612   1801     16   -126   -182       O  
ATOM    175  CB  HIS A  73      20.711  11.686   2.016  1.00 11.39           C  
ANISOU  175  CB  HIS A  73     1278   1573   1474     15   -116   -152       C  
ATOM    176  CG  HIS A  73      21.579  12.598   1.224  1.00 12.21           C  
ANISOU  176  CG  HIS A  73     1297   1759   1583     83    -91   -101       C  
ATOM    177  ND1 HIS A  73      21.077  13.656   0.500  1.00 15.54           N  
ANISOU  177  ND1 HIS A  73     1835   2168   1901     71    -88     36       N  
ATOM    178  CD2 HIS A  73      22.925  12.688   1.132  1.00 15.34           C  
ANISOU  178  CD2 HIS A  73     1519   2398   1910    175     72    141       C  
ATOM    179  CE1 HIS A  73      22.073  14.308  -0.072  1.00 15.27           C  
ANISOU  179  CE1 HIS A  73     1888   2106   1807     10    -22     14       C  
ATOM    180  NE2 HIS A  73      23.205  13.744   0.302  1.00 16.00           N  
ANISOU  180  NE2 HIS A  73     1822   2420   1836     84     45    153       N  
ATOM    181  N   LYS A  74      19.190  10.402   4.427  1.00 11.31           N  
ANISOU  181  N   LYS A  74     1086   1464   1744   -141     37   -145       N  
ATOM    182  CA  LYS A  74      17.993   9.689   4.878  1.00 12.24           C  
ANISOU  182  CA  LYS A  74     1281   1570   1798   -131     34   -130       C  
ATOM    183  C   LYS A  74      17.318  10.385   6.052  1.00 11.98           C  
ANISOU  183  C   LYS A  74     1172   1529   1848   -100     83   -160       C  
ATOM    184  O   LYS A  74      16.084  10.418   6.144  1.00 13.11           O  
ANISOU  184  O   LYS A  74     1020   1757   2203   -117    191   -314       O  
ATOM    185  CB  LYS A  74      18.335   8.242   5.246  1.00 12.91           C  
ANISOU  185  CB  LYS A  74     1394   1611   1897   -128     80   -145       C  
ATOM    186  CG  LYS A  74      17.127   7.395   5.620  1.00 17.37           C  
ANISOU  186  CG  LYS A  74     2012   2135   2451    -95     49   -125       C  
ATOM    187  CD  LYS A  74      16.113   7.287   4.476  1.00 22.78           C  
ANISOU  187  CD  LYS A  74     2845   2894   2915    -59     13     -2       C  
ATOM    188  CE  LYS A  74      15.121   6.149   4.706  1.00 25.42           C  
ANISOU  188  CE  LYS A  74     3239   3197   3222    -16    -12    -16       C  
ATOM    189  NZ  LYS A  74      14.309   5.856   3.497  1.00 28.28           N  
ANISOU  189  NZ  LYS A  74     3542   3603   3599     90    -46    -41       N  
ATOM    190  N   SER A  75      18.123  10.938   6.951  1.00 11.07           N  
ANISOU  190  N   SER A  75     1081   1438   1684    -70    112   -125       N  
ATOM    191  CA  SER A  75      17.621  11.627   8.128  1.00 11.13           C  
ANISOU  191  CA  SER A  75     1189   1414   1626    -39    151    -80       C  
ATOM    192  C   SER A  75      16.975  12.967   7.807  1.00 10.90           C  
ANISOU  192  C   SER A  75     1076   1392   1673     -5    105   -108       C  
ATOM    193  O   SER A  75      16.318  13.538   8.663  1.00 12.48           O  
ANISOU  193  O   SER A  75     1197   1598   1946     39    338   -156       O  
ATOM    194  CB  SER A  75      18.750  11.878   9.116  1.00 11.16           C  
ANISOU  194  CB  SER A  75     1209   1384   1648     -4    177   -128       C  
ATOM    195  OG  SER A  75      19.719  12.744   8.551  1.00 10.33           O  
ANISOU  195  OG  SER A  75      905   1328   1690    -29    182   -231       O  
ATOM    196  N   GLY A  76      17.193  13.497   6.610  1.00 10.13           N  
ANISOU  196  N   GLY A  76      972   1323   1554    -52     19   -131       N  
ATOM    197  CA  GLY A  76      16.750  14.833   6.275  1.00 10.10           C  
ANISOU  197  CA  GLY A  76     1028   1288   1520    -39     -5    -61       C  
ATOM    198  C   GLY A  76      17.766  15.916   6.584  1.00  9.05           C  
ANISOU  198  C   GLY A  76      888   1173   1375     28    -63    -43       C  
ATOM    199  O   GLY A  76      17.565  17.064   6.193  1.00 10.10           O  
ANISOU  199  O   GLY A  76      853   1280   1704      0   -135    -27       O  
ATOM    200  N   LEU A  77      18.864  15.570   7.261  1.00  8.52           N  
ANISOU  200  N   LEU A  77      816   1084   1337      3     31    -14       N  
ATOM    201  CA  LEU A  77      19.818  16.590   7.668  1.00  8.03           C  
ANISOU  201  CA  LEU A  77      840   1095   1114    -46    -15    -25       C  
ATOM    202  C   LEU A  77      20.554  17.221   6.488  1.00  7.21           C  
ANISOU  202  C   LEU A  77      685   1031   1022     39    -18    -62       C  
ATOM    203  O   LEU A  77      20.877  18.401   6.541  1.00  7.89           O  
ANISOU  203  O   LEU A  77      765   1107   1124    -38    -36     -9       O  
ATOM    204  CB  LEU A  77      20.815  16.020   8.660  1.00  8.06           C  
ANISOU  204  CB  LEU A  77      843   1116   1101    -58     -1      2       C  
ATOM    205  CG  LEU A  77      20.235  15.696  10.031  1.00  9.09           C  
ANISOU  205  CG  LEU A  77      935   1227   1289    -72     86    -57       C  
ATOM    206  CD1 LEU A  77      21.234  14.940  10.837  1.00 10.45           C  
ANISOU  206  CD1 LEU A  77     1064   1530   1375    -90    -37    175       C  
ATOM    207  CD2 LEU A  77      19.791  16.934  10.762  1.00 11.72           C  
ANISOU  207  CD2 LEU A  77     1549   1543   1360   -101    164    -19       C  
ATOM    208  N   ALA A  78      20.808  16.462   5.424  1.00  7.83           N  
ANISOU  208  N   ALA A  78      817   1066   1090     -6    -12    -88       N  
ATOM    209  CA  ALA A  78      21.581  16.968   4.295  1.00  8.47           C  
ANISOU  209  CA  ALA A  78      916   1187   1113     -6    -13    -75       C  
ATOM    210  C   ALA A  78      20.884  18.141   3.614  1.00  8.53           C  
ANISOU  210  C   ALA A  78      876   1196   1167    -54    -61    -41       C  
ATOM    211  O   ALA A  78      21.533  19.032   3.088  1.00  9.36           O  
ANISOU  211  O   ALA A  78      961   1353   1239     45   -147     73       O  
ATOM    212  CB  ALA A  78      21.839  15.872   3.289  1.00  9.03           C  
ANISOU  212  CB  ALA A  78     1073   1185   1173    -42     50    -92       C  
ATOM    213  N   ALA A  79      19.550  18.145   3.630  1.00  9.47           N  
ANISOU  213  N   ALA A  79      963   1316   1318     13   -138     -8       N  
ATOM    214  CA  ALA A  79      18.752  19.184   2.970  1.00 10.09           C  
ANISOU  214  CA  ALA A  79     1107   1387   1338     12   -181    -27       C  
ATOM    215  C   ALA A  79      18.653  20.471   3.783  1.00  9.92           C  
ANISOU  215  C   ALA A  79     1024   1407   1337     97   -207     -8       C  
ATOM    216  O   ALA A  79      18.143  21.473   3.292  1.00 11.33           O  
ANISOU  216  O   ALA A  79     1244   1529   1528    239   -471    -36       O  
ATOM    217  CB  ALA A  79      17.360  18.646   2.708  1.00 10.82           C  
ANISOU  217  CB  ALA A  79     1159   1487   1465      3   -228    -80       C  
ATOM    218  N   GLN A  80      19.116  20.441   5.033  1.00  9.26           N  
ANISOU  218  N   GLN A  80      919   1321   1277     88   -152    -99       N  
ATOM    219  CA  GLN A  80      19.085  21.596   5.919  1.00  9.29           C  
ANISOU  219  CA  GLN A  80      932   1331   1265     96    -60    -96       C  
ATOM    220  C   GLN A  80      20.326  22.465   5.664  1.00  9.11           C  
ANISOU  220  C   GLN A  80      898   1340   1223    144    -36   -101       C  
ATOM    221  O   GLN A  80      20.956  22.333   4.625  1.00  9.99           O  
ANISOU  221  O   GLN A  80     1023   1631   1142      8    -77   -160       O  
ATOM    222  CB  GLN A  80      18.933  21.118   7.359  1.00  9.29           C  
ANISOU  222  CB  GLN A  80      872   1338   1316    124    -29   -168       C  
ATOM    223  CG  GLN A  80      17.629  20.324   7.551  1.00 10.26           C  
ANISOU  223  CG  GLN A  80      959   1496   1443     62    -53    -93       C  
ATOM    224  CD  GLN A  80      17.451  19.716   8.934  1.00 12.16           C  
ANISOU  224  CD  GLN A  80      827   2060   1732    -70    -84   -122       C  
ATOM    225  OE1 GLN A  80      18.187  20.005   9.855  1.00 12.95           O  
ANISOU  225  OE1 GLN A  80      904   2186   1830   -402   -133     92       O  
ATOM    226  NE2 GLN A  80      16.436  18.870   9.074  1.00 15.56           N  
ANISOU  226  NE2 GLN A  80     1320   2324   2268   -571    -11   -295       N  
ATOM    227  N   GLU A  81      20.643  23.377   6.573  1.00  8.73           N  
ANISOU  227  N   GLU A  81      874   1267   1176    127    -36    -73       N  
ATOM    228  CA  GLU A  81      21.690  24.368   6.333  1.00  8.29           C  
ANISOU  228  CA  GLU A  81      841   1119   1188    179    -72     -5       C  
ATOM    229  C   GLU A  81      23.011  23.942   6.965  1.00  6.84           C  
ANISOU  229  C   GLU A  81      727    896    975    150    -41    -38       C  
ATOM    230  O   GLU A  81      23.063  23.575   8.143  1.00  6.87           O  
ANISOU  230  O   GLU A  81      651    964    996    109      1    -78       O  
ATOM    231  CB  GLU A  81      21.292  25.723   6.915  1.00  9.67           C  
ANISOU  231  CB  GLU A  81      961   1236   1475    198    -21      7       C  
ATOM    232  CG  GLU A  81      20.281  26.580   6.168  1.00 13.76           C  
ANISOU  232  CG  GLU A  81     1438   1782   2008    177   -116     14       C  
ATOM    233  CD  GLU A  81      20.492  28.042   6.545  1.00 16.85           C  
ANISOU  233  CD  GLU A  81     2287   1915   2198    278    -58     70       C  
ATOM    234  OE1 GLU A  81      21.004  28.826   5.719  1.00 18.18           O  
ANISOU  234  OE1 GLU A  81     2294   1824   2790    334   -325    -34       O  
ATOM    235  OE2 GLU A  81      20.210  28.388   7.713  1.00 19.24           O  
ANISOU  235  OE2 GLU A  81     2620   2215   2476     52   -256    -91       O  
ATOM    236  N   TRP A  82      24.055  24.069   6.162  1.00  6.78           N  
ANISOU  236  N   TRP A  82      760    921    893    135    -52     39       N  
ATOM    237  CA  TRP A  82      25.428  23.727   6.498  1.00  5.64           C  
ANISOU  237  CA  TRP A  82      657    743    740    114    -92     -8       C  
ATOM    238  C   TRP A  82      26.323  24.892   6.106  1.00  5.61           C  
ANISOU  238  C   TRP A  82      721    677    732     96    -87    -28       C  
ATOM    239  O   TRP A  82      25.987  25.707   5.245  1.00  6.42           O  
ANISOU  239  O   TRP A  82      772    824    842     91   -149     24       O  
ATOM    240  CB  TRP A  82      25.861  22.476   5.715  1.00  6.41           C  
ANISOU  240  CB  TRP A  82      760    795    880     74    -36      0       C  
ATOM    241  CG  TRP A  82      25.084  21.243   6.054  1.00  6.10           C  
ANISOU  241  CG  TRP A  82      720    664    931     55    -87   -108       C  
ATOM    242  CD1 TRP A  82      23.780  20.996   5.757  1.00  6.25           C  
ANISOU  242  CD1 TRP A  82      618    758    997    116   -177   -159       C  
ATOM    243  CD2 TRP A  82      25.558  20.090   6.748  1.00  5.81           C  
ANISOU  243  CD2 TRP A  82      585    740    881     33   -113   -165       C  
ATOM    244  NE1 TRP A  82      23.407  19.771   6.247  1.00  6.29           N  
ANISOU  244  NE1 TRP A  82      616    689   1084    -16   -157   -119       N  
ATOM    245  CE2 TRP A  82      24.477  19.195   6.865  1.00  6.66           C  
ANISOU  245  CE2 TRP A  82      806    715   1006     15    -42   -191       C  
ATOM    246  CE3 TRP A  82      26.794  19.722   7.294  1.00  6.08           C  
ANISOU  246  CE3 TRP A  82      786    598    925    -41    -13   -162       C  
ATOM    247  CZ2 TRP A  82      24.599  17.961   7.483  1.00  7.04           C  
ANISOU  247  CZ2 TRP A  82      707    836   1132    -38    -14   -173       C  
ATOM    248  CZ3 TRP A  82      26.914  18.497   7.903  1.00  6.38           C  
ANISOU  248  CZ3 TRP A  82      818    792    813     61   -142    -89       C  
ATOM    249  CH2 TRP A  82      25.832  17.632   7.997  1.00  7.28           C  
ANISOU  249  CH2 TRP A  82      945    799   1020    -11    -83   -149       C  
ATOM    250  N   VAL A  83      27.495  24.938   6.725  1.00  5.50           N  
ANISOU  250  N   VAL A  83      665    673    749     66    -65     13       N  
ATOM    251  CA  VAL A  83      28.558  25.853   6.334  1.00  5.35           C  
ANISOU  251  CA  VAL A  83      696    631    705     69    -79    -53       C  
ATOM    252  C   VAL A  83      29.852  25.080   6.127  1.00  5.46           C  
ANISOU  252  C   VAL A  83      716    650    706     92    -81      8       C  
ATOM    253  O   VAL A  83      30.092  24.049   6.745  1.00  6.18           O  
ANISOU  253  O   VAL A  83      768    727    852     93     43    117       O  
ATOM    254  CB  VAL A  83      28.792  26.978   7.383  1.00  5.76           C  
ANISOU  254  CB  VAL A  83      735    662    788     58    -39    -95       C  
ATOM    255  CG1 VAL A  83      27.590  27.932   7.390  1.00  6.61           C  
ANISOU  255  CG1 VAL A  83      941    773    794     79    -39   -135       C  
ATOM    256  CG2 VAL A  83      29.071  26.406   8.787  1.00  6.54           C  
ANISOU  256  CG2 VAL A  83      887    818    780     69    -36   -168       C  
ATOM    257  N   ALA A  84      30.707  25.624   5.272  1.00  5.43           N  
ANISOU  257  N   ALA A  84      692    683    687     65    -39     45       N  
ATOM    258  CA  ALA A  84      32.110  25.240   5.201  1.00  5.06           C  
ANISOU  258  CA  ALA A  84      614    693    615     92    -26     35       C  
ATOM    259  C   ALA A  84      32.946  26.392   5.715  1.00  5.11           C  
ANISOU  259  C   ALA A  84      646    588    705    138     35     21       C  
ATOM    260  O   ALA A  84      32.764  27.514   5.253  1.00  5.97           O  
ANISOU  260  O   ALA A  84      801    619    845     87   -127     82       O  
ATOM    261  CB  ALA A  84      32.527  24.920   3.791  1.00  6.31           C  
ANISOU  261  CB  ALA A  84      880    760    757     73      0    -17       C  
ATOM    262  N   CYS A  85      33.852  26.124   6.654  1.00  4.78           N  
ANISOU  262  N   CYS A  85      661    567    587     84    -13    -15       N  
ATOM    263  CA  CYS A  85      34.795  27.114   7.154  1.00  4.73           C  
ANISOU  263  CA  CYS A  85      631    587    578     63     76     12       C  
ATOM    264  C   CYS A  85      36.205  26.576   6.987  1.00  4.63           C  
ANISOU  264  C   CYS A  85      641    575    542     51     33    -21       C  
ATOM    265  O   CYS A  85      36.421  25.390   6.800  1.00  4.76           O  
ANISOU  265  O   CYS A  85      673    498    637     81     83    -13       O  
ATOM    266  CB  CYS A  85      34.535  27.427   8.627  1.00  5.52           C  
ANISOU  266  CB  CYS A  85      751    705    641     81    115    -47       C  
ATOM    267  SG  CYS A  85      32.869  28.017   9.012  1.00  7.11           S  
ANISOU  267  SG  CYS A  85      893    934    871    225    141    -45       S  
ATOM    268  N   GLU A  86      37.190  27.455   7.078  1.00  4.62           N  
ANISOU  268  N   GLU A  86      605    473    676     15     22    -20       N  
ATOM    269  CA  GLU A  86      38.571  27.044   6.878  1.00  4.45           C  
ANISOU  269  CA  GLU A  86      630    558    502    -11     35     36       C  
ATOM    270  C   GLU A  86      39.020  26.076   7.969  1.00  4.37           C  
ANISOU  270  C   GLU A  86      609    540    511     -6     46     11       C  
ATOM    271  O   GLU A  86      38.754  26.297   9.154  1.00  4.85           O  
ANISOU  271  O   GLU A  86      800    565    476     61     36     21       O  
ATOM    272  CB  GLU A  86      39.465  28.281   6.845  1.00  5.19           C  
ANISOU  272  CB  GLU A  86      731    632    606    -46     22     85       C  
ATOM    273  CG  GLU A  86      40.931  27.959   6.607  1.00  4.98           C  
ANISOU  273  CG  GLU A  86      687    627    578   -139     48     -4       C  
ATOM    274  CD  GLU A  86      41.812  29.159   6.344  1.00  6.64           C  
ANISOU  274  CD  GLU A  86      815    736    971    -14    -16      2       C  
ATOM    275  OE1 GLU A  86      41.342  30.314   6.471  1.00  7.94           O  
ANISOU  275  OE1 GLU A  86      992    736   1286   -127     99     42       O  
ATOM    276  OE2 GLU A  86      43.012  28.933   6.041  1.00  6.62           O  
ANISOU  276  OE2 GLU A  86      802    752    959   -115     84    134       O  
ATOM    277  N   LYS A  87      39.723  25.026   7.552  1.00  3.83           N  
ANISOU  277  N   LYS A  87      601    433    419     67     40     -9       N  
ATOM    278  CA  LYS A  87      40.425  24.140   8.472  1.00  3.94           C  
ANISOU  278  CA  LYS A  87      568    448    478     18     44      8       C  
ATOM    279  C   LYS A  87      41.850  24.659   8.607  1.00  3.95           C  
ANISOU  279  C   LYS A  87      554    466    479     23     86    -50       C  
ATOM    280  O   LYS A  87      42.583  24.714   7.619  1.00  4.64           O  
ANISOU  280  O   LYS A  87      637    663    460     -4    107   -168       O  
ATOM    281  CB  LYS A  87      40.406  22.700   7.983  1.00  4.21           C  
ANISOU  281  CB  LYS A  87      503    526    571    -14    -38     17       C  
ATOM    282  CG  LYS A  87      40.812  21.716   9.060  1.00  4.82           C  
ANISOU  282  CG  LYS A  87      656    466    707     53     35    -35       C  
ATOM    283  CD  LYS A  87      40.599  20.285   8.636  1.00  5.64           C  
ANISOU  283  CD  LYS A  87      798    543    801     87   -121    -54       C  
ATOM    284  CE  LYS A  87      40.745  19.292   9.788  1.00  6.04           C  
ANISOU  284  CE  LYS A  87     1018    427    849    -43    -53    -93       C  
ATOM    285  NZ  LYS A  87      42.137  19.250  10.300  1.00  6.11           N  
ANISOU  285  NZ  LYS A  87      888    654    777    170    -43     52       N  
ATOM    286  N   VAL A  88      42.191  25.106   9.813  1.00  4.11           N  
ANISOU  286  N   VAL A  88      507    540    514    -46     71    -40       N  
ATOM    287  CA  VAL A  88      43.484  25.722  10.086  1.00  4.45           C  
ANISOU  287  CA  VAL A  88      580    547    560    -10     47    -50       C  
ATOM    288  C   VAL A  88      44.463  24.675  10.618  1.00  3.93           C  
ANISOU  288  C   VAL A  88      483    537    472    -80     75    -27       C  
ATOM    289  O   VAL A  88      44.131  23.888  11.506  1.00  4.74           O  
ANISOU  289  O   VAL A  88      592    592    614    -58     57      6       O  
ATOM    290  CB  VAL A  88      43.302  26.914  11.068  1.00  4.47           C  
ANISOU  290  CB  VAL A  88      578    576    542     12     82    -79       C  
ATOM    291  CG1 VAL A  88      44.644  27.493  11.514  1.00  5.48           C  
ANISOU  291  CG1 VAL A  88      725    675    681     -4     -7    -89       C  
ATOM    292  CG2 VAL A  88      42.459  27.975  10.373  1.00  5.25           C  
ANISOU  292  CG2 VAL A  88      749    608    637    -15     99   -120       C  
ATOM    293  N   HIS A  89      45.670  24.687  10.054  1.00  4.36           N  
ANISOU  293  N   HIS A  89      571    532    553    -29      8     -8       N  
ATOM    294  CA  HIS A  89      46.730  23.760  10.416  1.00  4.44           C  
ANISOU  294  CA  HIS A  89      528    573    584     46     59    -93       C  
ATOM    295  C   HIS A  89      47.626  24.352  11.490  1.00  4.47           C  
ANISOU  295  C   HIS A  89      555    534    610     36     19   -110       C  
ATOM    296  O   HIS A  89      48.645  24.992  11.200  1.00  5.45           O  
ANISOU  296  O   HIS A  89      578    818    674   -134     60    -59       O  
ATOM    297  CB  HIS A  89      47.539  23.442   9.194  1.00  5.39           C  
ANISOU  297  CB  HIS A  89      625    734    686      7    -29    -72       C  
ATOM    298  CG  HIS A  89      48.572  22.385   9.383  1.00  5.84           C  
ANISOU  298  CG  HIS A  89      683    822    713     77    153    -58       C  
ATOM    299  ND1 HIS A  89      48.273  21.121   9.793  1.00  7.90           N  
ANISOU  299  ND1 HIS A  89      803    944   1254    199    139     20       N  
ATOM    300  CD2 HIS A  89      49.912  22.427   9.275  1.00  9.92           C  
ANISOU  300  CD2 HIS A  89      910    824   2033     33    230     73       C  
ATOM    301  CE1 HIS A  89      49.367  20.386   9.781  1.00  7.28           C  
ANISOU  301  CE1 HIS A  89      772    763   1230    171    290     -8       C  
ATOM    302  NE2 HIS A  89      50.363  21.139   9.389  1.00  7.99           N  
ANISOU  302  NE2 HIS A  89      863   1003   1169    162    -39   -133       N  
ATOM    303  N   GLY A  90      47.212  24.171  12.734  1.00  4.84           N  
ANISOU  303  N   GLY A  90      553    636    650    -38     69    -75       N  
ATOM    304  CA  GLY A  90      47.977  24.569  13.905  1.00  4.82           C  
ANISOU  304  CA  GLY A  90      618    568    643     42     67    -55       C  
ATOM    305  C   GLY A  90      47.968  23.416  14.884  1.00  4.31           C  
ANISOU  305  C   GLY A  90      547    528    562      8     57    -34       C  
ATOM    306  O   GLY A  90      48.231  22.268  14.522  1.00  5.30           O  
ANISOU  306  O   GLY A  90      757    559    695    113    100   -108       O  
ATOM    307  N   THR A  91      47.650  23.727  16.133  1.00  4.47           N  
ANISOU  307  N   THR A  91      599    533    564     44     29    -13       N  
ATOM    308  CA  THR A  91      47.488  22.698  17.144  1.00  5.08           C  
ANISOU  308  CA  THR A  91      728    552    648     84     71     14       C  
ATOM    309  C   THR A  91      46.227  23.006  17.947  1.00  4.89           C  
ANISOU  309  C   THR A  91      691    446    720     54     65     39       C  
ATOM    310  O   THR A  91      45.848  24.161  18.123  1.00  4.88           O  
ANISOU  310  O   THR A  91      709    436    707     85     41     53       O  
ATOM    311  CB  THR A  91      48.776  22.587  17.981  1.00  5.80           C  
ANISOU  311  CB  THR A  91      754    752    696    103     64     87       C  
ATOM    312  OG1 THR A  91      48.738  21.401  18.776  1.00  7.22           O  
ANISOU  312  OG1 THR A  91      846   1011    885    136     13    332       O  
ATOM    313  CG2 THR A  91      48.947  23.756  18.929  1.00  7.35           C  
ANISOU  313  CG2 THR A  91      954   1070    768    148    -66     42       C  
ATOM    314  N   ASN A  92      45.560  21.960  18.391  1.00  4.91           N  
ANISOU  314  N   ASN A  92      734    470    662     72     86    -18       N  
ATOM    315  CA  ASN A  92      44.301  22.113  19.093  1.00  5.14           C  
ANISOU  315  CA  ASN A  92      700    552    700     56     55     -2       C  
ATOM    316  C   ASN A  92      44.489  22.853  20.414  1.00  4.84           C  
ANISOU  316  C   ASN A  92      678    526    635    127     40     52       C  
ATOM    317  O   ASN A  92      45.438  22.578  21.157  1.00  5.79           O  
ANISOU  317  O   ASN A  92      832    654    714    211      7   -103       O  
ATOM    318  CB  ASN A  92      43.702  20.727  19.353  1.00  5.44           C  
ANISOU  318  CB  ASN A  92      772    533    761      0      5    -12       C  
ATOM    319  CG  ASN A  92      42.298  20.794  19.874  1.00  6.04           C  
ANISOU  319  CG  ASN A  92      868    686    738    -32    120    -38       C  
ATOM    320  OD1 ASN A  92      42.067  20.782  21.077  1.00  9.32           O  
ANISOU  320  OD1 ASN A  92      946   1827    766   -149     64   -114       O  
ATOM    321  ND2 ASN A  92      41.350  20.907  18.972  1.00  6.71           N  
ANISOU  321  ND2 ASN A  92      808    944    796    -44    -40     39       N  
ATOM    322  N   PHE A  93      43.585  23.765  20.710  1.00  5.58           N  
ANISOU  322  N   PHE A  93      811    681    628    196    -43    -54       N  
ATOM    323  CA  PHE A  93      43.744  24.595  21.888  1.00  6.28           C  
ANISOU  323  CA  PHE A  93      963    834    588    201    -12      6       C  
ATOM    324  C   PHE A  93      42.372  24.872  22.491  1.00  6.64           C  
ANISOU  324  C   PHE A  93      916   1054    553    354   -124    -30       C  
ATOM    325  O   PHE A  93      41.336  24.938  21.797  1.00 11.84           O  
ANISOU  325  O   PHE A  93     1389   2306    801    800     -6   -159       O  
ATOM    326  CB  PHE A  93      44.514  25.854  21.484  1.00  6.74           C  
ANISOU  326  CB  PHE A  93     1181    717    662    181     14     60       C  
ATOM    327  CG  PHE A  93      45.044  26.656  22.642  1.00  6.65           C  
ANISOU  327  CG  PHE A  93     1039    811    674    144    -33    107       C  
ATOM    328  CD1 PHE A  93      46.235  26.319  23.260  1.00  8.52           C  
ANISOU  328  CD1 PHE A  93     1077    981   1177    179     61    127       C  
ATOM    329  CD2 PHE A  93      44.360  27.767  23.113  1.00  6.80           C  
ANISOU  329  CD2 PHE A  93     1017    848    718     58    -75   -100       C  
ATOM    330  CE1 PHE A  93      46.720  27.067  24.325  1.00  9.10           C  
ANISOU  330  CE1 PHE A  93      986   1179   1293    -19   -240    428       C  
ATOM    331  CE2 PHE A  93      44.847  28.519  24.178  1.00  8.18           C  
ANISOU  331  CE2 PHE A  93     1112    990   1005    -40   -108    -19       C  
ATOM    332  CZ  PHE A  93      46.031  28.162  24.776  1.00  8.89           C  
ANISOU  332  CZ  PHE A  93     1195   1203    977    -71   -209     59       C  
ATOM    333  N   GLY A  94      42.300  24.959  23.791  1.00  5.27           N  
ANISOU  333  N   GLY A  94      761    787    454    128    -38     -5       N  
ATOM    334  CA  GLY A  94      41.063  25.306  24.447  1.00  5.53           C  
ANISOU  334  CA  GLY A  94      839    735    525    136     54    -41       C  
ATOM    335  C   GLY A  94      41.307  26.336  25.528  1.00  5.32           C  
ANISOU  335  C   GLY A  94      832    726    463    157     -4     27       C  
ATOM    336  O   GLY A  94      42.275  26.237  26.289  1.00  6.37           O  
ANISOU  336  O   GLY A  94     1012    887    520    314   -108    -22       O  
ATOM    337  N   ILE A  95      40.417  27.313  25.600  1.00  5.38           N  
ANISOU  337  N   ILE A  95      831    743    470    215    -16    -45       N  
ATOM    338  CA  ILE A  95      40.413  28.316  26.652  1.00  5.67           C  
ANISOU  338  CA  ILE A  95      878    759    514    144    -31    -49       C  
ATOM    339  C   ILE A  95      39.185  28.061  27.513  1.00  6.00           C  
ANISOU  339  C   ILE A  95      908    870    501    185     32   -118       C  
ATOM    340  O   ILE A  95      38.057  28.034  27.030  1.00  6.51           O  
ANISOU  340  O   ILE A  95      971    982    520    142     57    -87       O  
ATOM    341  CB  ILE A  95      40.343  29.725  26.042  1.00  6.28           C  
ANISOU  341  CB  ILE A  95      912    740    734    156    -36    -83       C  
ATOM    342  CG1 ILE A  95      41.534  29.973  25.112  1.00  7.15           C  
ANISOU  342  CG1 ILE A  95     1059    887    768    105     -5    -58       C  
ATOM    343  CG2 ILE A  95      40.270  30.771  27.132  1.00  7.90           C  
ANISOU  343  CG2 ILE A  95     1078    921   1003    146     51    -35       C  
ATOM    344  CD1 ILE A  95      41.367  31.118  24.145  1.00  8.23           C  
ANISOU  344  CD1 ILE A  95     1155   1027    945    -26    -29    -41       C  
ATOM    345  N   TYR A  96      39.433  27.859  28.798  1.00  6.44           N  
ANISOU  345  N   TYR A  96     1054    884    506     73      7    -16       N  
ATOM    346  CA  TYR A  96      38.417  27.482  29.757  1.00  7.18           C  
ANISOU  346  CA  TYR A  96     1004   1052    671     95      9    -50       C  
ATOM    347  C   TYR A  96      38.202  28.577  30.791  1.00  7.54           C  
ANISOU  347  C   TYR A  96     1138   1140    585    126    -20    -59       C  
ATOM    348  O   TYR A  96      39.158  29.130  31.312  1.00  8.77           O  
ANISOU  348  O   TYR A  96     1302   1394    634    165     23   -220       O  
ATOM    349  CB  TYR A  96      38.872  26.235  30.517  1.00  7.82           C  
ANISOU  349  CB  TYR A  96     1133   1156    682     61    108     38       C  
ATOM    350  CG  TYR A  96      38.843  24.964  29.703  1.00  7.38           C  
ANISOU  350  CG  TYR A  96     1219    939    644    169     31    143       C  
ATOM    351  CD1 TYR A  96      37.934  23.971  29.993  1.00  7.62           C  
ANISOU  351  CD1 TYR A  96     1216    947    730    268    123    105       C  
ATOM    352  CD2 TYR A  96      39.720  24.749  28.639  1.00  7.58           C  
ANISOU  352  CD2 TYR A  96     1165    999    716     78    117     97       C  
ATOM    353  CE1 TYR A  96      37.871  22.814  29.270  1.00  8.09           C  
ANISOU  353  CE1 TYR A  96     1346    887    838    164    150    155       C  
ATOM    354  CE2 TYR A  96      39.659  23.587  27.890  1.00  7.82           C  
ANISOU  354  CE2 TYR A  96     1308    852    810    260    124    155       C  
ATOM    355  CZ  TYR A  96      38.726  22.620  28.218  1.00  7.05           C  
ANISOU  355  CZ  TYR A  96     1269    792    616    279    107    108       C  
ATOM    356  OH  TYR A  96      38.628  21.447  27.518  1.00  8.76           O  
ANISOU  356  OH  TYR A  96     1733    692    902    100    262    234       O  
ATOM    357  N   LEU A  97      36.940  28.832  31.123  1.00  7.39           N  
ANISOU  357  N   LEU A  97     1149   1088    570    173     45    -91       N  
ATOM    358  CA  LEU A  97      36.602  29.617  32.301  1.00  7.48           C  
ANISOU  358  CA  LEU A  97     1223   1008    609    175      4    -70       C  
ATOM    359  C   LEU A  97      35.731  28.717  33.170  1.00  8.25           C  
ANISOU  359  C   LEU A  97     1348   1168    617    225     87    -28       C  
ATOM    360  O   LEU A  97      34.679  28.249  32.754  1.00  9.30           O  
ANISOU  360  O   LEU A  97     1550   1407    574    245    261     -4       O  
ATOM    361  CB  LEU A  97      35.855  30.893  31.933  1.00  8.20           C  
ANISOU  361  CB  LEU A  97     1342   1028    743    152    -48   -144       C  
ATOM    362  CG  LEU A  97      35.619  31.870  33.083  1.00 10.44           C  
ANISOU  362  CG  LEU A  97     1614   1236   1115    233    -57    -79       C  
ATOM    363  CD1 LEU A  97      36.893  32.376  33.661  1.00 12.92           C  
ANISOU  363  CD1 LEU A  97     1946   1433   1529    294   -138   -168       C  
ATOM    364  CD2 LEU A  97      34.813  33.035  32.587  1.00 13.72           C  
ANISOU  364  CD2 LEU A  97     2087   1508   1617    353   -156   -163       C  
ATOM    365  N   ILE A  98      36.192  28.453  34.388  1.00  9.59           N  
ANISOU  365  N   ILE A  98     1524   1364    753    215     82     15       N  
ATOM    366  CA  ILE A  98      35.572  27.483  35.291  1.00 11.31           C  
ANISOU  366  CA  ILE A  98     1691   1593   1013    175    189     56       C  
ATOM    367  C   ILE A  98      35.063  28.195  36.537  1.00 13.03           C  
ANISOU  367  C   ILE A  98     1847   1841   1262    152    167     19       C  
ATOM    368  O   ILE A  98      35.846  28.803  37.223  1.00 13.62           O  
ANISOU  368  O   ILE A  98     2159   2078    936    297    325   -152       O  
ATOM    369  CB  ILE A  98      36.626  26.432  35.705  1.00 11.51           C  
ANISOU  369  CB  ILE A  98     1724   1608   1042    195    168    122       C  
ATOM    370  CG1 ILE A  98      37.266  25.760  34.478  1.00 14.23           C  
ANISOU  370  CG1 ILE A  98     2031   1808   1564    279    203    247       C  
ATOM    371  CG2 ILE A  98      36.041  25.420  36.713  1.00 12.82           C  
ANISOU  371  CG2 ILE A  98     1986   1714   1169    119    185    127       C  
ATOM    372  CD1 ILE A  98      36.407  24.977  33.692  1.00 17.84           C  
ANISOU  372  CD1 ILE A  98     2244   2312   2221    197    219    147       C  
ATOM    373  N   ASN A  99      33.755  28.126  36.771  1.00 13.87           N  
ANISOU  373  N   ASN A  99     2019   1912   1336    138    294     21       N  
ATOM    374  CA  ASN A  99      33.124  28.671  37.963  1.00 15.86           C  
ANISOU  374  CA  ASN A  99     2175   2108   1742     87    207     28       C  
ATOM    375  C   ASN A  99      33.287  27.740  39.147  1.00 16.91           C  
ANISOU  375  C   ASN A  99     2413   2136   1874     25    186     29       C  
ATOM    376  O   ASN A  99      33.064  26.526  39.060  1.00 18.08           O  
ANISOU  376  O   ASN A  99     2732   2376   1760    -92    408    138       O  
ATOM    377  CB  ASN A  99      31.634  28.888  37.739  1.00 16.88           C  
ANISOU  377  CB  ASN A  99     2298   2218   1898     90    208    -52       C  
ATOM    378  CG  ASN A  99      30.971  29.502  38.937  1.00 18.71           C  
ANISOU  378  CG  ASN A  99     2533   2550   2025    154    281    -20       C  
ATOM    379  OD1 ASN A  99      30.409  28.800  39.777  1.00 21.30           O  
ANISOU  379  OD1 ASN A  99     3158   3203   1732    132    581   -164       O  
ATOM    380  ND2 ASN A  99      31.073  30.813  39.052  1.00 20.44           N  
ANISOU  380  ND2 ASN A  99     2942   2626   2195    310    362   -681       N  
ATOM    381  N   GLN A 100      33.694  28.340  40.249  1.00 17.83           N  
ANISOU  381  N   GLN A 100     2505   2293   1976     19    126     90       N  
ATOM    382  CA  GLN A 100      33.844  27.655  41.518  1.00 19.07           C  
ANISOU  382  CA  GLN A 100     2574   2472   2198     29     74     61       C  
ATOM    383  C   GLN A 100      33.106  28.467  42.579  1.00 19.98           C  
ANISOU  383  C   GLN A 100     2669   2583   2340     24     63     35       C  
ATOM    384  O   GLN A 100      33.696  28.935  43.547  1.00 20.42           O  
ANISOU  384  O   GLN A 100     2748   2732   2276     54     27    -10       O  
ATOM    385  CB  GLN A 100      35.326  27.532  41.833  1.00 19.00           C  
ANISOU  385  CB  GLN A 100     2587   2474   2155     53     78     32       C  
ATOM    386  CG  GLN A 100      36.072  26.694  40.803  1.00 20.95           C  
ANISOU  386  CG  GLN A 100     2791   2758   2408     79     81      1       C  
ATOM    387  CD  GLN A 100      37.569  26.712  40.988  1.00 23.06           C  
ANISOU  387  CD  GLN A 100     3053   3065   2641      9    112    -19       C  
ATOM    388  OE1 GLN A 100      38.112  27.582  41.673  1.00 25.81           O  
ANISOU  388  OE1 GLN A 100     3315   3407   3082    -64    200    -25       O  
ATOM    389  NE2 GLN A 100      38.248  25.753  40.365  1.00 24.14           N  
ANISOU  389  NE2 GLN A 100     3146   3221   2803    174    165     27       N  
ATOM    390  N   GLY A 101      31.803  28.633  42.384  1.00 21.10           N  
ANISOU  390  N   GLY A 101     2757   2719   2538     36     57      0       N  
ATOM    391  CA  GLY A 101      30.973  29.381  43.319  1.00 21.76           C  
ANISOU  391  CA  GLY A 101     2833   2809   2625     44     59    -31       C  
ATOM    392  C   GLY A 101      31.099  30.883  43.122  1.00 22.45           C  
ANISOU  392  C   GLY A 101     2950   2860   2719     40     36    -33       C  
ATOM    393  O   GLY A 101      30.743  31.399  42.061  1.00 22.91           O  
ANISOU  393  O   GLY A 101     3082   2969   2654    157     68    -92       O  
ATOM    394  N   ASP A 102      31.617  31.594  44.126  1.00 23.19           N  
ANISOU  394  N   ASP A 102     3049   2961   2800     21     36    -20       N  
ATOM    395  CA  ASP A 102      31.788  33.054  44.029  1.00 23.87           C  
ANISOU  395  CA  ASP A 102     3095   3025   2947      9     24    -19       C  
ATOM    396  C   ASP A 102      33.144  33.431  43.435  1.00 23.12           C  
ANISOU  396  C   ASP A 102     3028   2917   2840     11     38    -34       C  
ATOM    397  O   ASP A 102      33.490  34.611  43.376  1.00 23.97           O  
ANISOU  397  O   ASP A 102     3166   3004   2935     -3     68    -49       O  
ATOM    398  CB  ASP A 102      31.616  33.777  45.382  1.00 24.59           C  
ANISOU  398  CB  ASP A 102     3185   3123   3033      2     25    -19       C  
ATOM    399  CG  ASP A 102      31.047  32.897  46.460  1.00 27.28           C  
ANISOU  399  CG  ASP A 102     3476   3507   3382    -11    -57     56       C  
ATOM    400  OD1 ASP A 102      29.909  32.403  46.292  1.00 31.96           O  
ANISOU  400  OD1 ASP A 102     4029   4123   3988    -34   -130    104       O  
ATOM    401  OD2 ASP A 102      31.670  32.656  47.515  1.00 30.79           O  
ANISOU  401  OD2 ASP A 102     3993   4047   3659    104   -123    197       O  
ATOM    402  N   HIS A 103      33.911  32.430  43.012  1.00 22.02           N  
ANISOU  402  N   HIS A 103     2865   2800   2700     28     -7    -28       N  
ATOM    403  CA  HIS A 103      35.153  32.661  42.291  1.00 20.90           C  
ANISOU  403  CA  HIS A 103     2740   2706   2492     38    -29    -86       C  
ATOM    404  C   HIS A 103      35.204  31.797  41.031  1.00 19.27           C  
ANISOU  404  C   HIS A 103     2570   2510   2239     60    -42   -119       C  
ATOM    405  O   HIS A 103      34.331  30.965  40.802  1.00 18.91           O  
ANISOU  405  O   HIS A 103     2720   2524   1938    150     20   -196       O  
ATOM    406  CB  HIS A 103      36.371  32.411  43.196  1.00 21.40           C  
ANISOU  406  CB  HIS A 103     2786   2774   2567     28    -35    -79       C  
ATOM    407  CG  HIS A 103      36.353  31.089  43.900  1.00 23.28           C  
ANISOU  407  CG  HIS A 103     3066   3025   2751     53    -78    -34       C  
ATOM    408  ND1 HIS A 103      35.549  30.835  44.992  1.00 25.17           N  
ANISOU  408  ND1 HIS A 103     3466   3198   2899     42    -53     62       N  
ATOM    409  CD2 HIS A 103      37.063  29.958  43.684  1.00 25.49           C  
ANISOU  409  CD2 HIS A 103     3390   3289   3002    111     12    -17       C  
ATOM    410  CE1 HIS A 103      35.757  29.598  45.410  1.00 25.71           C  
ANISOU  410  CE1 HIS A 103     3492   3325   2950    122    -29     10       C  
ATOM    411  NE2 HIS A 103      36.668  29.043  44.630  1.00 26.20           N  
ANISOU  411  NE2 HIS A 103     3479   3397   3075    103    -51     76       N  
ATOM    412  N   GLU A 104      36.231  32.023  40.225  1.00 17.29           N  
ANISOU  412  N   GLU A 104     2383   2336   1848     74    -29   -233       N  
ATOM    413  CA  GLU A 104      36.398  31.323  38.945  1.00 16.62           C  
ANISOU  413  CA  GLU A 104     2257   2218   1839     90     -7   -190       C  
ATOM    414  C   GLU A 104      37.862  31.314  38.534  1.00 16.24           C  
ANISOU  414  C   GLU A 104     2187   2226   1755     77    -36   -198       C  
ATOM    415  O   GLU A 104      38.674  32.078  39.031  1.00 16.39           O  
ANISOU  415  O   GLU A 104     2337   2237   1652     87    -27   -442       O  
ATOM    416  CB  GLU A 104      35.565  31.995  37.846  1.00 17.03           C  
ANISOU  416  CB  GLU A 104     2298   2249   1922     92      6   -166       C  
ATOM    417  CG  GLU A 104      36.061  33.384  37.446  1.00 17.92           C  
ANISOU  417  CG  GLU A 104     2372   2362   2074     72     51   -111       C  
ATOM    418  CD  GLU A 104      35.096  34.158  36.557  1.00 20.00           C  
ANISOU  418  CD  GLU A 104     2535   2592   2472    -48     28    -35       C  
ATOM    419  OE1 GLU A 104      33.900  33.789  36.452  1.00 21.44           O  
ANISOU  419  OE1 GLU A 104     2613   2826   2708     12    -60    -34       O  
ATOM    420  OE2 GLU A 104      35.544  35.162  35.956  1.00 20.94           O  
ANISOU  420  OE2 GLU A 104     2816   2544   2596   -100    -83   -143       O  
ATOM    421  N   VAL A 105      38.184  30.479  37.558  1.00 14.06           N  
ANISOU  421  N   VAL A 105     1937   2057   1345    130    -42   -297       N  
ATOM    422  CA  VAL A 105      39.554  30.302  37.113  1.00 13.28           C  
ANISOU  422  CA  VAL A 105     1858   1907   1281    123    -69   -128       C  
ATOM    423  C   VAL A 105      39.618  30.150  35.600  1.00 11.33           C  
ANISOU  423  C   VAL A 105     1701   1623    981    194   -141   -209       C  
ATOM    424  O   VAL A 105      38.731  29.550  34.994  1.00 11.39           O  
ANISOU  424  O   VAL A 105     1849   1675    802    163   -178   -157       O  
ATOM    425  CB  VAL A 105      40.213  29.085  37.794  1.00 13.22           C  
ANISOU  425  CB  VAL A 105     1964   2112    944    142    -13    -63       C  
ATOM    426  CG1 VAL A 105      39.512  27.779  37.517  1.00 16.04           C  
ANISOU  426  CG1 VAL A 105     2149   2243   1703    244     49     76       C  
ATOM    427  CG2 VAL A 105      41.627  28.999  37.422  1.00 16.84           C  
ANISOU  427  CG2 VAL A 105     2254   2283   1859    105    -89     23       C  
ATOM    428  N   VAL A 106      40.686  30.681  35.023  1.00 10.61           N  
ANISOU  428  N   VAL A 106     1629   1518    883    138   -224   -226       N  
ATOM    429  CA  VAL A 106      40.963  30.535  33.590  1.00 10.24           C  
ANISOU  429  CA  VAL A 106     1483   1483    923    165   -125   -173       C  
ATOM    430  C   VAL A 106      42.037  29.464  33.416  1.00 10.18           C  
ANISOU  430  C   VAL A 106     1454   1494    919    197   -153   -180       C  
ATOM    431  O   VAL A 106      43.063  29.491  34.094  1.00 11.53           O  
ANISOU  431  O   VAL A 106     1636   1788    957    303   -303   -329       O  
ATOM    432  CB  VAL A 106      41.450  31.863  32.985  1.00 11.09           C  
ANISOU  432  CB  VAL A 106     1522   1526   1165    105   -140   -143       C  
ATOM    433  CG1 VAL A 106      41.789  31.708  31.521  1.00 11.92           C  
ANISOU  433  CG1 VAL A 106     1626   1503   1400    175     18     22       C  
ATOM    434  CG2 VAL A 106      40.417  32.966  33.137  1.00 13.07           C  
ANISOU  434  CG2 VAL A 106     1903   1608   1455    210    -23   -154       C  
ATOM    435  N   ARG A 107      41.799  28.513  32.520  1.00  9.45           N  
ANISOU  435  N   ARG A 107     1402   1393    792    216   -139   -165       N  
ATOM    436  CA  ARG A 107      42.738  27.431  32.247  1.00  9.04           C  
ANISOU  436  CA  ARG A 107     1321   1278    835    193    -68    -27       C  
ATOM    437  C   ARG A 107      42.893  27.256  30.746  1.00  7.69           C  
ANISOU  437  C   ARG A 107     1225   1013    681    146   -133    -44       C  
ATOM    438  O   ARG A 107      42.010  27.651  29.969  1.00  7.96           O  
ANISOU  438  O   ARG A 107     1224   1175    624    301   -169     19       O  
ATOM    439  CB  ARG A 107      42.226  26.126  32.877  1.00  9.73           C  
ANISOU  439  CB  ARG A 107     1496   1363    836    306      1    -47       C  
ATOM    440  CG  ARG A 107      42.115  26.154  34.398  1.00 12.87           C  
ANISOU  440  CG  ARG A 107     1809   1869   1212    161     53    -34       C  
ATOM    441  CD  ARG A 107      43.470  26.004  35.041  1.00 15.46           C  
ANISOU  441  CD  ARG A 107     2199   2174   1500     71      3   -157       C  
ATOM    442  NE  ARG A 107      43.418  25.960  36.499  1.00 18.29           N  
ANISOU  442  NE  ARG A 107     2493   2531   1925     18    -82    -80       N  
ATOM    443  CZ  ARG A 107      43.725  26.971  37.305  1.00 19.33           C  
ANISOU  443  CZ  ARG A 107     2662   2655   2026    -66      6    -75       C  
ATOM    444  NH1 ARG A 107      44.081  28.160  36.812  1.00 21.92           N  
ANISOU  444  NH1 ARG A 107     3057   2875   2396   -100    -51    -82       N  
ATOM    445  NH2 ARG A 107      43.643  26.809  38.623  1.00 20.68           N  
ANISOU  445  NH2 ARG A 107     2914   2876   2065     36   -141    -32       N  
ATOM    446  N   PHE A 108      44.002  26.642  30.358  1.00  6.72           N  
ANISOU  446  N   PHE A 108     1096    866    588    170   -125     36       N  
ATOM    447  CA  PHE A 108      44.342  26.451  28.953  1.00  6.30           C  
ANISOU  447  CA  PHE A 108     1008    810    575    130    -63     38       C  
ATOM    448  C   PHE A 108      44.654  24.994  28.698  1.00  6.31           C  
ANISOU  448  C   PHE A 108     1052    744    598    134   -130     84       C  
ATOM    449  O   PHE A 108      45.341  24.356  29.500  1.00  7.57           O  
ANISOU  449  O   PHE A 108     1310    872    693    172   -271    121       O  
ATOM    450  CB  PHE A 108      45.515  27.347  28.570  1.00  6.86           C  
ANISOU  450  CB  PHE A 108     1079    825    700    157   -110     45       C  
ATOM    451  CG  PHE A 108      45.228  28.792  28.811  1.00  6.48           C  
ANISOU  451  CG  PHE A 108     1128    653    680    140    -63     26       C  
ATOM    452  CD1 PHE A 108      44.420  29.487  27.931  1.00  7.32           C  
ANISOU  452  CD1 PHE A 108     1199    747    833    114    -84     24       C  
ATOM    453  CD2 PHE A 108      45.681  29.445  29.948  1.00  8.00           C  
ANISOU  453  CD2 PHE A 108     1321    851    867     92   -101    -43       C  
ATOM    454  CE1 PHE A 108      44.107  30.811  28.163  1.00  8.24           C  
ANISOU  454  CE1 PHE A 108     1243    770   1118     54   -164     76       C  
ATOM    455  CE2 PHE A 108      45.371  30.771  30.170  1.00  9.23           C  
ANISOU  455  CE2 PHE A 108     1528    915   1061    -40   -128   -123       C  
ATOM    456  CZ  PHE A 108      44.577  31.449  29.293  1.00  8.90           C  
ANISOU  456  CZ  PHE A 108     1483    748   1147     19      4    -16       C  
ATOM    457  N   ALA A 109      44.159  24.481  27.572  1.00  6.35           N  
ANISOU  457  N   ALA A 109     1064    717    629    129   -105     38       N  
ATOM    458  CA  ALA A 109      44.329  23.078  27.230  1.00  6.03           C  
ANISOU  458  CA  ALA A 109      968    692    631    104    -45     79       C  
ATOM    459  C   ALA A 109      44.941  22.919  25.860  1.00  5.82           C  
ANISOU  459  C   ALA A 109      950    677    585    137    -91     46       C  
ATOM    460  O   ALA A 109      44.664  23.676  24.928  1.00  6.89           O  
ANISOU  460  O   ALA A 109     1076    874    667    239    -49     83       O  
ATOM    461  CB  ALA A 109      43.026  22.353  27.254  1.00  6.99           C  
ANISOU  461  CB  ALA A 109     1095    827    733    103    -25     34       C  
ATOM    462  N   LYS A 110      45.758  21.876  25.744  1.00  5.87           N  
ANISOU  462  N   LYS A 110      953    620    657    119    -33     40       N  
ATOM    463  CA  LYS A 110      46.210  21.340  24.464  1.00  6.05           C  
ANISOU  463  CA  LYS A 110      900    635    763     72     27     21       C  
ATOM    464  C   LYS A 110      45.340  20.122  24.132  1.00  5.99           C  
ANISOU  464  C   LYS A 110      908    652    714    120     43     11       C  
ATOM    465  O   LYS A 110      44.358  19.851  24.815  1.00  6.73           O  
ANISOU  465  O   LYS A 110      952    815    787     54     40    -80       O  
ATOM    466  CB  LYS A 110      47.707  21.005  24.526  1.00  6.39           C  
ANISOU  466  CB  LYS A 110      897    690    840     19     67      0       C  
ATOM    467  CG  LYS A 110      48.100  20.021  25.607  1.00  7.59           C  
ANISOU  467  CG  LYS A 110     1093    788   1003     12   -107    109       C  
ATOM    468  CD  LYS A 110      49.601  19.769  25.628  1.00  9.27           C  
ANISOU  468  CD  LYS A 110     1216    949   1357     50   -191      7       C  
ATOM    469  CE  LYS A 110      49.979  18.842  26.751  1.00 12.58           C  
ANISOU  469  CE  LYS A 110     1598   1272   1910     88   -263     10       C  
ATOM    470  NZ  LYS A 110      51.442  18.589  26.775  1.00 14.24           N  
ANISOU  470  NZ  LYS A 110     1562   1375   2470    197   -760    -12       N  
ATOM    471  N   ARG A 111      45.694  19.367  23.103  1.00  6.58           N  
ANISOU  471  N   ARG A 111      958    724    815     10     59    -24       N  
ATOM    472  CA  ARG A 111      44.888  18.243  22.666  1.00  7.83           C  
ANISOU  472  CA  ARG A 111     1177    847    949    -36     20    -66       C  
ATOM    473  C   ARG A 111      44.595  17.264  23.785  1.00  7.77           C  
ANISOU  473  C   ARG A 111     1163    745   1045   -108     36   -123       C  
ATOM    474  O   ARG A 111      43.484  16.732  23.888  1.00  8.37           O  
ANISOU  474  O   ARG A 111     1101    786   1289   -152     35    -90       O  
ATOM    475  CB  ARG A 111      45.630  17.522  21.531  1.00  8.92           C  
ANISOU  475  CB  ARG A 111     1412    954   1021   -102     88   -122       C  
ATOM    476  CG  ARG A 111      45.165  16.130  21.170  1.00 11.40           C  
ANISOU  476  CG  ARG A 111     1616   1289   1424    -92    -41     14       C  
ATOM    477  CD  ARG A 111      43.858  16.171  20.472  1.00 12.12           C  
ANISOU  477  CD  ARG A 111     1537   1409   1656     38   -195    197       C  
ATOM    478  NE  ARG A 111      43.955  16.802  19.140  1.00 11.82           N  
ANISOU  478  NE  ARG A 111     1584   1403   1503    -32   -308     37       N  
ATOM    479  CZ  ARG A 111      42.902  17.211  18.428  1.00 10.37           C  
ANISOU  479  CZ  ARG A 111     1315   1311   1311     58   -164    148       C  
ATOM    480  NH1 ARG A 111      41.679  17.073  18.925  1.00 13.27           N  
ANISOU  480  NH1 ARG A 111     1502   1833   1703     12   -209    401       N  
ATOM    481  NH2 ARG A 111      43.064  17.777  17.234  1.00  9.71           N  
ANISOU  481  NH2 ARG A 111     1174   1305   1210    198   -126    -22       N  
ATOM    482  N   SER A 112      45.608  17.005  24.597  1.00  7.90           N  
ANISOU  482  N   SER A 112     1133    706   1162    -88    -19    -11       N  
ATOM    483  CA  SER A 112      45.563  15.939  25.586  1.00  8.27           C  
ANISOU  483  CA  SER A 112     1177    729   1233    -55     -1     45       C  
ATOM    484  C   SER A 112      45.229  16.353  27.002  1.00  7.90           C  
ANISOU  484  C   SER A 112     1191    668   1142     18    -56    109       C  
ATOM    485  O   SER A 112      45.206  15.493  27.868  1.00  9.49           O  
ANISOU  485  O   SER A 112     1664    661   1280     10   -176    232       O  
ATOM    486  CB  SER A 112      46.897  15.198  25.579  1.00  9.62           C  
ANISOU  486  CB  SER A 112     1342    807   1503    -14     27     65       C  
ATOM    487  OG  SER A 112      47.950  16.093  25.876  1.00 12.64           O  
ANISOU  487  OG  SER A 112     1312   1111   2380     23    -47    164       O  
ATOM    488  N   GLY A 113      44.960  17.629  27.263  1.00  7.00           N  
ANISOU  488  N   GLY A 113     1059    627    973    -81    -29    115       N  
ATOM    489  CA  GLY A 113      44.524  18.021  28.587  1.00  7.15           C  
ANISOU  489  CA  GLY A 113     1056    752    906    -18    -47    108       C  
ATOM    490  C   GLY A 113      44.823  19.451  28.915  1.00  6.24           C  
ANISOU  490  C   GLY A 113      982    619    769     23    -69    183       C  
ATOM    491  O   GLY A 113      45.505  20.161  28.178  1.00  6.75           O  
ANISOU  491  O   GLY A 113     1130    571    861    -47    -63    162       O  
ATOM    492  N   ILE A 114      44.272  19.892  30.039  1.00  6.59           N  
ANISOU  492  N   ILE A 114     1027    688    789    -28    -36    132       N  
ATOM    493  CA  ILE A 114      44.609  21.180  30.623  1.00  7.51           C  
ANISOU  493  CA  ILE A 114     1163    821    866     18    -99    118       C  
ATOM    494  C   ILE A 114      46.071  21.154  31.085  1.00  7.39           C  
ANISOU  494  C   ILE A 114     1142    758    905     17   -139    164       C  
ATOM    495  O   ILE A 114      46.553  20.159  31.643  1.00  8.44           O  
ANISOU  495  O   ILE A 114     1303    752   1150     73   -276    196       O  
ATOM    496  CB  ILE A 114      43.634  21.521  31.770  1.00  7.94           C  
ANISOU  496  CB  ILE A 114     1152    957    904     11   -112    104       C  
ATOM    497  CG1 ILE A 114      42.280  21.933  31.182  1.00  9.49           C  
ANISOU  497  CG1 ILE A 114     1297   1228   1080     20    -96    -34       C  
ATOM    498  CG2 ILE A 114      44.175  22.643  32.645  1.00  9.35           C  
ANISOU  498  CG2 ILE A 114     1377   1178    997     66   -127    -30       C  
ATOM    499  CD1 ILE A 114      41.160  22.050  32.203  1.00 11.08           C  
ANISOU  499  CD1 ILE A 114     1448   1451   1311     -2     27     12       C  
HETATM  500  N   MSE A 115      46.776  22.249  30.817  1.00  7.12           N  
ANISOU  500  N   MSE A 115     1183    677    843     35   -174    217       N  
HETATM  501  CA  MSE A 115      48.197  22.356  31.073  1.00  8.29           C  
ANISOU  501  CA  MSE A 115     1262    837   1050      0   -121    116       C  
HETATM  502  C   MSE A 115      48.520  23.012  32.399  1.00  8.40           C  
ANISOU  502  C   MSE A 115     1280    870   1041     39   -218    196       C  
HETATM  503  O   MSE A 115      47.846  23.932  32.858  1.00  8.84           O  
ANISOU  503  O   MSE A 115     1500    950    907     -5   -261    151       O  
HETATM  504  CB  MSE A 115      48.874  23.164  29.970  1.00  7.80           C  
ANISOU  504  CB  MSE A 115     1186    875    901     -3   -126     83       C  
HETATM  505  CG  MSE A 115      48.793  22.478  28.625  1.00  8.90           C  
ANISOU  505  CG  MSE A 115     1353    866   1163      7   -156     71       C  
HETATM  506 SE   MSE A 115      49.632  23.417  27.200  1.00 17.41          SE  
ANISOU  506 SE   MSE A 115     2266   2266   2082   -182    -41   -104      SE  
HETATM  507  CE  MSE A 115      48.262  24.733  26.890  1.00 11.29           C  
ANISOU  507  CE  MSE A 115     1773   1180   1335    -96   -228     -8       C  
ATOM    508  N   ASP A 116      49.598  22.540  33.015  1.00  9.01           N  
ANISOU  508  N   ASP A 116     1344    948   1130    -31   -280    185       N  
ATOM    509  CA  ASP A 116      50.231  23.259  34.090  1.00  9.89           C  
ANISOU  509  CA  ASP A 116     1403   1146   1209     -7   -295    171       C  
ATOM    510  C   ASP A 116      50.637  24.634  33.566  1.00  9.78           C  
ANISOU  510  C   ASP A 116     1349   1139   1225    -59   -264    131       C  
ATOM    511  O   ASP A 116      51.114  24.729  32.441  1.00  9.32           O  
ANISOU  511  O   ASP A 116     1394   1026   1118   -127   -354    120       O  
ATOM    512  CB  ASP A 116      51.465  22.494  34.566  1.00 11.31           C  
ANISOU  512  CB  ASP A 116     1570   1310   1416      2   -366    195       C  
ATOM    513  CG  ASP A 116      52.129  23.152  35.737  1.00 13.59           C  
ANISOU  513  CG  ASP A 116     1801   1706   1653   -130   -608    413       C  
ATOM    514  OD1 ASP A 116      51.845  22.754  36.883  1.00 20.03           O  
ANISOU  514  OD1 ASP A 116     2852   2685   2072   -560   -759    331       O  
ATOM    515  OD2 ASP A 116      52.931  24.074  35.589  1.00 15.04           O  
ANISOU  515  OD2 ASP A 116     2185   1753   1774   -199   -935    570       O  
ATOM    516  N   PRO A 117      50.465  25.691  34.358  1.00 10.22           N  
ANISOU  516  N   PRO A 117     1374   1209   1298    -45   -151     98       N  
ATOM    517  CA  PRO A 117      50.810  27.039  33.876  1.00 10.37           C  
ANISOU  517  CA  PRO A 117     1395   1216   1326    -18   -128     69       C  
ATOM    518  C   PRO A 117      52.275  27.245  33.468  1.00  9.46           C  
ANISOU  518  C   PRO A 117     1317   1104   1173     23   -148     67       C  
ATOM    519  O   PRO A 117      52.540  28.195  32.739  1.00  9.81           O  
ANISOU  519  O   PRO A 117     1408   1051   1266    -46   -232     89       O  
ATOM    520  CB  PRO A 117      50.448  27.940  35.058  1.00 11.62           C  
ANISOU  520  CB  PRO A 117     1566   1358   1488    -33    -83     39       C  
ATOM    521  CG  PRO A 117      49.481  27.171  35.833  1.00 13.84           C  
ANISOU  521  CG  PRO A 117     1807   1703   1746    -62     62    -65       C  
ATOM    522  CD  PRO A 117      49.874  25.734  35.707  1.00 11.98           C  
ANISOU  522  CD  PRO A 117     1586   1435   1529   -109    -97     18       C  
ATOM    523  N   ASN A 118      53.195  26.393  33.919  1.00  9.45           N  
ANISOU  523  N   ASN A 118     1312   1114   1165     30   -177     43       N  
ATOM    524  CA  ASN A 118      54.593  26.514  33.522  1.00  9.90           C  
ANISOU  524  CA  ASN A 118     1295   1170   1294     33   -160    -22       C  
ATOM    525  C   ASN A 118      55.027  25.540  32.428  1.00  9.61           C  
ANISOU  525  C   ASN A 118     1301   1142   1209     30   -168    -15       C  
ATOM    526  O   ASN A 118      56.213  25.429  32.133  1.00 10.66           O  
ANISOU  526  O   ASN A 118     1317   1237   1494     14   -215   -137       O  
ATOM    527  CB  ASN A 118      55.507  26.458  34.742  1.00 10.36           C  
ANISOU  527  CB  ASN A 118     1356   1255   1324      6   -170    -58       C  
ATOM    528  CG  ASN A 118      55.484  27.751  35.500  1.00 10.77           C  
ANISOU  528  CG  ASN A 118     1359   1314   1417    -31   -189   -126       C  
ATOM    529  OD1 ASN A 118      55.715  28.815  34.928  1.00 11.74           O  
ANISOU  529  OD1 ASN A 118     1549   1372   1537    -56   -292   -165       O  
ATOM    530  ND2 ASN A 118      55.193  27.678  36.782  1.00 14.19           N  
ANISOU  530  ND2 ASN A 118     2041   1776   1575   -131   -208    -85       N  
ATOM    531  N   GLU A 119      54.072  24.886  31.777  1.00  9.56           N  
ANISOU  531  N   GLU A 119     1305   1096   1232     70   -218     67       N  
ATOM    532  CA  GLU A 119      54.397  24.127  30.576  1.00  9.62           C  
ANISOU  532  CA  GLU A 119     1324   1112   1217     34   -174     41       C  
ATOM    533  C   GLU A 119      54.558  25.080  29.396  1.00  9.60           C  
ANISOU  533  C   GLU A 119     1399   1140   1105     -2   -252     21       C  
ATOM    534  O   GLU A 119      53.618  25.777  29.030  1.00  9.90           O  
ANISOU  534  O   GLU A 119     1516   1026   1220    169   -330     92       O  
ATOM    535  CB  GLU A 119      53.327  23.082  30.240  1.00  9.78           C  
ANISOU  535  CB  GLU A 119     1368   1032   1316     21   -189     81       C  
ATOM    536  CG  GLU A 119      53.690  22.332  28.961  1.00 11.09           C  
ANISOU  536  CG  GLU A 119     1547   1189   1476     30   -171     36       C  
ATOM    537  CD  GLU A 119      52.706  21.276  28.511  1.00 13.12           C  
ANISOU  537  CD  GLU A 119     1683   1301   2000    120   -169    -93       C  
ATOM    538  OE1 GLU A 119      51.808  20.897  29.276  1.00 14.30           O  
ANISOU  538  OE1 GLU A 119     1718   1426   2287     14   -238   -427       O  
ATOM    539  OE2 GLU A 119      52.853  20.804  27.364  1.00 15.19           O  
ANISOU  539  OE2 GLU A 119     1982   1604   2185   -105   -388   -312       O  
ATOM    540  N   ASN A 120      55.758  25.116  28.828  1.00 10.23           N  
ANISOU  540  N   ASN A 120     1458   1229   1199     19   -289    104       N  
ATOM    541  CA  ASN A 120      56.008  25.849  27.595  1.00 10.98           C  
ANISOU  541  CA  ASN A 120     1625   1311   1234    -89   -218     -5       C  
ATOM    542  C   ASN A 120      55.334  25.101  26.450  1.00 10.52           C  
ANISOU  542  C   ASN A 120     1609   1201   1187    -54   -267    -53       C  
ATOM    543  O   ASN A 120      55.632  23.941  26.216  1.00 12.07           O  
ANISOU  543  O   ASN A 120     1951   1157   1478     35   -513     18       O  
ATOM    544  CB  ASN A 120      57.513  25.976  27.344  1.00 12.40           C  
ANISOU  544  CB  ASN A 120     1845   1569   1297   -192   -232    -42       C  
ATOM    545  CG  ASN A 120      57.836  26.798  26.106  1.00 15.27           C  
ANISOU  545  CG  ASN A 120     2290   1660   1850   -515   -100   -140       C  
ATOM    546  OD1 ASN A 120      57.098  27.713  25.741  1.00 18.02           O  
ANISOU  546  OD1 ASN A 120     3199   1912   1736  -1134   -166    141       O  
ATOM    547  ND2 ASN A 120      58.960  26.488  25.473  1.00 18.47           N  
ANISOU  547  ND2 ASN A 120     3396   1889   1731   -739    358   -170       N  
ATOM    548  N   PHE A 121      54.407  25.762  25.768  1.00  9.08           N  
ANISOU  548  N   PHE A 121     1445   1050    952    -63   -299    -48       N  
ATOM    549  CA  PHE A 121      53.654  25.159  24.671  1.00  8.11           C  
ANISOU  549  CA  PHE A 121     1257    894    928    -28   -159    -59       C  
ATOM    550  C   PHE A 121      53.513  26.178  23.546  1.00  7.15           C  
ANISOU  550  C   PHE A 121     1087    763    865    -29   -161     -4       C  
ATOM    551  O   PHE A 121      52.587  26.996  23.509  1.00  6.94           O  
ANISOU  551  O   PHE A 121     1061    757    816    -10   -128    -61       O  
ATOM    552  CB  PHE A 121      52.304  24.691  25.182  1.00  8.53           C  
ANISOU  552  CB  PHE A 121     1438    963    838    -65   -184      7       C  
ATOM    553  CG  PHE A 121      51.474  23.991  24.154  1.00  8.50           C  
ANISOU  553  CG  PHE A 121     1332    990    905   -161    -91     52       C  
ATOM    554  CD1 PHE A 121      51.737  22.680  23.811  1.00  9.26           C  
ANISOU  554  CD1 PHE A 121     1504   1016    997   -113   -195     16       C  
ATOM    555  CD2 PHE A 121      50.403  24.632  23.549  1.00  9.28           C  
ANISOU  555  CD2 PHE A 121     1341   1258    924   -138    -80    -78       C  
ATOM    556  CE1 PHE A 121      50.958  22.022  22.872  1.00 10.37           C  
ANISOU  556  CE1 PHE A 121     1700   1118   1121   -251    -19     14       C  
ATOM    557  CE2 PHE A 121      49.628  23.973  22.610  1.00  9.99           C  
ANISOU  557  CE2 PHE A 121     1330   1573    891   -188    -24    224       C  
ATOM    558  CZ  PHE A 121      49.902  22.665  22.287  1.00  9.82           C  
ANISOU  558  CZ  PHE A 121     1436   1347    946   -442    -64    108       C  
ATOM    559  N   PHE A 122      54.482  26.143  22.648  1.00  7.02           N  
ANISOU  559  N   PHE A 122      980    781    903     39   -144     -4       N  
ATOM    560  CA  PHE A 122      54.491  26.952  21.442  1.00  6.44           C  
ANISOU  560  CA  PHE A 122      859    776    810    -23    -41     -4       C  
ATOM    561  C   PHE A 122      54.350  28.445  21.728  1.00  6.81           C  
ANISOU  561  C   PHE A 122      938    794    856    -47    -58     33       C  
ATOM    562  O   PHE A 122      53.843  29.191  20.903  1.00  8.01           O  
ANISOU  562  O   PHE A 122     1213    878    951    118    -74     32       O  
ATOM    563  CB  PHE A 122      53.418  26.473  20.464  1.00  6.74           C  
ANISOU  563  CB  PHE A 122      877    865    818    -22      4    -38       C  
ATOM    564  CG  PHE A 122      53.603  25.052  20.018  1.00  6.82           C  
ANISOU  564  CG  PHE A 122      936    826    829    -57   -104     33       C  
ATOM    565  CD1 PHE A 122      54.737  24.670  19.311  1.00  7.27           C  
ANISOU  565  CD1 PHE A 122     1075    716    968    -57    -78     63       C  
ATOM    566  CD2 PHE A 122      52.630  24.099  20.257  1.00  8.48           C  
ANISOU  566  CD2 PHE A 122     1029    991   1199    -26     71   -118       C  
ATOM    567  CE1 PHE A 122      54.907  23.372  18.890  1.00  7.87           C  
ANISOU  567  CE1 PHE A 122     1179    790   1019    -38    -25     19       C  
ATOM    568  CE2 PHE A 122      52.785  22.808  19.810  1.00 10.47           C  
ANISOU  568  CE2 PHE A 122     1376    950   1652   -214     -9   -157       C  
ATOM    569  CZ  PHE A 122      53.922  22.441  19.119  1.00 10.24           C  
ANISOU  569  CZ  PHE A 122     1459    862   1566    -27    -24   -141       C  
ATOM    570  N   GLY A 123      54.840  28.891  22.883  1.00  7.31           N  
ANISOU  570  N   GLY A 123      961    809   1004    -57    -71    -37       N  
ATOM    571  CA  GLY A 123      54.855  30.307  23.196  1.00  7.80           C  
ANISOU  571  CA  GLY A 123     1016    818   1127    -43    -83    -16       C  
ATOM    572  C   GLY A 123      53.510  30.920  23.516  1.00  7.05           C  
ANISOU  572  C   GLY A 123      979    760    938    -36    -92     29       C  
ATOM    573  O   GLY A 123      53.404  32.151  23.519  1.00  7.63           O  
ANISOU  573  O   GLY A 123     1031    715   1151     18      2     -8       O  
ATOM    574  N   TYR A 124      52.490  30.105  23.815  1.00  6.43           N  
ANISOU  574  N   TYR A 124      929    674    840    -29    -55     48       N  
ATOM    575  CA  TYR A 124      51.128  30.639  23.913  1.00  6.80           C  
ANISOU  575  CA  TYR A 124      916    715    952    -16   -115     11       C  
ATOM    576  C   TYR A 124      50.976  31.628  25.049  1.00  6.70           C  
ANISOU  576  C   TYR A 124      786    742   1017      0   -150     57       C  
ATOM    577  O   TYR A 124      50.046  32.412  25.055  1.00  7.01           O  
ANISOU  577  O   TYR A 124      802    685   1173     61   -211     56       O  
ATOM    578  CB  TYR A 124      50.072  29.528  24.050  1.00  6.55           C  
ANISOU  578  CB  TYR A 124      830    812    845    -53   -166      0       C  
ATOM    579  CG  TYR A 124      49.862  29.041  25.461  1.00  6.11           C  
ANISOU  579  CG  TYR A 124      815    719    785    -49   -209    -86       C  
ATOM    580  CD1 TYR A 124      48.870  29.605  26.262  1.00  6.80           C  
ANISOU  580  CD1 TYR A 124      983    822    775      2   -208     91       C  
ATOM    581  CD2 TYR A 124      50.652  28.044  26.000  1.00  7.29           C  
ANISOU  581  CD2 TYR A 124      918    944    905    -74    -64   -139       C  
ATOM    582  CE1 TYR A 124      48.669  29.184  27.555  1.00  7.32           C  
ANISOU  582  CE1 TYR A 124     1030    953    797    117    -29      1       C  
ATOM    583  CE2 TYR A 124      50.466  27.618  27.301  1.00  7.63           C  
ANISOU  583  CE2 TYR A 124     1199    831    866     41    -40    -48       C  
ATOM    584  CZ  TYR A 124      49.465  28.182  28.072  1.00  7.32           C  
ANISOU  584  CZ  TYR A 124     1251    838    689     75    -91    -31       C  
ATOM    585  OH  TYR A 124      49.280  27.772  29.363  1.00  8.99           O  
ANISOU  585  OH  TYR A 124     1456   1263    697    235     71    135       O  
ATOM    586  N   HIS A 125      51.896  31.605  26.006  1.00  6.71           N  
ANISOU  586  N   HIS A 125      855    718    976     67   -214    -16       N  
ATOM    587  CA  HIS A 125      51.852  32.570  27.082  1.00  7.27           C  
ANISOU  587  CA  HIS A 125      940    784   1036     52   -207      4       C  
ATOM    588  C   HIS A 125      51.810  34.008  26.575  1.00  7.37           C  
ANISOU  588  C   HIS A 125      905    760   1135    132   -266      3       C  
ATOM    589  O   HIS A 125      51.269  34.862  27.273  1.00  8.57           O  
ANISOU  589  O   HIS A 125     1174    723   1359    257   -356   -177       O  
ATOM    590  CB  HIS A 125      53.024  32.380  28.042  1.00  7.59           C  
ANISOU  590  CB  HIS A 125      953    816   1115     36   -236     18       C  
ATOM    591  CG  HIS A 125      52.969  31.081  28.758  1.00  8.71           C  
ANISOU  591  CG  HIS A 125     1107    980   1222      0   -479    -14       C  
ATOM    592  ND1 HIS A 125      53.320  29.901  28.148  1.00 11.90           N  
ANISOU  592  ND1 HIS A 125     1581   1075   1866    -32   -717     17       N  
ATOM    593  CD2 HIS A 125      52.537  30.761  29.998  1.00 10.43           C  
ANISOU  593  CD2 HIS A 125     1104   1159   1698     14   -377    149       C  
ATOM    594  CE1 HIS A 125      53.158  28.910  29.000  1.00 12.50           C  
ANISOU  594  CE1 HIS A 125     1522   1178   2047   -160   -732    367       C  
ATOM    595  NE2 HIS A 125      52.671  29.400  30.127  1.00 12.18           N  
ANISOU  595  NE2 HIS A 125     1337   1373   1918    -66   -615    578       N  
ATOM    596  N   ILE A 126      52.356  34.278  25.382  1.00  7.71           N  
ANISOU  596  N   ILE A 126      948    707   1274     63   -198     25       N  
ATOM    597  CA  ILE A 126      52.320  35.625  24.794  1.00  8.53           C  
ANISOU  597  CA  ILE A 126     1029    816   1394     66   -184     31       C  
ATOM    598  C   ILE A 126      50.874  36.118  24.576  1.00  8.32           C  
ANISOU  598  C   ILE A 126      998    819   1340     63   -152      7       C  
ATOM    599  O   ILE A 126      50.637  37.332  24.518  1.00  9.73           O  
ANISOU  599  O   ILE A 126     1189    719   1789    111   -251    107       O  
ATOM    600  CB  ILE A 126      53.146  35.657  23.465  1.00  9.65           C  
ANISOU  600  CB  ILE A 126     1071    968   1627     72    -83    139       C  
ATOM    601  CG1 ILE A 126      53.564  37.078  23.095  1.00 11.74           C  
ANISOU  601  CG1 ILE A 126     1441   1243   1773    -11   -133    146       C  
ATOM    602  CG2 ILE A 126      52.395  35.082  22.302  1.00  9.93           C  
ANISOU  602  CG2 ILE A 126     1023   1032   1716    106     67    101       C  
ATOM    603  CD1 ILE A 126      54.772  37.552  23.802  1.00 14.30           C  
ANISOU  603  CD1 ILE A 126     1835   1573   2023    -89    -68     83       C  
ATOM    604  N   LEU A 127      49.921  35.189  24.475  1.00  7.45           N  
ANISOU  604  N   LEU A 127      926    724   1179     67   -155      6       N  
ATOM    605  CA  LEU A 127      48.520  35.512  24.242  1.00  7.51           C  
ANISOU  605  CA  LEU A 127      939    857   1055     91   -144     28       C  
ATOM    606  C   LEU A 127      47.636  35.413  25.480  1.00  6.84           C  
ANISOU  606  C   LEU A 127      929    714    956    146   -193    -54       C  
ATOM    607  O   LEU A 127      46.453  35.712  25.390  1.00  7.31           O  
ANISOU  607  O   LEU A 127      833    933   1010    191   -167   -118       O  
ATOM    608  CB  LEU A 127      47.952  34.592  23.156  1.00  7.28           C  
ANISOU  608  CB  LEU A 127      859    897   1007    102    -86      4       C  
ATOM    609  CG  LEU A 127      48.616  34.673  21.772  1.00 10.63           C  
ANISOU  609  CG  LEU A 127     1348   1481   1210   -121     11     -9       C  
ATOM    610  CD1 LEU A 127      48.038  33.668  20.808  1.00 10.49           C  
ANISOU  610  CD1 LEU A 127     1246   1538   1202    160    101   -137       C  
ATOM    611  CD2 LEU A 127      48.526  36.045  21.200  1.00 13.35           C  
ANISOU  611  CD2 LEU A 127     1808   1736   1526   -102    -75    -43       C  
ATOM    612  N   ILE A 128      48.170  35.035  26.636  1.00  7.46           N  
ANISOU  612  N   ILE A 128      891    910   1033    118   -214    -59       N  
ATOM    613  CA  ILE A 128      47.315  34.801  27.794  1.00  7.64           C  
ANISOU  613  CA  ILE A 128      976    954    971    210   -222    -80       C  
ATOM    614  C   ILE A 128      46.564  36.036  28.244  1.00  8.00           C  
ANISOU  614  C   ILE A 128      989   1011   1039    159   -273    -98       C  
ATOM    615  O   ILE A 128      45.395  35.946  28.622  1.00  7.90           O  
ANISOU  615  O   ILE A 128      997   1094    908    240   -250   -167       O  
ATOM    616  CB  ILE A 128      48.113  34.172  28.965  1.00  8.29           C  
ANISOU  616  CB  ILE A 128     1085   1020   1042    149   -259    -97       C  
ATOM    617  CG1 ILE A 128      48.359  32.704  28.654  1.00  8.88           C  
ANISOU  617  CG1 ILE A 128     1093   1176   1104    191   -140    -73       C  
ATOM    618  CG2 ILE A 128      47.378  34.331  30.296  1.00  9.36           C  
ANISOU  618  CG2 ILE A 128     1269   1199   1087    307   -284    -19       C  
ATOM    619  CD1 ILE A 128      49.231  31.997  29.681  1.00  8.97           C  
ANISOU  619  CD1 ILE A 128     1293   1079   1035    171   -103     43       C  
ATOM    620  N   ASP A 129      47.204  37.195  28.238  1.00  8.51           N  
ANISOU  620  N   ASP A 129     1065    979   1186    173   -246   -178       N  
ATOM    621  CA  ASP A 129      46.471  38.393  28.669  1.00  9.49           C  
ANISOU  621  CA  ASP A 129     1216   1110   1277     95   -210   -226       C  
ATOM    622  C   ASP A 129      45.258  38.658  27.759  1.00  8.91           C  
ANISOU  622  C   ASP A 129     1109    965   1310     76   -162   -190       C  
ATOM    623  O   ASP A 129      44.168  38.989  28.229  1.00  9.24           O  
ANISOU  623  O   ASP A 129     1142   1033   1334    216   -274   -194       O  
ATOM    624  CB  ASP A 129      47.372  39.622  28.706  1.00 10.89           C  
ANISOU  624  CB  ASP A 129     1350   1246   1540    131   -243   -271       C  
ATOM    625  CG  ASP A 129      48.340  39.610  29.856  1.00 13.80           C  
ANISOU  625  CG  ASP A 129     1765   1539   1939    -72   -300   -297       C  
ATOM    626  OD1 ASP A 129      48.138  38.856  30.823  1.00 17.48           O  
ANISOU  626  OD1 ASP A 129     2298   2462   1882     75   -831   -619       O  
ATOM    627  OD2 ASP A 129      49.323  40.366  29.856  1.00 19.74           O  
ANISOU  627  OD2 ASP A 129     2156   2426   2917   -246   -730   -406       O  
ATOM    628  N   GLU A 130      45.460  38.513  26.457  1.00  8.36           N  
ANISOU  628  N   GLU A 130     1054    862   1258    134   -223   -119       N  
ATOM    629  CA  GLU A 130      44.391  38.671  25.493  1.00  8.11           C  
ANISOU  629  CA  GLU A 130     1077    823   1180    123   -166    -90       C  
ATOM    630  C   GLU A 130      43.299  37.622  25.713  1.00  6.96           C  
ANISOU  630  C   GLU A 130      964    745    935    196   -173    -89       C  
ATOM    631  O   GLU A 130      42.112  37.961  25.784  1.00  7.16           O  
ANISOU  631  O   GLU A 130      953    685   1081    219   -218   -151       O  
ATOM    632  CB  GLU A 130      44.946  38.571  24.087  1.00  9.64           C  
ANISOU  632  CB  GLU A 130     1219   1093   1348     53   -205     22       C  
ATOM    633  CG  GLU A 130      43.852  38.614  23.055  1.00 12.17           C  
ANISOU  633  CG  GLU A 130     1539   1551   1531    -64   -179    -47       C  
ATOM    634  CD  GLU A 130      44.363  38.888  21.677  1.00 16.53           C  
ANISOU  634  CD  GLU A 130     2292   2116   1870   -211   -112   -106       C  
ATOM    635  OE1 GLU A 130      44.823  40.028  21.454  1.00 19.73           O  
ANISOU  635  OE1 GLU A 130     3007   2243   2244   -301    -73   -327       O  
ATOM    636  OE2 GLU A 130      44.281  37.973  20.824  1.00 18.71           O  
ANISOU  636  OE2 GLU A 130     2725   2564   1820   -166    159   -199       O  
ATOM    637  N   PHE A 131      43.693  36.354  25.829  1.00  6.20           N  
ANISOU  637  N   PHE A 131      896    665    793    197   -145    -90       N  
ATOM    638  CA  PHE A 131      42.727  35.280  26.009  1.00  5.86           C  
ANISOU  638  CA  PHE A 131      870    677    677    177   -147    -72       C  
ATOM    639  C   PHE A 131      41.898  35.505  27.276  1.00  5.65           C  
ANISOU  639  C   PHE A 131      843    640    663    188   -192   -106       C  
ATOM    640  O   PHE A 131      40.712  35.194  27.325  1.00  6.76           O  
ANISOU  640  O   PHE A 131      904    878    785    228   -167    -86       O  
ATOM    641  CB  PHE A 131      43.431  33.935  26.173  1.00  5.88           C  
ANISOU  641  CB  PHE A 131      886    617    731    112   -192    -87       C  
ATOM    642  CG  PHE A 131      44.124  33.394  24.936  1.00  5.82           C  
ANISOU  642  CG  PHE A 131      884    676    648    129   -144    -69       C  
ATOM    643  CD1 PHE A 131      43.766  33.773  23.652  1.00  5.97           C  
ANISOU  643  CD1 PHE A 131      925    647    695    190   -185   -179       C  
ATOM    644  CD2 PHE A 131      45.111  32.440  25.076  1.00  6.62           C  
ANISOU  644  CD2 PHE A 131     1031    731    752    162   -166      6       C  
ATOM    645  CE1 PHE A 131      44.392  33.211  22.560  1.00  7.02           C  
ANISOU  645  CE1 PHE A 131     1134    828    703    174   -102   -112       C  
ATOM    646  CE2 PHE A 131      45.734  31.866  23.994  1.00  7.07           C  
ANISOU  646  CE2 PHE A 131     1047    823    814    187    -83    -50       C  
ATOM    647  CZ  PHE A 131      45.371  32.243  22.729  1.00  7.47           C  
ANISOU  647  CZ  PHE A 131     1197    917    724    144     -2   -183       C  
ATOM    648  N   THR A 132      42.555  35.965  28.331  1.00  6.76           N  
ANISOU  648  N   THR A 132      960    878    728    187   -155   -114       N  
ATOM    649  CA  THR A 132      41.902  36.153  29.618  1.00  7.15           C  
ANISOU  649  CA  THR A 132     1094    899    721    206   -179   -158       C  
ATOM    650  C   THR A 132      40.857  37.266  29.519  1.00  7.41           C  
ANISOU  650  C   THR A 132     1059    935    819    165   -203   -147       C  
ATOM    651  O   THR A 132      39.728  37.098  29.968  1.00  8.18           O  
ANISOU  651  O   THR A 132     1248    984    876    277   -210   -246       O  
ATOM    652  CB  THR A 132      42.961  36.466  30.671  1.00  8.08           C  
ANISOU  652  CB  THR A 132     1141   1079    850    244   -220   -171       C  
ATOM    653  OG1 THR A 132      43.837  35.319  30.799  1.00  9.23           O  
ANISOU  653  OG1 THR A 132     1307   1342    856    523   -286   -180       O  
ATOM    654  CG2 THR A 132      42.317  36.703  32.045  1.00  9.02           C  
ANISOU  654  CG2 THR A 132     1287   1356    784    270   -256   -156       C  
ATOM    655  N   ALA A 133      41.215  38.379  28.891  1.00  7.29           N  
ANISOU  655  N   ALA A 133     1005    873    889    205   -189   -176       N  
ATOM    656  CA  ALA A 133      40.238  39.447  28.691  1.00  7.46           C  
ANISOU  656  CA  ALA A 133     1002    897    936    180   -166   -165       C  
ATOM    657  C   ALA A 133      39.079  38.962  27.828  1.00  7.25           C  
ANISOU  657  C   ALA A 133      975    857    921    206   -173   -169       C  
ATOM    658  O   ALA A 133      37.913  39.251  28.110  1.00  7.60           O  
ANISOU  658  O   ALA A 133     1081    884    922    300   -187   -268       O  
ATOM    659  CB  ALA A 133      40.884  40.648  28.056  1.00  8.36           C  
ANISOU  659  CB  ALA A 133     1050    952   1173    154   -172   -236       C  
ATOM    660  N   GLN A 134      39.407  38.205  26.784  1.00  6.26           N  
ANISOU  660  N   GLN A 134      889    744    744    221   -140   -144       N  
ATOM    661  CA  GLN A 134      38.394  37.702  25.859  1.00  6.28           C  
ANISOU  661  CA  GLN A 134      834    761    790    164   -141   -104       C  
ATOM    662  C   GLN A 134      37.407  36.738  26.509  1.00  6.27           C  
ANISOU  662  C   GLN A 134      882    710    787    216   -118   -178       C  
ATOM    663  O   GLN A 134      36.205  36.841  26.290  1.00  6.30           O  
ANISOU  663  O   GLN A 134      886    793    713    171    -68   -167       O  
ATOM    664  CB  GLN A 134      39.060  37.054  24.649  1.00  6.43           C  
ANISOU  664  CB  GLN A 134      851    778    812    245   -121    -28       C  
ATOM    665  CG  GLN A 134      39.747  38.048  23.740  1.00  6.42           C  
ANISOU  665  CG  GLN A 134      898    704    834    196   -187    -53       C  
ATOM    666  CD  GLN A 134      40.540  37.383  22.629  1.00  6.15           C  
ANISOU  666  CD  GLN A 134      920    693    722    168   -105   -215       C  
ATOM    667  OE1 GLN A 134      41.037  36.266  22.794  1.00  7.30           O  
ANISOU  667  OE1 GLN A 134     1214    788    771    261    -54    -43       O  
ATOM    668  NE2 GLN A 134      40.687  38.079  21.495  1.00  7.31           N  
ANISOU  668  NE2 GLN A 134     1181    854    741     91   -107    -76       N  
ATOM    669  N   ILE A 135      37.909  35.763  27.259  1.00  6.39           N  
ANISOU  669  N   ILE A 135      927    746    754    201   -143    -81       N  
ATOM    670  CA  ILE A 135      37.024  34.747  27.817  1.00  6.48           C  
ANISOU  670  CA  ILE A 135      928    745    789    213    -63   -106       C  
ATOM    671  C   ILE A 135      36.096  35.353  28.876  1.00  6.64           C  
ANISOU  671  C   ILE A 135      973    734    812    144    -53   -153       C  
ATOM    672  O   ILE A 135      34.943  34.951  28.996  1.00  7.17           O  
ANISOU  672  O   ILE A 135     1074    838    812    201    -87   -119       O  
ATOM    673  CB  ILE A 135      37.833  33.529  28.330  1.00  6.63           C  
ANISOU  673  CB  ILE A 135      941    827    750    214    -46    -90       C  
ATOM    674  CG1 ILE A 135      36.926  32.298  28.454  1.00  7.79           C  
ANISOU  674  CG1 ILE A 135     1223    840    897    233      9   -145       C  
ATOM    675  CG2 ILE A 135      38.523  33.819  29.643  1.00  7.36           C  
ANISOU  675  CG2 ILE A 135     1010    890    897    182   -125     43       C  
ATOM    676  CD1 ILE A 135      36.492  31.699  27.135  1.00  7.75           C  
ANISOU  676  CD1 ILE A 135     1172    896    874    106     10    -30       C  
ATOM    677  N   ARG A 136      36.579  36.351  29.603  1.00  7.16           N  
ANISOU  677  N   ARG A 136     1005    894    818    181    -69   -149       N  
ATOM    678  CA  ARG A 136      35.733  37.068  30.557  1.00  7.70           C  
ANISOU  678  CA  ARG A 136     1073   1010    843    162    -15   -197       C  
ATOM    679  C   ARG A 136      34.602  37.809  29.868  1.00  7.78           C  
ANISOU  679  C   ARG A 136     1041   1032    883    139     23   -233       C  
ATOM    680  O   ARG A 136      33.452  37.779  30.320  1.00  8.74           O  
ANISOU  680  O   ARG A 136     1147   1162   1009    246    -11   -256       O  
ATOM    681  CB  ARG A 136      36.586  38.024  31.387  1.00  8.82           C  
ANISOU  681  CB  ARG A 136     1204   1176    971    161    -33   -161       C  
ATOM    682  CG  ARG A 136      37.486  37.287  32.364  1.00 11.28           C  
ANISOU  682  CG  ARG A 136     1388   1542   1353     60    -16   -210       C  
ATOM    683  CD  ARG A 136      38.308  38.210  33.240  1.00 16.68           C  
ANISOU  683  CD  ARG A 136     2165   2152   2019     94    -75   -203       C  
ATOM    684  NE  ARG A 136      39.379  37.515  33.958  1.00 19.66           N  
ANISOU  684  NE  ARG A 136     2454   2804   2211    114    -80   -241       N  
ATOM    685  CZ  ARG A 136      39.225  36.603  34.933  1.00 25.21           C  
ANISOU  685  CZ  ARG A 136     3076   3376   3126     43    -45   -129       C  
ATOM    686  NH1 ARG A 136      38.026  36.220  35.366  1.00 26.61           N  
ANISOU  686  NH1 ARG A 136     3299   3547   3261    -68    -26   -162       N  
ATOM    687  NH2 ARG A 136      40.308  36.055  35.490  1.00 27.27           N  
ANISOU  687  NH2 ARG A 136     3340   3615   3404    139     -1    -91       N  
ATOM    688  N   ILE A 137      34.923  38.447  28.753  1.00  7.28           N  
ANISOU  688  N   ILE A 137     1010    884    871    235    -35   -225       N  
ATOM    689  CA  ILE A 137      33.910  39.150  27.977  1.00  7.52           C  
ANISOU  689  CA  ILE A 137      976    918    962    252    -71   -209       C  
ATOM    690  C   ILE A 137      32.882  38.165  27.436  1.00  7.82           C  
ANISOU  690  C   ILE A 137      994   1041    935    257    -59   -268       C  
ATOM    691  O   ILE A 137      31.678  38.419  27.509  1.00  8.16           O  
ANISOU  691  O   ILE A 137     1065   1029   1004    364   -125   -241       O  
ATOM    692  CB  ILE A 137      34.570  39.969  26.861  1.00  7.44           C  
ANISOU  692  CB  ILE A 137      930    857   1039    268   -161   -280       C  
ATOM    693  CG1 ILE A 137      35.288  41.175  27.473  1.00  8.23           C  
ANISOU  693  CG1 ILE A 137     1182    868   1075    232   -274   -215       C  
ATOM    694  CG2 ILE A 137      33.541  40.430  25.819  1.00  8.01           C  
ANISOU  694  CG2 ILE A 137     1162    855   1025    149   -190   -232       C  
ATOM    695  CD1 ILE A 137      36.288  41.802  26.581  1.00  8.69           C  
ANISOU  695  CD1 ILE A 137     1260    737   1303    135   -376   -266       C  
ATOM    696  N   LEU A 138      33.341  37.031  26.914  1.00  7.13           N  
ANISOU  696  N   LEU A 138      948    865    896    207    -40   -198       N  
ATOM    697  CA  LEU A 138      32.428  36.052  26.362  1.00  6.77           C  
ANISOU  697  CA  LEU A 138      882    899    790    199    -22   -162       C  
ATOM    698  C   LEU A 138      31.484  35.537  27.444  1.00  7.24           C  
ANISOU  698  C   LEU A 138      942    974    834    213    -39   -209       C  
ATOM    699  O   LEU A 138      30.280  35.402  27.221  1.00  7.64           O  
ANISOU  699  O   LEU A 138      965   1126    809    239     27   -263       O  
ATOM    700  CB  LEU A 138      33.222  34.901  25.751  1.00  6.43           C  
ANISOU  700  CB  LEU A 138      858    899    685    199    -45   -123       C  
ATOM    701  CG  LEU A 138      32.372  33.769  25.143  1.00  6.81           C  
ANISOU  701  CG  LEU A 138      927    879    780    159     40   -161       C  
ATOM    702  CD1 LEU A 138      31.374  34.259  24.092  1.00  7.37           C  
ANISOU  702  CD1 LEU A 138      979    930    891    145    -84   -103       C  
ATOM    703  CD2 LEU A 138      33.283  32.694  24.548  1.00  7.04           C  
ANISOU  703  CD2 LEU A 138     1021    887    766    116     54   -197       C  
ATOM    704  N   ASN A 139      32.022  35.227  28.615  1.00  7.69           N  
ANISOU  704  N   ASN A 139      990   1016    913    249     29   -185       N  
ATOM    705  CA  ASN A 139      31.179  34.725  29.696  1.00  8.88           C  
ANISOU  705  CA  ASN A 139     1173   1186   1012    204     22    -88       C  
ATOM    706  C   ASN A 139      30.121  35.733  30.110  1.00  8.26           C  
ANISOU  706  C   ASN A 139     1054   1174    907    167     58   -117       C  
ATOM    707  O   ASN A 139      28.970  35.381  30.359  1.00  8.97           O  
ANISOU  707  O   ASN A 139     1168   1339    899    215     50   -140       O  
ATOM    708  CB  ASN A 139      32.006  34.325  30.910  1.00 10.53           C  
ANISOU  708  CB  ASN A 139     1375   1394   1229    271     51    -31       C  
ATOM    709  CG  ASN A 139      31.258  33.343  31.811  1.00 13.85           C  
ANISOU  709  CG  ASN A 139     1751   2062   1449    361     64    100       C  
ATOM    710  OD1 ASN A 139      30.800  32.294  31.358  1.00 20.46           O  
ANISOU  710  OD1 ASN A 139     2758   2619   2394    123    682    542       O  
ATOM    711  ND2 ASN A 139      31.112  33.694  33.074  1.00 20.27           N  
ANISOU  711  ND2 ASN A 139     2291   3187   2224    553    121    220       N  
ATOM    712  N   ASP A 140      30.510  36.993  30.192  1.00  8.25           N  
ANISOU  712  N   ASP A 140     1059   1174    902    242     64   -140       N  
ATOM    713  CA  ASP A 140      29.551  38.021  30.568  1.00  8.96           C  
ANISOU  713  CA  ASP A 140     1146   1155   1100    170     37   -180       C  
ATOM    714  C   ASP A 140      28.439  38.145  29.539  1.00  9.09           C  
ANISOU  714  C   ASP A 140     1122   1216   1112    171      1   -166       C  
ATOM    715  O   ASP A 140      27.270  38.315  29.896  1.00  9.58           O  
ANISOU  715  O   ASP A 140     1123   1333   1183    271      5   -355       O  
ATOM    716  CB  ASP A 140      30.250  39.360  30.716  1.00  9.99           C  
ANISOU  716  CB  ASP A 140     1231   1293   1269    160    -25   -140       C  
ATOM    717  CG  ASP A 140      30.991  39.498  32.014  1.00 13.07           C  
ANISOU  717  CG  ASP A 140     1784   1496   1686    106    -52    -50       C  
ATOM    718  OD1 ASP A 140      30.782  38.718  32.969  1.00 15.69           O  
ANISOU  718  OD1 ASP A 140     2163   2109   1690     34   -249   -128       O  
ATOM    719  OD2 ASP A 140      31.827  40.389  32.153  1.00 17.33           O  
ANISOU  719  OD2 ASP A 140     2204   1925   2455   -190   -365   -325       O  
ATOM    720  N   LEU A 141      28.796  38.069  28.259  1.00  8.34           N  
ANISOU  720  N   LEU A 141     1011   1180    977    292    -12   -217       N  
ATOM    721  CA  LEU A 141      27.812  38.139  27.185  1.00  8.76           C  
ANISOU  721  CA  LEU A 141     1087   1213   1026    243    -19   -161       C  
ATOM    722  C   LEU A 141      26.823  37.001  27.301  1.00  8.61           C  
ANISOU  722  C   LEU A 141     1060   1255    953    263    -37   -178       C  
ATOM    723  O   LEU A 141      25.617  37.197  27.147  1.00  9.66           O  
ANISOU  723  O   LEU A 141     1096   1453   1121    378    -44   -343       O  
ATOM    724  CB  LEU A 141      28.499  38.093  25.821  1.00  9.23           C  
ANISOU  724  CB  LEU A 141     1102   1335   1069    219   -157   -126       C  
ATOM    725  CG  LEU A 141      29.283  39.331  25.386  1.00 11.63           C  
ANISOU  725  CG  LEU A 141     1490   1619   1306    209   -148    -50       C  
ATOM    726  CD1 LEU A 141      30.194  39.025  24.181  1.00 13.38           C  
ANISOU  726  CD1 LEU A 141     1771   1829   1482    -32   -113    175       C  
ATOM    727  CD2 LEU A 141      28.340  40.495  25.079  1.00 15.02           C  
ANISOU  727  CD2 LEU A 141     1973   1769   1965    147    -42     -3       C  
ATOM    728  N   LEU A 142      27.332  35.794  27.521  1.00  7.77           N  
ANISOU  728  N   LEU A 142      962   1149    841    285     42   -217       N  
ATOM    729  CA  LEU A 142      26.488  34.618  27.594  1.00  8.97           C  
ANISOU  729  CA  LEU A 142     1106   1236   1066    155     -4   -128       C  
ATOM    730  C   LEU A 142      25.557  34.697  28.794  1.00  8.89           C  
ANISOU  730  C   LEU A 142     1069   1265   1042     94     39   -117       C  
ATOM    731  O   LEU A 142      24.374  34.409  28.687  1.00  9.44           O  
ANISOU  731  O   LEU A 142      987   1395   1203    191     74   -190       O  
ATOM    732  CB  LEU A 142      27.364  33.370  27.690  1.00  9.17           C  
ANISOU  732  CB  LEU A 142     1106   1201   1176    162    110   -143       C  
ATOM    733  CG  LEU A 142      28.029  32.967  26.382  1.00 12.44           C  
ANISOU  733  CG  LEU A 142     1544   1584   1596    100     50    -30       C  
ATOM    734  CD1 LEU A 142      29.111  31.926  26.614  1.00 13.30           C  
ANISOU  734  CD1 LEU A 142     1611   1711   1729    164    142     -6       C  
ATOM    735  CD2 LEU A 142      27.012  32.481  25.363  1.00 14.86           C  
ANISOU  735  CD2 LEU A 142     1864   1925   1855    106     53   -209       C  
ATOM    736  N   LYS A 143      26.086  35.071  29.945  1.00  8.72           N  
ANISOU  736  N   LYS A 143      961   1298   1051     96     37   -152       N  
ATOM    737  CA  LYS A 143      25.247  35.179  31.129  1.00  9.43           C  
ANISOU  737  CA  LYS A 143     1066   1342   1175     61     92    -77       C  
ATOM    738  C   LYS A 143      24.135  36.190  30.945  1.00  9.12           C  
ANISOU  738  C   LYS A 143      984   1354   1128     68     80   -143       C  
ATOM    739  O   LYS A 143      22.986  35.947  31.315  1.00  9.79           O  
ANISOU  739  O   LYS A 143      988   1465   1265    111    167   -130       O  
ATOM    740  CB  LYS A 143      26.070  35.573  32.358  1.00 10.87           C  
ANISOU  740  CB  LYS A 143     1179   1619   1331     89     93    -91       C  
ATOM    741  CG  LYS A 143      26.927  34.449  32.895  1.00 12.50           C  
ANISOU  741  CG  LYS A 143     1533   1824   1388     50     20    -26       C  
ATOM    742  CD  LYS A 143      27.774  34.808  34.134  1.00 17.01           C  
ANISOU  742  CD  LYS A 143     2088   2316   2057     95   -169     48       C  
ATOM    743  CE  LYS A 143      27.219  35.909  35.031  1.00 20.35           C  
ANISOU  743  CE  LYS A 143     2584   2720   2428      4   -127    -29       C  
ATOM    744  NZ  LYS A 143      28.290  36.404  35.958  1.00 22.49           N  
ANISOU  744  NZ  LYS A 143     2937   2991   2614    -99   -245   -156       N  
ATOM    745  N   GLN A 144      24.477  37.338  30.380  1.00  9.33           N  
ANISOU  745  N   GLN A 144     1043   1271   1229    176    127   -218       N  
ATOM    746  CA  GLN A 144      23.484  38.386  30.173  1.00  9.90           C  
ANISOU  746  CA  GLN A 144     1155   1292   1312    188     87   -184       C  
ATOM    747  C   GLN A 144      22.413  37.949  29.185  1.00  9.92           C  
ANISOU  747  C   GLN A 144     1078   1385   1304    201    103   -194       C  
ATOM    748  O   GLN A 144      21.219  38.112  29.441  1.00 10.62           O  
ANISOU  748  O   GLN A 144     1012   1630   1392    317    161   -325       O  
ATOM    749  CB  GLN A 144      24.165  39.648  29.681  1.00 11.12           C  
ANISOU  749  CB  GLN A 144     1309   1399   1515    184     52   -207       C  
ATOM    750  CG  GLN A 144      23.252  40.863  29.651  1.00 16.66           C  
ANISOU  750  CG  GLN A 144     2012   2066   2250     86     28    -87       C  
ATOM    751  CD  GLN A 144      23.946  42.124  29.165  1.00 22.47           C  
ANISOU  751  CD  GLN A 144     2699   2831   3005    195    227     -4       C  
ATOM    752  OE1 GLN A 144      25.029  42.061  28.571  1.00 28.37           O  
ANISOU  752  OE1 GLN A 144     3389   3601   3789    163    316     46       O  
ATOM    753  NE2 GLN A 144      23.322  43.274  29.408  1.00 27.03           N  
ANISOU  753  NE2 GLN A 144     3252   3437   3579    208    129     27       N  
ATOM    754  N   LYS A 145      22.831  37.399  28.051  1.00  9.15           N  
ANISOU  754  N   LYS A 145     1060   1301   1112    139     66   -192       N  
ATOM    755  CA  LYS A 145      21.873  37.049  27.008  1.00  9.55           C  
ANISOU  755  CA  LYS A 145     1132   1332   1164    156     23    -43       C  
ATOM    756  C   LYS A 145      20.959  35.892  27.422  1.00  9.49           C  
ANISOU  756  C   LYS A 145     1164   1314   1124    123    -50     11       C  
ATOM    757  O   LYS A 145      19.757  35.942  27.177  1.00 10.14           O  
ANISOU  757  O   LYS A 145     1206   1380   1266    194   -106     81       O  
ATOM    758  CB  LYS A 145      22.595  36.735  25.699  1.00 10.92           C  
ANISOU  758  CB  LYS A 145     1366   1550   1233    111     15    -53       C  
ATOM    759  CG  LYS A 145      23.169  37.962  25.020  1.00 14.73           C  
ANISOU  759  CG  LYS A 145     1803   1985   1809    121     59    -49       C  
ATOM    760  CD  LYS A 145      22.061  38.815  24.385  1.00 20.01           C  
ANISOU  760  CD  LYS A 145     2493   2593   2517     78    122     65       C  
ATOM    761  CE  LYS A 145      22.383  39.270  22.975  1.00 23.04           C  
ANISOU  761  CE  LYS A 145     2886   2963   2905     20      2     32       C  
ATOM    762  NZ  LYS A 145      21.226  39.984  22.373  1.00 24.54           N  
ANISOU  762  NZ  LYS A 145     2974   3091   3259     -4    -10     42       N  
ATOM    763  N   TYR A 146      21.526  34.871  28.057  1.00  9.20           N  
ANISOU  763  N   TYR A 146     1065   1160   1268    145    -77     31       N  
ATOM    764  CA  TYR A 146      20.797  33.655  28.402  1.00  9.85           C  
ANISOU  764  CA  TYR A 146     1162   1262   1318     78   -141     36       C  
ATOM    765  C   TYR A 146      20.220  33.676  29.806  1.00  9.54           C  
ANISOU  765  C   TYR A 146     1083   1241   1298     17   -142     61       C  
ATOM    766  O   TYR A 146      19.592  32.711  30.224  1.00 10.17           O  
ANISOU  766  O   TYR A 146     1163   1369   1332    -73   -249    166       O  
ATOM    767  CB  TYR A 146      21.712  32.449  28.204  1.00 10.46           C  
ANISOU  767  CB  TYR A 146     1155   1331   1489    169   -223     65       C  
ATOM    768  CG  TYR A 146      21.706  32.017  26.793  1.00 12.50           C  
ANISOU  768  CG  TYR A 146     1508   1450   1789    250   -298     58       C  
ATOM    769  CD1 TYR A 146      20.689  31.196  26.327  1.00 13.87           C  
ANISOU  769  CD1 TYR A 146     1512   1755   2003    297   -288   -340       C  
ATOM    770  CD2 TYR A 146      22.652  32.468  25.904  1.00 13.89           C  
ANISOU  770  CD2 TYR A 146     1901   1620   1755    152   -200    -78       C  
ATOM    771  CE1 TYR A 146      20.622  30.791  25.045  1.00 17.29           C  
ANISOU  771  CE1 TYR A 146     2256   2171   2139    317   -319   -203       C  
ATOM    772  CE2 TYR A 146      22.596  32.067  24.577  1.00 16.58           C  
ANISOU  772  CE2 TYR A 146     2421   2007   1870    169   -257    -30       C  
ATOM    773  CZ  TYR A 146      21.550  31.230  24.158  1.00 14.69           C  
ANISOU  773  CZ  TYR A 146     2195   1796   1590    302   -330   -265       C  
ATOM    774  OH  TYR A 146      21.427  30.773  22.869  1.00 20.44           O  
ANISOU  774  OH  TYR A 146     2925   2664   2178    500   -350   -390       O  
ATOM    775  N   GLY A 147      20.382  34.783  30.533  1.00  9.87           N  
ANISOU  775  N   GLY A 147     1170   1332   1247     64    -39    -27       N  
ATOM    776  CA  GLY A 147      19.760  34.911  31.843  1.00 11.72           C  
ANISOU  776  CA  GLY A 147     1381   1589   1482    -21    -11     32       C  
ATOM    777  C   GLY A 147      20.317  33.930  32.860  1.00 11.96           C  
ANISOU  777  C   GLY A 147     1387   1678   1479    -32     12    105       C  
ATOM    778  O   GLY A 147      19.573  33.338  33.645  1.00 14.02           O  
ANISOU  778  O   GLY A 147     1488   2116   1723     13     -9    351       O  
ATOM    779  N   LEU A 148      21.634  33.755  32.833  1.00 12.33           N  
ANISOU  779  N   LEU A 148     1481   1704   1498     45    -57    124       N  
ATOM    780  CA  LEU A 148      22.315  32.805  33.699  1.00 13.21           C  
ANISOU  780  CA  LEU A 148     1637   1783   1598     -7    -45     92       C  
ATOM    781  C   LEU A 148      23.043  33.542  34.822  1.00 13.34           C  
ANISOU  781  C   LEU A 148     1670   1912   1485     37      0     46       C  
ATOM    782  O   LEU A 148      23.757  34.504  34.578  1.00 14.39           O  
ANISOU  782  O   LEU A 148     1863   2164   1440    -70    -52    115       O  
ATOM    783  CB  LEU A 148      23.308  32.007  32.874  1.00 13.24           C  
ANISOU  783  CB  LEU A 148     1638   1742   1649     25   -128     39       C  
ATOM    784  CG  LEU A 148      22.738  31.345  31.623  1.00 13.77           C  
ANISOU  784  CG  LEU A 148     1783   1740   1707      5   -232     88       C  
ATOM    785  CD1 LEU A 148      23.872  30.706  30.851  1.00 14.42           C  
ANISOU  785  CD1 LEU A 148     1950   1766   1763     55   -258     36       C  
ATOM    786  CD2 LEU A 148      21.679  30.327  31.985  1.00 15.46           C  
ANISOU  786  CD2 LEU A 148     1824   1926   2123     94   -174    100       C  
ATOM    787  N   SER A 149      22.851  33.110  36.065  1.00 14.64           N  
ANISOU  787  N   SER A 149     1824   2091   1644     28     56      8       N  
ATOM    788  CA  SER A 149      23.582  33.722  37.180  1.00 15.91           C  
ANISOU  788  CA  SER A 149     2025   2193   1824     68     71    -74       C  
ATOM    789  C   SER A 149      25.016  33.220  37.239  1.00 15.74           C  
ANISOU  789  C   SER A 149     2026   2166   1786     69     28    -75       C  
ATOM    790  O   SER A 149      25.906  33.933  37.695  1.00 16.72           O  
ANISOU  790  O   SER A 149     2079   2355   1917    137     31   -236       O  
ATOM    791  CB  SER A 149      22.890  33.453  38.519  1.00 16.52           C  
ANISOU  791  CB  SER A 149     2113   2315   1849     68    114    -58       C  
ATOM    792  OG  SER A 149      22.665  32.072  38.720  1.00 20.31           O  
ANISOU  792  OG  SER A 149     2682   2906   2129    130    392     -4       O  
ATOM    793  N   ARG A 150      25.221  31.999  36.748  1.00 15.50           N  
ANISOU  793  N   ARG A 150     2008   2188   1694    145     47   -118       N  
ATOM    794  CA  ARG A 150      26.490  31.295  36.843  1.00 16.14           C  
ANISOU  794  CA  ARG A 150     2073   2187   1872     90     25   -114       C  
ATOM    795  C   ARG A 150      26.639  30.363  35.652  1.00 14.93           C  
ANISOU  795  C   ARG A 150     1872   2105   1695     84     72   -179       C  
ATOM    796  O   ARG A 150      25.674  29.747  35.218  1.00 15.33           O  
ANISOU  796  O   ARG A 150     1783   2254   1786     95    161   -213       O  
ATOM    797  CB  ARG A 150      26.466  30.468  38.126  1.00 17.63           C  
ANISOU  797  CB  ARG A 150     2311   2338   2049    141      2    -95       C  
ATOM    798  CG  ARG A 150      27.762  29.931  38.658  1.00 21.93           C  
ANISOU  798  CG  ARG A 150     2832   2766   2733     47     51    -66       C  
ATOM    799  CD  ARG A 150      27.513  28.940  39.794  1.00 25.74           C  
ANISOU  799  CD  ARG A 150     3312   3255   3210      4      4     -1       C  
ATOM    800  NE  ARG A 150      26.772  27.784  39.287  1.00 29.19           N  
ANISOU  800  NE  ARG A 150     3770   3599   3719    -18      2     -7       N  
ATOM    801  CZ  ARG A 150      27.311  26.636  38.869  1.00 31.21           C  
ANISOU  801  CZ  ARG A 150     3973   3915   3969      5     46    -27       C  
ATOM    802  NH1 ARG A 150      28.625  26.420  38.917  1.00 31.45           N  
ANISOU  802  NH1 ARG A 150     4035   3979   3934    -26     88     18       N  
ATOM    803  NH2 ARG A 150      26.515  25.677  38.414  1.00 32.28           N  
ANISOU  803  NH2 ARG A 150     4139   4069   4056    -20      2    -57       N  
ATOM    804  N   VAL A 151      27.867  30.218  35.170  1.00 13.94           N  
ANISOU  804  N   VAL A 151     1731   1999   1564     72    105   -211       N  
ATOM    805  CA  VAL A 151      28.190  29.245  34.131  1.00 13.24           C  
ANISOU  805  CA  VAL A 151     1730   1830   1470    106    103    -81       C  
ATOM    806  C   VAL A 151      29.282  28.382  34.721  1.00 13.11           C  
ANISOU  806  C   VAL A 151     1733   1840   1406    121    192     -9       C  
ATOM    807  O   VAL A 151      30.386  28.861  34.915  1.00 14.71           O  
ANISOU  807  O   VAL A 151     1880   2189   1517    141    157    201       O  
ATOM    808  CB  VAL A 151      28.658  29.931  32.811  1.00 13.33           C  
ANISOU  808  CB  VAL A 151     1712   1843   1508    109     82    -70       C  
ATOM    809  CG1 VAL A 151      29.171  28.898  31.808  1.00 13.35           C  
ANISOU  809  CG1 VAL A 151     1903   1807   1361    209    172     37       C  
ATOM    810  CG2 VAL A 151      27.533  30.745  32.208  1.00 14.29           C  
ANISOU  810  CG2 VAL A 151     1816   1950   1661    101     68    -50       C  
ATOM    811  N   GLY A 152      28.970  27.123  35.014  1.00 12.98           N  
ANISOU  811  N   GLY A 152     1688   1855   1388    117    296      7       N  
ATOM    812  CA  GLY A 152      29.930  26.217  35.624  1.00 12.76           C  
ANISOU  812  CA  GLY A 152     1703   1827   1317    102    274     67       C  
ATOM    813  C   GLY A 152      31.217  26.079  34.810  1.00 11.91           C  
ANISOU  813  C   GLY A 152     1698   1717   1111    128    329    113       C  
ATOM    814  O   GLY A 152      32.314  26.148  35.350  1.00 12.35           O  
ANISOU  814  O   GLY A 152     1866   1862    964    235    418    190       O  
ATOM    815  N   ARG A 153      31.089  25.903  33.500  1.00 10.91           N  
ANISOU  815  N   ARG A 153     1489   1655   1001    146    369    130       N  
ATOM    816  CA  ARG A 153      32.245  25.756  32.624  1.00  9.81           C  
ANISOU  816  CA  ARG A 153     1337   1372   1016    114    299     99       C  
ATOM    817  C   ARG A 153      31.927  26.335  31.268  1.00  8.79           C  
ANISOU  817  C   ARG A 153     1242   1240    858     82    201     80       C  
ATOM    818  O   ARG A 153      30.934  25.977  30.666  1.00  9.93           O  
ANISOU  818  O   ARG A 153     1416   1430    926    -10    346    203       O  
ATOM    819  CB  ARG A 153      32.551  24.291  32.430  1.00 11.43           C  
ANISOU  819  CB  ARG A 153     1428   1533   1382    118    258    118       C  
ATOM    820  CG  ARG A 153      33.448  23.672  33.433  1.00 14.18           C  
ANISOU  820  CG  ARG A 153     1884   1923   1579     59    242    113       C  
ATOM    821  CD  ARG A 153      34.202  22.494  32.854  1.00 15.21           C  
ANISOU  821  CD  ARG A 153     1975   1883   1922    325    -67     34       C  
ATOM    822  NE  ARG A 153      33.289  21.370  32.815  1.00 14.87           N  
ANISOU  822  NE  ARG A 153     2082   1743   1823    422    -38    100       N  
ATOM    823  CZ  ARG A 153      33.487  20.223  32.189  1.00 14.70           C  
ANISOU  823  CZ  ARG A 153     2101   1803   1680    306     16     40       C  
ATOM    824  NH1 ARG A 153      34.570  20.005  31.461  1.00 14.98           N  
ANISOU  824  NH1 ARG A 153     1979   1849   1861    239     57     91       N  
ATOM    825  NH2 ARG A 153      32.560  19.289  32.289  1.00 14.65           N  
ANISOU  825  NH2 ARG A 153     2059   1712   1793    272    153     67       N  
ATOM    826  N   LEU A 154      32.793  27.225  30.811  1.00  7.68           N  
ANISOU  826  N   LEU A 154     1164   1036    716     58    180     57       N  
ATOM    827  CA  LEU A 154      32.731  27.797  29.465  1.00  7.08           C  
ANISOU  827  CA  LEU A 154     1099   1005    585    109    158     17       C  
ATOM    828  C   LEU A 154      33.976  27.334  28.740  1.00  6.84           C  
ANISOU  828  C   LEU A 154     1046    991    560     64    156     22       C  
ATOM    829  O   LEU A 154      35.084  27.477  29.252  1.00  7.39           O  
ANISOU  829  O   LEU A 154     1105   1165    536    156    189    -99       O  
ATOM    830  CB  LEU A 154      32.725  29.319  29.560  1.00  7.50           C  
ANISOU  830  CB  LEU A 154     1193   1014    642     62    211     70       C  
ATOM    831  CG  LEU A 154      32.873  30.090  28.246  1.00  7.93           C  
ANISOU  831  CG  LEU A 154     1275   1002    733    134    177     36       C  
ATOM    832  CD1 LEU A 154      31.716  29.780  27.296  1.00  8.71           C  
ANISOU  832  CD1 LEU A 154     1378   1074    855    158    133    103       C  
ATOM    833  CD2 LEU A 154      32.968  31.599  28.534  1.00  9.02           C  
ANISOU  833  CD2 LEU A 154     1334   1079   1014     83     79     42       C  
ATOM    834  N   VAL A 155      33.809  26.791  27.538  1.00  6.03           N  
ANISOU  834  N   VAL A 155      930    890    471    125    197     24       N  
ATOM    835  CA  VAL A 155      34.926  26.255  26.773  1.00  5.89           C  
ANISOU  835  CA  VAL A 155      844    881    511     53    151     63       C  
ATOM    836  C   VAL A 155      34.917  26.873  25.374  1.00  5.54           C  
ANISOU  836  C   VAL A 155      771    862    469     94    192     30       C  
ATOM    837  O   VAL A 155      33.995  26.650  24.604  1.00  6.53           O  
ANISOU  837  O   VAL A 155      772   1128    581     91    130    125       O  
ATOM    838  CB  VAL A 155      34.909  24.716  26.680  1.00  6.76           C  
ANISOU  838  CB  VAL A 155     1029    904    635     98     80     85       C  
ATOM    839  CG1 VAL A 155      36.202  24.222  26.039  1.00  8.10           C  
ANISOU  839  CG1 VAL A 155     1260   1126    692    236    151     96       C  
ATOM    840  CG2 VAL A 155      34.719  24.094  28.047  1.00  7.70           C  
ANISOU  840  CG2 VAL A 155     1085   1000    838     60    212    118       C  
ATOM    841  N   LEU A 156      35.971  27.620  25.072  1.00  5.42           N  
ANISOU  841  N   LEU A 156      750    814    493     44    114     54       N  
ATOM    842  CA  LEU A 156      36.210  28.228  23.773  1.00  4.94           C  
ANISOU  842  CA  LEU A 156      694    710    470     54     90      4       C  
ATOM    843  C   LEU A 156      37.316  27.429  23.090  1.00  4.52           C  
ANISOU  843  C   LEU A 156      641    635    439     99      4     26       C  
ATOM    844  O   LEU A 156      38.484  27.506  23.490  1.00  5.44           O  
ANISOU  844  O   LEU A 156      829    710    526    139     -5    -70       O  
ATOM    845  CB  LEU A 156      36.607  29.690  23.974  1.00  5.60           C  
ANISOU  845  CB  LEU A 156      732    807    588    108     78     56       C  
ATOM    846  CG  LEU A 156      37.126  30.467  22.762  1.00  5.93           C  
ANISOU  846  CG  LEU A 156      792    804    653     67    130   -111       C  
ATOM    847  CD1 LEU A 156      36.117  30.508  21.646  1.00  7.16           C  
ANISOU  847  CD1 LEU A 156     1129    980    611    -82     57    124       C  
ATOM    848  CD2 LEU A 156      37.515  31.885  23.179  1.00  6.76           C  
ANISOU  848  CD2 LEU A 156     1002    755    809     31     63   -128       C  
ATOM    849  N   ASN A 157      36.939  26.585  22.137  1.00  4.47           N  
ANISOU  849  N   ASN A 157      588    651    458     59     74    -15       N  
ATOM    850  CA  ASN A 157      37.900  25.754  21.439  1.00  4.44           C  
ANISOU  850  CA  ASN A 157      649    568    466     68     66     19       C  
ATOM    851  C   ASN A 157      38.314  26.397  20.134  1.00  4.28           C  
ANISOU  851  C   ASN A 157      649    544    430     64     25    -33       C  
ATOM    852  O   ASN A 157      37.515  27.024  19.426  1.00  5.13           O  
ANISOU  852  O   ASN A 157      635    718    595    144     84     12       O  
ATOM    853  CB  ASN A 157      37.338  24.354  21.156  1.00  5.45           C  
ANISOU  853  CB  ASN A 157      838    690    542     19    110     61       C  
ATOM    854  CG  ASN A 157      37.386  23.438  22.362  1.00  6.41           C  
ANISOU  854  CG  ASN A 157     1076    641    718     47    147      9       C  
ATOM    855  OD1 ASN A 157      36.355  23.029  22.888  1.00  7.57           O  
ANISOU  855  OD1 ASN A 157     1211    775    888    -13    142    212       O  
ATOM    856  ND2 ASN A 157      38.584  23.089  22.788  1.00  7.23           N  
ANISOU  856  ND2 ASN A 157     1130    693    921    124     26    144       N  
ATOM    857  N   GLY A 158      39.575  26.223  19.792  1.00  4.11           N  
ANISOU  857  N   GLY A 158      596    505    459     92     13     -1       N  
ATOM    858  CA  GLY A 158      40.106  26.724  18.551  1.00  4.46           C  
ANISOU  858  CA  GLY A 158      607    560    525     70     49    -53       C  
ATOM    859  C   GLY A 158      41.468  26.157  18.254  1.00  4.13           C  
ANISOU  859  C   GLY A 158      592    458    519     46     -2     43       C  
ATOM    860  O   GLY A 158      41.892  25.186  18.866  1.00  5.49           O  
ANISOU  860  O   GLY A 158      703    948    434    193    135     64       O  
ATOM    861  N   GLU A 159      42.113  26.744  17.262  1.00  4.62           N  
ANISOU  861  N   GLU A 159      601    447    705     77     76     -1       N  
ATOM    862  CA  GLU A 159      43.398  26.297  16.776  1.00  4.24           C  
ANISOU  862  CA  GLU A 159      521    473    617     19    106    -54       C  
ATOM    863  C   GLU A 159      44.436  27.375  17.118  1.00  4.08           C  
ANISOU  863  C   GLU A 159      533    388    628     50    146    -15       C  
ATOM    864  O   GLU A 159      44.274  28.539  16.738  1.00  5.04           O  
ANISOU  864  O   GLU A 159      601    484    831     34     94     18       O  
ATOM    865  CB  GLU A 159      43.357  26.097  15.255  1.00  4.81           C  
ANISOU  865  CB  GLU A 159      608    458    759     22     37    -64       C  
ATOM    866  CG  GLU A 159      44.491  25.209  14.746  1.00  4.82           C  
ANISOU  866  CG  GLU A 159      643    598    590     53     78    -68       C  
ATOM    867  CD  GLU A 159      44.255  23.724  14.943  1.00  5.04           C  
ANISOU  867  CD  GLU A 159      680    574    660     41    189   -167       C  
ATOM    868  OE1 GLU A 159      43.231  23.336  15.565  1.00  5.75           O  
ANISOU  868  OE1 GLU A 159      692    603    889     22    190   -110       O  
ATOM    869  OE2 GLU A 159      45.100  22.944  14.442  1.00  5.39           O  
ANISOU  869  OE2 GLU A 159      708    557    779     73     78   -146       O  
ATOM    870  N   LEU A 160      45.512  26.994  17.809  1.00  4.36           N  
ANISOU  870  N   LEU A 160      617    444    595     14     61     48       N  
ATOM    871  CA  LEU A 160      46.659  27.846  18.004  1.00  4.34           C  
ANISOU  871  CA  LEU A 160      646    474    529     10     -1    -35       C  
ATOM    872  C   LEU A 160      47.510  27.688  16.759  1.00  4.36           C  
ANISOU  872  C   LEU A 160      527    468    662    -37     14    -10       C  
ATOM    873  O   LEU A 160      47.818  26.562  16.386  1.00  4.99           O  
ANISOU  873  O   LEU A 160      679    511    706     17     47   -114       O  
ATOM    874  CB  LEU A 160      47.418  27.418  19.261  1.00  5.25           C  
ANISOU  874  CB  LEU A 160      761    590    640     16     31      4       C  
ATOM    875  CG  LEU A 160      48.573  28.325  19.641  1.00  6.13           C  
ANISOU  875  CG  LEU A 160      848    750    728      3    -78    -76       C  
ATOM    876  CD1 LEU A 160      48.077  29.633  20.255  1.00  8.44           C  
ANISOU  876  CD1 LEU A 160     1196    963   1045    -34   -281    -68       C  
ATOM    877  CD2 LEU A 160      49.487  27.609  20.622  1.00  7.53           C  
ANISOU  877  CD2 LEU A 160     1092    875    892    -22   -164   -154       C  
ATOM    878  N   PHE A 161      47.880  28.783  16.109  1.00  4.43           N  
ANISOU  878  N   PHE A 161      603    521    558      5     28   -149       N  
ATOM    879  CA  PHE A 161      48.520  28.686  14.803  1.00  4.57           C  
ANISOU  879  CA  PHE A 161      602    566    566     12     17    -40       C  
ATOM    880  C   PHE A 161      49.470  29.848  14.572  1.00  4.40           C  
ANISOU  880  C   PHE A 161      571    552    548     28     60    -34       C  
ATOM    881  O   PHE A 161      49.467  30.843  15.289  1.00  4.89           O  
ANISOU  881  O   PHE A 161      646    602    609    -47    114    -74       O  
ATOM    882  CB  PHE A 161      47.470  28.598  13.676  1.00  4.76           C  
ANISOU  882  CB  PHE A 161      667    588    553     -1     40    -51       C  
ATOM    883  CG  PHE A 161      46.759  29.892  13.374  1.00  4.71           C  
ANISOU  883  CG  PHE A 161      629    684    473    -64     10     -4       C  
ATOM    884  CD1 PHE A 161      47.172  30.694  12.326  1.00  6.14           C  
ANISOU  884  CD1 PHE A 161      857    955    518    168    153     82       C  
ATOM    885  CD2 PHE A 161      45.676  30.319  14.130  1.00  4.51           C  
ANISOU  885  CD2 PHE A 161      592    533    588    -57     98    -51       C  
ATOM    886  CE1 PHE A 161      46.505  31.868  12.005  1.00  7.13           C  
ANISOU  886  CE1 PHE A 161      983   1035    690    129    206    296       C  
ATOM    887  CE2 PHE A 161      45.016  31.493  13.827  1.00  5.32           C  
ANISOU  887  CE2 PHE A 161      623    728    668    -45     61    -27       C  
ATOM    888  CZ  PHE A 161      45.428  32.269  12.761  1.00  5.93           C  
ANISOU  888  CZ  PHE A 161      730    841    680     78    154    115       C  
ATOM    889  N   GLY A 162      50.253  29.706  13.517  1.00  4.75           N  
ANISOU  889  N   GLY A 162      647    605    553    -16     38     29       N  
ATOM    890  CA  GLY A 162      51.142  30.763  13.090  1.00  5.04           C  
ANISOU  890  CA  GLY A 162      632    658    621     33     47     85       C  
ATOM    891  C   GLY A 162      52.583  30.559  13.483  1.00  4.90           C  
ANISOU  891  C   GLY A 162      648    627    585     25     15    114       C  
ATOM    892  O   GLY A 162      53.076  29.439  13.562  1.00  5.37           O  
ANISOU  892  O   GLY A 162      680    515    842     35     28    127       O  
ATOM    893  N   ALA A 163      53.268  31.674  13.690  1.00  5.47           N  
ANISOU  893  N   ALA A 163      700    617    761     -9     -7    127       N  
ATOM    894  CA  ALA A 163      54.698  31.727  13.990  1.00  6.11           C  
ANISOU  894  CA  ALA A 163      717    737    866    -35    -10    135       C  
ATOM    895  C   ALA A 163      55.544  31.086  12.892  1.00  5.70           C  
ANISOU  895  C   ALA A 163      679    682    804    -53    -18    178       C  
ATOM    896  O   ALA A 163      56.596  30.512  13.144  1.00  6.58           O  
ANISOU  896  O   ALA A 163      714    741   1042    -18   -114    115       O  
ATOM    897  CB  ALA A 163      54.994  31.162  15.378  1.00  6.60           C  
ANISOU  897  CB  ALA A 163      802    891    813    -75      3     24       C  
ATOM    898  N   LYS A 164      55.104  31.241  11.644  1.00  5.70           N  
ANISOU  898  N   LYS A 164      629    742    791    -30    -11    209       N  
ATOM    899  CA  LYS A 164      55.882  30.826  10.477  1.00  6.12           C  
ANISOU  899  CA  LYS A 164      711    720    891      9     32    161       C  
ATOM    900  C   LYS A 164      55.351  31.544   9.254  1.00  5.51           C  
ANISOU  900  C   LYS A 164      669    626    799    -22    106    192       C  
ATOM    901  O   LYS A 164      54.186  31.405   8.917  1.00  5.81           O  
ANISOU  901  O   LYS A 164      650    751    804    -45    166    160       O  
ATOM    902  CB  LYS A 164      55.801  29.314  10.266  1.00  6.71           C  
ANISOU  902  CB  LYS A 164      799    785    964     54     35    254       C  
ATOM    903  CG  LYS A 164      56.576  28.818   9.031  1.00  8.60           C  
ANISOU  903  CG  LYS A 164     1063    914   1290     66     70    271       C  
ATOM    904  CD  LYS A 164      56.468  27.308   8.790  1.00 11.35           C  
ANISOU  904  CD  LYS A 164     1538   1267   1506    200    122     93       C  
ATOM    905  CE  LYS A 164      57.221  26.868   7.551  1.00 14.30           C  
ANISOU  905  CE  LYS A 164     1933   1537   1962    203    -61    -38       C  
ATOM    906  NZ  LYS A 164      57.214  25.386   7.381  1.00 16.78           N  
ANISOU  906  NZ  LYS A 164     2171   1767   2436    232    -95   -166       N  
ATOM    907  N   TYR A 165      56.218  32.278   8.563  1.00  6.02           N  
ANISOU  907  N   TYR A 165      663    736    889    -31     35    268       N  
ATOM    908  CA  TYR A 165      55.830  32.906   7.305  1.00  5.96           C  
ANISOU  908  CA  TYR A 165      734    726    801    -17      7    152       C  
ATOM    909  C   TYR A 165      57.102  33.250   6.543  1.00  6.16           C  
ANISOU  909  C   TYR A 165      887    649    801    -42     22    213       C  
ATOM    910  O   TYR A 165      57.720  34.292   6.779  1.00  7.12           O  
ANISOU  910  O   TYR A 165      954    806    943   -230    -39    231       O  
ATOM    911  CB  TYR A 165      54.962  34.144   7.528  1.00  6.32           C  
ANISOU  911  CB  TYR A 165      846    764    788     39     44    145       C  
ATOM    912  CG  TYR A 165      54.187  34.508   6.293  1.00  5.81           C  
ANISOU  912  CG  TYR A 165      769    643    794     58     80    213       C  
ATOM    913  CD1 TYR A 165      52.976  33.902   6.023  1.00  6.02           C  
ANISOU  913  CD1 TYR A 165      749    703    832     15    179    279       C  
ATOM    914  CD2 TYR A 165      54.674  35.425   5.367  1.00  6.39           C  
ANISOU  914  CD2 TYR A 165      747    712    968    -35    -21    247       C  
ATOM    915  CE1 TYR A 165      52.254  34.211   4.892  1.00  6.30           C  
ANISOU  915  CE1 TYR A 165      702    675   1015    -74     43    277       C  
ATOM    916  CE2 TYR A 165      53.964  35.734   4.239  1.00  6.21           C  
ANISOU  916  CE2 TYR A 165      759    672    927    -80     82    304       C  
ATOM    917  CZ  TYR A 165      52.745  35.134   4.002  1.00  5.60           C  
ANISOU  917  CZ  TYR A 165      644    633    848    -12     78    226       C  
ATOM    918  OH  TYR A 165      52.013  35.422   2.871  1.00  6.88           O  
ANISOU  918  OH  TYR A 165      829    908    878    -91    -65    297       O  
ATOM    919  N   LYS A 166      57.500  32.377   5.633  1.00  6.45           N  
ANISOU  919  N   LYS A 166      761    759    928    -76    108    200       N  
ATOM    920  CA  LYS A 166      58.833  32.445   5.045  1.00  7.62           C  
ANISOU  920  CA  LYS A 166      933    886   1074     41    129    201       C  
ATOM    921  C   LYS A 166      58.873  33.338   3.812  1.00  7.29           C  
ANISOU  921  C   LYS A 166      978    812    979     -1    210    260       C  
ATOM    922  O   LYS A 166      59.074  32.889   2.688  1.00  9.59           O  
ANISOU  922  O   LYS A 166     1551    965   1125     30    115    298       O  
ATOM    923  CB  LYS A 166      59.318  31.032   4.731  1.00  8.54           C  
ANISOU  923  CB  LYS A 166      909   1028   1306     36    225    258       C  
ATOM    924  CG  LYS A 166      59.532  30.172   5.967  1.00 13.17           C  
ANISOU  924  CG  LYS A 166     1520   1573   1910     63    142    116       C  
ATOM    925  CD  LYS A 166      59.994  28.757   5.625  1.00 17.90           C  
ANISOU  925  CD  LYS A 166     2249   2161   2388     74     66    127       C  
ATOM    926  CE  LYS A 166      61.454  28.711   5.216  1.00 21.76           C  
ANISOU  926  CE  LYS A 166     2737   2642   2885    121     94     51       C  
ATOM    927  NZ  LYS A 166      61.883  27.319   4.891  1.00 23.52           N  
ANISOU  927  NZ  LYS A 166     3019   2798   3119     86    119    -51       N  
ATOM    928  N   HIS A 167      58.687  34.626   4.037  1.00  7.89           N  
ANISOU  928  N   HIS A 167     1184    851    961      9    253    225       N  
ATOM    929  CA  HIS A 167      58.818  35.647   2.997  1.00  7.31           C  
ANISOU  929  CA  HIS A 167     1034    818    923    -32    187    256       C  
ATOM    930  C   HIS A 167      59.863  36.638   3.462  1.00  7.93           C  
ANISOU  930  C   HIS A 167     1085    939    989    -21    214    388       C  
ATOM    931  O   HIS A 167      59.816  37.080   4.607  1.00  8.60           O  
ANISOU  931  O   HIS A 167     1139    981   1147    -67    136    377       O  
ATOM    932  CB  HIS A 167      57.490  36.361   2.794  1.00  7.32           C  
ANISOU  932  CB  HIS A 167     1035    818    929   -134    214    211       C  
ATOM    933  CG  HIS A 167      57.449  37.225   1.580  1.00  6.97           C  
ANISOU  933  CG  HIS A 167      879    745   1023   -144    143    267       C  
ATOM    934  ND1 HIS A 167      58.188  38.380   1.463  1.00  7.93           N  
ANISOU  934  ND1 HIS A 167      985    873   1153    -74     64    265       N  
ATOM    935  CD2 HIS A 167      56.758  37.086   0.425  1.00  7.78           C  
ANISOU  935  CD2 HIS A 167     1016    832   1106   -148    162    121       C  
ATOM    936  CE1 HIS A 167      57.937  38.921   0.287  1.00  7.91           C  
ANISOU  936  CE1 HIS A 167     1056   1004    945   -117    -27    411       C  
ATOM    937  NE2 HIS A 167      57.070  38.164  -0.360  1.00  8.24           N  
ANISOU  937  NE2 HIS A 167     1179    888   1064     90    139    235       N  
ATOM    938  N   PRO A 168      60.808  37.014   2.593  1.00  8.59           N  
ANISOU  938  N   PRO A 168     1069   1039   1155     33    151    261       N  
ATOM    939  CA  PRO A 168      61.913  37.873   3.023  1.00  9.49           C  
ANISOU  939  CA  PRO A 168     1120   1213   1270    -59     72    328       C  
ATOM    940  C   PRO A 168      61.504  39.276   3.476  1.00  9.50           C  
ANISOU  940  C   PRO A 168     1107   1176   1324   -107     41    308       C  
ATOM    941  O   PRO A 168      62.281  39.949   4.142  1.00 11.25           O  
ANISOU  941  O   PRO A 168     1228   1334   1710   -148   -108    373       O  
ATOM    942  CB  PRO A 168      62.822  37.933   1.786  1.00 10.48           C  
ANISOU  942  CB  PRO A 168     1134   1331   1515     -6    169    256       C  
ATOM    943  CG  PRO A 168      61.959  37.576   0.672  1.00 10.90           C  
ANISOU  943  CG  PRO A 168     1285   1432   1422     -1    235    241       C  
ATOM    944  CD  PRO A 168      60.958  36.589   1.193  1.00  9.10           C  
ANISOU  944  CD  PRO A 168     1085   1192   1181     23    245    253       C  
ATOM    945  N   LEU A 169      60.311  39.734   3.120  1.00  8.31           N  
ANISOU  945  N   LEU A 169     1007   1020   1128    -84     45    311       N  
ATOM    946  CA  LEU A 169      59.836  41.040   3.570  1.00  8.41           C  
ANISOU  946  CA  LEU A 169     1103    975   1116   -104     24    186       C  
ATOM    947  C   LEU A 169      59.017  40.970   4.856  1.00  8.86           C  
ANISOU  947  C   LEU A 169     1270    970   1126    -66     -4    177       C  
ATOM    948  O   LEU A 169      58.486  41.987   5.300  1.00 10.19           O  
ANISOU  948  O   LEU A 169     1600   1081   1190     13     52    228       O  
ATOM    949  CB  LEU A 169      59.023  41.723   2.467  1.00  8.31           C  
ANISOU  949  CB  LEU A 169     1075    925   1156   -191     31    248       C  
ATOM    950  CG  LEU A 169      59.792  41.953   1.178  1.00  8.27           C  
ANISOU  950  CG  LEU A 169      974    959   1208    -93    164    302       C  
ATOM    951  CD1 LEU A 169      58.910  42.692   0.185  1.00  7.88           C  
ANISOU  951  CD1 LEU A 169     1003    912   1079   -132    127    289       C  
ATOM    952  CD2 LEU A 169      61.095  42.704   1.371  1.00  9.21           C  
ANISOU  952  CD2 LEU A 169     1136   1133   1228   -129     64    442       C  
ATOM    953  N   VAL A 170      58.907  39.776   5.443  1.00  8.07           N  
ANISOU  953  N   VAL A 170     1082    960   1021   -120     51    216       N  
ATOM    954  CA  VAL A 170      58.132  39.565   6.643  1.00  8.21           C  
ANISOU  954  CA  VAL A 170     1062   1044   1013    -71     71    174       C  
ATOM    955  C   VAL A 170      59.086  39.053   7.713  1.00  8.68           C  
ANISOU  955  C   VAL A 170     1150   1094   1054   -206     36    182       C  
ATOM    956  O   VAL A 170      59.393  37.872   7.771  1.00  8.96           O  
ANISOU  956  O   VAL A 170     1062   1212   1131    -11     49    233       O  
ATOM    957  CB  VAL A 170      57.001  38.572   6.386  1.00  7.62           C  
ANISOU  957  CB  VAL A 170     1017    952    925    -62     77    162       C  
ATOM    958  CG1 VAL A 170      56.176  38.354   7.649  1.00  8.07           C  
ANISOU  958  CG1 VAL A 170     1034   1152    880    -45     67    191       C  
ATOM    959  CG2 VAL A 170      56.118  39.071   5.248  1.00  6.96           C  
ANISOU  959  CG2 VAL A 170      989    871    784    -95    177    191       C  
ATOM    960  N   PRO A 171      59.616  39.942   8.543  1.00  9.76           N  
ANISOU  960  N   PRO A 171     1319   1254   1135   -285    -42    217       N  
ATOM    961  CA  PRO A 171      60.525  39.500   9.599  1.00 10.36           C  
ANISOU  961  CA  PRO A 171     1326   1357   1250   -253    -15    182       C  
ATOM    962  C   PRO A 171      59.898  38.469  10.522  1.00  9.70           C  
ANISOU  962  C   PRO A 171     1218   1289   1178   -285    -15    214       C  
ATOM    963  O   PRO A 171      58.702  38.505  10.796  1.00  9.84           O  
ANISOU  963  O   PRO A 171     1263   1355   1120   -304     -4    243       O  
ATOM    964  CB  PRO A 171      60.825  40.794  10.357  1.00 11.81           C  
ANISOU  964  CB  PRO A 171     1562   1527   1398   -282    -59    168       C  
ATOM    965  CG  PRO A 171      60.617  41.873   9.351  1.00 12.29           C  
ANISOU  965  CG  PRO A 171     1581   1571   1516   -243    -32    132       C  
ATOM    966  CD  PRO A 171      59.460  41.410   8.533  1.00 10.90           C  
ANISOU  966  CD  PRO A 171     1542   1391   1207   -302    -98    155       C  
ATOM    967  N   LYS A 172      60.722  37.567  11.011  1.00 10.05           N  
ANISOU  967  N   LYS A 172     1211   1369   1238   -219     36    184       N  
ATOM    968  CA  LYS A 172      60.276  36.701  12.083  1.00 10.08           C  
ANISOU  968  CA  LYS A 172     1298   1304   1228   -161    -14    150       C  
ATOM    969  C   LYS A 172      59.886  37.539  13.303  1.00  9.08           C  
ANISOU  969  C   LYS A 172     1208   1138   1102   -205   -127    136       C  
ATOM    970  O   LYS A 172      60.333  38.681  13.476  1.00  9.92           O  
ANISOU  970  O   LYS A 172     1337   1244   1186   -376   -140    145       O  
ATOM    971  CB  LYS A 172      61.338  35.656  12.436  1.00 11.58           C  
ANISOU  971  CB  LYS A 172     1419   1519   1461    -83    -16     86       C  
ATOM    972  CG  LYS A 172      61.605  34.672  11.313  1.00 13.66           C  
ANISOU  972  CG  LYS A 172     1667   1910   1611    -50     55     93       C  
ATOM    973  CD  LYS A 172      62.384  33.454  11.751  1.00 16.99           C  
ANISOU  973  CD  LYS A 172     2151   2189   2116    -22     21    -48       C  
ATOM    974  CE  LYS A 172      61.490  32.415  12.416  1.00 18.27           C  
ANISOU  974  CE  LYS A 172     2336   2281   2325     24    -18     52       C  
ATOM    975  NZ  LYS A 172      62.228  31.163  12.739  1.00 19.99           N  
ANISOU  975  NZ  LYS A 172     2623   2455   2516    164   -130     50       N  
ATOM    976  N   SER A 173      59.056  36.964  14.160  1.00  8.96           N  
ANISOU  976  N   SER A 173     1220   1022   1159   -217    -67    162       N  
ATOM    977  CA  SER A 173      58.606  37.657  15.345  1.00  8.59           C  
ANISOU  977  CA  SER A 173     1136    996   1128   -180    -82     96       C  
ATOM    978  C   SER A 173      59.796  38.051  16.215  1.00  9.29           C  
ANISOU  978  C   SER A 173     1226   1070   1232   -177    -96     86       C  
ATOM    979  O   SER A 173      60.725  37.274  16.402  1.00  9.80           O  
ANISOU  979  O   SER A 173     1264   1198   1261   -247   -149     81       O  
ATOM    980  CB  SER A 173      57.679  36.765  16.168  1.00  7.98           C  
ANISOU  980  CB  SER A 173     1160    910    961   -178    -54    179       C  
ATOM    981  OG  SER A 173      57.270  37.437  17.349  1.00  8.75           O  
ANISOU  981  OG  SER A 173     1260    970   1094   -256    -75     21       O  
ATOM    982  N   GLU A 174      59.717  39.252  16.769  1.00  9.37           N  
ANISOU  982  N   GLU A 174     1262   1078   1220   -296   -149     77       N  
ATOM    983  CA  GLU A 174      60.665  39.738  17.763  1.00 10.66           C  
ANISOU  983  CA  GLU A 174     1340   1259   1449   -274   -118      6       C  
ATOM    984  C   GLU A 174      60.154  39.528  19.185  1.00  9.97           C  
ANISOU  984  C   GLU A 174     1334   1146   1308   -259   -147    -69       C  
ATOM    985  O   GLU A 174      60.818  39.925  20.144  1.00 11.45           O  
ANISOU  985  O   GLU A 174     1467   1367   1515   -431   -241   -130       O  
ATOM    986  CB  GLU A 174      60.946  41.223  17.529  1.00 11.75           C  
ANISOU  986  CB  GLU A 174     1588   1340   1536   -333    -44      5       C  
ATOM    987  CG  GLU A 174      61.622  41.529  16.198  1.00 16.35           C  
ANISOU  987  CG  GLU A 174     2128   2017   2063   -375     48      3       C  
ATOM    988  CD  GLU A 174      61.910  43.012  16.009  1.00 21.99           C  
ANISOU  988  CD  GLU A 174     2906   2668   2779   -248    189     10       C  
ATOM    989  OE1 GLU A 174      61.347  43.838  16.756  1.00 26.41           O  
ANISOU  989  OE1 GLU A 174     3593   2929   3512   -240    175     31       O  
ATOM    990  OE2 GLU A 174      62.695  43.358  15.107  1.00 27.62           O  
ANISOU  990  OE2 GLU A 174     3570   3365   3560   -280    200     46       O  
ATOM    991  N   LYS A 175      58.978  38.921  19.336  1.00  9.11           N  
ANISOU  991  N   LYS A 175     1238   1008   1212   -187   -154    -66       N  
ATOM    992  CA  LYS A 175      58.359  38.796  20.649  1.00  8.62           C  
ANISOU  992  CA  LYS A 175     1194    899   1182   -125   -104   -114       C  
ATOM    993  C   LYS A 175      58.905  37.613  21.426  1.00  8.33           C  
ANISOU  993  C   LYS A 175     1180    841   1141   -130    -90    -85       C  
ATOM    994  O   LYS A 175      59.348  36.621  20.854  1.00  8.34           O  
ANISOU  994  O   LYS A 175     1153    866   1147    -84    -22   -167       O  
ATOM    995  CB  LYS A 175      56.859  38.630  20.501  1.00  9.28           C  
ANISOU  995  CB  LYS A 175     1230   1063   1231    -48   -101    -69       C  
ATOM    996  CG  LYS A 175      56.179  39.782  19.789  1.00 10.49           C  
ANISOU  996  CG  LYS A 175     1389   1160   1436     -1   -103   -180       C  
ATOM    997  CD  LYS A 175      54.665  39.649  19.821  1.00 11.91           C  
ANISOU  997  CD  LYS A 175     1483   1343   1697    122   -116   -116       C  
ATOM    998  CE  LYS A 175      54.007  40.621  18.865  1.00 13.49           C  
ANISOU  998  CE  LYS A 175     1601   1555   1967    176   -258    -97       C  
ATOM    999  NZ  LYS A 175      52.540  40.684  19.055  1.00 16.30           N  
ANISOU  999  NZ  LYS A 175     1865   1758   2569      0   -205     48       N  
ATOM   1000  N   TRP A 176      58.847  37.730  22.746  1.00  9.09           N  
ANISOU 1000  N   TRP A 176     1273   1028   1152    -24    -68    -58       N  
ATOM   1001  CA  TRP A 176      59.259  36.679  23.672  1.00  9.48           C  
ANISOU 1001  CA  TRP A 176     1332   1088   1182      0    -35    -77       C  
ATOM   1002  C   TRP A 176      58.151  36.516  24.683  1.00 10.05           C  
ANISOU 1002  C   TRP A 176     1382   1161   1274     88     31    -59       C  
ATOM   1003  O   TRP A 176      57.694  37.516  25.237  1.00 12.24           O  
ANISOU 1003  O   TRP A 176     1872   1241   1538    135    274   -132       O  
ATOM   1004  CB  TRP A 176      60.541  37.066  24.438  1.00 10.67           C  
ANISOU 1004  CB  TRP A 176     1502   1283   1268     -6   -136    -68       C  
ATOM   1005  CG  TRP A 176      61.766  37.066  23.591  1.00 11.13           C  
ANISOU 1005  CG  TRP A 176     1315   1499   1415   -256   -227    -10       C  
ATOM   1006  CD1 TRP A 176      62.057  37.928  22.581  1.00 13.43           C  
ANISOU 1006  CD1 TRP A 176     1516   1798   1786   -272   -181     81       C  
ATOM   1007  CD2 TRP A 176      62.882  36.163  23.670  1.00 11.31           C  
ANISOU 1007  CD2 TRP A 176     1281   1656   1358   -350   -266   -121       C  
ATOM   1008  NE1 TRP A 176      63.266  37.607  22.013  1.00 13.19           N  
ANISOU 1008  NE1 TRP A 176     1509   1817   1685   -366   -157     93       N  
ATOM   1009  CE2 TRP A 176      63.796  36.533  22.664  1.00 12.63           C  
ANISOU 1009  CE2 TRP A 176     1320   1818   1661   -385   -218   -101       C  
ATOM   1010  CE3 TRP A 176      63.206  35.080  24.494  1.00 11.02           C  
ANISOU 1010  CE3 TRP A 176     1441   1362   1381   -283   -220   -180       C  
ATOM   1011  CZ2 TRP A 176      65.006  35.866  22.458  1.00 13.38           C  
ANISOU 1011  CZ2 TRP A 176     1392   1902   1788   -395   -113    -37       C  
ATOM   1012  CZ3 TRP A 176      64.418  34.420  24.289  1.00 12.37           C  
ANISOU 1012  CZ3 TRP A 176     1537   1717   1446   -141   -131      6       C  
ATOM   1013  CH2 TRP A 176      65.288  34.808  23.271  1.00 12.86           C  
ANISOU 1013  CH2 TRP A 176     1412   1772   1701   -267   -287   -177       C  
ATOM   1014  N   CYS A 177      57.725  35.287  24.942  1.00  9.33           N  
ANISOU 1014  N   CYS A 177     1180   1215   1147     69     -9     -8       N  
ATOM   1015  CA  CYS A 177      56.742  35.045  25.977  1.00  9.81           C  
ANISOU 1015  CA  CYS A 177     1175   1345   1206     49    -20     16       C  
ATOM   1016  C   CYS A 177      57.442  34.914  27.313  1.00  9.02           C  
ANISOU 1016  C   CYS A 177     1052   1284   1091     22     16     17       C  
ATOM   1017  O   CYS A 177      58.643  34.669  27.369  1.00  9.54           O  
ANISOU 1017  O   CYS A 177      956   1593   1075     47    -54    -14       O  
ATOM   1018  CB  CYS A 177      55.923  33.792  25.691  1.00 10.49           C  
ANISOU 1018  CB  CYS A 177     1255   1573   1155     -3   -100     27       C  
ATOM   1019  SG  CYS A 177      56.801  32.236  25.857  1.00 10.78           S  
ANISOU 1019  SG  CYS A 177     1369   1318   1409   -182   -142   -110       S  
ATOM   1020  N   THR A 178      56.672  35.069  28.383  1.00  9.38           N  
ANISOU 1020  N   THR A 178     1097   1301   1165     -1     63    -42       N  
ATOM   1021  CA  THR A 178      57.155  34.888  29.741  1.00  9.89           C  
ANISOU 1021  CA  THR A 178     1221   1279   1256    -35    121    -81       C  
ATOM   1022  C   THR A 178      56.216  33.958  30.490  1.00  9.84           C  
ANISOU 1022  C   THR A 178     1174   1273   1289    -30    127   -110       C  
ATOM   1023  O   THR A 178      55.011  34.197  30.549  1.00 10.99           O  
ANISOU 1023  O   THR A 178     1106   1445   1622     24    244     45       O  
ATOM   1024  CB  THR A 178      57.227  36.230  30.487  1.00 10.65           C  
ANISOU 1024  CB  THR A 178     1306   1421   1317   -146    178    -66       C  
ATOM   1025  OG1 THR A 178      58.014  37.179  29.745  1.00 11.94           O  
ANISOU 1025  OG1 THR A 178     1802   1358   1376   -145    375   -228       O  
ATOM   1026  CG2 THR A 178      57.939  36.057  31.839  1.00 12.01           C  
ANISOU 1026  CG2 THR A 178     1629   1471   1461    -86    168   -230       C  
ATOM   1027  N   LEU A 179      56.772  32.922  31.084  1.00  8.75           N  
ANISOU 1027  N   LEU A 179     1054   1171   1099   -121     -3   -103       N  
ATOM   1028  CA  LEU A 179      55.991  31.987  31.881  1.00  9.26           C  
ANISOU 1028  CA  LEU A 179     1250   1101   1165    -86    -25   -104       C  
ATOM   1029  C   LEU A 179      55.845  32.517  33.308  1.00  9.40           C  
ANISOU 1029  C   LEU A 179     1274   1138   1159    -94     -6   -171       C  
ATOM   1030  O   LEU A 179      56.611  33.385  33.730  1.00  9.19           O  
ANISOU 1030  O   LEU A 179     1328   1171    990   -216     24   -195       O  
ATOM   1031  CB  LEU A 179      56.675  30.630  31.928  1.00  9.62           C  
ANISOU 1031  CB  LEU A 179     1301   1134   1219    -78    -63   -174       C  
ATOM   1032  CG  LEU A 179      56.414  29.728  30.721  1.00 11.13           C  
ANISOU 1032  CG  LEU A 179     1568   1287   1371    -55     92   -170       C  
ATOM   1033  CD1 LEU A 179      56.749  30.366  29.381  1.00 11.24           C  
ANISOU 1033  CD1 LEU A 179     1577   1393   1298     66   -207   -300       C  
ATOM   1034  CD2 LEU A 179      57.190  28.440  30.918  1.00 12.55           C  
ANISOU 1034  CD2 LEU A 179     1823   1410   1532     65    -19   -231       C  
ATOM   1035  N   PRO A 180      54.898  31.992  34.086  1.00  9.92           N  
ANISOU 1035  N   PRO A 180     1348   1237   1183   -113     14   -125       N  
ATOM   1036  CA  PRO A 180      54.786  32.402  35.494  1.00 10.79           C  
ANISOU 1036  CA  PRO A 180     1468   1324   1306   -119     71   -133       C  
ATOM   1037  C   PRO A 180      56.083  32.269  36.295  1.00 11.11           C  
ANISOU 1037  C   PRO A 180     1592   1357   1271    -92     67   -132       C  
ATOM   1038  O   PRO A 180      56.319  33.083  37.190  1.00 11.48           O  
ANISOU 1038  O   PRO A 180     1761   1439   1161   -198     54   -332       O  
ATOM   1039  CB  PRO A 180      53.667  31.500  36.028  1.00 11.43           C  
ANISOU 1039  CB  PRO A 180     1556   1376   1408   -102     55    -63       C  
ATOM   1040  CG  PRO A 180      52.839  31.206  34.832  1.00 11.55           C  
ANISOU 1040  CG  PRO A 180     1542   1312   1533   -139      8    -53       C  
ATOM   1041  CD  PRO A 180      53.804  31.074  33.705  1.00 10.31           C  
ANISOU 1041  CD  PRO A 180     1294   1310   1311    -97    -64    -75       C  
ATOM   1042  N   ASN A 181      56.930  31.302  35.960  1.00 10.92           N  
ANISOU 1042  N   ASN A 181     1551   1350   1248    -87    -15   -148       N  
ATOM   1043  CA  ASN A 181      58.205  31.123  36.646  1.00 11.37           C  
ANISOU 1043  CA  ASN A 181     1569   1427   1324    -58    -79    -87       C  
ATOM   1044  C   ASN A 181      59.325  32.040  36.119  1.00 11.03           C  
ANISOU 1044  C   ASN A 181     1519   1407   1265    -66    -74   -122       C  
ATOM   1045  O   ASN A 181      60.452  31.953  36.582  1.00 12.35           O  
ANISOU 1045  O   ASN A 181     1571   1815   1304   -115   -241    -93       O  
ATOM   1046  CB  ASN A 181      58.634  29.655  36.612  1.00 11.75           C  
ANISOU 1046  CB  ASN A 181     1614   1461   1387    -62   -165    -47       C  
ATOM   1047  CG  ASN A 181      58.904  29.142  35.203  1.00 10.83           C  
ANISOU 1047  CG  ASN A 181     1428   1193   1493    -23   -190     23       C  
ATOM   1048  OD1 ASN A 181      59.071  29.921  34.272  1.00 12.14           O  
ANISOU 1048  OD1 ASN A 181     1874   1320   1415     83   -236   -134       O  
ATOM   1049  ND2 ASN A 181      58.969  27.823  35.058  1.00 12.88           N  
ANISOU 1049  ND2 ASN A 181     1529   1429   1936    141   -568      7       N  
ATOM   1050  N   GLY A 182      59.030  32.911  35.162  1.00 10.28           N  
ANISOU 1050  N   GLY A 182     1466   1274   1165    -57    -60   -173       N  
ATOM   1051  CA  GLY A 182      59.985  33.905  34.694  1.00 10.11           C  
ANISOU 1051  CA  GLY A 182     1342   1371   1127   -101    -56    -80       C  
ATOM   1052  C   GLY A 182      60.754  33.509  33.451  1.00  9.60           C  
ANISOU 1052  C   GLY A 182     1331   1263   1051   -125    -84    -53       C  
ATOM   1053  O   GLY A 182      61.374  34.354  32.791  1.00  9.78           O  
ANISOU 1053  O   GLY A 182     1278   1344   1094    -90     10    -68       O  
ATOM   1054  N   LYS A 183      60.711  32.230  33.112  1.00  9.62           N  
ANISOU 1054  N   LYS A 183     1234   1297   1121    -12    -81    -14       N  
ATOM   1055  CA  LYS A 183      61.376  31.783  31.902  1.00  9.57           C  
ANISOU 1055  CA  LYS A 183     1235   1276   1123     20    -49    -41       C  
ATOM   1056  C   LYS A 183      60.736  32.417  30.680  1.00  8.58           C  
ANISOU 1056  C   LYS A 183     1079   1275    906     34    -56   -139       C  
ATOM   1057  O   LYS A 183      59.523  32.581  30.626  1.00  9.50           O  
ANISOU 1057  O   LYS A 183      957   1557   1096     29   -122    -80       O  
ATOM   1058  CB  LYS A 183      61.303  30.273  31.785  1.00 10.30           C  
ANISOU 1058  CB  LYS A 183     1389   1315   1207     82    -44     12       C  
ATOM   1059  CG  LYS A 183      62.144  29.538  32.810  1.00 13.57           C  
ANISOU 1059  CG  LYS A 183     1752   1608   1795     96   -112     47       C  
ATOM   1060  CD  LYS A 183      62.013  28.037  32.637  1.00 17.46           C  
ANISOU 1060  CD  LYS A 183     2411   1959   2261      0    -43     95       C  
ATOM   1061  CE  LYS A 183      62.956  27.266  33.540  1.00 22.00           C  
ANISOU 1061  CE  LYS A 183     2900   2625   2832     39    -45     41       C  
ATOM   1062  NZ  LYS A 183      64.337  27.208  32.978  1.00 24.90           N  
ANISOU 1062  NZ  LYS A 183     3282   2902   3277    -40   -216     62       N  
ATOM   1063  N   LYS A 184      61.571  32.749  29.709  1.00  8.60           N  
ANISOU 1063  N   LYS A 184      983   1259   1023    110    -52   -105       N  
ATOM   1064  CA  LYS A 184      61.136  33.377  28.473  1.00  8.66           C  
ANISOU 1064  CA  LYS A 184     1091   1179   1020     87    -50   -117       C  
ATOM   1065  C   LYS A 184      61.575  32.560  27.281  1.00  8.38           C  
ANISOU 1065  C   LYS A 184     1025   1245    913    102    -57   -188       C  
ATOM   1066  O   LYS A 184      62.631  31.926  27.296  1.00  9.52           O  
ANISOU 1066  O   LYS A 184     1046   1500   1070    250   -238   -237       O  
ATOM   1067  CB  LYS A 184      61.710  34.789  28.341  1.00  8.92           C  
ANISOU 1067  CB  LYS A 184     1126   1255   1006    -17    -35    -77       C  
ATOM   1068  CG  LYS A 184      61.308  35.698  29.483  1.00 10.62           C  
ANISOU 1068  CG  LYS A 184     1419   1331   1285    -56    -19   -182       C  
ATOM   1069  CD  LYS A 184      61.877  37.106  29.313  1.00 13.78           C  
ANISOU 1069  CD  LYS A 184     1817   1683   1733    -46    110   -215       C  
ATOM   1070  CE  LYS A 184      61.080  37.915  28.293  1.00 17.14           C  
ANISOU 1070  CE  LYS A 184     2327   2051   2135    -17     82   -163       C  
ATOM   1071  NZ  LYS A 184      61.607  39.295  28.096  1.00 20.06           N  
ANISOU 1071  NZ  LYS A 184     2561   2442   2617     12     -6   -160       N  
ATOM   1072  N   PHE A 185      60.745  32.571  26.244  1.00  7.65           N  
ANISOU 1072  N   PHE A 185      928   1078    899     53   -120   -179       N  
ATOM   1073  CA  PHE A 185      61.039  31.869  25.000  1.00  8.19           C  
ANISOU 1073  CA  PHE A 185     1040   1107    963     61    -49   -187       C  
ATOM   1074  C   PHE A 185      60.693  32.752  23.829  1.00  8.06           C  
ANISOU 1074  C   PHE A 185      978   1114    967     34   -100   -185       C  
ATOM   1075  O   PHE A 185      59.695  33.465  23.851  1.00  8.20           O  
ANISOU 1075  O   PHE A 185      987   1186    940     93    -79   -169       O  
ATOM   1076  CB  PHE A 185      60.245  30.564  24.923  1.00  8.36           C  
ANISOU 1076  CB  PHE A 185     1177   1107    892    122    -43   -116       C  
ATOM   1077  CG  PHE A 185      60.611  29.603  25.989  1.00  9.35           C  
ANISOU 1077  CG  PHE A 185     1334   1074   1142    155    -74    -53       C  
ATOM   1078  CD1 PHE A 185      61.731  28.800  25.850  1.00 12.05           C  
ANISOU 1078  CD1 PHE A 185     1795   1418   1362    286      1     76       C  
ATOM   1079  CD2 PHE A 185      59.883  29.542  27.163  1.00  9.99           C  
ANISOU 1079  CD2 PHE A 185     1411   1195   1189    108   -194     22       C  
ATOM   1080  CE1 PHE A 185      62.118  27.957  26.868  1.00 13.62           C  
ANISOU 1080  CE1 PHE A 185     1848   1383   1942    307   -130     21       C  
ATOM   1081  CE2 PHE A 185      60.264  28.693  28.170  1.00 11.92           C  
ANISOU 1081  CE2 PHE A 185     1797   1458   1272    -24   -198    114       C  
ATOM   1082  CZ  PHE A 185      61.374  27.891  28.012  1.00 13.60           C  
ANISOU 1082  CZ  PHE A 185     1973   1559   1633     17   -239     75       C  
ATOM   1083  N   PRO A 186      61.501  32.693  22.782  1.00  7.82           N  
ANISOU 1083  N   PRO A 186      842   1064   1063    -13    -52    -89       N  
ATOM   1084  CA  PRO A 186      61.248  33.531  21.613  1.00  8.41           C  
ANISOU 1084  CA  PRO A 186      963   1130   1102    -82     -3    -62       C  
ATOM   1085  C   PRO A 186      60.178  32.945  20.712  1.00  7.33           C  
ANISOU 1085  C   PRO A 186      851    918   1014    -71     19    -69       C  
ATOM   1086  O   PRO A 186      60.206  31.761  20.386  1.00  7.40           O  
ANISOU 1086  O   PRO A 186      937    850   1022    -34      6    -39       O  
ATOM   1087  CB  PRO A 186      62.593  33.522  20.894  1.00  9.15           C  
ANISOU 1087  CB  PRO A 186     1021   1241   1214   -119     14     11       C  
ATOM   1088  CG  PRO A 186      63.220  32.206  21.259  1.00  8.98           C  
ANISOU 1088  CG  PRO A 186      960   1309   1140    -43    103    -50       C  
ATOM   1089  CD  PRO A 186      62.744  31.906  22.644  1.00  8.65           C  
ANISOU 1089  CD  PRO A 186      953   1252   1082      7    -50    -31       C  
ATOM   1090  N   ILE A 187      59.264  33.792  20.266  1.00  6.81           N  
ANISOU 1090  N   ILE A 187      847    806    934    -89     -4     -4       N  
ATOM   1091  CA  ILE A 187      58.280  33.354  19.295  1.00  6.79           C  
ANISOU 1091  CA  ILE A 187      836    779    965    -71     25      1       C  
ATOM   1092  C   ILE A 187      58.974  32.954  17.982  1.00  6.34           C  
ANISOU 1092  C   ILE A 187      752    840    815    -75    -27     63       C  
ATOM   1093  O   ILE A 187      58.506  32.054  17.290  1.00  6.69           O  
ANISOU 1093  O   ILE A 187      807    809    923    -78    -28    -23       O  
ATOM   1094  CB  ILE A 187      57.169  34.405  19.097  1.00  7.03           C  
ANISOU 1094  CB  ILE A 187      843    883    944    -40     13    -16       C  
ATOM   1095  CG1 ILE A 187      56.434  34.667  20.428  1.00  7.54           C  
ANISOU 1095  CG1 ILE A 187      967    885   1010      3     12    -13       C  
ATOM   1096  CG2 ILE A 187      56.193  33.962  18.009  1.00  7.55           C  
ANISOU 1096  CG2 ILE A 187      872    838   1156     45     76     76       C  
ATOM   1097  CD1 ILE A 187      55.840  33.452  21.069  1.00  9.05           C  
ANISOU 1097  CD1 ILE A 187     1080   1092   1265    -26    240      5       C  
ATOM   1098  N   ALA A 188      60.127  33.556  17.691  1.00  7.53           N  
ANISOU 1098  N   ALA A 188      971    909    980   -128     35    -22       N  
ATOM   1099  CA  ALA A 188      60.921  33.179  16.522  1.00  8.17           C  
ANISOU 1099  CA  ALA A 188      949   1138   1017   -129     74    -41       C  
ATOM   1100  C   ALA A 188      61.402  31.735  16.570  1.00  8.28           C  
ANISOU 1100  C   ALA A 188      886   1217   1043    -92     66    -56       C  
ATOM   1101  O   ALA A 188      61.772  31.197  15.532  1.00  9.78           O  
ANISOU 1101  O   ALA A 188     1077   1470   1168    -47    221   -243       O  
ATOM   1102  CB  ALA A 188      62.115  34.128  16.355  1.00  8.80           C  
ANISOU 1102  CB  ALA A 188     1029   1296   1018   -187    121    -16       C  
ATOM   1103  N   GLY A 189      61.413  31.108  17.746  1.00  8.00           N  
ANISOU 1103  N   GLY A 189      875   1086   1078    -32     24   -134       N  
ATOM   1104  CA  GLY A 189      61.808  29.720  17.888  1.00  8.74           C  
ANISOU 1104  CA  GLY A 189     1003   1123   1195     47      0    -96       C  
ATOM   1105  C   GLY A 189      60.657  28.726  17.836  1.00  8.25           C  
ANISOU 1105  C   GLY A 189      985    964   1183     63    -34    -53       C  
ATOM   1106  O   GLY A 189      60.901  27.524  17.876  1.00 10.20           O  
ANISOU 1106  O   GLY A 189     1201   1047   1626    185    -55    -17       O  
ATOM   1107  N   VAL A 190      59.416  29.208  17.734  1.00  7.28           N  
ANISOU 1107  N   VAL A 190      861    812   1092     11    -10    -32       N  
ATOM   1108  CA  VAL A 190      58.238  28.347  17.741  1.00  7.25           C  
ANISOU 1108  CA  VAL A 190      921    799   1034     -8    -42     36       C  
ATOM   1109  C   VAL A 190      57.976  27.745  16.364  1.00  7.08           C  
ANISOU 1109  C   VAL A 190      853    784   1054     20     -1     74       C  
ATOM   1110  O   VAL A 190      57.885  28.473  15.381  1.00  8.08           O  
ANISOU 1110  O   VAL A 190     1170    873   1024    -92     11     78       O  
ATOM   1111  CB  VAL A 190      57.010  29.141  18.207  1.00  7.51           C  
ANISOU 1111  CB  VAL A 190      963    853   1036      0      0     42       C  
ATOM   1112  CG1 VAL A 190      55.741  28.341  18.012  1.00  7.69           C  
ANISOU 1112  CG1 VAL A 190     1020    857   1045   -140    -23    -74       C  
ATOM   1113  CG2 VAL A 190      57.199  29.557  19.653  1.00  8.66           C  
ANISOU 1113  CG2 VAL A 190     1078    857   1353    -35     45    -24       C  
ATOM   1114  N   GLN A 191      57.850  26.421  16.301  1.00  7.44           N  
ANISOU 1114  N   GLN A 191      913    821   1090     34    -96      6       N  
ATOM   1115  CA  GLN A 191      57.515  25.714  15.066  1.00  7.88           C  
ANISOU 1115  CA  GLN A 191      887    946   1160     98    -59    -64       C  
ATOM   1116  C   GLN A 191      56.373  24.749  15.330  1.00  7.28           C  
ANISOU 1116  C   GLN A 191      881    770   1116     88    -99     -8       C  
ATOM   1117  O   GLN A 191      56.584  23.603  15.702  1.00  8.57           O  
ANISOU 1117  O   GLN A 191      970    940   1346    227   -139    121       O  
ATOM   1118  CB  GLN A 191      58.726  24.959  14.498  1.00  9.67           C  
ANISOU 1118  CB  GLN A 191     1011   1229   1432     32    -21   -135       C  
ATOM   1119  CG  GLN A 191      58.470  24.328  13.147  1.00 14.30           C  
ANISOU 1119  CG  GLN A 191     1650   1903   1880     28     13    -95       C  
ATOM   1120  CD  GLN A 191      59.644  23.508  12.631  1.00 19.11           C  
ANISOU 1120  CD  GLN A 191     2157   2401   2703    -58    216     30       C  
ATOM   1121  OE1 GLN A 191      60.633  24.062  12.157  1.00 23.71           O  
ANISOU 1121  OE1 GLN A 191     2504   3157   3347    127    394    101       O  
ATOM   1122  NE2 GLN A 191      59.527  22.185  12.715  1.00 21.06           N  
ANISOU 1122  NE2 GLN A 191     2317   2561   3122    130    352    -23       N  
ATOM   1123  N   ILE A 192      55.157  25.220  15.121  1.00  6.59           N  
ANISOU 1123  N   ILE A 192      722    748   1035     81    -87     43       N  
ATOM   1124  CA  ILE A 192      53.983  24.394  15.377  1.00  7.18           C  
ANISOU 1124  CA  ILE A 192      829    891   1006      8    -56     38       C  
ATOM   1125  C   ILE A 192      53.882  23.270  14.339  1.00  7.76           C  
ANISOU 1125  C   ILE A 192      916    885   1144    -39    -82     25       C  
ATOM   1126  O   ILE A 192      53.562  22.133  14.671  1.00  9.03           O  
ANISOU 1126  O   ILE A 192     1095    907   1429    -59    -75     12       O  
ATOM   1127  CB  ILE A 192      52.688  25.238  15.411  1.00  6.69           C  
ANISOU 1127  CB  ILE A 192      768    853    918      0    -49    -13       C  
ATOM   1128  CG1 ILE A 192      52.782  26.330  16.483  1.00  7.20           C  
ANISOU 1128  CG1 ILE A 192      773    943   1017     32    -53    -31       C  
ATOM   1129  CG2 ILE A 192      51.467  24.354  15.695  1.00  8.38           C  
ANISOU 1129  CG2 ILE A 192      822   1139   1221    -93      2   -130       C  
ATOM   1130  CD1 ILE A 192      51.634  27.319  16.449  1.00  7.82           C  
ANISOU 1130  CD1 ILE A 192      893   1031   1045    114    -36    -37       C  
ATOM   1131  N   GLN A 193      54.155  23.613  13.088  1.00  8.10           N  
ANISOU 1131  N   GLN A 193     1018    952   1106     24    -99    -72       N  
ATOM   1132  CA  GLN A 193      54.092  22.689  11.962  1.00  9.58           C  
ANISOU 1132  CA  GLN A 193     1084   1303   1251    -15    -55   -141       C  
ATOM   1133  C   GLN A 193      55.272  22.871  11.018  1.00 10.17           C  
ANISOU 1133  C   GLN A 193     1165   1350   1347     51     -9   -148       C  
ATOM   1134  O   GLN A 193      55.763  23.979  10.814  1.00 11.67           O  
ANISOU 1134  O   GLN A 193     1375   1560   1496     86     18   -181       O  
ATOM   1135  CB  GLN A 193      52.793  22.896  11.171  1.00 10.78           C  
ANISOU 1135  CB  GLN A 193     1266   1476   1353     80   -118   -184       C  
ATOM   1136  CG  GLN A 193      51.536  22.656  11.979  1.00 11.65           C  
ANISOU 1136  CG  GLN A 193     1276   1571   1580    177    -47   -289       C  
ATOM   1137  CD  GLN A 193      51.367  21.212  12.385  1.00 11.12           C  
ANISOU 1137  CD  GLN A 193      990   1603   1629    122     61   -326       C  
ATOM   1138  OE1 GLN A 193      52.082  20.337  11.902  1.00 11.75           O  
ANISOU 1138  OE1 GLN A 193     1116   1549   1800    275    141   -635       O  
ATOM   1139  NE2 GLN A 193      50.408  20.949  13.253  1.00 13.04           N  
ANISOU 1139  NE2 GLN A 193     1184   1894   1875    -29    117   -559       N  
ATOM   1140  N   ARG A 194      55.689  21.765  10.397  1.00 11.17           N  
ANISOU 1140  N   ARG A 194     1283   1476   1484    144     36   -158       N  
ATOM   1141  CA  ARG A 194      56.844  21.758   9.498  1.00 13.29           C  
ANISOU 1141  CA  ARG A 194     1517   1807   1725    159     65    -84       C  
ATOM   1142  C   ARG A 194      56.466  21.932   8.031  1.00 13.03           C  
ANISOU 1142  C   ARG A 194     1436   1843   1669    120     75    -97       C  
ATOM   1143  O   ARG A 194      57.320  22.208   7.199  1.00 14.34           O  
ANISOU 1143  O   ARG A 194     1500   2120   1827    220    247   -178       O  
ATOM   1144  CB  ARG A 194      57.678  20.472   9.673  1.00 14.11           C  
ANISOU 1144  CB  ARG A 194     1570   1941   1849    177     50    -14       C  
ATOM   1145  CG  ARG A 194      57.071  19.206   9.083  1.00 17.66           C  
ANISOU 1145  CG  ARG A 194     1999   2383   2325    193     45    -40       C  
ATOM   1146  CD  ARG A 194      57.966  17.967   9.177  1.00 22.86           C  
ANISOU 1146  CD  ARG A 194     2759   2952   2975    100     54     56       C  
ATOM   1147  NE  ARG A 194      57.202  16.731   9.392  1.00 27.76           N  
ANISOU 1147  NE  ARG A 194     3536   3453   3557     50    -42    -22       N  
ATOM   1148  CZ  ARG A 194      57.309  15.588   8.694  1.00 31.28           C  
ANISOU 1148  CZ  ARG A 194     3975   3979   3929      6     67      2       C  
ATOM   1149  NH1 ARG A 194      58.161  15.453   7.678  1.00 32.04           N  
ANISOU 1149  NH1 ARG A 194     3948   4145   4081     46    128     -8       N  
ATOM   1150  NH2 ARG A 194      56.545  14.550   9.026  1.00 32.86           N  
ANISOU 1150  NH2 ARG A 194     4212   4141   4132     -9     37     10       N  
ATOM   1151  N   GLU A 195      55.187  21.791   7.705  1.00 12.96           N  
ANISOU 1151  N   GLU A 195     1448   1801   1673    151     48   -153       N  
ATOM   1152  CA  GLU A 195      54.752  21.763   6.308  1.00 12.58           C  
ANISOU 1152  CA  GLU A 195     1469   1709   1600    144     76   -162       C  
ATOM   1153  C   GLU A 195      54.992  23.114   5.627  1.00 12.65           C  
ANISOU 1153  C   GLU A 195     1423   1738   1645    151     59   -200       C  
ATOM   1154  O   GLU A 195      54.856  24.154   6.269  1.00 13.06           O  
ANISOU 1154  O   GLU A 195     1416   1812   1731    192    106   -295       O  
ATOM   1155  CB  GLU A 195      53.264  21.376   6.230  1.00 13.24           C  
ANISOU 1155  CB  GLU A 195     1509   1824   1695    148     20   -140       C  
ATOM   1156  CG  GLU A 195      52.976  19.888   6.413  1.00 14.44           C  
ANISOU 1156  CG  GLU A 195     1736   1978   1771    188     23   -200       C  
ATOM   1157  CD  GLU A 195      53.127  19.383   7.843  1.00 14.99           C  
ANISOU 1157  CD  GLU A 195     1873   1823   1999    469    -36   -236       C  
ATOM   1158  OE1 GLU A 195      52.953  20.162   8.801  1.00 12.97           O  
ANISOU 1158  OE1 GLU A 195     1088   1974   1866    630     99   -450       O  
ATOM   1159  OE2 GLU A 195      53.432  18.181   8.019  1.00 19.96           O  
ANISOU 1159  OE2 GLU A 195     2880   2217   2486    414      2   -248       O  
ATOM   1160  N   PRO A 196      55.345  23.106   4.341  1.00 12.25           N  
ANISOU 1160  N   PRO A 196     1387   1621   1646    187    141   -186       N  
ATOM   1161  CA  PRO A 196      55.574  24.356   3.609  1.00 12.41           C  
ANISOU 1161  CA  PRO A 196     1444   1639   1630     65    155   -162       C  
ATOM   1162  C   PRO A 196      54.308  25.168   3.340  1.00 11.65           C  
ANISOU 1162  C   PRO A 196     1363   1466   1597     46    209   -184       C  
ATOM   1163  O   PRO A 196      54.395  26.354   3.020  1.00 12.10           O  
ANISOU 1163  O   PRO A 196     1332   1488   1777    -45    273   -297       O  
ATOM   1164  CB  PRO A 196      56.231  23.887   2.306  1.00 12.98           C  
ANISOU 1164  CB  PRO A 196     1444   1783   1705    145    186   -109       C  
ATOM   1165  CG  PRO A 196      55.740  22.533   2.143  1.00 13.34           C  
ANISOU 1165  CG  PRO A 196     1551   1870   1645    162    244   -172       C  
ATOM   1166  CD  PRO A 196      55.660  21.930   3.510  1.00 12.89           C  
ANISOU 1166  CD  PRO A 196     1470   1761   1665    164    131   -238       C  
ATOM   1167  N   PHE A 197      53.147  24.531   3.435  1.00  9.92           N  
ANISOU 1167  N   PHE A 197     1181   1241   1345    -39    208   -185       N  
ATOM   1168  CA  PHE A 197      51.881  25.253   3.394  1.00  9.07           C  
ANISOU 1168  CA  PHE A 197     1136   1027   1282    -30    163   -112       C  
ATOM   1169  C   PHE A 197      50.873  24.447   4.181  1.00  7.91           C  
ANISOU 1169  C   PHE A 197     1066    757   1180    -74    204    -81       C  
ATOM   1170  O   PHE A 197      51.018  23.235   4.296  1.00  9.46           O  
ANISOU 1170  O   PHE A 197     1252    812   1527     62    233   -190       O  
ATOM   1171  CB  PHE A 197      51.379  25.511   1.964  1.00  9.75           C  
ANISOU 1171  CB  PHE A 197     1189   1218   1296   -101    229   -141       C  
ATOM   1172  CG  PHE A 197      51.202  24.272   1.149  1.00 11.77           C  
ANISOU 1172  CG  PHE A 197     1430   1410   1631     42     39   -125       C  
ATOM   1173  CD1 PHE A 197      52.269  23.754   0.420  1.00 13.98           C  
ANISOU 1173  CD1 PHE A 197     1712   1789   1810     86     25   -224       C  
ATOM   1174  CD2 PHE A 197      49.981  23.609   1.102  1.00 13.21           C  
ANISOU 1174  CD2 PHE A 197     1785   1456   1775   -104      1    -81       C  
ATOM   1175  CE1 PHE A 197      52.124  22.598  -0.331  1.00 16.01           C  
ANISOU 1175  CE1 PHE A 197     1953   2040   2088     10     78   -231       C  
ATOM   1176  CE2 PHE A 197      49.833  22.430   0.354  1.00 14.91           C  
ANISOU 1176  CE2 PHE A 197     1802   1812   2049    -73    -41   -149       C  
ATOM   1177  CZ  PHE A 197      50.907  21.937  -0.355  1.00 16.01           C  
ANISOU 1177  CZ  PHE A 197     2001   1864   2215    -54    -76   -249       C  
ATOM   1178  N   PRO A 198      49.845  25.095   4.718  1.00  7.29           N  
ANISOU 1178  N   PRO A 198      950    768   1050    -36    221    -68       N  
ATOM   1179  CA  PRO A 198      49.670  26.554   4.747  1.00  6.26           C  
ANISOU 1179  CA  PRO A 198      869    713    795     -6    127     12       C  
ATOM   1180  C   PRO A 198      50.622  27.252   5.713  1.00  6.09           C  
ANISOU 1180  C   PRO A 198      850    723    737     36    119     80       C  
ATOM   1181  O   PRO A 198      50.997  26.681   6.721  1.00  7.17           O  
ANISOU 1181  O   PRO A 198     1090    728    905    -52     20    148       O  
ATOM   1182  CB  PRO A 198      48.226  26.708   5.243  1.00  6.74           C  
ANISOU 1182  CB  PRO A 198      891    837    833    -28     82    -63       C  
ATOM   1183  CG  PRO A 198      47.954  25.465   6.021  1.00  7.79           C  
ANISOU 1183  CG  PRO A 198      892    949   1118    -59     68     19       C  
ATOM   1184  CD  PRO A 198      48.739  24.384   5.377  1.00  7.64           C  
ANISOU 1184  CD  PRO A 198      969    918   1016   -175    168     42       C  
ATOM   1185  N   GLN A 199      50.972  28.488   5.391  1.00  5.41           N  
ANISOU 1185  N   GLN A 199      802    577    674     15     96     22       N  
ATOM   1186  CA  GLN A 199      51.658  29.403   6.300  1.00  5.67           C  
ANISOU 1186  CA  GLN A 199      753    615    785      3     66     41       C  
ATOM   1187  C   GLN A 199      50.791  30.633   6.469  1.00  5.08           C  
ANISOU 1187  C   GLN A 199      759    493    676     60     31     80       C  
ATOM   1188  O   GLN A 199      50.200  31.127   5.517  1.00  5.98           O  
ANISOU 1188  O   GLN A 199     1021    605    645    174     55     59       O  
ATOM   1189  CB  GLN A 199      53.018  29.827   5.745  1.00  6.20           C  
ANISOU 1189  CB  GLN A 199      812    641    902     10     78     32       C  
ATOM   1190  CG  GLN A 199      54.002  28.675   5.642  1.00  7.22           C  
ANISOU 1190  CG  GLN A 199      832    734   1178     31    166      3       C  
ATOM   1191  CD  GLN A 199      55.349  29.134   5.155  1.00  7.10           C  
ANISOU 1191  CD  GLN A 199      752    658   1287   -100    101     46       C  
ATOM   1192  OE1 GLN A 199      55.901  30.088   5.675  1.00  9.06           O  
ANISOU 1192  OE1 GLN A 199      884    956   1601   -185    186    102       O  
ATOM   1193  NE2 GLN A 199      55.899  28.437   4.178  1.00 10.88           N  
ANISOU 1193  NE2 GLN A 199     1206   1192   1732    -79    588   -227       N  
ATOM   1194  N   TYR A 200      50.723  31.116   7.706  1.00  4.83           N  
ANISOU 1194  N   TYR A 200      659    602    572    -12    -22     47       N  
ATOM   1195  CA  TYR A 200      49.723  32.110   8.070  1.00  4.98           C  
ANISOU 1195  CA  TYR A 200      633    633    625     58      9     61       C  
ATOM   1196  C   TYR A 200      50.260  33.483   8.471  1.00  5.10           C  
ANISOU 1196  C   TYR A 200      699    611    625     42     37    104       C  
ATOM   1197  O   TYR A 200      49.697  34.490   8.068  1.00  5.80           O  
ANISOU 1197  O   TYR A 200      764    586    852     54     -3    108       O  
ATOM   1198  CB  TYR A 200      48.867  31.566   9.201  1.00  5.07           C  
ANISOU 1198  CB  TYR A 200      664    706    555    -23    130     -4       C  
ATOM   1199  CG  TYR A 200      48.158  30.263   8.874  1.00  5.20           C  
ANISOU 1199  CG  TYR A 200      628    726    618     25    128      2       C  
ATOM   1200  CD1 TYR A 200      47.099  30.234   7.982  1.00  5.47           C  
ANISOU 1200  CD1 TYR A 200      703    652    723     53    -33     93       C  
ATOM   1201  CD2 TYR A 200      48.538  29.067   9.467  1.00  5.29           C  
ANISOU 1201  CD2 TYR A 200      655    708    645    -68     56    101       C  
ATOM   1202  CE1 TYR A 200      46.418  29.067   7.719  1.00  5.52           C  
ANISOU 1202  CE1 TYR A 200      582    776    738    -30    -89      8       C  
ATOM   1203  CE2 TYR A 200      47.871  27.884   9.190  1.00  5.58           C  
ANISOU 1203  CE2 TYR A 200      726    685    706     27     94     65       C  
ATOM   1204  CZ  TYR A 200      46.804  27.898   8.329  1.00  4.50           C  
ANISOU 1204  CZ  TYR A 200      614    581    513     38     72     -2       C  
ATOM   1205  OH  TYR A 200      46.142  26.725   8.111  1.00  5.39           O  
ANISOU 1205  OH  TYR A 200      724    591    731   -112     83     48       O  
ATOM   1206  N   SER A 201      51.298  33.515   9.306  1.00  4.77           N  
ANISOU 1206  N   SER A 201      643    546    620     17     24     62       N  
ATOM   1207  CA  SER A 201      51.721  34.757   9.955  1.00  5.39           C  
ANISOU 1207  CA  SER A 201      725    588    732      9     41     85       C  
ATOM   1208  C   SER A 201      53.006  34.492  10.711  1.00  4.93           C  
ANISOU 1208  C   SER A 201      658    602    612     -6     39     77       C  
ATOM   1209  O   SER A 201      53.189  33.385  11.219  1.00  5.48           O  
ANISOU 1209  O   SER A 201      744    615    723     27     -9    134       O  
ATOM   1210  CB  SER A 201      50.667  35.177  10.985  1.00  5.85           C  
ANISOU 1210  CB  SER A 201      733    668    822      9     34     51       C  
ATOM   1211  OG  SER A 201      51.086  36.309  11.740  1.00  6.39           O  
ANISOU 1211  OG  SER A 201      882    608    938    -25    -30    -48       O  
ATOM   1212  N   PRO A 202      53.862  35.498  10.862  1.00  5.41           N  
ANISOU 1212  N   PRO A 202      710    641    702    -42     -6    128       N  
ATOM   1213  CA  PRO A 202      55.037  35.345  11.730  1.00  5.85           C  
ANISOU 1213  CA  PRO A 202      718    715    788    -44     -5     81       C  
ATOM   1214  C   PRO A 202      54.701  35.376  13.218  1.00  5.55           C  
ANISOU 1214  C   PRO A 202      656    663    789   -111     -2    100       C  
ATOM   1215  O   PRO A 202      55.540  35.009  14.025  1.00  6.38           O  
ANISOU 1215  O   PRO A 202      789    808    824    -21    -35    102       O  
ATOM   1216  CB  PRO A 202      55.898  36.566  11.370  1.00  6.63           C  
ANISOU 1216  CB  PRO A 202      805    929    783   -179     53    123       C  
ATOM   1217  CG  PRO A 202      54.889  37.605  10.975  1.00  6.82           C  
ANISOU 1217  CG  PRO A 202      930    869    790   -191    113     70       C  
ATOM   1218  CD  PRO A 202      53.841  36.826  10.220  1.00  5.90           C  
ANISOU 1218  CD  PRO A 202      832    614    796    -19     40    193       C  
ATOM   1219  N   GLU A 203      53.502  35.841  13.570  1.00  5.46           N  
ANISOU 1219  N   GLU A 203      663    628    782    -52    -10     54       N  
ATOM   1220  CA  GLU A 203      53.075  35.906  14.956  1.00  5.75           C  
ANISOU 1220  CA  GLU A 203      820    613    752    -23     -2    -54       C  
ATOM   1221  C   GLU A 203      52.170  34.727  15.276  1.00  5.55           C  
ANISOU 1221  C   GLU A 203      783    602    722    -30     42    -23       C  
ATOM   1222  O   GLU A 203      51.694  34.022  14.379  1.00  5.62           O  
ANISOU 1222  O   GLU A 203      803    661    668    -54     39    -15       O  
ATOM   1223  CB  GLU A 203      52.371  37.224  15.280  1.00  6.31           C  
ANISOU 1223  CB  GLU A 203      878    629    890    -68      1     -5       C  
ATOM   1224  CG  GLU A 203      53.195  38.455  14.941  1.00  7.90           C  
ANISOU 1224  CG  GLU A 203     1103    725   1173    -67     81    -21       C  
ATOM   1225  CD  GLU A 203      54.517  38.574  15.686  1.00  8.63           C  
ANISOU 1225  CD  GLU A 203     1371    722   1183   -265    187     88       C  
ATOM   1226  OE1 GLU A 203      54.694  37.962  16.768  1.00  9.23           O  
ANISOU 1226  OE1 GLU A 203     1170   1008   1329   -330     67    -50       O  
ATOM   1227  OE2 GLU A 203      55.377  39.339  15.190  1.00 11.13           O  
ANISOU 1227  OE2 GLU A 203     1495   1177   1556   -398    -68    111       O  
ATOM   1228  N   LEU A 204      51.972  34.504  16.566  1.00  5.75           N  
ANISOU 1228  N   LEU A 204      784    700    698   -106    -20      8       N  
ATOM   1229  CA  LEU A 204      51.072  33.479  17.067  1.00  5.76           C  
ANISOU 1229  CA  LEU A 204      878    656    654    -74     33    -11       C  
ATOM   1230  C   LEU A 204      49.646  34.014  17.117  1.00  5.52           C  
ANISOU 1230  C   LEU A 204      824    557    716    -86     87    -16       C  
ATOM   1231  O   LEU A 204      49.429  35.159  17.501  1.00  6.90           O  
ANISOU 1231  O   LEU A 204      952    531   1136    -70    109   -180       O  
ATOM   1232  CB  LEU A 204      51.513  33.090  18.467  1.00  6.79           C  
ANISOU 1232  CB  LEU A 204     1020    771    789     44     34     25       C  
ATOM   1233  CG  LEU A 204      51.116  31.737  19.020  1.00  8.61           C  
ANISOU 1233  CG  LEU A 204     1078   1049   1141    -46    -66     29       C  
ATOM   1234  CD1 LEU A 204      51.774  30.615  18.238  1.00  9.26           C  
ANISOU 1234  CD1 LEU A 204     1531    760   1226    101   -294    -48       C  
ATOM   1235  CD2 LEU A 204      51.459  31.643  20.510  1.00  9.50           C  
ANISOU 1235  CD2 LEU A 204     1379   1104   1123    122     69    130       C  
ATOM   1236  N   HIS A 205      48.695  33.158  16.793  1.00  5.11           N  
ANISOU 1236  N   HIS A 205      731    545    663    -50     45    -41       N  
ATOM   1237  CA  HIS A 205      47.291  33.522  16.787  1.00  5.66           C  
ANISOU 1237  CA  HIS A 205      818    609    723    -33     25    -24       C  
ATOM   1238  C   HIS A 205      46.425  32.369  17.241  1.00  4.95           C  
ANISOU 1238  C   HIS A 205      724    568    587    -11     62    -27       C  
ATOM   1239  O   HIS A 205      46.871  31.225  17.327  1.00  5.39           O  
ANISOU 1239  O   HIS A 205      785    546    717     20    119    -15       O  
ATOM   1240  CB  HIS A 205      46.887  33.921  15.380  1.00  6.33           C  
ANISOU 1240  CB  HIS A 205      779    761    863    -56     60     95       C  
ATOM   1241  CG  HIS A 205      47.627  35.099  14.856  1.00  8.15           C  
ANISOU 1241  CG  HIS A 205      998    951   1147    -34     77    113       C  
ATOM   1242  ND1 HIS A 205      48.615  35.010  13.900  1.00 10.97           N  
ANISOU 1242  ND1 HIS A 205     1467   1461   1238   -181     77    393       N  
ATOM   1243  CD2 HIS A 205      47.579  36.399  15.216  1.00 11.21           C  
ANISOU 1243  CD2 HIS A 205     1874    925   1460    -46    487    126       C  
ATOM   1244  CE1 HIS A 205      49.079  36.218  13.632  1.00  8.85           C  
ANISOU 1244  CE1 HIS A 205     1290   1067   1004   -240     25    257       C  
ATOM   1245  NE2 HIS A 205      48.467  37.079  14.416  1.00 11.87           N  
ANISOU 1245  NE2 HIS A 205     1734   1250   1523   -247    173    160       N  
ATOM   1246  N   PHE A 206      45.160  32.676  17.484  1.00  5.04           N  
ANISOU 1246  N   PHE A 206      697    452    764     -4     73    -46       N  
ATOM   1247  CA  PHE A 206      44.154  31.697  17.883  1.00  4.86           C  
ANISOU 1247  CA  PHE A 206      752    496    597     -2     39    -59       C  
ATOM   1248  C   PHE A 206      42.938  31.843  16.978  1.00  4.41           C  
ANISOU 1248  C   PHE A 206      753    409    513     53     94    -84       C  
ATOM   1249  O   PHE A 206      42.390  32.925  16.839  1.00  6.04           O  
ANISOU 1249  O   PHE A 206     1042    526    726     79   -134    -99       O  
ATOM   1250  CB  PHE A 206      43.759  31.933  19.333  1.00  5.01           C  
ANISOU 1250  CB  PHE A 206      793    588    520     80    -39     -8       C  
ATOM   1251  CG  PHE A 206      42.633  31.062  19.820  1.00  4.47           C  
ANISOU 1251  CG  PHE A 206      723    549    425    -15     25    -18       C  
ATOM   1252  CD1 PHE A 206      42.840  29.719  20.106  1.00  4.98           C  
ANISOU 1252  CD1 PHE A 206      627    606    657     71    -42    -27       C  
ATOM   1253  CD2 PHE A 206      41.372  31.589  20.036  1.00  5.40           C  
ANISOU 1253  CD2 PHE A 206      892    562    596    144    118     44       C  
ATOM   1254  CE1 PHE A 206      41.810  28.920  20.558  1.00  5.46           C  
ANISOU 1254  CE1 PHE A 206      843    475    754    -39      1    -24       C  
ATOM   1255  CE2 PHE A 206      40.348  30.783  20.509  1.00  5.26           C  
ANISOU 1255  CE2 PHE A 206      886    546    566    114    170     30       C  
ATOM   1256  CZ  PHE A 206      40.565  29.466  20.778  1.00  5.67           C  
ANISOU 1256  CZ  PHE A 206      827    687    638     51     78    -79       C  
ATOM   1257  N   PHE A 207      42.541  30.735  16.374  1.00  4.19           N  
ANISOU 1257  N   PHE A 207      607    384    598     29     58    -29       N  
ATOM   1258  CA  PHE A 207      41.389  30.696  15.463  1.00  4.08           C  
ANISOU 1258  CA  PHE A 207      590    409    550     -5     47     -2       C  
ATOM   1259  C   PHE A 207      40.259  29.956  16.165  1.00  4.08           C  
ANISOU 1259  C   PHE A 207      556    441    552     16     59    -43       C  
ATOM   1260  O   PHE A 207      40.292  28.732  16.295  1.00  5.03           O  
ANISOU 1260  O   PHE A 207      733    468    708    -10    225    -17       O  
ATOM   1261  CB  PHE A 207      41.810  29.967  14.194  1.00  4.91           C  
ANISOU 1261  CB  PHE A 207      612    654    599      9     20    -47       C  
ATOM   1262  CG  PHE A 207      40.757  29.813  13.145  1.00  5.26           C  
ANISOU 1262  CG  PHE A 207      752    740    506     18    187   -110       C  
ATOM   1263  CD1 PHE A 207      40.491  30.805  12.229  1.00  7.36           C  
ANISOU 1263  CD1 PHE A 207      947    962    888    199    -58    -90       C  
ATOM   1264  CD2 PHE A 207      40.125  28.596  12.994  1.00  7.78           C  
ANISOU 1264  CD2 PHE A 207      916   1065    975   -110    -61   -338       C  
ATOM   1265  CE1 PHE A 207      39.559  30.566  11.189  1.00  8.93           C  
ANISOU 1265  CE1 PHE A 207     1081   1269   1040    375     49    -88       C  
ATOM   1266  CE2 PHE A 207      39.228  28.365  11.985  1.00  9.30           C  
ANISOU 1266  CE2 PHE A 207      963   1381   1190   -121    125   -586       C  
ATOM   1267  CZ  PHE A 207      38.957  29.326  11.076  1.00  9.56           C  
ANISOU 1267  CZ  PHE A 207      875   1660   1098    196    -18   -460       C  
ATOM   1268  N   ALA A 208      39.259  30.682  16.646  1.00  4.06           N  
ANISOU 1268  N   ALA A 208      570    382    589     58    101      2       N  
ATOM   1269  CA  ALA A 208      38.159  30.053  17.365  1.00  4.22           C  
ANISOU 1269  CA  ALA A 208      588    539    476     26     29    -20       C  
ATOM   1270  C   ALA A 208      37.280  29.262  16.420  1.00  4.03           C  
ANISOU 1270  C   ALA A 208      570    499    460     84    102    -26       C  
ATOM   1271  O   ALA A 208      36.950  29.759  15.341  1.00  4.52           O  
ANISOU 1271  O   ALA A 208      644    561    510     -1     64    -28       O  
ATOM   1272  CB  ALA A 208      37.314  31.116  18.066  1.00  4.33           C  
ANISOU 1272  CB  ALA A 208      633    482    527    100     43   -123       C  
ATOM   1273  N   PHE A 209      36.832  28.086  16.847  1.00  4.13           N  
ANISOU 1273  N   PHE A 209      617    508    443     78    -25    -84       N  
ATOM   1274  CA  PHE A 209      35.917  27.299  16.032  1.00  4.29           C  
ANISOU 1274  CA  PHE A 209      586    581    462     17     34    -46       C  
ATOM   1275  C   PHE A 209      34.767  26.643  16.799  1.00  4.92           C  
ANISOU 1275  C   PHE A 209      693    558    617      6     15    -26       C  
ATOM   1276  O   PHE A 209      33.910  26.054  16.175  1.00  5.88           O  
ANISOU 1276  O   PHE A 209      763    864    606   -210    -42    -73       O  
ATOM   1277  CB  PHE A 209      36.650  26.307  15.114  1.00  5.20           C  
ANISOU 1277  CB  PHE A 209      703    638    634     19     13   -128       C  
ATOM   1278  CG  PHE A 209      37.642  25.401  15.804  1.00  4.47           C  
ANISOU 1278  CG  PHE A 209      617    513    566     30     24    -87       C  
ATOM   1279  CD1 PHE A 209      38.946  25.329  15.351  1.00  5.09           C  
ANISOU 1279  CD1 PHE A 209      815    471    646      7    -46   -174       C  
ATOM   1280  CD2 PHE A 209      37.277  24.589  16.871  1.00  5.60           C  
ANISOU 1280  CD2 PHE A 209      755    557    814     69    158    -84       C  
ATOM   1281  CE1 PHE A 209      39.860  24.487  15.961  1.00  5.54           C  
ANISOU 1281  CE1 PHE A 209      707    515    881    -13     86   -144       C  
ATOM   1282  CE2 PHE A 209      38.197  23.770  17.490  1.00  5.62           C  
ANISOU 1282  CE2 PHE A 209      985    516    633    175    184     14       C  
ATOM   1283  CZ  PHE A 209      39.485  23.718  17.036  1.00  5.35           C  
ANISOU 1283  CZ  PHE A 209      915    433    683     71    -48   -239       C  
ATOM   1284  N   ASP A 210      34.671  26.790  18.117  1.00  4.48           N  
ANISOU 1284  N   ASP A 210      549    637    515     12     62      7       N  
ATOM   1285  CA  ASP A 210      33.506  26.278  18.829  1.00  4.54           C  
ANISOU 1285  CA  ASP A 210      596    600    527     27     61     -7       C  
ATOM   1286  C   ASP A 210      33.416  26.939  20.186  1.00  4.87           C  
ANISOU 1286  C   ASP A 210      653    694    503     70     47    -10       C  
ATOM   1287  O   ASP A 210      34.434  27.243  20.807  1.00  5.37           O  
ANISOU 1287  O   ASP A 210      615    793    632     47     77    -29       O  
ATOM   1288  CB  ASP A 210      33.563  24.747  18.986  1.00  5.40           C  
ANISOU 1288  CB  ASP A 210      715    677    661      2    109    -21       C  
ATOM   1289  CG  ASP A 210      32.703  24.004  17.990  1.00  6.24           C  
ANISOU 1289  CG  ASP A 210      583    801    985    123    122   -210       C  
ATOM   1290  OD1 ASP A 210      31.539  24.400  17.804  1.00  8.24           O  
ANISOU 1290  OD1 ASP A 210      765    893   1472     -7     91   -371       O  
ATOM   1291  OD2 ASP A 210      33.146  22.998  17.399  1.00  7.53           O  
ANISOU 1291  OD2 ASP A 210      822    935   1103    170    -36   -200       O  
ATOM   1292  N   ILE A 211      32.185  27.142  20.640  1.00  4.68           N  
ANISOU 1292  N   ILE A 211      494    709    574     20     76    -43       N  
ATOM   1293  CA  ILE A 211      31.895  27.621  21.985  1.00  5.50           C  
ANISOU 1293  CA  ILE A 211      690    796    601     -3     81     26       C  
ATOM   1294  C   ILE A 211      30.826  26.724  22.591  1.00  5.81           C  
ANISOU 1294  C   ILE A 211      682    784    738     17     96     57       C  
ATOM   1295  O   ILE A 211      29.774  26.520  21.974  1.00  6.36           O  
ANISOU 1295  O   ILE A 211      686    929    798    -64    110    155       O  
ATOM   1296  CB  ILE A 211      31.389  29.070  21.984  1.00  5.68           C  
ANISOU 1296  CB  ILE A 211      729    788    640     59     81      2       C  
ATOM   1297  CG1 ILE A 211      32.478  30.027  21.508  1.00  6.23           C  
ANISOU 1297  CG1 ILE A 211      851    820    696     43     77     66       C  
ATOM   1298  CG2 ILE A 211      30.879  29.474  23.380  1.00  6.65           C  
ANISOU 1298  CG2 ILE A 211      873    898    755     35     70    -42       C  
ATOM   1299  CD1 ILE A 211      31.979  31.393  21.132  1.00  7.18           C  
ANISOU 1299  CD1 ILE A 211     1059    911    758    -42     34     19       C  
ATOM   1300  N   LYS A 212      31.084  26.194  23.778  1.00  6.06           N  
ANISOU 1300  N   LYS A 212      656    883    764     11    150    122       N  
ATOM   1301  CA  LYS A 212      30.056  25.499  24.530  1.00  6.73           C  
ANISOU 1301  CA  LYS A 212      762    970    823     -1    170     84       C  
ATOM   1302  C   LYS A 212      30.102  25.925  25.984  1.00  7.26           C  
ANISOU 1302  C   LYS A 212      826   1055    877      0    238    164       C  
ATOM   1303  O   LYS A 212      31.136  26.343  26.501  1.00  7.49           O  
ANISOU 1303  O   LYS A 212      904   1076    865     44    284    100       O  
ATOM   1304  CB  LYS A 212      30.178  23.980  24.388  1.00  7.13           C  
ANISOU 1304  CB  LYS A 212      814    981    913    -70    204     74       C  
ATOM   1305  CG  LYS A 212      31.438  23.374  24.971  1.00  7.54           C  
ANISOU 1305  CG  LYS A 212      824    948   1091      5    263    160       C  
ATOM   1306  CD  LYS A 212      31.516  21.876  24.687  1.00  8.44           C  
ANISOU 1306  CD  LYS A 212     1024   1066   1115    130     92    148       C  
ATOM   1307  CE  LYS A 212      32.681  21.200  25.387  1.00  9.61           C  
ANISOU 1307  CE  LYS A 212     1172   1261   1218    142    169     51       C  
ATOM   1308  NZ  LYS A 212      32.762  19.757  25.023  1.00 10.24           N  
ANISOU 1308  NZ  LYS A 212     1316   1018   1556    263     -5   -120       N  
ATOM   1309  N   TYR A 213      28.964  25.807  26.652  1.00  8.18           N  
ANISOU 1309  N   TYR A 213      950   1287    868     33    244    140       N  
ATOM   1310  CA  TYR A 213      28.863  26.173  28.048  1.00  9.10           C  
ANISOU 1310  CA  TYR A 213     1137   1331    987      9    203    137       C  
ATOM   1311  C   TYR A 213      28.010  25.152  28.799  1.00  9.79           C  
ANISOU 1311  C   TYR A 213     1193   1497   1029    -11    272    182       C  
ATOM   1312  O   TYR A 213      27.052  24.616  28.258  1.00 10.39           O  
ANISOU 1312  O   TYR A 213     1205   1694   1046    -56    421    310       O  
ATOM   1313  CB  TYR A 213      28.288  27.585  28.209  1.00  9.99           C  
ANISOU 1313  CB  TYR A 213     1322   1393   1079     26    194    140       C  
ATOM   1314  CG  TYR A 213      26.865  27.751  27.724  1.00 10.25           C  
ANISOU 1314  CG  TYR A 213     1316   1469   1110     94    365     30       C  
ATOM   1315  CD1 TYR A 213      25.784  27.595  28.598  1.00 12.01           C  
ANISOU 1315  CD1 TYR A 213     1411   1916   1233    186    314     35       C  
ATOM   1316  CD2 TYR A 213      26.593  28.052  26.397  1.00 12.38           C  
ANISOU 1316  CD2 TYR A 213     1510   1827   1366    219    423    145       C  
ATOM   1317  CE1 TYR A 213      24.475  27.742  28.155  1.00 11.74           C  
ANISOU 1317  CE1 TYR A 213     1310   1834   1316    213    377    -34       C  
ATOM   1318  CE2 TYR A 213      25.287  28.190  25.946  1.00 12.74           C  
ANISOU 1318  CE2 TYR A 213     1591   1979   1270    304    288     78       C  
ATOM   1319  CZ  TYR A 213      24.232  28.035  26.833  1.00 13.36           C  
ANISOU 1319  CZ  TYR A 213     1434   2099   1541    234    205     80       C  
ATOM   1320  OH  TYR A 213      22.926  28.175  26.413  1.00 14.73           O  
ANISOU 1320  OH  TYR A 213     1467   2497   1633    505    218    -86       O  
ATOM   1321  N   SER A 214      28.401  24.861  30.028  1.00 10.36           N  
ANISOU 1321  N   SER A 214     1241   1563   1129     -2    314    240       N  
ATOM   1322  CA  SER A 214      27.632  23.989  30.905  1.00 11.23           C  
ANISOU 1322  CA  SER A 214     1409   1606   1251     11    347    179       C  
ATOM   1323  C   SER A 214      27.269  24.780  32.140  1.00 12.45           C  
ANISOU 1323  C   SER A 214     1561   1725   1444     64    321    174       C  
ATOM   1324  O   SER A 214      28.138  25.188  32.900  1.00 12.05           O  
ANISOU 1324  O   SER A 214     1614   1909   1054    115    608    223       O  
ATOM   1325  CB  SER A 214      28.446  22.771  31.309  1.00 11.65           C  
ANISOU 1325  CB  SER A 214     1579   1571   1273     35    305    207       C  
ATOM   1326  OG  SER A 214      27.737  22.044  32.291  1.00 13.02           O  
ANISOU 1326  OG  SER A 214     1768   1748   1429      7    533    519       O  
ATOM   1327  N   VAL A 215      25.977  25.012  32.330  1.00 12.94           N  
ANISOU 1327  N   VAL A 215     1610   1779   1526     35    396    152       N  
ATOM   1328  CA  VAL A 215      25.506  25.806  33.460  1.00 14.76           C  
ANISOU 1328  CA  VAL A 215     1880   1959   1769     27    296     61       C  
ATOM   1329  C   VAL A 215      25.888  25.132  34.784  1.00 14.82           C  
ANISOU 1329  C   VAL A 215     1866   2042   1724     17    416     61       C  
ATOM   1330  O   VAL A 215      26.523  25.743  35.618  1.00 14.66           O  
ANISOU 1330  O   VAL A 215     1894   2255   1420     -1    794     84       O  
ATOM   1331  CB  VAL A 215      23.993  26.079  33.344  1.00 15.29           C  
ANISOU 1331  CB  VAL A 215     1881   2040   1888     26    335     36       C  
ATOM   1332  CG1 VAL A 215      23.483  26.864  34.552  1.00 17.03           C  
ANISOU 1332  CG1 VAL A 215     2138   2239   2093     42    310    -36       C  
ATOM   1333  CG2 VAL A 215      23.682  26.820  32.027  1.00 17.22           C  
ANISOU 1333  CG2 VAL A 215     2122   2151   2267     44    251     -4       C  
ATOM   1334  N   SER A 216      25.588  23.846  34.916  1.00 15.58           N  
ANISOU 1334  N   SER A 216     2032   2081   1806     28    328     62       N  
ATOM   1335  CA  SER A 216      25.933  23.085  36.117  1.00 16.20           C  
ANISOU 1335  CA  SER A 216     2132   2148   1873     -3    233     91       C  
ATOM   1336  C   SER A 216      27.445  22.859  36.224  1.00 16.26           C  
ANISOU 1336  C   SER A 216     2168   2221   1786      0    241    118       C  
ATOM   1337  O   SER A 216      27.991  22.721  37.320  1.00 17.40           O  
ANISOU 1337  O   SER A 216     2345   2574   1689     56    383    151       O  
ATOM   1338  CB  SER A 216      25.210  21.737  36.095  1.00 16.70           C  
ANISOU 1338  CB  SER A 216     2213   2217   1914    -19    232    114       C  
ATOM   1339  OG  SER A 216      25.802  20.883  35.133  1.00 17.35           O  
ANISOU 1339  OG  SER A 216     2395   2111   2084    -78    485    294       O  
ATOM   1340  N   GLY A 217      28.118  22.834  35.072  1.00 15.37           N  
ANISOU 1340  N   GLY A 217     2087   2054   1696     13    247    146       N  
ATOM   1341  CA  GLY A 217      29.517  22.458  34.985  1.00 15.34           C  
ANISOU 1341  CA  GLY A 217     2075   1979   1774     -9    122    106       C  
ATOM   1342  C   GLY A 217      29.713  21.020  34.546  1.00 15.78           C  
ANISOU 1342  C   GLY A 217     2099   2051   1845     35     90    109       C  
ATOM   1343  O   GLY A 217      30.794  20.661  34.108  1.00 15.70           O  
ANISOU 1343  O   GLY A 217     2068   2073   1821    125    168    119       O  
ATOM   1344  N   ALA A 218      28.673  20.197  34.662  1.00 15.24           N  
ANISOU 1344  N   ALA A 218     2079   1971   1739     26    123    124       N  
ATOM   1345  CA  ALA A 218      28.756  18.795  34.282  1.00 15.76           C  
ANISOU 1345  CA  ALA A 218     2100   1968   1919     28     95    122       C  
ATOM   1346  C   ALA A 218      28.910  18.623  32.775  1.00 15.52           C  
ANISOU 1346  C   ALA A 218     2117   1890   1890     35    115    164       C  
ATOM   1347  O   ALA A 218      28.307  19.363  31.989  1.00 14.57           O  
ANISOU 1347  O   ALA A 218     2080   1706   1749     47    236    375       O  
ATOM   1348  CB  ALA A 218      27.532  18.046  34.772  1.00 16.73           C  
ANISOU 1348  CB  ALA A 218     2222   2101   2030      6    121    142       C  
ATOM   1349  N   GLU A 219      29.705  17.632  32.382  1.00 16.12           N  
ANISOU 1349  N   GLU A 219     2184   1953   1987     10     71    142       N  
ATOM   1350  CA  GLU A 219      29.967  17.343  30.976  1.00 16.67           C  
ANISOU 1350  CA  GLU A 219     2212   1992   2130    -16     96    109       C  
ATOM   1351  C   GLU A 219      28.684  17.103  30.180  1.00 16.86           C  
ANISOU 1351  C   GLU A 219     2215   2028   2163    -51    113    123       C  
ATOM   1352  O   GLU A 219      28.535  17.568  29.050  1.00 16.76           O  
ANISOU 1352  O   GLU A 219     2216   2005   2147   -158    175    163       O  
ATOM   1353  CB  GLU A 219      30.864  16.105  30.858  1.00 17.27           C  
ANISOU 1353  CB  GLU A 219     2278   2053   2229     15     86     85       C  
ATOM   1354  CG  GLU A 219      31.492  15.913  29.484  1.00 19.58           C  
ANISOU 1354  CG  GLU A 219     2592   2342   2506      7    189    106       C  
ATOM   1355  CD  GLU A 219      32.713  16.793  29.232  1.00 21.43           C  
ANISOU 1355  CD  GLU A 219     2802   2528   2811    -19    195    102       C  
ATOM   1356  OE1 GLU A 219      33.159  17.537  30.130  1.00 22.59           O  
ANISOU 1356  OE1 GLU A 219     2847   2614   3122   -201    481    273       O  
ATOM   1357  OE2 GLU A 219      33.250  16.717  28.122  1.00 23.75           O  
ANISOU 1357  OE2 GLU A 219     3102   2903   3016   -455    361    381       O  
ATOM   1358  N   GLU A 220      27.748  16.376  30.781  1.00 17.05           N  
ANISOU 1358  N   GLU A 220     2271   2002   2203    -69     88    168       N  
ATOM   1359  CA  GLU A 220      26.516  16.008  30.093  1.00 17.61           C  
ANISOU 1359  CA  GLU A 220     2290   2124   2277    -56     92    131       C  
ATOM   1360  C   GLU A 220      25.578  17.197  29.861  1.00 16.92           C  
ANISOU 1360  C   GLU A 220     2208   2027   2194    -83     98    161       C  
ATOM   1361  O   GLU A 220      24.645  17.093  29.075  1.00 17.81           O  
ANISOU 1361  O   GLU A 220     2386   2074   2304   -142     96    173       O  
ATOM   1362  CB  GLU A 220      25.789  14.888  30.836  1.00 18.53           C  
ANISOU 1362  CB  GLU A 220     2410   2217   2410    -75     77    145       C  
ATOM   1363  CG  GLU A 220      25.267  15.282  32.208  1.00 20.37           C  
ANISOU 1363  CG  GLU A 220     2725   2393   2620   -105    144    168       C  
ATOM   1364  CD  GLU A 220      26.232  14.956  33.338  1.00 21.82           C  
ANISOU 1364  CD  GLU A 220     2966   2493   2830   -199    158    273       C  
ATOM   1365  OE1 GLU A 220      27.466  14.945  33.101  1.00 21.37           O  
ANISOU 1365  OE1 GLU A 220     3203   2100   2814   -438    237    401       O  
ATOM   1366  OE2 GLU A 220      25.751  14.718  34.478  1.00 24.13           O  
ANISOU 1366  OE2 GLU A 220     3424   2741   3001   -387    309    312       O  
ATOM   1367  N   ASP A 221      25.822  18.311  30.545  1.00 15.84           N  
ANISOU 1367  N   ASP A 221     2030   1948   2040    -94    159    201       N  
ATOM   1368  CA  ASP A 221      24.996  19.506  30.399  1.00 15.23           C  
ANISOU 1368  CA  ASP A 221     1894   1932   1960   -101    216    197       C  
ATOM   1369  C   ASP A 221      25.567  20.556  29.458  1.00 13.46           C  
ANISOU 1369  C   ASP A 221     1608   1759   1747    -67    299    254       C  
ATOM   1370  O   ASP A 221      25.019  21.653  29.374  1.00 13.72           O  
ANISOU 1370  O   ASP A 221     1529   1835   1847    -51    501    451       O  
ATOM   1371  CB  ASP A 221      24.778  20.149  31.765  1.00 15.70           C  
ANISOU 1371  CB  ASP A 221     1984   1982   1996   -150    227    234       C  
ATOM   1372  CG  ASP A 221      23.989  19.274  32.694  1.00 18.25           C  
ANISOU 1372  CG  ASP A 221     2274   2354   2303   -316    366    303       C  
ATOM   1373  OD1 ASP A 221      23.201  18.448  32.193  1.00 21.13           O  
ANISOU 1373  OD1 ASP A 221     2593   3022   2412   -563    810    636       O  
ATOM   1374  OD2 ASP A 221      24.108  19.355  33.929  1.00 20.61           O  
ANISOU 1374  OD2 ASP A 221     2596   2687   2548   -511    824    453       O  
ATOM   1375  N   PHE A 222      26.648  20.252  28.748  1.00 12.34           N  
ANISOU 1375  N   PHE A 222     1465   1604   1619      1    257    248       N  
ATOM   1376  CA  PHE A 222      27.171  21.223  27.800  1.00 11.54           C  
ANISOU 1376  CA  PHE A 222     1389   1545   1448    -46    207    161       C  
ATOM   1377  C   PHE A 222      26.120  21.547  26.740  1.00 11.30           C  
ANISOU 1377  C   PHE A 222     1265   1523   1505    -46    188    127       C  
ATOM   1378  O   PHE A 222      25.434  20.654  26.228  1.00 12.86           O  
ANISOU 1378  O   PHE A 222     1406   1615   1865   -130    165    246       O  
ATOM   1379  CB  PHE A 222      28.449  20.714  27.121  1.00 11.73           C  
ANISOU 1379  CB  PHE A 222     1349   1633   1474    -13    251    132       C  
ATOM   1380  CG  PHE A 222      29.716  21.066  27.861  1.00 11.00           C  
ANISOU 1380  CG  PHE A 222     1312   1566   1301     23    239    218       C  
ATOM   1381  CD1 PHE A 222      30.053  22.388  28.100  1.00  9.98           C  
ANISOU 1381  CD1 PHE A 222     1219   1410   1161     -1    301    211       C  
ATOM   1382  CD2 PHE A 222      30.572  20.075  28.318  1.00 11.24           C  
ANISOU 1382  CD2 PHE A 222     1369   1552   1348    -15    240    215       C  
ATOM   1383  CE1 PHE A 222      31.214  22.716  28.773  1.00 10.17           C  
ANISOU 1383  CE1 PHE A 222     1341   1468   1052    -67    240    164       C  
ATOM   1384  CE2 PHE A 222      31.740  20.408  28.987  1.00 11.02           C  
ANISOU 1384  CE2 PHE A 222     1312   1576   1297     88    159    219       C  
ATOM   1385  CZ  PHE A 222      32.055  21.727  29.212  1.00 10.77           C  
ANISOU 1385  CZ  PHE A 222     1205   1547   1339    -65    302    251       C  
ATOM   1386  N   VAL A 223      26.035  22.828  26.411  1.00 10.43           N  
ANISOU 1386  N   VAL A 223     1093   1485   1383    -66    249    165       N  
ATOM   1387  CA  VAL A 223      25.230  23.347  25.315  1.00 10.08           C  
ANISOU 1387  CA  VAL A 223     1057   1479   1292    -35    236     89       C  
ATOM   1388  C   VAL A 223      26.205  23.972  24.318  1.00  8.82           C  
ANISOU 1388  C   VAL A 223      825   1318   1205    -42    219    105       C  
ATOM   1389  O   VAL A 223      26.967  24.855  24.669  1.00  8.59           O  
ANISOU 1389  O   VAL A 223      961   1268   1033    -49    276      3       O  
ATOM   1390  CB  VAL A 223      24.244  24.414  25.819  1.00 10.69           C  
ANISOU 1390  CB  VAL A 223     1151   1599   1309     18    273    103       C  
ATOM   1391  CG1 VAL A 223      23.513  25.057  24.660  1.00 11.99           C  
ANISOU 1391  CG1 VAL A 223     1264   1722   1569    124    257    122       C  
ATOM   1392  CG2 VAL A 223      23.257  23.799  26.816  1.00 12.04           C  
ANISOU 1392  CG2 VAL A 223     1234   1875   1463     67    365    110       C  
ATOM   1393  N   LEU A 224      26.168  23.493  23.088  1.00  8.70           N  
ANISOU 1393  N   LEU A 224      911   1156   1235    -75    226     72       N  
ATOM   1394  CA  LEU A 224      27.019  23.989  22.026  1.00  8.23           C  
ANISOU 1394  CA  LEU A 224      922   1110   1093    -52    157     32       C  
ATOM   1395  C   LEU A 224      26.317  25.098  21.264  1.00  7.49           C  
ANISOU 1395  C   LEU A 224      799   1026   1019    -19    129    -16       C  
ATOM   1396  O   LEU A 224      25.157  24.945  20.894  1.00  8.97           O  
ANISOU 1396  O   LEU A 224      810   1261   1337   -102     60     -2       O  
ATOM   1397  CB  LEU A 224      27.327  22.825  21.093  1.00  9.17           C  
ANISOU 1397  CB  LEU A 224     1020   1219   1242    -78    202      6       C  
ATOM   1398  CG  LEU A 224      28.348  23.056  19.987  1.00  9.77           C  
ANISOU 1398  CG  LEU A 224     1242   1286   1180     -7     96    -21       C  
ATOM   1399  CD1 LEU A 224      29.725  23.376  20.537  1.00  9.18           C  
ANISOU 1399  CD1 LEU A 224      998   1208   1283    -89    234    -76       C  
ATOM   1400  CD2 LEU A 224      28.410  21.834  19.078  1.00 10.60           C  
ANISOU 1400  CD2 LEU A 224     1195   1360   1470   -114    122   -291       C  
ATOM   1401  N   LEU A 225      26.994  26.218  21.040  1.00  7.19           N  
ANISOU 1401  N   LEU A 225      804   1023    902      4     79     -6       N  
ATOM   1402  CA  LEU A 225      26.421  27.253  20.188  1.00  7.00           C  
ANISOU 1402  CA  LEU A 225      748    955    956     38     77    -16       C  
ATOM   1403  C   LEU A 225      26.317  26.770  18.758  1.00  6.71           C  
ANISOU 1403  C   LEU A 225      713    865    968     51     13    -16       C  
ATOM   1404  O   LEU A 225      27.252  26.178  18.231  1.00  7.13           O  
ANISOU 1404  O   LEU A 225      790    883   1037    105    -20   -117       O  
ATOM   1405  CB  LEU A 225      27.243  28.549  20.247  1.00  6.82           C  
ANISOU 1405  CB  LEU A 225      754    971    867      9     54    -99       C  
ATOM   1406  CG  LEU A 225      27.296  29.274  21.595  1.00  8.80           C  
ANISOU 1406  CG  LEU A 225     1091   1242   1010     29     90    -98       C  
ATOM   1407  CD1 LEU A 225      27.938  30.630  21.427  1.00  8.14           C  
ANISOU 1407  CD1 LEU A 225      974   1011   1105    176    -40   -235       C  
ATOM   1408  CD2 LEU A 225      25.946  29.449  22.241  1.00 10.97           C  
ANISOU 1408  CD2 LEU A 225     1444   1491   1230    -76    111   -200       C  
ATOM   1409  N   GLY A 226      25.175  27.033  18.133  1.00  7.08           N  
ANISOU 1409  N   GLY A 226      746    929   1014     54     24    -67       N  
ATOM   1410  CA  GLY A 226      25.039  26.869  16.704  1.00  6.86           C  
ANISOU 1410  CA  GLY A 226      773    837    996     84    -25   -108       C  
ATOM   1411  C   GLY A 226      25.896  27.870  15.955  1.00  6.61           C  
ANISOU 1411  C   GLY A 226      685    807   1019     70    -25   -145       C  
ATOM   1412  O   GLY A 226      26.406  28.821  16.539  1.00  7.19           O  
ANISOU 1412  O   GLY A 226      854    761   1113    -37     -9   -210       O  
ATOM   1413  N   TYR A 227      26.044  27.687  14.646  1.00  6.91           N  
ANISOU 1413  N   TYR A 227      781    835   1007    -33     29   -166       N  
ATOM   1414  CA  TYR A 227      26.919  28.543  13.853  1.00  7.24           C  
ANISOU 1414  CA  TYR A 227      769    958   1024      2     74   -213       C  
ATOM   1415  C   TYR A 227      26.574  30.023  13.980  1.00  6.76           C  
ANISOU 1415  C   TYR A 227      751    954    861     -7     98   -228       C  
ATOM   1416  O   TYR A 227      27.445  30.851  14.203  1.00  6.25           O  
ANISOU 1416  O   TYR A 227      736    877    761   -117    102   -198       O  
ATOM   1417  CB  TYR A 227      26.930  28.122  12.352  1.00  7.91           C  
ANISOU 1417  CB  TYR A 227      861   1032   1113    -74    180   -343       C  
ATOM   1418  CG  TYR A 227      27.696  29.136  11.473  1.00  9.15           C  
ANISOU 1418  CG  TYR A 227     1058   1128   1291   -125    128   -539       C  
ATOM   1419  CD1 TYR A 227      29.083  29.141  11.432  1.00 10.29           C  
ANISOU 1419  CD1 TYR A 227     1215   1089   1604     45     -1   -336       C  
ATOM   1420  CD2 TYR A 227      27.011  30.140  10.784  1.00 10.53           C  
ANISOU 1420  CD2 TYR A 227     1443   1373   1183   -160    158   -149       C  
ATOM   1421  CE1 TYR A 227      29.782  30.112  10.719  1.00  8.22           C  
ANISOU 1421  CE1 TYR A 227     1129    903   1091    -52    312   -114       C  
ATOM   1422  CE2 TYR A 227      27.690  31.107  10.066  1.00 10.52           C  
ANISOU 1422  CE2 TYR A 227     1357   1311   1328    185    -27    104       C  
ATOM   1423  CZ  TYR A 227      29.078  31.065  10.038  1.00  9.31           C  
ANISOU 1423  CZ  TYR A 227     1053   1274   1209    247    -15   -230       C  
ATOM   1424  OH  TYR A 227      29.796  32.020   9.359  1.00 10.28           O  
ANISOU 1424  OH  TYR A 227     1245   1307   1352     49     93     37       O  
ATOM   1425  N   ASP A 228      25.310  30.366  13.791  1.00  7.22           N  
ANISOU 1425  N   ASP A 228      775    939   1026      2    -40   -155       N  
ATOM   1426  CA  ASP A 228      24.946  31.778  13.815  1.00  7.96           C  
ANISOU 1426  CA  ASP A 228      918   1043   1064     19    -35    -98       C  
ATOM   1427  C   ASP A 228      25.205  32.398  15.177  1.00  7.24           C  
ANISOU 1427  C   ASP A 228      826    895   1027    105    -23   -120       C  
ATOM   1428  O   ASP A 228      25.679  33.525  15.246  1.00  7.82           O  
ANISOU 1428  O   ASP A 228     1041    880   1050    120    -20    -95       O  
ATOM   1429  CB  ASP A 228      23.484  31.992  13.407  1.00  9.17           C  
ANISOU 1429  CB  ASP A 228     1005   1185   1294    -15   -193    -47       C  
ATOM   1430  CG  ASP A 228      23.252  31.843  11.931  1.00 11.34           C  
ANISOU 1430  CG  ASP A 228     1204   1629   1476    -18   -180      3       C  
ATOM   1431  OD1 ASP A 228      24.163  32.145  11.128  1.00 13.40           O  
ANISOU 1431  OD1 ASP A 228     1646   2215   1228   -106   -400   -120       O  
ATOM   1432  OD2 ASP A 228      22.162  31.439  11.489  1.00 14.93           O  
ANISOU 1432  OD2 ASP A 228     1601   2246   1824   -170   -564     99       O  
ATOM   1433  N   GLU A 229      24.890  31.673  16.250  1.00  7.21           N  
ANISOU 1433  N   GLU A 229      805    883   1052     77     32   -179       N  
ATOM   1434  CA  GLU A 229      25.155  32.179  17.590  1.00  7.44           C  
ANISOU 1434  CA  GLU A 229      923    941    961     50    117   -130       C  
ATOM   1435  C   GLU A 229      26.655  32.275  17.870  1.00  6.13           C  
ANISOU 1435  C   GLU A 229      752    789    786     21    157   -132       C  
ATOM   1436  O   GLU A 229      27.114  33.219  18.502  1.00  6.44           O  
ANISOU 1436  O   GLU A 229      846    792    805     69    112   -158       O  
ATOM   1437  CB  GLU A 229      24.560  31.264  18.656  1.00  9.08           C  
ANISOU 1437  CB  GLU A 229     1083   1342   1025     33    303   -238       C  
ATOM   1438  CG  GLU A 229      23.087  30.921  18.670  1.00 13.85           C  
ANISOU 1438  CG  GLU A 229     1646   1902   1712     61    145    -88       C  
ATOM   1439  CD  GLU A 229      22.817  29.847  19.722  1.00 18.14           C  
ANISOU 1439  CD  GLU A 229     2025   2446   2420    225    300    -57       C  
ATOM   1440  OE1 GLU A 229      23.134  28.620  19.554  1.00 17.67           O  
ANISOU 1440  OE1 GLU A 229     1535   2741   2436    732    602    284       O  
ATOM   1441  OE2 GLU A 229      22.359  30.263  20.782  1.00 22.73           O  
ANISOU 1441  OE2 GLU A 229     2889   2959   2786    523    158   -336       O  
ATOM   1442  N   PHE A 230      27.411  31.281  17.400  1.00  5.77           N  
ANISOU 1442  N   PHE A 230      699    681    809     31     64   -138       N  
ATOM   1443  CA  PHE A 230      28.858  31.280  17.530  1.00  5.97           C  
ANISOU 1443  CA  PHE A 230      728    777    761     48     81    -86       C  
ATOM   1444  C   PHE A 230      29.440  32.551  16.899  1.00  5.37           C  
ANISOU 1444  C   PHE A 230      630    704    706      6     39   -128       C  
ATOM   1445  O   PHE A 230      30.287  33.219  17.494  1.00  5.87           O  
ANISOU 1445  O   PHE A 230      689    773    768     13     52   -114       O  
ATOM   1446  CB  PHE A 230      29.439  30.020  16.878  1.00  5.88           C  
ANISOU 1446  CB  PHE A 230      759    748    724     26    127   -112       C  
ATOM   1447  CG  PHE A 230      30.927  30.071  16.714  1.00  5.41           C  
ANISOU 1447  CG  PHE A 230      652    690    711     23    127    -60       C  
ATOM   1448  CD1 PHE A 230      31.768  29.788  17.779  1.00  5.23           C  
ANISOU 1448  CD1 PHE A 230      796    610    580     66    126    -76       C  
ATOM   1449  CD2 PHE A 230      31.489  30.414  15.503  1.00  6.29           C  
ANISOU 1449  CD2 PHE A 230      903    894    591     80     18    -87       C  
ATOM   1450  CE1 PHE A 230      33.141  29.846  17.624  1.00  6.07           C  
ANISOU 1450  CE1 PHE A 230      772    760    773    106     69      0       C  
ATOM   1451  CE2 PHE A 230      32.870  30.471  15.352  1.00  6.24           C  
ANISOU 1451  CE2 PHE A 230      656    826    885     95    190     56       C  
ATOM   1452  CZ  PHE A 230      33.691  30.207  16.413  1.00  6.03           C  
ANISOU 1452  CZ  PHE A 230      665    687    935    152    174   -128       C  
ATOM   1453  N   VAL A 231      29.005  32.874  15.692  1.00  6.02           N  
ANISOU 1453  N   VAL A 231      806    762    719     -4     18   -141       N  
ATOM   1454  CA  VAL A 231      29.494  34.075  15.026  1.00  7.26           C  
ANISOU 1454  CA  VAL A 231     1051    875    831    -33    -40   -105       C  
ATOM   1455  C   VAL A 231      29.042  35.345  15.750  1.00  7.15           C  
ANISOU 1455  C   VAL A 231     1009    897    810    -23   -114    -78       C  
ATOM   1456  O   VAL A 231      29.809  36.292  15.914  1.00  7.68           O  
ANISOU 1456  O   VAL A 231     1107    844    966    -57   -163    -41       O  
ATOM   1457  CB  VAL A 231      29.039  34.095  13.559  1.00  8.59           C  
ANISOU 1457  CB  VAL A 231     1406    921    936    -21     42    -85       C  
ATOM   1458  CG1 VAL A 231      29.184  35.478  12.942  1.00  9.90           C  
ANISOU 1458  CG1 VAL A 231     1427   1171   1160      1    -20   -138       C  
ATOM   1459  CG2 VAL A 231      29.770  33.030  12.771  1.00  9.96           C  
ANISOU 1459  CG2 VAL A 231     1572   1152   1060    -63     84   -111       C  
ATOM   1460  N   GLU A 232      27.795  35.382  16.192  1.00  7.19           N  
ANISOU 1460  N   GLU A 232      990    841    898     84   -148   -100       N  
ATOM   1461  CA  GLU A 232      27.276  36.556  16.891  1.00  8.30           C  
ANISOU 1461  CA  GLU A 232     1180    962   1011    122   -125   -113       C  
ATOM   1462  C   GLU A 232      28.099  36.848  18.136  1.00  7.68           C  
ANISOU 1462  C   GLU A 232     1124    837    957    129   -136   -107       C  
ATOM   1463  O   GLU A 232      28.558  37.970  18.328  1.00  9.16           O  
ANISOU 1463  O   GLU A 232     1647    850    983    103   -298    -58       O  
ATOM   1464  CB  GLU A 232      25.816  36.329  17.257  1.00  9.62           C  
ANISOU 1464  CB  GLU A 232     1260   1160   1234    235   -137   -197       C  
ATOM   1465  CG  GLU A 232      25.122  37.393  18.094  1.00 16.37           C  
ANISOU 1465  CG  GLU A 232     2061   2171   1988    153    -92   -247       C  
ATOM   1466  CD  GLU A 232      23.752  36.913  18.571  1.00 22.64           C  
ANISOU 1466  CD  GLU A 232     2843   3210   2546     55    -99   -329       C  
ATOM   1467  OE1 GLU A 232      23.463  36.970  19.792  1.00 27.98           O  
ANISOU 1467  OE1 GLU A 232     3432   4141   3058    156    -91   -336       O  
ATOM   1468  OE2 GLU A 232      22.958  36.454  17.717  1.00 28.26           O  
ANISOU 1468  OE2 GLU A 232     3207   4231   3297    115   -204   -369       O  
ATOM   1469  N   PHE A 233      28.283  35.851  18.984  1.00  6.42           N  
ANISOU 1469  N   PHE A 233      933    812    693     67      1   -128       N  
ATOM   1470  CA  PHE A 233      29.073  36.053  20.182  1.00  6.59           C  
ANISOU 1470  CA  PHE A 233      938    840    724     99    -10   -109       C  
ATOM   1471  C   PHE A 233      30.542  36.335  19.861  1.00  5.94           C  
ANISOU 1471  C   PHE A 233      885    740    631     90    -52   -165       C  
ATOM   1472  O   PHE A 233      31.124  37.248  20.425  1.00  6.73           O  
ANISOU 1472  O   PHE A 233      974    812    769     35   -100   -228       O  
ATOM   1473  CB  PHE A 233      28.918  34.851  21.126  1.00  7.35           C  
ANISOU 1473  CB  PHE A 233     1038    973    779     64     -6   -125       C  
ATOM   1474  CG  PHE A 233      27.628  34.870  21.910  1.00  8.06           C  
ANISOU 1474  CG  PHE A 233     1255   1091    714    -18    198   -241       C  
ATOM   1475  CD1 PHE A 233      27.508  35.630  23.064  1.00 11.39           C  
ANISOU 1475  CD1 PHE A 233     1546   1656   1124   -125    249   -328       C  
ATOM   1476  CD2 PHE A 233      26.518  34.163  21.494  1.00  9.90           C  
ANISOU 1476  CD2 PHE A 233     1380   1369   1011    -96    332   -302       C  
ATOM   1477  CE1 PHE A 233      26.307  35.669  23.781  1.00 11.72           C  
ANISOU 1477  CE1 PHE A 233     1753   1731    966   -162    259   -620       C  
ATOM   1478  CE2 PHE A 233      25.323  34.204  22.217  1.00 11.98           C  
ANISOU 1478  CE2 PHE A 233     1614   1869   1066   -209    223   -414       C  
ATOM   1479  CZ  PHE A 233      25.219  34.953  23.352  1.00 12.17           C  
ANISOU 1479  CZ  PHE A 233     1641   1850   1132   -153    336   -408       C  
ATOM   1480  N   SER A 234      31.141  35.562  18.961  1.00  5.65           N  
ANISOU 1480  N   SER A 234      790    704    653     -2    -25   -163       N  
ATOM   1481  CA  SER A 234      32.563  35.737  18.674  1.00  6.07           C  
ANISOU 1481  CA  SER A 234      829    709    766     48    -15   -100       C  
ATOM   1482  C   SER A 234      32.854  37.127  18.121  1.00  6.37           C  
ANISOU 1482  C   SER A 234      809    763    846     21      4   -108       C  
ATOM   1483  O   SER A 234      33.880  37.712  18.422  1.00  6.95           O  
ANISOU 1483  O   SER A 234      922    671   1046    -34      1   -102       O  
ATOM   1484  CB  SER A 234      33.056  34.677  17.690  1.00  6.06           C  
ANISOU 1484  CB  SER A 234      710    823    768     75    -30    -69       C  
ATOM   1485  OG  SER A 234      33.032  33.383  18.253  1.00  6.86           O  
ANISOU 1485  OG  SER A 234      886    681   1037     97      0    -80       O  
ATOM   1486  N   SER A 235      31.927  37.648  17.327  1.00  6.64           N  
ANISOU 1486  N   SER A 235      917    808    796    -54    -42    -58       N  
ATOM   1487  CA  SER A 235      32.088  38.960  16.730  1.00  8.07           C  
ANISOU 1487  CA  SER A 235     1079    953   1032    -29    -58     61       C  
ATOM   1488  C   SER A 235      32.074  40.074  17.772  1.00  8.02           C  
ANISOU 1488  C   SER A 235     1095    840   1112    -14   -143     22       C  
ATOM   1489  O   SER A 235      32.512  41.179  17.487  1.00  9.81           O  
ANISOU 1489  O   SER A 235     1516    866   1343   -155    -58     60       O  
ATOM   1490  CB  SER A 235      30.990  39.214  15.689  1.00  9.11           C  
ANISOU 1490  CB  SER A 235     1259   1116   1085    -54    -67    108       C  
ATOM   1491  OG  SER A 235      29.741  39.475  16.288  1.00 11.64           O  
ANISOU 1491  OG  SER A 235     1518   1472   1432   -129   -382    449       O  
ATOM   1492  N   LYS A 236      31.562  39.791  18.961  1.00  7.48           N  
ANISOU 1492  N   LYS A 236     1061    701   1078    116   -173    -45       N  
ATOM   1493  CA  LYS A 236      31.507  40.755  20.050  1.00  8.33           C  
ANISOU 1493  CA  LYS A 236     1129    850   1183    139   -124   -103       C  
ATOM   1494  C   LYS A 236      32.664  40.610  21.030  1.00  7.71           C  
ANISOU 1494  C   LYS A 236     1111    770   1046    195   -181   -163       C  
ATOM   1495  O   LYS A 236      32.768  41.369  21.982  1.00  9.97           O  
ANISOU 1495  O   LYS A 236     1355   1046   1387    390   -242   -485       O  
ATOM   1496  CB  LYS A 236      30.182  40.620  20.791  1.00  9.18           C  
ANISOU 1496  CB  LYS A 236     1220    985   1281    209   -146    -88       C  
ATOM   1497  CG  LYS A 236      28.984  40.959  19.941  1.00 11.90           C  
ANISOU 1497  CG  LYS A 236     1407   1323   1788    166   -151   -148       C  
ATOM   1498  CD  LYS A 236      27.680  40.728  20.698  1.00 15.72           C  
ANISOU 1498  CD  LYS A 236     1878   1944   2149     89   -128    -85       C  
ATOM   1499  CE  LYS A 236      26.461  40.951  19.825  1.00 18.83           C  
ANISOU 1499  CE  LYS A 236     2182   2400   2571     75    -50    -68       C  
ATOM   1500  NZ  LYS A 236      25.221  40.474  20.501  1.00 23.29           N  
ANISOU 1500  NZ  LYS A 236     2819   2845   3185    -17    138    -65       N  
ATOM   1501  N   VAL A 237      33.530  39.630  20.824  1.00  7.05           N  
ANISOU 1501  N   VAL A 237      980    753    944    210   -117   -170       N  
ATOM   1502  CA  VAL A 237      34.682  39.423  21.688  1.00  7.08           C  
ANISOU 1502  CA  VAL A 237     1017    783    889     87   -115   -142       C  
ATOM   1503  C   VAL A 237      35.854  40.128  21.004  1.00  6.95           C  
ANISOU 1503  C   VAL A 237     1019    715    907    131   -154   -225       C  
ATOM   1504  O   VAL A 237      36.223  39.774  19.891  1.00  7.15           O  
ANISOU 1504  O   VAL A 237     1087    660    968     77   -130   -164       O  
ATOM   1505  CB  VAL A 237      34.966  37.932  21.869  1.00  6.70           C  
ANISOU 1505  CB  VAL A 237     1010    806    730     94   -117   -190       C  
ATOM   1506  CG1 VAL A 237      36.233  37.736  22.678  1.00  7.71           C  
ANISOU 1506  CG1 VAL A 237      992    982    956     55   -210   -115       C  
ATOM   1507  CG2 VAL A 237      33.807  37.235  22.539  1.00  7.40           C  
ANISOU 1507  CG2 VAL A 237     1115    907    788    118   -119    -49       C  
ATOM   1508  N   PRO A 238      36.429  41.156  21.629  1.00  7.80           N  
ANISOU 1508  N   PRO A 238     1091    786   1085     85    -68   -213       N  
ATOM   1509  CA  PRO A 238      37.351  42.034  20.903  1.00  7.31           C  
ANISOU 1509  CA  PRO A 238     1070    662   1042     97    -80   -209       C  
ATOM   1510  C   PRO A 238      38.607  41.300  20.442  1.00  7.45           C  
ANISOU 1510  C   PRO A 238     1099    591   1138    104    -98   -179       C  
ATOM   1511  O   PRO A 238      39.302  40.676  21.236  1.00  7.80           O  
ANISOU 1511  O   PRO A 238     1160    727   1074    160   -191   -157       O  
ATOM   1512  CB  PRO A 238      37.703  43.117  21.945  1.00  8.39           C  
ANISOU 1512  CB  PRO A 238     1186    758   1244     36    -15   -298       C  
ATOM   1513  CG  PRO A 238      37.468  42.480  23.263  1.00  9.12           C  
ANISOU 1513  CG  PRO A 238     1340    954   1172    102   -144   -367       C  
ATOM   1514  CD  PRO A 238      36.278  41.586  23.033  1.00  8.46           C  
ANISOU 1514  CD  PRO A 238     1172    929   1111     39   -143   -277       C  
ATOM   1515  N   ASN A 239      38.887  41.433  19.157  1.00  7.49           N  
ANISOU 1515  N   ASN A 239     1076    568   1200     79    -66    -14       N  
ATOM   1516  CA  ASN A 239      40.049  40.850  18.509  1.00  7.61           C  
ANISOU 1516  CA  ASN A 239     1046    694   1151     -1      0    -62       C  
ATOM   1517  C   ASN A 239      40.062  39.329  18.476  1.00  6.87           C  
ANISOU 1517  C   ASN A 239      959    598   1053     24     23   -102       C  
ATOM   1518  O   ASN A 239      41.108  38.726  18.303  1.00  8.98           O  
ANISOU 1518  O   ASN A 239     1025    768   1615     25     89   -190       O  
ATOM   1519  CB  ASN A 239      41.345  41.421  19.100  1.00  8.89           C  
ANISOU 1519  CB  ASN A 239     1198    797   1380    -42     43   -113       C  
ATOM   1520  CG  ASN A 239      41.437  42.911  18.908  1.00 10.73           C  
ANISOU 1520  CG  ASN A 239     1502   1006   1567   -249     35   -202       C  
ATOM   1521  OD1 ASN A 239      41.565  43.687  19.874  1.00 13.13           O  
ANISOU 1521  OD1 ASN A 239     1800   1159   2029   -227      9   -474       O  
ATOM   1522  ND2 ASN A 239      41.310  43.338  17.670  1.00 11.23           N  
ANISOU 1522  ND2 ASN A 239     2070    720   1475   -347    367   -280       N  
ATOM   1523  N   LEU A 240      38.906  38.699  18.628  1.00  6.33           N  
ANISOU 1523  N   LEU A 240      878    501   1025     71    -67    -31       N  
ATOM   1524  CA  LEU A 240      38.835  37.260  18.480  1.00  5.88           C  
ANISOU 1524  CA  LEU A 240      894    555    782    106    -62    -37       C  
ATOM   1525  C   LEU A 240      38.710  36.909  17.002  1.00  5.94           C  
ANISOU 1525  C   LEU A 240      834    607    816     81    -42     12       C  
ATOM   1526  O   LEU A 240      37.755  37.330  16.346  1.00  7.43           O  
ANISOU 1526  O   LEU A 240     1044    843    934    239   -156   -110       O  
ATOM   1527  CB  LEU A 240      37.652  36.692  19.242  1.00  6.12           C  
ANISOU 1527  CB  LEU A 240      888    658    776     79    -37    -25       C  
ATOM   1528  CG  LEU A 240      37.560  35.165  19.238  1.00  5.58           C  
ANISOU 1528  CG  LEU A 240      893    485    739     65    -74    -99       C  
ATOM   1529  CD1 LEU A 240      38.779  34.527  19.900  1.00  7.37           C  
ANISOU 1529  CD1 LEU A 240      975    768   1054     35    -72     86       C  
ATOM   1530  CD2 LEU A 240      36.280  34.719  19.917  1.00  7.15           C  
ANISOU 1530  CD2 LEU A 240      978    611   1127     72    -28     16       C  
ATOM   1531  N   LEU A 241      39.662  36.148  16.486  1.00  5.53           N  
ANISOU 1531  N   LEU A 241      794    592    713     40    -37     -8       N  
ATOM   1532  CA  LEU A 241      39.554  35.557  15.170  1.00  5.67           C  
ANISOU 1532  CA  LEU A 241      776    685    691     43     43     69       C  
ATOM   1533  C   LEU A 241      38.723  34.293  15.250  1.00  5.18           C  
ANISOU 1533  C   LEU A 241      765    637    565     51     55     37       C  
ATOM   1534  O   LEU A 241      38.920  33.501  16.165  1.00  5.39           O  
ANISOU 1534  O   LEU A 241      876    575    593     22    -19     57       O  
ATOM   1535  CB  LEU A 241      40.940  35.203  14.693  1.00  6.87           C  
ANISOU 1535  CB  LEU A 241      817    843    949    -35    -47     58       C  
ATOM   1536  CG  LEU A 241      41.057  34.675  13.300  1.00 10.90           C  
ANISOU 1536  CG  LEU A 241     1352   1389   1399     81     19    -47       C  
ATOM   1537  CD1 LEU A 241      40.632  35.696  12.263  1.00 14.35           C  
ANISOU 1537  CD1 LEU A 241     1824   1947   1680    193    133    -15       C  
ATOM   1538  CD2 LEU A 241      42.495  34.257  13.101  1.00 12.47           C  
ANISOU 1538  CD2 LEU A 241     1443   1703   1589     86     79    -49       C  
ATOM   1539  N   TYR A 242      37.825  34.094  14.294  1.00  5.77           N  
ANISOU 1539  N   TYR A 242      833    736    624    -54      3    156       N  
ATOM   1540  CA  TYR A 242      36.907  32.968  14.366  1.00  6.27           C  
ANISOU 1540  CA  TYR A 242      875    855    651    -64     19     66       C  
ATOM   1541  C   TYR A 242      36.560  32.453  12.987  1.00  5.79           C  
ANISOU 1541  C   TYR A 242      755    889    554   -101    -65    123       C  
ATOM   1542  O   TYR A 242      36.647  33.158  11.996  1.00  7.52           O  
ANISOU 1542  O   TYR A 242     1089   1151    615   -161    -42    175       O  
ATOM   1543  CB  TYR A 242      35.637  33.338  15.167  1.00  6.48           C  
ANISOU 1543  CB  TYR A 242      831    874    757    -97    -12     19       C  
ATOM   1544  CG  TYR A 242      34.825  34.445  14.570  1.00  7.39           C  
ANISOU 1544  CG  TYR A 242      867    980    960    -95    122     44       C  
ATOM   1545  CD1 TYR A 242      33.820  34.167  13.660  1.00  8.98           C  
ANISOU 1545  CD1 TYR A 242      890   1178   1343     68     10    183       C  
ATOM   1546  CD2 TYR A 242      35.068  35.766  14.893  1.00  9.16           C  
ANISOU 1546  CD2 TYR A 242     1147   1127   1206    103     98    153       C  
ATOM   1547  CE1 TYR A 242      33.080  35.177  13.089  1.00 12.00           C  
ANISOU 1547  CE1 TYR A 242     1141   1701   1715    208      8    337       C  
ATOM   1548  CE2 TYR A 242      34.326  36.800  14.306  1.00 11.19           C  
ANISOU 1548  CE2 TYR A 242     1409   1105   1737    206    165    246       C  
ATOM   1549  CZ  TYR A 242      33.327  36.485  13.412  1.00 12.73           C  
ANISOU 1549  CZ  TYR A 242     1420   1690   1726    253    172    427       C  
ATOM   1550  OH  TYR A 242      32.567  37.453  12.822  1.00 18.33           O  
ANISOU 1550  OH  TYR A 242     1953   2161   2850    326    117    589       O  
ATOM   1551  N   ALA A 243      36.145  31.196  12.961  1.00  6.23           N  
ANISOU 1551  N   ALA A 243      868    935    563    -65      4    -38       N  
ATOM   1552  CA  ALA A 243      35.753  30.512  11.743  1.00  6.83           C  
ANISOU 1552  CA  ALA A 243      816   1065    714     -4    -55   -110       C  
ATOM   1553  C   ALA A 243      34.511  31.147  11.153  1.00  7.34           C  
ANISOU 1553  C   ALA A 243      868   1194    724     50      0   -114       C  
ATOM   1554  O   ALA A 243      33.491  31.279  11.815  1.00  9.92           O  
ANISOU 1554  O   ALA A 243      910   1764   1094    134    -36    -38       O  
ATOM   1555  CB  ALA A 243      35.491  29.061  12.046  1.00  7.72           C  
ANISOU 1555  CB  ALA A 243     1067   1178    686    -20    -54   -169       C  
ATOM   1556  N   ARG A 244      34.626  31.574   9.908  1.00  8.03           N  
ANISOU 1556  N   ARG A 244      982   1259    807    139    -77    -72       N  
ATOM   1557  CA  ARG A 244      33.524  32.200   9.191  1.00  9.21           C  
ANISOU 1557  CA  ARG A 244     1221   1202   1073    147   -112   -109       C  
ATOM   1558  C   ARG A 244      33.220  31.423   7.931  1.00  7.37           C  
ANISOU 1558  C   ARG A 244     1040    962    796    100   -114   -100       C  
ATOM   1559  O   ARG A 244      34.126  30.957   7.237  1.00  7.97           O  
ANISOU 1559  O   ARG A 244     1006   1246    776    125   -103      0       O  
ATOM   1560  CB  ARG A 244      33.879  33.637   8.815  1.00 11.88           C  
ANISOU 1560  CB  ARG A 244     1580   1460   1473     92   -201   -150       C  
ATOM   1561  CG  ARG A 244      33.823  34.612   9.968  1.00 15.64           C  
ANISOU 1561  CG  ARG A 244     2068   1988   1886     81   -203    -51       C  
ATOM   1562  CD  ARG A 244      33.913  36.059   9.546  1.00 21.76           C  
ANISOU 1562  CD  ARG A 244     2843   2671   2751     19    -88    -57       C  
ATOM   1563  NE  ARG A 244      32.599  36.600   9.181  1.00 26.84           N  
ANISOU 1563  NE  ARG A 244     3401   3426   3370     31    -56     34       N  
ATOM   1564  CZ  ARG A 244      32.152  36.823   7.941  1.00 30.18           C  
ANISOU 1564  CZ  ARG A 244     3810   3873   3782     32     -8      2       C  
ATOM   1565  NH1 ARG A 244      32.899  36.555   6.871  1.00 32.17           N  
ANISOU 1565  NH1 ARG A 244     4076   4071   4074     30     25     33       N  
ATOM   1566  NH2 ARG A 244      30.929  37.325   7.771  1.00 31.73           N  
ANISOU 1566  NH2 ARG A 244     4015   4081   3959     58     31     -1       N  
ATOM   1567  N   ALA A 245      31.945  31.334   7.605  1.00  7.44           N  
ANISOU 1567  N   ALA A 245     1024    954    848    236    -44    -94       N  
ATOM   1568  CA  ALA A 245      31.513  30.532   6.477  1.00  7.08           C  
ANISOU 1568  CA  ALA A 245     1005    866    816    123    -14    -15       C  
ATOM   1569  C   ALA A 245      32.079  31.037   5.154  1.00  6.63           C  
ANISOU 1569  C   ALA A 245      995    769    755    181    -26     21       C  
ATOM   1570  O   ALA A 245      31.967  32.224   4.830  1.00  8.36           O  
ANISOU 1570  O   ALA A 245     1456    721    999    207      6     91       O  
ATOM   1571  CB  ALA A 245      30.004  30.502   6.410  1.00  8.07           C  
ANISOU 1571  CB  ALA A 245     1065   1088    910    104      3    -27       C  
ATOM   1572  N   LEU A 246      32.673  30.116   4.412  1.00  6.45           N  
ANISOU 1572  N   LEU A 246      960    726    761    121     26     68       N  
ATOM   1573  CA  LEU A 246      33.148  30.319   3.054  1.00  7.16           C  
ANISOU 1573  CA  LEU A 246     1024    901    795    -13      0     69       C  
ATOM   1574  C   LEU A 246      32.042  30.063   2.046  1.00  7.96           C  
ANISOU 1574  C   LEU A 246     1150   1057    815     90    -75    142       C  
ATOM   1575  O   LEU A 246      32.049  30.613   0.943  1.00  9.70           O  
ANISOU 1575  O   LEU A 246     1410   1422    850    -58   -185    307       O  
ATOM   1576  CB  LEU A 246      34.289  29.351   2.786  1.00  7.36           C  
ANISOU 1576  CB  LEU A 246     1010    971    815    -30     42     53       C  
ATOM   1577  CG  LEU A 246      35.485  29.487   3.723  1.00  8.34           C  
ANISOU 1577  CG  LEU A 246     1014   1177    978     -9    122     19       C  
ATOM   1578  CD1 LEU A 246      36.319  28.224   3.681  1.00  8.16           C  
ANISOU 1578  CD1 LEU A 246     1067   1245    787    126    -40     21       C  
ATOM   1579  CD2 LEU A 246      36.327  30.698   3.371  1.00 11.23           C  
ANISOU 1579  CD2 LEU A 246     1385   1369   1511    -42     73     21       C  
ATOM   1580  N   VAL A 247      31.129  29.180   2.418  1.00  7.89           N  
ANISOU 1580  N   VAL A 247     1071   1121    802     19   -156     58       N  
ATOM   1581  CA  VAL A 247      29.928  28.863   1.674  1.00  8.60           C  
ANISOU 1581  CA  VAL A 247     1142   1132    992     39   -112    -31       C  
ATOM   1582  C   VAL A 247      28.893  28.400   2.690  1.00  7.60           C  
ANISOU 1582  C   VAL A 247      970    984    932     75   -134     42       C  
ATOM   1583  O   VAL A 247      29.244  27.873   3.760  1.00  7.67           O  
ANISOU 1583  O   VAL A 247     1036    966    912     67   -213    120       O  
ATOM   1584  CB  VAL A 247      30.189  27.794   0.559  1.00 10.09           C  
ANISOU 1584  CB  VAL A 247     1262   1445   1123     23   -126   -172       C  
ATOM   1585  CG1 VAL A 247      30.693  26.520   1.131  1.00 11.96           C  
ANISOU 1585  CG1 VAL A 247     1617   1561   1366   -112    -61   -200       C  
ATOM   1586  CG2 VAL A 247      28.960  27.559  -0.292  1.00 13.81           C  
ANISOU 1586  CG2 VAL A 247     1727   1926   1594    102   -150   -262       C  
ATOM   1587  N   ARG A 248      27.626  28.610   2.372  1.00  8.03           N  
ANISOU 1587  N   ARG A 248     1012   1059    980    119   -119    161       N  
ATOM   1588  CA  ARG A 248      26.515  28.215   3.215  1.00  8.45           C  
ANISOU 1588  CA  ARG A 248     1042   1101   1066     84   -162     80       C  
ATOM   1589  C   ARG A 248      25.436  27.690   2.296  1.00  8.57           C  
ANISOU 1589  C   ARG A 248     1053   1139   1061     81   -186    121       C  
ATOM   1590  O   ARG A 248      25.138  28.306   1.266  1.00 10.13           O  
ANISOU 1590  O   ARG A 248     1320   1309   1218     37   -402    327       O  
ATOM   1591  CB  ARG A 248      26.011  29.411   4.010  1.00  8.73           C  
ANISOU 1591  CB  ARG A 248     1018   1145   1151     34   -159     67       C  
ATOM   1592  CG  ARG A 248      24.874  29.107   4.946  1.00 10.20           C  
ANISOU 1592  CG  ARG A 248     1251   1328   1294    178    -92    -58       C  
ATOM   1593  CD  ARG A 248      24.629  30.221   5.889  1.00 12.56           C  
ANISOU 1593  CD  ARG A 248     1517   1713   1540    -16     -9   -161       C  
ATOM   1594  NE  ARG A 248      23.535  29.925   6.797  1.00 12.40           N  
ANISOU 1594  NE  ARG A 248     1630   1566   1515     94    -76   -225       N  
ATOM   1595  CZ  ARG A 248      23.450  30.417   8.019  1.00 12.07           C  
ANISOU 1595  CZ  ARG A 248     1530   1641   1413    142   -111   -123       C  
ATOM   1596  NH1 ARG A 248      24.393  31.211   8.491  1.00 14.93           N  
ANISOU 1596  NH1 ARG A 248     1677   2242   1752    -57   -242    -75       N  
ATOM   1597  NH2 ARG A 248      22.412  30.111   8.783  1.00 12.80           N  
ANISOU 1597  NH2 ARG A 248     1444   1780   1637    160   -101   -117       N  
ATOM   1598  N   GLY A 249      24.828  26.579   2.659  1.00  7.88           N  
ANISOU 1598  N   GLY A 249      980   1038    977     71   -189     31       N  
ATOM   1599  CA  GLY A 249      23.780  25.988   1.840  1.00  8.60           C  
ANISOU 1599  CA  GLY A 249     1086   1113   1067     34   -142    -25       C  
ATOM   1600  C   GLY A 249      23.474  24.582   2.289  1.00  8.01           C  
ANISOU 1600  C   GLY A 249      988   1070    985     55   -110    -53       C  
ATOM   1601  O   GLY A 249      23.702  24.219   3.439  1.00  8.57           O  
ANISOU 1601  O   GLY A 249     1084   1180    992     -2   -130    -34       O  
ATOM   1602  N   THR A 250      22.967  23.762   1.382  1.00  7.92           N  
ANISOU 1602  N   THR A 250      904   1064   1040    113   -182    -55       N  
ATOM   1603  CA  THR A 250      22.789  22.362   1.694  1.00  7.64           C  
ANISOU 1603  CA  THR A 250      839   1072    991     85   -148    -86       C  
ATOM   1604  C   THR A 250      24.148  21.692   1.883  1.00  7.54           C  
ANISOU 1604  C   THR A 250      800   1013   1051     85   -114    -81       C  
ATOM   1605  O   THR A 250      25.204  22.225   1.534  1.00  7.53           O  
ANISOU 1605  O   THR A 250      842   1033    985     80   -125   -149       O  
ATOM   1606  CB  THR A 250      22.056  21.631   0.575  1.00  8.61           C  
ANISOU 1606  CB  THR A 250      928   1197   1144     56   -175    -92       C  
ATOM   1607  OG1 THR A 250      22.873  21.700  -0.596  1.00 10.06           O  
ANISOU 1607  OG1 THR A 250     1084   1560   1176     79   -216    -90       O  
ATOM   1608  CG2 THR A 250      20.701  22.271   0.249  1.00  9.74           C  
ANISOU 1608  CG2 THR A 250     1071   1507   1122     80   -162    -48       C  
ATOM   1609  N   LEU A 251      24.112  20.488   2.417  1.00  7.42           N  
ANISOU 1609  N   LEU A 251      852    954   1010     55    -52    -65       N  
ATOM   1610  CA  LEU A 251      25.330  19.708   2.550  1.00  7.45           C  
ANISOU 1610  CA  LEU A 251      875    971    981     58    -78    -87       C  
ATOM   1611  C   LEU A 251      26.045  19.600   1.197  1.00  7.52           C  
ANISOU 1611  C   LEU A 251      903    954    999      9   -114   -131       C  
ATOM   1612  O   LEU A 251      27.254  19.795   1.101  1.00  7.88           O  
ANISOU 1612  O   LEU A 251      891   1049   1054     53    -68   -100       O  
ATOM   1613  CB  LEU A 251      25.009  18.337   3.126  1.00  7.61           C  
ANISOU 1613  CB  LEU A 251      928    939   1021     60   -125   -107       C  
ATOM   1614  CG  LEU A 251      26.156  17.332   3.149  1.00  8.20           C  
ANISOU 1614  CG  LEU A 251      896   1067   1149     61    -15   -134       C  
ATOM   1615  CD1 LEU A 251      27.254  17.823   4.081  1.00  9.40           C  
ANISOU 1615  CD1 LEU A 251     1059   1254   1256    172   -194   -145       C  
ATOM   1616  CD2 LEU A 251      25.619  15.984   3.574  1.00 10.52           C  
ANISOU 1616  CD2 LEU A 251     1122   1318   1556    199     96      0       C  
ATOM   1617  N   ASP A 252      25.303  19.276   0.140  1.00  8.47           N  
ANISOU 1617  N   ASP A 252      970   1202   1044    -41    -84   -167       N  
ATOM   1618  CA  ASP A 252      25.914  19.128  -1.173  1.00  9.10           C  
ANISOU 1618  CA  ASP A 252     1111   1233   1110     12    -85   -146       C  
ATOM   1619  C   ASP A 252      26.521  20.425  -1.697  1.00  9.20           C  
ANISOU 1619  C   ASP A 252     1129   1330   1035     55    -37   -175       C  
ATOM   1620  O   ASP A 252      27.577  20.395  -2.307  1.00  9.74           O  
ANISOU 1620  O   ASP A 252     1146   1358   1197     -9     -3   -193       O  
ATOM   1621  CB  ASP A 252      24.906  18.548  -2.167  1.00 10.30           C  
ANISOU 1621  CB  ASP A 252     1241   1454   1218    -86    -82   -195       C  
ATOM   1622  CG  ASP A 252      24.785  17.048  -2.057  1.00 11.69           C  
ANISOU 1622  CG  ASP A 252     1270   1614   1554   -119   -258   -228       C  
ATOM   1623  OD1 ASP A 252      25.827  16.360  -1.967  1.00 15.13           O  
ANISOU 1623  OD1 ASP A 252     1863   1765   2119   -276   -291   -357       O  
ATOM   1624  OD2 ASP A 252      23.678  16.478  -2.067  1.00 16.09           O  
ANISOU 1624  OD2 ASP A 252     1735   2014   2363   -329   -178   -403       O  
ATOM   1625  N   GLU A 253      25.881  21.559  -1.434  1.00  8.69           N  
ANISOU 1625  N   GLU A 253     1082   1231    986     79    -71    -84       N  
ATOM   1626  CA  GLU A 253      26.433  22.836  -1.854  1.00  9.60           C  
ANISOU 1626  CA  GLU A 253     1207   1349   1090     92    -30    -25       C  
ATOM   1627  C   GLU A 253      27.767  23.097  -1.147  1.00  8.93           C  
ANISOU 1627  C   GLU A 253     1173   1206   1014     40    -21    -37       C  
ATOM   1628  O   GLU A 253      28.715  23.593  -1.758  1.00 10.39           O  
ANISOU 1628  O   GLU A 253     1284   1537   1127     -5    -11     39       O  
ATOM   1629  CB  GLU A 253      25.425  23.960  -1.627  1.00  9.69           C  
ANISOU 1629  CB  GLU A 253     1304   1295   1083    118    -75     65       C  
ATOM   1630  CG  GLU A 253      24.331  23.948  -2.685  1.00 11.84           C  
ANISOU 1630  CG  GLU A 253     1438   1721   1338    256   -191     48       C  
ATOM   1631  CD  GLU A 253      23.134  24.814  -2.371  1.00 13.84           C  
ANISOU 1631  CD  GLU A 253     1830   2115   1313    440   -342    140       C  
ATOM   1632  OE1 GLU A 253      22.884  25.175  -1.210  1.00 13.34           O  
ANISOU 1632  OE1 GLU A 253     1783   2052   1234    607   -423    -29       O  
ATOM   1633  OE2 GLU A 253      22.407  25.124  -3.328  1.00 19.92           O  
ANISOU 1633  OE2 GLU A 253     2554   3162   1852    733   -597    100       O  
ATOM   1634  N   CYS A 254      27.852  22.762   0.136  1.00  7.64           N  
ANISOU 1634  N   CYS A 254     1012    984    905     79      1    -65       N  
ATOM   1635  CA  CYS A 254      29.111  22.939   0.864  1.00  7.21           C  
ANISOU 1635  CA  CYS A 254      909    859    971     37    -10    -91       C  
ATOM   1636  C   CYS A 254      30.188  21.962   0.385  1.00  7.28           C  
ANISOU 1636  C   CYS A 254      933    833   1000     47     -8   -179       C  
ATOM   1637  O   CYS A 254      31.354  22.322   0.265  1.00  7.83           O  
ANISOU 1637  O   CYS A 254      901    986   1088    -11      0   -243       O  
ATOM   1638  CB  CYS A 254      28.871  22.790   2.351  1.00  7.70           C  
ANISOU 1638  CB  CYS A 254      834    982   1110     22    -17    -93       C  
ATOM   1639  SG  CYS A 254      27.923  24.157   3.070  1.00  7.64           S  
ANISOU 1639  SG  CYS A 254      996    929    978     35     31   -160       S  
ATOM   1640  N   LEU A 255      29.793  20.722   0.112  1.00  7.92           N  
ANISOU 1640  N   LEU A 255      919    879   1211     79     23   -234       N  
ATOM   1641  CA  LEU A 255      30.706  19.693  -0.386  1.00  8.45           C  
ANISOU 1641  CA  LEU A 255      997    999   1214     53     26   -231       C  
ATOM   1642  C   LEU A 255      31.281  20.029  -1.745  1.00  9.28           C  
ANISOU 1642  C   LEU A 255     1111   1095   1319     38     61   -252       C  
ATOM   1643  O   LEU A 255      32.314  19.480  -2.101  1.00 11.10           O  
ANISOU 1643  O   LEU A 255     1134   1461   1619     75    197   -312       O  
ATOM   1644  CB  LEU A 255      30.007  18.335  -0.438  1.00  8.64           C  
ANISOU 1644  CB  LEU A 255     1037    943   1302     63     28   -285       C  
ATOM   1645  CG  LEU A 255      29.841  17.656   0.910  1.00  9.49           C  
ANISOU 1645  CG  LEU A 255     1165    940   1498     78     29   -242       C  
ATOM   1646  CD1 LEU A 255      28.872  16.499   0.750  1.00 10.27           C  
ANISOU 1646  CD1 LEU A 255     1119   1110   1672    151    131   -232       C  
ATOM   1647  CD2 LEU A 255      31.168  17.175   1.465  1.00 11.05           C  
ANISOU 1647  CD2 LEU A 255     1315   1062   1820    -31   -152    -65       C  
ATOM   1648  N   ALA A 256      30.640  20.922  -2.490  1.00  9.20           N  
ANISOU 1648  N   ALA A 256     1123   1256   1114     19     89   -258       N  
ATOM   1649  CA  ALA A 256      31.129  21.362  -3.791  1.00 10.32           C  
ANISOU 1649  CA  ALA A 256     1265   1444   1210    -50     33   -182       C  
ATOM   1650  C   ALA A 256      32.193  22.439  -3.700  1.00 10.63           C  
ANISOU 1650  C   ALA A 256     1286   1567   1185    -94     21   -169       C  
ATOM   1651  O   ALA A 256      32.742  22.840  -4.719  1.00 12.02           O  
ANISOU 1651  O   ALA A 256     1438   1939   1191   -245     83   -281       O  
ATOM   1652  CB  ALA A 256      29.980  21.859  -4.637  1.00 11.40           C  
ANISOU 1652  CB  ALA A 256     1451   1589   1291    -34     32   -172       C  
ATOM   1653  N   PHE A 257      32.524  22.896  -2.499  1.00 10.37           N  
ANISOU 1653  N   PHE A 257     1252   1490   1198   -144      0   -176       N  
ATOM   1654  CA  PHE A 257      33.544  23.909  -2.344  1.00 10.14           C  
ANISOU 1654  CA  PHE A 257     1268   1383   1202    -98      1   -156       C  
ATOM   1655  C   PHE A 257      34.861  23.436  -2.951  1.00 10.83           C  
ANISOU 1655  C   PHE A 257     1376   1458   1280   -137    -15   -162       C  
ATOM   1656  O   PHE A 257      35.276  22.305  -2.742  1.00 12.45           O  
ANISOU 1656  O   PHE A 257     1594   1558   1575   -181    125   -254       O  
ATOM   1657  CB  PHE A 257      33.740  24.227  -0.868  1.00 10.13           C  
ANISOU 1657  CB  PHE A 257     1280   1413   1155    -34    -31   -175       C  
ATOM   1658  CG  PHE A 257      34.707  25.338  -0.625  1.00  9.98           C  
ANISOU 1658  CG  PHE A 257     1358   1395   1036   -174     39   -160       C  
ATOM   1659  CD1 PHE A 257      34.322  26.652  -0.808  1.00 12.51           C  
ANISOU 1659  CD1 PHE A 257     1625   1598   1527   -153     59   -147       C  
ATOM   1660  CD2 PHE A 257      36.007  25.075  -0.245  1.00 10.29           C  
ANISOU 1660  CD2 PHE A 257     1430   1546    932   -129      9     63       C  
ATOM   1661  CE1 PHE A 257      35.213  27.684  -0.604  1.00 12.81           C  
ANISOU 1661  CE1 PHE A 257     1834   1550   1480   -252     89   -207       C  
ATOM   1662  CE2 PHE A 257      36.908  26.105  -0.047  1.00 11.11           C  
ANISOU 1662  CE2 PHE A 257     1541   1860    820   -185     72   -136       C  
ATOM   1663  CZ  PHE A 257      36.514  27.402  -0.225  1.00 11.91           C  
ANISOU 1663  CZ  PHE A 257     1665   1655   1204   -356     94   -273       C  
ATOM   1664  N   ASP A 258      35.528  24.336  -3.658  1.00 11.44           N  
ANISOU 1664  N   ASP A 258     1443   1633   1268   -173     69   -155       N  
ATOM   1665  CA  ASP A 258      36.758  24.032  -4.383  1.00 12.78           C  
ANISOU 1665  CA  ASP A 258     1607   1829   1421   -120     72    -70       C  
ATOM   1666  C   ASP A 258      37.981  24.047  -3.453  1.00 12.12           C  
ANISOU 1666  C   ASP A 258     1539   1748   1317   -175     52   -115       C  
ATOM   1667  O   ASP A 258      38.750  25.011  -3.450  1.00 12.95           O  
ANISOU 1667  O   ASP A 258     1629   1777   1513   -305   -107     80       O  
ATOM   1668  CB  ASP A 258      36.924  25.048  -5.532  1.00 13.85           C  
ANISOU 1668  CB  ASP A 258     1696   2126   1440    -85     97    -45       C  
ATOM   1669  CG  ASP A 258      38.161  24.804  -6.379  1.00 17.35           C  
ANISOU 1669  CG  ASP A 258     2103   2631   1855    -18    316    103       C  
ATOM   1670  OD1 ASP A 258      38.827  23.768  -6.182  1.00 20.95           O  
ANISOU 1670  OD1 ASP A 258     2382   3389   2190    390    871   -143       O  
ATOM   1671  OD2 ASP A 258      38.524  25.603  -7.274  1.00 22.02           O  
ANISOU 1671  OD2 ASP A 258     2564   3638   2162     32    500    247       O  
ATOM   1672  N   VAL A 259      38.204  22.962  -2.717  1.00 11.97           N  
ANISOU 1672  N   VAL A 259     1645   1579   1323   -173    130   -199       N  
ATOM   1673  CA  VAL A 259      39.350  22.899  -1.796  1.00 12.53           C  
ANISOU 1673  CA  VAL A 259     1838   1551   1370    -74     67   -154       C  
ATOM   1674  C   VAL A 259      40.679  22.812  -2.502  1.00 11.56           C  
ANISOU 1674  C   VAL A 259     1758   1505   1128    -86     -7   -256       C  
ATOM   1675  O   VAL A 259      41.689  23.263  -1.967  1.00 12.04           O  
ANISOU 1675  O   VAL A 259     1896   1637   1042   -123    -88   -324       O  
ATOM   1676  CB  VAL A 259      39.329  21.707  -0.794  1.00 13.90           C  
ANISOU 1676  CB  VAL A 259     2122   1569   1588    -45    180   -182       C  
ATOM   1677  CG1 VAL A 259      38.391  21.969   0.354  1.00 15.60           C  
ANISOU 1677  CG1 VAL A 259     2280   1861   1783    -87    118    -91       C  
ATOM   1678  CG2 VAL A 259      39.043  20.365  -1.501  1.00 13.99           C  
ANISOU 1678  CG2 VAL A 259     2242   1436   1636    -25    211   -140       C  
ATOM   1679  N   GLU A 260      40.696  22.234  -3.701  1.00 11.67           N  
ANISOU 1679  N   GLU A 260     1721   1561   1151   -126    -55   -297       N  
ATOM   1680  CA  GLU A 260      41.948  22.057  -4.407  1.00 12.24           C  
ANISOU 1680  CA  GLU A 260     1701   1660   1289    -42    -13   -309       C  
ATOM   1681  C   GLU A 260      42.641  23.359  -4.725  1.00 12.16           C  
ANISOU 1681  C   GLU A 260     1659   1744   1214   -111     -3   -369       C  
ATOM   1682  O   GLU A 260      43.868  23.377  -4.798  1.00 14.65           O  
ANISOU 1682  O   GLU A 260     1819   2098   1647    -99     32   -524       O  
ATOM   1683  CB  GLU A 260      41.725  21.268  -5.692  1.00 12.78           C  
ANISOU 1683  CB  GLU A 260     1743   1778   1334    -73     -4   -327       C  
ATOM   1684  CG  GLU A 260      41.405  19.815  -5.443  1.00 14.52           C  
ANISOU 1684  CG  GLU A 260     2004   2016   1495     73    -26   -420       C  
ATOM   1685  CD  GLU A 260      42.546  19.114  -4.750  1.00 18.53           C  
ANISOU 1685  CD  GLU A 260     2630   2213   2195    318    203   -385       C  
ATOM   1686  OE1 GLU A 260      43.674  19.108  -5.296  1.00 21.82           O  
ANISOU 1686  OE1 GLU A 260     2769   3051   2472    364    109   -214       O  
ATOM   1687  OE2 GLU A 260      42.319  18.578  -3.667  1.00 20.59           O  
ANISOU 1687  OE2 GLU A 260     3161   2545   2116    628     47   -683       O  
ATOM   1688  N   ASN A 261      41.874  24.429  -4.914  1.00 11.57           N  
ANISOU 1688  N   ASN A 261     1674   1723    997   -129     23   -291       N  
ATOM   1689  CA  ASN A 261      42.413  25.739  -5.259  1.00 12.22           C  
ANISOU 1689  CA  ASN A 261     1820   1753   1070   -136     49   -160       C  
ATOM   1690  C   ASN A 261      42.213  26.799  -4.187  1.00 11.42           C  
ANISOU 1690  C   ASN A 261     1768   1647    922   -176     40   -129       C  
ATOM   1691  O   ASN A 261      42.382  27.980  -4.433  1.00 13.10           O  
ANISOU 1691  O   ASN A 261     2321   1814    840   -244    133      6       O  
ATOM   1692  CB  ASN A 261      41.770  26.235  -6.547  1.00 12.89           C  
ANISOU 1692  CB  ASN A 261     1898   1914   1085   -131     84   -148       C  
ATOM   1693  CG  ASN A 261      42.117  25.381  -7.712  1.00 15.89           C  
ANISOU 1693  CG  ASN A 261     2156   2491   1389   -263    237   -418       C  
ATOM   1694  OD1 ASN A 261      43.287  25.262  -8.065  1.00 17.97           O  
ANISOU 1694  OD1 ASN A 261     2192   3411   1224   -420    198   -697       O  
ATOM   1695  ND2 ASN A 261      41.118  24.742  -8.291  1.00 18.57           N  
ANISOU 1695  ND2 ASN A 261     2494   3158   1402   -390    365   -844       N  
ATOM   1696  N   PHE A 262      41.856  26.378  -2.986  1.00  9.73           N  
ANISOU 1696  N   PHE A 262     1477   1410    808   -193     39     14       N  
ATOM   1697  CA  PHE A 262      41.526  27.295  -1.909  1.00  8.47           C  
ANISOU 1697  CA  PHE A 262     1249   1206    761    -92     -8     17       C  
ATOM   1698  C   PHE A 262      42.820  27.756  -1.244  1.00  8.66           C  
ANISOU 1698  C   PHE A 262     1251   1194    844   -107      0     62       C  
ATOM   1699  O   PHE A 262      43.475  27.009  -0.504  1.00  9.02           O  
ANISOU 1699  O   PHE A 262     1296   1297    832   -140    -38     72       O  
ATOM   1700  CB  PHE A 262      40.623  26.577  -0.912  1.00  8.66           C  
ANISOU 1700  CB  PHE A 262     1248   1160    879   -181      3    100       C  
ATOM   1701  CG  PHE A 262      40.302  27.344   0.350  1.00  7.88           C  
ANISOU 1701  CG  PHE A 262     1102   1028    864   -144     -7     34       C  
ATOM   1702  CD1 PHE A 262      40.049  28.702   0.346  1.00  8.72           C  
ANISOU 1702  CD1 PHE A 262     1250   1171    891   -173   -147     76       C  
ATOM   1703  CD2 PHE A 262      40.215  26.663   1.545  1.00  7.66           C  
ANISOU 1703  CD2 PHE A 262      936   1163    811   -179    -54    -15       C  
ATOM   1704  CE1 PHE A 262      39.750  29.365   1.521  1.00  8.47           C  
ANISOU 1704  CE1 PHE A 262     1027   1049   1139    -75    -29    -13       C  
ATOM   1705  CE2 PHE A 262      39.907  27.317   2.718  1.00  8.62           C  
ANISOU 1705  CE2 PHE A 262      987   1398    887   -126     20    -33       C  
ATOM   1706  CZ  PHE A 262      39.678  28.680   2.701  1.00  8.68           C  
ANISOU 1706  CZ  PHE A 262      959   1373    964   -156     78   -101       C  
HETATM 1707  N   MSE A 263      43.203  28.997  -1.535  1.00  8.52           N  
ANISOU 1707  N   MSE A 263     1279   1164    794   -104    -23     73       N  
HETATM 1708  CA  MSE A 263      44.358  29.641  -0.914  1.00  8.76           C  
ANISOU 1708  CA  MSE A 263     1223   1158    946   -112     29     43       C  
HETATM 1709  C   MSE A 263      43.950  30.157   0.452  1.00  8.16           C  
ANISOU 1709  C   MSE A 263     1170   1053    876   -103     10     44       C  
HETATM 1710  O   MSE A 263      42.915  30.779   0.575  1.00  9.70           O  
ANISOU 1710  O   MSE A 263     1259   1425   1000      1   -117     31       O  
HETATM 1711  CB  MSE A 263      44.829  30.801  -1.787  1.00  9.69           C  
ANISOU 1711  CB  MSE A 263     1313   1313   1054   -177     47     87       C  
HETATM 1712  CG  MSE A 263      45.232  30.387  -3.190  1.00 12.20           C  
ANISOU 1712  CG  MSE A 263     1691   1618   1324    -86    113     87       C  
HETATM 1713 SE   MSE A 263      46.854  29.332  -3.232  1.00 21.92          SE  
ANISOU 1713 SE   MSE A 263     3432   2715   2180   -234    613     63      SE  
HETATM 1714  CE  MSE A 263      48.106  30.765  -2.917  1.00 17.85           C  
ANISOU 1714  CE  MSE A 263     2469   2182   2130   -116     90    -14       C  
ATOM   1715  N   THR A 264      44.754  29.951   1.483  1.00  7.18           N  
ANISOU 1715  N   THR A 264     1007    909    808   -143    -21     48       N  
ATOM   1716  CA  THR A 264      44.310  30.426   2.790  1.00  6.91           C  
ANISOU 1716  CA  THR A 264      949    825    848   -132     27     24       C  
ATOM   1717  C   THR A 264      44.162  31.945   2.755  1.00  6.96           C  
ANISOU 1717  C   THR A 264      948    847    849   -116    -23     73       C  
ATOM   1718  O   THR A 264      45.069  32.661   2.305  1.00  6.77           O  
ANISOU 1718  O   THR A 264      920    769    881    -89     59    124       O  
ATOM   1719  CB  THR A 264      45.199  30.004   3.962  1.00  6.73           C  
ANISOU 1719  CB  THR A 264      992    752    813   -110     51     39       C  
ATOM   1720  OG1 THR A 264      44.766  30.725   5.125  1.00  6.50           O  
ANISOU 1720  OG1 THR A 264      953    872    644   -137     99     79       O  
ATOM   1721  CG2 THR A 264      46.672  30.316   3.748  1.00  7.14           C  
ANISOU 1721  CG2 THR A 264     1165    726    822     25      1     86       C  
ATOM   1722  N   PRO A 265      43.010  32.460   3.210  1.00  7.37           N  
ANISOU 1722  N   PRO A 265      917    929    953    -85     60    104       N  
ATOM   1723  CA  PRO A 265      42.792  33.905   3.288  1.00  7.59           C  
ANISOU 1723  CA  PRO A 265      927    987    967     -9    -11     86       C  
ATOM   1724  C   PRO A 265      43.399  34.540   4.522  1.00  6.57           C  
ANISOU 1724  C   PRO A 265      784    807    902     -2     48    167       C  
ATOM   1725  O   PRO A 265      43.348  35.776   4.644  1.00  7.40           O  
ANISOU 1725  O   PRO A 265     1021    787   1002     41    -17    157       O  
ATOM   1726  CB  PRO A 265      41.271  34.014   3.362  1.00  8.08           C  
ANISOU 1726  CB  PRO A 265      946   1083   1038    -19    -56     45       C  
ATOM   1727  CG  PRO A 265      40.877  32.807   4.102  1.00  9.35           C  
ANISOU 1727  CG  PRO A 265      930   1300   1321    -92     54    126       C  
ATOM   1728  CD  PRO A 265      41.797  31.718   3.608  1.00  7.90           C  
ANISOU 1728  CD  PRO A 265     1001    968   1029   -133     60    144       C  
ATOM   1729  N   LEU A 266      43.947  33.752   5.439  1.00  5.91           N  
ANISOU 1729  N   LEU A 266      806    670    769    -23    103    151       N  
ATOM   1730  CA  LEU A 266      44.418  34.304   6.694  1.00  5.83           C  
ANISOU 1730  CA  LEU A 266      774    653    786     18     97    115       C  
ATOM   1731  C   LEU A 266      45.612  35.245   6.553  1.00  5.87           C  
ANISOU 1731  C   LEU A 266      787    633    808     34    106    120       C  
ATOM   1732  O   LEU A 266      45.612  36.270   7.213  1.00  6.39           O  
ANISOU 1732  O   LEU A 266      945    664    818     40    101     27       O  
ATOM   1733  CB  LEU A 266      44.657  33.201   7.723  1.00  6.28           C  
ANISOU 1733  CB  LEU A 266      828    674    881   -103    106    189       C  
ATOM   1734  CG  LEU A 266      43.361  32.643   8.324  1.00  7.17           C  
ANISOU 1734  CG  LEU A 266      966    807    948     18    156    138       C  
ATOM   1735  CD1 LEU A 266      43.595  31.367   9.083  1.00  8.53           C  
ANISOU 1735  CD1 LEU A 266     1123    961   1156    -95    246    200       C  
ATOM   1736  CD2 LEU A 266      42.802  33.658   9.297  1.00 10.46           C  
ANISOU 1736  CD2 LEU A 266     1483   1143   1347     60    534    171       C  
ATOM   1737  N   PRO A 267      46.626  34.954   5.736  1.00  5.91           N  
ANISOU 1737  N   PRO A 267      776    651    818      4    122    111       N  
ATOM   1738  CA  PRO A 267      47.726  35.925   5.597  1.00  5.93           C  
ANISOU 1738  CA  PRO A 267      759    622    872     28     82    103       C  
ATOM   1739  C   PRO A 267      47.230  37.330   5.280  1.00  6.09           C  
ANISOU 1739  C   PRO A 267      759    647    908     -2    165     94       C  
ATOM   1740  O   PRO A 267      47.655  38.291   5.911  1.00  6.71           O  
ANISOU 1740  O   PRO A 267      795    736   1017     -9    161     59       O  
ATOM   1741  CB  PRO A 267      48.579  35.342   4.465  1.00  6.05           C  
ANISOU 1741  CB  PRO A 267      738    661    898     23     74    137       C  
ATOM   1742  CG  PRO A 267      48.381  33.868   4.607  1.00  5.95           C  
ANISOU 1742  CG  PRO A 267      850    671    738     63    169     93       C  
ATOM   1743  CD  PRO A 267      46.923  33.707   5.008  1.00  6.39           C  
ANISOU 1743  CD  PRO A 267      864    790    772    -12     68    140       C  
ATOM   1744  N   ALA A 268      46.313  37.467   4.336  1.00  6.50           N  
ANISOU 1744  N   ALA A 268      801    653   1014     -4     73    164       N  
ATOM   1745  CA  ALA A 268      45.830  38.794   3.975  1.00  7.31           C  
ANISOU 1745  CA  ALA A 268      998    754   1023     27     75    171       C  
ATOM   1746  C   ALA A 268      45.059  39.426   5.135  1.00  7.77           C  
ANISOU 1746  C   ALA A 268      992    773   1183     66    120    202       C  
ATOM   1747  O   ALA A 268      45.175  40.622   5.400  1.00  9.40           O  
ANISOU 1747  O   ALA A 268     1354    780   1438     95    332    143       O  
ATOM   1748  CB  ALA A 268      44.990  38.739   2.733  1.00  8.84           C  
ANISOU 1748  CB  ALA A 268     1176    989   1191     38     59    208       C  
ATOM   1749  N   LEU A 269      44.290  38.632   5.858  1.00  7.70           N  
ANISOU 1749  N   LEU A 269      970    800   1156    120    195    131       N  
ATOM   1750  CA  LEU A 269      43.571  39.131   7.021  1.00  8.78           C  
ANISOU 1750  CA  LEU A 269     1078    959   1299    152    181     68       C  
ATOM   1751  C   LEU A 269      44.513  39.592   8.129  1.00  8.67           C  
ANISOU 1751  C   LEU A 269     1061    951   1280     99    223     17       C  
ATOM   1752  O   LEU A 269      44.162  40.465   8.927  1.00 11.70           O  
ANISOU 1752  O   LEU A 269     1371   1347   1726    327    232   -242       O  
ATOM   1753  CB  LEU A 269      42.623  38.051   7.538  1.00  9.17           C  
ANISOU 1753  CB  LEU A 269     1121   1124   1237     93    282     69       C  
ATOM   1754  CG  LEU A 269      41.425  37.770   6.620  1.00 14.21           C  
ANISOU 1754  CG  LEU A 269     1698   1784   1915     62    154     80       C  
ATOM   1755  CD1 LEU A 269      40.796  36.430   6.947  1.00 17.01           C  
ANISOU 1755  CD1 LEU A 269     1991   2239   2232    -35     98     17       C  
ATOM   1756  CD2 LEU A 269      40.384  38.891   6.696  1.00 16.85           C  
ANISOU 1756  CD2 LEU A 269     1920   2137   2342    118     56     70       C  
ATOM   1757  N   LEU A 270      45.702  39.009   8.182  1.00  8.04           N  
ANISOU 1757  N   LEU A 270     1111    912   1033    147    163     60       N  
ATOM   1758  CA  LEU A 270      46.694  39.279   9.211  1.00  8.18           C  
ANISOU 1758  CA  LEU A 270     1119    906   1082     15    115     72       C  
ATOM   1759  C   LEU A 270      47.805  40.198   8.699  1.00  7.68           C  
ANISOU 1759  C   LEU A 270     1080    831   1006     86     86     80       C  
ATOM   1760  O   LEU A 270      48.890  40.216   9.257  1.00  9.64           O  
ANISOU 1760  O   LEU A 270     1347    998   1315   -116    -43    151       O  
ATOM   1761  CB  LEU A 270      47.243  37.949   9.719  1.00  7.97           C  
ANISOU 1761  CB  LEU A 270     1086    936   1005      7     80     75       C  
ATOM   1762  CG  LEU A 270      46.165  37.027  10.311  1.00  8.11           C  
ANISOU 1762  CG  LEU A 270     1061   1051    969    -14    114    211       C  
ATOM   1763  CD1 LEU A 270      46.769  35.669  10.658  1.00  8.46           C  
ANISOU 1763  CD1 LEU A 270     1058   1120   1037   -174   -133    236       C  
ATOM   1764  CD2 LEU A 270      45.498  37.651  11.532  1.00 10.32           C  
ANISOU 1764  CD2 LEU A 270     1363   1439   1119      2    244     78       C  
ATOM   1765  N   GLY A 271      47.510  40.991   7.669  1.00  8.18           N  
ANISOU 1765  N   GLY A 271     1183    904   1021     88     84     76       N  
ATOM   1766  CA  GLY A 271      48.389  42.078   7.271  1.00  8.56           C  
ANISOU 1766  CA  GLY A 271     1258    856   1136    -26     93     81       C  
ATOM   1767  C   GLY A 271      49.392  41.770   6.183  1.00  7.69           C  
ANISOU 1767  C   GLY A 271     1165    723   1031    -73     82    144       C  
ATOM   1768  O   GLY A 271      50.221  42.624   5.871  1.00  9.09           O  
ANISOU 1768  O   GLY A 271     1454    771   1225   -268    201    109       O  
ATOM   1769  N   LEU A 272      49.310  40.586   5.585  1.00  6.80           N  
ANISOU 1769  N   LEU A 272      999    714    870    -50     63    154       N  
ATOM   1770  CA  LEU A 272      50.345  40.113   4.687  1.00  6.41           C  
ANISOU 1770  CA  LEU A 272      876    673    886    -53     92    155       C  
ATOM   1771  C   LEU A 272      49.899  40.009   3.248  1.00  6.37           C  
ANISOU 1771  C   LEU A 272      852    696    871    -55    108    229       C  
ATOM   1772  O   LEU A 272      50.517  39.307   2.463  1.00  6.70           O  
ANISOU 1772  O   LEU A 272     1082    658    806    -37    151    298       O  
ATOM   1773  CB  LEU A 272      50.892  38.781   5.181  1.00  6.24           C  
ANISOU 1773  CB  LEU A 272      797    668    904    -27     61    214       C  
ATOM   1774  CG  LEU A 272      51.331  38.756   6.636  1.00  6.83           C  
ANISOU 1774  CG  LEU A 272      965    794    836     54     27    264       C  
ATOM   1775  CD1 LEU A 272      51.709  37.345   7.022  1.00  8.25           C  
ANISOU 1775  CD1 LEU A 272     1128   1050    953     78   -103    221       C  
ATOM   1776  CD2 LEU A 272      52.459  39.716   6.927  1.00  8.47           C  
ANISOU 1776  CD2 LEU A 272     1120   1049   1050    -14    -57    173       C  
ATOM   1777  N   GLY A 273      48.874  40.756   2.872  1.00  7.25           N  
ANISOU 1777  N   GLY A 273      960    876    917    -19     75    253       N  
ATOM   1778  CA  GLY A 273      48.369  40.714   1.508  1.00  8.03           C  
ANISOU 1778  CA  GLY A 273      955   1100    996    -71    112    187       C  
ATOM   1779  C   GLY A 273      49.389  41.082   0.439  1.00  7.52           C  
ANISOU 1779  C   GLY A 273      880   1030    944    -71     62    247       C  
ATOM   1780  O   GLY A 273      49.311  40.593  -0.678  1.00  8.90           O  
ANISOU 1780  O   GLY A 273     1077   1319    983   -304    -42    280       O  
ATOM   1781  N   ASN A 274      50.370  41.913   0.763  1.00  6.68           N  
ANISOU 1781  N   ASN A 274      871    807    858    -25     60    330       N  
ATOM   1782  CA  ASN A 274      51.383  42.282  -0.214  1.00  6.38           C  
ANISOU 1782  CA  ASN A 274      882    715    826    -13     69    291       C  
ATOM   1783  C   ASN A 274      52.530  41.290  -0.329  1.00  6.49           C  
ANISOU 1783  C   ASN A 274      903    770    790    -34     51    334       C  
ATOM   1784  O   ASN A 274      53.406  41.491  -1.159  1.00  7.21           O  
ANISOU 1784  O   ASN A 274      959    790    989     70    199    484       O  
ATOM   1785  CB  ASN A 274      51.951  43.678   0.087  1.00  7.01           C  
ANISOU 1785  CB  ASN A 274      920    817    926      4     20    321       C  
ATOM   1786  CG  ASN A 274      51.003  44.792  -0.247  1.00  7.28           C  
ANISOU 1786  CG  ASN A 274     1064    720    980    136    231    257       C  
ATOM   1787  OD1 ASN A 274      50.859  45.761   0.518  1.00 10.65           O  
ANISOU 1787  OD1 ASN A 274     1612   1077   1359    172    241    277       O  
ATOM   1788  ND2 ASN A 274      50.366  44.679  -1.370  1.00  6.71           N  
ANISOU 1788  ND2 ASN A 274     1030    732    784    323    151    454       N  
ATOM   1789  N   TYR A 275      52.517  40.230   0.484  1.00  6.57           N  
ANISOU 1789  N   TYR A 275      873    763    858      6     99    314       N  
ATOM   1790  CA  TYR A 275      53.658  39.312   0.603  1.00  6.85           C  
ANISOU 1790  CA  TYR A 275      876    810    915    -10     59    235       C  
ATOM   1791  C   TYR A 275      53.219  37.871   0.374  1.00  7.10           C  
ANISOU 1791  C   TYR A 275      962    809    925      6     19    286       C  
ATOM   1792  O   TYR A 275      53.327  37.019   1.241  1.00  7.10           O  
ANISOU 1792  O   TYR A 275      911    759   1026    -27    103    498       O  
ATOM   1793  CB  TYR A 275      54.326  39.476   1.969  1.00  7.13           C  
ANISOU 1793  CB  TYR A 275      867    821   1020     57    -29    283       C  
ATOM   1794  CG  TYR A 275      54.532  40.920   2.333  1.00  6.92           C  
ANISOU 1794  CG  TYR A 275      854    877    898     40     33    253       C  
ATOM   1795  CD1 TYR A 275      55.316  41.748   1.547  1.00  7.46           C  
ANISOU 1795  CD1 TYR A 275      908    934    990      0    145    160       C  
ATOM   1796  CD2 TYR A 275      53.901  41.481   3.431  1.00  8.72           C  
ANISOU 1796  CD2 TYR A 275     1039   1011   1260    -31    237    191       C  
ATOM   1797  CE1 TYR A 275      55.484  43.092   1.850  1.00  8.44           C  
ANISOU 1797  CE1 TYR A 275      994    998   1213    -58    137    198       C  
ATOM   1798  CE2 TYR A 275      54.064  42.814   3.748  1.00  9.37           C  
ANISOU 1798  CE2 TYR A 275     1229   1078   1252    -33    223     80       C  
ATOM   1799  CZ  TYR A 275      54.847  43.629   2.946  1.00  8.80           C  
ANISOU 1799  CZ  TYR A 275      983    930   1430    -13    116    133       C  
ATOM   1800  OH  TYR A 275      54.991  44.950   3.266  1.00 10.72           O  
ANISOU 1800  OH  TYR A 275     1292   1126   1653   -119    188    -21       O  
ATOM   1801  N   PRO A 276      52.701  37.587  -0.810  1.00  8.66           N  
ANISOU 1801  N   PRO A 276     1367    845   1076    -37   -106    266       N  
ATOM   1802  CA  PRO A 276      52.164  36.251  -1.076  1.00  9.32           C  
ANISOU 1802  CA  PRO A 276     1360    994   1187    -47    -50    132       C  
ATOM   1803  C   PRO A 276      53.257  35.193  -1.120  1.00  9.09           C  
ANISOU 1803  C   PRO A 276     1271    944   1236   -111     96    244       C  
ATOM   1804  O   PRO A 276      54.396  35.470  -1.514  1.00 10.10           O  
ANISOU 1804  O   PRO A 276     1508    961   1369   -188    273    251       O  
ATOM   1805  CB  PRO A 276      51.504  36.421  -2.443  1.00 10.84           C  
ANISOU 1805  CB  PRO A 276     1614   1152   1352    -82   -186    140       C  
ATOM   1806  CG  PRO A 276      52.224  37.542  -3.065  1.00 11.09           C  
ANISOU 1806  CG  PRO A 276     1828   1148   1238     51   -132    240       C  
ATOM   1807  CD  PRO A 276      52.552  38.479  -1.975  1.00  9.53           C  
ANISOU 1807  CD  PRO A 276     1623    930   1068     23   -169    289       C  
ATOM   1808  N   LEU A 277      52.884  33.977  -0.732  1.00  8.45           N  
ANISOU 1808  N   LEU A 277     1198    821   1189    -52    118    231       N  
ATOM   1809  CA  LEU A 277      53.727  32.800  -0.875  1.00  8.89           C  
ANISOU 1809  CA  LEU A 277     1155    987   1235    -29    155    126       C  
ATOM   1810  C   LEU A 277      53.105  31.902  -1.932  1.00  9.49           C  
ANISOU 1810  C   LEU A 277     1334   1094   1177    -68    312     94       C  
ATOM   1811  O   LEU A 277      51.918  31.569  -1.880  1.00  9.55           O  
ANISOU 1811  O   LEU A 277     1419   1206   1003   -134    169    -73       O  
ATOM   1812  CB  LEU A 277      53.835  32.055   0.448  1.00  8.57           C  
ANISOU 1812  CB  LEU A 277     1119    846   1290    -23     65    135       C  
ATOM   1813  CG  LEU A 277      54.541  32.810   1.576  1.00 10.34           C  
ANISOU 1813  CG  LEU A 277     1351    972   1603     30    -32     67       C  
ATOM   1814  CD1 LEU A 277      54.434  32.070   2.892  1.00 11.22           C  
ANISOU 1814  CD1 LEU A 277     1531   1200   1532    246   -261    125       C  
ATOM   1815  CD2 LEU A 277      55.994  33.045   1.225  1.00 13.04           C  
ANISOU 1815  CD2 LEU A 277     1588   1441   1922      5    -32    122       C  
ATOM   1816  N   GLU A 278      53.900  31.515  -2.919  1.00 11.82           N  
ANISOU 1816  N   GLU A 278     1593   1455   1442   -194    396    -12       N  
ATOM   1817  CA  GLU A 278      53.408  30.657  -3.991  1.00 13.14           C  
ANISOU 1817  CA  GLU A 278     1798   1636   1559   -141    323    -31       C  
ATOM   1818  C   GLU A 278      52.920  29.330  -3.423  1.00 12.74           C  
ANISOU 1818  C   GLU A 278     1734   1631   1474   -127    401    -93       C  
ATOM   1819  O   GLU A 278      53.570  28.743  -2.584  1.00 13.72           O  
ANISOU 1819  O   GLU A 278     1802   1518   1892    -63    433   -301       O  
ATOM   1820  CB  GLU A 278      54.493  30.364  -5.029  1.00 15.03           C  
ANISOU 1820  CB  GLU A 278     2023   1914   1773   -125    290    -53       C  
ATOM   1821  CG  GLU A 278      54.884  31.546  -5.895  1.00 19.81           C  
ANISOU 1821  CG  GLU A 278     2597   2473   2456   -142    170    -20       C  
ATOM   1822  CD  GLU A 278      56.106  32.291  -5.398  0.00 25.21           C  
ANISOU 1822  CD  GLU A 278     3296   3137   3144   -184    -40     88       C  
ATOM   1823  OE1 GLU A 278      56.755  31.833  -4.429  0.00 30.12           O  
ANISOU 1823  OE1 GLU A 278     3857   3678   3907   -226   -135     76       O  
ATOM   1824  OE2 GLU A 278      56.425  33.341  -5.991  0.00 28.28           O  
ANISOU 1824  OE2 GLU A 278     3638   3349   3755   -449     42    153       O  
ATOM   1825  N   GLY A 279      51.776  28.881  -3.905  1.00 12.54           N  
ANISOU 1825  N   GLY A 279     1746   1653   1366    -79    327   -127       N  
ATOM   1826  CA  GLY A 279      51.238  27.597  -3.527  1.00 11.69           C  
ANISOU 1826  CA  GLY A 279     1632   1468   1340    -95    282   -126       C  
ATOM   1827  C   GLY A 279      50.755  27.516  -2.090  1.00  9.81           C  
ANISOU 1827  C   GLY A 279     1374   1235   1117    -85    299   -122       C  
ATOM   1828  O   GLY A 279      50.645  26.419  -1.557  1.00 10.54           O  
ANISOU 1828  O   GLY A 279     1528   1166   1310    -89    463   -164       O  
ATOM   1829  N   ASN A 280      50.441  28.653  -1.468  1.00  8.20           N  
ANISOU 1829  N   ASN A 280     1244    997    872   -113    323    -50       N  
ATOM   1830  CA  ASN A 280      50.025  28.690  -0.077  1.00  7.34           C  
ANISOU 1830  CA  ASN A 280     1063    960    764   -108    179     -2       C  
ATOM   1831  C   ASN A 280      48.545  28.329   0.098  1.00  6.50           C  
ANISOU 1831  C   ASN A 280     1005    792    670   -123    166    -41       C  
ATOM   1832  O   ASN A 280      47.701  29.134   0.514  1.00  7.06           O  
ANISOU 1832  O   ASN A 280     1085    822    773   -106    158    -48       O  
ATOM   1833  CB  ASN A 280      50.338  30.049   0.517  1.00  6.94           C  
ANISOU 1833  CB  ASN A 280      968    824    844   -191    215     96       C  
ATOM   1834  CG  ASN A 280      50.291  30.041   2.034  1.00  6.68           C  
ANISOU 1834  CG  ASN A 280      965    841    730   -113    192    171       C  
ATOM   1835  OD1 ASN A 280      50.340  28.986   2.656  1.00  7.71           O  
ANISOU 1835  OD1 ASN A 280     1374    782    774   -110    200     80       O  
ATOM   1836  ND2 ASN A 280      50.208  31.212   2.632  1.00  6.70           N  
ANISOU 1836  ND2 ASN A 280      935    686    925    -29    210     22       N  
ATOM   1837  N   LEU A 281      48.253  27.077  -0.217  1.00  7.21           N  
ANISOU 1837  N   LEU A 281     1115    858    766   -140    163    -38       N  
ATOM   1838  CA  LEU A 281      46.922  26.508  -0.091  1.00  7.12           C  
ANISOU 1838  CA  LEU A 281     1040    897    766   -189     88     -3       C  
ATOM   1839  C   LEU A 281      46.557  26.279   1.364  1.00  6.89           C  
ANISOU 1839  C   LEU A 281      925    926    765   -188     88     12       C  
ATOM   1840  O   LEU A 281      47.396  25.904   2.183  1.00  7.27           O  
ANISOU 1840  O   LEU A 281      979   1122    659   -108     99      7       O  
ATOM   1841  CB  LEU A 281      46.860  25.180  -0.831  1.00  8.36           C  
ANISOU 1841  CB  LEU A 281     1229   1017    931   -218    140     -7       C  
ATOM   1842  CG  LEU A 281      46.948  25.287  -2.354  1.00  9.69           C  
ANISOU 1842  CG  LEU A 281     1411   1308    961   -205    169   -103       C  
ATOM   1843  CD1 LEU A 281      47.295  23.940  -2.941  1.00 12.76           C  
ANISOU 1843  CD1 LEU A 281     1976   1548   1323   -106     58   -154       C  
ATOM   1844  CD2 LEU A 281      45.634  25.787  -2.931  1.00 11.18           C  
ANISOU 1844  CD2 LEU A 281     1612   1586   1047   -210    -42   -118       C  
ATOM   1845  N   ALA A 282      45.292  26.530   1.675  1.00  6.55           N  
ANISOU 1845  N   ALA A 282      851    878    760   -156     67     86       N  
ATOM   1846  CA  ALA A 282      44.723  26.126   2.941  1.00  6.25           C  
ANISOU 1846  CA  ALA A 282      855    832    686    -99     63    -25       C  
ATOM   1847  C   ALA A 282      44.790  24.620   3.094  1.00  5.72           C  
ANISOU 1847  C   ALA A 282      739    837    596    -86    116    -33       C  
ATOM   1848  O   ALA A 282      44.795  23.870   2.119  1.00  6.98           O  
ANISOU 1848  O   ALA A 282     1111    919    619   -131    216    -60       O  
ATOM   1849  CB  ALA A 282      43.296  26.593   3.022  1.00  6.29           C  
ANISOU 1849  CB  ALA A 282      864    859    665   -137    -21      5       C  
ATOM   1850  N   GLU A 283      44.789  24.160   4.337  1.00  5.17           N  
ANISOU 1850  N   GLU A 283      790    651    521    -98     98   -104       N  
ATOM   1851  CA  GLU A 283      44.709  22.726   4.588  1.00  5.70           C  
ANISOU 1851  CA  GLU A 283      759    716    689    -11     84    -19       C  
ATOM   1852  C   GLU A 283      43.454  22.121   3.961  1.00  5.30           C  
ANISOU 1852  C   GLU A 283      730    719    565      2     97   -108       C  
ATOM   1853  O   GLU A 283      43.499  21.039   3.369  1.00  6.26           O  
ANISOU 1853  O   GLU A 283      843    847    687     18     81   -279       O  
ATOM   1854  CB  GLU A 283      44.744  22.461   6.094  1.00  5.69           C  
ANISOU 1854  CB  GLU A 283      777    770    613    -11     74    -85       C  
ATOM   1855  CG  GLU A 283      44.480  21.017   6.455  1.00  6.55           C  
ANISOU 1855  CG  GLU A 283     1049    775    662    -43     77     -8       C  
ATOM   1856  CD  GLU A 283      44.361  20.745   7.929  1.00  6.26           C  
ANISOU 1856  CD  GLU A 283      970    518    887     10    129     38       C  
ATOM   1857  OE1 GLU A 283      44.705  21.602   8.755  1.00  6.99           O  
ANISOU 1857  OE1 GLU A 283     1106    757    791   -150    -25    -26       O  
ATOM   1858  OE2 GLU A 283      43.885  19.638   8.249  1.00  8.17           O  
ANISOU 1858  OE2 GLU A 283     1540    695    867    -82    326    -66       O  
ATOM   1859  N   GLY A 284      42.330  22.809   4.168  1.00  4.94           N  
ANISOU 1859  N   GLY A 284      649    608    619    -35     96   -116       N  
ATOM   1860  CA  GLY A 284      41.047  22.356   3.684  1.00  5.27           C  
ANISOU 1860  CA  GLY A 284      727    681    591    -35    109   -150       C  
ATOM   1861  C   GLY A 284      39.944  23.098   4.382  1.00  4.70           C  
ANISOU 1861  C   GLY A 284      656    638    490    -34     20   -111       C  
ATOM   1862  O   GLY A 284      40.120  24.239   4.774  1.00  4.81           O  
ANISOU 1862  O   GLY A 284      750    555    522    -55     37   -107       O  
ATOM   1863  N   VAL A 285      38.804  22.427   4.504  1.00  4.57           N  
ANISOU 1863  N   VAL A 285      598    605    531     -4     76    -78       N  
ATOM   1864  CA  VAL A 285      37.627  22.982   5.159  1.00  4.56           C  
ANISOU 1864  CA  VAL A 285      604    577    552     17     31    -61       C  
ATOM   1865  C   VAL A 285      37.010  21.981   6.115  1.00  4.61           C  
ANISOU 1865  C   VAL A 285      582    544    626     21     31    -54       C  
ATOM   1866  O   VAL A 285      37.176  20.763   5.970  1.00  4.93           O  
ANISOU 1866  O   VAL A 285      734    517    621     15    199    -86       O  
ATOM   1867  CB  VAL A 285      36.548  23.462   4.151  1.00  5.04           C  
ANISOU 1867  CB  VAL A 285      692    639    583     32     12    -37       C  
ATOM   1868  CG1 VAL A 285      37.097  24.614   3.321  1.00  6.08           C  
ANISOU 1868  CG1 VAL A 285      837    743    730     41    -48    -42       C  
ATOM   1869  CG2 VAL A 285      36.023  22.333   3.287  1.00  6.32           C  
ANISOU 1869  CG2 VAL A 285      838    785    776    -29    -42   -181       C  
ATOM   1870  N   VAL A 286      36.294  22.520   7.097  1.00  3.98           N  
ANISOU 1870  N   VAL A 286      549    429    535      5     56    -69       N  
ATOM   1871  CA  VAL A 286      35.398  21.760   7.949  1.00  4.31           C  
ANISOU 1871  CA  VAL A 286      604    488    545     47     80     14       C  
ATOM   1872  C   VAL A 286      33.979  22.163   7.581  1.00  4.45           C  
ANISOU 1872  C   VAL A 286      608    485    595     50     62    -11       C  
ATOM   1873  O   VAL A 286      33.669  23.355   7.470  1.00  5.08           O  
ANISOU 1873  O   VAL A 286      636    488    803     90     14     20       O  
ATOM   1874  CB  VAL A 286      35.682  22.050   9.432  1.00  4.84           C  
ANISOU 1874  CB  VAL A 286      672    576    591     44     70    -25       C  
ATOM   1875  CG1 VAL A 286      34.632  21.442  10.340  1.00  5.51           C  
ANISOU 1875  CG1 VAL A 286      781    728    584     57     40     13       C  
ATOM   1876  CG2 VAL A 286      37.072  21.519   9.801  1.00  5.34           C  
ANISOU 1876  CG2 VAL A 286      669    679    680    -47     48    -54       C  
ATOM   1877  N   ILE A 287      33.134  21.156   7.363  1.00  4.90           N  
ANISOU 1877  N   ILE A 287      627    522    711     73     35     -3       N  
ATOM   1878  CA  ILE A 287      31.742  21.361   6.970  1.00  4.88           C  
ANISOU 1878  CA  ILE A 287      591    517    745     60      7     30       C  
ATOM   1879  C   ILE A 287      30.880  20.861   8.110  1.00  4.87           C  
ANISOU 1879  C   ILE A 287      507    577    765     65     12     27       C  
ATOM   1880  O   ILE A 287      31.066  19.749   8.613  1.00  5.64           O  
ANISOU 1880  O   ILE A 287      644    597    901     81    108    112       O  
ATOM   1881  CB  ILE A 287      31.454  20.612   5.658  1.00  5.65           C  
ANISOU 1881  CB  ILE A 287      729    612    803     69    -56    -36       C  
ATOM   1882  CG1 ILE A 287      32.210  21.311   4.513  1.00  6.69           C  
ANISOU 1882  CG1 ILE A 287      856    819    864     23    -30      1       C  
ATOM   1883  CG2 ILE A 287      29.966  20.532   5.390  1.00  6.65           C  
ANISOU 1883  CG2 ILE A 287      797    924    803    -30    -40    -60       C  
ATOM   1884  CD1 ILE A 287      32.283  20.504   3.229  1.00  7.77           C  
ANISOU 1884  CD1 ILE A 287     1042   1004    904     20     36   -109       C  
ATOM   1885  N   ARG A 288      29.924  21.684   8.530  1.00  5.30           N  
ANISOU 1885  N   ARG A 288      594    612    808     69    118    120       N  
ATOM   1886  CA  ARG A 288      29.090  21.339   9.667  1.00  5.35           C  
ANISOU 1886  CA  ARG A 288      596    634    801     59     21     37       C  
ATOM   1887  C   ARG A 288      27.683  21.900   9.508  1.00  5.13           C  
ANISOU 1887  C   ARG A 288      566    602    778     98      1    -13       C  
ATOM   1888  O   ARG A 288      27.473  22.935   8.895  1.00  5.59           O  
ANISOU 1888  O   ARG A 288      591    651    880     89     10     13       O  
ATOM   1889  CB  ARG A 288      29.703  21.830  10.978  1.00  6.21           C  
ANISOU 1889  CB  ARG A 288      610    887    860     88     75     87       C  
ATOM   1890  CG  ARG A 288      29.902  23.331  11.047  1.00  7.15           C  
ANISOU 1890  CG  ARG A 288      779   1019    916    -37    -33     -4       C  
ATOM   1891  CD  ARG A 288      30.782  23.711  12.205  1.00  8.37           C  
ANISOU 1891  CD  ARG A 288      916   1228   1034   -116    -48    -76       C  
ATOM   1892  NE  ARG A 288      30.097  23.543  13.479  1.00  7.60           N  
ANISOU 1892  NE  ARG A 288      719   1260    908   -209    -26    -49       N  
ATOM   1893  CZ  ARG A 288      30.712  23.360  14.638  1.00  7.30           C  
ANISOU 1893  CZ  ARG A 288      750   1067    955   -106   -133    -66       C  
ATOM   1894  NH1 ARG A 288      32.034  23.243  14.700  1.00  7.77           N  
ANISOU 1894  NH1 ARG A 288      822   1167    963    132   -108   -255       N  
ATOM   1895  NH2 ARG A 288      30.000  23.243  15.750  1.00  7.40           N  
ANISOU 1895  NH2 ARG A 288      723   1166    922    106    -81    -25       N  
ATOM   1896  N   HIS A 289      26.735  21.216  10.119  1.00  5.36           N  
ANISOU 1896  N   HIS A 289      601    640    797     97    -49     -5       N  
ATOM   1897  CA  HIS A 289      25.347  21.661  10.166  1.00  4.88           C  
ANISOU 1897  CA  HIS A 289      544    606    702    104      1    -30       C  
ATOM   1898  C   HIS A 289      25.287  22.902  11.031  1.00  5.22           C  
ANISOU 1898  C   HIS A 289      515    648    820     76    -19    -83       C  
ATOM   1899  O   HIS A 289      25.900  22.941  12.095  1.00  5.93           O  
ANISOU 1899  O   HIS A 289      588    809    854     38    -21    -78       O  
ATOM   1900  CB  HIS A 289      24.492  20.531  10.767  1.00  5.71           C  
ANISOU 1900  CB  HIS A 289      653    593    923     58     33     10       C  
ATOM   1901  CG  HIS A 289      23.022  20.736  10.654  1.00  6.16           C  
ANISOU 1901  CG  HIS A 289      694    750    896     72     73   -124       C  
ATOM   1902  ND1 HIS A 289      22.381  21.815  11.195  1.00  7.90           N  
ANISOU 1902  ND1 HIS A 289      669    824   1507   -105     71   -227       N  
ATOM   1903  CD2 HIS A 289      22.054  19.930  10.165  1.00  8.97           C  
ANISOU 1903  CD2 HIS A 289      920    882   1604     45     13   -171       C  
ATOM   1904  CE1 HIS A 289      21.091  21.723  10.938  1.00  7.86           C  
ANISOU 1904  CE1 HIS A 289      712    691   1580     95     91   -188       C  
ATOM   1905  NE2 HIS A 289      20.866  20.595  10.304  1.00  8.11           N  
ANISOU 1905  NE2 HIS A 289      660   1114   1305     87      0    -65       N  
ATOM   1906  N   VAL A 290      24.521  23.905  10.630  1.00  5.87           N  
ANISOU 1906  N   VAL A 290      638    731    857     67     -3   -142       N  
ATOM   1907  CA  VAL A 290      24.488  25.142  11.390  1.00  6.53           C  
ANISOU 1907  CA  VAL A 290      749    698   1034     38     69   -115       C  
ATOM   1908  C   VAL A 290      23.858  25.000  12.770  1.00  6.52           C  
ANISOU 1908  C   VAL A 290      709    676   1089     72     53    -88       C  
ATOM   1909  O   VAL A 290      24.050  25.878  13.606  1.00  6.88           O  
ANISOU 1909  O   VAL A 290      777    710   1124      9     71   -223       O  
ATOM   1910  CB  VAL A 290      23.836  26.310  10.618  1.00  7.79           C  
ANISOU 1910  CB  VAL A 290      973    774   1212    113    133    -35       C  
ATOM   1911  CG1 VAL A 290      24.584  26.591   9.329  1.00  8.54           C  
ANISOU 1911  CG1 VAL A 290     1124    887   1234    139    117     13       C  
ATOM   1912  CG2 VAL A 290      22.356  26.089  10.409  1.00  8.74           C  
ANISOU 1912  CG2 VAL A 290     1078   1006   1236    210    101    -29       C  
ATOM   1913  N   ARG A 291      23.121  23.919  13.011  1.00  6.70           N  
ANISOU 1913  N   ARG A 291      714    823   1007     32     78    -97       N  
ATOM   1914  CA  ARG A 291      22.558  23.636  14.325  1.00  7.46           C  
ANISOU 1914  CA  ARG A 291      743    961   1131     26    172    -87       C  
ATOM   1915  C   ARG A 291      23.140  22.375  14.932  1.00  7.30           C  
ANISOU 1915  C   ARG A 291      767    914   1093     20    167   -117       C  
ATOM   1916  O   ARG A 291      22.545  21.780  15.815  1.00  8.31           O  
ANISOU 1916  O   ARG A 291      843   1082   1232     40    338    -28       O  
ATOM   1917  CB  ARG A 291      21.029  23.594  14.277  1.00  8.90           C  
ANISOU 1917  CB  ARG A 291      913   1153   1314     54    207    -77       C  
ATOM   1918  CG  ARG A 291      20.465  24.959  13.915  1.00 13.01           C  
ANISOU 1918  CG  ARG A 291     1252   1805   1886    215    283    154       C  
ATOM   1919  CD  ARG A 291      20.653  26.061  14.968  1.00 19.77           C  
ANISOU 1919  CD  ARG A 291     2372   2489   2648     43    122    103       C  
ATOM   1920  NE  ARG A 291      19.893  25.853  16.209  1.00 23.69           N  
ANISOU 1920  NE  ARG A 291     2943   2992   3064    114    176    -75       N  
ATOM   1921  CZ  ARG A 291      19.894  26.689  17.259  1.00 27.86           C  
ANISOU 1921  CZ  ARG A 291     3511   3546   3527    -68    111    -20       C  
ATOM   1922  NH1 ARG A 291      20.636  27.794  17.257  1.00 29.34           N  
ANISOU 1922  NH1 ARG A 291     3791   3645   3711    -37    157    -35       N  
ATOM   1923  NH2 ARG A 291      19.166  26.403  18.335  1.00 29.81           N  
ANISOU 1923  NH2 ARG A 291     3798   3779   3749    -44     94      7       N  
ATOM   1924  N   ARG A 292      24.344  22.007  14.512  1.00  7.26           N  
ANISOU 1924  N   ARG A 292      815    924   1018     51    171   -129       N  
ATOM   1925  CA  ARG A 292      25.083  20.949  15.190  1.00  7.74           C  
ANISOU 1925  CA  ARG A 292      875   1062   1005     48    118    -45       C  
ATOM   1926  C   ARG A 292      25.039  21.172  16.702  1.00  8.11           C  
ANISOU 1926  C   ARG A 292      915   1060   1105     60    158    -87       C  
ATOM   1927  O   ARG A 292      25.284  22.279  17.190  1.00  8.45           O  
ANISOU 1927  O   ARG A 292      991   1207   1010      3    275   -197       O  
ATOM   1928  CB  ARG A 292      26.533  20.932  14.719  1.00  7.31           C  
ANISOU 1928  CB  ARG A 292      823   1004    947     98    181   -148       C  
ATOM   1929  CG  ARG A 292      27.425  20.000  15.474  1.00  9.06           C  
ANISOU 1929  CG  ARG A 292      990   1369   1081    314    127    -18       C  
ATOM   1930  CD  ARG A 292      28.706  19.723  14.710  1.00  9.52           C  
ANISOU 1930  CD  ARG A 292      925   1522   1167    422     95     81       C  
ATOM   1931  NE  ARG A 292      29.514  18.683  15.360  1.00 13.46           N  
ANISOU 1931  NE  ARG A 292     1248   2296   1569    459    461    -50       N  
ATOM   1932  CZ  ARG A 292      30.316  18.903  16.352  1.00 13.64           C  
ANISOU 1932  CZ  ARG A 292     1240   2210   1732    376    465    -97       C  
ATOM   1933  NH1 ARG A 292      30.499  20.135  16.795  1.00 15.43           N  
ANISOU 1933  NH1 ARG A 292     1683   2119   2059    288    -64   -170       N  
ATOM   1934  NH2 ARG A 292      30.976  17.893  16.905  1.00 12.06           N  
ANISOU 1934  NH2 ARG A 292     1453   1560   1568    468     31    151       N  
ATOM   1935  N   GLY A 293      24.719  20.120  17.436  1.00  9.14           N  
ANISOU 1935  N   GLY A 293     1071   1290   1111     10    171    -62       N  
ATOM   1936  CA  GLY A 293      24.597  20.200  18.880  1.00  9.93           C  
ANISOU 1936  CA  GLY A 293     1212   1387   1173    -53    105    -31       C  
ATOM   1937  C   GLY A 293      23.178  20.390  19.386  1.00 10.47           C  
ANISOU 1937  C   GLY A 293     1341   1486   1152    -54    266   -102       C  
ATOM   1938  O   GLY A 293      22.904  20.105  20.557  1.00 12.86           O  
ANISOU 1938  O   GLY A 293     1734   1975   1176    -71    361    -10       O  
ATOM   1939  N   ASP A 294      22.271  20.868  18.544  1.00 10.45           N  
ANISOU 1939  N   ASP A 294     1297   1434   1239      1    352   -141       N  
ATOM   1940  CA  ASP A 294      20.880  21.052  18.953  1.00 11.81           C  
ANISOU 1940  CA  ASP A 294     1447   1553   1488     44    292   -139       C  
ATOM   1941  C   ASP A 294      20.230  19.687  19.098  1.00 11.76           C  
ANISOU 1941  C   ASP A 294     1419   1612   1434     14    350   -132       C  
ATOM   1942  O   ASP A 294      20.431  18.826  18.249  1.00 10.49           O  
ANISOU 1942  O   ASP A 294     1186   1361   1438     36    360   -201       O  
ATOM   1943  CB  ASP A 294      20.135  21.853  17.899  1.00 12.62           C  
ANISOU 1943  CB  ASP A 294     1463   1577   1752    118    316   -138       C  
ATOM   1944  CG  ASP A 294      18.711  22.155  18.305  1.00 16.43           C  
ANISOU 1944  CG  ASP A 294     1910   1905   2425    184    255   -129       C  
ATOM   1945  OD1 ASP A 294      18.454  23.275  18.779  1.00 23.07           O  
ANISOU 1945  OD1 ASP A 294     2654   2742   3369    331    492   -263       O  
ATOM   1946  OD2 ASP A 294      17.794  21.334  18.205  1.00 20.46           O  
ANISOU 1946  OD2 ASP A 294     1908   2522   3341    411    538     32       O  
ATOM   1947  N   PRO A 295      19.465  19.452  20.170  1.00 13.04           N  
ANISOU 1947  N   PRO A 295     1646   1729   1579    -45    314   -117       N  
ATOM   1948  CA  PRO A 295      18.816  18.148  20.347  1.00 13.41           C  
ANISOU 1948  CA  PRO A 295     1655   1787   1653    -56    298    -57       C  
ATOM   1949  C   PRO A 295      18.017  17.647  19.148  1.00 12.36           C  
ANISOU 1949  C   PRO A 295     1440   1669   1585    -45    394    -25       C  
ATOM   1950  O   PRO A 295      18.015  16.451  18.918  1.00 12.76           O  
ANISOU 1950  O   PRO A 295     1504   1556   1788      0    502   -101       O  
ATOM   1951  CB  PRO A 295      17.896  18.370  21.551  1.00 14.58           C  
ANISOU 1951  CB  PRO A 295     1835   2001   1702    -59    290    -64       C  
ATOM   1952  CG  PRO A 295      18.516  19.459  22.304  1.00 15.54           C  
ANISOU 1952  CG  PRO A 295     2001   2045   1857    -23    236    -48       C  
ATOM   1953  CD  PRO A 295      19.209  20.343  21.320  1.00 14.11           C  
ANISOU 1953  CD  PRO A 295     1791   1926   1643    -63    305   -109       C  
ATOM   1954  N   ALA A 296      17.338  18.515  18.414  1.00 12.24           N  
ANISOU 1954  N   ALA A 296     1357   1626   1664    126    386    -95       N  
ATOM   1955  CA  ALA A 296      16.563  18.083  17.260  1.00 12.75           C  
ANISOU 1955  CA  ALA A 296     1489   1645   1708     76    165    -37       C  
ATOM   1956  C   ALA A 296      17.464  17.609  16.115  1.00 12.44           C  
ANISOU 1956  C   ALA A 296     1454   1599   1671     89    150    -73       C  
ATOM   1957  O   ALA A 296      17.038  16.817  15.286  1.00 14.64           O  
ANISOU 1957  O   ALA A 296     1550   1993   2020    -89     86   -103       O  
ATOM   1958  CB  ALA A 296      15.620  19.183  16.774  1.00 14.02           C  
ANISOU 1958  CB  ALA A 296     1638   1813   1875    114     74    -12       C  
ATOM   1959  N   VAL A 297      18.696  18.101  16.050  1.00 11.35           N  
ANISOU 1959  N   VAL A 297     1373   1411   1525     62    201   -129       N  
ATOM   1960  CA  VAL A 297      19.686  17.573  15.102  1.00 11.37           C  
ANISOU 1960  CA  VAL A 297     1414   1489   1417    -34    187   -137       C  
ATOM   1961  C   VAL A 297      20.300  16.291  15.638  1.00 10.85           C  
ANISOU 1961  C   VAL A 297     1226   1405   1490     -5    215   -158       C  
ATOM   1962  O   VAL A 297      20.427  15.294  14.932  1.00 11.02           O  
ANISOU 1962  O   VAL A 297     1231   1415   1539     25    238   -377       O  
ATOM   1963  CB  VAL A 297      20.802  18.600  14.840  1.00 12.26           C  
ANISOU 1963  CB  VAL A 297     1549   1636   1471    -98    225   -123       C  
ATOM   1964  CG1 VAL A 297      22.001  17.964  14.107  1.00 12.81           C  
ANISOU 1964  CG1 VAL A 297     1645   1715   1505   -225    159   -151       C  
ATOM   1965  CG2 VAL A 297      20.248  19.746  14.046  1.00 14.27           C  
ANISOU 1965  CG2 VAL A 297     1875   1780   1767    -74      9   -216       C  
ATOM   1966  N   GLU A 298      20.707  16.327  16.889  1.00 11.35           N  
ANISOU 1966  N   GLU A 298     1321   1416   1575     67    123    -88       N  
ATOM   1967  CA  GLU A 298      21.426  15.211  17.495  1.00 12.68           C  
ANISOU 1967  CA  GLU A 298     1542   1538   1736     90     31    -45       C  
ATOM   1968  C   GLU A 298      20.585  13.956  17.631  1.00 12.10           C  
ANISOU 1968  C   GLU A 298     1511   1463   1620    126     49    -31       C  
ATOM   1969  O   GLU A 298      21.129  12.866  17.694  1.00 12.22           O  
ANISOU 1969  O   GLU A 298     1590   1419   1633    286     -3     52       O  
ATOM   1970  CB  GLU A 298      21.936  15.613  18.882  1.00 13.76           C  
ANISOU 1970  CB  GLU A 298     1685   1670   1872    125    -44    -43       C  
ATOM   1971  CG  GLU A 298      22.959  16.729  18.859  1.00 15.90           C  
ANISOU 1971  CG  GLU A 298     1931   1884   2225    144    -25   -112       C  
ATOM   1972  CD  GLU A 298      24.120  16.391  17.957  1.00 17.80           C  
ANISOU 1972  CD  GLU A 298     2176   2078   2509     75     61   -165       C  
ATOM   1973  OE1 GLU A 298      24.715  15.318  18.185  1.00 17.49           O  
ANISOU 1973  OE1 GLU A 298     2065   2077   2503     33    232    148       O  
ATOM   1974  OE2 GLU A 298      24.419  17.155  16.998  1.00 18.24           O  
ANISOU 1974  OE2 GLU A 298     2038   2099   2791    397   -167   -375       O  
ATOM   1975  N   LYS A 299      19.264  14.103  17.649  1.00 12.00           N  
ANISOU 1975  N   LYS A 299     1512   1459   1588     39    103     31       N  
ATOM   1976  CA  LYS A 299      18.387  12.960  17.831  1.00 11.96           C  
ANISOU 1976  CA  LYS A 299     1481   1481   1580      6    153     67       C  
ATOM   1977  C   LYS A 299      18.562  11.933  16.722  1.00 11.04           C  
ANISOU 1977  C   LYS A 299     1355   1393   1447    -12    187    138       C  
ATOM   1978  O   LYS A 299      18.241  10.778  16.910  1.00 11.87           O  
ANISOU 1978  O   LYS A 299     1637   1345   1527   -123    335    269       O  
ATOM   1979  CB  LYS A 299      16.916  13.406  17.924  1.00 13.12           C  
ANISOU 1979  CB  LYS A 299     1549   1671   1765    -64    245     36       C  
ATOM   1980  CG  LYS A 299      16.315  13.879  16.622  1.00 14.63           C  
ANISOU 1980  CG  LYS A 299     1541   1976   2042     61    264      1       C  
ATOM   1981  CD  LYS A 299      14.823  14.207  16.734  1.00 18.08           C  
ANISOU 1981  CD  LYS A 299     1921   2520   2428     66    187      2       C  
ATOM   1982  CE  LYS A 299      14.305  14.851  15.448  1.00 20.05           C  
ANISOU 1982  CE  LYS A 299     2020   2933   2665    162     44   -155       C  
ATOM   1983  NZ  LYS A 299      12.830  15.127  15.487  1.00 22.97           N  
ANISOU 1983  NZ  LYS A 299     2148   3365   3213    147    163   -107       N  
ATOM   1984  N   HIS A 300      19.021  12.354  15.549  1.00  9.79           N  
ANISOU 1984  N   HIS A 300     1164   1164   1390     32    207    228       N  
ATOM   1985  CA  HIS A 300      19.188  11.434  14.433  1.00  8.95           C  
ANISOU 1985  CA  HIS A 300     1064   1146   1191     17    129    175       C  
ATOM   1986  C   HIS A 300      20.392  10.511  14.561  1.00  8.41           C  
ANISOU 1986  C   HIS A 300     1057    977   1160     22    200    164       C  
ATOM   1987  O   HIS A 300      20.546   9.589  13.774  1.00  9.88           O  
ANISOU 1987  O   HIS A 300     1229   1194   1330     96    138     66       O  
ATOM   1988  CB  HIS A 300      19.297  12.219  13.143  1.00  9.44           C  
ANISOU 1988  CB  HIS A 300     1107   1190   1288    -24     90    138       C  
ATOM   1989  CG  HIS A 300      18.084  13.033  12.848  1.00  9.82           C  
ANISOU 1989  CG  HIS A 300      986   1301   1444    102     73     79       C  
ATOM   1990  ND1 HIS A 300      17.022  12.550  12.117  1.00 13.98           N  
ANISOU 1990  ND1 HIS A 300     1361   1772   2176    115    -79     40       N  
ATOM   1991  CD2 HIS A 300      17.739  14.283  13.236  1.00 13.47           C  
ANISOU 1991  CD2 HIS A 300     1501   1526   2089    151   -257    -39       C  
ATOM   1992  CE1 HIS A 300      16.102  13.489  12.018  1.00 13.24           C  
ANISOU 1992  CE1 HIS A 300     1391   1656   1981    284   -190     -4       C  
ATOM   1993  NE2 HIS A 300      16.508  14.548  12.692  1.00 13.57           N  
ANISOU 1993  NE2 HIS A 300     1337   1706   2113    419   -221   -144       N  
ATOM   1994  N   ASN A 301      21.261  10.773  15.525  1.00  8.92           N  
ANISOU 1994  N   ASN A 301     1128   1026   1234      4    212    102       N  
ATOM   1995  CA  ASN A 301      22.418   9.916  15.780  1.00  8.79           C  
ANISOU 1995  CA  ASN A 301     1095   1064   1179     18    179    101       C  
ATOM   1996  C   ASN A 301      23.349   9.811  14.570  1.00  8.93           C  
ANISOU 1996  C   ASN A 301     1132   1020   1240    -10    221     65       C  
ATOM   1997  O   ASN A 301      23.896   8.747  14.298  1.00  9.88           O  
ANISOU 1997  O   ASN A 301     1418    996   1340     47    459    125       O  
ATOM   1998  CB  ASN A 301      21.966   8.525  16.227  1.00  9.31           C  
ANISOU 1998  CB  ASN A 301     1165   1148   1221      4    176    154       C  
ATOM   1999  CG  ASN A 301      23.099   7.680  16.756  1.00 10.16           C  
ANISOU 1999  CG  ASN A 301     1264   1316   1278     -2     43    140       C  
ATOM   2000  OD1 ASN A 301      23.968   8.160  17.495  1.00 11.85           O  
ANISOU 2000  OD1 ASN A 301     1491   1601   1410     46    -34    294       O  
ATOM   2001  ND2 ASN A 301      23.075   6.396  16.413  1.00 11.13           N  
ANISOU 2001  ND2 ASN A 301     1404   1403   1419     94    194    341       N  
ATOM   2002  N   VAL A 302      23.537  10.932  13.878  1.00  8.78           N  
ANISOU 2002  N   VAL A 302     1128   1019   1189    -77    281     34       N  
ATOM   2003  CA  VAL A 302      24.481  11.024  12.775  1.00  9.58           C  
ANISOU 2003  CA  VAL A 302     1207   1099   1330    -85    261     44       C  
ATOM   2004  C   VAL A 302      25.357  12.247  12.994  1.00  8.39           C  
ANISOU 2004  C   VAL A 302     1068    932   1185   -110    264     90       C  
ATOM   2005  O   VAL A 302      24.862  13.374  13.199  1.00  9.60           O  
ANISOU 2005  O   VAL A 302     1085    920   1643    -99    364     94       O  
ATOM   2006  CB  VAL A 302      23.778  11.098  11.420  1.00 10.12           C  
ANISOU 2006  CB  VAL A 302     1218   1189   1436   -351    296     27       C  
ATOM   2007  CG1 VAL A 302      22.907  12.263  11.285  1.00 16.11           C  
ANISOU 2007  CG1 VAL A 302     1962   2211   1947    -70    180     23       C  
ATOM   2008  CG2 VAL A 302      24.795  11.046  10.295  1.00 11.28           C  
ANISOU 2008  CG2 VAL A 302     1498   1377   1409   -256    300    -11       C  
ATOM   2009  N   SER A 303      26.668  12.049  12.975  1.00  8.16           N  
ANISOU 2009  N   SER A 303     1027    877   1194    -11    209     87       N  
ATOM   2010  CA  SER A 303      27.566  13.173  13.179  1.00  7.82           C  
ANISOU 2010  CA  SER A 303     1009    900   1062     -1    135     75       C  
ATOM   2011  C   SER A 303      27.408  14.210  12.060  1.00  6.73           C  
ANISOU 2011  C   SER A 303      829    814    914    -11    149     37       C  
ATOM   2012  O   SER A 303      27.357  13.875  10.881  1.00  7.09           O  
ANISOU 2012  O   SER A 303      929    837    926    -70    244    -79       O  
ATOM   2013  CB  SER A 303      29.006  12.687  13.260  1.00  9.01           C  
ANISOU 2013  CB  SER A 303     1086   1075   1262     30     36    165       C  
ATOM   2014  OG  SER A 303      29.881  13.779  13.215  1.00 10.60           O  
ANISOU 2014  OG  SER A 303     1138   1203   1686    -43   -114    141       O  
ATOM   2015  N   THR A 304      27.349  15.471  12.457  1.00  6.52           N  
ANISOU 2015  N   THR A 304      812    734    930    -28    104     -4       N  
ATOM   2016  CA  THR A 304      27.143  16.556  11.494  1.00  7.00           C  
ANISOU 2016  CA  THR A 304      764    771   1124    -11    110     65       C  
ATOM   2017  C   THR A 304      28.367  17.437  11.337  1.00  5.94           C  
ANISOU 2017  C   THR A 304      716    681    859    -46     54     69       C  
ATOM   2018  O   THR A 304      28.245  18.641  11.132  1.00  6.73           O  
ANISOU 2018  O   THR A 304      734    685   1136     45     32      4       O  
ATOM   2019  CB  THR A 304      25.940  17.380  11.818  1.00  9.22           C  
ANISOU 2019  CB  THR A 304      943   1038   1519     -2    255     62       C  
ATOM   2020  OG1 THR A 304      26.086  17.865  13.140  1.00 11.87           O  
ANISOU 2020  OG1 THR A 304      974   1315   2218   -180    748   -234       O  
ATOM   2021  CG2 THR A 304      24.658  16.565  11.778  1.00 11.20           C  
ANISOU 2021  CG2 THR A 304     1056   1230   1968     61     95     73       C  
ATOM   2022  N   ILE A 305      29.539  16.822  11.373  1.00  5.67           N  
ANISOU 2022  N   ILE A 305      685    618    851     55    101     28       N  
ATOM   2023  CA  ILE A 305      30.775  17.524  11.063  1.00  5.33           C  
ANISOU 2023  CA  ILE A 305      725    570    731     26    115     60       C  
ATOM   2024  C   ILE A 305      31.656  16.609  10.238  1.00  5.43           C  
ANISOU 2024  C   ILE A 305      726    558    778     12     68     34       C  
ATOM   2025  O   ILE A 305      31.798  15.420  10.545  1.00  5.98           O  
ANISOU 2025  O   ILE A 305      929    568    772     78    211    -23       O  
ATOM   2026  CB  ILE A 305      31.451  18.050  12.354  1.00  5.68           C  
ANISOU 2026  CB  ILE A 305      762    605    791      5    160     -7       C  
ATOM   2027  CG1 ILE A 305      32.569  19.040  12.052  1.00  5.86           C  
ANISOU 2027  CG1 ILE A 305      700    738    788     61     89    -92       C  
ATOM   2028  CG2 ILE A 305      31.916  16.920  13.274  1.00  6.65           C  
ANISOU 2028  CG2 ILE A 305      823    802    901    -17    150     68       C  
ATOM   2029  CD1 ILE A 305      32.917  19.887  13.254  1.00  7.12           C  
ANISOU 2029  CD1 ILE A 305      879    875    951   -151    206    -76       C  
ATOM   2030  N   ILE A 306      32.219  17.161   9.169  1.00  5.17           N  
ANISOU 2030  N   ILE A 306      626    620    716     84     66     60       N  
ATOM   2031  CA  ILE A 306      33.111  16.423   8.276  1.00  5.81           C  
ANISOU 2031  CA  ILE A 306      751    749    705    -60     23   -127       C  
ATOM   2032  C   ILE A 306      34.209  17.376   7.816  1.00  5.02           C  
ANISOU 2032  C   ILE A 306      630    584    692     30     32   -108       C  
ATOM   2033  O   ILE A 306      34.140  18.584   8.040  1.00  5.64           O  
ANISOU 2033  O   ILE A 306      681    595    865     31    136   -101       O  
ATOM   2034  CB  ILE A 306      32.398  15.812   7.056  1.00  7.65           C  
ANISOU 2034  CB  ILE A 306      925   1139    841   -140     76    -55       C  
ATOM   2035  CG1 ILE A 306      31.693  16.886   6.281  1.00  9.32           C  
ANISOU 2035  CG1 ILE A 306     1033   1166   1339    -97    149   -209       C  
ATOM   2036  CG2 ILE A 306      31.446  14.687   7.431  1.00  9.83           C  
ANISOU 2036  CG2 ILE A 306     1238   1345   1149   -142    -59   -171       C  
ATOM   2037  CD1 ILE A 306      31.159  16.426   4.941  1.00 11.43           C  
ANISOU 2037  CD1 ILE A 306     1436   1496   1412     99   -115    -75       C  
ATOM   2038  N   LYS A 307      35.231  16.835   7.169  1.00  5.32           N  
ANISOU 2038  N   LYS A 307      666    593    761     25    185    -87       N  
ATOM   2039  CA  LYS A 307      36.295  17.661   6.612  1.00  5.83           C  
ANISOU 2039  CA  LYS A 307      783    655    777     -5    174    -50       C  
ATOM   2040  C   LYS A 307      36.569  17.255   5.173  1.00  5.53           C  
ANISOU 2040  C   LYS A 307      761    546    794     59    200    -95       C  
ATOM   2041  O   LYS A 307      36.283  16.131   4.755  1.00  6.58           O  
ANISOU 2041  O   LYS A 307      974    660    866    -56    297   -190       O  
ATOM   2042  CB  LYS A 307      37.584  17.519   7.428  1.00  6.65           C  
ANISOU 2042  CB  LYS A 307      845    799    881    -95    113   -139       C  
ATOM   2043  CG  LYS A 307      38.237  16.162   7.232  1.00  7.79           C  
ANISOU 2043  CG  LYS A 307      971    909   1080      9     68   -157       C  
ATOM   2044  CD  LYS A 307      39.383  15.905   8.181  1.00  8.29           C  
ANISOU 2044  CD  LYS A 307     1108    875   1166     95     28   -331       C  
ATOM   2045  CE  LYS A 307      39.971  14.529   7.957  1.00  8.40           C  
ANISOU 2045  CE  LYS A 307      951   1046   1195    139     70   -429       C  
ATOM   2046  NZ  LYS A 307      40.613  14.028   9.188  1.00  9.13           N  
ANISOU 2046  NZ  LYS A 307     1192   1128   1145     35    -98   -387       N  
ATOM   2047  N   LEU A 308      37.139  18.196   4.427  1.00  5.82           N  
ANISOU 2047  N   LEU A 308      851    586    774    -55    214   -182       N  
ATOM   2048  CA  LEU A 308      37.752  17.954   3.130  1.00  6.00           C  
ANISOU 2048  CA  LEU A 308      874    673    732      0    205   -191       C  
ATOM   2049  C   LEU A 308      39.129  18.587   3.165  1.00  6.06           C  
ANISOU 2049  C   LEU A 308      831    656    814    -45    152   -165       C  
ATOM   2050  O   LEU A 308      39.283  19.699   3.664  1.00  7.15           O  
ANISOU 2050  O   LEU A 308      912    616   1187    -86    271   -268       O  
ATOM   2051  CB  LEU A 308      36.969  18.622   2.011  1.00  7.02           C  
ANISOU 2051  CB  LEU A 308     1012    734    921    -10    178   -226       C  
ATOM   2052  CG  LEU A 308      35.516  18.234   1.803  1.00  7.68           C  
ANISOU 2052  CG  LEU A 308      919    958   1041     41     82   -168       C  
ATOM   2053  CD1 LEU A 308      34.886  19.114   0.754  1.00  9.04           C  
ANISOU 2053  CD1 LEU A 308     1067   1035   1329    202     20   -152       C  
ATOM   2054  CD2 LEU A 308      35.368  16.778   1.413  1.00  8.18           C  
ANISOU 2054  CD2 LEU A 308      845   1030   1232    -27     26   -127       C  
ATOM   2055  N   ARG A 309      40.132  17.898   2.636  1.00  5.98           N  
ANISOU 2055  N   ARG A 309      807    696    765    -60    151   -174       N  
ATOM   2056  CA  ARG A 309      41.481  18.443   2.547  1.00  6.61           C  
ANISOU 2056  CA  ARG A 309      873    827    810    -83     94   -216       C  
ATOM   2057  C   ARG A 309      41.906  18.560   1.114  1.00  7.19           C  
ANISOU 2057  C   ARG A 309      957    889    885   -181    131   -220       C  
ATOM   2058  O   ARG A 309      41.480  17.790   0.243  1.00  8.20           O  
ANISOU 2058  O   ARG A 309     1059   1144    911   -337    222   -407       O  
ATOM   2059  CB  ARG A 309      42.493  17.607   3.309  1.00  7.76           C  
ANISOU 2059  CB  ARG A 309      907    993   1048    -61    124   -192       C  
ATOM   2060  CG  ARG A 309      42.378  17.774   4.797  1.00  8.42           C  
ANISOU 2060  CG  ARG A 309     1038   1090   1070     20    -26   -150       C  
ATOM   2061  CD  ARG A 309      43.117  16.728   5.552  1.00 11.67           C  
ANISOU 2061  CD  ARG A 309     1737   1481   1213    158      1   -330       C  
ATOM   2062  NE  ARG A 309      43.581  17.189   6.854  1.00 10.69           N  
ANISOU 2062  NE  ARG A 309     1510   1323   1226     80     55    -77       N  
ATOM   2063  CZ  ARG A 309      43.845  16.373   7.856  1.00  9.43           C  
ANISOU 2063  CZ  ARG A 309     1289   1012   1281    184    135    -89       C  
ATOM   2064  NH1 ARG A 309      43.625  15.061   7.751  1.00 11.12           N  
ANISOU 2064  NH1 ARG A 309     1469   1252   1502    -18    175   -165       N  
ATOM   2065  NH2 ARG A 309      44.341  16.863   8.970  1.00  9.97           N  
ANISOU 2065  NH2 ARG A 309     1390   1106   1289     22     78    -97       N  
ATOM   2066  N   CYS A 310      42.770  19.524   0.828  1.00  7.77           N  
ANISOU 2066  N   CYS A 310      903   1046   1003   -195    144   -203       N  
ATOM   2067  CA  CYS A 310      43.314  19.567  -0.523  1.00  8.99           C  
ANISOU 2067  CA  CYS A 310     1041   1195   1178   -147    222   -124       C  
ATOM   2068  C   CYS A 310      44.339  18.455  -0.711  1.00  9.35           C  
ANISOU 2068  C   CYS A 310     1097   1235   1218   -106    213   -139       C  
ATOM   2069  O   CYS A 310      45.044  18.057   0.208  1.00  9.61           O  
ANISOU 2069  O   CYS A 310     1144   1295   1212     32    415   -268       O  
ATOM   2070  CB  CYS A 310      43.857  20.929  -0.918  1.00 10.03           C  
ANISOU 2070  CB  CYS A 310     1125   1254   1431   -148    349    -75       C  
ATOM   2071  SG  CYS A 310      45.369  21.434  -0.112  1.00 11.95           S  
ANISOU 2071  SG  CYS A 310     1529   1428   1582   -198    264   -290       S  
ATOM   2072  N   SER A 311      44.400  17.953  -1.933  1.00 10.32           N  
ANISOU 2072  N   SER A 311     1274   1380   1266   -102    143   -204       N  
ATOM   2073  CA  SER A 311      45.300  16.868  -2.266  1.00 11.85           C  
ANISOU 2073  CA  SER A 311     1534   1567   1400     13     76   -245       C  
ATOM   2074  C   SER A 311      46.750  17.269  -2.058  1.00 11.66           C  
ANISOU 2074  C   SER A 311     1530   1565   1334     77    145   -320       C  
ATOM   2075  O   SER A 311      47.546  16.462  -1.609  1.00 12.98           O  
ANISOU 2075  O   SER A 311     1654   1729   1545    183    139   -502       O  
ATOM   2076  CB  SER A 311      45.065  16.404  -3.709  1.00 12.27           C  
ANISOU 2076  CB  SER A 311     1654   1588   1418    -59     50   -297       C  
ATOM   2077  OG  SER A 311      45.466  17.394  -4.643  1.00 16.04           O  
ANISOU 2077  OG  SER A 311     2340   2212   1541     45     62   -368       O  
ATOM   2078  N   SER A 312      47.073  18.521  -2.352  1.00 12.23           N  
ANISOU 2078  N   SER A 312     1457   1748   1441     49    187   -243       N  
ATOM   2079  CA  SER A 312      48.435  19.024  -2.196  1.00 13.57           C  
ANISOU 2079  CA  SER A 312     1621   1845   1688     -5    111   -191       C  
ATOM   2080  C   SER A 312      48.900  18.887  -0.744  1.00 12.78           C  
ANISOU 2080  C   SER A 312     1442   1772   1641     25     93   -280       C  
ATOM   2081  O   SER A 312      50.044  18.513  -0.483  1.00 14.18           O  
ANISOU 2081  O   SER A 312     1457   2023   1905     27     23   -469       O  
ATOM   2082  CB  SER A 312      48.512  20.482  -2.665  1.00 14.03           C  
ANISOU 2082  CB  SER A 312     1693   1921   1714   -106    112   -114       C  
ATOM   2083  OG  SER A 312      48.261  20.581  -4.059  1.00 18.53           O  
ANISOU 2083  OG  SER A 312     2285   2419   2337   -165    154    -13       O  
ATOM   2084  N   PHE A 313      48.006  19.197   0.198  1.00 12.15           N  
ANISOU 2084  N   PHE A 313     1458   1664   1491     22     62   -372       N  
ATOM   2085  CA  PHE A 313      48.311  19.067   1.617  1.00 12.15           C  
ANISOU 2085  CA  PHE A 313     1537   1541   1537     65     -4   -271       C  
ATOM   2086  C   PHE A 313      48.464  17.610   2.025  1.00 12.90           C  
ANISOU 2086  C   PHE A 313     1628   1645   1626    176    -14   -278       C  
ATOM   2087  O   PHE A 313      49.384  17.264   2.757  1.00 13.39           O  
ANISOU 2087  O   PHE A 313     1850   1563   1672    439    -47   -429       O  
ATOM   2088  CB  PHE A 313      47.228  19.736   2.465  1.00 11.67           C  
ANISOU 2088  CB  PHE A 313     1508   1444   1479    160    -43   -327       C  
ATOM   2089  CG  PHE A 313      47.461  19.608   3.946  1.00 11.86           C  
ANISOU 2089  CG  PHE A 313     1459   1552   1494    251   -178   -303       C  
ATOM   2090  CD1 PHE A 313      48.280  20.508   4.614  1.00 13.24           C  
ANISOU 2090  CD1 PHE A 313     2056   1296   1678    299   -307   -354       C  
ATOM   2091  CD2 PHE A 313      46.865  18.594   4.661  1.00 12.34           C  
ANISOU 2091  CD2 PHE A 313     1542   1726   1421    341   -149   -342       C  
ATOM   2092  CE1 PHE A 313      48.513  20.373   5.976  1.00 14.12           C  
ANISOU 2092  CE1 PHE A 313     2008   1601   1756    194   -358   -421       C  
ATOM   2093  CE2 PHE A 313      47.089  18.456   6.020  1.00 13.24           C  
ANISOU 2093  CE2 PHE A 313     1587   1752   1689    305    -50   -142       C  
ATOM   2094  CZ  PHE A 313      47.902  19.359   6.681  1.00 14.42           C  
ANISOU 2094  CZ  PHE A 313     1947   1899   1633    341   -207   -233       C  
HETATM 2095  N   MSE A 314      47.546  16.767   1.565  1.00 14.30           N  
ANISOU 2095  N   MSE A 314     1894   1740   1797     96      7   -207       N  
HETATM 2096  CA  MSE A 314      47.574  15.344   1.906  1.00 17.04           C  
ANISOU 2096  CA  MSE A 314     2258   2058   2159     98     -1   -125       C  
HETATM 2097  C   MSE A 314      48.876  14.697   1.427  1.00 18.17           C  
ANISOU 2097  C   MSE A 314     2373   2169   2361    104    -47   -110       C  
HETATM 2098  O   MSE A 314      49.415  13.826   2.101  1.00 19.59           O  
ANISOU 2098  O   MSE A 314     2667   2301   2474    258   -150   -133       O  
HETATM 2099  CB  MSE A 314      46.334  14.601   1.354  1.00 17.98           C  
ANISOU 2099  CB  MSE A 314     2364   2138   2328     63     -1   -119       C  
HETATM 2100  CG  MSE A 314      44.962  15.138   1.866  1.00 22.32           C  
ANISOU 2100  CG  MSE A 314     2829   2681   2968    -53     59   -131       C  
HETATM 2101 SE  AMSE A 314      43.366  14.034   1.742  0.50 25.64          SE  
ANISOU 2101 SE  AMSE A 314     3149   3024   3566   -111     -2   -185      SE  
HETATM 2102 SE  BMSE A 314      45.570  14.850   3.710  0.50 33.86          SE  
ANISOU 2102 SE  BMSE A 314     4508   4213   4142     76    207     61      SE  
HETATM 2103  CE AMSE A 314      42.742  14.682   0.005  0.50 26.97           C  
ANISOU 2103  CE AMSE A 314     3350   3394   3502     39    -10    -76       C  
HETATM 2104  CE BMSE A 314      41.560  14.056   2.331  0.50 28.88           C  
ANISOU 2104  CE BMSE A 314     3632   3690   3651    -21    182     17       C  
ATOM   2105  N   GLU A 315      49.404  15.167   0.301  1.00 18.78           N  
ANISOU 2105  N   GLU A 315     2448   2252   2436    158    -31   -141       N  
ATOM   2106  CA  GLU A 315      50.629  14.623  -0.282  1.00 20.66           C  
ANISOU 2106  CA  GLU A 315     2599   2570   2680     92      4    -82       C  
ATOM   2107  C   GLU A 315      51.880  14.980   0.523  1.00 21.30           C  
ANISOU 2107  C   GLU A 315     2641   2658   2791    116      0   -120       C  
ATOM   2108  O   GLU A 315      52.905  14.318   0.386  1.00 22.18           O  
ANISOU 2108  O   GLU A 315     2650   2752   3024    272    -17   -127       O  
ATOM   2109  CB  GLU A 315      50.796  15.124  -1.715  1.00 20.60           C  
ANISOU 2109  CB  GLU A 315     2568   2588   2668    105     40   -100       C  
ATOM   2110  CG  GLU A 315      49.827  14.509  -2.714  1.00 23.14           C  
ANISOU 2110  CG  GLU A 315     2931   2910   2949     75     70    -65       C  
ATOM   2111  CD  GLU A 315      49.696  15.322  -3.992  1.00 26.97           C  
ANISOU 2111  CD  GLU A 315     3414   3437   3396     -7     85    -55       C  
ATOM   2112  OE1 GLU A 315      50.562  16.189  -4.251  1.00 29.88           O  
ANISOU 2112  OE1 GLU A 315     3859   3805   3686   -148    165     34       O  
ATOM   2113  OE2 GLU A 315      48.725  15.094  -4.744  1.00 30.02           O  
ANISOU 2113  OE2 GLU A 315     3830   3943   3633     49    127    -90       O  
ATOM   2114  N   LEU A 316      51.812  16.028   1.343  1.00 22.13           N  
ANISOU 2114  N   LEU A 316     2742   2802   2864     86    -37    -89       N  
ATOM   2115  CA  LEU A 316      52.936  16.402   2.205  1.00 22.92           C  
ANISOU 2115  CA  LEU A 316     2860   2897   2949     24    -21    -58       C  
ATOM   2116  C   LEU A 316      53.189  15.335   3.270  1.00 23.60           C  
ANISOU 2116  C   LEU A 316     2931   2973   3061      2    -20    -27       C  
ATOM   2117  O   LEU A 316      52.284  14.591   3.657  1.00 25.02           O  
ANISOU 2117  O   LEU A 316     3079   3150   3274     18    -30    -14       O  
ATOM   2118  CB  LEU A 316      52.680  17.749   2.881  1.00 22.93           C  
ANISOU 2118  CB  LEU A 316     2861   2935   2916     -1    -53    -90       C  
ATOM   2119  CG  LEU A 316      52.494  18.953   1.961  1.00 22.56           C  
ANISOU 2119  CG  LEU A 316     2833   2867   2872      3     17   -110       C  
ATOM   2120  CD1 LEU A 316      52.050  20.171   2.774  1.00 22.84           C  
ANISOU 2120  CD1 LEU A 316     2924   2957   2797    -30    -80   -139       C  
ATOM   2121  CD2 LEU A 316      53.762  19.249   1.167  1.00 22.88           C  
ANISOU 2121  CD2 LEU A 316     2901   2938   2854     28     11   -101       C  
TER    2122      LEU A 316                                                      
HETATM 2123 MG    MG A 502      45.408  19.600  12.379  1.00  5.17          MG  
ANISOU 2123 MG    MG A 502      683    555    724     49     -8    -33      MG  
HETATM 2124  PG  ATP A 501      46.034  17.442  14.649  1.00  8.07           P  
ANISOU 2124  PG  ATP A 501     1049    858   1156    103   -185     10       P  
HETATM 2125  O1G ATP A 501      46.554  18.251  13.486  1.00  6.46           O  
ANISOU 2125  O1G ATP A 501      841    780    833    141    -77    -20       O  
HETATM 2126  O2G ATP A 501      47.012  16.440  15.214  1.00  9.86           O  
ANISOU 2126  O2G ATP A 501     1237    949   1559    287   -271    142       O  
HETATM 2127  O3G ATP A 501      45.415  18.289  15.759  1.00  9.14           O  
ANISOU 2127  O3G ATP A 501     1443    976   1050    128     34    -44       O  
HETATM 2128  PB  ATP A 501      44.166  16.669  12.640  1.00  6.53           P  
ANISOU 2128  PB  ATP A 501      865    579   1035     51    -49    -22       P  
HETATM 2129  O1B ATP A 501      44.846  15.767  11.696  1.00  8.60           O  
ANISOU 2129  O1B ATP A 501     1217    670   1381    142    -44   -222       O  
HETATM 2130  O2B ATP A 501      44.015  18.092  12.214  1.00  5.78           O  
ANISOU 2130  O2B ATP A 501      796    521    879     44    -67    -30       O  
HETATM 2131  O3B ATP A 501      44.807  16.562  14.092  1.00  7.50           O  
ANISOU 2131  O3B ATP A 501     1215    778    855      0   -149    143       O  
HETATM 2132  PA  ATP A 501      41.441  16.004  12.024  1.00  6.54           P  
ANISOU 2132  PA  ATP A 501      979    589    915    -10   -107   -103       P  
HETATM 2133  O1A ATP A 501      41.868  15.977  10.607  1.00  8.18           O  
ANISOU 2133  O1A ATP A 501     1081   1121    905   -142   -154   -199       O  
HETATM 2134  O2A ATP A 501      40.573  14.911  12.597  1.00  7.34           O  
ANISOU 2134  O2A ATP A 501     1001    528   1259    -15    -22    -31       O  
HETATM 2135  O3A ATP A 501      42.720  16.073  13.004  1.00  6.94           O  
ANISOU 2135  O3A ATP A 501     1019    658    958    -43    -81     52       O  
HETATM 2136  O5' ATP A 501      40.761  17.421  12.230  1.00  6.65           O  
ANISOU 2136  O5' ATP A 501     1078    581    868     88   -113    -12       O  
HETATM 2137  C5' ATP A 501      40.228  17.831  13.474  1.00  6.42           C  
ANISOU 2137  C5' ATP A 501      807    712    917    -12    -29      5       C  
HETATM 2138  C4' ATP A 501      41.034  18.978  14.030  1.00  5.20           C  
ANISOU 2138  C4' ATP A 501      744    524    707    -14     70    -29       C  
HETATM 2139  O4' ATP A 501      41.042  20.083  13.138  1.00  4.96           O  
ANISOU 2139  O4' ATP A 501      755    401    727     56     46    -22       O  
HETATM 2140  C3' ATP A 501      40.382  19.568  15.268  1.00  5.52           C  
ANISOU 2140  C3' ATP A 501      830    602    665     66    100     63       C  
HETATM 2141  O3' ATP A 501      40.575  18.803  16.426  1.00  7.48           O  
ANISOU 2141  O3' ATP A 501     1253    818    768    122    105     91       O  
HETATM 2142  C2' ATP A 501      40.973  20.967  15.342  1.00  4.80           C  
ANISOU 2142  C2' ATP A 501      653    589    581    121     53    -44       C  
HETATM 2143  O2' ATP A 501      42.117  20.993  16.172  1.00  6.19           O  
ANISOU 2143  O2' ATP A 501      800    944    608     84    -83     32       O  
HETATM 2144  C1' ATP A 501      41.343  21.265  13.892  1.00  4.22           C  
ANISOU 2144  C1' ATP A 501      601    442    560     93     58    -77       C  
HETATM 2145  N9  ATP A 501      40.602  22.354  13.240  1.00  3.78           N  
ANISOU 2145  N9  ATP A 501      361    535    537     67     30     -5       N  
HETATM 2146  C8  ATP A 501      41.171  23.310  12.442  1.00  4.18           C  
ANISOU 2146  C8  ATP A 501      562    558    468    -99     72     -5       C  
HETATM 2147  N7  ATP A 501      40.249  24.145  11.942  1.00  4.47           N  
ANISOU 2147  N7  ATP A 501      576    605    515    -10     48     -5       N  
HETATM 2148  C5  ATP A 501      39.058  23.679  12.418  1.00  3.65           C  
ANISOU 2148  C5  ATP A 501      505    444    435     33     55    -43       C  
HETATM 2149  C6  ATP A 501      37.744  24.121  12.264  1.00  4.22           C  
ANISOU 2149  C6  ATP A 501      607    350    644    120     -7      1       C  
HETATM 2150  N6  ATP A 501      37.382  25.103  11.430  1.00  5.27           N  
ANISOU 2150  N6  ATP A 501      745    524    732    137     -9    -94       N  
HETATM 2151  N1  ATP A 501      36.760  23.458  12.935  1.00  4.95           N  
ANISOU 2151  N1  ATP A 501      520    746    613    -63    110   -121       N  
HETATM 2152  C2  ATP A 501      37.057  22.401  13.740  1.00  4.70           C  
ANISOU 2152  C2  ATP A 501      624    581    579    -41    -22      1       C  
HETATM 2153  N3  ATP A 501      38.297  21.903  13.909  1.00  4.79           N  
ANISOU 2153  N3  ATP A 501      667    555    596    -55     83    -64       N  
HETATM 2154  C4  ATP A 501      39.267  22.569  13.244  1.00  3.29           C  
ANISOU 2154  C4  ATP A 501      514    379    354    -22     56    -29       C  
HETATM 2155  O   HOH A 503      44.809  17.970  37.617  1.00 36.08           O  
ANISOU 2155  O   HOH A 503     4386   5537   3785   -520   -992  -1082       O  
HETATM 2156  O   HOH A 504      42.954  19.170  36.304  1.00 24.50           O  
ANISOU 2156  O   HOH A 504     2833   3518   2958     -2   -622  -1395       O  
HETATM 2157  O   HOH A 505      40.660  20.162  36.149  1.00 27.10           O  
ANISOU 2157  O   HOH A 505     3805   1890   4602   -257     16    196       O  
HETATM 2158  O   HOH A 506      44.237  20.691  37.847  1.00 31.69           O  
ANISOU 2158  O   HOH A 506     3809   4155   4075    198   -499    958       O  
HETATM 2159  O   HOH A 507      17.460   9.609   1.448  1.00 34.71           O  
ANISOU 2159  O   HOH A 507     4608   4863   3714   -192   -175   -460       O  
HETATM 2160  O   HOH A 508      33.710  21.548  35.755  1.00 34.55           O  
ANISOU 2160  O   HOH A 508     5177   5332   2618    160   -225    101       O  
HETATM 2161  O   HOH A 509      58.096  33.599  10.856  1.00 10.13           O  
ANISOU 2161  O   HOH A 509     1082   1042   1723   -139   -196    -17       O  
HETATM 2162  O   HOH A 510      55.267  27.929  14.039  1.00  7.63           O  
ANISOU 2162  O   HOH A 510      953    759   1183    -28     38    198       O  
HETATM 2163  O   HOH A 511      41.922  35.290  18.063  1.00  6.88           O  
ANISOU 2163  O   HOH A 511      938    678    996    199    -67    -96       O  
HETATM 2164  O   HOH A 512      58.073  34.302  13.567  1.00  8.10           O  
ANISOU 2164  O   HOH A 512      801    973   1303    -96     11    107       O  
HETATM 2165  O   HOH A 513      50.287  27.048  12.279  1.00  8.03           O  
ANISOU 2165  O   HOH A 513      825    826   1398    -48    156   -300       O  
HETATM 2166  O   HOH A 514      46.968  20.960  12.454  1.00  5.94           O  
ANISOU 2166  O   HOH A 514      726    663    867      7     40    -61       O  
HETATM 2167  O   HOH A 515      35.931  20.580  24.045  1.00 12.46           O  
ANISOU 2167  O   HOH A 515     1207   1404   2122    -92   -279    833       O  
HETATM 2168  O   HOH A 516      27.187  24.141  16.304  1.00  7.65           O  
ANISOU 2168  O   HOH A 516      820   1054   1031    138    -44   -167       O  
HETATM 2169  O   HOH A 517      39.455  21.182  24.948  1.00  8.14           O  
ANISOU 2169  O   HOH A 517     1202   1000    890    211     40    119       O  
HETATM 2170  O   HOH A 518      53.280  36.276  18.496  1.00  7.92           O  
ANISOU 2170  O   HOH A 518     1150    917    940   -141   -136   -144       O  
HETATM 2171  O   HOH A 519      61.158  36.077  18.867  1.00  8.92           O  
ANISOU 2171  O   HOH A 519     1027   1075   1285   -151   -112    101       O  
HETATM 2172  O   HOH A 520      46.186  19.099  10.482  1.00  6.57           O  
ANISOU 2172  O   HOH A 520      850    760    883     81    101   -233       O  
HETATM 2173  O   HOH A 521      30.077  26.561  18.558  1.00  6.94           O  
ANISOU 2173  O   HOH A 521      729    873   1032     20     12     -4       O  
HETATM 2174  O   HOH A 522      33.420  13.556  11.668  1.00  7.95           O  
ANISOU 2174  O   HOH A 522      935    884   1199    134      3     34       O  
HETATM 2175  O   HOH A 523      27.466  24.688  13.601  1.00  7.89           O  
ANISOU 2175  O   HOH A 523      897    962   1136    112   -110   -166       O  
HETATM 2176  O   HOH A 524      57.172  45.969   2.224  1.00 14.78           O  
ANISOU 2176  O   HOH A 524     1595   1560   2460   -463    604    -55       O  
HETATM 2177  O   HOH A 525      52.082  29.977   9.907  1.00  6.93           O  
ANISOU 2177  O   HOH A 525      738   1150    742    -23     52    135       O  
HETATM 2178  O   HOH A 526      35.850  39.285  16.890  1.00  8.23           O  
ANISOU 2178  O   HOH A 526     1316    712   1095    172    -99    -30       O  
HETATM 2179  O   HOH A 527      58.622  31.792  14.517  1.00  7.79           O  
ANISOU 2179  O   HOH A 527      810   1088   1061   -137    -34    161       O  
HETATM 2180  O   HOH A 528      44.239  21.032  11.319  1.00  5.59           O  
ANISOU 2180  O   HOH A 528      709    588    824    106     79      4       O  
HETATM 2181  O   HOH A 529      23.047  28.449  13.575  1.00  9.59           O  
ANISOU 2181  O   HOH A 529      883   1043   1717    141     79   -216       O  
HETATM 2182  O   HOH A 530      44.639  20.395  14.092  1.00  5.86           O  
ANISOU 2182  O   HOH A 530      773    642    811     34     34    -69       O  
HETATM 2183  O   HOH A 531      57.423  40.860  16.055  1.00 12.10           O  
ANISOU 2183  O   HOH A 531     1638   1146   1813   -146    -51    -64       O  
HETATM 2184  O   HOH A 532      42.580  35.536  20.672  1.00  9.97           O  
ANISOU 2184  O   HOH A 532     1367   1589    833    600   -127   -187       O  
HETATM 2185  O   HOH A 533      41.861  14.510  23.280  1.00 10.06           O  
ANISOU 2185  O   HOH A 533     1393    924   1505    -87   -127    207       O  
HETATM 2186  O   HOH A 534      58.410  35.573   9.030  1.00 12.96           O  
ANISOU 2186  O   HOH A 534     2520   1235   1168   -389   -198    159       O  
HETATM 2187  O   HOH A 535      37.675  41.407  29.946  1.00  9.02           O  
ANISOU 2187  O   HOH A 535     1505    931    989    160   -126   -352       O  
HETATM 2188  O   HOH A 536      46.386  19.244  17.947  1.00  9.72           O  
ANISOU 2188  O   HOH A 536     1343    994   1355    324   -192   -326       O  
HETATM 2189  O   HOH A 537      33.957  24.389  22.521  1.00  9.05           O  
ANISOU 2189  O   HOH A 537     1055   1466    915     47    199    108       O  
HETATM 2190  O   HOH A 538      51.195  26.221  30.174  1.00 11.66           O  
ANISOU 2190  O   HOH A 538     2295   1123   1011    478   -380    181       O  
HETATM 2191  O   HOH A 539      36.665  41.930  17.362  1.00 10.20           O  
ANISOU 2191  O   HOH A 539     1563    923   1389    156   -358    -93       O  
HETATM 2192  O   HOH A 540      32.690  24.707   9.752  1.00 11.68           O  
ANISOU 2192  O   HOH A 540     2163    957   1317    146    643     -4       O  
HETATM 2193  O   HOH A 541      46.038  26.111  32.387  1.00 11.65           O  
ANISOU 2193  O   HOH A 541     2200   1246    977    631   -426   -152       O  
HETATM 2194  O   HOH A 542      50.835  38.785  10.605  1.00 12.82           O  
ANISOU 2194  O   HOH A 542     1363   1021   2485   -104   -227    655       O  
HETATM 2195  O   HOH A 543      47.253  20.607  20.998  1.00  7.41           O  
ANISOU 2195  O   HOH A 543     1112    846    856    286     47     69       O  
HETATM 2196  O   HOH A 544      30.225  18.438  24.882  1.00 19.29           O  
ANISOU 2196  O   HOH A 544     1980   2601   2748   -454    173    -19       O  
HETATM 2197  O   HOH A 545      36.676  30.186   7.840  1.00  7.92           O  
ANISOU 2197  O   HOH A 545     1054    730   1222    199     37   -161       O  
HETATM 2198  O   HOH A 546      54.547  28.621  26.010  1.00 15.77           O  
ANISOU 2198  O   HOH A 546     3622    966   1403   -336  -1290      0       O  
HETATM 2199  O   HOH A 547      23.626  23.992  18.610  1.00 16.59           O  
ANISOU 2199  O   HOH A 547     1590   1857   2854   -231    342  -1086       O  
HETATM 2200  O   HOH A 548      24.281  21.253  22.644  1.00 16.66           O  
ANISOU 2200  O   HOH A 548     2164   2535   1631  -1018    278   -129       O  
HETATM 2201  O   HOH A 549      41.100  32.482  -0.400  1.00 18.61           O  
ANISOU 2201  O   HOH A 549     2198   2334   2538    281   -632    745       O  
HETATM 2202  O   HOH A 550      61.194  35.875   6.823  1.00 18.15           O  
ANISOU 2202  O   HOH A 550     2126   2545   2223    568    135    331       O  
HETATM 2203  O   HOH A 551      47.247  31.935   0.640  1.00  8.72           O  
ANISOU 2203  O   HOH A 551     1243    955   1113   -130    180    167       O  
HETATM 2204  O   HOH A 552      54.972  40.671  12.879  1.00 13.50           O  
ANISOU 2204  O   HOH A 552     1909   1159   2060   -135    147    268       O  
HETATM 2205  O   HOH A 553      41.617  37.400   3.258  1.00 19.94           O  
ANISOU 2205  O   HOH A 553     2042   1800   3734   -157   -895    900       O  
HETATM 2206  O   HOH A 554      32.150  10.566   7.405  1.00 10.95           O  
ANISOU 2206  O   HOH A 554     1188   1779   1193   -186     88   -173       O  
HETATM 2207  O   HOH A 555      22.644  18.077   0.346  1.00 11.45           O  
ANISOU 2207  O   HOH A 555     1230   1717   1402   -234   -124   -349       O  
HETATM 2208  O   HOH A 556      34.011  19.700  22.549  1.00 13.80           O  
ANISOU 2208  O   HOH A 556     1514   1855   1872    290     52    342       O  
HETATM 2209  O   HOH A 557      32.974  22.004  21.336  1.00 13.88           O  
ANISOU 2209  O   HOH A 557     1691   1889   1693    262     53     94       O  
HETATM 2210  O   HOH A 558      22.426  13.567  14.354  1.00 14.62           O  
ANISOU 2210  O   HOH A 558     1608   1172   2773     58   1171     94       O  
HETATM 2211  O   HOH A 559      57.043  40.605  11.123  1.00 13.42           O  
ANISOU 2211  O   HOH A 559     1666   1380   2051   -368    152   -130       O  
HETATM 2212  O   HOH A 560      22.846  26.497  21.560  1.00 14.76           O  
ANISOU 2212  O   HOH A 560     1475   2446   1687    327    299     54       O  
HETATM 2213  O   HOH A 561      54.395  19.248  11.019  1.00 18.56           O  
ANISOU 2213  O   HOH A 561     2479   1470   3100    501    293   -315       O  
HETATM 2214  O   HOH A 562      56.465  34.623  -2.914  1.00 21.44           O  
ANISOU 2214  O   HOH A 562     2402   1969   3774   -240    981    -22       O  
HETATM 2215  O   HOH A 563      58.853  41.091  13.616  1.00 17.00           O  
ANISOU 2215  O   HOH A 563     2137   1617   2705   -196    -68    765       O  
HETATM 2216  O   HOH A 564      23.463  14.234  -3.586  1.00 27.64           O  
ANISOU 2216  O   HOH A 564     3858   3156   3488   -563   -689   -919       O  
HETATM 2217  O   HOH A 565      50.519  43.542   3.186  1.00 10.59           O  
ANISOU 2217  O   HOH A 565     1406   1059   1557   -150    226    197       O  
HETATM 2218  O   HOH A 566      41.176  18.078  22.800  1.00 11.00           O  
ANISOU 2218  O   HOH A 566     1154   1242   1782     49    -68    439       O  
HETATM 2219  O   HOH A 567      50.137  37.387  27.918  1.00 14.39           O  
ANISOU 2219  O   HOH A 567     1465   1238   2762    150   -560   -658       O  
HETATM 2220  O   HOH A 568      32.412   8.815   9.471  1.00 18.92           O  
ANISOU 2220  O   HOH A 568     3167   1530   2490   -102    286    382       O  
HETATM 2221  O   HOH A 569      54.697  26.269  11.920  1.00 10.11           O  
ANISOU 2221  O   HOH A 569     1257   1203   1381    138      4    137       O  
HETATM 2222  O   HOH A 570      21.011   5.743  14.434  1.00 17.98           O  
ANISOU 2222  O   HOH A 570     2634   2355   1841   -654   -468    384       O  
HETATM 2223  O   HOH A 571      42.523  14.177  36.676  1.00 21.25           O  
ANISOU 2223  O   HOH A 571     3558   2756   1758   1250    353    559       O  
HETATM 2224  O   HOH A 572      44.619  35.597  17.453  1.00 15.59           O  
ANISOU 2224  O   HOH A 572     1747    901   3275    176    669     15       O  
HETATM 2225  O   HOH A 573      34.858  19.666  -3.099  1.00 19.19           O  
ANISOU 2225  O   HOH A 573     1744   1864   3681   -122    608   -500       O  
HETATM 2226  O   HOH A 574      41.914  21.004  23.799  1.00 14.88           O  
ANISOU 2226  O   HOH A 574     1202   3598    853    415    134    244       O  
HETATM 2227  O   HOH A 575      15.551  17.392  11.850  1.00 16.98           O  
ANISOU 2227  O   HOH A 575     1992   1850   2609    505    -49    360       O  
HETATM 2228  O   HOH A 576      63.838  30.155  29.191  1.00 13.60           O  
ANISOU 2228  O   HOH A 576     1467   1378   2323    112   -458    -17       O  
HETATM 2229  O   HOH A 577      58.559  24.907  18.682  1.00 13.04           O  
ANISOU 2229  O   HOH A 577     2065   1317   1570    281   -279    302       O  
HETATM 2230  O   HOH A 578      48.234  35.299   0.767  1.00 12.38           O  
ANISOU 2230  O   HOH A 578     1541   1502   1659    -67     73     36       O  
HETATM 2231  O   HOH A 579      38.917  10.599   7.947  1.00 14.83           O  
ANISOU 2231  O   HOH A 579     1959   1975   1699   1090    -54     37       O  
HETATM 2232  O   HOH A 580      38.565  32.821   0.778  1.00 20.24           O  
ANISOU 2232  O   HOH A 580     2210   2202   3277     47   -556     59       O  
HETATM 2233  O   HOH A 581      34.182  26.985  -4.302  1.00 25.09           O  
ANISOU 2233  O   HOH A 581     4209   2850   2472    655    522    427       O  
HETATM 2234  O   HOH A 582      19.844  17.925  -0.158  1.00 20.36           O  
ANISOU 2234  O   HOH A 582     1920   3159   2656     69   -350   -621       O  
HETATM 2235  O   HOH A 583      45.767  35.385   2.173  1.00  8.64           O  
ANISOU 2235  O   HOH A 583     1221    960   1100    -47     -1    220       O  
HETATM 2236  O   HOH A 584      50.558  38.912  22.088  1.00 14.41           O  
ANISOU 2236  O   HOH A 584     2256   1582   1634    329    125     -6       O  
HETATM 2237  O   HOH A 585      54.110  36.275  27.751  1.00 13.65           O  
ANISOU 2237  O   HOH A 585     1093   2182   1910    190   -288   -540       O  
HETATM 2238  O   HOH A 586      56.378  23.928  22.732  1.00 15.42           O  
ANISOU 2238  O   HOH A 586     1811   2038   2007    644    -58    513       O  
HETATM 2239  O   HOH A 587      40.913  12.345  11.835  1.00 19.22           O  
ANISOU 2239  O   HOH A 587     3184   1606   2510    567    174   -372       O  
HETATM 2240  O   HOH A 588      51.418  37.523  -6.861  1.00 20.80           O  
ANISOU 2240  O   HOH A 588     2960   1955   2986   -123   -924    320       O  
HETATM 2241  O   HOH A 589      52.668  40.646  11.267  1.00 25.28           O  
ANISOU 2241  O   HOH A 589     2432   1558   5615   -323  -1253   -281       O  
HETATM 2242  O   HOH A 590      29.085   2.121   3.477  1.00 34.85           O  
ANISOU 2242  O   HOH A 590     4489   4023   4727   -504     68   -610       O  
HETATM 2243  O   HOH A 591      39.038  31.613   7.222  1.00 11.20           O  
ANISOU 2243  O   HOH A 591     1262    980   2012   -137     81    130       O  
HETATM 2244  O   HOH A 592      35.693   8.400   6.469  1.00 16.24           O  
ANISOU 2244  O   HOH A 592     1834   1312   3025    108   -217     41       O  
HETATM 2245  O   HOH A 593      57.658  25.838  21.163  1.00 14.54           O  
ANISOU 2245  O   HOH A 593     1409   1770   2342    190   -242   -273       O  
HETATM 2246  O   HOH A 594      24.129   4.709   6.271  1.00 21.80           O  
ANISOU 2246  O   HOH A 594     2581   1758   3942   -439    551   -652       O  
HETATM 2247  O   HOH A 595      60.720  29.280  21.427  1.00 14.72           O  
ANISOU 2247  O   HOH A 595     2608   1301   1682    152   -609    -62       O  
HETATM 2248  O   HOH A 596      37.705  34.223   2.911  1.00 20.54           O  
ANISOU 2248  O   HOH A 596     2249   2476   3078    463    -77    750       O  
HETATM 2249  O   HOH A 597      58.920  33.175  -5.180  1.00 21.68           O  
ANISOU 2249  O   HOH A 597     2110   1639   4487   -411    236   -895       O  
HETATM 2250  O   HOH A 598      50.548  33.727   1.188  1.00  8.23           O  
ANISOU 2250  O   HOH A 598     1166    840   1119     20     36    266       O  
HETATM 2251  O   HOH A 599      40.630  15.011  20.904  1.00 17.50           O  
ANISOU 2251  O   HOH A 599     2369   2643   1636    576   -617   -183       O  
HETATM 2252  O   HOH A 600      25.216  35.475  13.354  1.00 17.39           O  
ANISOU 2252  O   HOH A 600     2807   1752   2047     -5   -643    508       O  
HETATM 2253  O   HOH A 601      48.564  17.177  23.417  1.00 15.79           O  
ANISOU 2253  O   HOH A 601     1770   1653   2576   -105    -36   -108       O  
HETATM 2254  O   HOH A 602      49.882  39.791  16.106  1.00 22.86           O  
ANISOU 2254  O   HOH A 602     3765   1389   3531    341    486    394       O  
HETATM 2255  O   HOH A 603      48.221  38.681  25.445  1.00 11.29           O  
ANISOU 2255  O   HOH A 603     1067   1030   2190    -82   -140   -173       O  
HETATM 2256  O   HOH A 604      21.741  20.625  -2.803  1.00 19.23           O  
ANISOU 2256  O   HOH A 604     2083   3302   1922    -56   -193   -513       O  
HETATM 2257  O   HOH A 605      63.949  36.354  18.812  1.00 14.82           O  
ANISOU 2257  O   HOH A 605     1212   1955   2462   -194    128   -233       O  
HETATM 2258  O   HOH A 606      40.519  17.316  38.462  1.00 27.41           O  
ANISOU 2258  O   HOH A 606     4054   4021   2336   -341    630    274       O  
HETATM 2259  O   HOH A 607      34.900  33.438   5.438  1.00 21.24           O  
ANISOU 2259  O   HOH A 607     2459   2421   3188   -418    397   -125       O  
HETATM 2260  O   HOH A 608      41.275  30.909  -2.808  1.00 20.87           O  
ANISOU 2260  O   HOH A 608     3104   2138   2687    207  -1551    538       O  
HETATM 2261  O   HOH A 609      28.469  33.924   8.205  1.00 24.25           O  
ANISOU 2261  O   HOH A 609     3091   1743   4377    630  -1106    437       O  
HETATM 2262  O   HOH A 610      52.526  27.199  10.436  1.00 13.00           O  
ANISOU 2262  O   HOH A 610     1337   1231   2368   -238     80    351       O  
HETATM 2263  O   HOH A 611      42.200  23.609   0.812  1.00  9.52           O  
ANISOU 2263  O   HOH A 611     1482   1262    874    -84     94   -187       O  
HETATM 2264  O   HOH A 612      27.656   9.319  12.658  1.00 15.04           O  
ANISOU 2264  O   HOH A 612     1796   1022   2895    148    662    188       O  
HETATM 2265  O   HOH A 613      18.902  24.272   9.246  1.00 16.07           O  
ANISOU 2265  O   HOH A 613     1228   2242   2636    509    299    -71       O  
HETATM 2266  O   HOH A 614      41.498  11.681   7.950  1.00 18.55           O  
ANISOU 2266  O   HOH A 614     2128   1894   3024    583   -438  -1198       O  
HETATM 2267  O   HOH A 615      22.478  28.245  23.673  1.00 20.84           O  
ANISOU 2267  O   HOH A 615     3327   2663   1928   1121    -38   -398       O  
HETATM 2268  O   HOH A 616      50.804  25.462   9.237  1.00 18.30           O  
ANISOU 2268  O   HOH A 616     2426   2126   2399   -233    194      2       O  
HETATM 2269  O   HOH A 617      45.489  42.127  25.458  1.00 20.80           O  
ANISOU 2269  O   HOH A 617     2381   2655   2865    545   -472    -18       O  
HETATM 2270  O   HOH A 618      41.148  12.471  20.013  1.00 15.50           O  
ANISOU 2270  O   HOH A 618     2452   1763   1673    517   -596     68       O  
HETATM 2271  O   HOH A 619      57.813  23.182  29.581  1.00 21.52           O  
ANISOU 2271  O   HOH A 619     2242   3441   2490   1224    -73    707       O  
HETATM 2272  O   HOH A 620      48.005  41.266  24.459  1.00 20.52           O  
ANISOU 2272  O   HOH A 620     2262   1977   3557    173    252    397       O  
HETATM 2273  O   HOH A 621      63.522  28.681  21.788  1.00 31.85           O  
ANISOU 2273  O   HOH A 621     4407   2681   5012   1562     34    362       O  
HETATM 2274  O   HOH A 622      59.384  27.350  22.636  1.00 18.47           O  
ANISOU 2274  O   HOH A 622     2780   2503   1733   -424      5    -84       O  
HETATM 2275  O   HOH A 623      49.347  37.793  17.857  1.00 12.90           O  
ANISOU 2275  O   HOH A 623     2254    951   1696    259   -287    -79       O  
HETATM 2276  O   HOH A 624      23.354  22.652  33.326  1.00 21.34           O  
ANISOU 2276  O   HOH A 624     2904   2246   2955     66    557      0       O  
HETATM 2277  O   HOH A 625      58.073  28.571   2.186  1.00 24.97           O  
ANISOU 2277  O   HOH A 625     3488   2372   3627   -644   1911   -600       O  
HETATM 2278  O   HOH A 626      27.350  30.709   0.276  1.00 20.33           O  
ANISOU 2278  O   HOH A 626     2596   2773   2353    116   -345   1119       O  
HETATM 2279  O   HOH A 627      51.412  38.126  19.580  1.00 12.82           O  
ANISOU 2279  O   HOH A 627     1736   1509   1625    452    -35     48       O  
HETATM 2280  O  AHOH A 628      45.236  31.575  33.709  0.60 15.73           O  
ANISOU 2280  O  AHOH A 628     2052   2147   1776    140   -192   -109       O  
HETATM 2281  O  BHOH A 628      46.573  32.468  33.347  0.40 15.50           O  
ANISOU 2281  O  BHOH A 628     1783   1954   2151     50    -36    120       O  
HETATM 2282  O   HOH A 629      25.636  34.399  10.900  1.00 25.32           O  
ANISOU 2282  O   HOH A 629     4450   3090   2078   -986    -83   -248       O  
HETATM 2283  O   HOH A 630      62.833  39.708  13.130  1.00 25.37           O  
ANISOU 2283  O   HOH A 630     2155   4479   3006  -1271   -457    723       O  
HETATM 2284  O   HOH A 631      31.595   6.284   8.704  1.00 20.83           O  
ANISOU 2284  O   HOH A 631     3294   2376   2243   -245   -318    301       O  
HETATM 2285  O   HOH A 632      48.053  40.062  21.879  1.00 25.67           O  
ANISOU 2285  O   HOH A 632     1926   3901   3925    519   -132   -616       O  
HETATM 2286  O   HOH A 633      45.209  12.625  21.087  1.00 18.80           O  
ANISOU 2286  O   HOH A 633     2410   2375   2357   -301    722    921       O  
HETATM 2287  O   HOH A 634      34.021  24.170  12.391  1.00 11.83           O  
ANISOU 2287  O   HOH A 634     1203   1698   1592     -3    -27   -233       O  
HETATM 2288  O   HOH A 635      41.173  42.595  22.660  1.00 13.25           O  
ANISOU 2288  O   HOH A 635     1962   1443   1626     77   -471   -290       O  
HETATM 2289  O   HOH A 636      15.796  21.601  20.036  1.00 26.90           O  
ANISOU 2289  O   HOH A 636     2342   3749   4129    602    560    189       O  
HETATM 2290  O   HOH A 637      32.596  42.014  30.052  1.00 20.53           O  
ANISOU 2290  O   HOH A 637     2564   2137   3098     42    431   -557       O  
HETATM 2291  O   HOH A 638      43.911  42.155  23.250  1.00 18.71           O  
ANISOU 2291  O   HOH A 638     2115   2277   2715     93   -425   -486       O  
HETATM 2292  O   HOH A 639      47.333  17.062  10.252  1.00 29.87           O  
ANISOU 2292  O   HOH A 639     4133   3585   3629   1007   -487   -506       O  
HETATM 2293  O  AHOH A 640      29.272  26.761  15.657  0.50  7.85           O  
ANISOU 2293  O  AHOH A 640      804   1105   1071    212    -86     67       O  
HETATM 2294  O  BHOH A 640      30.862  26.742  15.480  0.50 10.13           O  
ANISOU 2294  O  BHOH A 640     1636   1302    909    -94    -35      0       O  
HETATM 2295  O   HOH A 641      30.939  41.377  27.960  1.00 17.32           O  
ANISOU 2295  O   HOH A 641     2391   2306   1881    458    277   -189       O  
HETATM 2296  O   HOH A 642      37.258  36.211  12.221  1.00 22.48           O  
ANISOU 2296  O   HOH A 642     4230   2168   2143    358    406    825       O  
HETATM 2297  O   HOH A 643      31.171  43.189  23.268  1.00 16.97           O  
ANISOU 2297  O   HOH A 643     2138   1616   2694    427    255   -569       O  
HETATM 2298  O   HOH A 644      49.519  37.535   0.507  1.00 17.15           O  
ANISOU 2298  O   HOH A 644     2751   1897   1866   -508     74   -249       O  
HETATM 2299  O   HOH A 645      63.628  37.693  10.392  1.00 22.43           O  
ANISOU 2299  O   HOH A 645     1483   3436   3603    -86    474    830       O  
HETATM 2300  O   HOH A 646      42.725  13.444   5.559  1.00 21.59           O  
ANISOU 2300  O   HOH A 646     3193   2713   2294  -1075    101   -816       O  
HETATM 2301  O   HOH A 647      28.516  25.464  -3.798  1.00 23.97           O  
ANISOU 2301  O   HOH A 647     5325   2131   1650    880    569    781       O  
HETATM 2302  O   HOH A 648      18.203  15.182   3.312  1.00 15.79           O  
ANISOU 2302  O   HOH A 648     1398   1979   2620    127    122     -5       O  
HETATM 2303  O   HOH A 649      34.417  42.956  18.430  1.00 23.30           O  
ANISOU 2303  O   HOH A 649     1768   2058   5026     41    341   -723       O  
HETATM 2304  O   HOH A 650      44.203  13.536  10.204  1.00 22.30           O  
ANISOU 2304  O   HOH A 650     4165   1561   2745    596  -1025   -369       O  
HETATM 2305  O   HOH A 651      17.174  21.855   0.788  1.00 17.69           O  
ANISOU 2305  O   HOH A 651     1430   3378   1914    554   -299    229       O  
HETATM 2306  O   HOH A 652      47.673  33.742  -1.282  1.00 15.96           O  
ANISOU 2306  O   HOH A 652     2534   1792   1738   -293    379    592       O  
HETATM 2307  O   HOH A 653      18.650  38.285  26.150  1.00 14.48           O  
ANISOU 2307  O   HOH A 653     1669   1722   2108    361   -346   -311       O  
HETATM 2308  O   HOH A 654      44.798  34.387  33.192  1.00 19.47           O  
ANISOU 2308  O   HOH A 654     2605   3301   1492   1159    -69   -109       O  
HETATM 2309  O   HOH A 655      38.135  27.725  -3.627  1.00 26.97           O  
ANISOU 2309  O   HOH A 655     4067   3176   3004    637   -355    155       O  
HETATM 2310  O   HOH A 656      49.840  39.588  13.347  1.00 26.49           O  
ANISOU 2310  O   HOH A 656     3803   3237   3025   -685   1057   -227       O  
HETATM 2311  O   HOH A 657      26.347  32.915   6.934  1.00 20.73           O  
ANISOU 2311  O   HOH A 657     2432   3554   1889   -892     10   -151       O  
HETATM 2312  O   HOH A 658      54.753  21.452  25.809  1.00 18.87           O  
ANISOU 2312  O   HOH A 658     3307   1444   2416   -356    191   -451       O  
HETATM 2313  O   HOH A 659      20.730  29.028  12.395  1.00 24.49           O  
ANISOU 2313  O   HOH A 659     2237   4067   3000    638    -14    366       O  
HETATM 2314  O   HOH A 660      58.881  25.929  32.783  1.00 16.49           O  
ANISOU 2314  O   HOH A 660     1753   2025   2485    139   -423   -452       O  
HETATM 2315  O   HOH A 661      61.146  33.326   7.769  1.00 16.44           O  
ANISOU 2315  O   HOH A 661     1539   2319   2387     39    -84    296       O  
HETATM 2316  O   HOH A 662      56.836  38.379  27.574  1.00 21.42           O  
ANISOU 2316  O   HOH A 662     4080   2069   1987    891    600   -298       O  
HETATM 2317  O   HOH A 663      56.595  43.183   6.890  1.00 24.82           O  
ANISOU 2317  O   HOH A 663     3859   3356   2214   1140    141   -610       O  
HETATM 2318  O   HOH A 664      33.125  26.415  13.627  1.00 13.10           O  
ANISOU 2318  O   HOH A 664     1605   1902   1470    192   -279   -167       O  
HETATM 2319  O   HOH A 665      19.682  31.699  18.300  1.00 15.89           O  
ANISOU 2319  O   HOH A 665     1108   3049   1878    177    329   -265       O  
HETATM 2320  O   HOH A 666      64.236  24.813  26.283  1.00 32.00           O  
ANISOU 2320  O   HOH A 666     3215   3793   5148    510   -442  -1294       O  
HETATM 2321  O   HOH A 667      21.980  21.124  24.274  1.00 29.19           O  
ANISOU 2321  O   HOH A 667     2987   4556   3548   -769    844   -782       O  
HETATM 2322  O   HOH A 668      26.017   7.441   9.924  1.00 28.06           O  
ANISOU 2322  O   HOH A 668     3660   4274   2725   1276    395    618       O  
HETATM 2323  O   HOH A 669      30.036  26.457  13.081  1.00 16.05           O  
ANISOU 2323  O   HOH A 669     1972   2029   2096    -48   -205   -123       O  
HETATM 2324  O  AHOH A 670      22.489  32.559  21.370  0.50 24.12           O  
ANISOU 2324  O  AHOH A 670     2864   3234   3065    -68     35   -127       O  
HETATM 2325  O  BHOH A 670      22.322  34.197  20.774  0.50 27.00           O  
ANISOU 2325  O  BHOH A 670     3206   3709   3344     39     15     29       O  
HETATM 2326  O  AHOH A 671      17.607  24.331  14.881  0.50 28.87           O  
ANISOU 2326  O  AHOH A 671     3749   3630   3587     34    -20     21       O  
HETATM 2327  O  BHOH A 671      17.056  25.381  16.221  0.50 26.45           O  
ANISOU 2327  O  BHOH A 671     3051   3333   3665    176   -158   -455       O  
HETATM 2328  O   HOH A 672      64.124  25.889  23.919  1.00 33.33           O  
ANISOU 2328  O   HOH A 672     3352   4636   4674   -750    702   -550       O  
HETATM 2329  O   HOH A 673      59.251  40.295  26.609  1.00 30.10           O  
ANISOU 2329  O   HOH A 673     3489   3975   3972    314   -111   -345       O  
HETATM 2330  O   HOH A 674      58.463  40.260  23.701  1.00 27.18           O  
ANISOU 2330  O   HOH A 674     5807   2163   2355    312    219    -42       O  
HETATM 2331  O   HOH A 675      21.011  28.268  28.349  1.00 27.54           O  
ANISOU 2331  O   HOH A 675     2673   2968   4823    750    -95   -296       O  
HETATM 2332  O   HOH A 676      20.730  26.426  -0.372  1.00 27.92           O  
ANISOU 2332  O   HOH A 676     2406   4334   3866   1639   -162   -497       O  
HETATM 2333  O   HOH A 677      56.911  31.982  -2.357  1.00 28.02           O  
ANISOU 2333  O   HOH A 677     3186   2080   5377     17   1615   -456       O  
HETATM 2334  O   HOH A 678      55.340  45.362   5.976  1.00 22.41           O  
ANISOU 2334  O   HOH A 678     3454   2337   2721    487   -468   -244       O  
HETATM 2335  O   HOH A 679      59.155  31.943   9.051  1.00 14.23           O  
ANISOU 2335  O   HOH A 679     1406   1808   2191    191   -199    581       O  
HETATM 2336  O   HOH A 680      47.542  22.339  36.764  1.00 12.94           O  
ANISOU 2336  O   HOH A 680     2532   1368   1013   -486   -210    259       O  
HETATM 2337  O   HOH A 681      20.615  34.137  18.903  1.00 19.88           O  
ANISOU 2337  O   HOH A 681     1854   2787   2911    161    694    207       O  
HETATM 2338  O   HOH A 682      37.720  33.632   5.575  1.00 20.92           O  
ANISOU 2338  O   HOH A 682     2234   2518   3194    643    132    156       O  
HETATM 2339  O   HOH A 683      57.102  22.010  32.136  1.00 29.76           O  
ANISOU 2339  O   HOH A 683     4106   3412   3789    652   -437   1029       O  
HETATM 2340  O   HOH A 684      25.531   7.472  12.589  1.00 16.30           O  
ANISOU 2340  O   HOH A 684     2239   1742   2210    162    695    191       O  
HETATM 2341  O   HOH A 685      26.840  27.493  -3.381  1.00 26.93           O  
ANISOU 2341  O   HOH A 685     4079   3155   2996   1327   -524    748       O  
HETATM 2342  O   HOH A 686      47.265  25.724  38.339  1.00 38.02           O  
ANISOU 2342  O   HOH A 686     4618   5516   4311   -234    328   -359       O  
HETATM 2343  O   HOH A 687      48.345  19.414  34.684  1.00 23.50           O  
ANISOU 2343  O   HOH A 687     3704   2209   3016    184   -210    769       O  
HETATM 2344  O   HOH A 688      54.071  25.182  37.709  1.00 21.15           O  
ANISOU 2344  O   HOH A 688     3177   3029   1828   -962   -470    308       O  
HETATM 2345  O   HOH A 689      49.889  14.064  26.287  1.00 18.45           O  
ANISOU 2345  O   HOH A 689     2167   2390   2454   -280   -297    667       O  
HETATM 2346  O   HOH A 690      14.405  21.937   1.366  1.00 23.86           O  
ANISOU 2346  O   HOH A 690     2053   4088   2925    749   -104   -315       O  
HETATM 2347  O   HOH A 691      30.982  14.695  16.103  1.00 25.33           O  
ANISOU 2347  O   HOH A 691     3608   2517   3500    688    549    903       O  
HETATM 2348  O   HOH A 692      19.016  15.427   0.720  1.00 19.35           O  
ANISOU 2348  O   HOH A 692     2239   2787   2323    128   -282   -405       O  
HETATM 2349  O   HOH A 693      48.273  28.229  31.890  1.00 19.82           O  
ANISOU 2349  O   HOH A 693     2291   3326   1912   1202   -177    338       O  
HETATM 2350  O   HOH A 694      58.698  28.969  12.067  1.00 18.35           O  
ANISOU 2350  O   HOH A 694     1729   2798   2444    655   -226   -336       O  
HETATM 2351  O   HOH A 695      38.296  30.061  -2.574  1.00 27.20           O  
ANISOU 2351  O   HOH A 695     4115   3485   2731    214   -411    418       O  
HETATM 2352  O   HOH A 696      28.439  18.469  -4.005  1.00 24.19           O  
ANISOU 2352  O   HOH A 696     2615   3177   3397    310   -243  -1128       O  
HETATM 2353  O   HOH A 697      39.226  10.624  10.659  1.00 19.42           O  
ANISOU 2353  O   HOH A 697     2611   2357   2408    444   -477    -48       O  
HETATM 2354  O   HOH A 698      45.996  14.724  30.781  1.00 23.37           O  
ANISOU 2354  O   HOH A 698     2787   3046   3046   -287   -275   -525       O  
HETATM 2355  O   HOH A 699      43.794  40.190  30.677  1.00 22.71           O  
ANISOU 2355  O   HOH A 699     3146   3354   2129    216   -557  -1294       O  
HETATM 2356  O   HOH A 700      26.837  39.436  32.434  1.00 20.85           O  
ANISOU 2356  O   HOH A 700     2233   3387   2302    222    215  -1130       O  
HETATM 2357  O   HOH A 701      36.935  23.003  39.194  1.00 30.47           O  
ANISOU 2357  O   HOH A 701     3528   4420   3629    -28    230    460       O  
HETATM 2358  O   HOH A 702      49.563  20.012  16.335  1.00 24.31           O  
ANISOU 2358  O   HOH A 702     2268   2944   4022   -153    635   -839       O  
HETATM 2359  O   HOH A 703      45.680  38.737  32.268  1.00 28.30           O  
ANISOU 2359  O   HOH A 703     3646   4333   2771    126   -648   -975       O  
HETATM 2360  O   HOH A 704      24.758  27.869  -1.413  1.00 27.20           O  
ANISOU 2360  O   HOH A 704     4705   3513   2115    443   -665    236       O  
HETATM 2361  O   HOH A 705      36.976  12.371  18.083  1.00 18.84           O  
ANISOU 2361  O   HOH A 705     3075   2040   2040   -593    184    205       O  
HETATM 2362  O   HOH A 706      54.835  19.845  23.846  1.00 30.56           O  
ANISOU 2362  O   HOH A 706     4479   3059   4071    141    220  -1152       O  
HETATM 2363  O   HOH A 707      60.141  25.757  30.392  1.00 28.58           O  
ANISOU 2363  O   HOH A 707     4348   3629   2881   -128    116    343       O  
HETATM 2364  O   HOH A 708      37.908  38.702  13.871  1.00 26.16           O  
ANISOU 2364  O   HOH A 708     3973   3242   2722   1067    488    849       O  
HETATM 2365  O   HOH A 709      64.461  41.681   2.842  1.00 29.89           O  
ANISOU 2365  O   HOH A 709     3295   4065   3993   -124    185    829       O  
HETATM 2366  O   HOH A 710      27.225  32.919   4.451  1.00 25.83           O  
ANISOU 2366  O   HOH A 710     3858   2534   3421   -710    568    300       O  
HETATM 2367  O   HOH A 711      47.391  15.320  32.554  1.00 23.86           O  
ANISOU 2367  O   HOH A 711     2417   2505   4142    433    163    -14       O  
HETATM 2368  O   HOH A 712      58.586  26.092  37.492  1.00 25.83           O  
ANISOU 2368  O   HOH A 712     3420   2445   3948    277   -493   1137       O  
HETATM 2369  O   HOH A 713      19.289  21.747  -3.284  1.00 28.20           O  
ANISOU 2369  O   HOH A 713     2635   4833   3244    985   -574   -266       O  
HETATM 2370  O   HOH A 714      54.262  34.491  38.300  1.00 17.47           O  
ANISOU 2370  O   HOH A 714     2304   2076   2257   -300    254   -511       O  
HETATM 2371  O   HOH A 715      23.873  23.504  30.815  1.00 21.66           O  
ANISOU 2371  O   HOH A 715     2463   2957   2809     68   1129    608       O  
HETATM 2372  O   HOH A 716      49.305  31.884  33.285  1.00 24.04           O  
ANISOU 2372  O   HOH A 716     2986   3706   2441    838   -554   -104       O  
HETATM 2373  O   HOH A 717      55.037  21.472  21.959  1.00 29.72           O  
ANISOU 2373  O   HOH A 717     2899   4965   3425   -227   -415     -9       O  
HETATM 2374  O   HOH A 718      45.360  38.431  -0.899  1.00 28.68           O  
ANISOU 2374  O   HOH A 718     4495   3142   3259   -965    -24    967       O  
HETATM 2375  O   HOH A 719      52.996  46.711   2.634  1.00 21.45           O  
ANISOU 2375  O   HOH A 719     2811   3210   2129    792    -16     80       O  
HETATM 2376  O   HOH A 720      38.124  33.344   9.407  1.00 25.78           O  
ANISOU 2376  O   HOH A 720     4268   2946   2580   1744    920    151       O  
HETATM 2377  O   HOH A 721      38.540  17.840  -4.661  1.00 26.33           O  
ANISOU 2377  O   HOH A 721     3169   3221   3614   -251   1133      7       O  
HETATM 2378  O   HOH A 722      42.500  32.397  36.652  1.00 23.34           O  
ANISOU 2378  O   HOH A 722     3446   3589   1832   -750   -139   -904       O  
HETATM 2379  O   HOH A 723      31.666  16.565  34.423  1.00 26.59           O  
ANISOU 2379  O   HOH A 723     4306   2954   2841    493   -364   1163       O  
HETATM 2380  O   HOH A 724      59.933  18.041   6.476  1.00 19.19           O  
ANISOU 2380  O   HOH A 724     1196   2488   3606    262   -277    -24       O  
HETATM 2381  O   HOH A 725      58.583  25.029   4.963  1.00 20.68           O  
ANISOU 2381  O   HOH A 725     2361   2658   2835    228   -148   -441       O  
HETATM 2382  O   HOH A 726      28.495  16.946  26.485  1.00 25.96           O  
ANISOU 2382  O   HOH A 726     3749   2623   3491   -247    711    -46       O  
HETATM 2383  O   HOH A 727      32.421  30.060  33.667  1.00 20.06           O  
ANISOU 2383  O   HOH A 727     1940   2772   2906    168    856   -106       O  
HETATM 2384  O   HOH A 728      20.828  33.320   9.874  1.00 22.09           O  
ANISOU 2384  O   HOH A 728     2820   3008   2562    476   -318    181       O  
HETATM 2385  O   HOH A 729      34.245  32.100   0.086  1.00 23.39           O  
ANISOU 2385  O   HOH A 729     2499   3268   3118   -580    129   1445       O  
HETATM 2386  O   HOH A 730      33.020  37.179  33.039  1.00 21.61           O  
ANISOU 2386  O   HOH A 730     3363   3568   1279    322      4      0       O  
HETATM 2387  O   HOH A 731      60.541  29.003  14.312  1.00 18.50           O  
ANISOU 2387  O   HOH A 731     1660   2165   3203    238    311   -553       O  
HETATM 2388  O   HOH A 732      32.460  23.831  37.092  1.00 26.08           O  
ANISOU 2388  O   HOH A 732     3880   3527   2501    196    217   1237       O  
HETATM 2389  O   HOH A 733      30.490  34.241   6.083  1.00 22.97           O  
ANISOU 2389  O   HOH A 733     3601   2136   2990    782    832    220       O  
HETATM 2390  O   HOH A 734      63.621  40.064  20.176  1.00 27.38           O  
ANISOU 2390  O   HOH A 734     2469   3791   4141   -780   -410    900       O  
HETATM 2391  O   HOH A 735      29.836  32.254  35.655  1.00 22.35           O  
ANISOU 2391  O   HOH A 735     2293   2987   3212    324   -265   -413       O  
HETATM 2392  O   HOH A 736      33.922  13.330  14.307  1.00 22.64           O  
ANISOU 2392  O   HOH A 736     3286   3733   1581  -1243   -562    498       O  
HETATM 2393  O   HOH A 737      34.985  40.551  14.546  1.00 25.02           O  
ANISOU 2393  O   HOH A 737     3942   2365   3199   -278   -430    520       O  
HETATM 2394  O   HOH A 738      62.133  41.163   6.507  1.00 24.79           O  
ANISOU 2394  O   HOH A 738     2458   3782   3177   -653    -91   -709       O  
HETATM 2395  O   HOH A 739      59.202  30.715   1.121  1.00 18.06           O  
ANISOU 2395  O   HOH A 739     3086   1484   2289   -547    772   -308       O  
HETATM 2396  O   HOH A 740      35.784  15.348  30.002  1.00 26.35           O  
ANISOU 2396  O   HOH A 740     2854   2914   4241   -199   -110    121       O  
HETATM 2397  O   HOH A 741      53.234  28.474   1.913  1.00 23.22           O  
ANISOU 2397  O   HOH A 741     2725   2848   3249   -161    -71     71       O  
HETATM 2398  O   HOH A 742      49.988  33.364  -2.490  1.00 22.74           O  
ANISOU 2398  O   HOH A 742     2626   2631   3380    -22    367   1317       O  
HETATM 2399  O   HOH A 743      64.277  40.090  28.362  1.00 38.47           O  
ANISOU 2399  O   HOH A 743     4745   5198   4672    656    -17   -292       O  
HETATM 2400  O   HOH A 744      61.877  24.361   7.126  1.00 25.07           O  
ANISOU 2400  O   HOH A 744     2549   3194   3781    229   -355   -119       O  
HETATM 2401  O   HOH A 745      28.303   6.259   9.425  1.00 26.35           O  
ANISOU 2401  O   HOH A 745     2709   3848   3452   -181    275   -401       O  
HETATM 2402  O   HOH A 746      58.978  20.406   5.604  1.00 26.85           O  
ANISOU 2402  O   HOH A 746     3295   3615   3291   1028    631    825       O  
HETATM 2403  O   HOH A 747      49.984  34.014  -4.951  1.00 29.85           O  
ANISOU 2403  O   HOH A 747     3932   3839   3567   -760   -502    -28       O  
HETATM 2404  O   HOH A 748      41.775  37.609   0.853  1.00 34.36           O  
ANISOU 2404  O   HOH A 748     4683   4621   3750    813   -409    668       O  
HETATM 2405  O   HOH A 749      38.992  36.785   2.816  1.00 26.32           O  
ANISOU 2405  O   HOH A 749     2609   3109   4281    549   -584    451       O  
HETATM 2406  O   HOH A 750      41.695  21.224  -9.506  1.00 38.45           O  
ANISOU 2406  O   HOH A 750     5396   4987   4223    316    200   -928       O  
HETATM 2407  O   HOH A 751      24.250  12.874  16.797  1.00 23.01           O  
ANISOU 2407  O   HOH A 751     2669   2423   3648    400    -19   -584       O  
HETATM 2408  O   HOH A 752      47.586  30.232  33.423  1.00 25.93           O  
ANISOU 2408  O   HOH A 752     3504   3591   2754    497   -406   -269       O  
HETATM 2409  O   HOH A 753      60.099  29.568   9.777  1.00 24.60           O  
ANISOU 2409  O   HOH A 753     2977   2412   3958    693   -301    427       O  
HETATM 2410  O   HOH A 754      41.697  38.757  34.454  1.00 41.89           O  
ANISOU 2410  O   HOH A 754     5361   5257   5296   -104    655   -711       O  
HETATM 2411  O   HOH A 755      41.570  15.861  -2.620  1.00 27.88           O  
ANISOU 2411  O   HOH A 755     2241   3712   4639  -1020    573    244       O  
HETATM 2412  O   HOH A 756      27.937  16.046  -3.675  1.00 23.25           O  
ANISOU 2412  O   HOH A 756     2761   3054   3018      6    197    205       O  
HETATM 2413  O   HOH A 757      47.465  15.826  29.506  1.00 28.78           O  
ANISOU 2413  O   HOH A 757     3952   4098   2886    304   -602   -839       O  
HETATM 2414  O   HOH A 758      64.843  32.255  13.653  1.00 23.52           O  
ANISOU 2414  O   HOH A 758     2579   3156   3198    356  -1106     23       O  
HETATM 2415  O   HOH A 759      26.298  37.957  13.702  1.00 26.20           O  
ANISOU 2415  O   HOH A 759     3530   2380   4042    229   -472    365       O  
HETATM 2416  O   HOH A 760      17.857  19.682  -0.805  1.00 22.77           O  
ANISOU 2416  O   HOH A 760     2111   3859   2681    576   -431   -377       O  
HETATM 2417  O   HOH A 761      37.368  34.762  40.781  1.00 30.12           O  
ANISOU 2417  O   HOH A 761     4330   4227   2887   -282   -269   -920       O  
HETATM 2418  O   HOH A 762      23.338  20.995  -5.087  1.00 24.46           O  
ANISOU 2418  O   HOH A 762     3074   4347   1871   -268      1   -503       O  
HETATM 2419  O   HOH A 763      59.940  22.806   8.188  1.00 34.80           O  
ANISOU 2419  O   HOH A 763     3524   4876   4822    402    453     41       O  
HETATM 2420  O   HOH A 764      16.578   9.815  11.847  1.00 24.93           O  
ANISOU 2420  O   HOH A 764     3025   2180   4265   -584   -112   -708       O  
HETATM 2421  O   HOH A 765      22.263  34.136  16.218  1.00 34.15           O  
ANISOU 2421  O   HOH A 765     3898   3731   5344    572    159    232       O  
HETATM 2422  O   HOH A 766      25.845  21.397  -5.032  1.00 25.14           O  
ANISOU 2422  O   HOH A 766     3488   3577   2484   -769   -263   -612       O  
HETATM 2423  O   HOH A 767      55.518  29.857  38.995  1.00 22.35           O  
ANISOU 2423  O   HOH A 767     4065   2527   1899   -239    286   -261       O  
HETATM 2424  O   HOH A 768      27.125  19.316  -6.141  1.00 35.97           O  
ANISOU 2424  O   HOH A 768     4999   4444   4221    363   -374   -291       O  
HETATM 2425  O   HOH A 769      43.947  36.357   0.365  1.00 20.93           O  
ANISOU 2425  O   HOH A 769     3374   1632   2945     17   -974    668       O  
HETATM 2426  O   HOH A 770      38.154  20.936  -5.053  1.00 26.89           O  
ANISOU 2426  O   HOH A 770     3498   3394   3324    545   -480  -1694       O  
HETATM 2427  O   HOH A 771      60.218  43.344  13.167  1.00 30.43           O  
ANISOU 2427  O   HOH A 771     5576   2192   3793  -1437   -125   -275       O  
HETATM 2428  O   HOH A 772      45.477  20.873  -4.141  1.00 21.11           O  
ANISOU 2428  O   HOH A 772     2458   3277   2285   -398    681   -498       O  
HETATM 2429  O   HOH A 773      62.422  34.677   4.288  1.00 29.88           O  
ANISOU 2429  O   HOH A 773     3690   2868   4793   1341   -480    777       O  
HETATM 2430  O   HOH A 774      52.336  33.986  -5.563  1.00 32.42           O  
ANISOU 2430  O   HOH A 774     3555   4586   4176  -1359   -194   -231       O  
HETATM 2431  O   HOH A 775      59.494  38.909  31.323  1.00 26.99           O  
ANISOU 2431  O   HOH A 775     4264   2791   3198  -1135   -491  -1034       O  
HETATM 2432  O   HOH A 776      62.379  43.859   6.063  1.00 30.21           O  
ANISOU 2432  O   HOH A 776     4384   3231   3862   -222    -50    -18       O  
HETATM 2433  O   HOH A 777      46.353  15.691  17.755  1.00 18.73           O  
ANISOU 2433  O   HOH A 777     2507   2409   2201    562    311    684       O  
HETATM 2434  O   HOH A 778      27.416  41.759  31.248  1.00 36.13           O  
ANISOU 2434  O   HOH A 778     4376   4295   5057    -22    561   -243       O  
HETATM 2435  O   HOH A 779      55.453  41.674   8.977  1.00 24.32           O  
ANISOU 2435  O   HOH A 779     3591   2805   2842    469     25    318       O  
HETATM 2436  O   HOH A 780      21.548  24.154  29.857  1.00 26.95           O  
ANISOU 2436  O   HOH A 780     2273   3590   4374    526    882    -15       O  
HETATM 2437  O   HOH A 781      14.920  22.599   4.023  1.00 27.82           O  
ANISOU 2437  O   HOH A 781     3847   3745   2976    243    526   -242       O  
HETATM 2438  O   HOH A 782      54.557  35.293  -5.132  1.00 19.21           O  
ANISOU 2438  O   HOH A 782     1895   1667   3735   -213   -263    473       O  
HETATM 2439  O   HOH A 783      58.999  24.803   9.380  1.00 28.21           O  
ANISOU 2439  O   HOH A 783     4007   2443   4266    550   -638   -238       O  
HETATM 2440  O   HOH A 784      25.594  13.965  -0.956  1.00 25.95           O  
ANISOU 2440  O   HOH A 784     1698   3252   4909    483    622   1204       O  
HETATM 2441  O   HOH A 785      33.130  39.873  12.905  1.00 22.30           O  
ANISOU 2441  O   HOH A 785     3590   1937   2944    195   -338    651       O  
HETATM 2442  O   HOH A 786      46.508  23.982  35.592  1.00 26.51           O  
ANISOU 2442  O   HOH A 786     3775   3583   2712    656   -898   -990       O  
HETATM 2443  O   HOH A 787      20.015  10.033  18.784  1.00 41.97           O  
ANISOU 2443  O   HOH A 787     5863   4711   5373    679    -36   -143       O  
HETATM 2444  O   HOH A 788      65.337  35.582  11.445  1.00 28.47           O  
ANISOU 2444  O   HOH A 788     3130   3354   4333    371    178   -368       O  
HETATM 2445  O   HOH A 789      50.773  33.884  32.528  1.00 28.90           O  
ANISOU 2445  O   HOH A 789     3185   4185   3608  -1111   -444   -391       O  
HETATM 2446  O   HOH A 790      18.963  26.917   9.798  1.00 32.93           O  
ANISOU 2446  O   HOH A 790     3395   3554   5562    814    541    335       O  
HETATM 2447  O   HOH A 791      21.360  17.947  -2.683  1.00 26.31           O  
ANISOU 2447  O   HOH A 791     2364   3228   4405   -328   -651   -383       O  
HETATM 2448  O   HOH A 792      52.149  18.829  -2.280  1.00 29.50           O  
ANISOU 2448  O   HOH A 792     2746   4730   3731    202   1389   -307       O  
HETATM 2449  O   HOH A 793      23.201  13.758  34.548  1.00 24.88           O  
ANISOU 2449  O   HOH A 793     3592   2048   3814    -84     99   1005       O  
HETATM 2450  O   HOH A 794      31.074  18.446  -5.872  1.00 30.82           O  
ANISOU 2450  O   HOH A 794     5207   3179   3321    -36    812   -979       O  
HETATM 2451  O   HOH A 795      49.393  18.881  21.559  1.00 18.08           O  
ANISOU 2451  O   HOH A 795     2369   1917   2581    541   -120    251       O  
HETATM 2452  O   HOH A 796      26.158  19.330  23.125  1.00 33.65           O  
ANISOU 2452  O   HOH A 796     3516   4414   4855    217   -433    600       O  
HETATM 2453  O   HOH A 797      62.432  40.346  30.679  1.00 32.32           O  
ANISOU 2453  O   HOH A 797     4578   4205   3496   -145    448    221       O  
HETATM 2454  O   HOH A 798      53.254  34.203  32.637  1.00 22.99           O  
ANISOU 2454  O   HOH A 798     3098   2604   3031    198    344    403       O  
HETATM 2455  O   HOH A 799      51.351  35.238  30.262  1.00 33.31           O  
ANISOU 2455  O   HOH A 799     4151   4418   4086   -105   -866    -53       O  
HETATM 2456  O   HOH A 800      31.692  27.292  -3.136  1.00 25.93           O  
ANISOU 2456  O   HOH A 800     3405   3975   2472    643    194    151       O  
HETATM 2457  O   HOH A 801      65.919  38.064  19.933  1.00 31.34           O  
ANISOU 2457  O   HOH A 801     3911   4144   3851   -588    415    183       O  
HETATM 2458  O   HOH A 802      61.282  36.991  33.536  1.00 23.19           O  
ANISOU 2458  O   HOH A 802     3605   1922   3283   -627   1339   -824       O  
HETATM 2459  O   HOH A 803      21.001  31.596  15.983  1.00 20.96           O  
ANISOU 2459  O   HOH A 803     2632   3092   2239   1187    409    199       O  
HETATM 2460  O   HOH A 804      64.967  25.793  28.766  1.00 30.03           O  
ANISOU 2460  O   HOH A 804     3863   2703   4841    815    131    -62       O  
HETATM 2461  O   HOH A 805      17.424   9.605  19.297  1.00 25.75           O  
ANISOU 2461  O   HOH A 805     3891   2298   3593    621   1073    877       O  
HETATM 2462  O   HOH A 806      48.537  17.723  19.154  1.00 23.78           O  
ANISOU 2462  O   HOH A 806     2715   3713   2606   1132   -412   -820       O  
HETATM 2463  O   HOH A 807      59.005  26.367   2.642  1.00 39.96           O  
ANISOU 2463  O   HOH A 807     5168   4982   5030   -110    321   -204       O  
HETATM 2464  O   HOH A 808      52.418  20.423  16.445  1.00 23.36           O  
ANISOU 2464  O   HOH A 808     3348   2623   2902  -1288    -35    747       O  
HETATM 2465  O   HOH A 809      20.134   7.864   1.883  1.00 26.32           O  
ANISOU 2465  O   HOH A 809     3086   3962   2952   -491   -293   -659       O  
HETATM 2466  O   HOH A 810      28.793  20.057  23.248  1.00 32.70           O  
ANISOU 2466  O   HOH A 810     3819   3628   4978   -524   -669    489       O  
HETATM 2467  O   HOH A 811      28.109  41.722  28.785  1.00 28.51           O  
ANISOU 2467  O   HOH A 811     3294   4012   3524    855    413    -14       O  
HETATM 2468  O   HOH A 812      31.020  19.916  20.859  1.00 36.96           O  
ANISOU 2468  O   HOH A 812     4566   4222   5256   1410   -656   -470       O  
HETATM 2469  O   HOH A 813      21.519  21.315  29.052  1.00 27.49           O  
ANISOU 2469  O   HOH A 813     3156   3773   3516   -470    612    718       O  
HETATM 2470  O   HOH A 814      44.894  41.335  18.827  1.00 33.89           O  
ANISOU 2470  O   HOH A 814     3335   3886   5654   -541     70    178       O  
HETATM 2471  O   HOH A 815      45.670  26.252  -6.949  1.00 22.80           O  
ANISOU 2471  O   HOH A 815     2860   3961   1840   -887     55    222       O  
HETATM 2472  O   HOH A 816      16.906   8.287   9.104  1.00 35.60           O  
ANISOU 2472  O   HOH A 816     4527   4423   4575    362   -153    656       O  
HETATM 2473  O   HOH A 817      35.986  13.870  22.222  1.00 26.67           O  
ANISOU 2473  O   HOH A 817     4796   2662   2674   -564    216    698       O  
HETATM 2474  O   HOH A 818      63.923  29.068  14.798  1.00 31.22           O  
ANISOU 2474  O   HOH A 818     2874   4678   4308    654    559   -401       O  
HETATM 2475  O   HOH A 819      36.873  31.027  -0.212  1.00 24.08           O  
ANISOU 2475  O   HOH A 819     2722   3362   3063   -238     77    415       O  
HETATM 2476  O   HOH A 820      20.505  38.443  32.190  1.00 27.61           O  
ANISOU 2476  O   HOH A 820     3055   4489   2946   -179   1034  -1047       O  
HETATM 2477  O   HOH A 821      34.477  15.686  25.096  1.00 29.24           O  
ANISOU 2477  O   HOH A 821     3201   3923   3983  -1079    807   -222       O  
HETATM 2478  O   HOH A 822      44.201  19.755  -7.901  1.00 37.51           O  
ANISOU 2478  O   HOH A 822     5005   5604   3643    463    769    -45       O  
HETATM 2479  O   HOH A 823      20.024  31.300   6.044  1.00 25.36           O  
ANISOU 2479  O   HOH A 823     3857   2397   3380    714   -406    522       O  
HETATM 2480  O   HOH A 824      48.826  15.244  21.599  1.00 22.90           O  
ANISOU 2480  O   HOH A 824     3170   2908   2620   -520   -462    390       O  
HETATM 2481  O   HOH A 825      49.658  30.259  -6.068  1.00 37.11           O  
ANISOU 2481  O   HOH A 825     5209   5251   3637    -29    754    -37       O  
HETATM 2482  O   HOH A 826      57.991  22.973  24.726  1.00 26.70           O  
ANISOU 2482  O   HOH A 826     3394   3333   3417    854   -478    421       O  
HETATM 2483  O   HOH A 827      40.724  39.955  14.855  1.00 40.96           O  
ANISOU 2483  O   HOH A 827     5645   4924   4993   -330    171   -541       O  
HETATM 2484  O   HOH A 828      62.630  25.316  30.111  1.00 24.66           O  
ANISOU 2484  O   HOH A 828     2997   2745   3625    922     13    532       O  
HETATM 2485  O   HOH A 829      47.103  13.915  14.401  1.00 40.71           O  
ANISOU 2485  O   HOH A 829     5663   4305   5497    838     70   -112       O  
HETATM 2486  O   HOH A 830      45.268  37.884  16.123  1.00 25.94           O  
ANISOU 2486  O   HOH A 830     3091   2755   4007     56    841   -949       O  
HETATM 2487  O   HOH A 831      26.239   6.866  18.139  1.00 30.27           O  
ANISOU 2487  O   HOH A 831     2759   3670   5069    908  -1195    573       O  
HETATM 2488  O   HOH A 832      46.910  38.721  18.628  1.00 25.42           O  
ANISOU 2488  O   HOH A 832     2606   3646   3406    982     26    -60       O  
HETATM 2489  O   HOH A 833      25.857  18.066  25.503  1.00 33.70           O  
ANISOU 2489  O   HOH A 833     4407   3467   4928    382   -323   -478       O  
HETATM 2490  O   HOH A 834      51.352  17.788  11.298  1.00 35.60           O  
ANISOU 2490  O   HOH A 834     4642   3142   5740    234   -305   -100       O  
HETATM 2491  O   HOH A 835      49.381  31.327  35.941  1.00 27.09           O  
ANISOU 2491  O   HOH A 835     3021   3836   3434    627    364   -234       O  
HETATM 2492  O   HOH A 836      28.150  41.870  16.398  1.00 34.16           O  
ANISOU 2492  O   HOH A 836     4108   4209   4662   1194   -480     97       O  
HETATM 2493  O   HOH A 837      51.974  39.505  25.605  1.00 25.81           O  
ANISOU 2493  O   HOH A 837     2857   2183   4764   -625   -593   -668       O  
HETATM 2494  O   HOH A 838      46.969  16.138  34.627  1.00 25.00           O  
ANISOU 2494  O   HOH A 838     3596   2511   3390    362  -1316   1102       O  
HETATM 2495  O   HOH A 839      21.987  33.554   7.266  1.00 39.39           O  
ANISOU 2495  O   HOH A 839     4169   5490   5307    617   -247    370       O  
HETATM 2496  O   HOH A 840      43.889  38.842  18.208  1.00 29.39           O  
ANISOU 2496  O   HOH A 840     3748   3548   3871    257    427   -336       O  
HETATM 2497  O   HOH A 841      34.373  16.053  33.974  1.00 35.62           O  
ANISOU 2497  O   HOH A 841     5245   3845   4441    -21     -4    394       O  
HETATM 2498  O   HOH A 842      48.793  18.610  30.765  1.00 30.28           O  
ANISOU 2498  O   HOH A 842     3246   2973   5284   1130    520    363       O  
HETATM 2499  O   HOH A 843      27.461  15.845  17.861  1.00 33.03           O  
ANISOU 2499  O   HOH A 843     2652   5263   4633   -417    760    388       O  
HETATM 2500  O   HOH A 844      41.380  40.044   3.233  1.00 29.73           O  
ANISOU 2500  O   HOH A 844     4032   2064   5200    277    198    687       O  
HETATM 2501  O   HOH A 845      27.731  17.982  19.359  1.00 33.06           O  
ANISOU 2501  O   HOH A 845     4186   3495   4878   -374    385    681       O  
HETATM 2502  O   HOH A 846      62.703  30.021  10.049  1.00 31.50           O  
ANISOU 2502  O   HOH A 846     3554   3822   4589    557   -111    548       O  
HETATM 2503  O   HOH A 847      12.842  17.151  17.507  1.00 30.10           O  
ANISOU 2503  O   HOH A 847     3731   3011   4694    211    837    661       O  
HETATM 2504  O   HOH A 848      45.454  34.322  -2.775  1.00 42.79           O  
ANISOU 2504  O   HOH A 848     5987   5171   5100    236   -642    548       O  
HETATM 2505  O   HOH A 849      43.238  34.570  35.389  1.00 26.06           O  
ANISOU 2505  O   HOH A 849     4637   3636   1626    238    568   -154       O  
HETATM 2506  O   HOH A 850      45.989  33.376  -5.452  1.00 33.11           O  
ANISOU 2506  O   HOH A 850     5104   3803   3673   -214   -513    554       O  
HETATM 2507  O   HOH A 851      60.455  24.303  26.231  1.00 39.74           O  
ANISOU 2507  O   HOH A 851     5295   5119   4683    306   1082   -298       O  
HETATM 2508  O   HOH A 852      26.787  23.920  -5.852  1.00 31.28           O  
ANISOU 2508  O   HOH A 852     4248   4900   2737    112   -749    538       O  
HETATM 2509  O   HOH A 853      14.508  16.804  19.716  1.00 31.73           O  
ANISOU 2509  O   HOH A 853     2644   4589   4822    122    811     26       O  
HETATM 2510  O   HOH A 854      19.794  24.659   3.056  1.00 25.16           O  
ANISOU 2510  O   HOH A 854     3778   3440   2339   1842   -258    251       O  
HETATM 2511  O   HOH A 855      55.539  22.621  34.276  1.00 35.67           O  
ANISOU 2511  O   HOH A 855     3947   4275   5330    134    136    585       O  
HETATM 2512  O   HOH A 856      16.229  24.906  19.318  1.00 25.20           O  
ANISOU 2512  O   HOH A 856     2371   2992   4212    -65    315    -51       O  
HETATM 2513  O   HOH A 857      41.687  41.486   9.570  1.00 33.44           O  
ANISOU 2513  O   HOH A 857     4040   4330   4335    309    146   -300       O  
HETATM 2514  O   HOH A 858      34.967  34.172   2.476  1.00 32.57           O  
ANISOU 2514  O   HOH A 858     3283   3890   5202    638    -55    306       O  
HETATM 2515  O   HOH A 859      47.335  18.546  36.809  1.00 31.62           O  
ANISOU 2515  O   HOH A 859     4767   3242   4004  -1190   -468    647       O  
HETATM 2516  O   HOH A 860      47.272  12.870  -4.358  1.00 32.05           O  
ANISOU 2516  O   HOH A 860     4314   3574   4286   -252    -48   -566       O  
HETATM 2517  O   HOH A 861      16.209  22.897  16.373  1.00 35.79           O  
ANISOU 2517  O   HOH A 861     4252   4717   4626   1039   -607    324       O  
HETATM 2518  O   HOH A 862      14.383  19.505  20.829  1.00 36.49           O  
ANISOU 2518  O   HOH A 862     3931   4975   4955    393   -238    328       O  
HETATM 2519  O   HOH A 863      53.101  42.660   9.543  1.00 32.89           O  
ANISOU 2519  O   HOH A 863     4609   3868   4018   -140   -797   -143       O  
HETATM 2520  O   HOH A 864      61.517  25.695  23.135  1.00 27.99           O  
ANISOU 2520  O   HOH A 864     3264   2963   4406   1026    228    525       O  
HETATM 2521  O   HOH A 865      60.327  45.390   7.934  1.00 33.57           O  
ANISOU 2521  O   HOH A 865     5364   3449   3940    -75    347   -113       O  
HETATM 2522  O   HOH A 866      34.326  14.261  31.905  1.00 29.34           O  
ANISOU 2522  O   HOH A 866     4414   3301   3431   -455    664   -313       O  
HETATM 2523  O   HOH A 867      58.352  21.651  16.170  1.00 27.42           O  
ANISOU 2523  O   HOH A 867     3257   2686   4476   1094   -364   1122       O  
HETATM 2524  O   HOH A 868      62.356  24.280   4.300  1.00 32.55           O  
ANISOU 2524  O   HOH A 868     5012   3155   4199    378  -1024    988       O  
HETATM 2525  O   HOH A 869      24.129  10.187  19.250  1.00 31.89           O  
ANISOU 2525  O   HOH A 869     4946   3617   3553   -414    118   -575       O  
HETATM 2526  O   HOH A 870      51.076  29.992  38.005  1.00 34.67           O  
ANISOU 2526  O   HOH A 870     5448   4982   2743   -476    281     44       O  
HETATM 2527  O   HOH A 871      49.426  17.465  15.933  1.00 28.04           O  
ANISOU 2527  O   HOH A 871     2724   3103   4824    718   -547   -738       O  
HETATM 2528  O   HOH A 872      18.497   6.758  15.373  1.00 28.56           O  
ANISOU 2528  O   HOH A 872     2898   5100   2852    386     35   1430       O  
HETATM 2529  O   HOH A 873      55.429  17.042   6.573  1.00 34.56           O  
ANISOU 2529  O   HOH A 873     3396   4408   5325    329    225   -369       O  
HETATM 2530  O   HOH A 874      56.254  18.677   4.649  1.00 33.06           O  
ANISOU 2530  O   HOH A 874     3356   4188   5014   1085    299     96       O  
HETATM 2531  O   HOH A 875      49.554  36.520  -5.512  1.00 27.45           O  
ANISOU 2531  O   HOH A 875     3736   3497   3194   -712   -843   -124       O  
HETATM 2532  O   HOH A 876      17.920  24.176  -0.695  1.00 31.11           O  
ANISOU 2532  O   HOH A 876     3250   3976   4594    840   -829    549       O  
HETATM 2533  O   HOH A 877      24.354  25.427  -6.384  1.00 43.39           O  
ANISOU 2533  O   HOH A 877     5589   5509   5387   -105   -727    254       O  
HETATM 2534  O   HOH A 878      52.519  17.951  24.013  1.00 32.40           O  
ANISOU 2534  O   HOH A 878     3657   4147   4506   1241    498   -597       O  
HETATM 2535  O   HOH A 879      19.047   8.612  11.709  1.00 24.64           O  
ANISOU 2535  O   HOH A 879     2626   3854   2882   -143   -150   -295       O  
HETATM 2536  O   HOH A 880      56.904  21.231  13.856  1.00 30.00           O  
ANISOU 2536  O   HOH A 880     3342   4037   4019    -85   -108   -725       O  
HETATM 2537  O   HOH A 881      18.235  32.211  35.680  1.00 23.35           O  
ANISOU 2537  O   HOH A 881     2562   4320   1987     49    244    612       O  
HETATM 2538  O   HOH A 882      22.809  30.093   1.696  1.00 33.80           O  
ANISOU 2538  O   HOH A 882     4560   4232   4049    920   -266    637       O  
HETATM 2539  O   HOH A 883      36.933  10.212  16.059  1.00 29.57           O  
ANISOU 2539  O   HOH A 883     3372   4252   3609   -121   -378   -106       O  
HETATM 2540  O   HOH A 884      25.651  42.711  22.635  1.00 37.92           O  
ANISOU 2540  O   HOH A 884     4839   4574   4995    542     72   -195       O  
HETATM 2541  O   HOH A 885      46.357  13.692  -6.648  1.00 38.13           O  
ANISOU 2541  O   HOH A 885     5358   3862   5266   -621   -122   -120       O  
HETATM 2542  O   HOH A 886      49.183  18.237  13.042  1.00 24.98           O  
ANISOU 2542  O   HOH A 886     1768   2784   4938    167    434   1420       O  
HETATM 2543  O   HOH A 887      28.676  43.823  22.300  1.00 26.84           O  
ANISOU 2543  O   HOH A 887     3683   2746   3768    321  -1180  -1091       O  
HETATM 2544  O   HOH A 888      62.831  22.797  11.174  1.00 27.99           O  
ANISOU 2544  O   HOH A 888     1805   4585   4243    769    474     22       O  
HETATM 2545  O   HOH A 889      44.193  26.545   6.340  1.00  5.93           O  
ANISOU 2545  O   HOH A 889      666    941    646   -142     33     36       O  
HETATM 2546  O   HOH A 890      21.864  25.437  17.622  1.00 24.67           O  
ANISOU 2546  O   HOH A 890     2661   3312   3401    398   -568     16       O  
HETATM 2547  O   HOH A 891      21.611  23.620  35.078  1.00 35.52           O  
ANISOU 2547  O   HOH A 891     4791   4165   4537   -114    409    110       O  
HETATM 2548  O   HOH A 892      51.935  41.819  16.302  1.00 34.17           O  
ANISOU 2548  O   HOH A 892     4514   4145   4323   1068  -1121   -175       O  
HETATM 2549  O   HOH A 893      20.950  24.229  21.657  1.00 33.03           O  
ANISOU 2549  O   HOH A 893     3689   4370   4489   -919   -420    891       O  
HETATM 2550  O   HOH A 894      24.389  39.038  33.754  1.00 28.67           O  
ANISOU 2550  O   HOH A 894     3487   3540   3865    203    882  -1170       O  
HETATM 2551  O   HOH A 895      52.757  25.219   8.099  1.00 24.63           O  
ANISOU 2551  O   HOH A 895     3420   3874   2063   1996    146    -15       O  
HETATM 2552  O   HOH A 896      43.112  34.532  -1.430  1.00 42.44           O  
ANISOU 2552  O   HOH A 896     5566   4902   5654    192   -442    -70       O  
HETATM 2553  O   HOH A 897      29.061  31.867   2.923  1.00 30.18           O  
ANISOU 2553  O   HOH A 897     4273   3606   3587    349    -38   -273       O  
HETATM 2554  O   HOH A 898      21.305  28.395   3.121  1.00 28.52           O  
ANISOU 2554  O   HOH A 898     3783   4094   2958    636    284   -722       O  
HETATM 2555  O   HOH A 899      19.588   8.209   8.948  1.00 25.26           O  
ANISOU 2555  O   HOH A 899     3871   2953   2772   -165    104   -519       O  
HETATM 2556  O   HOH A 900      54.049  38.881  27.406  1.00 31.41           O  
ANISOU 2556  O   HOH A 900     3335   3551   5047    783   -238   -225       O  
HETATM 2557  O   HOH A 901      31.641  29.920  -1.844  1.00 28.57           O  
ANISOU 2557  O   HOH A 901     4425   4278   2149   -423   -221   -219       O  
HETATM 2558  O   HOH A 902      18.801  32.151   8.325  1.00 26.95           O  
ANISOU 2558  O   HOH A 902     2537   3836   3865    564   -162     59       O  
HETATM 2559  O   HOH A 903      58.374  22.128  18.693  1.00 26.58           O  
ANISOU 2559  O   HOH A 903     2973   2095   5031    493   -180   -205       O  
HETATM 2560  O   HOH A 904      51.967  17.265  29.271  1.00 33.39           O  
ANISOU 2560  O   HOH A 904     4673   4475   3539    -48   -441    618       O  
HETATM 2561  O   HOH A 905      31.789  12.647  32.154  1.00 30.15           O  
ANISOU 2561  O   HOH A 905     4420   3110   3925    -66   -633   -648       O  
HETATM 2562  O   HOH A 906      20.589   5.842   8.379  1.00 33.01           O  
ANISOU 2562  O   HOH A 906     4352   4095   4093    138    680   -272       O  
HETATM 2563  O   HOH A 907      22.153  17.902  22.163  1.00 30.75           O  
ANISOU 2563  O   HOH A 907     4304   3313   4065   -908    274    977       O  
HETATM 2564  O   HOH A 908      64.343  27.572  29.981  1.00 24.21           O  
ANISOU 2564  O   HOH A 908     3270   3120   2807    382    272     29       O  
HETATM 2565  O   HOH A 909      62.763  42.734  12.602  1.00 35.42           O  
ANISOU 2565  O   HOH A 909     4667   4331   4460   -669   -376   -635       O  
HETATM 2566  O   HOH A 910      58.712  44.835  16.217  1.00 39.96           O  
ANISOU 2566  O   HOH A 910     5745   4577   4860   -423    334    544       O  
HETATM 2567  O   HOH A 911      58.595  15.841   4.732  1.00 36.90           O  
ANISOU 2567  O   HOH A 911     4125   4941   4954     68   -183   -414       O  
HETATM 2568  O   HOH A 912      59.823  15.896   9.545  1.00 26.64           O  
ANISOU 2568  O   HOH A 912     4265   2926   2930   1719    746   -308       O  
HETATM 2569  O   HOH A 913      32.571  31.455  35.964  1.00 20.77           O  
ANISOU 2569  O   HOH A 913     2227   2848   2815     48   -336    274       O  
HETATM 2570  O   HOH A 914      32.282  20.774  18.922  1.00 23.77           O  
ANISOU 2570  O   HOH A 914     2559   3057   3412    -25    283    -23       O  
HETATM 2571  O   HOH A 915      41.522  22.667  35.995  1.00 28.37           O  
ANISOU 2571  O   HOH A 915     5459   3369   1951   1133   -119    578       O  
HETATM 2572  O   HOH A 916      21.366   5.375   5.849  1.00 27.01           O  
ANISOU 2572  O   HOH A 916     2475   3086   4700   -433    329   -810       O  
HETATM 2573  O   HOH A 917      56.894  23.833  37.535  1.00 42.79           O  
ANISOU 2573  O   HOH A 917     4976   5436   5844     34   -285    277       O  
HETATM 2574  O   HOH A 918      34.739  37.534  35.019  1.00 29.85           O  
ANISOU 2574  O   HOH A 918     4093   4274   2974    336   -840    -62       O  
HETATM 2575  O   HOH A 919      58.024  44.777   8.833  1.00 28.59           O  
ANISOU 2575  O   HOH A 919     3986   2944   3930   -164   -202   -240       O  
HETATM 2576  O   HOH A 920      25.504  16.006  14.921  1.00 19.07           O  
ANISOU 2576  O   HOH A 920     2547   2576   2123   -253    921   -128       O  
HETATM 2577  O   HOH A 921      64.972  35.188  13.990  1.00 26.90           O  
ANISOU 2577  O   HOH A 921     2186   4712   3322   -603   -368    -81       O  
HETATM 2578  O   HOH A 922      30.071  31.308  -0.884  1.00 32.80           O  
ANISOU 2578  O   HOH A 922     4562   4329   3569    450   -684    744       O  
HETATM 2579  O   HOH A 923      43.597  32.412  -5.696  1.00 38.82           O  
ANISOU 2579  O   HOH A 923     5240   4972   4536   -226    129    108       O  
HETATM 2580  O   HOH A 924      22.877  29.472  16.051  1.00 11.50           O  
ANISOU 2580  O   HOH A 924     1417   1176   1775    184    266    123       O  
HETATM 2581  O   HOH A 925      46.878  42.398   4.075  1.00 12.95           O  
ANISOU 2581  O   HOH A 925     1565   1299   2057    299    646    611       O  
HETATM 2582  O   HOH A 926      28.569  15.981  15.071  1.00 14.91           O  
ANISOU 2582  O   HOH A 926     1894   1684   2085   -179    193    120       O  
HETATM 2583  O   HOH A 927      40.282  23.184  20.626  1.00 13.91           O  
ANISOU 2583  O   HOH A 927     1852   1536   1896    -41    316    -70       O  
HETATM 2584  O   HOH A 928      29.397   8.068  10.931  1.00 27.00           O  
ANISOU 2584  O   HOH A 928     4479   2257   3521    477    813    -54       O  
HETATM 2585  O   HOH A 929      51.081  20.409  31.746  1.00 15.73           O  
ANISOU 2585  O   HOH A 929     2336   1210   2429    310    195     84       O  
HETATM 2586  O   HOH A 930      51.266  24.482  -2.961  1.00 28.66           O  
ANISOU 2586  O   HOH A 930     4579   2830   3479    522    114  -1017       O  
HETATM 2587  O   HOH A 931      59.120  46.278   3.983  1.00 23.56           O  
ANISOU 2587  O   HOH A 931     2922   2714   3315   -696   -897   1282       O  
HETATM 2588  O   HOH A 932      25.251  40.332  26.256  1.00 32.79           O  
ANISOU 2588  O   HOH A 932     3700   4729   4028    374    446    -53       O  
HETATM 2589  O   HOH A 933      48.001  38.515  -1.583  1.00 25.06           O  
ANISOU 2589  O   HOH A 933     3325   3087   3108  -1390   -551   -365       O  
HETATM 2590  O   HOH A 934      22.525  40.964  26.745  1.00 36.40           O  
ANISOU 2590  O   HOH A 934     4234   4058   5536    223    342    -73       O  
HETATM 2591  O   HOH A 935      59.889  44.197   5.600  1.00 26.57           O  
ANISOU 2591  O   HOH A 935     4709   2195   3190   -467  -1165      0       O  
HETATM 2592  O   HOH A 936      22.762  24.292  37.416  1.00 35.61           O  
ANISOU 2592  O   HOH A 936     4516   4576   4436    -58    897    182       O  
HETATM 2593  O   HOH A 937      22.233  23.679  -5.606  1.00 33.83           O  
ANISOU 2593  O   HOH A 937     4157   5022   3672    111    212   -272       O  
HETATM 2594  O   HOH A 938      15.954   9.146  15.144  1.00 40.23           O  
ANISOU 2594  O   HOH A 938     5144   4676   5462   -400   -116    708       O  
HETATM 2595  O   HOH A 939      26.733   1.174  -2.562  1.00 34.97           O  
ANISOU 2595  O   HOH A 939     4015   4252   5019   -440    274   -362       O  
HETATM 2596  O   HOH A 940      52.175  41.324  22.151  1.00 33.14           O  
ANISOU 2596  O   HOH A 940     4232   4168   4191   -200    490   -592       O  
HETATM 2597  O   HOH A 941      45.057  13.303  18.392  1.00 31.99           O  
ANISOU 2597  O   HOH A 941     4340   4137   3675   -943    605    569       O  
HETATM 2598  O   HOH A 942      47.583  44.846   5.544  1.00 28.65           O  
ANISOU 2598  O   HOH A 942     4042   2640   4203    733     19   1339       O  
CONECT  494  500                                                                
CONECT  500  494  501                                                           
CONECT  501  500  502  504                                                      
CONECT  502  501  503  508                                                      
CONECT  503  502                                                                
CONECT  504  501  505                                                           
CONECT  505  504  506                                                           
CONECT  506  505  507                                                           
CONECT  507  506                                                                
CONECT  508  502                                                                
CONECT 1698 1707                                                                
CONECT 1707 1698 1708                                                           
CONECT 1708 1707 1709 1711                                                      
CONECT 1709 1708 1710 1715                                                      
CONECT 1710 1709                                                                
CONECT 1711 1708 1712                                                           
CONECT 1712 1711 1713                                                           
CONECT 1713 1712 1714                                                           
CONECT 1714 1713                                                                
CONECT 1715 1709                                                                
CONECT 2086 2095                                                                
CONECT 2095 2086 2096                                                           
CONECT 2096 2095 2097 2099                                                      
CONECT 2097 2096 2098 2105                                                      
CONECT 2098 2097                                                                
CONECT 2099 2096 2100                                                           
CONECT 2100 2099 2101 2102                                                      
CONECT 2101 2100 2103                                                           
CONECT 2102 2100 2104                                                           
CONECT 2103 2101                                                                
CONECT 2104 2102                                                                
CONECT 2105 2097                                                                
CONECT 2123 2125 2130 2166 2172                                                 
CONECT 2123 2180 2182                                                           
CONECT 2124 2125 2126 2127 2131                                                 
CONECT 2125 2123 2124                                                           
CONECT 2126 2124                                                                
CONECT 2127 2124                                                                
CONECT 2128 2129 2130 2131 2135                                                 
CONECT 2129 2128                                                                
CONECT 2130 2123 2128                                                           
CONECT 2131 2124 2128                                                           
CONECT 2132 2133 2134 2135 2136                                                 
CONECT 2133 2132                                                                
CONECT 2134 2132                                                                
CONECT 2135 2128 2132                                                           
CONECT 2136 2132 2137                                                           
CONECT 2137 2136 2138                                                           
CONECT 2138 2137 2139 2140                                                      
CONECT 2139 2138 2144                                                           
CONECT 2140 2138 2141 2142                                                      
CONECT 2141 2140                                                                
CONECT 2142 2140 2143 2144                                                      
CONECT 2143 2142                                                                
CONECT 2144 2139 2142 2145                                                      
CONECT 2145 2144 2146 2154                                                      
CONECT 2146 2145 2147                                                           
CONECT 2147 2146 2148                                                           
CONECT 2148 2147 2149 2154                                                      
CONECT 2149 2148 2150 2151                                                      
CONECT 2150 2149                                                                
CONECT 2151 2149 2152                                                           
CONECT 2152 2151 2153                                                           
CONECT 2153 2152 2154                                                           
CONECT 2154 2145 2148 2153                                                      
CONECT 2166 2123                                                                
CONECT 2172 2123                                                                
CONECT 2180 2123                                                                
CONECT 2182 2123                                                                
MASTER      304    0    5   12   18    0    9    6 2591    1   69   22          
END