CNRS Nantes University UFIP UFIP
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***  6gha  ***

elNémo ID: 220107231334129920

Job options:

ID        	=	 220107231334129920
JOBID     	=	 6gha
USERID    	=	 foldyne
PRIVAT    	=	 0

NMODES    	=	 5
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER 6gha

HEADER    HYDROLASE                               06-MAY-18   6GHA              
TITLE     USP15 CATALYTIC DOMAIN STRUCTURE                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 15,UBIQUITIN         
COMPND   3 CARBOXYL-TERMINAL HYDROLASE 15;                                      
COMPND   4 CHAIN: A;                                                            
COMPND   5 SYNONYM: DEUBIQUITINATING ENZYME 15,UBIQUITIN THIOESTERASE 15,       
COMPND   6 UBIQUITIN-SPECIFIC-PROCESSING PROTEASE 15,UNPH-2,UNPH4,              
COMPND   7 DEUBIQUITINATING ENZYME 15,UBIQUITIN THIOESTERASE 15,UBIQUITIN-      
COMPND   8 SPECIFIC-PROCESSING PROTEASE 15,UNPH-2,UNPH4;                        
COMPND   9 EC: 3.4.19.12,3.4.19.12;                                             
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 OTHER_DETAILS: USP15 CATALYTIC CORE DOMAIN (D1D2) WITH THE INSERT    
COMPND  12 BETWEEN THE TWO SUB-DOMAINS HARBOURING A PREDICTED UBL DOMAIN        
COMPND  13 REPLACED BY A SHORT LINKER (BASED ON THE USP8 STRUCTURE PDB ID:      
COMPND  14 2GFO),USP15 CATALYTIC CORE DOMAIN (D1D2) WITH THE INSERT BETWEEN THE 
COMPND  15 TWO SUB-DOMAINS HARBOURING A PREDICTED UBL DOMAIN REPLACED BY A SHORT
COMPND  16 LINKER (BASED ON THE USP8 STRUCTURE PDB ID: 2GFO),USP15 CATALYTIC    
COMPND  17 CORE DOMAIN (D1D2) WITH THE INSERT BETWEEN THE TWO SUB-DOMAINS       
COMPND  18 HARBOURING A PREDICTED UBL DOMAIN REPLACED BY A SHORT LINKER (BASED  
COMPND  19 ON THE USP8 STRUCTURE PDB ID: 2GFO),USP15 CATALYTIC CORE DOMAIN      
COMPND  20 (D1D2) WITH THE INSERT BETWEEN THE TWO SUB-DOMAINS HARBOURING A      
COMPND  21 PREDICTED UBL DOMAIN REPLACED BY A SHORT LINKER (BASED ON THE USP8   
COMPND  22 STRUCTURE PDB ID: 2GFO)                                              
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: USP15, KIAA0529;                                               
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    PROTEASE, UBIQUITIN, UBIQUITIN SPECIFIC PROTEASE, HYDROLASE           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.J.WARD,H.E.GRATTON,S.G.CAULTON,J.EMSLEY,I.DREVENY                   
REVDAT   3   21-NOV-18 6GHA    1       JRNL                                     
REVDAT   2   03-OCT-18 6GHA    1       JRNL                                     
REVDAT   1   26-SEP-18 6GHA    0                                                
JRNL        AUTH   S.J.WARD,H.E.GRATTON,P.INDRAYUDHA,C.MICHAVILA,               
JRNL        AUTH 2 R.MUKHOPADHYAY,S.K.MAURER,S.G.CAULTON,J.EMSLEY,I.DREVENY     
JRNL        TITL   THE STRUCTURE OF THE DEUBIQUITINASE USP15 REVEALS A          
JRNL        TITL 2 MISALIGNED CATALYTIC TRIAD AND AN OPEN UBIQUITIN-BINDING     
JRNL        TITL 3 CHANNEL.                                                     
JRNL        REF    J. BIOL. CHEM.                V. 293 17362 2018              
JRNL        REFN                   ESSN 1083-351X                               
JRNL        PMID   30228188                                                     
JRNL        DOI    10.1074/JBC.RA118.003857                                     
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.98 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX                                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.98                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 35.25                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 24564                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.200                           
REMARK   3   R VALUE            (WORKING SET) : 0.198                           
REMARK   3   FREE R VALUE                     : 0.234                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.600                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1129                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 35.2535 -  3.9585    0.98     2985   161  0.1935 0.2102        
REMARK   3     2  3.9585 -  3.1426    0.98     2949   146  0.1736 0.2063        
REMARK   3     3  3.1426 -  2.7455    0.99     2970   131  0.1901 0.2412        
REMARK   3     4  2.7455 -  2.4946    0.99     2945   145  0.1962 0.2571        
REMARK   3     5  2.4946 -  2.3158    0.98     2924   133  0.2059 0.2668        
REMARK   3     6  2.3158 -  2.1793    0.97     2938   128  0.2132 0.2380        
REMARK   3     7  2.1793 -  2.0702    0.97     2872   132  0.2618 0.3624        
REMARK   3     8  2.0702 -  1.9801    0.96     2852   153  0.2967 0.3367        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.280            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.960           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 33.52                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 48.26                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :   NULL           NULL                                  
REMARK   3   ANGLE     :   NULL           NULL                                  
REMARK   3   CHIRALITY :   NULL           NULL                                  
REMARK   3   PLANARITY :   NULL           NULL                                  
REMARK   3   DIHEDRAL  :   NULL           NULL                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 255 THROUGH 400 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  21.4356   6.3308  16.6137              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1774 T22:   0.1676                                     
REMARK   3      T33:   0.2518 T12:  -0.0036                                     
REMARK   3      T13:  -0.0316 T23:   0.0427                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2381 L22:   3.7912                                     
REMARK   3      L33:   7.1093 L12:  -0.3506                                     
REMARK   3      L13:  -2.0473 L23:   2.0189                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0020 S12:  -0.0803 S13:   0.1566                       
REMARK   3      S21:  -0.0733 S22:   0.0186 S23:  -0.1911                       
REMARK   3      S31:  -0.2412 S32:   0.3516 S33:  -0.0270                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 401 THROUGH 912 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   8.3043  -3.0716   7.8706              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2686 T22:   0.2894                                     
REMARK   3      T33:   0.2519 T12:  -0.0169                                     
REMARK   3      T13:   0.0029 T23:  -0.0328                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0861 L22:   2.1355                                     
REMARK   3      L33:   5.1923 L12:  -0.2206                                     
REMARK   3      L13:  -1.5483 L23:   1.0195                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0547 S12:   0.4101 S13:  -0.1515                       
REMARK   3      S21:  -0.2888 S22:  -0.1567 S23:   0.2645                       
REMARK   3      S31:   0.2631 S32:  -0.8255 S33:   0.1697                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6GHA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 07-MAY-18.                  
REMARK 100 THE DEPOSITION ID IS D_1200009915.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-NOV-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : MASSIF-1                           
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.966                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 2M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS 0.6.2                      
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 24858                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.970                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 46.860                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.3                               
REMARK 200  DATA REDUNDANCY                : 3.000                              
REMARK 200  R MERGE                    (I) : 0.11100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 4.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.97                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.02                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 86.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.06000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 2Y6E                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.59                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS-CL PH 8.5, 20% PEG 2000,      
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293.15K                  
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       31.31050            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2                             
REMARK 350 SURFACE AREA OF THE COMPLEX: 15200 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL                          
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     MET A   254                                                      
REMARK 465     GLN A   343                                                      
REMARK 465     PHE A   344                                                      
REMARK 465     SER A   345                                                      
REMARK 465     GLY A   346                                                      
REMARK 465     TYR A   347                                                      
REMARK 465     GLN A   348                                                      
REMARK 465     GLN A   349                                                      
REMARK 465     GLN A   350                                                      
REMARK 465     ASP A   351                                                      
REMARK 465     CYS A   352                                                      
REMARK 465     GLN A   353                                                      
REMARK 465     SER A   753                                                      
REMARK 465     THR A   754                                                      
REMARK 465     TYR A   811                                                      
REMARK 465     SER A   812                                                      
REMARK 465     ARG A   813                                                      
REMARK 465     TYR A   814                                                      
REMARK 465     MET A   815                                                      
REMARK 465     ARG A   816                                                      
REMARK 465     MET A   858                                                      
REMARK 465     GLY A   859                                                      
REMARK 465     PHE A   913                                                      
REMARK 465     PRO A   914                                                      
REMARK 465     LEU A   915                                                      
REMARK 465     ASP A   916                                                      
REMARK 465     ARG A   917                                                      
REMARK 465     GLU A   918                                                      
REMARK 465     THR A   919                                                      
REMARK 465     ALA A   920                                                      
REMARK 465     ALA A   921                                                      
REMARK 465     ALA A   922                                                      
REMARK 465     LEU A   923                                                      
REMARK 465     GLU A   924                                                      
REMARK 465     HIS A   925                                                      
REMARK 465     HIS A   926                                                      
REMARK 465     HIS A   927                                                      
REMARK 465     HIS A   928                                                      
REMARK 465     HIS A   929                                                      
REMARK 465     HIS A   930                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A 421    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 775    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 776    CG   OD1  OD2                                       
REMARK 470     GLU A 785    CG   CD   OE1  OE2                                  
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    ASN A 267     -116.14     60.08                                   
REMARK 500    CYS A 269     -131.23     61.16                                   
REMARK 500    PRO A 330       38.61    -89.59                                   
REMARK 500    ASP A 880     -116.25     48.50                                   
REMARK 500    TYR A 897      -48.45   -131.00                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A1230        DISTANCE =  6.49 ANGSTROMS                       
REMARK 525    HOH A1231        DISTANCE =  6.83 ANGSTROMS                       
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                              ZN A1001  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 419   SG                                                     
REMARK 620 2 CYS A 422   SG  104.8                                              
REMARK 620 3 CYS A 780   SG  107.0 103.7                                        
REMARK 620 4 CYS A 783   SG  116.0 119.2 105.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1001                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 6GH9   RELATED DB: PDB                                   
DBREF  6GHA A  255   439  UNP    Q9Y4E8   UBP15_HUMAN    255    439             
DBREF  6GHA A  757   919  UNP    Q9Y4E8   UBP15_HUMAN    757    919             
SEQADV 6GHA MET A  254  UNP  Q9Y4E8              INITIATING METHIONINE          
SEQADV 6GHA ALA A  440  UNP  Q9Y4E8              LINKER                         
SEQADV 6GHA SER A  753  UNP  Q9Y4E8              LINKER                         
SEQADV 6GHA THR A  754  UNP  Q9Y4E8              LINKER                         
SEQADV 6GHA SER A  755  UNP  Q9Y4E8              LINKER                         
SEQADV 6GHA LYS A  756  UNP  Q9Y4E8              LINKER                         
SEQADV 6GHA ALA A  920  UNP  Q9Y4E8              EXPRESSION TAG                 
SEQADV 6GHA ALA A  921  UNP  Q9Y4E8              EXPRESSION TAG                 
SEQADV 6GHA ALA A  922  UNP  Q9Y4E8              EXPRESSION TAG                 
SEQADV 6GHA LEU A  923  UNP  Q9Y4E8              EXPRESSION TAG                 
SEQADV 6GHA GLU A  924  UNP  Q9Y4E8              EXPRESSION TAG                 
SEQADV 6GHA HIS A  925  UNP  Q9Y4E8              EXPRESSION TAG                 
SEQADV 6GHA HIS A  926  UNP  Q9Y4E8              EXPRESSION TAG                 
SEQADV 6GHA HIS A  927  UNP  Q9Y4E8              EXPRESSION TAG                 
SEQADV 6GHA HIS A  928  UNP  Q9Y4E8              EXPRESSION TAG                 
SEQADV 6GHA HIS A  929  UNP  Q9Y4E8              EXPRESSION TAG                 
SEQADV 6GHA HIS A  930  UNP  Q9Y4E8              EXPRESSION TAG                 
SEQRES   1 A  365  MET GLU GLN PRO GLY LEU CYS GLY LEU SER ASN LEU GLY          
SEQRES   2 A  365  ASN THR CYS PHE MET ASN SER ALA ILE GLN CYS LEU SER          
SEQRES   3 A  365  ASN THR PRO PRO LEU THR GLU TYR PHE LEU ASN ASP LYS          
SEQRES   4 A  365  TYR GLN GLU GLU LEU ASN PHE ASP ASN PRO LEU GLY MET          
SEQRES   5 A  365  ARG GLY GLU ILE ALA LYS SER TYR ALA GLU LEU ILE LYS          
SEQRES   6 A  365  GLN MET TRP SER GLY LYS PHE SER TYR VAL THR PRO ARG          
SEQRES   7 A  365  ALA PHE LYS THR GLN VAL GLY ARG PHE ALA PRO GLN PHE          
SEQRES   8 A  365  SER GLY TYR GLN GLN GLN ASP CYS GLN GLU LEU LEU ALA          
SEQRES   9 A  365  PHE LEU LEU ASP GLY LEU HIS GLU ASP LEU ASN ARG ILE          
SEQRES  10 A  365  ARG LYS LYS PRO TYR ILE GLN LEU LYS ASP ALA ASP GLY          
SEQRES  11 A  365  ARG PRO ASP LYS VAL VAL ALA GLU GLU ALA TRP GLU ASN          
SEQRES  12 A  365  HIS LEU LYS ARG ASN ASP SER ILE ILE VAL ASP ILE PHE          
SEQRES  13 A  365  HIS GLY LEU PHE LYS SER THR LEU VAL CYS PRO GLU CYS          
SEQRES  14 A  365  ALA LYS ILE SER VAL THR PHE ASP PRO PHE CYS TYR LEU          
SEQRES  15 A  365  THR LEU PRO LEU ALA SER THR SER LYS VAL LYS LEU LYS          
SEQRES  16 A  365  ASP CYS ILE GLU LEU PHE THR THR LYS GLU LYS LEU GLY          
SEQRES  17 A  365  ALA GLU ASP PRO TRP TYR CYS PRO ASN CYS LYS GLU HIS          
SEQRES  18 A  365  GLN GLN ALA THR LYS LYS LEU ASP LEU TRP SER LEU PRO          
SEQRES  19 A  365  PRO VAL LEU VAL VAL HIS LEU LYS ARG PHE SER TYR SER          
SEQRES  20 A  365  ARG TYR MET ARG ASP LYS LEU ASP THR LEU VAL ASP PHE          
SEQRES  21 A  365  PRO ILE ASN ASP LEU ASP MET SER GLU PHE LEU ILE ASN          
SEQRES  22 A  365  PRO ASN ALA GLY PRO CYS ARG TYR ASN LEU ILE ALA VAL          
SEQRES  23 A  365  SER ASN HIS TYR GLY GLY MET GLY GLY GLY HIS TYR THR          
SEQRES  24 A  365  ALA PHE ALA LYS ASN LYS ASP ASP GLY LYS TRP TYR TYR          
SEQRES  25 A  365  PHE ASP ASP SER SER VAL SER THR ALA SER GLU ASP GLN          
SEQRES  26 A  365  ILE VAL SER LYS ALA ALA TYR VAL LEU PHE TYR GLN ARG          
SEQRES  27 A  365  GLN ASP THR PHE SER GLY THR GLY PHE PHE PRO LEU ASP          
SEQRES  28 A  365  ARG GLU THR ALA ALA ALA LEU GLU HIS HIS HIS HIS HIS          
SEQRES  29 A  365  HIS                                                          
HET     ZN  A1001       1                                                       
HETNAM      ZN ZINC ION                                                         
FORMUL   2   ZN    ZN 2+                                                        
FORMUL   3  HOH   *131(H2 O)                                                    
HELIX    1 AA1 PHE A  270  ASN A  280  1                                  11    
HELIX    2 AA2 THR A  281  ASN A  290  1                                  10    
HELIX    3 AA3 TYR A  293  LEU A  297  5                                   5    
HELIX    4 AA4 GLY A  307  TRP A  321  1                                  15    
HELIX    5 AA5 PRO A  330  ALA A  341  1                                  12    
HELIX    6 AA6 LEU A  355  LEU A  367  1                                  13    
HELIX    7 AA7 PRO A  385  ASN A  401  1                                  17    
HELIX    8 AA8 SER A  403  HIS A  410  1                                   8    
HELIX    9 AA9 LEU A  759  THR A  767  1                                   9    
HELIX   10 AB1 SER A  833  LEU A  836  5                                   4    
HELIX   11 AB2 SER A  887  ILE A  891  5                                   5    
HELIX   12 AB3 ASP A  905  PHE A  907  5                                   3    
SHEET    1 AA1 2 GLY A 261  LEU A 262  0                                        
SHEET    2 AA1 2 TYR A 327  VAL A 328  1  O  VAL A 328   N  GLY A 261           
SHEET    1 AA2 4 ILE A 425  PHE A 432  0                                        
SHEET    2 AA2 4 GLY A 411  VAL A 418 -1  N  SER A 415   O  THR A 428           
SHEET    3 AA2 4 THR A 790  SER A 797 -1  O  ASP A 794   N  LYS A 414           
SHEET    4 AA2 4 GLU A 770  LYS A 771 -1  N  GLU A 770   O  LYS A 791           
SHEET    1 AA3 5 LEU A 435  LEU A 437  0                                        
SHEET    2 AA3 5 VAL A 801  LEU A 806  1  O  HIS A 805   N  LEU A 437           
SHEET    3 AA3 5 ALA A 896  ARG A 903 -1  O  LEU A 899   N  VAL A 804           
SHEET    4 AA3 5 ARG A 845  TYR A 855 -1  N  ILE A 849   O  PHE A 900           
SHEET    5 AA3 5 LEU A 830  ASP A 831 -1  N  LEU A 830   O  TYR A 846           
SHEET    1 AA4 7 LEU A 435  LEU A 437  0                                        
SHEET    2 AA4 7 VAL A 801  LEU A 806  1  O  HIS A 805   N  LEU A 437           
SHEET    3 AA4 7 ALA A 896  ARG A 903 -1  O  LEU A 899   N  VAL A 804           
SHEET    4 AA4 7 ARG A 845  TYR A 855 -1  N  ILE A 849   O  PHE A 900           
SHEET    5 AA4 7 HIS A 862  LYS A 868 -1  O  HIS A 862   N  TYR A 855           
SHEET    6 AA4 7 TRP A 875  ASP A 879 -1  O  PHE A 878   N  ALA A 865           
SHEET    7 AA4 7 SER A 882  THR A 885 -1  O  SER A 882   N  ASP A 879           
SHEET    1 AA5 2 LYS A 756  LYS A 758  0                                        
SHEET    2 AA5 2 LEU A 822  ASP A 824  1  O  ASP A 824   N  VAL A 757           
SHEET    1 AA6 2 TRP A 778  CYS A 780  0                                        
SHEET    2 AA6 2 GLU A 785  GLN A 787 -1  O  GLU A 785   N  CYS A 780           
LINK         SG  CYS A 419                ZN    ZN A1001     1555   1555  2.46  
LINK         SG  CYS A 422                ZN    ZN A1001     1555   1555  2.27  
LINK         SG  CYS A 780                ZN    ZN A1001     1555   1555  2.41  
LINK         SG  CYS A 783                ZN    ZN A1001     1555   1555  2.64  
SITE     1 AC1  4 CYS A 419  CYS A 422  CYS A 780  CYS A 783                    
CRYST1   48.505   62.621   62.043  90.00 104.97  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      0.020616  0.000000  0.005511        0.00000                         
SCALE2      0.000000  0.015969  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016684        0.00000                         
ATOM      1  N   GLU A 255      13.194   0.680  41.950  1.00 66.32           N  
ANISOU    1  N   GLU A 255    12660   7059   5478     22   1631    313       N  
ATOM      2  CA  GLU A 255      12.580   0.673  40.627  1.00 64.62           C  
ANISOU    2  CA  GLU A 255    12141   6829   5581   -167   1775    244       C  
ATOM      3  C   GLU A 255      13.285  -0.299  39.678  1.00 70.60           C  
ANISOU    3  C   GLU A 255    12900   7515   6410    -16   1645    401       C  
ATOM      4  O   GLU A 255      14.514  -0.392  39.673  1.00 76.21           O  
ANISOU    4  O   GLU A 255    13640   8329   6986    276   1311    530       O  
ATOM      5  CB  GLU A 255      12.588   2.086  40.037  1.00 70.38           C  
ANISOU    5  CB  GLU A 255    12458   7788   6494   -217   1616     90       C  
ATOM      6  CG  GLU A 255      11.441   2.964  40.507  1.00 71.85           C  
ANISOU    6  CG  GLU A 255    12517   8005   6779   -425   1868   -131       C  
ATOM      7  CD  GLU A 255      10.120   2.561  39.884  1.00 77.03           C  
ANISOU    7  CD  GLU A 255    12977   8594   7698   -679   2234   -253       C  
ATOM      8  OE1 GLU A 255       9.070   3.063  40.333  1.00 86.18           O  
ANISOU    8  OE1 GLU A 255    14032   9784   8927   -838   2493   -439       O  
ATOM      9  OE2 GLU A 255      10.132   1.741  38.939  1.00 81.73           O  
ANISOU    9  OE2 GLU A 255    13487   9129   8440   -718   2251   -183       O  
ATOM     10  N   GLN A 256      12.514  -1.022  38.872  1.00 61.72           N  
ANISOU   10  N   GLN A 256    11702   6240   5509   -217   1899    358       N  
ATOM     11  CA  GLN A 256      13.141  -1.981  37.972  1.00 51.26           C  
ANISOU   11  CA  GLN A 256    10396   4824   4257    -82   1802    478       C  
ATOM     12  C   GLN A 256      13.758  -1.252  36.781  1.00 45.58           C  
ANISOU   12  C   GLN A 256     9315   4311   3695    -12   1542    509       C  
ATOM     13  O   GLN A 256      13.088  -0.434  36.144  1.00 41.91           O  
ANISOU   13  O   GLN A 256     8424   3973   3527   -207   1556    339       O  
ATOM     14  CB  GLN A 256      12.153  -3.026  37.482  1.00 56.89           C  
ANISOU   14  CB  GLN A 256    11163   5315   5138   -342   2144    382       C  
ATOM     15  CG  GLN A 256      12.766  -3.924  36.422  1.00 61.17           C  
ANISOU   15  CG  GLN A 256    11694   5778   5769   -220   2054    466       C  
ATOM     16  CD  GLN A 256      11.900  -5.107  36.061  1.00 75.37           C  
ANISOU   16  CD  GLN A 256    13634   7342   7660   -461   2384    343       C  
ATOM     17  OE1 GLN A 256      11.015  -5.499  36.822  1.00 86.10           O  
ANISOU   17  OE1 GLN A 256    15210   8546   8960   -665   2673    229       O  
ATOM     18  NE2 GLN A 256      12.155  -5.691  34.896  1.00 68.49           N  
ANISOU   18  NE2 GLN A 256    12650   6449   6925   -453   2348    346       N  
ATOM     19  N   PRO A 257      15.032  -1.499  36.485  1.00 47.10           N  
ANISOU   19  N   PRO A 257     9505   4575   3817    295   1223    655       N  
ATOM     20  CA  PRO A 257      15.659  -0.862  35.322  1.00 43.31           C  
ANISOU   20  CA  PRO A 257     8551   4296   3609    351    928    624       C  
ATOM     21  C   PRO A 257      14.837  -1.056  34.056  1.00 42.03           C  
ANISOU   21  C   PRO A 257     8117   4068   3784    111   1096    528       C  
ATOM     22  O   PRO A 257      14.278  -2.126  33.814  1.00 42.44           O  
ANISOU   22  O   PRO A 257     8408   3901   3817    -11   1381    555       O  
ATOM     23  CB  PRO A 257      17.007  -1.577  35.230  1.00 38.93           C  
ANISOU   23  CB  PRO A 257     8153   3767   2871    712    690    812       C  
ATOM     24  CG  PRO A 257      17.330  -1.883  36.678  1.00 42.93           C  
ANISOU   24  CG  PRO A 257     8972   4265   3073    891    660    849       C  
ATOM     25  CD  PRO A 257      16.002  -2.249  37.300  1.00 48.33           C  
ANISOU   25  CD  PRO A 257     9929   4701   3734    621   1060    776       C  
ATOM     26  N   GLY A 258      14.754   0.008  33.251  1.00 33.09           N  
ANISOU   26  N   GLY A 258     6507   3124   2939     35    924    404       N  
ATOM     27  CA  GLY A 258      13.991  -0.015  32.023  1.00 29.13           C  
ANISOU   27  CA  GLY A 258     5707   2626   2734   -154   1021    299       C  
ATOM     28  C   GLY A 258      12.515   0.268  32.185  1.00 37.34           C  
ANISOU   28  C   GLY A 258     6632   3670   3885   -421   1294    113       C  
ATOM     29  O   GLY A 258      11.867   0.676  31.208  1.00 33.10           O  
ANISOU   29  O   GLY A 258     5732   3243   3601   -532   1286    -16       O  
ATOM     30  N   LEU A 259      11.961   0.077  33.392  1.00 32.07           N  
ANISOU   30  N   LEU A 259     6254   2911   3021   -510   1535     84       N  
ATOM     31  CA  LEU A 259      10.567   0.414  33.677  1.00 38.48           C  
ANISOU   31  CA  LEU A 259     6921   3769   3929   -758   1816   -123       C  
ATOM     32  C   LEU A 259      10.473   1.883  34.092  1.00 38.61           C  
ANISOU   32  C   LEU A 259     6705   3955   4009   -674   1663   -222       C  
ATOM     33  O   LEU A 259      10.121   2.246  35.217  1.00 41.63           O  
ANISOU   33  O   LEU A 259     7256   4324   4239   -707   1803   -280       O  
ATOM     34  CB  LEU A 259      10.001  -0.512  34.751  1.00 38.27           C  
ANISOU   34  CB  LEU A 259     7348   3543   3651   -927   2207   -119       C  
ATOM     35  CG  LEU A 259      10.011  -2.004  34.402  1.00 37.65           C  
ANISOU   35  CG  LEU A 259     7573   3227   3505  -1027   2406    -44       C  
ATOM     36  CD1 LEU A 259       9.162  -2.821  35.387  1.00 41.47           C  
ANISOU   36  CD1 LEU A 259     8341   3523   3893  -1204   2704   -156       C  
ATOM     37  CD2 LEU A 259       9.535  -2.232  32.974  1.00 43.16           C  
ANISOU   37  CD2 LEU A 259     7907   4010   4483  -1205   2432   -163       C  
ATOM     38  N   CYS A 260      10.832   2.734  33.147  1.00 32.73           N  
ANISOU   38  N   CYS A 260     5613   3345   3477   -562   1386   -239       N  
ATOM     39  CA  CYS A 260      11.020   4.149  33.405  1.00 33.77           C  
ANISOU   39  CA  CYS A 260     5592   3580   3659   -453   1211   -303       C  
ATOM     40  C   CYS A 260      10.274   4.934  32.338  1.00 40.35           C  
ANISOU   40  C   CYS A 260     6018   4537   4777   -451   1170   -433       C  
ATOM     41  O   CYS A 260      10.446   4.682  31.138  1.00 30.73           O  
ANISOU   41  O   CYS A 260     4613   3356   3706   -429   1050   -394       O  
ATOM     42  CB  CYS A 260      12.519   4.495  33.430  1.00 27.97           C  
ANISOU   42  CB  CYS A 260     4937   2861   2827   -281    888   -166       C  
ATOM     43  SG  CYS A 260      12.891   6.249  33.639  1.00 33.34           S  
ANISOU   43  SG  CYS A 260     5475   3625   3566   -213    693   -267       S  
ATOM     44  N   GLY A 261       9.412   5.849  32.781  1.00 30.82           N  
ANISOU   44  N   GLY A 261     4692   3393   3625   -447   1280   -591       N  
ATOM     45  CA  GLY A 261       8.615   6.643  31.872  1.00 28.93           C  
ANISOU   45  CA  GLY A 261     4090   3284   3617   -369   1243   -716       C  
ATOM     46  C   GLY A 261       9.372   7.842  31.340  1.00 30.64           C  
ANISOU   46  C   GLY A 261     4259   3477   3907   -183    975   -658       C  
ATOM     47  O   GLY A 261      10.540   8.077  31.641  1.00 32.47           O  
ANISOU   47  O   GLY A 261     4683   3622   4032   -158    816   -549       O  
ATOM     48  N   LEU A 262       8.680   8.620  30.518  1.00 28.05           N  
ANISOU   48  N   LEU A 262     3672   3235   3750    -50    934   -744       N  
ATOM     49  CA  LEU A 262       9.249   9.835  29.950  1.00 28.64           C  
ANISOU   49  CA  LEU A 262     3756   3239   3887    124    739   -695       C  
ATOM     50  C   LEU A 262       8.236  10.957  30.064  1.00 28.57           C  
ANISOU   50  C   LEU A 262     3642   3260   3952    310    827   -841       C  
ATOM     51  O   LEU A 262       7.105  10.819  29.585  1.00 34.40           O  
ANISOU   51  O   LEU A 262     4101   4174   4796    396    901   -953       O  
ATOM     52  CB  LEU A 262       9.627   9.629  28.480  1.00 29.19           C  
ANISOU   52  CB  LEU A 262     3682   3345   4065    181    555   -595       C  
ATOM     53  CG  LEU A 262      10.674   8.562  28.214  1.00 28.27           C  
ANISOU   53  CG  LEU A 262     3656   3195   3889     48    466   -453       C  
ATOM     54  CD1 LEU A 262      10.652   8.204  26.733  1.00 28.69           C  
ANISOU   54  CD1 LEU A 262     3527   3320   4053     90    354   -404       C  
ATOM     55  CD2 LEU A 262      12.058   9.062  28.618  1.00 26.90           C  
ANISOU   55  CD2 LEU A 262     3687   2912   3621     38    329   -360       C  
ATOM     56  N   SER A 263       8.635  12.074  30.668  1.00 29.19           N  
ANISOU   56  N   SER A 263     3935   3184   3972    384    820   -858       N  
ATOM     57  CA  SER A 263       7.688  13.171  30.814  1.00 37.87           C  
ANISOU   57  CA  SER A 263     4988   4273   5129    610    926   -993       C  
ATOM     58  C   SER A 263       7.371  13.792  29.458  1.00 41.54           C  
ANISOU   58  C   SER A 263     5301   4760   5722    876    791   -955       C  
ATOM     59  O   SER A 263       8.168  13.744  28.524  1.00 37.69           O  
ANISOU   59  O   SER A 263     4857   4210   5256    861    615   -814       O  
ATOM     60  CB  SER A 263       8.228  14.235  31.774  1.00 51.50           C  
ANISOU   60  CB  SER A 263     7041   5783   6742    606    973  -1033       C  
ATOM     61  OG  SER A 263       9.486  14.742  31.343  1.00 56.92           O  
ANISOU   61  OG  SER A 263     7924   6303   7402    547    797   -920       O  
ATOM     62  N   ASN A 264       6.181  14.365  29.352  1.00 51.14           N  
ANISOU   62  N   ASN A 264     6340   6084   7007   1144    880  -1086       N  
ATOM     63  CA  ASN A 264       5.766  15.052  28.140  1.00 59.20           C  
ANISOU   63  CA  ASN A 264     7251   7138   8104   1486    746  -1053       C  
ATOM     64  C   ASN A 264       6.267  16.488  28.210  1.00 55.80           C  
ANISOU   64  C   ASN A 264     7203   6376   7624   1677    745   -998       C  
ATOM     65  O   ASN A 264       5.759  17.293  28.995  1.00 62.01           O  
ANISOU   65  O   ASN A 264     8108   7069   8385   1832    903  -1116       O  
ATOM     66  CB  ASN A 264       4.251  15.004  27.998  1.00 66.21           C  
ANISOU   66  CB  ASN A 264     7743   8343   9069   1735    826  -1239       C  
ATOM     67  CG  ASN A 264       3.776  15.579  26.682  1.00 75.28           C  
ANISOU   67  CG  ASN A 264     8750   9595  10258   2140    642  -1201       C  
ATOM     68  OD1 ASN A 264       4.551  16.168  25.936  1.00 82.61           O  
ANISOU   68  OD1 ASN A 264     9955  10288  11146   2248    498  -1025       O  
ATOM     69  ND2 ASN A 264       2.494  15.405  26.387  1.00 74.79           N  
ANISOU   69  ND2 ASN A 264     8253   9907  10257   2366    652  -1379       N  
ATOM     70  N   LEU A 265       7.269  16.810  27.391  1.00 65.19           N  
ANISOU   70  N   LEU A 265     8608   7370   8792   1644    600   -833       N  
ATOM     71  CA  LEU A 265       7.749  18.189  27.354  1.00 66.56           C  
ANISOU   71  CA  LEU A 265     9191   7189   8910   1783    638   -790       C  
ATOM     72  C   LEU A 265       6.692  19.119  26.775  1.00 76.47           C  
ANISOU   72  C   LEU A 265    10453   8420  10182   2291    659   -816       C  
ATOM     73  O   LEU A 265       6.569  20.280  27.181  1.00 82.60           O  
ANISOU   73  O   LEU A 265    11522   8947  10914   2435    776   -848       O  
ATOM     74  CB  LEU A 265       9.038  18.283  26.541  1.00 65.93           C  
ANISOU   74  CB  LEU A 265     9325   6924   8803   1598    516   -626       C  
ATOM     75  CG  LEU A 265      10.125  17.304  27.003  1.00 60.56           C  
ANISOU   75  CG  LEU A 265     8587   6323   8099   1166    459   -598       C  
ATOM     76  CD1 LEU A 265      11.367  17.479  26.162  1.00 64.23           C  
ANISOU   76  CD1 LEU A 265     9218   6640   8548   1005    363   -468       C  
ATOM     77  CD2 LEU A 265      10.443  17.503  28.478  1.00 69.95           C  
ANISOU   77  CD2 LEU A 265     9936   7435   9205    957    580   -720       C  
ATOM     78  N   GLY A 266       5.904  18.620  25.845  1.00 75.88           N  
ANISOU   78  N   GLY A 266    10029   8642  10158   2526    529   -805       N  
ATOM     79  CA  GLY A 266       4.952  19.453  25.157  1.00 77.50           C  
ANISOU   79  CA  GLY A 266    10170   8918  10358   2877    472   -771       C  
ATOM     80  C   GLY A 266       4.926  19.125  23.683  1.00 86.32           C  
ANISOU   80  C   GLY A 266    11153  10194  11451   2965    253   -630       C  
ATOM     81  O   GLY A 266       5.866  19.452  22.950  1.00 87.04           O  
ANISOU   81  O   GLY A 266    11550  10046  11476   2888    185   -461       O  
ATOM     82  N   ASN A 267       3.850  18.461  23.249  1.00 89.35           N  
ANISOU   82  N   ASN A 267    11079  10997  11873   3082    158   -718       N  
ATOM     83  CA  ASN A 267       3.700  17.950  21.885  1.00 84.66           C  
ANISOU   83  CA  ASN A 267    10303  10629  11233   3125    -57   -633       C  
ATOM     84  C   ASN A 267       4.845  16.975  21.670  1.00 79.13           C  
ANISOU   84  C   ASN A 267     9644   9866  10558   2806   -103   -566       C  
ATOM     85  O   ASN A 267       4.889  15.951  22.379  1.00 82.42           O  
ANISOU   85  O   ASN A 267     9822  10437  11058   2580    -36   -702       O  
ATOM     86  CB  ASN A 267       3.635  19.117  20.894  1.00 87.86           C  
ANISOU   86  CB  ASN A 267    11013  10867  11504   3419   -151   -472       C  
ATOM     87  CG  ASN A 267       2.446  20.001  21.122  1.00 91.74           C  
ANISOU   87  CG  ASN A 267    11440  11453  11966   3779   -119   -550       C  
ATOM     88  OD1 ASN A 267       1.320  19.525  21.253  1.00 95.26           O  
ANISOU   88  OD1 ASN A 267    11448  12287  12461   3872   -152   -713       O  
ATOM     89  ND2 ASN A 267       2.681  21.305  21.161  1.00 95.05           N  
ANISOU   89  ND2 ASN A 267    12300  11521  12295   3971    -43   -447       N  
ATOM     90  N   THR A 268       5.769  17.239  20.746  1.00 80.98           N  
ANISOU   90  N   THR A 268    10171   9882  10715   2769   -196   -376       N  
ATOM     91  CA  THR A 268       6.926  16.419  20.393  1.00 74.14           C  
ANISOU   91  CA  THR A 268     9374   8934   9862   2496   -249   -290       C  
ATOM     92  C   THR A 268       6.527  15.142  19.661  1.00 72.02           C  
ANISOU   92  C   THR A 268     8705   9042   9618   2407   -389   -348       C  
ATOM     93  O   THR A 268       7.377  14.239  19.524  1.00 70.40           O  
ANISOU   93  O   THR A 268     8491   8816   9440   2101   -407   -303       O  
ATOM     94  CB  THR A 268       7.794  16.047  21.601  1.00 70.22           C  
ANISOU   94  CB  THR A 268     8980   8272   9428   2133   -110   -328       C  
ATOM     95  OG1 THR A 268       7.104  15.107  22.421  1.00 74.18           O  
ANISOU   95  OG1 THR A 268     9128   9053  10003   1976    -44   -494       O  
ATOM     96  CG2 THR A 268       8.132  17.295  22.432  1.00 72.00           C  
ANISOU   96  CG2 THR A 268     9596   8142   9620   2189     42   -326       C  
ATOM     97  N   CYS A 269       5.289  15.030  19.179  1.00 73.61           N  
ANISOU   97  N   CYS A 269     8598   9578   9792   2565   -467   -446       N  
ATOM     98  CA  CYS A 269       4.879  13.967  18.251  1.00 75.09           C  
ANISOU   98  CA  CYS A 269     8469  10105   9958   2459   -604   -509       C  
ATOM     99  C   CYS A 269       5.081  12.618  18.956  1.00 61.45           C  
ANISOU   99  C   CYS A 269     6476   8519   8353   2114   -520   -653       C  
ATOM    100  O   CYS A 269       4.665  12.459  20.106  1.00 68.52           O  
ANISOU  100  O   CYS A 269     7222   9475   9337   2036   -364   -806       O  
ATOM    101  CB  CYS A 269       5.618  14.140  16.942  1.00 82.22           C  
ANISOU  101  CB  CYS A 269     9627  10870  10740   2492   -733   -319       C  
ATOM    102  SG  CYS A 269       4.663  15.013  15.670  1.00 96.46           S  
ANISOU  102  SG  CYS A 269    11328  12952  12369   2786   -919   -332       S  
ATOM    103  N   PHE A 270       5.723  11.632  18.330  1.00 51.97           N  
ANISOU  103  N   PHE A 270     5237   7355   7153   1890   -588   -619       N  
ATOM    104  CA  PHE A 270       5.846  10.350  19.008  1.00 49.36           C  
ANISOU  104  CA  PHE A 270     4768   7085   6900   1454   -443   -718       C  
ATOM    105  C   PHE A 270       7.246  10.120  19.549  1.00 36.53           C  
ANISOU  105  C   PHE A 270     3487   5111   5282   1185   -352   -544       C  
ATOM    106  O   PHE A 270       7.672   8.975  19.673  1.00 37.53           O  
ANISOU  106  O   PHE A 270     3601   5236   5424    879   -286   -548       O  
ATOM    107  CB  PHE A 270       5.371   9.188  18.125  1.00 64.15           C  
ANISOU  107  CB  PHE A 270     6346   9268   8761   1290   -516   -849       C  
ATOM    108  CG  PHE A 270       6.358   8.639  17.135  1.00 51.99           C  
ANISOU  108  CG  PHE A 270     4994   7602   7160   1157   -608   -697       C  
ATOM    109  CD1 PHE A 270       6.890   9.425  16.145  1.00 58.24           C  
ANISOU  109  CD1 PHE A 270     6034   8234   7862   1396   -753   -506       C  
ATOM    110  CD2 PHE A 270       6.667   7.282  17.154  1.00 48.51           C  
ANISOU  110  CD2 PHE A 270     4487   7206   6739    793   -522   -767       C  
ATOM    111  CE1 PHE A 270       7.768   8.880  15.214  1.00 60.63           C  
ANISOU  111  CE1 PHE A 270     6487   8446   8104   1263   -811   -389       C  
ATOM    112  CE2 PHE A 270       7.539   6.730  16.226  1.00 58.08           C  
ANISOU  112  CE2 PHE A 270     5860   8315   7893    690   -589   -649       C  
ATOM    113  CZ  PHE A 270       8.092   7.535  15.254  1.00 56.11           C  
ANISOU  113  CZ  PHE A 270     5822   7934   7563    924   -736   -464       C  
ATOM    114  N   MET A 271       7.927  11.196  19.975  1.00 36.72           N  
ANISOU  114  N   MET A 271     3816   4850   5287   1298   -331   -416       N  
ATOM    115  CA  MET A 271       9.295  11.026  20.449  1.00 32.06           C  
ANISOU  115  CA  MET A 271     3492   3999   4690   1050   -275   -285       C  
ATOM    116  C   MET A 271       9.361  10.055  21.624  1.00 28.98           C  
ANISOU  116  C   MET A 271     3049   3636   4326    770   -134   -358       C  
ATOM    117  O   MET A 271      10.161   9.122  21.602  1.00 29.38           O  
ANISOU  117  O   MET A 271     3157   3644   4363    557   -125   -292       O  
ATOM    118  CB  MET A 271       9.916  12.356  20.851  1.00 37.08           C  
ANISOU  118  CB  MET A 271     4439   4354   5297   1154   -244   -200       C  
ATOM    119  CG  MET A 271      11.427  12.224  21.071  1.00 45.50           C  
ANISOU  119  CG  MET A 271     5719   5225   6344    897   -228    -89       C  
ATOM    120  SD  MET A 271      12.215  13.702  21.768  1.00 60.46           S  
ANISOU  120  SD  MET A 271     7967   6806   8200    886   -147    -61       S  
ATOM    121  CE  MET A 271      11.301  13.870  23.300  1.00 59.87           C  
ANISOU  121  CE  MET A 271     7836   6774   8135    919    -25   -219       C  
ATOM    122  N   ASN A 272       8.545  10.256  22.671  1.00 31.29           N  
ANISOU  122  N   ASN A 272     3264   3988   4638    790     -6   -491       N  
ATOM    123  CA  ASN A 272       8.598   9.335  23.811  1.00 26.74           C  
ANISOU  123  CA  ASN A 272     2707   3408   4044    528    155   -546       C  
ATOM    124  C   ASN A 272       8.292   7.905  23.381  1.00 24.67           C  
ANISOU  124  C   ASN A 272     2284   3295   3794    324    201   -601       C  
ATOM    125  O   ASN A 272       8.956   6.950  23.812  1.00 26.64           O  
ANISOU  125  O   ASN A 272     2685   3443   3995    115    275   -537       O  
ATOM    126  CB  ASN A 272       7.619   9.791  24.906  1.00 26.96           C  
ANISOU  126  CB  ASN A 272     2665   3498   4081    583    318   -703       C  
ATOM    127  CG  ASN A 272       8.094  11.046  25.614  1.00 31.25           C  
ANISOU  127  CG  ASN A 272     3462   3826   4584    708    325   -657       C  
ATOM    128  OD1 ASN A 272       9.214  11.520  25.383  1.00 30.89           O  
ANISOU  128  OD1 ASN A 272     3644   3589   4504    698    223   -521       O  
ATOM    129  ND2 ASN A 272       7.261  11.578  26.496  1.00 28.27           N  
ANISOU  129  ND2 ASN A 272     3050   3483   4208    798    471   -796       N  
ATOM    130  N   SER A 273       7.276   7.746  22.529  1.00 28.40           N  
ANISOU  130  N   SER A 273     2463   4016   4313    394    159   -733       N  
ATOM    131  CA  SER A 273       6.914   6.425  22.021  1.00 27.47           C  
ANISOU  131  CA  SER A 273     2191   4047   4202    160    217   -831       C  
ATOM    132  C   SER A 273       8.087   5.776  21.294  1.00 29.72           C  
ANISOU  132  C   SER A 273     2674   4172   4447     69    127   -659       C  
ATOM    133  O   SER A 273       8.401   4.591  21.503  1.00 23.86           O  
ANISOU  133  O   SER A 273     2039   3351   3674   -171    251   -653       O  
ATOM    134  CB  SER A 273       5.714   6.569  21.081  1.00 34.02           C  
ANISOU  134  CB  SER A 273     2637   5222   5067    288    123  -1020       C  
ATOM    135  OG  SER A 273       5.340   5.332  20.530  1.00 39.60           O  
ANISOU  135  OG  SER A 273     3186   6088   5771     19    181  -1156       O  
ATOM    136  N   ALA A 274       8.772   6.559  20.460  1.00 27.78           N  
ANISOU  136  N   ALA A 274     2513   3853   4188    268    -61   -517       N  
ATOM    137  CA  ALA A 274       9.925   6.042  19.720  1.00 25.26           C  
ANISOU  137  CA  ALA A 274     2359   3404   3836    199   -133   -366       C  
ATOM    138  C   ALA A 274      11.094   5.720  20.643  1.00 22.09           C  
ANISOU  138  C   ALA A 274     2204   2785   3404     88    -60   -240       C  
ATOM    139  O   ALA A 274      11.785   4.704  20.463  1.00 34.24           O  
ANISOU  139  O   ALA A 274     3844   4253   4911    -32    -25   -178       O  
ATOM    140  CB  ALA A 274      10.346   7.071  18.676  1.00 32.29           C  
ANISOU  140  CB  ALA A 274     3305   4258   4704    424   -308   -255       C  
ATOM    141  N   ILE A 275      11.339   6.575  21.634  1.00 25.88           N  
ANISOU  141  N   ILE A 275     2789   3170   3875    150    -42   -210       N  
ATOM    142  CA  ILE A 275      12.416   6.318  22.580  1.00 22.41           C  
ANISOU  142  CA  ILE A 275     2552   2589   3375     67     -8   -117       C  
ATOM    143  C   ILE A 275      12.138   5.036  23.336  1.00 24.76           C  
ANISOU  143  C   ILE A 275     2913   2879   3617    -88    152   -156       C  
ATOM    144  O   ILE A 275      13.054   4.269  23.634  1.00 25.71           O  
ANISOU  144  O   ILE A 275     3199   2906   3662   -129    163    -57       O  
ATOM    145  CB  ILE A 275      12.601   7.513  23.532  1.00 24.20           C  
ANISOU  145  CB  ILE A 275     2877   2737   3579    134    -13   -124       C  
ATOM    146  CG1 ILE A 275      13.101   8.727  22.742  1.00 24.69           C  
ANISOU  146  CG1 ILE A 275     2978   2729   3673    253   -130    -65       C  
ATOM    147  CG2 ILE A 275      13.556   7.177  24.705  1.00 22.64           C  
ANISOU  147  CG2 ILE A 275     2859   2465   3279     47     10    -71       C  
ATOM    148  CD1 ILE A 275      13.027  10.017  23.538  1.00 22.73           C  
ANISOU  148  CD1 ILE A 275     2849   2377   3409    317   -100   -110       C  
ATOM    149  N   GLN A 276      10.872   4.773  23.667  1.00 28.39           N  
ANISOU  149  N   GLN A 276     3256   3434   4099   -168    296   -306       N  
ATOM    150  CA  GLN A 276      10.577   3.555  24.411  1.00 26.44           C  
ANISOU  150  CA  GLN A 276     3135   3133   3779   -359    509   -348       C  
ATOM    151  C   GLN A 276      10.800   2.316  23.547  1.00 30.68           C  
ANISOU  151  C   GLN A 276     3717   3634   4307   -475    546   -327       C  
ATOM    152  O   GLN A 276      11.280   1.286  24.031  1.00 26.17           O  
ANISOU  152  O   GLN A 276     3404   2904   3636   -558    671   -254       O  
ATOM    153  CB  GLN A 276       9.149   3.596  24.945  1.00 25.80           C  
ANISOU  153  CB  GLN A 276     2891   3183   3730   -468    698   -552       C  
ATOM    154  CG  GLN A 276       8.950   4.692  26.071  1.00 25.91           C  
ANISOU  154  CG  GLN A 276     2939   3185   3721   -359    726   -578       C  
ATOM    155  CD  GLN A 276       9.671   4.352  27.393  1.00 30.29           C  
ANISOU  155  CD  GLN A 276     3836   3557   4115   -415    822   -475       C  
ATOM    156  OE1 GLN A 276      10.418   3.382  27.459  1.00 33.71           O  
ANISOU  156  OE1 GLN A 276     4489   3868   4452   -473    838   -356       O  
ATOM    157  NE2 GLN A 276       9.448   5.163  28.438  1.00 28.02           N  
ANISOU  157  NE2 GLN A 276     3611   3257   3776   -365    878   -523       N  
ATOM    158  N   CYS A 277      10.428   2.382  22.267  1.00 27.95           N  
ANISOU  158  N   CYS A 277     3155   3425   4042   -464    447   -394       N  
ATOM    159  CA  CYS A 277      10.753   1.249  21.393  1.00 24.21           C  
ANISOU  159  CA  CYS A 277     2755   2898   3546   -574    479   -380       C  
ATOM    160  C   CYS A 277      12.272   1.050  21.273  1.00 25.60           C  
ANISOU  160  C   CYS A 277     3155   2903   3668   -447    382   -169       C  
ATOM    161  O   CYS A 277      12.769  -0.082  21.355  1.00 30.70           O  
ANISOU  161  O   CYS A 277     4024   3399   4242   -507    495   -111       O  
ATOM    162  CB  CYS A 277      10.115   1.441  20.019  1.00 21.50           C  
ANISOU  162  CB  CYS A 277     2141   2764   3265   -569    359   -499       C  
ATOM    163  SG  CYS A 277       8.274   1.443  20.092  1.00 37.24           S  
ANISOU  163  SG  CYS A 277     3778   5059   5312   -728    472   -811       S  
ATOM    164  N   LEU A 278      13.026   2.140  21.106  1.00 24.56           N  
ANISOU  164  N   LEU A 278     2975   2792   3563   -268    193    -66       N  
ATOM    165  CA  LEU A 278      14.489   2.028  20.974  1.00 17.14           C  
ANISOU  165  CA  LEU A 278     2170   1760   2584   -163    102     93       C  
ATOM    166  C   LEU A 278      15.134   1.591  22.278  1.00 18.65           C  
ANISOU  166  C   LEU A 278     2571   1848   2667   -128    161    172       C  
ATOM    167  O   LEU A 278      16.093   0.807  22.286  1.00 25.72           O  
ANISOU  167  O   LEU A 278     3613   2670   3491    -51    160    272       O  
ATOM    168  CB  LEU A 278      15.094   3.366  20.507  1.00 23.68           C  
ANISOU  168  CB  LEU A 278     2897   2638   3462    -47    -70    146       C  
ATOM    169  CG  LEU A 278      14.730   3.868  19.096  1.00 28.16           C  
ANISOU  169  CG  LEU A 278     3334   3283   4084    -11   -156    119       C  
ATOM    170  CD1 LEU A 278      15.196   5.309  18.928  1.00 25.78           C  
ANISOU  170  CD1 LEU A 278     3030   2961   3803     90   -262    173       C  
ATOM    171  CD2 LEU A 278      15.282   2.975  17.976  1.00 33.93           C  
ANISOU  171  CD2 LEU A 278     4093   4002   4797    -35   -154    157       C  
ATOM    172  N   SER A 279      14.597   2.062  23.402  1.00 26.55           N  
ANISOU  172  N   SER A 279     3603   2853   3633   -154    214    126       N  
ATOM    173  CA  SER A 279      15.108   1.673  24.711  1.00 21.33           C  
ANISOU  173  CA  SER A 279     3174   2109   2822   -108    264    196       C  
ATOM    174  C   SER A 279      14.958   0.182  24.942  1.00 21.48           C  
ANISOU  174  C   SER A 279     3449   1979   2733   -163    458    230       C  
ATOM    175  O   SER A 279      15.799  -0.439  25.599  1.00 26.26           O  
ANISOU  175  O   SER A 279     4299   2494   3184    -29    456    350       O  
ATOM    176  CB  SER A 279      14.373   2.460  25.811  1.00 23.24           C  
ANISOU  176  CB  SER A 279     3416   2378   3036   -154    322    113       C  
ATOM    177  OG  SER A 279      14.571   1.862  27.093  1.00 29.30           O  
ANISOU  177  OG  SER A 279     4461   3054   3616   -140    423    165       O  
ATOM    178  N   ASN A 280      13.876  -0.405  24.439  1.00 25.57           N  
ANISOU  178  N   ASN A 280     3933   2472   3311   -354    636    113       N  
ATOM    179  CA  ASN A 280      13.616  -1.827  24.572  1.00 24.87           C  
ANISOU  179  CA  ASN A 280     4132   2196   3123   -475    882    112       C  
ATOM    180  C   ASN A 280      14.031  -2.600  23.315  1.00 27.79           C  
ANISOU  180  C   ASN A 280     4513   2510   3534   -473    872    131       C  
ATOM    181  O   ASN A 280      13.522  -3.698  23.048  1.00 31.27           O  
ANISOU  181  O   ASN A 280     5134   2807   3939   -654   1101     60       O  
ATOM    182  CB  ASN A 280      12.151  -2.031  24.942  1.00 27.51           C  
ANISOU  182  CB  ASN A 280     4428   2544   3479   -756   1136    -77       C  
ATOM    183  CG  ASN A 280      11.839  -1.447  26.318  1.00 26.47           C  
ANISOU  183  CG  ASN A 280     4374   2421   3264   -744   1200    -82       C  
ATOM    184  OD1 ASN A 280      12.064  -2.095  27.325  1.00 30.90           O  
ANISOU  184  OD1 ASN A 280     5304   2799   3639   -735   1358      6       O  
ATOM    185  ND2 ASN A 280      11.405  -0.200  26.354  1.00 24.18           N  
ANISOU  185  ND2 ASN A 280     3777   2325   3084   -706   1071   -168       N  
ATOM    186  N   THR A 281      14.980  -2.051  22.569  1.00 25.83           N  
ANISOU  186  N   THR A 281     4105   2359   3349   -292    638    213       N  
ATOM    187  CA  THR A 281      15.738  -2.789  21.560  1.00 24.62           C  
ANISOU  187  CA  THR A 281     4022   2138   3196   -213    622    272       C  
ATOM    188  C   THR A 281      17.032  -3.255  22.218  1.00 22.84           C  
ANISOU  188  C   THR A 281     4031   1812   2834     57    578    448       C  
ATOM    189  O   THR A 281      17.953  -2.450  22.382  1.00 25.10           O  
ANISOU  189  O   THR A 281     4160   2245   3132    232    368    518       O  
ATOM    190  CB  THR A 281      16.016  -1.900  20.344  1.00 25.56           C  
ANISOU  190  CB  THR A 281     3833   2435   3444   -176    421    249       C  
ATOM    191  OG1 THR A 281      14.776  -1.479  19.760  1.00 25.21           O  
ANISOU  191  OG1 THR A 281     3575   2515   3487   -359    432     89       O  
ATOM    192  CG2 THR A 281      16.861  -2.651  19.276  1.00 26.56           C  
ANISOU  192  CG2 THR A 281     4032   2498   3560    -92    424    302       C  
ATOM    193  N   PRO A 282      17.129  -4.522  22.624  1.00 26.93           N  
ANISOU  193  N   PRO A 282     4931   2095   3208    103    777    511       N  
ATOM    194  CA  PRO A 282      18.214  -4.951  23.532  1.00 36.68           C  
ANISOU  194  CA  PRO A 282     6423   3254   4258    426    726    683       C  
ATOM    195  C   PRO A 282      19.615  -4.675  23.004  1.00 42.31           C  
ANISOU  195  C   PRO A 282     6942   4134   4999    711    493    765       C  
ATOM    196  O   PRO A 282      20.463  -4.226  23.782  1.00 29.61           O  
ANISOU  196  O   PRO A 282     5273   2675   3302    935    311    839       O  
ATOM    197  CB  PRO A 282      17.966  -6.457  23.694  1.00 34.36           C  
ANISOU  197  CB  PRO A 282     6523   2712   3820    408    990    678       C  
ATOM    198  CG  PRO A 282      16.490  -6.591  23.545  1.00 43.94           C  
ANISOU  198  CG  PRO A 282     7756   3835   5102      7   1225    512       C  
ATOM    199  CD  PRO A 282      16.101  -5.575  22.476  1.00 32.97           C  
ANISOU  199  CD  PRO A 282     5944   2643   3939   -159   1084    408       C  
ATOM    200  N   PRO A 283      19.945  -4.985  21.737  1.00 40.24           N  
ANISOU  200  N   PRO A 283     6582   3870   4836    713    502    740       N  
ATOM    201  CA  PRO A 283      21.335  -4.738  21.298  1.00 38.55           C  
ANISOU  201  CA  PRO A 283     6166   3838   4643    981    315    802       C  
ATOM    202  C   PRO A 283      21.724  -3.263  21.354  1.00 29.44           C  
ANISOU  202  C   PRO A 283     4617   2976   3595    930     82    755       C  
ATOM    203  O   PRO A 283      22.874  -2.940  21.691  1.00 33.53           O  
ANISOU  203  O   PRO A 283     4982   3687   4069   1142    -83    792       O  
ATOM    204  CB  PRO A 283      21.361  -5.267  19.855  1.00 43.18           C  
ANISOU  204  CB  PRO A 283     6735   4350   5321    914    417    753       C  
ATOM    205  CG  PRO A 283      20.175  -6.118  19.725  1.00 47.42           C  
ANISOU  205  CG  PRO A 283     7559   4628   5830    678    665    686       C  
ATOM    206  CD  PRO A 283      19.139  -5.567  20.647  1.00 34.13           C  
ANISOU  206  CD  PRO A 283     5859   2963   4144    471    683    633       C  
ATOM    207  N   LEU A 284      20.779  -2.359  21.098  1.00 21.75           N  
ANISOU  207  N   LEU A 284     3483   2040   2740    661     74    661       N  
ATOM    208  CA  LEU A 284      21.085  -0.929  21.166  1.00 20.92           C  
ANISOU  208  CA  LEU A 284     3090   2141   2720    601   -103    617       C  
ATOM    209  C   LEU A 284      21.344  -0.485  22.615  1.00 33.01           C  
ANISOU  209  C   LEU A 284     4653   3753   4138    680   -200    634       C  
ATOM    210  O   LEU A 284      22.395   0.108  22.934  1.00 31.28           O  
ANISOU  210  O   LEU A 284     4262   3729   3893    778   -362    628       O  
ATOM    211  CB  LEU A 284      19.943  -0.145  20.510  1.00 20.38           C  
ANISOU  211  CB  LEU A 284     2904   2062   2777    364    -75    526       C  
ATOM    212  CG  LEU A 284      20.227   1.346  20.282  1.00 28.18           C  
ANISOU  212  CG  LEU A 284     3667   3186   3852    302   -210    488       C  
ATOM    213  CD1 LEU A 284      21.399   1.484  19.334  1.00 25.92           C  
ANISOU  213  CD1 LEU A 284     3249   2993   3607    357   -263    510       C  
ATOM    214  CD2 LEU A 284      19.019   2.115  19.773  1.00 29.20           C  
ANISOU  214  CD2 LEU A 284     3732   3297   4066    160   -193    416       C  
ATOM    215  N   THR A 285      20.425  -0.829  23.523  1.00 37.59           N  
ANISOU  215  N   THR A 285     5456   4198   4627    626    -90    639       N  
ATOM    216  CA  THR A 285      20.597  -0.438  24.921  1.00 27.47           C  
ANISOU  216  CA  THR A 285     4252   2983   3203    697   -169    652       C  
ATOM    217  C   THR A 285      21.854  -1.067  25.528  1.00 31.90           C  
ANISOU  217  C   THR A 285     4906   3638   3578   1012   -287    748       C  
ATOM    218  O   THR A 285      22.587  -0.403  26.261  1.00 33.61           O  
ANISOU  218  O   THR A 285     4994   4067   3712   1098   -473    721       O  
ATOM    219  CB  THR A 285      19.336  -0.799  25.715  1.00 35.52           C  
ANISOU  219  CB  THR A 285     5526   3825   4147    568     25    635       C  
ATOM    220  OG1 THR A 285      18.292   0.126  25.384  1.00 31.16           O  
ANISOU  220  OG1 THR A 285     4787   3298   3755    332     64    514       O  
ATOM    221  CG2 THR A 285      19.598  -0.726  27.206  1.00 32.75           C  
ANISOU  221  CG2 THR A 285     5363   3503   3576    691    -25    678       C  
ATOM    222  N  AGLU A 286      22.119  -2.343  25.227  0.50 34.69           N  
ANISOU  222  N  AGLU A 286     5484   3846   3851   1202   -184    845       N  
ATOM    223  N  BGLU A 286      22.124  -2.344  25.232  0.50 34.70           N  
ANISOU  223  N  BGLU A 286     5486   3848   3850   1204   -185    846       N  
ATOM    224  CA AGLU A 286      23.338  -2.982  25.716  0.50 37.89           C  
ANISOU  224  CA AGLU A 286     5950   4367   4079   1561   -303    926       C  
ATOM    225  CA BGLU A 286      23.346  -2.964  25.740  0.50 37.94           C  
ANISOU  225  CA BGLU A 286     5954   4378   4082   1563   -308    926       C  
ATOM    226  C  AGLU A 286      24.587  -2.271  25.203  0.50 36.98           C  
ANISOU  226  C  AGLU A 286     5410   4586   4054   1655   -528    863       C  
ATOM    227  C  BGLU A 286      24.590  -2.254  25.211  0.50 36.86           C  
ANISOU  227  C  BGLU A 286     5392   4575   4039   1655   -531    862       C  
ATOM    228  O  AGLU A 286      25.576  -2.136  25.933  0.50 36.16           O  
ANISOU  228  O  AGLU A 286     5169   4734   3836   1819   -700    829       O  
ATOM    229  O  BGLU A 286      25.580  -2.105  25.937  0.50 36.33           O  
ANISOU  229  O  BGLU A 286     5184   4761   3860   1816   -704    827       O  
ATOM    230  CB AGLU A 286      23.356  -4.456  25.311  0.50 41.62           C  
ANISOU  230  CB AGLU A 286     6685   4623   4507   1654   -101    965       C  
ATOM    231  CB BGLU A 286      23.394  -4.449  25.372  0.50 41.88           C  
ANISOU  231  CB BGLU A 286     6717   4665   4530   1665   -109    966       C  
ATOM    232  CG AGLU A 286      22.424  -5.331  26.137  0.50 45.82           C  
ANISOU  232  CG AGLU A 286     7651   4876   4882   1593    127    996       C  
ATOM    233  CG BGLU A 286      22.215  -5.277  25.873  0.50 45.61           C  
ANISOU  233  CG BGLU A 286     7607   4819   4903   1526    158    985       C  
ATOM    234  CD AGLU A 286      22.221  -6.714  25.544  0.50 45.10           C  
ANISOU  234  CD AGLU A 286     7835   4537   4763   1600    371    997       C  
ATOM    235  CD BGLU A 286      22.513  -6.082  27.116  0.50 51.82           C  
ANISOU  235  CD BGLU A 286     8706   5549   5433   1744    196   1036       C  
ATOM    236  OE1AGLU A 286      21.533  -7.532  26.187  0.50 55.10           O  
ANISOU  236  OE1AGLU A 286     9473   5574   5888   1543    588    998       O  
ATOM    237  OE1BGLU A 286      22.997  -5.500  28.109  0.50 57.38           O  
ANISOU  237  OE1BGLU A 286     9341   6445   6017   1880      9   1052       O  
ATOM    238  OE2AGLU A 286      22.737  -6.985  24.441  0.50 44.31           O  
ANISOU  238  OE2AGLU A 286     7599   4466   4769   1651    363    983       O  
ATOM    239  OE2BGLU A 286      22.252  -7.304  27.099  0.50 59.02           O  
ANISOU  239  OE2BGLU A 286     9955   6222   6248   1778    421   1049       O  
ATOM    240  N   TYR A 287      24.569  -1.825  23.942  1.00 40.22           N  
ANISOU  240  N   TYR A 287     5584   5019   4681   1479   -496    801       N  
ATOM    241  CA  TYR A 287      25.708  -1.078  23.408  1.00 48.47           C  
ANISOU  241  CA  TYR A 287     6225   6370   5822   1486   -651    713       C  
ATOM    242  C   TYR A 287      25.976   0.175  24.237  1.00 35.48           C  
ANISOU  242  C   TYR A 287     4366   4957   4157   1346   -821    604       C  
ATOM    243  O   TYR A 287      27.127   0.474  24.578  1.00 38.89           O  
ANISOU  243  O   TYR A 287     4539   5709   4526   1466   -996    531       O  
ATOM    244  CB  TYR A 287      25.440  -0.736  21.939  1.00 44.50           C  
ANISOU  244  CB  TYR A 287     5583   5792   5532   1254   -539    665       C  
ATOM    245  CG  TYR A 287      26.437   0.159  21.227  1.00 35.04           C  
ANISOU  245  CG  TYR A 287     4013   4849   4452   1156   -618    561       C  
ATOM    246  CD1 TYR A 287      27.566  -0.366  20.605  1.00 35.14           C  
ANISOU  246  CD1 TYR A 287     3852   5028   4472   1352   -624    551       C  
ATOM    247  CD2 TYR A 287      26.206   1.521  21.114  1.00 35.38           C  
ANISOU  247  CD2 TYR A 287     3907   4938   4596    857   -645    466       C  
ATOM    248  CE1 TYR A 287      28.456   0.454  19.913  1.00 29.36           C  
ANISOU  248  CE1 TYR A 287     2777   4530   3851   1207   -644    433       C  
ATOM    249  CE2 TYR A 287      27.087   2.346  20.433  1.00 37.78           C  
ANISOU  249  CE2 TYR A 287     3931   5427   4996    713   -659    364       C  
ATOM    250  CZ  TYR A 287      28.208   1.810  19.841  1.00 34.93           C  
ANISOU  250  CZ  TYR A 287     3372   5253   4645    865   -652    341       C  
ATOM    251  OH  TYR A 287      29.065   2.651  19.167  1.00 43.07           O  
ANISOU  251  OH  TYR A 287     4123   6472   5770    670   -621    217       O  
ATOM    252  N   PHE A 288      24.921   0.886  24.621  1.00 26.99           N  
ANISOU  252  N   PHE A 288     3395   3741   3119   1098   -767    572       N  
ATOM    253  CA  PHE A 288      25.144   2.107  25.405  1.00 30.67           C  
ANISOU  253  CA  PHE A 288     3707   4386   3559    946   -900    452       C  
ATOM    254  C   PHE A 288      25.461   1.834  26.875  1.00 37.67           C  
ANISOU  254  C   PHE A 288     4718   5404   4189   1147  -1037    466       C  
ATOM    255  O   PHE A 288      26.355   2.477  27.445  1.00 35.90           O  
ANISOU  255  O   PHE A 288     4273   5482   3885   1149  -1224    348       O  
ATOM    256  CB  PHE A 288      23.944   3.040  25.277  1.00 31.28           C  
ANISOU  256  CB  PHE A 288     3853   4271   3760    656   -789    403       C  
ATOM    257  CG  PHE A 288      23.855   3.684  23.934  1.00 30.48           C  
ANISOU  257  CG  PHE A 288     3600   4118   3863    472   -719    365       C  
ATOM    258  CD1 PHE A 288      24.774   4.641  23.564  1.00 29.58           C  
ANISOU  258  CD1 PHE A 288     3250   4173   3816    337   -784    260       C  
ATOM    259  CD2 PHE A 288      22.884   3.297  23.021  1.00 35.28           C  
ANISOU  259  CD2 PHE A 288     4313   4520   4571    425   -579    422       C  
ATOM    260  CE1 PHE A 288      24.711   5.236  22.308  1.00 32.81           C  
ANISOU  260  CE1 PHE A 288     3590   4500   4377    176   -691    243       C  
ATOM    261  CE2 PHE A 288      22.817   3.883  21.779  1.00 37.57           C  
ANISOU  261  CE2 PHE A 288     4500   4773   5003    296   -532    399       C  
ATOM    262  CZ  PHE A 288      23.746   4.859  21.422  1.00 32.84           C  
ANISOU  262  CZ  PHE A 288     3722   4300   4455    182   -580    325       C  
ATOM    263  N   LEU A 289      24.769   0.886  27.515  1.00 37.66           N  
ANISOU  263  N   LEU A 289     5081   5194   4033   1303   -941    593       N  
ATOM    264  CA  LEU A 289      25.041   0.635  28.935  1.00 36.73           C  
ANISOU  264  CA  LEU A 289     5148   5184   3624   1515  -1065    624       C  
ATOM    265  C   LEU A 289      26.429   0.048  29.151  1.00 43.15           C  
ANISOU  265  C   LEU A 289     5812   6260   4321   1810  -1224    623       C  
ATOM    266  O   LEU A 289      27.021   0.244  30.218  1.00 47.66           O  
ANISOU  266  O   LEU A 289     6349   7047   4712   1900  -1379    563       O  
ATOM    267  CB  LEU A 289      23.979  -0.298  29.532  1.00 35.33           C  
ANISOU  267  CB  LEU A 289     5453   4673   3298   1581   -858    763       C  
ATOM    268  CG  LEU A 289      22.511   0.135  29.443  1.00 34.72           C  
ANISOU  268  CG  LEU A 289     5488   4340   3365   1237   -630    717       C  
ATOM    269  CD1 LEU A 289      21.625  -0.951  30.061  1.00 37.39           C  
ANISOU  269  CD1 LEU A 289     6297   4380   3530   1291   -393    833       C  
ATOM    270  CD2 LEU A 289      22.284   1.454  30.139  1.00 36.21           C  
ANISOU  270  CD2 LEU A 289     5546   4654   3559   1034   -714    579       C  
ATOM    271  N   ASN A 290      26.964  -0.678  28.169  1.00 44.12           N  
ANISOU  271  N   ASN A 290     5841   6356   4565   1917  -1151    659       N  
ATOM    272  CA  ASN A 290      28.326  -1.194  28.269  1.00 44.84           C  
ANISOU  272  CA  ASN A 290     5748   6696   4593   2158  -1259    619       C  
ATOM    273  C   ASN A 290      29.373  -0.183  27.815  1.00 42.98           C  
ANISOU  273  C   ASN A 290     5010   6832   4487   2019  -1417    438       C  
ATOM    274  O   ASN A 290      30.552  -0.546  27.717  1.00 45.18           O  
ANISOU  274  O   ASN A 290     5076   7348   4744   2197  -1490    379       O  
ATOM    275  CB  ASN A 290      28.478  -2.481  27.447  1.00 50.21           C  
ANISOU  275  CB  ASN A 290     6585   7180   5313   2351  -1091    718       C  
ATOM    276  CG  ASN A 290      27.744  -3.660  28.058  1.00 52.59           C  
ANISOU  276  CG  ASN A 290     7396   7149   5439   2504   -917    856       C  
ATOM    277  OD1 ASN A 290      27.860  -3.933  29.256  1.00 61.00           O  
ANISOU  277  OD1 ASN A 290     8653   8245   6279   2673   -976    884       O  
ATOM    278  ND2 ASN A 290      26.993  -4.377  27.232  1.00 54.03           N  
ANISOU  278  ND2 ASN A 290     7808   7009   5711   2429   -686    925       N  
ATOM    279  N   ASP A 291      28.965   1.054  27.507  1.00 45.93           N  
ANISOU  279  N   ASP A 291     5203   7256   4992   1698  -1444    336       N  
ATOM    280  CA  ASP A 291      29.883   2.137  27.164  1.00 46.59           C  
ANISOU  280  CA  ASP A 291     4850   7661   5193   1469  -1543    128       C  
ATOM    281  C   ASP A 291      30.666   1.861  25.883  1.00 45.17           C  
ANISOU  281  C   ASP A 291     4421   7556   5186   1482  -1458    100       C  
ATOM    282  O   ASP A 291      31.794   2.332  25.729  1.00 52.87           O  
ANISOU  282  O   ASP A 291     5049   8833   6206   1393  -1518    -67       O  
ATOM    283  CB  ASP A 291      30.855   2.422  28.313  1.00 44.93           C  
ANISOU  283  CB  ASP A 291     4479   7781   4812   1524  -1731     -8       C  
ATOM    284  CG  ASP A 291      30.163   3.017  29.513  1.00 50.82           C  
ANISOU  284  CG  ASP A 291     5417   8499   5393   1423  -1818    -36       C  
ATOM    285  OD1 ASP A 291      29.535   4.080  29.350  1.00 45.96           O  
ANISOU  285  OD1 ASP A 291     4771   7827   4866   1104  -1792   -131       O  
ATOM    286  OD2 ASP A 291      30.230   2.411  30.605  1.00 62.63           O  
ANISOU  286  OD2 ASP A 291     7119  10019   6658   1668  -1898     32       O  
ATOM    287  N   LYS A 292      30.098   1.101  24.953  1.00 39.92           N  
ANISOU  287  N   LYS A 292     3935   6622   4610   1576  -1300    243       N  
ATOM    288  CA  LYS A 292      30.830   0.848  23.718  1.00 41.57           C  
ANISOU  288  CA  LYS A 292     3926   6905   4965   1589  -1208    208       C  
ATOM    289  C   LYS A 292      30.803   2.039  22.767  1.00 41.68           C  
ANISOU  289  C   LYS A 292     3676   6989   5172   1226  -1146     86       C  
ATOM    290  O   LYS A 292      31.550   2.039  21.785  1.00 63.67           O  
ANISOU  290  O   LYS A 292     6234   9888   8069   1180  -1060     19       O  
ATOM    291  CB  LYS A 292      30.279  -0.403  23.025  1.00 40.52           C  
ANISOU  291  CB  LYS A 292     4097   6457   4841   1797  -1044    381       C  
ATOM    292  CG  LYS A 292      30.456  -1.670  23.870  1.00 55.70           C  
ANISOU  292  CG  LYS A 292     6308   8294   6563   2140  -1053    484       C  
ATOM    293  CD  LYS A 292      29.998  -2.918  23.141  1.00 63.00           C  
ANISOU  293  CD  LYS A 292     7550   8895   7492   2290   -855    614       C  
ATOM    294  CE  LYS A 292      30.903  -3.232  21.963  1.00 69.03           C  
ANISOU  294  CE  LYS A 292     8089   9776   8364   2372   -790    561       C  
ATOM    295  NZ  LYS A 292      32.239  -3.708  22.414  1.00 77.03           N  
ANISOU  295  NZ  LYS A 292     8933  11075   9259   2664   -896    502       N  
ATOM    296  N   TYR A 293      29.990   3.059  23.049  1.00 46.38           N  
ANISOU  296  N   TYR A 293     4334   7490   5798    944  -1152     48       N  
ATOM    297  CA  TYR A 293      29.812   4.183  22.133  1.00 39.47           C  
ANISOU  297  CA  TYR A 293     3391   6504   5103    540  -1004    -39       C  
ATOM    298  C   TYR A 293      30.929   5.219  22.224  1.00 40.02           C  
ANISOU  298  C   TYR A 293     3090   6915   5203    277  -1051   -279       C  
ATOM    299  O   TYR A 293      31.108   5.989  21.273  1.00 42.81           O  
ANISOU  299  O   TYR A 293     3372   7202   5691    -27   -887   -354       O  
ATOM    300  CB  TYR A 293      28.465   4.872  22.395  1.00 35.98           C  
ANISOU  300  CB  TYR A 293     3259   5725   4689    335   -934     15       C  
ATOM    301  CG  TYR A 293      28.353   5.512  23.773  1.00 40.45           C  
ANISOU  301  CG  TYR A 293     3854   6382   5132    262  -1065    -76       C  
ATOM    302  CD1 TYR A 293      28.066   4.745  24.901  1.00 39.58           C  
ANISOU  302  CD1 TYR A 293     3904   6293   4841    527  -1183      3       C  
ATOM    303  CD2 TYR A 293      28.516   6.885  23.938  1.00 40.67           C  
ANISOU  303  CD2 TYR A 293     3805   6444   5205    -81  -1044   -245       C  
ATOM    304  CE1 TYR A 293      27.965   5.327  26.158  1.00 38.82           C  
ANISOU  304  CE1 TYR A 293     3858   6287   4604    461  -1298    -87       C  
ATOM    305  CE2 TYR A 293      28.415   7.479  25.191  1.00 42.51           C  
ANISOU  305  CE2 TYR A 293     4086   6754   5312   -164  -1152   -352       C  
ATOM    306  CZ  TYR A 293      28.139   6.699  26.295  1.00 47.36           C  
ANISOU  306  CZ  TYR A 293     4831   7423   5742    111  -1289   -274       C  
ATOM    307  OH  TYR A 293      28.035   7.289  27.537  1.00 52.69           O  
ANISOU  307  OH  TYR A 293     5576   8179   6265     28  -1391   -386       O  
ATOM    308  N   GLN A 294      31.671   5.269  23.338  1.00 43.25           N  
ANISOU  308  N   GLN A 294     3351   7605   5478    354  -1224   -394       N  
ATOM    309  CA  GLN A 294      32.701   6.298  23.488  1.00 47.33           C  
ANISOU  309  CA  GLN A 294     3604   8359   6022     40  -1213   -635       C  
ATOM    310  C   GLN A 294      33.800   6.151  22.443  1.00 52.89           C  
ANISOU  310  C   GLN A 294     4040   9223   6832      1  -1088   -715       C  
ATOM    311  O   GLN A 294      34.288   7.149  21.904  1.00 63.64           O  
ANISOU  311  O   GLN A 294     5269  10623   8289   -376   -942   -877       O  
ATOM    312  CB  GLN A 294      33.314   6.261  24.886  1.00 45.97           C  
ANISOU  312  CB  GLN A 294     3360   8440   5665    163  -1413   -732       C  
ATOM    313  CG  GLN A 294      32.507   6.974  25.940  1.00 59.11           C  
ANISOU  313  CG  GLN A 294     5224  10007   7229     13  -1496   -767       C  
ATOM    314  CD  GLN A 294      31.643   6.018  26.714  1.00 61.89           C  
ANISOU  314  CD  GLN A 294     5868  10225   7422    375  -1610   -563       C  
ATOM    315  OE1 GLN A 294      31.268   4.965  26.201  1.00 64.68           O  
ANISOU  315  OE1 GLN A 294     6359  10423   7793    657  -1561   -367       O  
ATOM    316  NE2 GLN A 294      31.339   6.362  27.964  1.00 61.53           N  
ANISOU  316  NE2 GLN A 294     5956  10218   7205    358  -1734   -613       N  
ATOM    317  N   GLU A 295      34.215   4.922  22.150  1.00 45.90           N  
ANISOU  317  N   GLU A 295     3112   8410   5919    378  -1114   -608       N  
ATOM    318  CA  GLU A 295      35.279   4.735  21.166  1.00 48.96           C  
ANISOU  318  CA  GLU A 295     3235   8971   6396    362   -989   -698       C  
ATOM    319  C   GLU A 295      34.802   4.929  19.738  1.00 47.49           C  
ANISOU  319  C   GLU A 295     3114   8560   6368    173   -758   -638       C  
ATOM    320  O   GLU A 295      35.622   4.888  18.815  1.00 58.39           O  
ANISOU  320  O   GLU A 295     4300  10058   7826    105   -611   -719       O  
ATOM    321  CB  GLU A 295      35.910   3.349  21.303  1.00 60.13           C  
ANISOU  321  CB  GLU A 295     4607  10523   7718    842  -1075   -617       C  
ATOM    322  CG  GLU A 295      34.919   2.210  21.405  1.00 65.74           C  
ANISOU  322  CG  GLU A 295     5684  10931   8362   1194  -1098   -365       C  
ATOM    323  CD  GLU A 295      34.710   1.754  22.839  1.00 80.16           C  
ANISOU  323  CD  GLU A 295     7697  12772   9986   1448  -1289   -296       C  
ATOM    324  OE1 GLU A 295      33.881   2.364  23.552  1.00 74.94           O  
ANISOU  324  OE1 GLU A 295     7196  11996   9284   1291  -1352   -278       O  
ATOM    325  OE2 GLU A 295      35.391   0.791  23.255  1.00 79.15           O  
ANISOU  325  OE2 GLU A 295     7568  12777   9729   1811  -1367   -266       O  
ATOM    326  N   GLU A 296      33.504   5.136  19.534  1.00 37.00           N  
ANISOU  326  N   GLU A 296     2050   6933   5075     92   -718   -506       N  
ATOM    327  CA  GLU A 296      32.946   5.242  18.201  1.00 34.56           C  
ANISOU  327  CA  GLU A 296     1861   6390   4880    -52   -505   -424       C  
ATOM    328  C   GLU A 296      32.269   6.576  17.956  1.00 41.83           C  
ANISOU  328  C   GLU A 296     3019   7019   5856   -471   -373   -443       C  
ATOM    329  O   GLU A 296      31.760   6.794  16.855  1.00 35.32           O  
ANISOU  329  O   GLU A 296     2426   5905   5090   -587   -188   -346       O  
ATOM    330  CB  GLU A 296      31.964   4.095  17.947  1.00 38.61           C  
ANISOU  330  CB  GLU A 296     2716   6592   5361    279   -507   -180       C  
ATOM    331  CG  GLU A 296      32.616   2.741  18.180  1.00 45.74           C  
ANISOU  331  CG  GLU A 296     3482   7708   6187    733   -602   -141       C  
ATOM    332  CD  GLU A 296      31.910   1.619  17.468  1.00 47.18           C  
ANISOU  332  CD  GLU A 296     3988   7572   6366    964   -493     49       C  
ATOM    333  OE1 GLU A 296      30.661   1.558  17.519  1.00 44.16           O  
ANISOU  333  OE1 GLU A 296     3963   6844   5974    904   -467    178       O  
ATOM    334  OE2 GLU A 296      32.612   0.796  16.850  1.00 45.47           O  
ANISOU  334  OE2 GLU A 296     3656   7466   6154   1198   -421     45       O  
ATOM    335  N   LEU A 297      32.254   7.478  18.939  1.00 40.66           N  
ANISOU  335  N   LEU A 297     2848   6933   5668   -680   -459   -569       N  
ATOM    336  CA  LEU A 297      31.726   8.811  18.690  1.00 40.34           C  
ANISOU  336  CA  LEU A 297     3061   6597   5670  -1064   -300   -603       C  
ATOM    337  C   LEU A 297      32.495   9.452  17.541  1.00 36.86           C  
ANISOU  337  C   LEU A 297     2527   6170   5307  -1392    -41   -716       C  
ATOM    338  O   LEU A 297      33.726   9.420  17.514  1.00 40.76           O  
ANISOU  338  O   LEU A 297     2726   6960   5803  -1444    -17   -873       O  
ATOM    339  CB  LEU A 297      31.832   9.677  19.944  1.00 42.96           C  
ANISOU  339  CB  LEU A 297     3349   7038   5938  -1267   -409   -777       C  
ATOM    340  CG  LEU A 297      30.917   9.340  21.124  1.00 41.80           C  
ANISOU  340  CG  LEU A 297     3391   6799   5690  -1024   -609   -672       C  
ATOM    341  CD1 LEU A 297      31.305  10.157  22.340  1.00 43.07           C  
ANISOU  341  CD1 LEU A 297     3447   7157   5762  -1241   -718   -895       C  
ATOM    342  CD2 LEU A 297      29.464   9.580  20.752  1.00 40.78           C  
ANISOU  342  CD2 LEU A 297     3697   6199   5597   -988   -510   -473       C  
ATOM    343  N   ASN A 298      31.764  10.003  16.578  1.00 33.61           N  
ANISOU  343  N   ASN A 298     2488   5358   4923  -1519    154   -586       N  
ATOM    344  CA  ASN A 298      32.356  10.691  15.433  1.00 38.89           C  
ANISOU  344  CA  ASN A 298     3198   5950   5629  -1843    446   -658       C  
ATOM    345  C   ASN A 298      32.174  12.194  15.634  1.00 36.82           C  
ANISOU  345  C   ASN A 298     3242   5412   5335  -2192    592   -734       C  
ATOM    346  O   ASN A 298      31.055  12.708  15.531  1.00 45.62           O  
ANISOU  346  O   ASN A 298     4758   6148   6425  -2184    627   -592       O  
ATOM    347  CB  ASN A 298      31.696  10.211  14.140  1.00 33.60           C  
ANISOU  347  CB  ASN A 298     2812   5005   4951  -1665    556   -433       C  
ATOM    348  CG  ASN A 298      32.391  10.720  12.913  1.00 40.20           C  
ANISOU  348  CG  ASN A 298     3696   5786   5791  -1952    867   -492       C  
ATOM    349  OD1 ASN A 298      32.972  11.801  12.918  1.00 39.84           O  
ANISOU  349  OD1 ASN A 298     3720   5691   5725  -2266   1023   -627       O  
ATOM    350  ND2 ASN A 298      32.340   9.937  11.842  1.00 38.72           N  
ANISOU  350  ND2 ASN A 298     3558   5564   5590  -1770    939   -371       N  
ATOM    351  N   PHE A 299      33.269  12.899  15.920  1.00 40.76           N  
ANISOU  351  N   PHE A 299     3604   6075   5808  -2418    667   -941       N  
ATOM    352  CA  PHE A 299      33.201  14.324  16.225  1.00 49.26           C  
ANISOU  352  CA  PHE A 299     4986   6903   6828  -2709    808  -1034       C  
ATOM    353  C   PHE A 299      33.336  15.244  15.015  1.00 55.08           C  
ANISOU  353  C   PHE A 299     6082   7323   7524  -2930   1133  -1004       C  
ATOM    354  O   PHE A 299      33.141  16.454  15.170  1.00 62.80           O  
ANISOU  354  O   PHE A 299     7400   8028   8433  -3125   1278  -1051       O  
ATOM    355  CB  PHE A 299      34.285  14.691  17.243  1.00 58.57           C  
ANISOU  355  CB  PHE A 299     5857   8425   7970  -2874    737  -1305       C  
ATOM    356  CG  PHE A 299      34.168  13.943  18.531  1.00 56.98           C  
ANISOU  356  CG  PHE A 299     5382   8515   7752  -2635    411  -1333       C  
ATOM    357  CD1 PHE A 299      33.254  14.338  19.493  1.00 58.14           C  
ANISOU  357  CD1 PHE A 299     5746   8488   7857  -2614    295  -1302       C  
ATOM    358  CD2 PHE A 299      34.955  12.828  18.770  1.00 63.52           C  
ANISOU  358  CD2 PHE A 299     5776   9775   8584  -2391    227  -1380       C  
ATOM    359  CE1 PHE A 299      33.136  13.645  20.684  1.00 60.45           C  
ANISOU  359  CE1 PHE A 299     5831   9041   8098  -2384      2  -1322       C  
ATOM    360  CE2 PHE A 299      34.843  12.122  19.958  1.00 62.72           C  
ANISOU  360  CE2 PHE A 299     5493   9916   8421  -2114    -74  -1379       C  
ATOM    361  CZ  PHE A 299      33.934  12.532  20.919  1.00 60.31           C  
ANISOU  361  CZ  PHE A 299     5412   9442   8061  -2122   -186  -1350       C  
ATOM    362  N   ASP A 300      33.663  14.730  13.820  1.00 50.70           N  
ANISOU  362  N   ASP A 300     5493   6785   6984  -2891   1265   -931       N  
ATOM    363  CA  ASP A 300      33.943  15.612  12.683  1.00 55.18           C  
ANISOU  363  CA  ASP A 300     6404   7086   7475  -3104   1580   -927       C  
ATOM    364  C   ASP A 300      33.144  15.226  11.445  1.00 44.05           C  
ANISOU  364  C   ASP A 300     5309   5401   6028  -2912   1659   -669       C  
ATOM    365  O   ASP A 300      33.574  15.473  10.320  1.00 70.00           O  
ANISOU  365  O   ASP A 300     8762   8587   9249  -3015   1889   -659       O  
ATOM    366  CB  ASP A 300      35.439  15.648  12.363  1.00 57.13           C  
ANISOU  366  CB  ASP A 300     6329   7648   7731  -3340   1736  -1167       C  
ATOM    367  CG  ASP A 300      36.138  16.850  12.987  1.00 80.20           C  
ANISOU  367  CG  ASP A 300     9285  10592  10595  -3692   1868  -1422       C  
ATOM    368  OD1 ASP A 300      35.727  17.996  12.701  1.00 86.01           O  
ANISOU  368  OD1 ASP A 300    10509  10936  11235  -3857   2076  -1392       O  
ATOM    369  OD2 ASP A 300      37.085  16.652  13.779  1.00 91.14           O  
ANISOU  369  OD2 ASP A 300    10226  12391  12013  -3784   1764  -1658       O  
ATOM    370  N   ASN A 301      31.971  14.651  11.644  1.00 47.03           N  
ANISOU  370  N   ASN A 301     5789   5654   6425  -2641   1475   -472       N  
ATOM    371  CA  ASN A 301      31.118  14.199  10.556  1.00 44.45           C  
ANISOU  371  CA  ASN A 301     5748   5099   6040  -2426   1507   -232       C  
ATOM    372  C   ASN A 301      30.275  15.365  10.059  1.00 46.65           C  
ANISOU  372  C   ASN A 301     6611   4937   6177  -2385   1610    -95       C  
ATOM    373  O   ASN A 301      29.496  15.923  10.841  1.00 42.56           O  
ANISOU  373  O   ASN A 301     6267   4251   5651  -2308   1506    -63       O  
ATOM    374  CB  ASN A 301      30.221  13.068  11.038  1.00 45.67           C  
ANISOU  374  CB  ASN A 301     5754   5336   6265  -2151   1262   -111       C  
ATOM    375  CG  ASN A 301      29.507  12.348   9.903  1.00 37.84           C  
ANISOU  375  CG  ASN A 301     4959   4226   5193  -1850   1228    100       C  
ATOM    376  OD1 ASN A 301      29.339  12.891   8.804  1.00 35.89           O  
ANISOU  376  OD1 ASN A 301     5090   3723   4826  -1912   1427    202       O  
ATOM    377  ND2 ASN A 301      29.081  11.126  10.167  1.00 38.49           N  
ANISOU  377  ND2 ASN A 301     4820   4487   5319  -1530    987    159       N  
ATOM    378  N   PRO A 302      30.394  15.773   8.788  1.00 50.23           N  
ANISOU  378  N   PRO A 302     7382   5203   6499  -2399   1811    -20       N  
ATOM    379  CA  PRO A 302      29.535  16.865   8.286  1.00 42.05           C  
ANISOU  379  CA  PRO A 302     6909   3773   5294  -2273   1883    117       C  
ATOM    380  C   PRO A 302      28.049  16.524   8.298  1.00 38.95           C  
ANISOU  380  C   PRO A 302     6700   3238   4860  -1881   1648    337       C  
ATOM    381  O   PRO A 302      27.211  17.433   8.217  1.00 45.86           O  
ANISOU  381  O   PRO A 302     7959   3848   5616  -1708   1640    429       O  
ATOM    382  CB  PRO A 302      30.035  17.086   6.847  1.00 53.03           C  
ANISOU  382  CB  PRO A 302     8546   5062   6541  -2340   2121    147       C  
ATOM    383  CG  PRO A 302      31.316  16.316   6.730  1.00 54.33           C  
ANISOU  383  CG  PRO A 302     8260   5562   6819  -2573   2217    -21       C  
ATOM    384  CD  PRO A 302      31.266  15.218   7.736  1.00 46.49           C  
ANISOU  384  CD  PRO A 302     6777   4879   6006  -2487   1973    -56       C  
ATOM    385  N   LEU A 303      27.704  15.251   8.392  1.00 35.70           N  
ANISOU  385  N   LEU A 303     6021   3011   4533  -1724   1468    408       N  
ATOM    386  CA  LEU A 303      26.322  14.814   8.491  1.00 33.02           C  
ANISOU  386  CA  LEU A 303     5795   2588   4163  -1369   1234    578       C  
ATOM    387  C   LEU A 303      25.857  14.608   9.928  1.00 30.92           C  
ANISOU  387  C   LEU A 303     5323   2391   4036  -1331   1049    524       C  
ATOM    388  O   LEU A 303      24.692  14.266  10.138  1.00 38.65           O  
ANISOU  388  O   LEU A 303     6312   3371   5000  -1003    823    617       O  
ATOM    389  CB  LEU A 303      26.135  13.503   7.723  1.00 31.10           C  
ANISOU  389  CB  LEU A 303     5416   2499   3901  -1204   1148    671       C  
ATOM    390  CG  LEU A 303      26.581  13.553   6.250  1.00 33.14           C  
ANISOU  390  CG  LEU A 303     5885   2705   4002  -1237   1332    723       C  
ATOM    391  CD1 LEU A 303      26.251  12.252   5.576  1.00 35.77           C  
ANISOU  391  CD1 LEU A 303     6094   3196   4299  -1041   1215    795       C  
ATOM    392  CD2 LEU A 303      25.939  14.719   5.520  1.00 35.53           C  
ANISOU  392  CD2 LEU A 303     6650   2746   4102  -1077   1363    817       C  
ATOM    393  N   GLY A 304      26.735  14.767  10.922  1.00 47.99           N  
ANISOU  393  N   GLY A 304     7216   4700   6318  -1613   1094    336       N  
ATOM    394  CA  GLY A 304      26.423  14.451  12.285  1.00 38.70           C  
ANISOU  394  CA  GLY A 304     5771   3690   5244  -1527    872    254       C  
ATOM    395  C   GLY A 304      26.371  15.677  13.185  1.00 45.24           C  
ANISOU  395  C   GLY A 304     6805   4316   6068  -1718    957    155       C  
ATOM    396  O   GLY A 304      26.456  16.823  12.739  1.00 43.32           O  
ANISOU  396  O   GLY A 304     6881   3855   5722  -1776   1124    155       O  
ATOM    397  N   MET A 305      26.235  15.412  14.481  1.00 35.67           N  
ANISOU  397  N   MET A 305     5343   3281   4929  -1683    774     55       N  
ATOM    398  CA  MET A 305      26.073  16.453  15.486  1.00 40.23           C  
ANISOU  398  CA  MET A 305     6098   3691   5496  -1832    821    -57       C  
ATOM    399  C   MET A 305      27.295  16.554  16.387  1.00 39.51           C  
ANISOU  399  C   MET A 305     5671   3891   5449  -2156    827   -310       C  
ATOM    400  O   MET A 305      27.187  16.978  17.540  1.00 48.80           O  
ANISOU  400  O   MET A 305     6834   5089   6621  -2220    758   -432       O  
ATOM    401  CB  MET A 305      24.827  16.175  16.326  1.00 50.05           C  
ANISOU  401  CB  MET A 305     7346   4922   6748  -1495    600     15       C  
ATOM    402  CG  MET A 305      23.521  16.505  15.648  1.00 51.52           C  
ANISOU  402  CG  MET A 305     7879   4831   6865  -1160    593    207       C  
ATOM    403  SD  MET A 305      23.281  18.280  15.547  1.00 51.29           S  
ANISOU  403  SD  MET A 305     8350   4415   6722  -1197    810    197       S  
ATOM    404  CE  MET A 305      23.303  18.824  17.252  1.00 56.22           C  
ANISOU  404  CE  MET A 305     8927   5044   7391  -1358    790      0       C  
ATOM    405  N   ARG A 306      28.449  16.117  15.889  1.00 39.79           N  
ANISOU  405  N   ARG A 306     5410   4195   5514  -2319    888   -399       N  
ATOM    406  CA  ARG A 306      29.677  16.065  16.682  1.00 47.17           C  
ANISOU  406  CA  ARG A 306     5944   5506   6474  -2542    844   -646       C  
ATOM    407  C   ARG A 306      29.506  15.178  17.918  1.00 34.99           C  
ANISOU  407  C   ARG A 306     4065   4259   4969  -2413    559   -707       C  
ATOM    408  O   ARG A 306      30.080  15.453  18.974  1.00 53.22           O  
ANISOU  408  O   ARG A 306     6189   6786   7245  -2527    470   -894       O  
ATOM    409  CB  ARG A 306      30.137  17.473  17.082  1.00 54.37           C  
ANISOU  409  CB  ARG A 306     7062   6288   7310  -2808   1014   -811       C  
ATOM    410  CG  ARG A 306      30.605  18.324  15.904  1.00 61.89           C  
ANISOU  410  CG  ARG A 306     8298   7026   8191  -2977   1316   -804       C  
ATOM    411  CD  ARG A 306      30.569  19.818  16.213  1.00 76.55           C  
ANISOU  411  CD  ARG A 306    10541   8602   9942  -3170   1517   -901       C  
ATOM    412  NE  ARG A 306      29.375  20.459  15.665  1.00 84.08           N  
ANISOU  412  NE  ARG A 306    12024   9107  10815  -2942   1600   -684       N  
ATOM    413  CZ  ARG A 306      29.285  20.936  14.427  1.00 86.15           C  
ANISOU  413  CZ  ARG A 306    12637   9117  10979  -2902   1803   -564       C  
ATOM    414  NH1 ARG A 306      28.158  21.500  14.013  1.00 85.27           N  
ANISOU  414  NH1 ARG A 306    12977   8652  10771  -2623   1830   -371       N  
ATOM    415  NH2 ARG A 306      30.319  20.847  13.601  1.00 88.83           N  
ANISOU  415  NH2 ARG A 306    12872   9579  11303  -3118   1973   -647       N  
ATOM    416  N   GLY A 307      28.722  14.107  17.785  1.00 31.73           N  
ANISOU  416  N   GLY A 307     3612   3869   4575  -2046    386   -515       N  
ATOM    417  CA  GLY A 307      28.480  13.170  18.862  1.00 38.88           C  
ANISOU  417  CA  GLY A 307     4285   5020   5466  -1782    115   -506       C  
ATOM    418  C   GLY A 307      27.360  13.536  19.822  1.00 35.35           C  
ANISOU  418  C   GLY A 307     4076   4379   4976  -1659     24   -462       C  
ATOM    419  O   GLY A 307      26.989  12.696  20.648  1.00 34.33           O  
ANISOU  419  O   GLY A 307     3828   4400   4816  -1419   -170   -420       O  
ATOM    420  N   GLU A 308      26.785  14.741  19.717  1.00 39.77           N  
ANISOU  420  N   GLU A 308     5002   4589   5520  -1793    181   -465       N  
ATOM    421  CA  GLU A 308      25.902  15.252  20.766  1.00 32.20           C  
ANISOU  421  CA  GLU A 308     4242   3477   4517  -1721    126   -486       C  
ATOM    422  C   GLU A 308      24.582  14.498  20.838  1.00 35.54           C  
ANISOU  422  C   GLU A 308     4728   3830   4946  -1328      0   -295       C  
ATOM    423  O   GLU A 308      23.988  14.394  21.923  1.00 38.00           O  
ANISOU  423  O   GLU A 308     5051   4167   5218  -1222    -99   -323       O  
ATOM    424  CB  GLU A 308      25.642  16.754  20.566  1.00 36.15           C  
ANISOU  424  CB  GLU A 308     5162   3584   4991  -1929    359   -537       C  
ATOM    425  CG  GLU A 308      26.855  17.648  20.774  1.00 41.85           C  
ANISOU  425  CG  GLU A 308     5850   4369   5683  -2345    509   -769       C  
ATOM    426  CD  GLU A 308      27.393  17.612  22.207  1.00 56.58           C  
ANISOU  426  CD  GLU A 308     7463   6538   7496  -2478    358   -989       C  
ATOM    427  OE1 GLU A 308      28.554  18.014  22.421  1.00 62.63           O  
ANISOU  427  OE1 GLU A 308     8043   7526   8227  -2718    405  -1173       O  
ATOM    428  OE2 GLU A 308      26.667  17.183  23.122  1.00 56.25           O  
ANISOU  428  OE2 GLU A 308     7417   6531   7425  -2319    192   -979       O  
ATOM    429  N   ILE A 309      24.110  13.949  19.717  1.00 32.77           N  
ANISOU  429  N   ILE A 309     4409   3411   4630  -1135     11   -124       N  
ATOM    430  CA  ILE A 309      22.892  13.149  19.760  1.00 29.58           C  
ANISOU  430  CA  ILE A 309     4008   2996   4233   -817   -100      9       C  
ATOM    431  C   ILE A 309      23.164  11.801  20.423  1.00 29.81           C  
ANISOU  431  C   ILE A 309     3763   3307   4257   -712   -252      8       C  
ATOM    432  O   ILE A 309      22.403  11.358  21.289  1.00 29.02           O  
ANISOU  432  O   ILE A 309     3668   3230   4130   -572   -329     21       O  
ATOM    433  CB  ILE A 309      22.298  12.971  18.353  1.00 30.31           C  
ANISOU  433  CB  ILE A 309     4214   2964   4337   -658    -56    160       C  
ATOM    434  CG1 ILE A 309      21.689  14.267  17.852  1.00 39.37           C  
ANISOU  434  CG1 ILE A 309     5713   3799   5445   -631     69    200       C  
ATOM    435  CG2 ILE A 309      21.220  11.890  18.366  1.00 34.33           C  
ANISOU  435  CG2 ILE A 309     4625   3558   4859   -397   -176    244       C  
ATOM    436  CD1 ILE A 309      20.860  14.054  16.603  1.00 43.00           C  
ANISOU  436  CD1 ILE A 309     6286   4181   5871   -389     53    349       C  
ATOM    437  N   ALA A 310      24.257  11.136  20.029  1.00 32.98           N  
ANISOU  437  N   ALA A 310     3947   3913   4670   -764   -276     -9       N  
ATOM    438  CA  ALA A 310      24.631   9.867  20.645  1.00 32.60           C  
ANISOU  438  CA  ALA A 310     3689   4111   4589   -613   -412      1       C  
ATOM    439  C   ALA A 310      24.909  10.030  22.139  1.00 32.87           C  
ANISOU  439  C   ALA A 310     3665   4289   4535   -648   -520   -114       C  
ATOM    440  O   ALA A 310      24.520   9.181  22.948  1.00 31.83           O  
ANISOU  440  O   ALA A 310     3538   4224   4332   -462   -616    -65       O  
ATOM    441  CB  ALA A 310      25.852   9.286  19.932  1.00 26.27           C  
ANISOU  441  CB  ALA A 310     2657   3515   3810   -636   -403    -19       C  
ATOM    442  N   LYS A 311      25.569  11.120  22.531  1.00 27.98           N  
ANISOU  442  N   LYS A 311     3024   3708   3897   -904   -489   -278       N  
ATOM    443  CA  LYS A 311      25.904  11.292  23.941  1.00 30.78           C  
ANISOU  443  CA  LYS A 311     3315   4241   4137   -955   -610   -417       C  
ATOM    444  C   LYS A 311      24.665  11.620  24.766  1.00 36.11           C  
ANISOU  444  C   LYS A 311     4250   4704   4766   -879   -596   -385       C  
ATOM    445  O   LYS A 311      24.497  11.100  25.883  1.00 39.80           O  
ANISOU  445  O   LYS A 311     4716   5291   5114   -756   -710   -395       O  
ATOM    446  CB  LYS A 311      26.964  12.375  24.115  1.00 38.97           C  
ANISOU  446  CB  LYS A 311     4246   5399   5161  -1309   -565   -650       C  
ATOM    447  CG  LYS A 311      28.341  11.979  23.625  1.00 45.03           C  
ANISOU  447  CG  LYS A 311     4655   6505   5951  -1394   -602   -749       C  
ATOM    448  CD  LYS A 311      29.402  13.001  24.043  1.00 52.95           C  
ANISOU  448  CD  LYS A 311     5493   7707   6920  -1796   -567  -1047       C  
ATOM    449  CE  LYS A 311      29.169  14.358  23.393  1.00 57.13           C  
ANISOU  449  CE  LYS A 311     6320   7864   7522  -2147   -291  -1106       C  
ATOM    450  NZ  LYS A 311      30.340  15.276  23.536  1.00 69.24           N  
ANISOU  450  NZ  LYS A 311     7752   9526   9028  -2451   -179  -1327       N  
ATOM    451  N   SER A 312      23.782  12.476  24.243  1.00 28.09           N  
ANISOU  451  N   SER A 312     3471   3378   3823   -922   -448   -346       N  
ATOM    452  CA  SER A 312      22.570  12.762  25.002  1.00 30.28           C  
ANISOU  452  CA  SER A 312     3955   3485   4066   -815   -420   -332       C  
ATOM    453  C   SER A 312      21.667  11.532  25.068  1.00 27.84           C  
ANISOU  453  C   SER A 312     3617   3205   3756   -552   -468   -188       C  
ATOM    454  O   SER A 312      21.080  11.247  26.117  1.00 29.68           O  
ANISOU  454  O   SER A 312     3917   3455   3905   -473   -489   -204       O  
ATOM    455  CB  SER A 312      21.843  13.965  24.408  1.00 25.25           C  
ANISOU  455  CB  SER A 312     3574   2526   3493   -853   -258   -325       C  
ATOM    456  OG  SER A 312      21.254  13.619  23.172  1.00 33.20           O  
ANISOU  456  OG  SER A 312     4598   3435   4582   -687   -222   -170       O  
ATOM    457  N   TYR A 313      21.591  10.753  23.980  1.00 26.89           N  
ANISOU  457  N   TYR A 313     3414   3093   3711   -446   -464    -65       N  
ATOM    458  CA  TYR A 313      20.832   9.505  24.013  1.00 23.59           C  
ANISOU  458  CA  TYR A 313     2978   2699   3284   -258   -480     39       C  
ATOM    459  C   TYR A 313      21.438   8.501  24.982  1.00 27.43           C  
ANISOU  459  C   TYR A 313     3408   3367   3647   -183   -576     44       C  
ATOM    460  O   TYR A 313      20.709   7.802  25.689  1.00 29.42           O  
ANISOU  460  O   TYR A 313     3760   3592   3828    -82   -553     83       O  
ATOM    461  CB  TYR A 313      20.729   8.894  22.611  1.00 30.07           C  
ANISOU  461  CB  TYR A 313     3740   3495   4192   -190   -452    140       C  
ATOM    462  CG  TYR A 313      19.874   7.650  22.593  1.00 23.06           C  
ANISOU  462  CG  TYR A 313     2860   2606   3296    -58   -432    210       C  
ATOM    463  CD1 TYR A 313      18.492   7.744  22.588  1.00 24.27           C  
ANISOU  463  CD1 TYR A 313     3070   2671   3481    -14   -366    198       C  
ATOM    464  CD2 TYR A 313      20.452   6.385  22.627  1.00 24.06           C  
ANISOU  464  CD2 TYR A 313     2945   2824   3373     21   -461    267       C  
ATOM    465  CE1 TYR A 313      17.706   6.626  22.591  1.00 25.64           C  
ANISOU  465  CE1 TYR A 313     3241   2855   3646     34   -312    218       C  
ATOM    466  CE2 TYR A 313      19.679   5.253  22.620  1.00 26.33           C  
ANISOU  466  CE2 TYR A 313     3303   3062   3641     95   -395    315       C  
ATOM    467  CZ  TYR A 313      18.301   5.377  22.606  1.00 36.87           C  
ANISOU  467  CZ  TYR A 313     4678   4315   5015     66   -312    278       C  
ATOM    468  OH  TYR A 313      17.518   4.245  22.631  1.00 27.41           O  
ANISOU  468  OH  TYR A 313     3540   3078   3795     69   -212    284       O  
ATOM    469  N   ALA A 314      22.768   8.424  25.039  1.00 25.44           N  
ANISOU  469  N   ALA A 314     3005   3310   3349   -222   -675     -2       N  
ATOM    470  CA  ALA A 314      23.428   7.502  25.947  1.00 30.08           C  
ANISOU  470  CA  ALA A 314     3544   4103   3784    -76   -800      8       C  
ATOM    471  C   ALA A 314      23.149   7.864  27.401  1.00 37.78           C  
ANISOU  471  C   ALA A 314     4648   5106   4601    -93   -848    -68       C  
ATOM    472  O   ALA A 314      22.858   6.985  28.222  1.00 32.51           O  
ANISOU  472  O   ALA A 314     4113   4453   3785     76   -872      3       O  
ATOM    473  CB  ALA A 314      24.933   7.508  25.686  1.00 28.13           C  
ANISOU  473  CB  ALA A 314     3037   4128   3522   -102   -913    -69       C  
ATOM    474  N  AGLU A 315      23.250   9.150  27.743  0.50 36.65           N  
ANISOU  474  N  AGLU A 315     4513   4948   4466   -303   -838   -217       N  
ATOM    475  N  BGLU A 315      23.261   9.151  27.742  0.50 36.65           N  
ANISOU  475  N  BGLU A 315     4511   4950   4465   -304   -839   -218       N  
ATOM    476  CA AGLU A 315      22.937   9.555  29.111  0.50 38.14           C  
ANISOU  476  CA AGLU A 315     4851   5149   4493   -335   -866   -309       C  
ATOM    477  CA BGLU A 315      22.930   9.596  29.095  0.50 38.06           C  
ANISOU  477  CA BGLU A 315     4841   5135   4487   -342   -862   -312       C  
ATOM    478  C  AGLU A 315      21.480   9.258  29.451  0.50 31.75           C  
ANISOU  478  C  AGLU A 315     4264   4117   3684   -238   -724   -223       C  
ATOM    479  C  BGLU A 315      21.487   9.251  29.441  0.50 31.71           C  
ANISOU  479  C  BGLU A 315     4256   4112   3679   -237   -725   -222       C  
ATOM    480  O  AGLU A 315      21.175   8.783  30.556  0.50 34.03           O  
ANISOU  480  O  AGLU A 315     4698   4436   3794   -149   -735   -212       O  
ATOM    481  O  BGLU A 315      21.194   8.757  30.541  0.50 33.99           O  
ANISOU  481  O  BGLU A 315     4690   4435   3790   -146   -738   -210       O  
ATOM    482  CB AGLU A 315      23.255  11.035  29.314  0.50 45.19           C  
ANISOU  482  CB AGLU A 315     5752   6014   5403   -608   -837   -504       C  
ATOM    483  CB BGLU A 315      23.165  11.102  29.232  0.50 45.28           C  
ANISOU  483  CB BGLU A 315     5776   5996   5433   -615   -819   -500       C  
ATOM    484  CG AGLU A 315      24.743  11.344  29.278  0.50 51.48           C  
ANISOU  484  CG AGLU A 315     6300   7102   6157   -772   -969   -660       C  
ATOM    485  CG BGLU A 315      24.602  11.550  29.022  0.50 51.20           C  
ANISOU  485  CG BGLU A 315     6290   6992   6173   -809   -920   -655       C  
ATOM    486  CD AGLU A 315      25.534  10.523  30.283  0.50 56.10           C  
ANISOU  486  CD AGLU A 315     6757   8044   6516   -612  -1196   -695       C  
ATOM    487  CD BGLU A 315      24.757  13.061  29.078  0.50 53.83           C  
ANISOU  487  CD BGLU A 315     6716   7198   6541  -1139   -810   -854       C  
ATOM    488  OE1AGLU A 315      25.029  10.296  31.404  0.50 52.22           O  
ANISOU  488  OE1AGLU A 315     6456   7546   5841   -501  -1238   -682       O  
ATOM    489  OE1BGLU A 315      23.784  13.753  29.452  0.50 55.83           O  
ANISOU  489  OE1BGLU A 315     7235   7183   6796  -1163   -684   -868       O  
ATOM    490  OE2AGLU A 315      26.661  10.097  29.947  0.50 60.52           O  
ANISOU  490  OE2AGLU A 315     7030   8900   7064   -569  -1327   -733       O  
ATOM    491  OE2BGLU A 315      25.853  13.558  28.745  0.50 55.45           O  
ANISOU  491  OE2BGLU A 315     6736   7564   6769  -1382   -826  -1010       O  
ATOM    492  N   LEU A 316      20.568   9.506  28.506  1.00 28.58           N  
ANISOU  492  N   LEU A 316     3884   3513   3464   -248   -586   -171       N  
ATOM    493  CA  LEU A 316      19.160   9.183  28.736  1.00 28.57           C  
ANISOU  493  CA  LEU A 316     4011   3364   3481   -168   -445   -126       C  
ATOM    494  C   LEU A 316      18.953   7.687  28.989  1.00 31.59           C  
ANISOU  494  C   LEU A 316     4445   3783   3774    -36   -427    -12       C  
ATOM    495  O   LEU A 316      18.308   7.295  29.968  1.00 31.96           O  
ANISOU  495  O   LEU A 316     4655   3793   3695     -6   -341    -15       O  
ATOM    496  CB  LEU A 316      18.326   9.662  27.544  1.00 22.76           C  
ANISOU  496  CB  LEU A 316     3228   2481   2938   -162   -348   -104       C  
ATOM    497  CG  LEU A 316      16.825   9.388  27.649  1.00 28.17           C  
ANISOU  497  CG  LEU A 316     3952   3085   3666    -86   -207   -104       C  
ATOM    498  CD1 LEU A 316      16.234  10.010  28.933  1.00 30.18           C  
ANISOU  498  CD1 LEU A 316     4347   3294   3825   -107   -120   -213       C  
ATOM    499  CD2 LEU A 316      16.117   9.932  26.446  1.00 23.51           C  
ANISOU  499  CD2 LEU A 316     3285   2416   3231    -29   -168    -96       C  
ATOM    500  N   ILE A 317      19.495   6.835  28.112  1.00 25.83           N  
ANISOU  500  N   ILE A 317     3619   3100   3094     37   -475     86       N  
ATOM    501  CA  ILE A 317      19.379   5.384  28.284  1.00 21.01           C  
ANISOU  501  CA  ILE A 317     3124   2471   2388    167   -428    198       C  
ATOM    502  C   ILE A 317      19.945   4.953  29.627  1.00 29.85           C  
ANISOU  502  C   ILE A 317     4408   3684   3251    278   -507    217       C  
ATOM    503  O   ILE A 317      19.356   4.114  30.335  1.00 30.96           O  
ANISOU  503  O   ILE A 317     4789   3724   3249    343   -388    280       O  
ATOM    504  CB  ILE A 317      20.081   4.664  27.112  1.00 28.60           C  
ANISOU  504  CB  ILE A 317     3965   3469   3433    244   -476    282       C  
ATOM    505  CG1 ILE A 317      19.295   4.909  25.836  1.00 34.84           C  
ANISOU  505  CG1 ILE A 317     4659   4157   4423    153   -383    273       C  
ATOM    506  CG2 ILE A 317      20.209   3.164  27.355  1.00 32.36           C  
ANISOU  506  CG2 ILE A 317     4620   3901   3776    411   -427    399       C  
ATOM    507  CD1 ILE A 317      17.823   4.562  25.958  1.00 37.24           C  
ANISOU  507  CD1 ILE A 317     5054   4340   4754    102   -214    250       C  
ATOM    508  N   LYS A 318      21.093   5.518  30.007  1.00 30.54           N  
ANISOU  508  N   LYS A 318     4378   3972   3252    292   -700    151       N  
ATOM    509  CA  LYS A 318      21.696   5.132  31.275  1.00 30.28           C  
ANISOU  509  CA  LYS A 318     4483   4088   2934    439   -824    158       C  
ATOM    510  C   LYS A 318      20.774   5.477  32.431  1.00 31.82           C  
ANISOU  510  C   LYS A 318     4922   4176   2991    365   -712    108       C  
ATOM    511  O   LYS A 318      20.597   4.676  33.358  1.00 39.33           O  
ANISOU  511  O   LYS A 318     6146   5096   3703    505   -674    189       O  
ATOM    512  CB  LYS A 318      23.059   5.808  31.441  1.00 35.94           C  
ANISOU  512  CB  LYS A 318     4954   5110   3591    420  -1065     34       C  
ATOM    513  CG  LYS A 318      24.137   5.201  30.552  1.00 39.31           C  
ANISOU  513  CG  LYS A 318     5146   5708   4081    563  -1179     85       C  
ATOM    514  CD  LYS A 318      25.474   5.844  30.825  1.00 41.67           C  
ANISOU  514  CD  LYS A 318     5151   6375   4305    519  -1406    -85       C  
ATOM    515  CE  LYS A 318      26.559   5.265  29.950  1.00 43.22           C  
ANISOU  515  CE  LYS A 318     5067   6782   4571    670  -1500    -61       C  
ATOM    516  NZ  LYS A 318      27.853   5.917  30.279  1.00 45.10           N  
ANISOU  516  NZ  LYS A 318     4958   7444   4733    590  -1713   -277       N  
ATOM    517  N   GLN A 319      20.167   6.662  32.378  1.00 30.84           N  
ANISOU  517  N   GLN A 319     4741   3975   3003    162   -633    -21       N  
ATOM    518  CA  GLN A 319      19.180   7.031  33.384  1.00 33.82           C  
ANISOU  518  CA  GLN A 319     5333   4239   3278     93   -484    -87       C  
ATOM    519  C   GLN A 319      18.025   6.039  33.422  1.00 31.32           C  
ANISOU  519  C   GLN A 319     5196   3742   2962    132   -247     12       C  
ATOM    520  O   GLN A 319      17.637   5.573  34.493  1.00 29.77           O  
ANISOU  520  O   GLN A 319     5269   3500   2544    168   -143     33       O  
ATOM    521  CB  GLN A 319      18.673   8.438  33.111  1.00 30.03           C  
ANISOU  521  CB  GLN A 319     4763   3673   2976    -82   -412   -234       C  
ATOM    522  CG  GLN A 319      19.606   9.515  33.609  1.00 35.29           C  
ANISOU  522  CG  GLN A 319     5386   4470   3553   -199   -565   -390       C  
ATOM    523  CD  GLN A 319      19.033  10.877  33.372  1.00 49.03           C  
ANISOU  523  CD  GLN A 319     7138   6044   5446   -352   -442   -522       C  
ATOM    524  OE1 GLN A 319      18.387  11.117  32.348  1.00 46.46           O  
ANISOU  524  OE1 GLN A 319     6740   5569   5344   -340   -334   -478       O  
ATOM    525  NE2 GLN A 319      19.245  11.780  34.314  1.00 42.60           N  
ANISOU  525  NE2 GLN A 319     6445   5249   4491   -474   -456   -690       N  
ATOM    526  N   MET A 320      17.483   5.683  32.252  1.00 32.65           N  
ANISOU  526  N   MET A 320     5230   3816   3359    104   -147     59       N  
ATOM    527  CA  MET A 320      16.279   4.855  32.205  1.00 32.17           C  
ANISOU  527  CA  MET A 320     5287   3608   3329     61    106     89       C  
ATOM    528  C   MET A 320      16.533   3.444  32.724  1.00 33.04           C  
ANISOU  528  C   MET A 320     5688   3649   3216    169    174    226       C  
ATOM    529  O   MET A 320      15.617   2.816  33.272  1.00 29.12           O  
ANISOU  529  O   MET A 320     5418   3018   2629     96    425    228       O  
ATOM    530  CB  MET A 320      15.717   4.799  30.773  1.00 29.78           C  
ANISOU  530  CB  MET A 320     4749   3269   3298      2    160     79       C  
ATOM    531  CG  MET A 320      15.209   6.156  30.260  1.00 32.25           C  
ANISOU  531  CG  MET A 320     4850   3602   3802    -56    140    -39       C  
ATOM    532  SD  MET A 320      14.673   6.155  28.519  1.00 31.22           S  
ANISOU  532  SD  MET A 320     4459   3473   3929    -62    140    -38       S  
ATOM    533  CE  MET A 320      13.215   5.131  28.601  1.00 29.89           C  
ANISOU  533  CE  MET A 320     4298   3280   3779   -158    398   -102       C  
ATOM    534  N   TRP A 321      17.758   2.935  32.573  1.00 26.99           N  
ANISOU  534  N   TRP A 321     4938   2969   2348    352    -24    334       N  
ATOM    535  CA  TRP A 321      18.113   1.600  33.026  1.00 28.90           C  
ANISOU  535  CA  TRP A 321     5507   3123   2351    538     25    489       C  
ATOM    536  C   TRP A 321      18.950   1.612  34.306  1.00 34.97           C  
ANISOU  536  C   TRP A 321     6485   4023   2779    740   -148    531       C  
ATOM    537  O   TRP A 321      19.480   0.569  34.708  1.00 35.27           O  
ANISOU  537  O   TRP A 321     6811   4019   2570    991   -171    681       O  
ATOM    538  CB  TRP A 321      18.830   0.839  31.896  1.00 32.33           C  
ANISOU  538  CB  TRP A 321     5836   3559   2890    673    -55    588       C  
ATOM    539  CG  TRP A 321      17.881   0.538  30.737  1.00 26.29           C  
ANISOU  539  CG  TRP A 321     4962   2643   2382    479    148    552       C  
ATOM    540  CD1 TRP A 321      17.593   1.352  29.686  1.00 25.94           C  
ANISOU  540  CD1 TRP A 321     4574   2671   2612    334    101    453       C  
ATOM    541  CD2 TRP A 321      17.076  -0.643  30.566  1.00 29.55           C  
ANISOU  541  CD2 TRP A 321     5637   2820   2770    398    432    595       C  
ATOM    542  NE1 TRP A 321      16.658   0.761  28.866  1.00 27.86           N  
ANISOU  542  NE1 TRP A 321     4804   2787   2993    192    299    424       N  
ATOM    543  CE2 TRP A 321      16.333  -0.471  29.375  1.00 25.24           C  
ANISOU  543  CE2 TRP A 321     4826   2269   2496    196    513    493       C  
ATOM    544  CE3 TRP A 321      16.913  -1.828  31.305  1.00 29.68           C  
ANISOU  544  CE3 TRP A 321     6120   2618   2539    468    642    703       C  
ATOM    545  CZ2 TRP A 321      15.441  -1.442  28.896  1.00 25.85           C  
ANISOU  545  CZ2 TRP A 321     5031   2173   2619     24    783    459       C  
ATOM    546  CZ3 TRP A 321      16.023  -2.793  30.831  1.00 38.09           C  
ANISOU  546  CZ3 TRP A 321     7363   3451   3657    275    955    682       C  
ATOM    547  CH2 TRP A 321      15.292  -2.592  29.641  1.00 28.38           C  
ANISOU  547  CH2 TRP A 321     5804   2263   2716     35   1018    542       C  
ATOM    548  N   SER A 322      19.056   2.757  34.977  1.00 38.09           N  
ANISOU  548  N   SER A 322     6776   4570   3129    653   -266    398       N  
ATOM    549  CA  SER A 322      19.699   2.778  36.291  1.00 35.88           C  
ANISOU  549  CA  SER A 322     6718   4434   2482    818   -422    407       C  
ATOM    550  C   SER A 322      18.818   2.204  37.393  1.00 45.21           C  
ANISOU  550  C   SER A 322     8368   5413   3398    815   -166    468       C  
ATOM    551  O   SER A 322      19.344   1.779  38.427  1.00 41.07           O  
ANISOU  551  O   SER A 322     8153   4955   2496   1035   -267    548       O  
ATOM    552  CB  SER A 322      20.087   4.203  36.682  1.00 39.36           C  
ANISOU  552  CB  SER A 322     6926   5090   2940    677   -607    208       C  
ATOM    553  OG  SER A 322      18.926   4.985  36.896  1.00 38.73           O  
ANISOU  553  OG  SER A 322     6880   4854   2981    435   -381     89       O  
ATOM    554  N   GLY A 323      17.498   2.199  37.218  1.00 41.15           N  
ANISOU  554  N   GLY A 323     7908   4678   3049    576    165    419       N  
ATOM    555  CA  GLY A 323      16.632   1.778  38.304  1.00 39.25           C  
ANISOU  555  CA  GLY A 323     8091   4260   2561    512    454    437       C  
ATOM    556  C   GLY A 323      16.447   2.817  39.387  1.00 39.21           C  
ANISOU  556  C   GLY A 323     8137   4359   2402    430    429    292       C  
ATOM    557  O   GLY A 323      15.920   2.495  40.460  1.00 51.61           O  
ANISOU  557  O   GLY A 323    10105   5815   3690    411    642    312       O  
ATOM    558  N   LYS A 324      16.864   4.057  39.138  1.00 44.25           N  
ANISOU  558  N   LYS A 324     8423   5188   3202    364    206    140       N  
ATOM    559  CA  LYS A 324      16.735   5.136  40.105  1.00 47.25           C  
ANISOU  559  CA  LYS A 324     8853   5652   3447    267    185    -28       C  
ATOM    560  C   LYS A 324      15.515   6.002  39.857  1.00 42.78           C  
ANISOU  560  C   LYS A 324     8130   4969   3157     37    442   -192       C  
ATOM    561  O   LYS A 324      15.164   6.807  40.718  1.00 43.89           O  
ANISOU  561  O   LYS A 324     8379   5117   3182    -47    519   -336       O  
ATOM    562  CB  LYS A 324      17.993   6.013  40.080  1.00 47.15           C  
ANISOU  562  CB  LYS A 324     8597   5911   3407    311   -195   -129       C  
ATOM    563  CG  LYS A 324      19.271   5.249  40.390  1.00 58.01           C  
ANISOU  563  CG  LYS A 324    10053   7498   4489    588   -497     -6       C  
ATOM    564  CD  LYS A 324      20.521   6.068  40.095  1.00 64.46           C  
ANISOU  564  CD  LYS A 324    10500   8635   5356    577   -855   -147       C  
ATOM    565  CE  LYS A 324      20.699   7.219  41.072  1.00 73.33           C  
ANISOU  565  CE  LYS A 324    11654   9909   6300    418   -952   -377       C  
ATOM    566  NZ  LYS A 324      22.146   7.513  41.311  1.00 78.70           N  
ANISOU  566  NZ  LYS A 324    12109  10995   6798    492  -1346   -496       N  
ATOM    567  N   PHE A 325      14.855   5.849  38.714  1.00 36.60           N  
ANISOU  567  N   PHE A 325     7098   4094   2714    -40    573   -184       N  
ATOM    568  CA  PHE A 325      13.805   6.763  38.304  1.00 41.70           C  
ANISOU  568  CA  PHE A 325     7517   4690   3638   -181    747   -345       C  
ATOM    569  C   PHE A 325      12.550   5.998  37.932  1.00 46.94           C  
ANISOU  569  C   PHE A 325     8153   5243   4440   -279   1072   -344       C  
ATOM    570  O   PHE A 325      12.611   4.961  37.260  1.00 44.43           O  
ANISOU  570  O   PHE A 325     7827   4877   4177   -271   1098   -225       O  
ATOM    571  CB  PHE A 325      14.245   7.616  37.101  1.00 35.08           C  
ANISOU  571  CB  PHE A 325     6319   3913   3098   -175    541   -384       C  
ATOM    572  CG  PHE A 325      15.484   8.417  37.356  1.00 40.75           C  
ANISOU  572  CG  PHE A 325     7016   4754   3713   -154    255   -432       C  
ATOM    573  CD1 PHE A 325      15.436   9.560  38.141  1.00 53.71           C  
ANISOU  573  CD1 PHE A 325     8744   6397   5265   -233    265   -602       C  
ATOM    574  CD2 PHE A 325      16.700   8.009  36.848  1.00 31.76           C  
ANISOU  574  CD2 PHE A 325     5770   3744   2555    -73     -6   -335       C  
ATOM    575  CE1 PHE A 325      16.580  10.293  38.394  1.00 59.54           C  
ANISOU  575  CE1 PHE A 325     9458   7266   5899   -277     20   -691       C  
ATOM    576  CE2 PHE A 325      17.850   8.737  37.095  1.00 32.71           C  
ANISOU  576  CE2 PHE A 325     5817   4032   2580    -97   -257   -425       C  
ATOM    577  CZ  PHE A 325      17.789   9.883  37.870  1.00 53.93           C  
ANISOU  577  CZ  PHE A 325     8590   6723   5178   -223   -244   -612       C  
ATOM    578  N   SER A 326      11.414   6.527  38.372  1.00 43.48           N  
ANISOU  578  N   SER A 326     7689   4778   4055   -383   1333   -504       N  
ATOM    579  CA  SER A 326      10.133   6.104  37.827  1.00 44.89           C  
ANISOU  579  CA  SER A 326     7679   4936   4442   -504   1622   -585       C  
ATOM    580  C   SER A 326       9.886   6.729  36.459  1.00 35.06           C  
ANISOU  580  C   SER A 326     6000   3774   3546   -455   1488   -643       C  
ATOM    581  O   SER A 326       9.252   6.104  35.596  1.00 38.91           O  
ANISOU  581  O   SER A 326     6280   4294   4208   -525   1587   -659       O  
ATOM    582  CB  SER A 326       9.013   6.475  38.797  1.00 37.82           C  
ANISOU  582  CB  SER A 326     6863   4033   3475   -608   1954   -762       C  
ATOM    583  OG  SER A 326       9.055   7.865  39.025  1.00 42.72           O  
ANISOU  583  OG  SER A 326     7387   4696   4149   -517   1850   -885       O  
ATOM    584  N   TYR A 327      10.403   7.937  36.231  1.00 38.70           N  
ANISOU  584  N   TYR A 327     6353   4265   4088   -346   1268   -678       N  
ATOM    585  CA  TYR A 327      10.392   8.525  34.896  1.00 35.35           C  
ANISOU  585  CA  TYR A 327     5610   3882   3938   -263   1112   -685       C  
ATOM    586  C   TYR A 327      11.432   9.630  34.857  1.00 32.70           C  
ANISOU  586  C   TYR A 327     5321   3516   3587   -192    869   -675       C  
ATOM    587  O   TYR A 327      11.870  10.140  35.897  1.00 35.25           O  
ANISOU  587  O   TYR A 327     5861   3812   3720   -217    852   -727       O  
ATOM    588  CB  TYR A 327       9.016   9.092  34.528  1.00 32.62           C  
ANISOU  588  CB  TYR A 327     5003   3598   3792   -222   1292   -851       C  
ATOM    589  CG  TYR A 327       8.652  10.288  35.380  1.00 36.32           C  
ANISOU  589  CG  TYR A 327     5565   4025   4212   -153   1388   -994       C  
ATOM    590  CD1 TYR A 327       8.108  10.124  36.651  1.00 42.52           C  
ANISOU  590  CD1 TYR A 327     6538   4798   4820   -242   1642  -1093       C  
ATOM    591  CD2 TYR A 327       8.863  11.586  34.916  1.00 39.42           C  
ANISOU  591  CD2 TYR A 327     5907   4357   4713     -3   1254  -1031       C  
ATOM    592  CE1 TYR A 327       7.783  11.222  37.433  1.00 41.91           C  
ANISOU  592  CE1 TYR A 327     6565   4670   4688   -175   1747  -1238       C  
ATOM    593  CE2 TYR A 327       8.537  12.686  35.685  1.00 47.14           C  
ANISOU  593  CE2 TYR A 327     7019   5255   5639     67   1368  -1171       C  
ATOM    594  CZ  TYR A 327       8.000  12.499  36.939  1.00 48.92           C  
ANISOU  594  CZ  TYR A 327     7400   5490   5699    -15   1607  -1280       C  
ATOM    595  OH  TYR A 327       7.680  13.594  37.690  1.00 52.25           O  
ANISOU  595  OH  TYR A 327     7970   5822   6062     59   1733  -1431       O  
ATOM    596  N   VAL A 328      11.810  10.013  33.637  1.00 30.92           N  
ANISOU  596  N   VAL A 328     4904   3296   3550   -129    700   -625       N  
ATOM    597  CA  VAL A 328      12.826  11.033  33.433  1.00 39.25           C  
ANISOU  597  CA  VAL A 328     6000   4305   4607   -118    509   -628       C  
ATOM    598  C   VAL A 328      12.361  11.970  32.335  1.00 36.47           C  
ANISOU  598  C   VAL A 328     5495   3887   4474    -13    503   -659       C  
ATOM    599  O   VAL A 328      11.391  11.703  31.622  1.00 31.36           O  
ANISOU  599  O   VAL A 328     4659   3286   3970     80    580   -663       O  
ATOM    600  CB  VAL A 328      14.201  10.437  33.078  1.00 34.95           C  
ANISOU  600  CB  VAL A 328     5449   3831   4001   -157    285   -502       C  
ATOM    601  CG1 VAL A 328      14.683   9.557  34.197  1.00 36.57           C  
ANISOU  601  CG1 VAL A 328     5846   4105   3946   -181    266   -457       C  
ATOM    602  CG2 VAL A 328      14.112   9.660  31.793  1.00 35.29           C  
ANISOU  602  CG2 VAL A 328     5299   3902   4208   -113    247   -388       C  
ATOM    603  N   THR A 329      13.064  13.073  32.216  1.00 32.26           N  
ANISOU  603  N   THR A 329     5063   3252   3944    -29    416   -693       N  
ATOM    604  CA  THR A 329      12.745  13.985  31.133  1.00 40.93           C  
ANISOU  604  CA  THR A 329     6106   4238   5208     99    414   -690       C  
ATOM    605  C   THR A 329      13.756  13.829  30.014  1.00 41.12           C  
ANISOU  605  C   THR A 329     6059   4267   5297     45    246   -571       C  
ATOM    606  O   THR A 329      14.969  13.828  30.265  1.00 54.30           O  
ANISOU  606  O   THR A 329     7788   5961   6880   -116    139   -565       O  
ATOM    607  CB  THR A 329      12.716  15.435  31.615  1.00 55.85           C  
ANISOU  607  CB  THR A 329     8227   5931   7063    119    502   -815       C  
ATOM    608  OG1 THR A 329      12.597  16.298  30.483  1.00 58.33           O  
ANISOU  608  OG1 THR A 329     8569   6092   7502    262    494   -774       O  
ATOM    609  CG2 THR A 329      13.978  15.790  32.401  1.00 57.87           C  
ANISOU  609  CG2 THR A 329     8668   6160   7161   -118    424   -881       C  
ATOM    610  N   PRO A 330      13.293  13.653  28.803  1.00 39.95           N  
ANISOU  610  N   PRO A 330     5762   4133   5283    176    221   -492       N  
ATOM    611  CA  PRO A 330      14.205  13.502  27.660  1.00 35.80           C  
ANISOU  611  CA  PRO A 330     5184   3606   4811    128     91   -379       C  
ATOM    612  C   PRO A 330      14.561  14.835  27.014  1.00 36.44           C  
ANISOU  612  C   PRO A 330     5439   3480   4925    152    106   -382       C  
ATOM    613  O   PRO A 330      14.705  14.922  25.786  1.00 33.75           O  
ANISOU  613  O   PRO A 330     5073   3101   4651    218     60   -287       O  
ATOM    614  CB  PRO A 330      13.392  12.621  26.712  1.00 31.13           C  
ANISOU  614  CB  PRO A 330     4379   3135   4314    255     75   -311       C  
ATOM    615  CG  PRO A 330      11.982  13.125  26.938  1.00 37.67           C  
ANISOU  615  CG  PRO A 330     5165   3965   5183    442    191   -409       C  
ATOM    616  CD  PRO A 330      11.884  13.459  28.422  1.00 28.38           C  
ANISOU  616  CD  PRO A 330     4133   2740   3910    368    307   -520       C  
ATOM    617  N   ARG A 331      14.749  15.870  27.842  1.00 34.81           N  
ANISOU  617  N   ARG A 331     5456   3118   4650     79    190   -495       N  
ATOM    618  CA  ARG A 331      14.807  17.247  27.347  1.00 41.49           C  
ANISOU  618  CA  ARG A 331     6564   3688   5512    126    279   -516       C  
ATOM    619  C   ARG A 331      16.095  17.537  26.580  1.00 42.67           C  
ANISOU  619  C   ARG A 331     6787   3762   5663    -92    238   -473       C  
ATOM    620  O   ARG A 331      16.056  18.127  25.491  1.00 44.89           O  
ANISOU  620  O   ARG A 331     7208   3865   5983      4    283   -389       O  
ATOM    621  CB  ARG A 331      14.655  18.224  28.518  1.00 51.25           C  
ANISOU  621  CB  ARG A 331     8053   4756   6662     73    415   -678       C  
ATOM    622  CG  ARG A 331      14.240  19.637  28.118  1.00 63.42           C  
ANISOU  622  CG  ARG A 331     9928   5954   8213    235    569   -701       C  
ATOM    623  CD  ARG A 331      14.176  20.547  29.335  1.00 71.66           C  
ANISOU  623  CD  ARG A 331    11251   6818   9160    146    722   -885       C  
ATOM    624  NE  ARG A 331      13.202  21.625  29.182  1.00 81.62           N  
ANISOU  624  NE  ARG A 331    12787   7793  10434    469    894   -906       N  
ATOM    625  CZ  ARG A 331      12.015  21.650  29.781  1.00 79.85           C  
ANISOU  625  CZ  ARG A 331    12501   7622  10217    747    977   -971       C  
ATOM    626  NH1 ARG A 331      11.192  22.672  29.584  1.00 81.12           N  
ANISOU  626  NH1 ARG A 331    12781   7658  10385   1043   1069   -948       N  
ATOM    627  NH2 ARG A 331      11.652  20.658  30.584  1.00 72.78           N  
ANISOU  627  NH2 ARG A 331    11318   7023   9311    692    933  -1022       N  
ATOM    628  N   ALA A 332      17.253  17.183  27.153  1.00 35.62           N  
ANISOU  628  N   ALA A 332     5814   3013   4709   -378    164   -542       N  
ATOM    629  CA  ALA A 332      18.520  17.433  26.464  1.00 36.06           C  
ANISOU  629  CA  ALA A 332     5875   3055   4773   -620    147   -543       C  
ATOM    630  C   ALA A 332      18.574  16.696  25.132  1.00 33.40           C  
ANISOU  630  C   ALA A 332     5372   2796   4522   -508     79   -373       C  
ATOM    631  O   ALA A 332      18.984  17.261  24.103  1.00 44.21           O  
ANISOU  631  O   ALA A 332     6872   4009   5919   -565    151   -323       O  
ATOM    632  CB  ALA A 332      19.692  17.030  27.361  1.00 30.47           C  
ANISOU  632  CB  ALA A 332     5010   2594   3973   -893     39   -671       C  
ATOM    633  N   PHE A 333      18.140  15.432  25.134  1.00 32.97           N  
ANISOU  633  N   PHE A 333     5072   2961   4492   -360    -33   -289       N  
ATOM    634  CA  PHE A 333      18.106  14.645  23.912  1.00 31.23           C  
ANISOU  634  CA  PHE A 333     4703   2822   4340   -256    -92   -150       C  
ATOM    635  C   PHE A 333      17.174  15.257  22.877  1.00 33.00           C  
ANISOU  635  C   PHE A 333     5067   2867   4604    -33    -32    -67       C  
ATOM    636  O   PHE A 333      17.480  15.257  21.680  1.00 38.56           O  
ANISOU  636  O   PHE A 333     5796   3530   5324    -16    -37     28       O  
ATOM    637  CB  PHE A 333      17.672  13.211  24.234  1.00 28.94           C  
ANISOU  637  CB  PHE A 333     4189   2752   4054   -158   -180   -104       C  
ATOM    638  CG  PHE A 333      17.528  12.342  23.032  1.00 26.50           C  
ANISOU  638  CG  PHE A 333     3746   2520   3804    -64   -227     10       C  
ATOM    639  CD1 PHE A 333      18.633  11.948  22.318  1.00 27.37           C  
ANISOU  639  CD1 PHE A 333     3779   2697   3923   -169   -269     60       C  
ATOM    640  CD2 PHE A 333      16.278  11.906  22.616  1.00 36.55           C  
ANISOU  640  CD2 PHE A 333     4947   3826   5115    119   -221     41       C  
ATOM    641  CE1 PHE A 333      18.498  11.143  21.198  1.00 24.28           C  
ANISOU  641  CE1 PHE A 333     3293   2364   3570    -86   -298    153       C  
ATOM    642  CE2 PHE A 333      16.137  11.108  21.502  1.00 37.78           C  
ANISOU  642  CE2 PHE A 333     4987   4063   5304    177   -267    116       C  
ATOM    643  CZ  PHE A 333      17.247  10.723  20.794  1.00 29.61           C  
ANISOU  643  CZ  PHE A 333     3927   3056   4269     78   -302    180       C  
ATOM    644  N   LYS A 334      16.015  15.763  23.316  1.00 38.04           N  
ANISOU  644  N   LYS A 334     5796   3419   5240    170     21   -105       N  
ATOM    645  CA  LYS A 334      15.114  16.426  22.376  1.00 50.03           C  
ANISOU  645  CA  LYS A 334     7449   4796   6765    458     53    -34       C  
ATOM    646  C   LYS A 334      15.748  17.683  21.791  1.00 39.69           C  
ANISOU  646  C   LYS A 334     6506   3170   5404    401    168      0       C  
ATOM    647  O   LYS A 334      15.590  17.963  20.601  1.00 44.88           O  
ANISOU  647  O   LYS A 334     7293   3726   6034    565    168    118       O  
ATOM    648  CB  LYS A 334      13.785  16.776  23.045  1.00 55.58           C  
ANISOU  648  CB  LYS A 334     8147   5497   7472    717     99   -110       C  
ATOM    649  CG  LYS A 334      13.169  18.052  22.471  1.00 63.65           C  
ANISOU  649  CG  LYS A 334     9466   6263   8454   1019    176    -73       C  
ATOM    650  CD  LYS A 334      11.659  18.088  22.569  1.00 69.29           C  
ANISOU  650  CD  LYS A 334    10033   7107   9188   1404    160   -120       C  
ATOM    651  CE  LYS A 334      11.118  19.339  21.897  1.00 79.28           C  
ANISOU  651  CE  LYS A 334    11596   8144  10382   1763    210    -57       C  
ATOM    652  NZ  LYS A 334      11.552  19.419  20.471  1.00 81.66           N  
ANISOU  652  NZ  LYS A 334    11975   8430  10620   1766    132    103       N  
ATOM    653  N   THR A 335      16.456  18.462  22.616  1.00 36.21           N  
ANISOU  653  N   THR A 335     6268   2562   4928    155    282   -113       N  
ATOM    654  CA  THR A 335      17.145  19.655  22.110  1.00 36.55           C  
ANISOU  654  CA  THR A 335     6703   2268   4915     12    448   -111       C  
ATOM    655  C   THR A 335      18.132  19.283  21.002  1.00 41.69           C  
ANISOU  655  C   THR A 335     7298   2970   5573   -175    437    -24       C  
ATOM    656  O   THR A 335      18.175  19.924  19.937  1.00 42.36           O  
ANISOU  656  O   THR A 335     7603   2893   5599    -97    523     80       O  
ATOM    657  CB  THR A 335      17.870  20.358  23.263  1.00 40.27           C  
ANISOU  657  CB  THR A 335     7329   2625   5347   -324    566   -304       C  
ATOM    658  OG1 THR A 335      16.952  20.621  24.335  1.00 46.35           O  
ANISOU  658  OG1 THR A 335     8147   3365   6100   -152    587   -393       O  
ATOM    659  CG2 THR A 335      18.471  21.684  22.820  1.00 39.42           C  
ANISOU  659  CG2 THR A 335     7505   2313   5160   -481    747   -314       C  
ATOM    660  N   GLN A 336      18.899  18.208  21.216  1.00 30.20           N  
ANISOU  660  N   GLN A 336     5480   1828   4166   -382    316    -60       N  
ATOM    661  CA  GLN A 336      19.878  17.807  20.205  1.00 41.93           C  
ANISOU  661  CA  GLN A 336     6878   3391   5664   -555    322      0       C  
ATOM    662  C   GLN A 336      19.197  17.282  18.939  1.00 43.55           C  
ANISOU  662  C   GLN A 336     7059   3623   5866   -261    252    179       C  
ATOM    663  O   GLN A 336      19.619  17.598  17.808  1.00 42.23           O  
ANISOU  663  O   GLN A 336     7072   3320   5652   -300    342    267       O  
ATOM    664  CB  GLN A 336      20.838  16.772  20.801  1.00 29.58           C  
ANISOU  664  CB  GLN A 336     4928   2173   4139   -774    202    -88       C  
ATOM    665  CG  GLN A 336      21.664  17.320  22.007  1.00 28.47           C  
ANISOU  665  CG  GLN A 336     4784   2070   3963  -1090    242   -297       C  
ATOM    666  CD  GLN A 336      22.378  18.635  21.678  1.00 41.80           C  
ANISOU  666  CD  GLN A 336     6785   3483   5616  -1399    470   -398       C  
ATOM    667  OE1 GLN A 336      22.794  18.856  20.547  1.00 41.03           O  
ANISOU  667  OE1 GLN A 336     6801   3267   5523  -1477    589   -324       O  
ATOM    668  NE2 GLN A 336      22.517  19.506  22.669  1.00 48.29           N  
ANISOU  668  NE2 GLN A 336     7773   4189   6385  -1594    556   -576       N  
ATOM    669  N   VAL A 337      18.138  16.486  19.104  1.00 42.27           N  
ANISOU  669  N   VAL A 337     6684   3641   5735     10    104    217       N  
ATOM    670  CA  VAL A 337      17.408  15.984  17.945  1.00 41.89           C  
ANISOU  670  CA  VAL A 337     6584   3666   5667    276     17    344       C  
ATOM    671  C   VAL A 337      16.825  17.140  17.146  1.00 45.71           C  
ANISOU  671  C   VAL A 337     7448   3871   6051    525     95    436       C  
ATOM    672  O   VAL A 337      16.836  17.123  15.907  1.00 56.09           O  
ANISOU  672  O   VAL A 337     8877   5148   7287    637     83    554       O  
ATOM    673  CB  VAL A 337      16.318  14.985  18.379  1.00 42.05           C  
ANISOU  673  CB  VAL A 337     6297   3942   5737    465   -123    313       C  
ATOM    674  CG1 VAL A 337      15.356  14.693  17.220  1.00 44.65           C  
ANISOU  674  CG1 VAL A 337     6578   4363   6024    756   -220    394       C  
ATOM    675  CG2 VAL A 337      16.955  13.702  18.836  1.00 30.66           C  
ANISOU  675  CG2 VAL A 337     4568   2730   4351    264   -185    275       C  
ATOM    676  N   GLY A 338      16.329  18.170  17.836  1.00 40.63           N  
ANISOU  676  N   GLY A 338     7042   3015   5383    637    184    387       N  
ATOM    677  CA  GLY A 338      15.775  19.318  17.135  1.00 49.39           C  
ANISOU  677  CA  GLY A 338     8400   3997   6371    866    249    452       C  
ATOM    678  C   GLY A 338      16.817  20.145  16.408  1.00 61.95           C  
ANISOU  678  C   GLY A 338    10287   5387   7865    634    422    492       C  
ATOM    679  O   GLY A 338      16.491  20.860  15.451  1.00 58.45           O  
ANISOU  679  O   GLY A 338    10077   4849   7281    826    466    584       O  
ATOM    680  N   ARG A 339      18.072  20.093  16.864  1.00 58.06           N  
ANISOU  680  N   ARG A 339     9787   4844   7428    214    532    403       N  
ATOM    681  CA  ARG A 339      19.132  20.742  16.093  1.00 58.85           C  
ANISOU  681  CA  ARG A 339    10104   4814   7443    -44    714    413       C  
ATOM    682  C   ARG A 339      19.503  19.921  14.860  1.00 52.15           C  
ANISOU  682  C   ARG A 339     9147   4090   6576    -45    660    522       C  
ATOM    683  O   ARG A 339      19.863  20.481  13.813  1.00 62.20           O  
ANISOU  683  O   ARG A 339    10658   5253   7723    -66    787    586       O  
ATOM    684  CB  ARG A 339      20.359  20.985  16.968  1.00 57.55           C  
ANISOU  684  CB  ARG A 339     9895   4634   7336   -508    845    237       C  
ATOM    685  CG  ARG A 339      20.158  22.048  18.026  1.00 55.17           C  
ANISOU  685  CG  ARG A 339     9792   4169   7000   -559    953    117       C  
ATOM    686  CD  ARG A 339      21.472  22.728  18.382  1.00 69.21           C  
ANISOU  686  CD  ARG A 339    11641   5905   8751  -1026   1148    -54       C  
ATOM    687  NE  ARG A 339      21.930  22.390  19.727  1.00 67.56           N  
ANISOU  687  NE  ARG A 339    11183   5861   8625  -1282   1080   -245       N  
ATOM    688  CZ  ARG A 339      21.834  23.200  20.776  1.00 60.03           C  
ANISOU  688  CZ  ARG A 339    10371   4808   7628  -1375   1159   -383       C  
ATOM    689  NH1 ARG A 339      21.299  24.403  20.637  1.00 60.39           N  
ANISOU  689  NH1 ARG A 339    10816   4566   7562  -1233   1328   -343       N  
ATOM    690  NH2 ARG A 339      22.281  22.812  21.964  1.00 65.34           N  
ANISOU  690  NH2 ARG A 339    10800   5679   8347  -1602   1068   -563       N  
ATOM    691  N   PHE A 340      19.437  18.594  14.972  1.00 42.86           N  
ANISOU  691  N   PHE A 340     7647   3133   5506    -28    493    537       N  
ATOM    692  CA  PHE A 340      19.693  17.723  13.829  1.00 40.78           C  
ANISOU  692  CA  PHE A 340     7279   3000   5217     -4    437    637       C  
ATOM    693  C   PHE A 340      18.605  17.843  12.769  1.00 53.61           C  
ANISOU  693  C   PHE A 340     9009   4651   6708    390    334    761       C  
ATOM    694  O   PHE A 340      18.882  17.784  11.571  1.00 54.48           O  
ANISOU  694  O   PHE A 340     9226   4764   6710    404    370    841       O  
ATOM    695  CB  PHE A 340      19.812  16.268  14.300  1.00 33.82           C  
ANISOU  695  CB  PHE A 340     5994   2393   4463    -63    278    599       C  
ATOM    696  CG  PHE A 340      20.164  15.276  13.215  1.00 36.09           C  
ANISOU  696  CG  PHE A 340     6123   2860   4730    -66    228    667       C  
ATOM    697  CD1 PHE A 340      21.456  15.200  12.713  1.00 32.26           C  
ANISOU  697  CD1 PHE A 340     5632   2378   4247   -365    379    644       C  
ATOM    698  CD2 PHE A 340      19.211  14.388  12.732  1.00 35.22           C  
ANISOU  698  CD2 PHE A 340     5844   2939   4599    204     46    721       C  
ATOM    699  CE1 PHE A 340      21.777  14.280  11.726  1.00 42.75           C  
ANISOU  699  CE1 PHE A 340     6829   3863   5551   -354    355    696       C  
ATOM    700  CE2 PHE A 340      19.519  13.469  11.752  1.00 40.65           C  
ANISOU  700  CE2 PHE A 340     6417   3775   5255    188     13    762       C  
ATOM    701  CZ  PHE A 340      20.806  13.403  11.242  1.00 43.52           C  
ANISOU  701  CZ  PHE A 340     6807   4112   5615    -74    169    760       C  
ATOM    702  N   ALA A 341      17.340  18.000  13.197  1.00 55.90           N  
ANISOU  702  N   ALA A 341     9249   4996   6995    713    203    757       N  
ATOM    703  CA  ALA A 341      16.197  17.992  12.291  1.00 51.56           C  
ANISOU  703  CA  ALA A 341     8696   4571   6324   1092     62    830       C  
ATOM    704  C   ALA A 341      15.186  19.059  12.705  1.00 53.69           C  
ANISOU  704  C   ALA A 341     9116   4753   6531   1375     67    810       C  
ATOM    705  O   ALA A 341      14.439  18.870  13.678  1.00 66.55           O  
ANISOU  705  O   ALA A 341    10544   6482   8259   1492    -13    731       O  
ATOM    706  CB  ALA A 341      15.534  16.618  12.267  1.00 58.64           C  
ANISOU  706  CB  ALA A 341     9208   5780   7293   1215   -155    809       C  
ATOM    707  N   PRO A 342      15.119  20.185  11.977  1.00 71.17           N  
ANISOU  707  N   PRO A 342    11699   6778   8565   1506    175    876       N  
ATOM    708  CA  PRO A 342      14.256  21.342  12.271  1.00 74.93           C  
ANISOU  708  CA  PRO A 342    12403   7124   8943   1794    217    873       C  
ATOM    709  C   PRO A 342      12.796  21.007  12.604  1.00 80.76           C  
ANISOU  709  C   PRO A 342    12845   8126   9714   2163     11    827       C  
ATOM    710  O   PRO A 342      12.260  19.989  12.159  1.00 84.61           O  
ANISOU  710  O   PRO A 342    13002   8918  10228   2268   -182    816       O  
ATOM    711  CB  PRO A 342      14.330  22.152  10.977  1.00 76.22           C  
ANISOU  711  CB  PRO A 342    12966   7132   8861   1944    304    982       C  
ATOM    712  CG  PRO A 342      15.683  21.857  10.446  1.00 73.55           C  
ANISOU  712  CG  PRO A 342    12718   6698   8529   1562    442   1005       C  
ATOM    713  CD  PRO A 342      15.948  20.411  10.781  1.00 70.75           C  
ANISOU  713  CD  PRO A 342    11907   6605   8371   1380    293    960       C  
ATOM    714  N   GLU A 354       8.832  11.334   9.021  1.00 63.13           N  
ANISOU  714  N   GLU A 354     7808   8578   7600   2117  -1315    199       N  
ATOM    715  CA  GLU A 354       8.721  10.616  10.282  1.00 57.26           C  
ANISOU  715  CA  GLU A 354     6788   7908   7060   1919  -1253     71       C  
ATOM    716  C   GLU A 354       9.985  10.761  11.123  1.00 54.57           C  
ANISOU  716  C   GLU A 354     6663   7230   6840   1762  -1111    200       C  
ATOM    717  O   GLU A 354      11.110  10.712  10.617  1.00 61.11           O  
ANISOU  717  O   GLU A 354     7739   7855   7626   1660  -1067    338       O  
ATOM    718  CB  GLU A 354       8.422   9.134  10.043  1.00 68.60           C  
ANISOU  718  CB  GLU A 354     7899   9640   8526   1689  -1313   -112       C  
ATOM    719  CG  GLU A 354       8.527   8.266  11.301  1.00 64.74           C  
ANISOU  719  CG  GLU A 354     7184   9176   8237   1430  -1207   -239       C  
ATOM    720  CD  GLU A 354       8.036   6.854  11.083  1.00 68.17           C  
ANISOU  720  CD  GLU A 354     7334   9876   8692   1138  -1195   -457       C  
ATOM    721  OE1 GLU A 354       7.252   6.635  10.137  1.00 74.69           O  
ANISOU  721  OE1 GLU A 354     8018  10970   9392   1193  -1314   -576       O  
ATOM    722  OE2 GLU A 354       8.436   5.963  11.856  1.00 69.35           O  
ANISOU  722  OE2 GLU A 354     7481   9905   8966    810  -1010   -496       O  
ATOM    723  N   LEU A 355       9.772  10.918  12.429  1.00 55.82           N  
ANISOU  723  N   LEU A 355     6717   7349   7144   1734  -1034    133       N  
ATOM    724  CA  LEU A 355      10.872  11.172  13.346  1.00 49.97           C  
ANISOU  724  CA  LEU A 355     6181   6298   6507   1532   -873    224       C  
ATOM    725  C   LEU A 355      11.827   9.988  13.446  1.00 45.70           C  
ANISOU  725  C   LEU A 355     5590   5735   6038   1166   -790    226       C  
ATOM    726  O   LEU A 355      13.022  10.185  13.684  1.00 39.81           O  
ANISOU  726  O   LEU A 355     5039   4766   5322   1007   -690    328       O  
ATOM    727  CB  LEU A 355      10.308  11.533  14.717  1.00 52.73           C  
ANISOU  727  CB  LEU A 355     6426   6643   6967   1557   -795    126       C  
ATOM    728  CG  LEU A 355      11.313  11.979  15.772  1.00 49.17           C  
ANISOU  728  CG  LEU A 355     6191   5902   6592   1362   -641    190       C  
ATOM    729  CD1 LEU A 355      12.183  13.103  15.234  1.00 54.07           C  
ANISOU  729  CD1 LEU A 355     7199   6217   7127   1430   -598    347       C  
ATOM    730  CD2 LEU A 355      10.577  12.422  17.026  1.00 57.94           C  
ANISOU  730  CD2 LEU A 355     7221   7023   7769   1438   -571     80       C  
ATOM    731  N   LEU A 356      11.335   8.760  13.257  1.00 49.01           N  
ANISOU  731  N   LEU A 356     5758   6386   6478   1033   -820     99       N  
ATOM    732  CA  LEU A 356      12.181   7.590  13.475  1.00 43.83           C  
ANISOU  732  CA  LEU A 356     5095   5675   5882    733   -717    100       C  
ATOM    733  C   LEU A 356      13.377   7.574  12.533  1.00 28.80           C  
ANISOU  733  C   LEU A 356     3399   3630   3915    684   -704    239       C  
ATOM    734  O   LEU A 356      14.501   7.247  12.948  1.00 29.77           O  
ANISOU  734  O   LEU A 356     3602   3614   4095    518   -602    301       O  
ATOM    735  CB  LEU A 356      11.366   6.310  13.311  1.00 50.91           C  
ANISOU  735  CB  LEU A 356     5753   6803   6787    591   -717    -74       C  
ATOM    736  CG  LEU A 356      12.134   5.057  13.726  1.00 46.48           C  
ANISOU  736  CG  LEU A 356     5245   6136   6281    320   -574    -72       C  
ATOM    737  CD1 LEU A 356      12.694   5.182  15.140  1.00 39.63           C  
ANISOU  737  CD1 LEU A 356     4459   5103   5496    252   -463    -15       C  
ATOM    738  CD2 LEU A 356      11.245   3.834  13.608  1.00 53.78           C  
ANISOU  738  CD2 LEU A 356     5993   7239   7203    138   -522   -267       C  
ATOM    739  N   ALA A 357      13.150   7.890  11.255  1.00 35.13           N  
ANISOU  739  N   ALA A 357     4277   4492   4579    837   -805    276       N  
ATOM    740  CA  ALA A 357      14.257   7.984  10.307  1.00 36.25           C  
ANISOU  740  CA  ALA A 357     4642   4491   4639    790   -758    405       C  
ATOM    741  C   ALA A 357      15.304   8.969  10.794  1.00 33.99           C  
ANISOU  741  C   ALA A 357     4572   3947   4396    745   -641    527       C  
ATOM    742  O   ALA A 357      16.504   8.688  10.744  1.00 32.20           O  
ANISOU  742  O   ALA A 357     4406   3624   4206    563   -530    574       O  
ATOM    743  CB  ALA A 357      13.741   8.396   8.928  1.00 39.72           C  
ANISOU  743  CB  ALA A 357     5196   5020   4877   1009   -887    441       C  
ATOM    744  N   PHE A 358      14.865  10.108  11.330  1.00 33.84           N  
ANISOU  744  N   PHE A 358     4653   3828   4377    899   -652    552       N  
ATOM    745  CA  PHE A 358      15.809  11.100  11.825  1.00 38.56           C  
ANISOU  745  CA  PHE A 358     5476   4169   5006    808   -519    629       C  
ATOM    746  C   PHE A 358      16.547  10.618  13.066  1.00 35.00           C  
ANISOU  746  C   PHE A 358     4878   3718   4704    565   -441    566       C  
ATOM    747  O   PHE A 358      17.750  10.856  13.200  1.00 36.70           O  
ANISOU  747  O   PHE A 358     5176   3824   4945    379   -335    594       O  
ATOM    748  CB  PHE A 358      15.080  12.412  12.090  1.00 39.35           C  
ANISOU  748  CB  PHE A 358     5767   4132   5052   1053   -532    658       C  
ATOM    749  CG  PHE A 358      14.660  13.107  10.841  1.00 52.82           C  
ANISOU  749  CG  PHE A 358     7729   5777   6565   1325   -586    762       C  
ATOM    750  CD1 PHE A 358      15.542  13.930  10.171  1.00 52.14           C  
ANISOU  750  CD1 PHE A 358     7977   5451   6382   1230   -432    867       C  
ATOM    751  CD2 PHE A 358      13.397  12.904  10.309  1.00 59.43           C  
ANISOU  751  CD2 PHE A 358     8386   6875   7320   1570   -748    700       C  
ATOM    752  CE1 PHE A 358      15.164  14.566   9.002  1.00 60.23           C  
ANISOU  752  CE1 PHE A 358     9205   6462   7216   1415   -445    930       C  
ATOM    753  CE2 PHE A 358      13.014  13.533   9.141  1.00 61.83           C  
ANISOU  753  CE2 PHE A 358     8871   7188   7433   1761   -784    759       C  
ATOM    754  CZ  PHE A 358      13.899  14.367   8.487  1.00 64.15           C  
ANISOU  754  CZ  PHE A 358     9549   7209   7618   1702   -634    885       C  
ATOM    755  N   LEU A 359      15.855   9.947  13.988  1.00 29.14           N  
ANISOU  755  N   LEU A 359     3918   3114   4041    563   -487    470       N  
ATOM    756  CA  LEU A 359      16.533   9.421  15.171  1.00 27.83           C  
ANISOU  756  CA  LEU A 359     3653   2953   3966    378   -429    426       C  
ATOM    757  C   LEU A 359      17.603   8.411  14.784  1.00 31.00           C  
ANISOU  757  C   LEU A 359     3996   3403   4378    236   -394    452       C  
ATOM    758  O   LEU A 359      18.743   8.463  15.267  1.00 29.63           O  
ANISOU  758  O   LEU A 359     3822   3201   4236    109   -342    459       O  
ATOM    759  CB  LEU A 359      15.517   8.765  16.106  1.00 27.66           C  
ANISOU  759  CB  LEU A 359     3462   3056   3993    401   -450    327       C  
ATOM    760  CG  LEU A 359      14.396   9.665  16.644  1.00 41.69           C  
ANISOU  760  CG  LEU A 359     5239   4829   5774    562   -466    269       C  
ATOM    761  CD1 LEU A 359      13.520   8.872  17.610  1.00 42.98           C  
ANISOU  761  CD1 LEU A 359     5215   5130   5985    517   -435    150       C  
ATOM    762  CD2 LEU A 359      14.990  10.869  17.337  1.00 42.95           C  
ANISOU  762  CD2 LEU A 359     5591   4792   5935    544   -405    297       C  
ATOM    763  N   LEU A 360      17.236   7.449  13.941  1.00 25.21           N  
ANISOU  763  N   LEU A 360     3196   2769   3613    262   -423    442       N  
ATOM    764  CA  LEU A 360      18.207   6.434  13.562  1.00 30.78           C  
ANISOU  764  CA  LEU A 360     3868   3502   4323    165   -370    461       C  
ATOM    765  C   LEU A 360      19.352   7.051  12.760  1.00 27.62           C  
ANISOU  765  C   LEU A 360     3573   3031   3892    112   -307    529       C  
ATOM    766  O   LEU A 360      20.515   6.690  12.955  1.00 32.97           O  
ANISOU  766  O   LEU A 360     4191   3731   4605     21   -243    530       O  
ATOM    767  CB  LEU A 360      17.507   5.327  12.784  1.00 25.94           C  
ANISOU  767  CB  LEU A 360     3206   2983   3669    179   -389    411       C  
ATOM    768  CG  LEU A 360      16.525   4.507  13.646  1.00 35.97           C  
ANISOU  768  CG  LEU A 360     4369   4320   4976    145   -385    311       C  
ATOM    769  CD1 LEU A 360      15.883   3.453  12.817  1.00 35.88           C  
ANISOU  769  CD1 LEU A 360     4320   4397   4916     94   -377    223       C  
ATOM    770  CD2 LEU A 360      17.214   3.886  14.861  1.00 28.67           C  
ANISOU  770  CD2 LEU A 360     3455   3337   4100     85   -310    327       C  
ATOM    771  N   ASP A 361      19.046   8.013  11.895  1.00 27.47           N  
ANISOU  771  N   ASP A 361     3716   2930   3791    178   -311    581       N  
ATOM    772  CA  ASP A 361      20.085   8.669  11.097  1.00 25.10           C  
ANISOU  772  CA  ASP A 361     3572   2527   3439     89   -197    643       C  
ATOM    773  C   ASP A 361      21.032   9.491  11.968  1.00 34.37           C  
ANISOU  773  C   ASP A 361     4757   3622   4682    -73   -105    617       C  
ATOM    774  O   ASP A 361      22.248   9.465  11.760  1.00 29.39           O  
ANISOU  774  O   ASP A 361     4082   3013   4071   -236      8    598       O  
ATOM    775  CB  ASP A 361      19.419   9.542  10.036  1.00 33.73           C  
ANISOU  775  CB  ASP A 361     4917   3514   4383    233   -215    721       C  
ATOM    776  CG  ASP A 361      20.388  10.013   8.950  1.00 48.98           C  
ANISOU  776  CG  ASP A 361     7068   5326   6215    132    -61    793       C  
ATOM    777  OD1 ASP A 361      21.172   9.186   8.442  1.00 47.69           O  
ANISOU  777  OD1 ASP A 361     6810   5250   6062     23     11    773       O  
ATOM    778  OD2 ASP A 361      20.343  11.208   8.590  1.00 58.20           O  
ANISOU  778  OD2 ASP A 361     8535   6297   7282    170     13    869       O  
ATOM    779  N   GLY A 362      20.501  10.203  12.970  1.00 29.99           N  
ANISOU  779  N   GLY A 362     4235   3000   4161    -43   -144    588       N  
ATOM    780  CA  GLY A 362      21.351  11.007  13.828  1.00 24.87           C  
ANISOU  780  CA  GLY A 362     3605   2286   3559   -228    -60    529       C  
ATOM    781  C   GLY A 362      22.252  10.174  14.717  1.00 29.23           C  
ANISOU  781  C   GLY A 362     3887   3032   4187   -340    -90    447       C  
ATOM    782  O   GLY A 362      23.444  10.479  14.862  1.00 27.44           O  
ANISOU  782  O   GLY A 362     3586   2858   3980   -534     -8    379       O  
ATOM    783  N   LEU A 363      21.707   9.101  15.315  1.00 24.49           N  
ANISOU  783  N   LEU A 363     3141   2552   3613   -215   -197    441       N  
ATOM    784  CA  LEU A 363      22.565   8.162  16.036  1.00 21.99           C  
ANISOU  784  CA  LEU A 363     2622   2410   3325   -239   -232    396       C  
ATOM    785  C   LEU A 363      23.620   7.561  15.107  1.00 25.73           C  
ANISOU  785  C   LEU A 363     2997   2978   3801   -272   -167    406       C  
ATOM    786  O   LEU A 363      24.812   7.489  15.449  1.00 23.24           O  
ANISOU  786  O   LEU A 363     2512   2814   3505   -352   -150    338       O  
ATOM    787  CB  LEU A 363      21.709   7.053  16.658  1.00 25.09           C  
ANISOU  787  CB  LEU A 363     2977   2844   3712    -96   -306    412       C  
ATOM    788  CG  LEU A 363      20.806   7.514  17.815  1.00 36.90           C  
ANISOU  788  CG  LEU A 363     4524   4292   5204    -74   -348    375       C  
ATOM    789  CD1 LEU A 363      19.697   6.480  18.138  1.00 26.12           C  
ANISOU  789  CD1 LEU A 363     3158   2939   3830     23   -359    379       C  
ATOM    790  CD2 LEU A 363      21.673   7.796  19.042  1.00 31.24           C  
ANISOU  790  CD2 LEU A 363     3744   3659   4467   -149   -383    311       C  
ATOM    791  N   HIS A 364      23.184   7.094  13.933  1.00 24.33           N  
ANISOU  791  N   HIS A 364     2904   2748   3594   -201   -133    469       N  
ATOM    792  CA  HIS A 364      24.109   6.469  12.993  1.00 25.60           C  
ANISOU  792  CA  HIS A 364     2996   2985   3746   -218    -45    473       C  
ATOM    793  C   HIS A 364      25.266   7.397  12.671  1.00 19.76           C  
ANISOU  793  C   HIS A 364     2221   2271   3017   -413     80    423       C  
ATOM    794  O   HIS A 364      26.434   7.014  12.797  1.00 32.17           O  
ANISOU  794  O   HIS A 364     3577   4022   4625   -459    125    351       O  
ATOM    795  CB  HIS A 364      23.386   6.078  11.708  1.00 31.09           C  
ANISOU  795  CB  HIS A 364     3838   3601   4373   -147    -22    533       C  
ATOM    796  CG  HIS A 364      24.323   5.810  10.568  1.00 28.30           C  
ANISOU  796  CG  HIS A 364     3484   3282   3986   -198    112    535       C  
ATOM    797  ND1 HIS A 364      25.255   4.793  10.602  1.00 26.30           N  
ANISOU  797  ND1 HIS A 364     3063   3161   3770   -153    162    495       N  
ATOM    798  CD2 HIS A 364      24.507   6.453   9.388  1.00 28.78           C  
ANISOU  798  CD2 HIS A 364     3710   3260   3966   -277    225    571       C  
ATOM    799  CE1 HIS A 364      25.959   4.810   9.478  1.00 33.97           C  
ANISOU  799  CE1 HIS A 364     4060   4146   4700   -217    308    490       C  
ATOM    800  NE2 HIS A 364      25.533   5.815   8.730  1.00 30.61           N  
ANISOU  800  NE2 HIS A 364     3849   3585   4197   -311    355    538       N  
ATOM    801  N   GLU A 365      24.969   8.650  12.283  1.00 22.81           N  
ANISOU  801  N   GLU A 365     2822   2481   3364   -528    154    446       N  
ATOM    802  CA  GLU A 365      26.077   9.513  11.869  1.00 30.21           C  
ANISOU  802  CA  GLU A 365     3775   3405   4298   -777    339    382       C  
ATOM    803  C   GLU A 365      26.944   9.908  13.054  1.00 35.30           C  
ANISOU  803  C   GLU A 365     4198   4203   5012   -952    329    235       C  
ATOM    804  O   GLU A 365      28.168  10.057  12.903  1.00 31.06           O  
ANISOU  804  O   GLU A 365     3473   3823   4503  -1155    453    116       O  
ATOM    805  CB  GLU A 365      25.585  10.770  11.136  1.00 33.16           C  
ANISOU  805  CB  GLU A 365     4528   3493   4578   -854    462    455       C  
ATOM    806  CG  GLU A 365      24.850  10.510   9.805  1.00 35.52           C  
ANISOU  806  CG  GLU A 365     5060   3679   4755   -681    467    589       C  
ATOM    807  CD  GLU A 365      25.739   9.896   8.703  1.00 44.87           C  
ANISOU  807  CD  GLU A 365     6190   4954   5902   -758    614    583       C  
ATOM    808  OE1 GLU A 365      26.965   9.729   8.885  1.00 33.68           O  
ANISOU  808  OE1 GLU A 365     4539   3693   4563   -942    735    472       O  
ATOM    809  OE2 GLU A 365      25.188   9.572   7.638  1.00 34.60           O  
ANISOU  809  OE2 GLU A 365     5069   3595   4482   -622    605    673       O  
ATOM    810  N   ASP A 366      26.347  10.078  14.240  1.00 28.95           N  
ANISOU  810  N   ASP A 366     3388   3387   4223   -888    186    216       N  
ATOM    811  CA  ASP A 366      27.161  10.347  15.421  1.00 27.02           C  
ANISOU  811  CA  ASP A 366     2922   3334   4011  -1035    139     59       C  
ATOM    812  C   ASP A 366      28.056   9.172  15.797  1.00 27.99           C  
ANISOU  812  C   ASP A 366     2685   3792   4156   -917     38     -1       C  
ATOM    813  O   ASP A 366      29.000   9.355  16.574  1.00 31.40           O  
ANISOU  813  O   ASP A 366     2864   4473   4595  -1037     -4   -160       O  
ATOM    814  CB  ASP A 366      26.257  10.693  16.612  1.00 26.27           C  
ANISOU  814  CB  ASP A 366     2932   3149   3899   -962     11     59       C  
ATOM    815  CG  ASP A 366      26.052  12.186  16.778  1.00 42.31           C  
ANISOU  815  CG  ASP A 366     5220   4945   5910  -1176    131      2       C  
ATOM    816  OD1 ASP A 366      26.601  12.986  15.978  1.00 33.99           O  
ANISOU  816  OD1 ASP A 366     4302   3767   4845  -1402    328    -30       O  
ATOM    817  OD2 ASP A 366      25.342  12.562  17.730  1.00 46.78           O  
ANISOU  817  OD2 ASP A 366     5888   5427   6459  -1122     56    -15       O  
ATOM    818  N   LEU A 367      27.763   7.967  15.298  1.00 27.08           N  
ANISOU  818  N   LEU A 367     2556   3696   4038   -667     -6    109       N  
ATOM    819  CA  LEU A 367      28.558   6.784  15.617  1.00 29.41           C  
ANISOU  819  CA  LEU A 367     2581   4260   4333   -476    -86     78       C  
ATOM    820  C   LEU A 367      29.161   6.135  14.370  1.00 33.86           C  
ANISOU  820  C   LEU A 367     3074   4877   4914   -427     48     96       C  
ATOM    821  O   LEU A 367      29.550   4.960  14.403  1.00 28.65           O  
ANISOU  821  O   LEU A 367     2286   4356   4244   -183      4    114       O  
ATOM    822  CB  LEU A 367      27.704   5.766  16.380  1.00 23.78           C  
ANISOU  822  CB  LEU A 367     1963   3496   3578   -199   -233    179       C  
ATOM    823  CG  LEU A 367      27.175   6.336  17.712  1.00 27.21           C  
ANISOU  823  CG  LEU A 367     2456   3907   3977   -235   -351    148       C  
ATOM    824  CD1 LEU A 367      26.009   5.506  18.239  1.00 26.57           C  
ANISOU  824  CD1 LEU A 367     2561   3682   3852    -35   -418    259       C  
ATOM    825  CD2 LEU A 367      28.290   6.410  18.749  1.00 30.41           C  
ANISOU  825  CD2 LEU A 367     2593   4624   4339   -241   -465     11       C  
ATOM    826  N   ASN A 368      29.280   6.877  13.284  1.00 26.82           N  
ANISOU  826  N   ASN A 368     2298   3864   4029   -640    230     92       N  
ATOM    827  CA  ASN A 368      29.733   6.274  12.038  1.00 27.45           C  
ANISOU  827  CA  ASN A 368     2364   3965   4101   -598    378    114       C  
ATOM    828  C   ASN A 368      31.234   5.999  12.111  1.00 29.93           C  
ANISOU  828  C   ASN A 368     2285   4625   4461   -630    447    -46       C  
ATOM    829  O   ASN A 368      32.035   6.912  12.333  1.00 37.74           O  
ANISOU  829  O   ASN A 368     3095   5763   5483   -907    532   -201       O  
ATOM    830  CB  ASN A 368      29.383   7.185  10.869  1.00 25.81           C  
ANISOU  830  CB  ASN A 368     2450   3514   3843   -801    560    169       C  
ATOM    831  CG  ASN A 368      29.452   6.470   9.520  1.00 39.28           C  
ANISOU  831  CG  ASN A 368     4252   5177   5496   -717    689    229       C  
ATOM    832  OD1 ASN A 368      30.006   5.372   9.408  1.00 29.72           O  
ANISOU  832  OD1 ASN A 368     2848   4136   4310   -548    692    197       O  
ATOM    833  ND2 ASN A 368      28.898   7.105   8.487  1.00 28.71           N  
ANISOU  833  ND2 ASN A 368     3243   3606   4060   -809    800    316       N  
ATOM    834  N   ARG A 369      31.611   4.733  11.931  1.00 36.95           N  
ANISOU  834  N   ARG A 369     3037   5653   5349   -344    423    -28       N  
ATOM    835  CA  ARG A 369      33.014   4.340  11.989  1.00 35.31           C  
ANISOU  835  CA  ARG A 369     2416   5821   5179   -279    470   -184       C  
ATOM    836  C   ARG A 369      33.804   4.831  10.787  1.00 33.71           C  
ANISOU  836  C   ARG A 369     2130   5676   5003   -541    754   -285       C  
ATOM    837  O   ARG A 369      35.041   4.790  10.815  1.00 38.00           O  
ANISOU  837  O   ARG A 369     2265   6579   5592   -582    833   -470       O  
ATOM    838  CB  ARG A 369      33.120   2.809  12.110  1.00 41.89           C  
ANISOU  838  CB  ARG A 369     3206   6728   5984    165    385   -115       C  
ATOM    839  CG  ARG A 369      32.551   2.250  13.417  1.00 37.64           C  
ANISOU  839  CG  ARG A 369     2743   6166   5392    431    138    -32       C  
ATOM    840  CD  ARG A 369      32.116   0.784  13.299  1.00 40.74           C  
ANISOU  840  CD  ARG A 369     3358   6396   5726    807    126    103       C  
ATOM    841  NE  ARG A 369      31.429   0.343  14.517  1.00 40.97           N  
ANISOU  841  NE  ARG A 369     3552   6331   5683    998    -57    196       N  
ATOM    842  CZ  ARG A 369      30.479  -0.588  14.554  1.00 42.03           C  
ANISOU  842  CZ  ARG A 369     4034   6175   5759   1158    -45    328       C  
ATOM    843  NH1 ARG A 369      30.087  -1.190  13.436  1.00 39.59           N  
ANISOU  843  NH1 ARG A 369     3931   5656   5456   1154    116    372       N  
ATOM    844  NH2 ARG A 369      29.911  -0.914  15.713  1.00 38.86           N  
ANISOU  844  NH2 ARG A 369     3790   5694   5280   1292   -175    400       N  
ATOM    845  N   ILE A 370      33.121   5.293   9.745  1.00 33.07           N  
ANISOU  845  N   ILE A 370     2419   5271   4875   -709    910   -178       N  
ATOM    846  CA  ILE A 370      33.782   5.858   8.576  1.00 36.26           C  
ANISOU  846  CA  ILE A 370     2843   5669   5264   -989   1216   -252       C  
ATOM    847  C   ILE A 370      34.050   7.330   8.844  1.00 36.84           C  
ANISOU  847  C   ILE A 370     2938   5709   5352  -1414   1333   -361       C  
ATOM    848  O   ILE A 370      33.134   8.080   9.206  1.00 34.66           O  
ANISOU  848  O   ILE A 370     2970   5161   5039  -1494   1248   -264       O  
ATOM    849  CB  ILE A 370      32.914   5.680   7.318  1.00 40.53           C  
ANISOU  849  CB  ILE A 370     3829   5876   5696   -946   1321    -79       C  
ATOM    850  CG1 ILE A 370      32.546   4.201   7.077  1.00 37.75           C  
ANISOU  850  CG1 ILE A 370     3509   5516   5320   -569   1221      5       C  
ATOM    851  CG2 ILE A 370      33.583   6.338   6.134  1.00 39.93           C  
ANISOU  851  CG2 ILE A 370     3844   5762   5565  -1245   1660   -141       C  
ATOM    852  CD1 ILE A 370      33.726   3.227   6.919  1.00 41.54           C  
ANISOU  852  CD1 ILE A 370     3640   6293   5851   -385   1322   -118       C  
ATOM    853  N   ARG A 371      35.300   7.748   8.666  1.00 44.78           N  
ANISOU  853  N   ARG A 371     3646   6969   6400  -1671   1530   -569       N  
ATOM    854  CA  ARG A 371      35.695   9.119   8.955  1.00 56.66           C  
ANISOU  854  CA  ARG A 371     5258   8386   7883  -2022   1597   -676       C  
ATOM    855  C   ARG A 371      35.426  10.066   7.790  1.00 64.61           C  
ANISOU  855  C   ARG A 371     6755   9011   8782  -2276   1872   -592       C  
ATOM    856  O   ARG A 371      34.969  11.192   8.010  1.00 69.66           O  
ANISOU  856  O   ARG A 371     7725   9377   9366  -2463   1899   -565       O  
ATOM    857  CB  ARG A 371      37.178   9.154   9.353  1.00 59.89           C  
ANISOU  857  CB  ARG A 371     5226   9189   8341  -2097   1595   -924       C  
ATOM    858  CG  ARG A 371      37.486   8.309  10.599  1.00 61.66           C  
ANISOU  858  CG  ARG A 371     5031   9778   8619  -1784   1279   -992       C  
ATOM    859  CD  ARG A 371      38.954   8.360  11.015  1.00 73.42           C  
ANISOU  859  CD  ARG A 371     6095  11673  10127  -1834   1255  -1241       C  
ATOM    860  NE  ARG A 371      39.268   9.518  11.848  1.00 79.23           N  
ANISOU  860  NE  ARG A 371     6821  12448  10835  -2152   1223  -1414       N  
ATOM    861  CZ  ARG A 371      39.313   9.497  13.178  1.00 81.29           C  
ANISOU  861  CZ  ARG A 371     6905  12905  11075  -2042    952  -1487       C  
ATOM    862  NH1 ARG A 371      39.066   8.374  13.838  1.00 81.90           N  
ANISOU  862  NH1 ARG A 371     6828  13140  11149  -1604    682  -1384       N  
ATOM    863  NH2 ARG A 371      39.607  10.601  13.850  1.00 87.82           N  
ANISOU  863  NH2 ARG A 371     7752  13756  11862  -2364    965  -1664       N  
ATOM    864  N   LYS A 372      35.695   9.643   6.554  1.00 44.08           N  
ANISOU  864  N   LYS A 372     4246   6376   6127  -2248   2073   -548       N  
ATOM    865  CA  LYS A 372      35.431  10.464   5.370  1.00 49.50           C  
ANISOU  865  CA  LYS A 372     5443   6700   6664  -2422   2312   -450       C  
ATOM    866  C   LYS A 372      34.780   9.576   4.321  1.00 54.49           C  
ANISOU  866  C   LYS A 372     6293   7207   7204  -2195   2361   -268       C  
ATOM    867  O   LYS A 372      35.422   8.648   3.813  1.00 49.50           O  
ANISOU  867  O   LYS A 372     5410   6797   6599  -2089   2447   -332       O  
ATOM    868  CB  LYS A 372      36.711  11.094   4.814  1.00 50.12           C  
ANISOU  868  CB  LYS A 372     5444   6874   6725  -2712   2569   -647       C  
ATOM    869  CG  LYS A 372      36.467  12.106   3.694  1.00 60.71           C  
ANISOU  869  CG  LYS A 372     7360   7817   7889  -2897   2819   -564       C  
ATOM    870  CD  LYS A 372      37.757  12.466   2.966  1.00 71.23           C  
ANISOU  870  CD  LYS A 372     8601   9260   9202  -3175   3117   -766       C  
ATOM    871  CE  LYS A 372      37.535  13.534   1.892  1.00 79.57           C  
ANISOU  871  CE  LYS A 372    10272   9898  10061  -3355   3379   -695       C  
ATOM    872  NZ  LYS A 372      36.572  13.119   0.834  1.00 78.47           N  
ANISOU  872  NZ  LYS A 372    10554   9500   9761  -3099   3368   -437       N  
ATOM    873  N   LYS A 373      33.522   9.866   3.990  1.00 51.56           N  
ANISOU  873  N   LYS A 373     6396   6489   6705  -2098   2298    -55       N  
ATOM    874  CA  LYS A 373      32.750   9.019   3.081  1.00 39.15           C  
ANISOU  874  CA  LYS A 373     5063   4799   5011  -1866   2295    115       C  
ATOM    875  C   LYS A 373      33.291   9.157   1.665  1.00 45.58           C  
ANISOU  875  C   LYS A 373     6106   5537   5674  -1946   2538    109       C  
ATOM    876  O   LYS A 373      33.380  10.283   1.151  1.00 51.27           O  
ANISOU  876  O   LYS A 373     7165   6037   6279  -2113   2662    121       O  
ATOM    877  CB  LYS A 373      31.272   9.391   3.114  1.00 40.61           C  
ANISOU  877  CB  LYS A 373     5681   4674   5075  -1693   2094    327       C  
ATOM    878  CG  LYS A 373      30.596   9.188   4.467  1.00 33.94           C  
ANISOU  878  CG  LYS A 373     4633   3895   4366  -1509   1752    332       C  
ATOM    879  CD  LYS A 373      29.078   9.420   4.390  1.00 39.91           C  
ANISOU  879  CD  LYS A 373     5758   4404   5001  -1273   1526    516       C  
ATOM    880  CE  LYS A 373      28.426   9.227   5.777  1.00 30.75           C  
ANISOU  880  CE  LYS A 373     4390   3315   3978  -1122   1232    503       C  
ATOM    881  NZ  LYS A 373      27.019   8.730   5.714  1.00 39.15           N  
ANISOU  881  NZ  LYS A 373     5597   4306   4973   -824    978    621       N  
ATOM    882  N   PRO A 374      33.675   8.069   1.007  1.00 45.27           N  
ANISOU  882  N   PRO A 374     5917   5659   5624  -1825   2632     76       N  
ATOM    883  CA  PRO A 374      34.123   8.173  -0.385  1.00 51.95           C  
ANISOU  883  CA  PRO A 374     7015   6418   6308  -1897   2863     73       C  
ATOM    884  C   PRO A 374      32.940   8.355  -1.322  1.00 44.04           C  
ANISOU  884  C   PRO A 374     6581   5102   5050  -1752   2794    282       C  
ATOM    885  O   PRO A 374      31.828   7.896  -1.055  1.00 45.27           O  
ANISOU  885  O   PRO A 374     6853   5190   5158  -1533   2574    414       O  
ATOM    886  CB  PRO A 374      34.827   6.830  -0.629  1.00 50.86           C  
ANISOU  886  CB  PRO A 374     6508   6569   6249  -1754   2949    -37       C  
ATOM    887  CG  PRO A 374      34.112   5.862   0.287  1.00 43.37           C  
ANISOU  887  CG  PRO A 374     5363   5712   5405  -1493   2732     11       C  
ATOM    888  CD  PRO A 374      33.670   6.675   1.497  1.00 42.93           C  
ANISOU  888  CD  PRO A 374     5255   5606   5451  -1568   2514     38       C  
ATOM    889  N   TYR A 375      33.173   9.077  -2.411  1.00 47.80           N  
ANISOU  889  N   TYR A 375     7416   5398   5349  -1866   2971    299       N  
ATOM    890  CA  TYR A 375      32.188   9.100  -3.482  1.00 53.63           C  
ANISOU  890  CA  TYR A 375     8652   5912   5813  -1679   2897    468       C  
ATOM    891  C   TYR A 375      32.140   7.725  -4.134  1.00 61.48           C  
ANISOU  891  C   TYR A 375     9565   7050   6743  -1513   2902    459       C  
ATOM    892  O   TYR A 375      33.181   7.149  -4.467  1.00 66.84           O  
ANISOU  892  O   TYR A 375     9995   7903   7499  -1601   3115    319       O  
ATOM    893  CB  TYR A 375      32.515  10.169  -4.531  1.00 61.02           C  
ANISOU  893  CB  TYR A 375    10008   6617   6559  -1825   3110    479       C  
ATOM    894  CG  TYR A 375      31.663  10.010  -5.772  1.00 65.06           C  
ANISOU  894  CG  TYR A 375    10977   6974   6771  -1606   3037    623       C  
ATOM    895  CD1 TYR A 375      30.313  10.356  -5.763  1.00 58.72           C  
ANISOU  895  CD1 TYR A 375    10480   6023   5808  -1348   2756    789       C  
ATOM    896  CD2 TYR A 375      32.196   9.469  -6.945  1.00 68.62           C  
ANISOU  896  CD2 TYR A 375    11522   7461   7091  -1637   3230    575       C  
ATOM    897  CE1 TYR A 375      29.521  10.177  -6.894  1.00 62.60           C  
ANISOU  897  CE1 TYR A 375    11339   6436   6010  -1126   2648    896       C  
ATOM    898  CE2 TYR A 375      31.415   9.291  -8.074  1.00 67.06           C  
ANISOU  898  CE2 TYR A 375    11728   7149   6601  -1437   3140    689       C  
ATOM    899  CZ  TYR A 375      30.082   9.647  -8.044  1.00 68.31           C  
ANISOU  899  CZ  TYR A 375    12166   7192   6597  -1182   2839    846       C  
ATOM    900  OH  TYR A 375      29.311   9.470  -9.167  1.00 75.53           O  
ANISOU  900  OH  TYR A 375    13440   8050   7208   -971   2719    936       O  
ATOM    901  N   ILE A 376      30.935   7.187  -4.305  1.00 64.77           N  
ANISOU  901  N   ILE A 376    10183   7410   7016  -1265   2666    584       N  
ATOM    902  CA  ILE A 376      30.754   5.870  -4.904  1.00 60.36           C  
ANISOU  902  CA  ILE A 376     9606   6961   6368  -1109   2657    556       C  
ATOM    903  C   ILE A 376      29.781   5.981  -6.070  1.00 69.49           C  
ANISOU  903  C   ILE A 376    11234   7973   7196   -961   2527    666       C  
ATOM    904  O   ILE A 376      28.678   6.518  -5.915  1.00 74.25           O  
ANISOU  904  O   ILE A 376    12054   8473   7683   -822   2273    790       O  
ATOM    905  CB  ILE A 376      30.254   4.838  -3.876  1.00 64.94           C  
ANISOU  905  CB  ILE A 376     9891   7675   7108   -943   2462    536       C  
ATOM    906  CG1 ILE A 376      31.354   4.560  -2.850  1.00 61.34           C  
ANISOU  906  CG1 ILE A 376     8912   7423   6972  -1018   2558    392       C  
ATOM    907  CG2 ILE A 376      29.823   3.563  -4.582  1.00 66.76           C  
ANISOU  907  CG2 ILE A 376    10192   7957   7218   -757   2383    490       C  
ATOM    908  CD1 ILE A 376      30.986   3.552  -1.814  1.00 53.10           C  
ANISOU  908  CD1 ILE A 376     7546   6502   6128   -785   2273    348       C  
ATOM    909  N   GLN A 377      30.193   5.481  -7.233  1.00 76.77           N  
ANISOU  909  N   GLN A 377    12292   8911   7966   -971   2689    609       N  
ATOM    910  CA  GLN A 377      29.321   5.395  -8.398  1.00 89.49           C  
ANISOU  910  CA  GLN A 377    14309  10443   9249   -822   2557    680       C  
ATOM    911  C   GLN A 377      28.506   4.107  -8.305  1.00 96.02           C  
ANISOU  911  C   GLN A 377    15067  11403  10015   -650   2354    635       C  
ATOM    912  O   GLN A 377      29.069   3.009  -8.222  1.00100.02           O  
ANISOU  912  O   GLN A 377    15351  12019  10633   -666   2494    507       O  
ATOM    913  CB  GLN A 377      30.134   5.466  -9.697  1.00 94.74           C  
ANISOU  913  CB  GLN A 377    15179  11054   9764   -932   2832    628       C  
ATOM    914  CG  GLN A 377      31.025   4.260 -10.037  1.00100.28           C  
ANISOU  914  CG  GLN A 377    15649  11905  10549   -979   3055    468       C  
ATOM    915  CD  GLN A 377      32.162   4.034  -9.052  1.00100.71           C  
ANISOU  915  CD  GLN A 377    15213  12107  10945  -1103   3243    348       C  
ATOM    916  OE1 GLN A 377      32.395   4.840  -8.152  1.00 99.21           O  
ANISOU  916  OE1 GLN A 377    14855  11911  10928  -1212   3233    370       O  
ATOM    917  NE2 GLN A 377      32.877   2.928  -9.223  1.00100.06           N  
ANISOU  917  NE2 GLN A 377    14892  12175  10953  -1064   3405    207       N  
ATOM    918  N   LEU A 378      27.181   4.244  -8.281  1.00 94.54           N  
ANISOU  918  N   LEU A 378    15056  11211   9654   -477   2026    719       N  
ATOM    919  CA  LEU A 378      26.283   3.100  -8.153  1.00 94.89           C  
ANISOU  919  CA  LEU A 378    15049  11389   9616   -353   1811    644       C  
ATOM    920  C   LEU A 378      25.948   2.585  -9.546  1.00 95.85           C  
ANISOU  920  C   LEU A 378    15437  11554   9428   -300   1779    576       C  
ATOM    921  O   LEU A 378      25.177   3.214 -10.279  1.00 94.44           O  
ANISOU  921  O   LEU A 378    15523  11369   8991   -184   1581    654       O  
ATOM    922  CB  LEU A 378      25.014   3.479  -7.393  1.00 96.60           C  
ANISOU  922  CB  LEU A 378    15206  11646   9850   -200   1427    709       C  
ATOM    923  CG  LEU A 378      24.035   2.327  -7.140  1.00 97.91           C  
ANISOU  923  CG  LEU A 378    15163  11977  10062   -113   1142    556       C  
ATOM    924  CD1 LEU A 378      24.557   1.397  -6.048  1.00 97.26           C  
ANISOU  924  CD1 LEU A 378    14681  11914  10362   -180   1215    444       C  
ATOM    925  CD2 LEU A 378      22.642   2.844  -6.799  1.00 98.86           C  
ANISOU  925  CD2 LEU A 378    15272  12188  10102     53    756    598       C  
ATOM    926  N   LYS A 379      26.522   1.441  -9.911  1.00 93.59           N  
ANISOU  926  N   LYS A 379    15075  11315   9171   -364   1969    424       N  
ATOM    927  CA  LYS A 379      26.267   0.855 -11.217  1.00 88.68           C  
ANISOU  927  CA  LYS A 379    14694  10732   8267   -342   1957    333       C  
ATOM    928  C   LYS A 379      24.883   0.221 -11.254  1.00 86.88           C  
ANISOU  928  C   LYS A 379    14516  10647   7849   -246   1610    241       C  
ATOM    929  O   LYS A 379      24.421  -0.363 -10.268  1.00 89.18           O  
ANISOU  929  O   LYS A 379    14587  10994   8303   -240   1484    164       O  
ATOM    930  CB  LYS A 379      27.316  -0.205 -11.556  1.00 88.26           C  
ANISOU  930  CB  LYS A 379    14539  10670   8327   -426   2275    180       C  
ATOM    931  CG  LYS A 379      28.746   0.131 -11.174  1.00 84.58           C  
ANISOU  931  CG  LYS A 379    13849  10155   8133   -524   2607    196       C  
ATOM    932  CD  LYS A 379      29.652  -1.021 -11.583  1.00 85.05           C  
ANISOU  932  CD  LYS A 379    13799  10241   8276   -531   2874     30       C  
ATOM    933  CE  LYS A 379      30.906  -1.096 -10.735  1.00 86.33           C  
ANISOU  933  CE  LYS A 379    13566  10458   8778   -554   3120    -13       C  
ATOM    934  NZ  LYS A 379      31.570  -2.421 -10.895  1.00 82.42           N  
ANISOU  934  NZ  LYS A 379    12933  10001   8382   -458   3306   -178       N  
ATOM    935  N   ASP A 380      24.219   0.343 -12.400  1.00 96.57           N  
ANISOU  935  N   ASP A 380    15992  11952   8749   -179   1441    227       N  
ATOM    936  CA  ASP A 380      23.009  -0.427 -12.623  1.00 94.76           C  
ANISOU  936  CA  ASP A 380    15756  11922   8327   -137   1134     60       C  
ATOM    937  C   ASP A 380      23.371  -1.904 -12.733  1.00 87.65           C  
ANISOU  937  C   ASP A 380    14790  11010   7504   -277   1321   -172       C  
ATOM    938  O   ASP A 380      24.526  -2.267 -12.975  1.00 89.77           O  
ANISOU  938  O   ASP A 380    15068  11142   7900   -345   1664   -184       O  
ATOM    939  CB  ASP A 380      22.291   0.051 -13.885  1.00 99.13           C  
ANISOU  939  CB  ASP A 380    16553  12606   8504    -18    916     86       C  
ATOM    940  CG  ASP A 380      20.791  -0.131 -13.802  1.00104.21           C  
ANISOU  940  CG  ASP A 380    17080  13535   8979     85    476    -34       C  
ATOM    941  OD1 ASP A 380      20.217   0.150 -12.729  1.00100.33           O  
ANISOU  941  OD1 ASP A 380    16475  13103   8544    233    238     77       O  
ATOM    942  OD2 ASP A 380      20.189  -0.559 -14.807  1.00111.89           O  
ANISOU  942  OD2 ASP A 380    18047  14688   9776      9    375   -261       O  
ATOM    943  N   ALA A 381      22.368  -2.763 -12.535  1.00 77.81           N  
ANISOU  943  N   ALA A 381    13458   9906   6199   -322   1097   -376       N  
ATOM    944  CA  ALA A 381      22.619  -4.203 -12.512  1.00 67.73           C  
ANISOU  944  CA  ALA A 381    12136   8561   5035   -461   1281   -607       C  
ATOM    945  C   ALA A 381      23.408  -4.664 -13.739  1.00 69.01           C  
ANISOU  945  C   ALA A 381    12497   8647   5076   -497   1534   -658       C  
ATOM    946  O   ALA A 381      24.311  -5.501 -13.619  1.00 69.33           O  
ANISOU  946  O   ALA A 381    12502   8526   5313   -538   1839   -730       O  
ATOM    947  CB  ALA A 381      21.302  -4.966 -12.407  1.00 62.88           C  
ANISOU  947  CB  ALA A 381    11439   8126   4327   -562    996   -853       C  
ATOM    948  N   ASP A 382      23.105  -4.104 -14.917  1.00 56.51           N  
ANISOU  948  N   ASP A 382    11123   7178   3168   -451   1413   -614       N  
ATOM    949  CA  ASP A 382      23.790  -4.475 -16.173  1.00 64.91           C  
ANISOU  949  CA  ASP A 382    12409   8181   4071   -491   1642   -664       C  
ATOM    950  C   ASP A 382      23.645  -5.970 -16.452  1.00 67.44           C  
ANISOU  950  C   ASP A 382    12739   8487   4400   -618   1721   -940       C  
ATOM    951  O   ASP A 382      24.580  -6.632 -16.902  1.00 67.54           O  
ANISOU  951  O   ASP A 382    12835   8345   4482   -655   2036   -996       O  
ATOM    952  CB  ASP A 382      25.272  -4.066 -16.138  1.00 66.59           C  
ANISOU  952  CB  ASP A 382    12627   8191   4482   -483   2027   -514       C  
ATOM    953  CG  ASP A 382      25.976  -4.211 -17.495  1.00 79.61           C  
ANISOU  953  CG  ASP A 382    14523   9788   5936   -518   2260   -542       C  
ATOM    954  OD1 ASP A 382      25.733  -3.372 -18.388  1.00 80.07           O  
ANISOU  954  OD1 ASP A 382    14815   9900   5706   -474   2167   -433       O  
ATOM    955  OD2 ASP A 382      26.777  -5.161 -17.659  1.00 81.75           O  
ANISOU  955  OD2 ASP A 382    14765   9957   6340   -570   2542   -667       O  
ATOM    956  N   GLY A 383      22.472  -6.521 -16.144  1.00 76.64           N  
ANISOU  956  N   GLY A 383    13802   9804   5514   -693   1448  -1125       N  
ATOM    957  CA  GLY A 383      22.238  -7.937 -16.342  1.00 79.38           C  
ANISOU  957  CA  GLY A 383    14167  10103   5890   -853   1528  -1399       C  
ATOM    958  C   GLY A 383      23.084  -8.869 -15.497  1.00 77.41           C  
ANISOU  958  C   GLY A 383    13844   9564   6006   -884   1851  -1429       C  
ATOM    959  O   GLY A 383      23.017 -10.087 -15.700  1.00 66.76           O  
ANISOU  959  O   GLY A 383    12567   8102   4695  -1001   1972  -1629       O  
ATOM    960  N   ARG A 384      23.885  -8.344 -14.569  1.00 57.50           N  
ANISOU  960  N   ARG A 384    11182   6919   3747   -764   1995  -1236       N  
ATOM    961  CA  ARG A 384      24.617  -9.192 -13.648  1.00 55.99           C  
ANISOU  961  CA  ARG A 384    10881   6498   3894   -723   2251  -1256       C  
ATOM    962  C   ARG A 384      23.633  -9.883 -12.706  1.00 54.66           C  
ANISOU  962  C   ARG A 384    10612   6306   3849   -833   2097  -1395       C  
ATOM    963  O   ARG A 384      22.491  -9.443 -12.563  1.00 54.17           O  
ANISOU  963  O   ARG A 384    10477   6444   3660   -926   1786  -1447       O  
ATOM    964  CB  ARG A 384      25.632  -8.369 -12.851  1.00 53.51           C  
ANISOU  964  CB  ARG A 384    10384   6135   3812   -563   2397  -1034       C  
ATOM    965  CG  ARG A 384      26.794  -7.815 -13.684  1.00 55.26           C  
ANISOU  965  CG  ARG A 384    10662   6350   3984   -497   2632   -924       C  
ATOM    966  CD  ARG A 384      27.705  -6.939 -12.830  1.00 59.90           C  
ANISOU  966  CD  ARG A 384    11006   6940   4815   -394   2753   -739       C  
ATOM    967  NE  ARG A 384      27.003  -5.761 -12.328  1.00 51.03           N  
ANISOU  967  NE  ARG A 384     9834   5921   3636   -415   2500   -593       N  
ATOM    968  CZ  ARG A 384      27.403  -5.038 -11.285  1.00 61.90           C  
ANISOU  968  CZ  ARG A 384    10982   7305   5232   -362   2521   -453       C  
ATOM    969  NH1 ARG A 384      28.499  -5.371 -10.615  1.00 59.01           N  
ANISOU  969  NH1 ARG A 384    10374   6893   5156   -276   2762   -453       N  
ATOM    970  NH2 ARG A 384      26.701  -3.983 -10.902  1.00 51.58           N  
ANISOU  970  NH2 ARG A 384     9676   6069   3852   -375   2286   -318       N  
ATOM    971  N   PRO A 385      24.038 -10.989 -12.080  1.00 54.56           N  
ANISOU  971  N   PRO A 385    10599   6054   4079   -817   2311  -1461       N  
ATOM    972  CA  PRO A 385      23.134 -11.664 -11.140  1.00 53.66           C  
ANISOU  972  CA  PRO A 385    10417   5873   4099   -947   2208  -1579       C  
ATOM    973  C   PRO A 385      22.807 -10.786  -9.943  1.00 50.13           C  
ANISOU  973  C   PRO A 385     9745   5514   3788   -887   2038  -1452       C  
ATOM    974  O   PRO A 385      23.594  -9.926  -9.540  1.00 48.13           O  
ANISOU  974  O   PRO A 385     9385   5277   3627   -702   2096  -1253       O  
ATOM    975  CB  PRO A 385      23.914 -12.915 -10.718  1.00 61.78           C  
ANISOU  975  CB  PRO A 385    11546   6575   5353   -856   2519  -1594       C  
ATOM    976  CG  PRO A 385      25.289 -12.771 -11.293  1.00 62.21           C  
ANISOU  976  CG  PRO A 385    11636   6576   5424   -638   2759  -1482       C  
ATOM    977  CD  PRO A 385      25.218 -11.806 -12.411  1.00 56.37           C  
ANISOU  977  CD  PRO A 385    10934   6066   4417   -695   2649  -1461       C  
ATOM    978  N   ASP A 386      21.614 -11.011  -9.384  1.00 49.73           N  
ANISOU  978  N   ASP A 386     9608   5537   3752  -1071   1836  -1585       N  
ATOM    979  CA  ASP A 386      21.194 -10.290  -8.184  1.00 46.66           C  
ANISOU  979  CA  ASP A 386     9012   5221   3495  -1038   1675  -1495       C  
ATOM    980  C   ASP A 386      22.213 -10.427  -7.066  1.00 44.49           C  
ANISOU  980  C   ASP A 386     8645   4714   3547   -816   1878  -1304       C  
ATOM    981  O   ASP A 386      22.491  -9.458  -6.362  1.00 41.97           O  
ANISOU  981  O   ASP A 386     8065   4482   3402   -665   1747  -1081       O  
ATOM    982  CB  ASP A 386      19.837 -10.792  -7.686  1.00 47.19           C  
ANISOU  982  CB  ASP A 386     8968   5368   3594  -1293   1493  -1698       C  
ATOM    983  CG  ASP A 386      18.684 -10.290  -8.516  1.00 57.85           C  
ANISOU  983  CG  ASP A 386    10216   7090   4676  -1440   1158  -1845       C  
ATOM    984  OD1 ASP A 386      18.927  -9.551  -9.493  1.00 52.34           O  
ANISOU  984  OD1 ASP A 386     9595   6554   3736  -1323   1058  -1767       O  
ATOM    985  OD2 ASP A 386      17.528 -10.634  -8.184  1.00 59.74           O  
ANISOU  985  OD2 ASP A 386    10280   7473   4946  -1653    995  -2032       O  
ATOM    986  N   LYS A 387      22.756 -11.627  -6.856  1.00 45.80           N  
ANISOU  986  N   LYS A 387     8973   4598   3831   -768   2152  -1360       N  
ATOM    987  CA  LYS A 387      23.687 -11.793  -5.741  1.00 53.22           C  
ANISOU  987  CA  LYS A 387     9836   5352   5033   -501   2320  -1198       C  
ATOM    988  C   LYS A 387      24.881 -10.857  -5.890  1.00 43.75           C  
ANISOU  988  C   LYS A 387     8454   4274   3896   -257   2372   -998       C  
ATOM    989  O   LYS A 387      25.269 -10.169  -4.943  1.00 45.03           O  
ANISOU  989  O   LYS A 387     8332   4506   4271   -107   2271   -811       O  
ATOM    990  CB  LYS A 387      24.163 -13.239  -5.636  1.00 55.25           C  
ANISOU  990  CB  LYS A 387    10287   5308   5397   -422   2560  -1227       C  
ATOM    991  CG  LYS A 387      25.231 -13.427  -4.555  1.00 56.95           C  
ANISOU  991  CG  LYS A 387    10409   5382   5846    -64   2694  -1041       C  
ATOM    992  CD  LYS A 387      25.882 -14.803  -4.629  1.00 66.75           C  
ANISOU  992  CD  LYS A 387    11875   6354   7134     90   2930  -1035       C  
ATOM    993  CE  LYS A 387      27.178 -14.856  -3.834  1.00 69.45           C  
ANISOU  993  CE  LYS A 387    12065   6668   7654    524   3025   -852       C  
ATOM    994  NZ  LYS A 387      27.862 -16.170  -3.974  1.00 82.25           N  
ANISOU  994  NZ  LYS A 387    13917   8055   9278    724   3242   -840       N  
ATOM    995  N   VAL A 388      25.471 -10.817  -7.089  1.00 45.23           N  
ANISOU  995  N   VAL A 388     8766   4502   3916   -247   2513  -1035       N  
ATOM    996  CA  VAL A 388      26.621  -9.952  -7.325  1.00 44.94           C  
ANISOU  996  CA  VAL A 388     8573   4584   3917    -79   2629   -886       C  
ATOM    997  C   VAL A 388      26.253  -8.492  -7.078  1.00 46.82           C  
ANISOU  997  C   VAL A 388     8581   5037   4170   -144   2352   -720       C  
ATOM    998  O   VAL A 388      26.982  -7.749  -6.407  1.00 41.21           O  
ANISOU  998  O   VAL A 388     7604   4398   3658    -21   2352   -560       O  
ATOM    999  CB  VAL A 388      27.153 -10.156  -8.757  1.00 47.87           C  
ANISOU  999  CB  VAL A 388     9102   4969   4119   -116   2774   -947       C  
ATOM   1000  CG1 VAL A 388      28.223  -9.134  -9.073  1.00 47.94           C  
ANISOU 1000  CG1 VAL A 388     8945   5121   4150    -25   2893   -811       C  
ATOM   1001  CG2 VAL A 388      27.693 -11.569  -8.929  1.00 50.41           C  
ANISOU 1001  CG2 VAL A 388     9557   5074   4523     -9   2991  -1043       C  
ATOM   1002  N   VAL A 389      25.116  -8.059  -7.629  1.00 42.72           N  
ANISOU 1002  N   VAL A 389     8163   4635   3432   -327   2107   -770       N  
ATOM   1003  CA  VAL A 389      24.743  -6.657  -7.549  1.00 42.80           C  
ANISOU 1003  CA  VAL A 389     8031   4822   3409   -343   1857   -607       C  
ATOM   1004  C   VAL A 389      24.425  -6.276  -6.107  1.00 38.37           C  
ANISOU 1004  C   VAL A 389     7174   4272   3134   -290   1669   -496       C  
ATOM   1005  O   VAL A 389      24.779  -5.187  -5.643  1.00 38.97           O  
ANISOU 1005  O   VAL A 389     7073   4413   3322   -227   1600   -323       O  
ATOM   1006  CB  VAL A 389      23.570  -6.361  -8.500  1.00 42.70           C  
ANISOU 1006  CB  VAL A 389     8199   4964   3059   -477   1616   -698       C  
ATOM   1007  CG1 VAL A 389      23.163  -4.902  -8.411  1.00 49.07           C  
ANISOU 1007  CG1 VAL A 389     8913   5919   3810   -421   1363   -511       C  
ATOM   1008  CG2 VAL A 389      23.967  -6.676  -9.943  1.00 45.80           C  
ANISOU 1008  CG2 VAL A 389     8918   5351   3132   -522   1811   -799       C  
ATOM   1009  N   ALA A 390      23.790  -7.185  -5.367  1.00 41.06           N  
ANISOU 1009  N   ALA A 390     7489   4526   3586   -335   1618   -605       N  
ATOM   1010  CA  ALA A 390      23.400  -6.898  -3.985  1.00 35.93           C  
ANISOU 1010  CA  ALA A 390     6594   3880   3177   -299   1452   -514       C  
ATOM   1011  C   ALA A 390      24.607  -6.859  -3.066  1.00 35.82           C  
ANISOU 1011  C   ALA A 390     6408   3787   3415   -100   1601   -376       C  
ATOM   1012  O   ALA A 390      24.691  -5.993  -2.187  1.00 33.40           O  
ANISOU 1012  O   ALA A 390     5870   3556   3264    -46   1464   -238       O  
ATOM   1013  CB  ALA A 390      22.397  -7.935  -3.488  1.00 35.71           C  
ANISOU 1013  CB  ALA A 390     6634   3764   3171   -438   1413   -685       C  
ATOM   1014  N   GLU A 391      25.549  -7.790  -3.239  1.00 43.55           N  
ANISOU 1014  N   GLU A 391     7489   4633   4425     28   1873   -426       N  
ATOM   1015  CA  GLU A 391      26.753  -7.747  -2.418  1.00 44.03           C  
ANISOU 1015  CA  GLU A 391     7335   4695   4700    264   1990   -317       C  
ATOM   1016  C   GLU A 391      27.565  -6.494  -2.715  1.00 36.24           C  
ANISOU 1016  C   GLU A 391     6140   3894   3737    264   2003   -211       C  
ATOM   1017  O   GLU A 391      28.139  -5.894  -1.799  1.00 39.93           O  
ANISOU 1017  O   GLU A 391     6328   4457   4389    353   1949   -112       O  
ATOM   1018  CB  GLU A 391      27.590  -9.016  -2.619  1.00 39.25           C  
ANISOU 1018  CB  GLU A 391     6885   3928   4100    463   2284   -404       C  
ATOM   1019  CG  GLU A 391      26.851 -10.284  -2.211  1.00 43.34           C  
ANISOU 1019  CG  GLU A 391     7679   4192   4598    451   2327   -505       C  
ATOM   1020  CD  GLU A 391      27.715 -11.534  -2.280  1.00 53.68           C  
ANISOU 1020  CD  GLU A 391     9197   5286   5913    717   2634   -567       C  
ATOM   1021  OE1 GLU A 391      27.345 -12.546  -1.651  1.00 60.55           O  
ANISOU 1021  OE1 GLU A 391    10288   5911   6809    770   2688   -592       O  
ATOM   1022  OE2 GLU A 391      28.764 -11.510  -2.951  1.00 51.23           O  
ANISOU 1022  OE2 GLU A 391     8831   5052   5583    874   2822   -579       O  
ATOM   1023  N   GLU A 392      27.612  -6.075  -3.984  1.00 36.61           N  
ANISOU 1023  N   GLU A 392     6346   3988   3578    142   2086   -241       N  
ATOM   1024  CA  GLU A 392      28.264  -4.811  -4.326  1.00 38.01           C  
ANISOU 1024  CA  GLU A 392     6407   4296   3740     81   2134   -141       C  
ATOM   1025  C   GLU A 392      27.577  -3.631  -3.642  1.00 41.61           C  
ANISOU 1025  C   GLU A 392     6746   4812   4251     -2   1863    -15       C  
ATOM   1026  O   GLU A 392      28.237  -2.740  -3.093  1.00 35.69           O  
ANISOU 1026  O   GLU A 392     5783   4137   3640    -11   1883     71       O  
ATOM   1027  CB  GLU A 392      28.262  -4.630  -5.846  1.00 45.93           C  
ANISOU 1027  CB  GLU A 392     7703   5299   4450    -35   2274   -187       C  
ATOM   1028  CG  GLU A 392      28.519  -3.198  -6.315  1.00 55.84           C  
ANISOU 1028  CG  GLU A 392     8987   6626   5602   -154   2296    -65       C  
ATOM   1029  CD  GLU A 392      28.445  -3.058  -7.835  1.00 63.98           C  
ANISOU 1029  CD  GLU A 392    10384   7639   6286   -247   2431    -95       C  
ATOM   1030  OE1 GLU A 392      27.376  -2.666  -8.370  1.00 56.99           O  
ANISOU 1030  OE1 GLU A 392     9739   6760   5154   -297   2208    -62       O  
ATOM   1031  OE2 GLU A 392      29.465  -3.351  -8.494  1.00 69.21           O  
ANISOU 1031  OE2 GLU A 392    11087   8303   6907   -251   2761   -160       O  
ATOM   1032  N   ALA A 393      26.246  -3.598  -3.687  1.00 40.08           N  
ANISOU 1032  N   ALA A 393     6684   4601   3944    -71   1617    -26       N  
ATOM   1033  CA  ALA A 393      25.516  -2.508  -3.053  1.00 34.96           C  
ANISOU 1033  CA  ALA A 393     5938   4007   3340   -106   1364     84       C  
ATOM   1034  C   ALA A 393      25.775  -2.475  -1.548  1.00 34.74           C  
ANISOU 1034  C   ALA A 393     5624   3979   3596    -33   1299    134       C  
ATOM   1035  O   ALA A 393      25.983  -1.401  -0.964  1.00 36.83           O  
ANISOU 1035  O   ALA A 393     5751   4286   3957    -51   1233    236       O  
ATOM   1036  CB  ALA A 393      24.027  -2.650  -3.347  1.00 34.31           C  
ANISOU 1036  CB  ALA A 393     5984   3963   3089   -158   1114     18       C  
ATOM   1037  N   TRP A 394      25.793  -3.647  -0.907  1.00 31.00           N  
ANISOU 1037  N   TRP A 394     5102   3440   3237     52   1334     60       N  
ATOM   1038  CA  TRP A 394      26.025  -3.696   0.534  1.00 31.94           C  
ANISOU 1038  CA  TRP A 394     4995   3561   3580    153   1264    113       C  
ATOM   1039  C   TRP A 394      27.459  -3.299   0.879  1.00 32.10           C  
ANISOU 1039  C   TRP A 394     4783   3679   3734    249   1403    158       C  
ATOM   1040  O   TRP A 394      27.690  -2.558   1.840  1.00 33.14           O  
ANISOU 1040  O   TRP A 394     4700   3892   4001    253   1300    222       O  
ATOM   1041  CB  TRP A 394      25.703  -5.088   1.080  1.00 34.25           C  
ANISOU 1041  CB  TRP A 394     5380   3718   3914    239   1302     36       C  
ATOM   1042  CG  TRP A 394      25.737  -5.106   2.550  1.00 39.93           C  
ANISOU 1042  CG  TRP A 394     5935   4430   4806    346   1203    103       C  
ATOM   1043  CD1 TRP A 394      26.722  -5.619   3.343  1.00 44.42           C  
ANISOU 1043  CD1 TRP A 394     6394   4995   5490    572   1290    137       C  
ATOM   1044  CD2 TRP A 394      24.759  -4.545   3.433  1.00 32.13           C  
ANISOU 1044  CD2 TRP A 394     4872   3463   3873    258    992    144       C  
ATOM   1045  NE1 TRP A 394      26.410  -5.420   4.664  1.00 38.40           N  
ANISOU 1045  NE1 TRP A 394     5522   4239   4829    618   1138    203       N  
ATOM   1046  CE2 TRP A 394      25.211  -4.762   4.747  1.00 34.61           C  
ANISOU 1046  CE2 TRP A 394     5062   3764   4324    412    971    205       C  
ATOM   1047  CE3 TRP A 394      23.548  -3.872   3.236  1.00 31.91           C  
ANISOU 1047  CE3 TRP A 394     4862   3486   3778     96    815    128       C  
ATOM   1048  CZ2 TRP A 394      24.487  -4.339   5.871  1.00 35.59           C  
ANISOU 1048  CZ2 TRP A 394     5106   3896   4519    371    806    249       C  
ATOM   1049  CZ3 TRP A 394      22.828  -3.446   4.358  1.00 36.13           C  
ANISOU 1049  CZ3 TRP A 394     5280   4042   4406     73    654    164       C  
ATOM   1050  CH2 TRP A 394      23.308  -3.670   5.648  1.00 29.39           C  
ANISOU 1050  CH2 TRP A 394     4329   3149   3689    191    663    224       C  
ATOM   1051  N   GLU A 395      28.437  -3.764   0.101  1.00 30.91           N  
ANISOU 1051  N   GLU A 395     4652   3551   3543    312   1643     98       N  
ATOM   1052  CA  GLU A 395      29.809  -3.324   0.324  1.00 46.14           C  
ANISOU 1052  CA  GLU A 395     6297   5644   5591    371   1788     97       C  
ATOM   1053  C   GLU A 395      29.946  -1.810   0.158  1.00 35.00           C  
ANISOU 1053  C   GLU A 395     4813   4316   4169    151   1771    156       C  
ATOM   1054  O   GLU A 395      30.642  -1.157   0.942  1.00 33.14           O  
ANISOU 1054  O   GLU A 395     4293   4219   4078    127   1762    160       O  
ATOM   1055  CB  GLU A 395      30.756  -4.067  -0.623  1.00 51.71           C  
ANISOU 1055  CB  GLU A 395     7039   6371   6236    470   2080      0       C  
ATOM   1056  CG  GLU A 395      32.040  -4.539   0.041  1.00 70.14           C  
ANISOU 1056  CG  GLU A 395     9042   8873   8733    722   2195    -53       C  
ATOM   1057  CD  GLU A 395      31.782  -5.424   1.256  1.00 84.06           C  
ANISOU 1057  CD  GLU A 395    10780  10567  10591    988   2039    -20       C  
ATOM   1058  OE1 GLU A 395      30.771  -6.161   1.269  1.00 85.15           O  
ANISOU 1058  OE1 GLU A 395    11229  10471  10652    994   1972     -5       O  
ATOM   1059  OE2 GLU A 395      32.593  -5.378   2.206  1.00 89.40           O  
ANISOU 1059  OE2 GLU A 395    11134  11434  11401   1181   1989    -21       O  
ATOM   1060  N   ASN A 396      29.298  -1.234  -0.856  1.00 32.42           N  
ANISOU 1060  N   ASN A 396     4766   3901   3649     -8   1774    193       N  
ATOM   1061  CA  ASN A 396      29.390   0.212  -1.064  1.00 32.37           C  
ANISOU 1061  CA  ASN A 396     4800   3904   3596   -198   1794    269       C  
ATOM   1062  C   ASN A 396      28.764   0.970   0.109  1.00 35.48           C  
ANISOU 1062  C   ASN A 396     5086   4286   4107   -217   1547    344       C  
ATOM   1063  O   ASN A 396      29.341   1.944   0.632  1.00 36.84           O  
ANISOU 1063  O   ASN A 396     5111   4511   4378   -336   1592    360       O  
ATOM   1064  CB  ASN A 396      28.692   0.590  -2.375  1.00 33.32           C  
ANISOU 1064  CB  ASN A 396     5313   3914   3432   -284   1812    317       C  
ATOM   1065  CG  ASN A 396      29.542   0.297  -3.616  1.00 51.24           C  
ANISOU 1065  CG  ASN A 396     7719   6195   5554   -339   2129    253       C  
ATOM   1066  OD1 ASN A 396      30.769   0.232  -3.543  1.00 45.43           O  
ANISOU 1066  OD1 ASN A 396     6758   5562   4941   -370   2375    182       O  
ATOM   1067  ND2 ASN A 396      28.885   0.138  -4.761  1.00 40.22           N  
ANISOU 1067  ND2 ASN A 396     6679   4723   3881   -349   2121    261       N  
ATOM   1068  N   HIS A 397      27.579   0.523   0.532  1.00 30.83           N  
ANISOU 1068  N   HIS A 397     4572   3635   3507   -126   1309    365       N  
ATOM   1069  CA  HIS A 397      26.924   1.072   1.718  1.00 27.02           C  
ANISOU 1069  CA  HIS A 397     3979   3146   3140   -117   1086    418       C  
ATOM   1070  C   HIS A 397      27.872   1.057   2.914  1.00 30.51           C  
ANISOU 1070  C   HIS A 397     4101   3698   3794    -80   1109    390       C  
ATOM   1071  O   HIS A 397      28.068   2.077   3.581  1.00 36.68           O  
ANISOU 1071  O   HIS A 397     4775   4511   4652   -177   1065    417       O  
ATOM   1072  CB  HIS A 397      25.655   0.258   2.006  1.00 27.12           C  
ANISOU 1072  CB  HIS A 397     4065   3113   3126    -33    891    394       C  
ATOM   1073  CG  HIS A 397      24.839   0.757   3.161  1.00 26.99           C  
ANISOU 1073  CG  HIS A 397     3953   3094   3208    -21    680    434       C  
ATOM   1074  ND1 HIS A 397      24.334   2.039   3.226  1.00 27.36           N  
ANISOU 1074  ND1 HIS A 397     4060   3119   3215    -69    576    509       N  
ATOM   1075  CD2 HIS A 397      24.392   0.121   4.272  1.00 28.77           C  
ANISOU 1075  CD2 HIS A 397     4068   3315   3549     43    576    408       C  
ATOM   1076  CE1 HIS A 397      23.641   2.180   4.345  1.00 30.12           C  
ANISOU 1076  CE1 HIS A 397     4300   3474   3669    -34    415    514       C  
ATOM   1077  NE2 HIS A 397      23.663   1.029   4.997  1.00 27.51           N  
ANISOU 1077  NE2 HIS A 397     3864   3158   3430     19    415    454       N  
ATOM   1078  N   LEU A 398      28.504  -0.091   3.172  1.00 31.83           N  
ANISOU 1078  N   LEU A 398     4130   3930   4034     75   1181    325       N  
ATOM   1079  CA  LEU A 398      29.405  -0.204   4.315  1.00 32.61           C  
ANISOU 1079  CA  LEU A 398     3911   4183   4295    179   1163    291       C  
ATOM   1080  C   LEU A 398      30.646   0.660   4.152  1.00 38.63           C  
ANISOU 1080  C   LEU A 398     4439   5125   5113     39   1325    229       C  
ATOM   1081  O   LEU A 398      31.273   1.039   5.149  1.00 37.55           O  
ANISOU 1081  O   LEU A 398     4013   5160   5095     37   1264    183       O  
ATOM   1082  CB  LEU A 398      29.817  -1.655   4.518  1.00 32.58           C  
ANISOU 1082  CB  LEU A 398     3868   4194   4318    446   1217    247       C  
ATOM   1083  CG  LEU A 398      28.826  -2.553   5.252  1.00 38.15           C  
ANISOU 1083  CG  LEU A 398     4737   4742   5015    579   1073    287       C  
ATOM   1084  CD1 LEU A 398      29.442  -3.931   5.476  1.00 49.72           C  
ANISOU 1084  CD1 LEU A 398     6218   6184   6489    875   1177    255       C  
ATOM   1085  CD2 LEU A 398      28.434  -1.919   6.556  1.00 41.52           C  
ANISOU 1085  CD2 LEU A 398     5042   5209   5524    555    870    338       C  
ATOM   1086  N   LYS A 399      31.039   0.940   2.912  1.00 32.22           N  
ANISOU 1086  N   LYS A 399     3746   4292   4202    -97   1547    204       N  
ATOM   1087  CA  LYS A 399      32.139   1.864   2.690  1.00 34.82           C  
ANISOU 1087  CA  LYS A 399     3887   4770   4572   -315   1753    126       C  
ATOM   1088  C   LYS A 399      31.771   3.281   3.088  1.00 35.33           C  
ANISOU 1088  C   LYS A 399     4037   4749   4637   -562   1690    176       C  
ATOM   1089  O   LYS A 399      32.668   4.083   3.365  1.00 34.30           O  
ANISOU 1089  O   LYS A 399     3694   4756   4582   -776   1824     81       O  
ATOM   1090  CB  LYS A 399      32.578   1.853   1.224  1.00 42.13           C  
ANISOU 1090  CB  LYS A 399     4992   5656   5359   -426   2047     95       C  
ATOM   1091  CG  LYS A 399      33.370   0.616   0.783  1.00 43.35           C  
ANISOU 1091  CG  LYS A 399     4996   5943   5533   -215   2212     -8       C  
ATOM   1092  CD  LYS A 399      33.952   0.845  -0.619  1.00 47.64           C  
ANISOU 1092  CD  LYS A 399     5689   6474   5938   -388   2553    -60       C  
ATOM   1093  CE  LYS A 399      34.172  -0.452  -1.392  1.00 53.68           C  
ANISOU 1093  CE  LYS A 399     6534   7230   6631   -163   2695   -119       C  
ATOM   1094  NZ  LYS A 399      34.798  -0.197  -2.739  1.00 58.83           N  
ANISOU 1094  NZ  LYS A 399     7331   7886   7136   -343   3056   -183       N  
ATOM   1095  N   ARG A 400      30.476   3.619   3.109  1.00 30.31           N  
ANISOU 1095  N   ARG A 400     3706   3897   3914   -543   1506    303       N  
ATOM   1096  CA  ARG A 400      30.103   4.940   3.600  1.00 29.98           C  
ANISOU 1096  CA  ARG A 400     3765   3749   3875   -718   1445    353       C  
ATOM   1097  C   ARG A 400      29.402   4.935   4.957  1.00 30.55           C  
ANISOU 1097  C   ARG A 400     3726   3829   4055   -606   1168    378       C  
ATOM   1098  O   ARG A 400      29.389   5.970   5.633  1.00 31.67           O  
ANISOU 1098  O   ARG A 400     3858   3934   4241   -751   1138    373       O  
ATOM   1099  CB  ARG A 400      29.206   5.653   2.578  1.00 30.16           C  
ANISOU 1099  CB  ARG A 400     4244   3527   3688   -768   1469    480       C  
ATOM   1100  CG  ARG A 400      29.945   6.040   1.304  1.00 42.07           C  
ANISOU 1100  CG  ARG A 400     5948   4985   5054   -946   1788    470       C  
ATOM   1101  CD  ARG A 400      28.975   6.406   0.211  1.00 39.62           C  
ANISOU 1101  CD  ARG A 400     6118   4460   4478   -883   1761    610       C  
ATOM   1102  NE  ARG A 400      28.019   7.422   0.628  1.00 37.60           N  
ANISOU 1102  NE  ARG A 400     6092   4030   4166   -847   1592    724       N  
ATOM   1103  CZ  ARG A 400      28.195   8.724   0.438  1.00 41.76           C  
ANISOU 1103  CZ  ARG A 400     6909   4360   4598  -1016   1759    788       C  
ATOM   1104  NH1 ARG A 400      29.301   9.163  -0.154  1.00 41.71           N  
ANISOU 1104  NH1 ARG A 400     6949   4336   4564  -1260   2074    719       N  
ATOM   1105  NH2 ARG A 400      27.269   9.588   0.826  1.00 46.38           N  
ANISOU 1105  NH2 ARG A 400     7727   4771   5125   -918   1600    894       N  
ATOM   1106  N   ASN A 401      28.828   3.809   5.358  1.00 28.27           N  
ANISOU 1106  N   ASN A 401     3314   3684   3745   -498   1637   -360       N  
ATOM   1107  CA  ASN A 401      27.988   3.720   6.549  1.00 29.52           C  
ANISOU 1107  CA  ASN A 401     3471   3789   3955   -415   1453   -344       C  
ATOM   1108  C   ASN A 401      28.323   2.424   7.259  1.00 30.46           C  
ANISOU 1108  C   ASN A 401     3402   4097   4076   -209   1321   -388       C  
ATOM   1109  O   ASN A 401      28.061   1.340   6.734  1.00 35.88           O  
ANISOU 1109  O   ASN A 401     4160   4754   4718    -30   1280   -334       O  
ATOM   1110  CB  ASN A 401      26.520   3.759   6.170  1.00 24.14           C  
ANISOU 1110  CB  ASN A 401     3059   2871   3240   -326   1367   -201       C  
ATOM   1111  CG  ASN A 401      26.183   4.980   5.373  1.00 34.48           C  
ANISOU 1111  CG  ASN A 401     4588   3991   4523   -460   1498   -122       C  
ATOM   1112  OD1 ASN A 401      26.079   6.065   5.922  1.00 30.51           O  
ANISOU 1112  OD1 ASN A 401     4128   3385   4081   -591   1546   -140       O  
ATOM   1113  ND2 ASN A 401      26.056   4.822   4.060  1.00 29.59           N  
ANISOU 1113  ND2 ASN A 401     4125   3319   3799   -424   1571    -35       N  
ATOM   1114  N   ASP A 402      28.916   2.545   8.433  1.00 35.29           N  
ANISOU 1114  N   ASP A 402     3786   4897   4726   -233   1264   -490       N  
ATOM   1115  CA  ASP A 402      29.358   1.393   9.211  1.00 37.67           C  
ANISOU 1115  CA  ASP A 402     3903   5401   5008     -9   1143   -516       C  
ATOM   1116  C   ASP A 402      29.250   1.820  10.669  1.00 29.46           C  
ANISOU 1116  C   ASP A 402     2742   4466   3986    -50   1028   -572       C  
ATOM   1117  O   ASP A 402      30.089   2.580  11.156  1.00 37.93           O  
ANISOU 1117  O   ASP A 402     3604   5736   5069   -218   1071   -714       O  
ATOM   1118  CB  ASP A 402      30.781   0.981   8.842  1.00 40.86           C  
ANISOU 1118  CB  ASP A 402     4055   6081   5390     39   1235   -619       C  
ATOM   1119  CG  ASP A 402      31.308  -0.152   9.712  1.00 50.48           C  
ANISOU 1119  CG  ASP A 402     5078   7525   6576    321   1108   -632       C  
ATOM   1120  OD1 ASP A 402      30.510  -0.797  10.428  1.00 44.60           O  
ANISOU 1120  OD1 ASP A 402     4454   6672   5819    487    969   -533       O  
ATOM   1121  OD2 ASP A 402      32.530  -0.392   9.685  1.00 57.36           O  
ANISOU 1121  OD2 ASP A 402     5674   8693   7425    386   1156   -736       O  
ATOM   1122  N   SER A 403      28.207   1.348  11.347  1.00 28.34           N  
ANISOU 1122  N   SER A 403     2731   4202   3836     79    893   -477       N  
ATOM   1123  CA  SER A 403      27.964   1.754  12.721  1.00 28.93           C  
ANISOU 1123  CA  SER A 403     2724   4363   3904     44    788   -523       C  
ATOM   1124  C   SER A 403      27.089   0.702  13.387  1.00 29.54           C  
ANISOU 1124  C   SER A 403     2911   4369   3943    262    655   -401       C  
ATOM   1125  O   SER A 403      26.623  -0.247  12.749  1.00 30.66           O  
ANISOU 1125  O   SER A 403     3205   4366   4080    402    654   -296       O  
ATOM   1126  CB  SER A 403      27.296   3.128  12.789  1.00 28.28           C  
ANISOU 1126  CB  SER A 403     2768   4102   3875   -191    844   -559       C  
ATOM   1127  OG  SER A 403      25.942   3.031  12.390  1.00 28.52           O  
ANISOU 1127  OG  SER A 403     3055   3863   3920   -131    816   -425       O  
ATOM   1128  N   ILE A 404      26.855   0.904  14.684  1.00 27.18           N  
ANISOU 1128  N   ILE A 404     2545   4172   3609    264    557   -428       N  
ATOM   1129  CA  ILE A 404      25.952   0.034  15.428  1.00 27.51           C  
ANISOU 1129  CA  ILE A 404     2708   4138   3606    429    456   -308       C  
ATOM   1130  C   ILE A 404      24.542   0.129  14.860  1.00 29.58           C  
ANISOU 1130  C   ILE A 404     3216   4102   3919    371    478   -222       C  
ATOM   1131  O   ILE A 404      23.766  -0.834  14.924  1.00 29.97           O  
ANISOU 1131  O   ILE A 404     3403   4035   3950    488    441   -115       O  
ATOM   1132  CB  ILE A 404      25.992   0.405  16.931  1.00 24.99           C  
ANISOU 1132  CB  ILE A 404     2265   4014   3216    415    362   -369       C  
ATOM   1133  CG1 ILE A 404      25.191  -0.606  17.760  1.00 31.34           C  
ANISOU 1133  CG1 ILE A 404     3194   4767   3948    597    278   -229       C  
ATOM   1134  CG2 ILE A 404      25.484   1.840  17.166  1.00 23.41           C  
ANISOU 1134  CG2 ILE A 404     2093   3735   3068    166    403   -478       C  
ATOM   1135  CD1 ILE A 404      25.730  -2.018  17.633  1.00 25.53           C  
ANISOU 1135  CD1 ILE A 404     2471   4071   3157    863    258   -116       C  
ATOM   1136  N   ILE A 405      24.182   1.287  14.300  1.00 29.52           N  
ANISOU 1136  N   ILE A 405     3271   3975   3972    192    546   -267       N  
ATOM   1137  CA  ILE A 405      22.844   1.442  13.734  1.00 25.81           C  
ANISOU 1137  CA  ILE A 405     3001   3275   3532    170    551   -188       C  
ATOM   1138  C   ILE A 405      22.708   0.603  12.462  1.00 26.79           C  
ANISOU 1138  C   ILE A 405     3236   3294   3647    243    583   -115       C  
ATOM   1139  O   ILE A 405      21.686  -0.065  12.243  1.00 28.90           O  
ANISOU 1139  O   ILE A 405     3629   3450   3903    297    544    -46       O  
ATOM   1140  CB  ILE A 405      22.546   2.937  13.498  1.00 23.80           C  
ANISOU 1140  CB  ILE A 405     2802   2914   3328      8    620   -240       C  
ATOM   1141  CG1 ILE A 405      22.674   3.707  14.812  1.00 25.55           C  
ANISOU 1141  CG1 ILE A 405     2925   3232   3553    -76    598   -346       C  
ATOM   1142  CG2 ILE A 405      21.141   3.142  12.918  1.00 21.73           C  
ANISOU 1142  CG2 ILE A 405     2719   2460   3078     35    608   -152       C  
ATOM   1143  CD1 ILE A 405      21.680   3.186  15.859  1.00 25.22           C  
ANISOU 1143  CD1 ILE A 405     2903   3207   3471     20    498   -302       C  
ATOM   1144  N   VAL A 406      23.739   0.613  11.609  1.00 29.28           N  
ANISOU 1144  N   VAL A 406     3500   3664   3962    228    665   -150       N  
ATOM   1145  CA  VAL A 406      23.749  -0.274  10.451  1.00 21.81           C  
ANISOU 1145  CA  VAL A 406     2652   2646   2989    308    704   -107       C  
ATOM   1146  C   VAL A 406      23.643  -1.724  10.899  1.00 24.76           C  
ANISOU 1146  C   VAL A 406     3052   3018   3339    480    647    -64       C  
ATOM   1147  O   VAL A 406      22.866  -2.500  10.335  1.00 27.11           O  
ANISOU 1147  O   VAL A 406     3504   3177   3621    515    644    -22       O  
ATOM   1148  CB  VAL A 406      25.011  -0.062   9.589  1.00 23.69           C  
ANISOU 1148  CB  VAL A 406     2801   2981   3220    273    820   -166       C  
ATOM   1149  CG1 VAL A 406      24.990  -1.041   8.411  1.00 24.84           C  
ANISOU 1149  CG1 VAL A 406     3061   3055   3322    367    866   -137       C  
ATOM   1150  CG2 VAL A 406      25.101   1.364   9.103  1.00 23.36           C  
ANISOU 1150  CG2 VAL A 406     2785   2892   3197     81    913   -192       C  
ATOM   1151  N   ASP A 407      24.431  -2.100  11.924  1.00 27.65           N  
ANISOU 1151  N   ASP A 407     3276   3541   3690    587    609    -78       N  
ATOM   1152  CA  ASP A 407      24.492  -3.481  12.411  1.00 30.15           C  
ANISOU 1152  CA  ASP A 407     3643   3840   3972    790    577    -12       C  
ATOM   1153  C   ASP A 407      23.146  -3.958  12.934  1.00 24.64           C  
ANISOU 1153  C   ASP A 407     3115   2977   3269    775    529     66       C  
ATOM   1154  O   ASP A 407      22.818  -5.141  12.816  1.00 29.99           O  
ANISOU 1154  O   ASP A 407     3944   3518   3934    874    552    122       O  
ATOM   1155  CB  ASP A 407      25.523  -3.626  13.535  1.00 36.11           C  
ANISOU 1155  CB  ASP A 407     4203   4837   4681    931    524    -24       C  
ATOM   1156  CG  ASP A 407      26.920  -3.178  13.130  1.00 47.45           C  
ANISOU 1156  CG  ASP A 407     5410   6502   6118    934    573   -128       C  
ATOM   1157  OD1 ASP A 407      27.204  -3.107  11.917  1.00 45.47           O  
ANISOU 1157  OD1 ASP A 407     5188   6193   5898    882    671   -166       O  
ATOM   1158  OD2 ASP A 407      27.739  -2.915  14.040  1.00 50.06           O  
ANISOU 1158  OD2 ASP A 407     5518   7099   6403    982    515   -182       O  
ATOM   1159  N   ILE A 408      22.379  -3.079  13.570  1.00 25.38           N  
ANISOU 1159  N   ILE A 408     3189   3083   3373    648    480     58       N  
ATOM   1160  CA  ILE A 408      21.128  -3.531  14.173  1.00 22.93           C  
ANISOU 1160  CA  ILE A 408     3001   2661   3051    626    447    120       C  
ATOM   1161  C   ILE A 408      19.939  -3.406  13.215  1.00 24.80           C  
ANISOU 1161  C   ILE A 408     3355   2751   3317    504    463    110       C  
ATOM   1162  O   ILE A 408      19.068  -4.275  13.184  1.00 26.59           O  
ANISOU 1162  O   ILE A 408     3703   2865   3535    489    472    141       O  
ATOM   1163  CB  ILE A 408      20.887  -2.747  15.486  1.00 23.30           C  
ANISOU 1163  CB  ILE A 408     2950   2829   3074    580    388    106       C  
ATOM   1164  CG1 ILE A 408      21.943  -3.121  16.539  1.00 21.11           C  
ANISOU 1164  CG1 ILE A 408     2559   2738   2722    726    348    124       C  
ATOM   1165  CG2 ILE A 408      19.500  -2.978  15.962  1.00 21.31           C  
ANISOU 1165  CG2 ILE A 408     2802   2481   2816    520    376    150       C  
ATOM   1166  CD1 ILE A 408      21.954  -2.213  17.758  1.00 29.94           C  
ANISOU 1166  CD1 ILE A 408     3552   4031   3794    665    290     67       C  
ATOM   1167  N   PHE A 409      19.850  -2.314  12.444  1.00 22.31           N  
ANISOU 1167  N   PHE A 409     3007   2443   3025    412    471     66       N  
ATOM   1168  CA  PHE A 409      18.609  -1.913  11.783  1.00 18.74           C  
ANISOU 1168  CA  PHE A 409     2628   1918   2575    327    454     65       C  
ATOM   1169  C   PHE A 409      18.642  -1.936  10.246  1.00 25.83           C  
ANISOU 1169  C   PHE A 409     3601   2768   3445    309    488     51       C  
ATOM   1170  O   PHE A 409      17.568  -1.878   9.628  1.00 26.53           O  
ANISOU 1170  O   PHE A 409     3746   2830   3504    265    456     50       O  
ATOM   1171  CB  PHE A 409      18.220  -0.468  12.202  1.00 20.61           C  
ANISOU 1171  CB  PHE A 409     2804   2188   2838    269    433     48       C  
ATOM   1172  CG  PHE A 409      17.837  -0.312  13.670  1.00 25.51           C  
ANISOU 1172  CG  PHE A 409     3362   2866   3465    266    397     41       C  
ATOM   1173  CD1 PHE A 409      16.574  -0.663  14.120  1.00 29.43           C  
ANISOU 1173  CD1 PHE A 409     3884   3349   3950    247    366     58       C  
ATOM   1174  CD2 PHE A 409      18.745   0.209  14.591  1.00 19.96           C  
ANISOU 1174  CD2 PHE A 409     2561   2260   2764    266    399      1       C  
ATOM   1175  CE1 PHE A 409      16.229  -0.510  15.463  1.00 33.42           C  
ANISOU 1175  CE1 PHE A 409     4337   3920   4443    242    350     51       C  
ATOM   1176  CE2 PHE A 409      18.410   0.375  15.928  1.00 26.57           C  
ANISOU 1176  CE2 PHE A 409     3346   3173   3577    263    366    -16       C  
ATOM   1177  CZ  PHE A 409      17.139   0.011  16.370  1.00 24.31           C  
ANISOU 1177  CZ  PHE A 409     3105   2855   3275    257    347     17       C  
ATOM   1178  N   HIS A 410      19.811  -1.949   9.601  1.00 26.81           N  
ANISOU 1178  N   HIS A 410     3710   2915   3562    341    552     34       N  
ATOM   1179  CA  HIS A 410      19.841  -1.763   8.143  1.00 26.82           C  
ANISOU 1179  CA  HIS A 410     3788   2890   3511    314    597     24       C  
ATOM   1180  C   HIS A 410      19.668  -3.092   7.407  1.00 28.93           C  
ANISOU 1180  C   HIS A 410     4158   3102   3733    346    615     -8       C  
ATOM   1181  O   HIS A 410      20.388  -4.059   7.671  1.00 29.71           O  
ANISOU 1181  O   HIS A 410     4262   3178   3849    427    658    -25       O  
ATOM   1182  CB  HIS A 410      21.142  -1.083   7.691  1.00 24.01           C  
ANISOU 1182  CB  HIS A 410     3373   2592   3158    301    689      7       C  
ATOM   1183  CG  HIS A 410      21.181   0.388   7.975  1.00 27.90           C  
ANISOU 1183  CG  HIS A 410     3830   3088   3683    217    708     20       C  
ATOM   1184  ND1 HIS A 410      21.878   1.286   7.191  1.00 25.48           N  
ANISOU 1184  ND1 HIS A 410     3544   2779   3360    144    815     21       N  
ATOM   1185  CD2 HIS A 410      20.598   1.121   8.958  1.00 24.00           C  
ANISOU 1185  CD2 HIS A 410     3304   2578   3235    186    657     26       C  
ATOM   1186  CE1 HIS A 410      21.726   2.504   7.680  1.00 28.95           C  
ANISOU 1186  CE1 HIS A 410     3986   3173   3843     68    834     28       C  
ATOM   1187  NE2 HIS A 410      20.950   2.431   8.750  1.00 27.62           N  
ANISOU 1187  NE2 HIS A 410     3780   3000   3713    101    735     24       N  
ATOM   1188  N   GLY A 411      18.726  -3.124   6.464  1.00 34.25           N  
ANISOU 1188  N   GLY A 411     4916   3761   4336    291    586    -25       N  
ATOM   1189  CA  GLY A 411      18.588  -4.244   5.547  1.00 29.93           C  
ANISOU 1189  CA  GLY A 411     4477   3170   3725    283    617    -94       C  
ATOM   1190  C   GLY A 411      18.744  -3.790   4.101  1.00 26.41           C  
ANISOU 1190  C   GLY A 411     4086   2782   3167    267    648   -111       C  
ATOM   1191  O   GLY A 411      19.031  -2.619   3.852  1.00 27.06           O  
ANISOU 1191  O   GLY A 411     4138   2912   3230    269    661    -47       O  
ATOM   1192  N   LEU A 412      18.514  -4.683   3.145  1.00 27.07           N  
ANISOU 1192  N   LEU A 412     4270   2852   3162    241    670   -198       N  
ATOM   1193  CA  LEU A 412      18.672  -4.345   1.732  1.00 33.00           C  
ANISOU 1193  CA  LEU A 412     5088   3683   3769    232    703   -218       C  
ATOM   1194  C   LEU A 412      17.435  -4.796   0.965  1.00 28.56           C  
ANISOU 1194  C   LEU A 412     4587   3186   3079    154    618   -302       C  
ATOM   1195  O   LEU A 412      16.972  -5.927   1.146  1.00 32.38           O  
ANISOU 1195  O   LEU A 412     5114   3606   3585     88    616   -411       O  
ATOM   1196  CB  LEU A 412      19.936  -5.004   1.194  1.00 29.77           C  
ANISOU 1196  CB  LEU A 412     4723   3241   3349    289    841   -279       C  
ATOM   1197  CG  LEU A 412      20.591  -4.516  -0.109  1.00 37.74           C  
ANISOU 1197  CG  LEU A 412     5781   4339   4220    294    932   -281       C  
ATOM   1198  CD1 LEU A 412      21.219  -3.137   0.061  1.00 32.39           C  
ANISOU 1198  CD1 LEU A 412     5029   3706   3570    292    976   -161       C  
ATOM   1199  CD2 LEU A 412      21.630  -5.560  -0.558  1.00 35.12           C  
ANISOU 1199  CD2 LEU A 412     5488   3971   3883    359   1070   -390       C  
ATOM   1200  N   PHE A 413      16.886  -3.915   0.132  1.00 27.18           N  
ANISOU 1200  N   PHE A 413     4420   3146   2763    159    552   -253       N  
ATOM   1201  CA  PHE A 413      15.776  -4.304  -0.723  1.00 36.09           C  
ANISOU 1201  CA  PHE A 413     5573   4412   3728     95    456   -350       C  
ATOM   1202  C   PHE A 413      16.127  -4.038  -2.182  1.00 40.07           C  
ANISOU 1202  C   PHE A 413     6175   5030   4020    127    490   -353       C  
ATOM   1203  O   PHE A 413      17.027  -3.259  -2.503  1.00 37.49           O  
ANISOU 1203  O   PHE A 413     5893   4682   3671    197    581   -241       O  
ATOM   1204  CB  PHE A 413      14.451  -3.605  -0.328  1.00 45.43           C  
ANISOU 1204  CB  PHE A 413     6646   5720   4893    102    301   -297       C  
ATOM   1205  CG  PHE A 413      14.416  -2.115  -0.586  1.00 45.85           C  
ANISOU 1205  CG  PHE A 413     6700   5838   4883    233    267   -123       C  
ATOM   1206  CD1 PHE A 413      14.987  -1.224   0.307  1.00 46.24           C  
ANISOU 1206  CD1 PHE A 413     6731   5757   5082    291    324      2       C  
ATOM   1207  CD2 PHE A 413      13.769  -1.610  -1.696  1.00 46.77           C  
ANISOU 1207  CD2 PHE A 413     6849   6145   4779    302    180    -89       C  
ATOM   1208  CE1 PHE A 413      14.938   0.149   0.080  1.00 46.44           C  
ANISOU 1208  CE1 PHE A 413     6801   5787   5059    399    323    156       C  
ATOM   1209  CE2 PHE A 413      13.714  -0.240  -1.931  1.00 44.65           C  
ANISOU 1209  CE2 PHE A 413     6628   5893   4445    450    167     96       C  
ATOM   1210  CZ  PHE A 413      14.304   0.638  -1.039  1.00 45.46           C  
ANISOU 1210  CZ  PHE A 413     6742   5810   4721    491    252    217       C  
ATOM   1211  N   LYS A 414      15.419  -4.735  -3.056  1.00 36.04           N  
ANISOU 1211  N   LYS A 414     5701   4650   3342     53    431   -499       N  
ATOM   1212  CA  LYS A 414      15.607  -4.658  -4.497  1.00 35.49           C  
ANISOU 1212  CA  LYS A 414     5732   4730   3024     71    450   -534       C  
ATOM   1213  C   LYS A 414      14.491  -3.835  -5.123  1.00 33.22           C  
ANISOU 1213  C   LYS A 414     5401   4695   2525    128    281   -465       C  
ATOM   1214  O   LYS A 414      13.322  -3.993  -4.761  1.00 38.49           O  
ANISOU 1214  O   LYS A 414     5949   5482   3195     82    136   -529       O  
ATOM   1215  CB  LYS A 414      15.609  -6.067  -5.085  1.00 32.47           C  
ANISOU 1215  CB  LYS A 414     5427   4340   2572    -53    502   -779       C  
ATOM   1216  CG  LYS A 414      15.936  -6.172  -6.575  1.00 36.61           C  
ANISOU 1216  CG  LYS A 414     6068   5015   2825    -47    550   -858       C  
ATOM   1217  CD  LYS A 414      15.651  -7.567  -7.061  1.00 35.17           C  
ANISOU 1217  CD  LYS A 414     5957   4829   2575   -199    580  -1142       C  
ATOM   1218  CE  LYS A 414      16.061  -7.721  -8.529  1.00 37.54           C  
ANISOU 1218  CE  LYS A 414     6384   5286   2595   -194    645  -1244       C  
ATOM   1219  NZ  LYS A 414      15.438  -8.876  -9.199  1.00 49.31           N  
ANISOU 1219  NZ  LYS A 414     7935   6859   3941   -369    626  -1549       N  
ATOM   1220  N   SER A 415      14.854  -2.977  -6.085  1.00 35.96           N  
ANISOU 1220  N   SER A 415     5848   5140   2677    237    308   -332       N  
ATOM   1221  CA  SER A 415      13.920  -2.165  -6.851  1.00 41.01           C  
ANISOU 1221  CA  SER A 415     6485   6032   3065    353    157   -232       C  
ATOM   1222  C   SER A 415      14.105  -2.442  -8.331  1.00 42.72           C  
ANISOU 1222  C   SER A 415     6826   6442   2964    351    176   -301       C  
ATOM   1223  O   SER A 415      15.221  -2.333  -8.858  1.00 40.76           O  
ANISOU 1223  O   SER A 415     6718   6098   2671    359    351   -252       O  
ATOM   1224  CB  SER A 415      14.129  -0.667  -6.615  1.00 40.93           C  
ANISOU 1224  CB  SER A 415     6532   5936   3082    524    185     48       C  
ATOM   1225  OG  SER A 415      14.003  -0.347  -5.250  1.00 54.39           O  
ANISOU 1225  OG  SER A 415     8131   7470   5064    525    178     98       O  
ATOM   1226  N   THR A 416      13.006  -2.756  -9.003  1.00 42.24           N  
ANISOU 1226  N   THR A 416     6697   6684   2667    339     -2   -422       N  
ATOM   1227  CA  THR A 416      13.000  -3.006 -10.434  1.00 45.26           C  
ANISOU 1227  CA  THR A 416     7182   7318   2695    341    -21   -506       C  
ATOM   1228  C   THR A 416      12.066  -1.996 -11.069  1.00 43.80           C  
ANISOU 1228  C   THR A 416     6975   7445   2223    548   -210   -334       C  
ATOM   1229  O   THR A 416      10.865  -1.992 -10.779  1.00 46.88           O  
ANISOU 1229  O   THR A 416     7176   8051   2585    573   -414   -391       O  
ATOM   1230  CB  THR A 416      12.543  -4.433 -10.736  1.00 47.09           C  
ANISOU 1230  CB  THR A 416     7353   7673   2868    120    -66   -859       C  
ATOM   1231  OG1 THR A 416      13.387  -5.344 -10.036  1.00 46.39           O  
ANISOU 1231  OG1 THR A 416     7310   7252   3066    -21    118   -985       O  
ATOM   1232  CG2 THR A 416      12.597  -4.738 -12.240  1.00 46.04           C  
ANISOU 1232  CG2 THR A 416     7333   7815   2347    105    -75   -984       C  
ATOM   1233  N   LEU A 417      12.612  -1.135 -11.915  1.00 47.29           N  
ANISOU 1233  N   LEU A 417     7607   7914   2446    707   -133   -115       N  
ATOM   1234  CA  LEU A 417      11.820  -0.197 -12.690  1.00 48.08           C  
ANISOU 1234  CA  LEU A 417     7726   8281   2262    928   -293     78       C  
ATOM   1235  C   LEU A 417      11.925  -0.578 -14.157  1.00 51.33           C  
ANISOU 1235  C   LEU A 417     8217   8899   2387    860   -296    -10       C  
ATOM   1236  O   LEU A 417      13.024  -0.834 -14.654  1.00 58.88           O  
ANISOU 1236  O   LEU A 417     9339   9729   3303    769    -91    -32       O  
ATOM   1237  CB  LEU A 417      12.308   1.230 -12.464  1.00 54.60           C  
ANISOU 1237  CB  LEU A 417     8707   8858   3182   1120   -176    437       C  
ATOM   1238  CG  LEU A 417      12.115   1.726 -11.035  1.00 62.01           C  
ANISOU 1238  CG  LEU A 417     9557   9637   4368   1229   -222    546       C  
ATOM   1239  CD1 LEU A 417      12.748   3.092 -10.830  1.00 67.92           C  
ANISOU 1239  CD1 LEU A 417    10429   9954   5423   1161     29    675       C  
ATOM   1240  CD2 LEU A 417      10.634   1.748 -10.713  1.00 58.60           C  
ANISOU 1240  CD2 LEU A 417     9073   9320   3870   1478   -381    753       C  
ATOM   1241  N   VAL A 418      10.787  -0.655 -14.840  1.00 54.35           N  
ANISOU 1241  N   VAL A 418     8470   9606   2575    899   -523    -78       N  
ATOM   1242  CA  VAL A 418      10.751  -0.915 -16.275  1.00 58.02           C  
ANISOU 1242  CA  VAL A 418     9016  10292   2735    863   -554   -145       C  
ATOM   1243  C   VAL A 418      10.191   0.320 -16.960  1.00 68.27           C  
ANISOU 1243  C   VAL A 418    10351  11735   3852   1133   -668    153       C  
ATOM   1244  O   VAL A 418       9.114   0.811 -16.592  1.00 61.90           O  
ANISOU 1244  O   VAL A 418     9368  11071   3079   1299   -858    225       O  
ATOM   1245  CB  VAL A 418       9.919  -2.166 -16.610  1.00 59.75           C  
ANISOU 1245  CB  VAL A 418     9064  10771   2870    665   -709   -513       C  
ATOM   1246  CG1 VAL A 418      10.058  -2.522 -18.109  1.00 63.59           C  
ANISOU 1246  CG1 VAL A 418     9676  11449   3037    612   -708   -607       C  
ATOM   1247  CG2 VAL A 418      10.338  -3.331 -15.720  1.00 57.99           C  
ANISOU 1247  CG2 VAL A 418     8802  10344   2889    418   -593   -795       C  
ATOM   1248  N   CYS A 419      10.931   0.831 -17.934  1.00 63.06           N  
ANISOU 1248  N   CYS A 419     9919  11032   3008   1183   -535    323       N  
ATOM   1249  CA  CYS A 419      10.485   1.988 -18.695  1.00 68.18           C  
ANISOU 1249  CA  CYS A 419    10650  11793   3464   1442   -615    611       C  
ATOM   1250  C   CYS A 419       9.333   1.597 -19.614  1.00 70.70           C  
ANISOU 1250  C   CYS A 419    10820  12544   3498   1490   -871    468       C  
ATOM   1251  O   CYS A 419       9.448   0.613 -20.352  1.00 72.12           O  
ANISOU 1251  O   CYS A 419    11007  12892   3505   1295   -879    215       O  
ATOM   1252  CB  CYS A 419      11.641   2.549 -19.519  1.00 70.35           C  
ANISOU 1252  CB  CYS A 419    11211  11909   3612   1437   -380    808       C  
ATOM   1253  SG  CYS A 419      11.261   4.074 -20.389  1.00 80.30           S  
ANISOU 1253  SG  CYS A 419    12638  13214   4657   1760   -421   1201       S  
ATOM   1254  N   PRO A 420       8.212   2.328 -19.596  1.00 75.65           N  
ANISOU 1254  N   PRO A 420    11306  13360   4078   1749  -1072    607       N  
ATOM   1255  CA  PRO A 420       7.136   2.052 -20.562  1.00 77.64           C  
ANISOU 1255  CA  PRO A 420    11401  14063   4036   1820  -1310    488       C  
ATOM   1256  C   PRO A 420       7.480   2.478 -21.969  1.00 86.37           C  
ANISOU 1256  C   PRO A 420    12736  15287   4792   1919  -1275    643       C  
ATOM   1257  O   PRO A 420       6.765   2.098 -22.907  1.00 85.96           O  
ANISOU 1257  O   PRO A 420    12584  15623   4456   1937  -1453    511       O  
ATOM   1258  CB  PRO A 420       5.966   2.878 -20.024  1.00 78.83           C  
ANISOU 1258  CB  PRO A 420    11343  14341   4268   2115  -1490    632       C  
ATOM   1259  CG  PRO A 420       6.643   4.050 -19.376  1.00 83.15           C  
ANISOU 1259  CG  PRO A 420    12107  14470   5017   2291  -1306    967       C  
ATOM   1260  CD  PRO A 420       7.890   3.477 -18.734  1.00 81.44           C  
ANISOU 1260  CD  PRO A 420    12022  13906   5016   2006  -1075    874       C  
ATOM   1261  N   GLU A 421       8.540   3.265 -22.145  1.00 81.26           N  
ANISOU 1261  N   GLU A 421    12387  14333   4155   1973  -1047    916       N  
ATOM   1262  CA  GLU A 421       8.898   3.804 -23.448  1.00 98.96           C  
ANISOU 1262  CA  GLU A 421    14869  16664   6066   2075   -988   1107       C  
ATOM   1263  C   GLU A 421      10.039   3.022 -24.091  1.00 97.42           C  
ANISOU 1263  C   GLU A 421    14853  16406   5756   1782   -787    950       C  
ATOM   1264  O   GLU A 421       9.890   2.517 -25.208  1.00 92.48           O  
ANISOU 1264  O   GLU A 421    14265  16066   4808   1723   -857    819       O  
ATOM   1265  CB  GLU A 421       9.254   5.292 -23.318  1.00 96.23           C  
ANISOU 1265  CB  GLU A 421    14745  16026   5793   2330   -848   1522       C  
ATOM   1266  N   CYS A 422      11.177   2.896 -23.402  1.00 89.56           N  
ANISOU 1266  N   CYS A 422    13957  15055   5016   1604   -533    945       N  
ATOM   1267  CA  CYS A 422      12.351   2.268 -23.997  1.00 83.19           C  
ANISOU 1267  CA  CYS A 422    13315  14177   4117   1356   -301    816       C  
ATOM   1268  C   CYS A 422      12.602   0.856 -23.488  1.00 81.23           C  
ANISOU 1268  C   CYS A 422    12943  13898   4020   1081   -266    425       C  
ATOM   1269  O   CYS A 422      13.569   0.221 -23.926  1.00 77.49           O  
ANISOU 1269  O   CYS A 422    12591  13359   3494    882    -63    275       O  
ATOM   1270  CB  CYS A 422      13.600   3.132 -23.768  1.00 79.24           C  
ANISOU 1270  CB  CYS A 422    13013  13325   3769   1346      3   1080       C  
ATOM   1271  SG  CYS A 422      14.382   2.963 -22.132  1.00 73.03           S  
ANISOU 1271  SG  CYS A 422    12130  12141   3475   1216    184   1021       S  
ATOM   1272  N   ALA A 423      11.764   0.354 -22.578  1.00 77.82           N  
ANISOU 1272  N   ALA A 423    12281  13506   3783   1070   -442    253       N  
ATOM   1273  CA  ALA A 423      11.834  -0.997 -22.021  1.00 73.03           C  
ANISOU 1273  CA  ALA A 423    11557  12851   3338    827   -426   -122       C  
ATOM   1274  C   ALA A 423      13.125  -1.262 -21.254  1.00 72.18           C  
ANISOU 1274  C   ALA A 423    11538  12388   3500    683   -140   -150       C  
ATOM   1275  O   ALA A 423      13.394  -2.416 -20.888  1.00 74.48           O  
ANISOU 1275  O   ALA A 423    11791  12589   3918    493    -73   -455       O  
ATOM   1276  CB  ALA A 423      11.643  -2.073 -23.101  1.00 76.31           C  
ANISOU 1276  CB  ALA A 423    12002  13501   3490    673   -478   -435       C  
ATOM   1277  N   LYS A 424      13.928  -0.230 -20.995  1.00 70.98           N  
ANISOU 1277  N   LYS A 424    11495  12022   3452    778     36    153       N  
ATOM   1278  CA  LYS A 424      15.066  -0.384 -20.104  1.00 64.01           C  
ANISOU 1278  CA  LYS A 424    10623  10830   2866    674    284    137       C  
ATOM   1279  C   LYS A 424      14.599  -0.933 -18.764  1.00 67.72           C  
ANISOU 1279  C   LYS A 424    10916  11191   3624    640    190    -16       C  
ATOM   1280  O   LYS A 424      13.572  -0.515 -18.223  1.00 60.11           O  
ANISOU 1280  O   LYS A 424     9830  10293   2717    770    -17     66       O  
ATOM   1281  CB  LYS A 424      15.784   0.950 -19.898  1.00 63.54           C  
ANISOU 1281  CB  LYS A 424    10678  10544   2919    799    452    496       C  
ATOM   1282  CG  LYS A 424      16.854   0.925 -18.807  1.00 69.66           C  
ANISOU 1282  CG  LYS A 424    11429  10993   4047    721    678    495       C  
ATOM   1283  CD  LYS A 424      17.476   2.297 -18.578  1.00 72.45           C  
ANISOU 1283  CD  LYS A 424    11907  11089   4531    813    839    827       C  
ATOM   1284  CE  LYS A 424      18.681   2.198 -17.656  1.00 73.47           C  
ANISOU 1284  CE  LYS A 424    12008  10922   4987    692   1083    787       C  
ATOM   1285  NZ  LYS A 424      19.670   1.195 -18.144  1.00 78.79           N  
ANISOU 1285  NZ  LYS A 424    12649  11663   5625    533   1258    553       N  
ATOM   1286  N   ILE A 425      15.343  -1.900 -18.253  1.00 64.35           N  
ANISOU 1286  N   ILE A 425    10467  10610   3373    474    349   -250       N  
ATOM   1287  CA  ILE A 425      15.079  -2.512 -16.965  1.00 58.93           C  
ANISOU 1287  CA  ILE A 425     9643   9785   2963    424    305   -405       C  
ATOM   1288  C   ILE A 425      16.179  -2.039 -16.030  1.00 58.97           C  
ANISOU 1288  C   ILE A 425     9684   9467   3255    465    525   -249       C  
ATOM   1289  O   ILE A 425      17.340  -2.443 -16.166  1.00 69.87           O  
ANISOU 1289  O   ILE A 425    11118  10713   4716    384    755   -326       O  
ATOM   1290  CB  ILE A 425      15.035  -4.041 -17.059  1.00 56.32           C  
ANISOU 1290  CB  ILE A 425     9294   9464   2640    225    319   -803       C  
ATOM   1291  CG1 ILE A 425      13.831  -4.483 -17.896  1.00 71.20           C  
ANISOU 1291  CG1 ILE A 425    11129  11633   4291    196     78   -964       C  
ATOM   1292  CG2 ILE A 425      14.988  -4.646 -15.664  1.00 51.76           C  
ANISOU 1292  CG2 ILE A 425     8599   8690   2377    169    330   -942       C  
ATOM   1293  CD1 ILE A 425      13.882  -5.934 -18.335  1.00 78.29           C  
ANISOU 1293  CD1 ILE A 425    12057  12513   5178     36    117  -1339       C  
ATOM   1294  N   SER A 426      15.821  -1.162 -15.098  1.00 57.03           N  
ANISOU 1294  N   SER A 426     9402   9090   3178    593    458    -33       N  
ATOM   1295  CA  SER A 426      16.758  -0.604 -14.138  1.00 47.26           C  
ANISOU 1295  CA  SER A 426     8210   7520   2228    610    652    121       C  
ATOM   1296  C   SER A 426      16.556  -1.327 -12.811  1.00 49.76           C  
ANISOU 1296  C   SER A 426     8373   7672   2863    529    603    -45       C  
ATOM   1297  O   SER A 426      15.487  -1.232 -12.197  1.00 45.71           O  
ANISOU 1297  O   SER A 426     7724   7220   2424    571    399    -44       O  
ATOM   1298  CB  SER A 426      16.550   0.902 -13.999  1.00 54.30           C  
ANISOU 1298  CB  SER A 426     9165   8320   3148    767    632    462       C  
ATOM   1299  OG  SER A 426      17.391   1.439 -12.993  1.00 63.20           O  
ANISOU 1299  OG  SER A 426    10320   9125   4568    739    814    576       O  
ATOM   1300  N   VAL A 427      17.575  -2.062 -12.380  1.00 48.83           N  
ANISOU 1300  N   VAL A 427     8230   7349   2975    403    784   -188       N  
ATOM   1301  CA  VAL A 427      17.548  -2.806 -11.127  1.00 45.21           C  
ANISOU 1301  CA  VAL A 427     7614   6695   2868    314    760   -329       C  
ATOM   1302  C   VAL A 427      18.552  -2.173 -10.177  1.00 40.14           C  
ANISOU 1302  C   VAL A 427     6944   5791   2517    327    917   -175       C  
ATOM   1303  O   VAL A 427      19.709  -1.941 -10.545  1.00 45.43           O  
ANISOU 1303  O   VAL A 427     7687   6400   3174    315   1128   -129       O  
ATOM   1304  CB  VAL A 427      17.858  -4.297 -11.353  1.00 44.16           C  
ANISOU 1304  CB  VAL A 427     7482   6541   2757    187    830   -636       C  
ATOM   1305  CG1 VAL A 427      18.021  -5.017 -10.023  1.00 49.74           C  
ANISOU 1305  CG1 VAL A 427     8074   6997   3827    125    850   -730       C  
ATOM   1306  CG2 VAL A 427      16.765  -4.943 -12.190  1.00 42.84           C  
ANISOU 1306  CG2 VAL A 427     7321   6642   2314    123    663   -835       C  
ATOM   1307  N   THR A 428      18.112  -1.877  -8.963  1.00 35.73           N  
ANISOU 1307  N   THR A 428     6264   5105   2205    340    822   -112       N  
ATOM   1308  CA  THR A 428      19.014  -1.342  -7.956  1.00 35.31           C  
ANISOU 1308  CA  THR A 428     6158   4831   2426    332    951     -7       C  
ATOM   1309  C   THR A 428      18.738  -2.056  -6.648  1.00 36.76           C  
ANISOU 1309  C   THR A 428     6188   4892   2886    288    871   -117       C  
ATOM   1310  O   THR A 428      17.634  -2.541  -6.415  1.00 38.76           O  
ANISOU 1310  O   THR A 428     6382   5213   3130    271    704   -201       O  
ATOM   1311  CB  THR A 428      18.849   0.171  -7.764  1.00 42.74           C  
ANISOU 1311  CB  THR A 428     7158   5717   3364    411    951    249       C  
ATOM   1312  OG1 THR A 428      17.474   0.465  -7.487  1.00 51.98           O  
ANISOU 1312  OG1 THR A 428     8282   6971   4496    499    731    299       O  
ATOM   1313  CG2 THR A 428      19.296   0.941  -9.010  1.00 50.71           C  
ANISOU 1313  CG2 THR A 428     8365   6799   4104    451   1083    397       C  
ATOM   1314  N   PHE A 429      19.754  -2.146  -5.809  1.00 37.18           N  
ANISOU 1314  N   PHE A 429     6170   4788   3168    265    996   -121       N  
ATOM   1315  CA  PHE A 429      19.565  -2.577  -4.434  1.00 32.93           C  
ANISOU 1315  CA  PHE A 429     5502   4127   2882    250    930   -164       C  
ATOM   1316  C   PHE A 429      19.872  -1.389  -3.540  1.00 40.45           C  
ANISOU 1316  C   PHE A 429     6394   4990   3986    268    953     -4       C  
ATOM   1317  O   PHE A 429      20.832  -0.654  -3.783  1.00 45.54           O  
ANISOU 1317  O   PHE A 429     7066   5610   4627    254   1101     75       O  
ATOM   1318  CB  PHE A 429      20.447  -3.777  -4.089  1.00 29.06           C  
ANISOU 1318  CB  PHE A 429     4975   3546   2520    241   1037   -314       C  
ATOM   1319  CG  PHE A 429      20.041  -5.047  -4.779  1.00 37.67           C  
ANISOU 1319  CG  PHE A 429     6148   4663   3499    206   1024   -503       C  
ATOM   1320  CD1 PHE A 429      20.344  -5.257  -6.123  1.00 40.70           C  
ANISOU 1320  CD1 PHE A 429     6643   5158   3661    198   1108   -581       C  
ATOM   1321  CD2 PHE A 429      19.370  -6.042  -4.083  1.00 42.88           C  
ANISOU 1321  CD2 PHE A 429     6793   5229   4270    161    949   -616       C  
ATOM   1322  CE1 PHE A 429      19.982  -6.420  -6.753  1.00 43.45           C  
ANISOU 1322  CE1 PHE A 429     7079   5525   3904    146   1108   -789       C  
ATOM   1323  CE2 PHE A 429      19.007  -7.212  -4.715  1.00 41.38           C  
ANISOU 1323  CE2 PHE A 429     6704   5032   3987     93    965   -816       C  
ATOM   1324  CZ  PHE A 429      19.309  -7.401  -6.054  1.00 40.94           C  
ANISOU 1324  CZ  PHE A 429     6752   5090   3713     84   1039   -914       C  
ATOM   1325  N   ASP A 430      19.029  -1.182  -2.528  1.00 33.93           N  
ANISOU 1325  N   ASP A 430     5488   4121   3283    279    821     28       N  
ATOM   1326  CA  ASP A 430      19.100   0.001  -1.703  1.00 31.39           C  
ANISOU 1326  CA  ASP A 430     5129   3715   3083    294    828    160       C  
ATOM   1327  C   ASP A 430      18.931  -0.360  -0.232  1.00 32.88           C  
ANISOU 1327  C   ASP A 430     5181   3830   3484    278    764    112       C  
ATOM   1328  O   ASP A 430      18.156  -1.269   0.100  1.00 31.96           O  
ANISOU 1328  O   ASP A 430     5022   3735   3387    269    661     26       O  
ATOM   1329  CB  ASP A 430      18.025   1.012  -2.111  1.00 40.85           C  
ANISOU 1329  CB  ASP A 430     6406   4961   4153    373    729    293       C  
ATOM   1330  CG  ASP A 430      18.427   1.831  -3.325  1.00 57.22           C  
ANISOU 1330  CG  ASP A 430     8650   7058   6033    408    837    417       C  
ATOM   1331  OD1 ASP A 430      19.545   2.386  -3.322  1.00 62.14           O  
ANISOU 1331  OD1 ASP A 430     9315   7582   6713    344   1016    466       O  
ATOM   1332  OD2 ASP A 430      17.625   1.917  -4.277  1.00 65.00           O  
ANISOU 1332  OD2 ASP A 430     9722   8180   6796    492    746    463       O  
ATOM   1333  N   PRO A 431      19.652   0.322   0.655  1.00 39.44           N  
ANISOU 1333  N   PRO A 431     5945   4581   4460    257    834    157       N  
ATOM   1334  CA  PRO A 431      19.514   0.063   2.091  1.00 40.81           C  
ANISOU 1334  CA  PRO A 431     5994   4709   4803    251    771    122       C  
ATOM   1335  C   PRO A 431      18.209   0.610   2.638  1.00 29.61           C  
ANISOU 1335  C   PRO A 431     4565   3286   3401    281    643    173       C  
ATOM   1336  O   PRO A 431      17.624   1.551   2.109  1.00 29.69           O  
ANISOU 1336  O   PRO A 431     4651   3302   3327    327    620    263       O  
ATOM   1337  CB  PRO A 431      20.705   0.806   2.706  1.00 31.18           C  
ANISOU 1337  CB  PRO A 431     4702   3454   3690    204    886    137       C  
ATOM   1338  CG  PRO A 431      20.995   1.906   1.736  1.00 41.53           C  
ANISOU 1338  CG  PRO A 431     6132   4740   4907    168    995    223       C  
ATOM   1339  CD  PRO A 431      20.688   1.333   0.369  1.00 39.50           C  
ANISOU 1339  CD  PRO A 431     5989   4551   4469    210    990    224       C  
ATOM   1340  N   PHE A 432      17.762   0.005   3.734  1.00 33.99           N  
ANISOU 1340  N   PHE A 432     5025   3831   4057    272    570    121       N  
ATOM   1341  CA  PHE A 432      16.652   0.568   4.487  1.00 32.17           C  
ANISOU 1341  CA  PHE A 432     4746   3609   3867    296    474    154       C  
ATOM   1342  C   PHE A 432      16.951   0.428   5.971  1.00 25.91           C  
ANISOU 1342  C   PHE A 432     3854   2775   3217    270    478    126       C  
ATOM   1343  O   PHE A 432      17.696  -0.458   6.385  1.00 27.09           O  
ANISOU 1343  O   PHE A 432     3970   2911   3412    254    515     79       O  
ATOM   1344  CB  PHE A 432      15.308  -0.094   4.128  1.00 32.13           C  
ANISOU 1344  CB  PHE A 432     4724   3705   3779    299    356    108       C  
ATOM   1345  CG  PHE A 432      15.216  -1.558   4.495  1.00 38.95           C  
ANISOU 1345  CG  PHE A 432     5561   4560   4679    220    350      1       C  
ATOM   1346  CD1 PHE A 432      14.838  -1.945   5.770  1.00 28.58           C  
ANISOU 1346  CD1 PHE A 432     4173   3214   3471    186    329    -19       C  
ATOM   1347  CD2 PHE A 432      15.479  -2.545   3.556  1.00 34.31           C  
ANISOU 1347  CD2 PHE A 432     5050   3979   4009    180    383    -79       C  
ATOM   1348  CE1 PHE A 432      14.736  -3.278   6.107  1.00 26.84           C  
ANISOU 1348  CE1 PHE A 432     3976   2943   3278    114    351    -94       C  
ATOM   1349  CE2 PHE A 432      15.378  -3.883   3.882  1.00 39.21           C  
ANISOU 1349  CE2 PHE A 432     5693   4537   4668    108    406   -177       C  
ATOM   1350  CZ  PHE A 432      15.010  -4.248   5.174  1.00 35.21           C  
ANISOU 1350  CZ  PHE A 432     5131   3972   4273     76    395   -173       C  
ATOM   1351  N   CYS A 433      16.378   1.313   6.775  1.00 27.30           N  
ANISOU 1351  N   CYS A 433     3989   2936   3447    289    443    157       N  
ATOM   1352  CA  CYS A 433      16.452   1.118   8.210  1.00 28.62           C  
ANISOU 1352  CA  CYS A 433     4062   3100   3713    265    431    122       C  
ATOM   1353  C   CYS A 433      15.092   0.823   8.821  1.00 35.47           C  
ANISOU 1353  C   CYS A 433     4874   4019   4583    272    344    105       C  
ATOM   1354  O   CYS A 433      15.014   0.610  10.035  1.00 30.97           O  
ANISOU 1354  O   CYS A 433     4238   3457   4071    251    337     83       O  
ATOM   1355  CB  CYS A 433      17.111   2.315   8.899  1.00 36.05           C  
ANISOU 1355  CB  CYS A 433     4981   3992   4723    246    492    128       C  
ATOM   1356  SG  CYS A 433      16.378   3.894   8.547  1.00 42.28           S  
ANISOU 1356  SG  CYS A 433     5862   4699   5503    299    509    191       S  
ATOM   1357  N   TYR A 434      14.036   0.788   8.008  1.00 24.21           N  
ANISOU 1357  N   TYR A 434     3461   2660   3080    298    279    108       N  
ATOM   1358  CA  TYR A 434      12.726   0.267   8.382  1.00 23.35           C  
ANISOU 1358  CA  TYR A 434     3266   2650   2957    272    203     61       C  
ATOM   1359  C   TYR A 434      11.903   0.151   7.109  1.00 31.94           C  
ANISOU 1359  C   TYR A 434     4357   3857   3921    294    130     44       C  
ATOM   1360  O   TYR A 434      12.232   0.750   6.080  1.00 31.76           O  
ANISOU 1360  O   TYR A 434     4417   3833   3819    369    133    101       O  
ATOM   1361  CB  TYR A 434      12.009   1.152   9.424  1.00 25.50           C  
ANISOU 1361  CB  TYR A 434     3453   2952   3285    323    182     71       C  
ATOM   1362  CG  TYR A 434      11.737   2.562   8.978  1.00 32.23           C  
ANISOU 1362  CG  TYR A 434     4340   3791   4116    458    173    136       C  
ATOM   1363  CD1 TYR A 434      10.601   2.872   8.241  1.00 36.18           C  
ANISOU 1363  CD1 TYR A 434     4798   4421   4526    563     88    153       C  
ATOM   1364  CD2 TYR A 434      12.601   3.591   9.309  1.00 44.17           C  
ANISOU 1364  CD2 TYR A 434     5929   5164   5690    485    254    176       C  
ATOM   1365  CE1 TYR A 434      10.345   4.176   7.828  1.00 47.73           C  
ANISOU 1365  CE1 TYR A 434     6329   5848   5959    737     88    241       C  
ATOM   1366  CE2 TYR A 434      12.356   4.893   8.906  1.00 58.05           C  
ANISOU 1366  CE2 TYR A 434     7773   6850   7433    611    278    246       C  
ATOM   1367  CZ  TYR A 434      11.227   5.182   8.166  1.00 54.65           C  
ANISOU 1367  CZ  TYR A 434     7331   6523   6911    759    196    294       C  
ATOM   1368  OH  TYR A 434      10.978   6.478   7.766  1.00 63.46           O  
ANISOU 1368  OH  TYR A 434     8564   7545   8001    932    228    391       O  
ATOM   1369  N   LEU A 435      10.829  -0.624   7.196  1.00 27.27           N  
ANISOU 1369  N   LEU A 435     3674   3389   3299    217     71    -41       N  
ATOM   1370  CA  LEU A 435       9.971  -0.952   6.068  1.00 34.29           C  
ANISOU 1370  CA  LEU A 435     4524   4452   4052    200    -14   -104       C  
ATOM   1371  C   LEU A 435       8.649  -0.234   6.233  1.00 34.72           C  
ANISOU 1371  C   LEU A 435     4418   4704   4068    291   -113   -107       C  
ATOM   1372  O   LEU A 435       7.935  -0.476   7.209  1.00 33.73           O  
ANISOU 1372  O   LEU A 435     4168   4637   4012    224   -112   -163       O  
ATOM   1373  CB  LEU A 435       9.727  -2.461   5.986  1.00 32.62           C  
ANISOU 1373  CB  LEU A 435     4314   4251   3831      4      8   -240       C  
ATOM   1374  CG  LEU A 435      10.924  -3.320   5.618  1.00 40.21           C  
ANISOU 1374  CG  LEU A 435     5438   5033   4806    -52    105   -257       C  
ATOM   1375  CD1 LEU A 435      10.525  -4.791   5.524  1.00 36.98           C  
ANISOU 1375  CD1 LEU A 435     5065   4598   4387   -244    146   -402       C  
ATOM   1376  CD2 LEU A 435      11.530  -2.810   4.311  1.00 36.56           C  
ANISOU 1376  CD2 LEU A 435     5062   4601   4229     44     94   -216       C  
ATOM   1377  N   THR A 436       8.302   0.607   5.269  1.00 34.13           N  
ANISOU 1377  N   THR A 436     4347   4750   3871    457   -192    -44       N  
ATOM   1378  CA  THR A 436       7.000   1.261   5.256  1.00 38.51           C  
ANISOU 1378  CA  THR A 436     4734   5538   4361    600   -302    -45       C  
ATOM   1379  C   THR A 436       6.037   0.396   4.448  1.00 46.11           C  
ANISOU 1379  C   THR A 436     5547   6796   5175    500   -414   -188       C  
ATOM   1380  O   THR A 436       6.198   0.235   3.230  1.00 37.35           O  
ANISOU 1380  O   THR A 436     4506   5777   3908    521   -468   -192       O  
ATOM   1381  CB  THR A 436       7.125   2.671   4.684  1.00 39.40           C  
ANISOU 1381  CB  THR A 436     4952   5614   4405    873   -322    120       C  
ATOM   1382  OG1 THR A 436       7.816   3.490   5.630  1.00 37.81           O  
ANISOU 1382  OG1 THR A 436     4853   5155   4358    921   -208    203       O  
ATOM   1383  CG2 THR A 436       5.763   3.275   4.375  1.00 39.05           C  
ANISOU 1383  CG2 THR A 436     4738   5856   4245   1087   -458    129       C  
ATOM   1384  N   LEU A 437       5.025  -0.156   5.122  1.00 34.09           N  
ANISOU 1384  N   LEU A 437     3815   5445   3691    372   -441   -322       N  
ATOM   1385  CA  LEU A 437       4.099  -1.091   4.492  1.00 31.71           C  
ANISOU 1385  CA  LEU A 437     3347   5435   3268    199   -526   -508       C  
ATOM   1386  C   LEU A 437       2.794  -0.411   4.152  1.00 36.34           C  
ANISOU 1386  C   LEU A 437     3673   6410   3724    379   -683   -536       C  
ATOM   1387  O   LEU A 437       2.193   0.237   5.019  1.00 34.67           O  
ANISOU 1387  O   LEU A 437     3320   6260   3593    502   -682   -503       O  
ATOM   1388  CB  LEU A 437       3.816  -2.271   5.411  1.00 36.30           C  
ANISOU 1388  CB  LEU A 437     3866   5962   3966   -112   -426   -659       C  
ATOM   1389  CG  LEU A 437       4.974  -3.198   5.776  1.00 38.78           C  
ANISOU 1389  CG  LEU A 437     4422   5922   4392   -286   -274   -650       C  
ATOM   1390  CD1 LEU A 437       4.368  -4.415   6.427  1.00 36.18           C  
ANISOU 1390  CD1 LEU A 437     4029   5597   4122   -591   -187   -810       C  
ATOM   1391  CD2 LEU A 437       5.753  -3.580   4.527  1.00 43.77           C  
ANISOU 1391  CD2 LEU A 437     5226   6486   4918   -294   -281   -665       C  
ATOM   1392  N   PRO A 438       2.312  -0.543   2.921  1.00 39.66           N  
ANISOU 1392  N   PRO A 438     4010   7127   3931    416   -820   -605       N  
ATOM   1393  CA  PRO A 438       0.957  -0.090   2.619  1.00 51.47           C  
ANISOU 1393  CA  PRO A 438     5196   9077   5282    575   -989   -668       C  
ATOM   1394  C   PRO A 438      -0.052  -1.058   3.203  1.00 51.59           C  
ANISOU 1394  C   PRO A 438     4925   9336   5342    267   -982   -919       C  
ATOM   1395  O   PRO A 438       0.245  -2.224   3.473  1.00 48.98           O  
ANISOU 1395  O   PRO A 438     4669   8847   5096    -90   -865  -1060       O  
ATOM   1396  CB  PRO A 438       0.912  -0.094   1.087  1.00 51.74           C  
ANISOU 1396  CB  PRO A 438     5255   9358   5046    671  -1134   -679       C  
ATOM   1397  CG  PRO A 438       1.839  -1.195   0.707  1.00 51.97           C  
ANISOU 1397  CG  PRO A 438     5499   9153   5095    366  -1028   -776       C  
ATOM   1398  CD  PRO A 438       2.939  -1.204   1.762  1.00 47.89           C  
ANISOU 1398  CD  PRO A 438     5215   8145   4838    302   -830   -657       C  
ATOM   1399  N   LEU A 439      -1.257  -0.548   3.412  1.00 53.83           N  
ANISOU 1399  N   LEU A 439     4883  10001   5569    415  -1090   -972       N  
ATOM   1400  CA  LEU A 439      -2.293  -1.301   4.100  1.00 56.99           C  
ANISOU 1400  CA  LEU A 439     4972  10658   6023    129  -1060  -1206       C  
ATOM   1401  C   LEU A 439      -3.324  -1.800   3.094  1.00 59.26           C  
ANISOU 1401  C   LEU A 439     5026  11373   6116     21  -1173  -1403       C  
ATOM   1402  O   LEU A 439      -3.856  -1.017   2.297  1.00 53.67           O  
ANISOU 1402  O   LEU A 439     4239  10902   5251    340  -1300  -1321       O  
ATOM   1403  CB  LEU A 439      -2.945  -0.451   5.193  1.00 55.02           C  
ANISOU 1403  CB  LEU A 439     4531  10489   5884    338  -1034  -1142       C  
ATOM   1404  CG  LEU A 439      -1.997  -0.066   6.335  1.00 51.65           C  
ANISOU 1404  CG  LEU A 439     4384   9564   5677    381   -854   -966       C  
ATOM   1405  CD1 LEU A 439      -2.769   0.125   7.632  1.00 52.93           C  
ANISOU 1405  CD1 LEU A 439     4325   9826   5960    359   -767  -1025       C  
ATOM   1406  CD2 LEU A 439      -0.893  -1.098   6.517  1.00 53.37           C  
ANISOU 1406  CD2 LEU A 439     4902   9381   5996     57   -706   -974       C  
ATOM   1407  N   ALA A 440      -3.575  -3.110   3.120  1.00 56.39           N  
ANISOU 1407  N   ALA A 440     4628  11015   5781   -425  -1072  -1635       N  
ATOM   1408  CA  ALA A 440      -4.567  -3.754   2.269  1.00 72.12           C  
ANISOU 1408  CA  ALA A 440     6441  13332   7628   -594  -1108  -1840       C  
ATOM   1409  C   ALA A 440      -5.950  -3.576   2.871  1.00 76.74           C  
ANISOU 1409  C   ALA A 440     6708  14222   8230   -587  -1082  -1933       C  
ATOM   1410  O   ALA A 440      -6.736  -2.749   2.421  1.00 86.33           O  
ANISOU 1410  O   ALA A 440     7731  15756   9313   -274  -1209  -1889       O  
ATOM   1411  CB  ALA A 440      -4.258  -5.239   2.088  1.00 75.50           C  
ANISOU 1411  CB  ALA A 440     7010  13582   8095  -1074   -971  -2048       C  
ATOM   1412  N   SER A 755     -10.926  -2.113   6.556  1.00 83.71           N  
ANISOU 1412  N   SER A 755     6496  16075   9235   -435   -856  -2216       N  
ATOM   1413  CA  SER A 755     -11.547  -3.345   7.113  1.00 90.85           C  
ANISOU 1413  CA  SER A 755     7293  17035  10191   -894   -675  -2434       C  
ATOM   1414  C   SER A 755     -10.574  -4.027   8.081  1.00 89.44           C  
ANISOU 1414  C   SER A 755     7386  16390  10207  -1181   -481  -2375       C  
ATOM   1415  O   SER A 755     -10.222  -3.407   9.104  1.00 87.03           O  
ANISOU 1415  O   SER A 755     7142  15898  10027  -1053   -408  -2243       O  
ATOM   1416  CB  SER A 755     -11.965  -4.281   6.009  1.00 98.13           C  
ANISOU 1416  CB  SER A 755     8110  18199  10976  -1222   -682  -2674       C  
ATOM   1417  OG  SER A 755     -10.892  -4.512   5.108  1.00 96.97           O  
ANISOU 1417  OG  SER A 755     8115  17991  10738  -1132   -816  -2618       O  
ATOM   1418  N   LYS A 756     -10.172  -5.261   7.762  1.00 84.50           N  
ANISOU 1418  N   LYS A 756     6931  15577   9596  -1566   -387  -2479       N  
ATOM   1419  CA  LYS A 756      -9.216  -6.038   8.596  1.00 81.73           C  
ANISOU 1419  CA  LYS A 756     6878  14765   9412  -1850   -192  -2422       C  
ATOM   1420  C   LYS A 756      -8.254  -6.782   7.665  1.00 71.61           C  
ANISOU 1420  C   LYS A 756     5842  13251   8114  -2026   -200  -2445       C  
ATOM   1421  O   LYS A 756      -8.730  -7.379   6.685  1.00 75.68           O  
ANISOU 1421  O   LYS A 756     6281  13964   8510  -2199   -229  -2625       O  
ATOM   1422  CB  LYS A 756      -9.957  -7.026   9.501  1.00 84.67           C  
ANISOU 1422  CB  LYS A 756     7210  15132   9829  -2237     32  -2573       C  
ATOM   1423  CG  LYS A 756      -9.089  -8.148  10.054  1.00 88.85           C  
ANISOU 1423  CG  LYS A 756     8076  15234  10450  -2634    237  -2596       C  
ATOM   1424  CD  LYS A 756      -9.664  -8.836  11.273  1.00 92.81           C  
ANISOU 1424  CD  LYS A 756     8639  15592  11032  -2915    482  -2627       C  
ATOM   1425  CE  LYS A 756      -8.651  -9.710  11.981  1.00 90.10           C  
ANISOU 1425  CE  LYS A 756     8717  14695  10822  -3075    658  -2480       C  
ATOM   1426  NZ  LYS A 756      -9.166 -10.226  13.271  1.00 89.24           N  
ANISOU 1426  NZ  LYS A 756     8717  14406  10783  -3274    890  -2442       N  
ATOM   1427  N   VAL A 757      -6.957  -6.765   7.983  1.00 68.26           N  
ANISOU 1427  N   VAL A 757     5705  12429   7801  -1970   -175  -2275       N  
ATOM   1428  CA  VAL A 757      -5.967  -7.423   7.156  1.00 59.22           C  
ANISOU 1428  CA  VAL A 757     4824  11030   6647  -2099   -181  -2282       C  
ATOM   1429  C   VAL A 757      -4.918  -8.020   8.082  1.00 58.20           C  
ANISOU 1429  C   VAL A 757     5028  10398   6689  -2278     11  -2176       C  
ATOM   1430  O   VAL A 757      -4.804  -7.653   9.253  1.00 52.77           O  
ANISOU 1430  O   VAL A 757     4353   9587   6110  -2218     98  -2057       O  
ATOM   1431  CB  VAL A 757      -5.316  -6.461   6.137  1.00 64.38           C  
ANISOU 1431  CB  VAL A 757     5487  11771   7204  -1730   -414  -2160       C  
ATOM   1432  CG1 VAL A 757      -6.369  -5.633   5.405  1.00 66.70           C  
ANISOU 1432  CG1 VAL A 757     5465  12549   7327  -1448   -601  -2195       C  
ATOM   1433  CG2 VAL A 757      -4.318  -5.577   6.825  1.00 55.86           C  
ANISOU 1433  CG2 VAL A 757     4537  10447   6239  -1471   -438  -1932       C  
ATOM   1434  N   LYS A 758      -4.145  -8.946   7.534  1.00 58.17           N  
ANISOU 1434  N   LYS A 758     5306  10100   6695  -2478     83  -2218       N  
ATOM   1435  CA  LYS A 758      -2.995  -9.511   8.216  1.00 51.26           C  
ANISOU 1435  CA  LYS A 758     4796   8719   5962  -2588    252  -2097       C  
ATOM   1436  C   LYS A 758      -1.726  -8.796   7.783  1.00 51.66           C  
ANISOU 1436  C   LYS A 758     4989   8615   6022  -2336    117  -1955       C  
ATOM   1437  O   LYS A 758      -1.648  -8.211   6.698  1.00 58.07           O  
ANISOU 1437  O   LYS A 758     5703   9654   6707  -2144    -84  -1978       O  
ATOM   1438  CB  LYS A 758      -2.871 -11.003   7.930  1.00 52.04           C  
ANISOU 1438  CB  LYS A 758     5167   8536   6071  -2923    443  -2218       C  
ATOM   1439  CG  LYS A 758      -4.013 -11.812   8.476  1.00 56.78           C  
ANISOU 1439  CG  LYS A 758     5681   9227   6664  -3211    614  -2357       C  
ATOM   1440  CD  LYS A 758      -3.602 -13.252   8.607  1.00 67.49           C  
ANISOU 1440  CD  LYS A 758     7410  10157   8077  -3493    857  -2394       C  
ATOM   1441  CE  LYS A 758      -4.683 -14.156   8.058  1.00 80.31           C  
ANISOU 1441  CE  LYS A 758     8924  11982   9609  -3804    942  -2653       C  
ATOM   1442  NZ  LYS A 758      -4.913 -13.868   6.607  1.00 87.67           N  
ANISOU 1442  NZ  LYS A 758     9655  13250  10404  -3744    741  -2807       N  
ATOM   1443  N   LEU A 759      -0.721  -8.852   8.657  1.00 39.45           N  
ANISOU 1443  N   LEU A 759     3735   6646   4608  -2255    248  -1752       N  
ATOM   1444  CA  LEU A 759       0.572  -8.250   8.333  1.00 40.89           C  
ANISOU 1444  CA  LEU A 759     4159   6573   4804  -1911    177  -1533       C  
ATOM   1445  C   LEU A 759       1.155  -8.823   7.039  1.00 41.43           C  
ANISOU 1445  C   LEU A 759     4403   6551   4788  -1965    139  -1622       C  
ATOM   1446  O   LEU A 759       1.729  -8.085   6.225  1.00 50.21           O  
ANISOU 1446  O   LEU A 759     5548   7707   5824  -1689      0  -1527       O  
ATOM   1447  CB  LEU A 759       1.536  -8.471   9.489  1.00 33.85           C  
ANISOU 1447  CB  LEU A 759     3551   5258   4050  -1856    342  -1332       C  
ATOM   1448  CG  LEU A 759       2.912  -7.810   9.372  1.00 38.79           C  
ANISOU 1448  CG  LEU A 759     4389   5642   4706  -1520    290  -1112       C  
ATOM   1449  CD1 LEU A 759       2.754  -6.311   9.291  1.00 35.32           C  
ANISOU 1449  CD1 LEU A 759     3756   5430   4233  -1202    125  -1011       C  
ATOM   1450  CD2 LEU A 759       3.810  -8.197  10.547  1.00 39.31           C  
ANISOU 1450  CD2 LEU A 759     4703   5348   4883  -1494    447   -947       C  
ATOM   1451  N   LYS A 760       1.029 -10.139   6.840  1.00 42.70           N  
ANISOU 1451  N   LYS A 760     4701   6566   4957  -2327    285  -1809       N  
ATOM   1452  CA  LYS A 760       1.564 -10.763   5.629  1.00 41.16           C  
ANISOU 1452  CA  LYS A 760     4688   6274   4678  -2398    273  -1929       C  
ATOM   1453  C   LYS A 760       0.927 -10.169   4.385  1.00 49.90           C  
ANISOU 1453  C   LYS A 760     5525   7850   5586  -2325     42  -2068       C  
ATOM   1454  O   LYS A 760       1.593 -10.002   3.357  1.00 43.15           O  
ANISOU 1454  O   LYS A 760     4790   6978   4626  -2171    -43  -2048       O  
ATOM   1455  CB  LYS A 760       1.330 -12.277   5.643  1.00 54.47           C  
ANISOU 1455  CB  LYS A 760     6564   7728   6405  -2756    491  -2090       C  
ATOM   1456  CG  LYS A 760       1.960 -13.039   6.796  1.00 67.09           C  
ANISOU 1456  CG  LYS A 760     8480   8848   8163  -2810    733  -1941       C  
ATOM   1457  CD  LYS A 760       3.459 -12.906   6.803  1.00 66.78           C  
ANISOU 1457  CD  LYS A 760     8742   8447   8186  -2576    756  -1771       C  
ATOM   1458  CE  LYS A 760       4.105 -14.104   7.471  1.00 60.62           C  
ANISOU 1458  CE  LYS A 760     8330   7192   7511  -2618   1003  -1667       C  
ATOM   1459  NZ  LYS A 760       3.890 -15.359   6.719  1.00 56.00           N  
ANISOU 1459  NZ  LYS A 760     7893   6500   6884  -2801   1123  -1825       N  
ATOM   1460  N   ASP A 761      -0.380  -9.889   4.444  1.00 45.47           N  
ANISOU 1460  N   ASP A 761     4607   7708   4960  -2392    -43  -2179       N  
ATOM   1461  CA  ASP A 761      -1.054  -9.265   3.312  1.00 45.34           C  
ANISOU 1461  CA  ASP A 761     4329   8155   4745  -2229   -266  -2251       C  
ATOM   1462  C   ASP A 761      -0.440  -7.905   2.984  1.00 51.49           C  
ANISOU 1462  C   ASP A 761     5086   9035   5441  -1811   -465  -2052       C  
ATOM   1463  O   ASP A 761      -0.267  -7.563   1.807  1.00 54.19           O  
ANISOU 1463  O   ASP A 761     5431   9562   5599  -1653   -616  -2061       O  
ATOM   1464  CB  ASP A 761      -2.547  -9.138   3.606  1.00 57.80           C  
ANISOU 1464  CB  ASP A 761     5547  10124   6292  -2284   -288  -2346       C  
ATOM   1465  CG  ASP A 761      -3.175 -10.464   4.035  1.00 70.19           C  
ANISOU 1465  CG  ASP A 761     7166  11570   7935  -2689    -56  -2518       C  
ATOM   1466  OD1 ASP A 761      -2.759 -11.529   3.525  1.00 76.32           O  
ANISOU 1466  OD1 ASP A 761     8185  12100   8712  -2911     65  -2622       O  
ATOM   1467  OD2 ASP A 761      -4.082 -10.443   4.891  1.00 76.10           O  
ANISOU 1467  OD2 ASP A 761     7725  12458   8730  -2772     17  -2545       O  
ATOM   1468  N   CYS A 762      -0.076  -7.128   4.011  1.00 42.59           N  
ANISOU 1468  N   CYS A 762     4006   7715   4462  -1571   -421  -1806       N  
ATOM   1469  CA  CYS A 762       0.556  -5.827   3.787  1.00 38.15           C  
ANISOU 1469  CA  CYS A 762     3509   7116   3870  -1130   -533  -1545       C  
ATOM   1470  C   CYS A 762       1.951  -5.982   3.197  1.00 47.01           C  
ANISOU 1470  C   CYS A 762     4983   7885   4994  -1047   -477  -1428       C  
ATOM   1471  O   CYS A 762       2.354  -5.198   2.327  1.00 42.63           O  
ANISOU 1471  O   CYS A 762     4480   7404   4312   -783   -590  -1312       O  
ATOM   1472  CB  CYS A 762       0.623  -5.032   5.097  1.00 44.76           C  
ANISOU 1472  CB  CYS A 762     4323   7812   4872   -947   -472  -1355       C  
ATOM   1473  SG  CYS A 762      -0.994  -4.564   5.757  1.00 47.79           S  
ANISOU 1473  SG  CYS A 762     4264   8654   5241   -944   -544  -1465       S  
ATOM   1474  N   ILE A 763       2.712  -6.976   3.652  1.00 39.70           N  
ANISOU 1474  N   ILE A 763     4307   6576   4200  -1251   -291  -1449       N  
ATOM   1475  CA  ILE A 763       4.037  -7.178   3.063  1.00 39.82           C  
ANISOU 1475  CA  ILE A 763     4624   6292   4212  -1162   -230  -1362       C  
ATOM   1476  C   ILE A 763       3.905  -7.610   1.605  1.00 44.53           C  
ANISOU 1476  C   ILE A 763     5231   7085   4603  -1251   -310  -1541       C  
ATOM   1477  O   ILE A 763       4.594  -7.096   0.708  1.00 43.34           O  
ANISOU 1477  O   ILE A 763     5190   6940   4337  -1047   -371  -1446       O  
ATOM   1478  CB  ILE A 763       4.839  -8.202   3.882  1.00 46.83           C  
ANISOU 1478  CB  ILE A 763     5768   6749   5276  -1320    -16  -1346       C  
ATOM   1479  CG1 ILE A 763       4.966  -7.735   5.331  1.00 33.86           C  
ANISOU 1479  CG1 ILE A 763     4108   4961   3796  -1220     48  -1168       C  
ATOM   1480  CG2 ILE A 763       6.203  -8.439   3.253  1.00 44.33           C  
ANISOU 1480  CG2 ILE A 763     5726   6164   4952  -1207     51  -1276       C  
ATOM   1481  CD1 ILE A 763       5.444  -8.807   6.269  1.00 40.73           C  
ANISOU 1481  CD1 ILE A 763     5189   5479   4806  -1385    248  -1157       C  
ATOM   1482  N   GLU A 764       3.010  -8.563   1.353  1.00 47.45           N  
ANISOU 1482  N   GLU A 764     5488   7630   4912  -1580   -299  -1817       N  
ATOM   1483  CA  GLU A 764       2.739  -9.009  -0.002  1.00 56.01           C  
ANISOU 1483  CA  GLU A 764     6546   8961   5774  -1705   -387  -2039       C  
ATOM   1484  C   GLU A 764       2.398  -7.820  -0.889  1.00 57.80           C  
ANISOU 1484  C   GLU A 764     6588   9596   5777  -1396   -623  -1945       C  
ATOM   1485  O   GLU A 764       2.971  -7.659  -1.969  1.00 50.39           O  
ANISOU 1485  O   GLU A 764     5781   8694   4669  -1272   -677  -1922       O  
ATOM   1486  CB  GLU A 764       1.610 -10.042   0.016  1.00 59.62           C  
ANISOU 1486  CB  GLU A 764     6841   9589   6223  -2099   -339  -2335       C  
ATOM   1487  CG  GLU A 764       1.532 -10.932  -1.215  1.00 78.53           C  
ANISOU 1487  CG  GLU A 764     9317  12026   8496  -2254   -312  -2520       C  
ATOM   1488  CD  GLU A 764       0.781 -10.284  -2.362  1.00 93.01           C  
ANISOU 1488  CD  GLU A 764    10890  14366  10081  -2101   -541  -2563       C  
ATOM   1489  OE1 GLU A 764       1.034 -10.654  -3.530  1.00101.16           O  
ANISOU 1489  OE1 GLU A 764    12022  15452  10963  -2121   -567  -2661       O  
ATOM   1490  OE2 GLU A 764      -0.064  -9.405  -2.096  1.00 98.32           O  
ANISOU 1490  OE2 GLU A 764    11267  15382  10709  -1938   -689  -2490       O  
ATOM   1491  N   LEU A 765       1.507  -6.938  -0.418  1.00 54.11           N  
ANISOU 1491  N   LEU A 765     5836   9422   5302  -1236   -752  -1867       N  
ATOM   1492  CA  LEU A 765       1.158  -5.758  -1.207  1.00 58.68           C  
ANISOU 1492  CA  LEU A 765     6266  10366   5665   -885   -970  -1741       C  
ATOM   1493  C   LEU A 765       2.374  -4.859  -1.410  1.00 52.99           C  
ANISOU 1493  C   LEU A 765     5824   9347   4964   -551   -936  -1434       C  
ATOM   1494  O   LEU A 765       2.563  -4.284  -2.491  1.00 48.38           O  
ANISOU 1494  O   LEU A 765     5294   8931   4158   -335  -1049  -1351       O  
ATOM   1495  CB  LEU A 765       0.017  -4.992  -0.532  1.00 55.34           C  
ANISOU 1495  CB  LEU A 765     5501  10265   5262   -741  -1084  -1707       C  
ATOM   1496  CG  LEU A 765      -0.455  -3.718  -1.241  1.00 55.62           C  
ANISOU 1496  CG  LEU A 765     5390  10650   5092   -313  -1294  -1541       C  
ATOM   1497  CD1 LEU A 765      -0.857  -4.012  -2.687  1.00 49.55           C  
ANISOU 1497  CD1 LEU A 765     4587  10145   4095   -322  -1385  -1641       C  
ATOM   1498  CD2 LEU A 765      -1.598  -3.061  -0.481  1.00 60.90           C  
ANISOU 1498  CD2 LEU A 765     5753  11541   5844   -158  -1336  -1501       C  
ATOM   1499  N   PHE A 766       3.213  -4.738  -0.381  1.00 40.98           N  
ANISOU 1499  N   PHE A 766     4482   7398   3692   -519   -774  -1270       N  
ATOM   1500  CA  PHE A 766       4.466  -3.999  -0.492  1.00 44.50           C  
ANISOU 1500  CA  PHE A 766     5186   7541   4182   -276   -706  -1019       C  
ATOM   1501  C   PHE A 766       5.350  -4.535  -1.618  1.00 47.56           C  
ANISOU 1501  C   PHE A 766     5795   7837   4437   -333   -658  -1070       C  
ATOM   1502  O   PHE A 766       6.082  -3.766  -2.245  1.00 39.53           O  
ANISOU 1502  O   PHE A 766     4928   6763   3328   -110   -661   -892       O  
ATOM   1503  CB  PHE A 766       5.183  -4.042   0.863  1.00 40.60           C  
ANISOU 1503  CB  PHE A 766     4807   6652   3967   -307   -540   -906       C  
ATOM   1504  CG  PHE A 766       6.606  -3.554   0.844  1.00 35.65           C  
ANISOU 1504  CG  PHE A 766     4433   5701   3413   -150   -435   -710       C  
ATOM   1505  CD1 PHE A 766       6.902  -2.212   1.015  1.00 40.72           C  
ANISOU 1505  CD1 PHE A 766     5104   6295   4073    121   -457   -489       C  
ATOM   1506  CD2 PHE A 766       7.656  -4.449   0.685  1.00 52.11           C  
ANISOU 1506  CD2 PHE A 766     6721   7525   5553   -281   -296   -760       C  
ATOM   1507  CE1 PHE A 766       8.218  -1.772   1.021  1.00 43.13           C  
ANISOU 1507  CE1 PHE A 766     5619   6321   4449    213   -342   -338       C  
ATOM   1508  CE2 PHE A 766       8.968  -4.011   0.673  1.00 54.08           C  
ANISOU 1508  CE2 PHE A 766     7155   7530   5865   -148   -197   -602       C  
ATOM   1509  CZ  PHE A 766       9.249  -2.671   0.847  1.00 43.54           C  
ANISOU 1509  CZ  PHE A 766     5826   6170   4546     77   -219   -398       C  
ATOM   1510  N   THR A 767       5.293  -5.834  -1.900  1.00 51.96           N  
ANISOU 1510  N   THR A 767     6393   8373   4979   -635   -593  -1318       N  
ATOM   1511  CA  THR A 767       6.135  -6.418  -2.942  1.00 47.31           C  
ANISOU 1511  CA  THR A 767     6021   7686   4266   -693   -525  -1398       C  
ATOM   1512  C   THR A 767       5.419  -6.583  -4.275  1.00 45.97           C  
ANISOU 1512  C   THR A 767     5749   7939   3780   -745   -681  -1584       C  
ATOM   1513  O   THR A 767       5.983  -7.184  -5.191  1.00 45.12           O  
ANISOU 1513  O   THR A 767     5809   7792   3542   -831   -624  -1704       O  
ATOM   1514  CB  THR A 767       6.681  -7.780  -2.504  1.00 48.36           C  
ANISOU 1514  CB  THR A 767     6328   7475   4570   -964   -327  -1558       C  
ATOM   1515  OG1 THR A 767       5.637  -8.757  -2.555  1.00 54.38           O  
ANISOU 1515  OG1 THR A 767     6964   8406   5291  -1285   -344  -1851       O  
ATOM   1516  CG2 THR A 767       7.230  -7.704  -1.099  1.00 46.10           C  
ANISOU 1516  CG2 THR A 767     6109   6841   4567   -917   -198  -1390       C  
ATOM   1517  N   THR A 768       4.194  -6.085  -4.406  1.00 44.33           N  
ANISOU 1517  N   THR A 768     5256   8157   3431   -686   -877  -1625       N  
ATOM   1518  CA  THR A 768       3.422  -6.267  -5.629  1.00 50.51           C  
ANISOU 1518  CA  THR A 768     5893   9409   3890   -735  -1050  -1820       C  
ATOM   1519  C   THR A 768       3.755  -5.179  -6.641  1.00 47.85           C  
ANISOU 1519  C   THR A 768     5641   9235   3303   -370  -1164  -1585       C  
ATOM   1520  O   THR A 768       3.873  -3.999  -6.290  1.00 49.22           O  
ANISOU 1520  O   THR A 768     5822   9373   3505    -52  -1205  -1299       O  
ATOM   1521  CB  THR A 768       1.925  -6.249  -5.320  1.00 64.10           C  
ANISOU 1521  CB  THR A 768     7253  11453   5650   -793  -1166  -1911       C  
ATOM   1522  OG1 THR A 768       1.627  -5.106  -4.516  1.00 74.09           O  
ANISOU 1522  OG1 THR A 768     8381  12793   6975   -511  -1250  -1693       O  
ATOM   1523  CG2 THR A 768       1.520  -7.494  -4.564  1.00 59.14           C  
ANISOU 1523  CG2 THR A 768     6568  10666   5236  -1203  -1017  -2156       C  
ATOM   1524  N   LYS A 769       3.906  -5.585  -7.901  1.00 52.16           N  
ANISOU 1524  N   LYS A 769     6282   9879   3656   -416  -1175  -1675       N  
ATOM   1525  CA  LYS A 769       4.266  -4.660  -8.965  1.00 54.86           C  
ANISOU 1525  CA  LYS A 769     6750  10345   3750   -106  -1250  -1453       C  
ATOM   1526  C   LYS A 769       3.142  -3.660  -9.194  1.00 59.95           C  
ANISOU 1526  C   LYS A 769     7156  11335   4287    172  -1447  -1300       C  
ATOM   1527  O   LYS A 769       2.001  -4.047  -9.469  1.00 63.59           O  
ANISOU 1527  O   LYS A 769     7352  12109   4703     68  -1559  -1478       O  
ATOM   1528  CB  LYS A 769       4.564  -5.422 -10.257  1.00 54.82           C  
ANISOU 1528  CB  LYS A 769     6875  10397   3555   -249  -1219  -1621       C  
ATOM   1529  CG  LYS A 769       5.055  -4.529 -11.387  1.00 61.44           C  
ANISOU 1529  CG  LYS A 769     7888  11327   4130     40  -1259  -1386       C  
ATOM   1530  CD  LYS A 769       4.946  -5.203 -12.750  1.00 72.62           C  
ANISOU 1530  CD  LYS A 769     9348  12932   5314    -82  -1290  -1571       C  
ATOM   1531  CE  LYS A 769       5.769  -6.478 -12.828  1.00 70.83           C  
ANISOU 1531  CE  LYS A 769     9307  12431   5174   -383  -1098  -1826       C  
ATOM   1532  NZ  LYS A 769       5.620  -7.130 -14.172  1.00 79.16           N  
ANISOU 1532  NZ  LYS A 769    10404  13676   5997   -493  -1129  -2019       N  
ATOM   1533  N   GLU A 770       3.471  -2.377  -9.097  1.00 53.75           N  
ANISOU 1533  N   GLU A 770     6477  10477   3470    530  -1466   -972       N  
ATOM   1534  CA  GLU A 770       2.538  -1.299  -9.372  1.00 63.69           C  
ANISOU 1534  CA  GLU A 770     7576  11990   4633    860  -1617   -784       C  
ATOM   1535  C   GLU A 770       3.045  -0.482 -10.552  1.00 72.24           C  
ANISOU 1535  C   GLU A 770     8897  13074   5479   1126  -1623   -541       C  
ATOM   1536  O   GLU A 770       4.215  -0.567 -10.933  1.00 74.01           O  
ANISOU 1536  O   GLU A 770     9412  13058   5652   1082  -1487   -471       O  
ATOM   1537  CB  GLU A 770       2.379  -0.386  -8.160  1.00 60.60           C  
ANISOU 1537  CB  GLU A 770     7129  11452   4446   1073  -1603   -588       C  
ATOM   1538  CG  GLU A 770       3.609   0.469  -7.928  1.00 71.69           C  
ANISOU 1538  CG  GLU A 770     8867  12474   5898   1271  -1464   -294       C  
ATOM   1539  CD  GLU A 770       3.462   1.395  -6.745  1.00 74.75           C  
ANISOU 1539  CD  GLU A 770     9222  12685   6495   1481  -1437   -108       C  
ATOM   1540  OE1 GLU A 770       4.174   1.189  -5.739  1.00 71.17           O  
ANISOU 1540  OE1 GLU A 770     8857  11912   6271   1348  -1301   -111       O  
ATOM   1541  OE2 GLU A 770       2.631   2.324  -6.824  1.00 80.58           O  
ANISOU 1541  OE2 GLU A 770     9853  13549   7213   1763  -1519     31       O  
ATOM   1542  N   LYS A 771       2.153   0.318 -11.127  1.00 76.39           N  
ANISOU 1542  N   LYS A 771     9296  13869   5859   1405  -1761   -414       N  
ATOM   1543  CA  LYS A 771       2.534   1.299 -12.135  1.00 76.67           C  
ANISOU 1543  CA  LYS A 771     9566  13878   5687   1702  -1756   -134       C  
ATOM   1544  C   LYS A 771       2.678   2.665 -11.474  1.00 85.42           C  
ANISOU 1544  C   LYS A 771    10797  14727   6933   2035  -1689    194       C  
ATOM   1545  O   LYS A 771       1.864   3.043 -10.625  1.00 88.38           O  
ANISOU 1545  O   LYS A 771    10962  15162   7457   2155  -1747    199       O  
ATOM   1546  CB  LYS A 771       1.508   1.365 -13.269  1.00 77.66           C  
ANISOU 1546  CB  LYS A 771     9515  14452   5540   1827  -1936   -189       C  
ATOM   1547  CG  LYS A 771       1.974   2.167 -14.482  1.00 77.92           C  
ANISOU 1547  CG  LYS A 771     9818  14474   5314   2075  -1923     67       C  
ATOM   1548  CD  LYS A 771       0.887   2.261 -15.538  1.00 83.65           C  
ANISOU 1548  CD  LYS A 771    10346  15680   5756   2232  -2119     15       C  
ATOM   1549  CE  LYS A 771       1.325   3.115 -16.719  1.00 96.25           C  
ANISOU 1549  CE  LYS A 771    12226  17262   7084   2497  -2101    292       C  
ATOM   1550  NZ  LYS A 771       2.449   2.497 -17.482  1.00 99.07           N  
ANISOU 1550  NZ  LYS A 771    12852  17480   7309   2260  -1985    238       N  
ATOM   1551  N   LEU A 772       3.725   3.395 -11.855  1.00 82.19           N  
ANISOU 1551  N   LEU A 772    10735  14010   6484   2162  -1543    453       N  
ATOM   1552  CA  LEU A 772       3.994   4.693 -11.246  1.00 79.38           C  
ANISOU 1552  CA  LEU A 772    10549  13328   6283   2432  -1431    751       C  
ATOM   1553  C   LEU A 772       3.002   5.735 -11.745  1.00 86.65           C  
ANISOU 1553  C   LEU A 772    11408  14436   7077   2798  -1539    919       C  
ATOM   1554  O   LEU A 772       2.763   5.857 -12.952  1.00 90.26           O  
ANISOU 1554  O   LEU A 772    11906  15124   7265   2908  -1617    967       O  
ATOM   1555  CB  LEU A 772       5.423   5.141 -11.547  1.00 76.07           C  
ANISOU 1555  CB  LEU A 772    10517  12515   5869   2407  -1209    954       C  
ATOM   1556  CG  LEU A 772       6.409   4.985 -10.391  1.00 78.22           C  
ANISOU 1556  CG  LEU A 772    10902  12406   6413   2240  -1029    952       C  
ATOM   1557  CD1 LEU A 772       6.307   3.597  -9.806  1.00 76.96           C  
ANISOU 1557  CD1 LEU A 772    10531  12390   6319   1944  -1093    638       C  
ATOM   1558  CD2 LEU A 772       7.825   5.276 -10.845  1.00 76.04           C  
ANISOU 1558  CD2 LEU A 772    10966  11806   6120   2164   -796   1103       C  
ATOM   1559  N   GLY A 773       2.431   6.494 -10.813  1.00 90.05           N  
ANISOU 1559  N   GLY A 773    11751  14772   7694   2999  -1534   1006       N  
ATOM   1560  CA  GLY A 773       1.496   7.533 -11.176  1.00 93.24           C  
ANISOU 1560  CA  GLY A 773    12111  15325   7992   3376  -1611   1163       C  
ATOM   1561  C   GLY A 773       2.184   8.795 -11.652  1.00 95.27           C  
ANISOU 1561  C   GLY A 773    12760  15231   8207   3618  -1450   1491       C  
ATOM   1562  O   GLY A 773       3.387   8.992 -11.476  1.00 90.29           O  
ANISOU 1562  O   GLY A 773    12420  14197   7689   3486  -1254   1601       O  
ATOM   1563  N   ALA A 774       1.388   9.670 -12.274  1.00 97.34           N  
ANISOU 1563  N   ALA A 774    13025  15660   8298   3973  -1524   1642       N  
ATOM   1564  CA  ALA A 774       1.901  10.965 -12.702  1.00 93.04           C  
ANISOU 1564  CA  ALA A 774    12860  14777   7714   4225  -1361   1956       C  
ATOM   1565  C   ALA A 774       2.327  11.829 -11.524  1.00 92.03           C  
ANISOU 1565  C   ALA A 774    12908  14164   7897   4265  -1161   2068       C  
ATOM   1566  O   ALA A 774       3.038  12.821 -11.723  1.00 90.55           O  
ANISOU 1566  O   ALA A 774    13077  13591   7736   4361   -966   2297       O  
ATOM   1567  CB  ALA A 774       0.853  11.699 -13.536  1.00101.16           C  
ANISOU 1567  CB  ALA A 774    13842  16107   8487   4630  -1492   2086       C  
ATOM   1568  N   GLU A 775       1.910  11.472 -10.304  1.00 88.38           N  
ANISOU 1568  N   GLU A 775    12203  13713   7664   4173  -1197   1900       N  
ATOM   1569  CA  GLU A 775       2.330  12.180  -9.102  1.00 87.19           C  
ANISOU 1569  CA  GLU A 775    12196  13120   7812   4167  -1012   1965       C  
ATOM   1570  C   GLU A 775       3.706  11.746  -8.616  1.00 89.63           C  
ANISOU 1570  C   GLU A 775    12682  13069   8304   3820   -838   1935       C  
ATOM   1571  O   GLU A 775       4.305  12.445  -7.792  1.00 94.06           O  
ANISOU 1571  O   GLU A 775    13433  13212   9092   3788   -647   2012       O  
ATOM   1572  CB  GLU A 775       1.305  11.975  -7.984  1.00 85.51           C  
ANISOU 1572  CB  GLU A 775    11647  13088   7755   4211  -1117   1795       C  
ATOM   1573  N   ASP A 776       4.214  10.609  -9.095  1.00 79.52           N  
ANISOU 1573  N   ASP A 776    11340  11950   6925   3556   -894   1808       N  
ATOM   1574  CA  ASP A 776       5.558  10.148  -8.746  1.00 71.47           C  
ANISOU 1574  CA  ASP A 776    10490  10624   6043   3245   -724   1780       C  
ATOM   1575  C   ASP A 776       6.147   9.382  -9.932  1.00 74.33           C  
ANISOU 1575  C   ASP A 776    10925  11149   6168   3083   -743   1746       C  
ATOM   1576  O   ASP A 776       6.230   8.153  -9.917  1.00 80.18           O  
ANISOU 1576  O   ASP A 776    11497  12098   6868   2851   -832   1536       O  
ATOM   1577  CB  ASP A 776       5.527   9.276  -7.492  1.00 64.68           C  
ANISOU 1577  CB  ASP A 776     9404   9774   5397   3035   -762   1574       C  
ATOM   1578  N   PRO A 777       6.563  10.098 -10.975  1.00 76.80           N  
ANISOU 1578  N   PRO A 777    11500  11366   6315   3195   -649   1942       N  
ATOM   1579  CA  PRO A 777       7.194   9.432 -12.125  1.00 74.44           C  
ANISOU 1579  CA  PRO A 777    11293  11207   5782   3035   -641   1914       C  
ATOM   1580  C   PRO A 777       8.640   9.056 -11.820  1.00 72.53           C  
ANISOU 1580  C   PRO A 777    11225  10653   5681   2729   -418   1884       C  
ATOM   1581  O   PRO A 777       9.183   9.349 -10.755  1.00 67.25           O  
ANISOU 1581  O   PRO A 777    10611   9656   5285   2640   -271   1895       O  
ATOM   1582  CB  PRO A 777       7.111  10.489 -13.235  1.00 78.70           C  
ANISOU 1582  CB  PRO A 777    12068  11725   6110   3288   -597   2163       C  
ATOM   1583  CG  PRO A 777       7.110  11.789 -12.514  1.00 79.54           C  
ANISOU 1583  CG  PRO A 777    12340  11457   6423   3471   -449   2343       C  
ATOM   1584  CD  PRO A 777       6.418  11.548 -11.186  1.00 77.78           C  
ANISOU 1584  CD  PRO A 777    11854  11263   6437   3479   -542   2190       C  
ATOM   1585  N   TRP A 778       9.263   8.380 -12.782  1.00 74.93           N  
ANISOU 1585  N   TRP A 778    11602  11082   5787   2564   -388   1829       N  
ATOM   1586  CA  TRP A 778      10.643   7.928 -12.643  1.00 69.16           C  
ANISOU 1586  CA  TRP A 778    11010  10115   5154   2279   -170   1777       C  
ATOM   1587  C   TRP A 778      11.459   8.427 -13.824  1.00 60.04           C  
ANISOU 1587  C   TRP A 778    10119   8875   3818   2261     -4   1936       C  
ATOM   1588  O   TRP A 778      11.030   8.309 -14.974  1.00 64.30           O  
ANISOU 1588  O   TRP A 778    10671   9697   4063   2353   -117   1960       O  
ATOM   1589  CB  TRP A 778      10.715   6.402 -12.550  1.00 63.60           C  
ANISOU 1589  CB  TRP A 778    10118   9645   4403   2045   -259   1490       C  
ATOM   1590  CG  TRP A 778      12.099   5.839 -12.587  1.00 56.53           C  
ANISOU 1590  CG  TRP A 778     9351   8566   3561   1784    -35   1416       C  
ATOM   1591  CD1 TRP A 778      13.061   5.944 -11.618  1.00 60.13           C  
ANISOU 1591  CD1 TRP A 778     9873   8686   4288   1645    168   1422       C  
ATOM   1592  CD2 TRP A 778      12.670   5.042 -13.636  1.00 62.18           C  
ANISOU 1592  CD2 TRP A 778    10122   9446   4059   1627     14   1298       C  
ATOM   1593  NE1 TRP A 778      14.201   5.278 -12.011  1.00 62.64           N  
ANISOU 1593  NE1 TRP A 778    10268   8957   4575   1429    343   1321       N  
ATOM   1594  CE2 TRP A 778      13.987   4.717 -13.245  1.00 60.15           C  
ANISOU 1594  CE2 TRP A 778     9953   8937   3963   1418    260   1242       C  
ATOM   1595  CE3 TRP A 778      12.200   4.583 -14.873  1.00 56.29           C  
ANISOU 1595  CE3 TRP A 778     9351   9040   2996   1641   -118   1221       C  
ATOM   1596  CZ2 TRP A 778      14.834   3.949 -14.041  1.00 56.90           C  
ANISOU 1596  CZ2 TRP A 778     9600   8603   3416   1242    383   1110       C  
ATOM   1597  CZ3 TRP A 778      13.043   3.820 -15.663  1.00 64.62           C  
ANISOU 1597  CZ3 TRP A 778    10487  10159   3906   1447      3   1088       C  
ATOM   1598  CH2 TRP A 778      14.345   3.510 -15.243  1.00 64.82           C  
ANISOU 1598  CH2 TRP A 778    10594   9927   4106   1259    257   1034       C  
ATOM   1599  N   TYR A 779      12.626   8.987 -13.540  1.00 58.19           N  
ANISOU 1599  N   TYR A 779    10084   8270   3755   2129    264   2033       N  
ATOM   1600  CA  TYR A 779      13.474   9.551 -14.585  1.00 68.80           C  
ANISOU 1600  CA  TYR A 779    11680   9507   4953   2086    456   2188       C  
ATOM   1601  C   TYR A 779      14.229   8.411 -15.257  1.00 63.86           C  
ANISOU 1601  C   TYR A 779    11022   9065   4178   1848    507   2020       C  
ATOM   1602  O   TYR A 779      15.194   7.882 -14.699  1.00 71.73           O  
ANISOU 1602  O   TYR A 779    11989   9915   5351   1615    665   1892       O  
ATOM   1603  CB  TYR A 779      14.431  10.578 -13.992  1.00 72.97           C  
ANISOU 1603  CB  TYR A 779    12401   9587   5736   1995    735   2314       C  
ATOM   1604  CG  TYR A 779      15.398  11.159 -14.997  1.00 81.37           C  
ANISOU 1604  CG  TYR A 779    13717  10528   6672   1906    963   2459       C  
ATOM   1605  CD1 TYR A 779      15.029  12.225 -15.808  1.00 76.86           C  
ANISOU 1605  CD1 TYR A 779    13364   9910   5928   2122    985   2697       C  
ATOM   1606  CD2 TYR A 779      16.680  10.644 -15.133  1.00 80.72           C  
ANISOU 1606  CD2 TYR A 779    13649  10384   6636   1614   1167   2356       C  
ATOM   1607  CE1 TYR A 779      15.910  12.758 -16.725  1.00 86.10           C  
ANISOU 1607  CE1 TYR A 779    14777  10967   6971   2031   1206   2836       C  
ATOM   1608  CE2 TYR A 779      17.565  11.168 -16.050  1.00 73.51           C  
ANISOU 1608  CE2 TYR A 779    12945   9383   5604   1518   1386   2478       C  
ATOM   1609  CZ  TYR A 779      17.179  12.226 -16.842  1.00 82.73           C  
ANISOU 1609  CZ  TYR A 779    14343  10494   6596   1716   1407   2722       C  
ATOM   1610  OH  TYR A 779      18.067  12.750 -17.758  1.00 86.92           O  
ANISOU 1610  OH  TYR A 779    15094  10933   6996   1609   1638   2851       O  
ATOM   1611  N   CYS A 780      13.797   8.012 -16.452  1.00 67.45           N  
ANISOU 1611  N   CYS A 780    11475   9850   4303   1909    378   2002       N  
ATOM   1612  CA  CYS A 780      14.539   6.960 -17.147  1.00 68.39           C  
ANISOU 1612  CA  CYS A 780    11582  10134   4269   1680    450   1823       C  
ATOM   1613  C   CYS A 780      15.842   7.530 -17.691  1.00 72.24           C  
ANISOU 1613  C   CYS A 780    12295  10403   4752   1553    749   1956       C  
ATOM   1614  O   CYS A 780      15.811   8.463 -18.506  1.00 71.59           O  
ANISOU 1614  O   CYS A 780    12408  10291   4504   1679    802   2183       O  
ATOM   1615  CB  CYS A 780      13.746   6.337 -18.286  1.00 69.24           C  
ANISOU 1615  CB  CYS A 780    11626  10665   4016   1743    237   1729       C  
ATOM   1616  SG  CYS A 780      14.821   5.287 -19.318  1.00 74.69           S  
ANISOU 1616  SG  CYS A 780    12377  11504   4497   1468    395   1534       S  
ATOM   1617  N   PRO A 781      16.999   6.995 -17.291  1.00 72.64           N  
ANISOU 1617  N   PRO A 781    12316  10313   4972   1308    955   1819       N  
ATOM   1618  CA  PRO A 781      18.273   7.568 -17.742  1.00 70.24           C  
ANISOU 1618  CA  PRO A 781    12182   9817   4690   1165   1252   1926       C  
ATOM   1619  C   PRO A 781      18.583   7.313 -19.206  1.00 75.68           C  
ANISOU 1619  C   PRO A 781    12972  10749   5034   1126   1303   1937       C  
ATOM   1620  O   PRO A 781      19.495   7.959 -19.733  1.00 85.12           O  
ANISOU 1620  O   PRO A 781    14329  11813   6200   1039   1540   2069       O  
ATOM   1621  CB  PRO A 781      19.302   6.885 -16.832  1.00 72.74           C  
ANISOU 1621  CB  PRO A 781    12364   9987   5286    934   1416   1725       C  
ATOM   1622  CG  PRO A 781      18.671   5.579 -16.482  1.00 72.54           C  
ANISOU 1622  CG  PRO A 781    12141  10183   5238    933   1215   1477       C  
ATOM   1623  CD  PRO A 781      17.191   5.845 -16.390  1.00 73.00           C  
ANISOU 1623  CD  PRO A 781    12163  10375   5199   1159    930   1553       C  
ATOM   1624  N   ASN A 782      17.859   6.414 -19.884  1.00 73.78           N  
ANISOU 1624  N   ASN A 782    12644  10863   4527   1170   1097   1791       N  
ATOM   1625  CA  ASN A 782      18.183   6.113 -21.278  1.00 77.26           C  
ANISOU 1625  CA  ASN A 782    13180  11551   4624   1111   1152   1772       C  
ATOM   1626  C   ASN A 782      17.590   7.140 -22.236  1.00 83.51           C  
ANISOU 1626  C   ASN A 782    14172  12417   5141   1318   1084   2054       C  
ATOM   1627  O   ASN A 782      18.240   7.511 -23.221  1.00 79.08           O  
ANISOU 1627  O   ASN A 782    13785  11884   4378   1266   1254   2174       O  
ATOM   1628  CB  ASN A 782      17.712   4.706 -21.650  1.00 70.70           C  
ANISOU 1628  CB  ASN A 782    12190  11059   3614   1034    980   1461       C  
ATOM   1629  CG  ASN A 782      18.091   4.311 -23.086  1.00 77.82           C  
ANISOU 1629  CG  ASN A 782    13190  12224   4153    946   1050   1399       C  
ATOM   1630  OD1 ASN A 782      19.186   4.617 -23.576  1.00 75.71           O  
ANISOU 1630  OD1 ASN A 782    13033  11877   3857    841   1308   1476       O  
ATOM   1631  ND2 ASN A 782      17.175   3.629 -23.762  1.00 77.61           N  
ANISOU 1631  ND2 ASN A 782    13117  12522   3848    976    821   1245       N  
ATOM   1632  N   CYS A 783      16.366   7.611 -21.991  1.00 86.82           N  
ANISOU 1632  N   CYS A 783    14565  12882   5539   1566    845   2165       N  
ATOM   1633  CA  CYS A 783      15.811   8.669 -22.832  1.00 90.12           C  
ANISOU 1633  CA  CYS A 783    15183  13343   5718   1810    792   2452       C  
ATOM   1634  C   CYS A 783      15.599   9.983 -22.094  1.00 83.56           C  
ANISOU 1634  C   CYS A 783    14472  12156   5120   1998    852   2705       C  
ATOM   1635  O   CYS A 783      15.128  10.946 -22.709  1.00 85.87           O  
ANISOU 1635  O   CYS A 783    14951  12436   5238   2235    827   2958       O  
ATOM   1636  CB  CYS A 783      14.499   8.228 -23.506  1.00 94.66           C  
ANISOU 1636  CB  CYS A 783    15649  14336   5983   1998    464   2386       C  
ATOM   1637  SG  CYS A 783      13.433   7.062 -22.635  1.00 80.58           S  
ANISOU 1637  SG  CYS A 783    13508  12785   4323   1984    161   2058       S  
ATOM   1638  N   LYS A 784      15.977  10.063 -20.816  1.00 79.71           N  
ANISOU 1638  N   LYS A 784    13902  11371   5013   1896    948   2638       N  
ATOM   1639  CA  LYS A 784      15.977  11.320 -20.062  1.00 88.08           C  
ANISOU 1639  CA  LYS A 784    15100  12043   6324   2012   1062   2838       C  
ATOM   1640  C   LYS A 784      14.590  11.952 -20.005  1.00 95.75           C  
ANISOU 1640  C   LYS A 784    16066  13092   7221   2373    830   2977       C  
ATOM   1641  O   LYS A 784      14.448  13.177 -20.072  1.00 92.90           O  
ANISOU 1641  O   LYS A 784    15925  12495   6879   2560    923   3218       O  
ATOM   1642  CB  LYS A 784      16.989  12.320 -20.635  1.00 89.04           C  
ANISOU 1642  CB  LYS A 784    15520  11893   6417   1928   1370   3050       C  
ATOM   1643  CG  LYS A 784      18.399  11.778 -20.781  1.00 83.79           C  
ANISOU 1643  CG  LYS A 784    14841  11185   5812   1583   1620   2916       C  
ATOM   1644  CD  LYS A 784      18.636  11.280 -22.188  1.00 87.80           C  
ANISOU 1644  CD  LYS A 784    15412  12010   5939   1538   1631   2918       C  
ATOM   1645  CE  LYS A 784      19.809  10.326 -22.242  1.00 91.79           C  
ANISOU 1645  CE  LYS A 784    15790  12589   6496   1225   1805   2688       C  
ATOM   1646  NZ  LYS A 784      19.905   9.664 -23.570  1.00 88.63           N  
ANISOU 1646  NZ  LYS A 784    15415  12550   5711   1186   1783   2634       N  
ATOM   1647  N   GLU A 785      13.559  11.122 -19.903  1.00 99.32           N  
ANISOU 1647  N   GLU A 785    16265  13887   7586   2474    536   2813       N  
ATOM   1648  CA  GLU A 785      12.202  11.585 -19.679  1.00103.30           C  
ANISOU 1648  CA  GLU A 785    16677  14513   8060   2807    302   2890       C  
ATOM   1649  C   GLU A 785      11.657  10.952 -18.406  1.00 95.76           C  
ANISOU 1649  C   GLU A 785    15429  13586   7368   2766    156   2674       C  
ATOM   1650  O   GLU A 785      12.097   9.874 -17.986  1.00 96.95           O  
ANISOU 1650  O   GLU A 785    15422  13797   7616   2507    158   2439       O  
ATOM   1651  CB  GLU A 785      11.289  11.253 -20.866  1.00103.88           C  
ANISOU 1651  CB  GLU A 785    16688  15048   7734   2994     59   2896       C  
ATOM   1652  N   HIS A 786      10.712  11.644 -17.781  1.00 94.05           N  
ANISOU 1652  N   HIS A 786    15151  13318   7265   3031     47   2757       N  
ATOM   1653  CA  HIS A 786       9.988  11.066 -16.665  1.00 86.14           C  
ANISOU 1653  CA  HIS A 786    13850  12413   6466   3029   -121   2561       C  
ATOM   1654  C   HIS A 786       8.917  10.131 -17.203  1.00 84.42           C  
ANISOU 1654  C   HIS A 786    13356  12715   6007   3098   -424   2386       C  
ATOM   1655  O   HIS A 786       8.273  10.414 -18.218  1.00 79.29           O  
ANISOU 1655  O   HIS A 786    12731  12330   5066   3314   -551   2485       O  
ATOM   1656  CB  HIS A 786       9.385  12.158 -15.786  1.00 87.06           C  
ANISOU 1656  CB  HIS A 786    13992  12294   6793   3276   -106   2691       C  
ATOM   1657  CG  HIS A 786      10.391  12.824 -14.900  1.00 85.91           C  
ANISOU 1657  CG  HIS A 786    14035  11649   6958   3121    172   2752       C  
ATOM   1658  ND1 HIS A 786      10.764  12.306 -13.678  1.00 84.11           N  
ANISOU 1658  ND1 HIS A 786    13663  11274   7021   2905    216   2578       N  
ATOM   1659  CD2 HIS A 786      11.120  13.952 -15.068  1.00 88.38           C  
ANISOU 1659  CD2 HIS A 786    14666  11586   7329   3129    427   2952       C  
ATOM   1660  CE1 HIS A 786      11.670  13.093 -13.125  1.00 82.42           C  
ANISOU 1660  CE1 HIS A 786    13651  10634   7031   2786    475   2656       C  
ATOM   1661  NE2 HIS A 786      11.903  14.099 -13.948  1.00 85.19           N  
ANISOU 1661  NE2 HIS A 786    14282  10834   7252   2905    612   2874       N  
ATOM   1662  N   GLN A 787       8.762   8.994 -16.538  1.00 78.57           N  
ANISOU 1662  N   GLN A 787    12355  12121   5378   2896   -530   2113       N  
ATOM   1663  CA  GLN A 787       7.987   7.889 -17.064  1.00 80.43           C  
ANISOU 1663  CA  GLN A 787    12333  12827   5399   2837   -773   1875       C  
ATOM   1664  C   GLN A 787       7.056   7.345 -15.997  1.00 73.25           C  
ANISOU 1664  C   GLN A 787    11091  12067   4674   2828   -948   1670       C  
ATOM   1665  O   GLN A 787       7.346   7.409 -14.800  1.00 66.16           O  
ANISOU 1665  O   GLN A 787    10168  10897   4073   2753   -855   1650       O  
ATOM   1666  CB  GLN A 787       8.901   6.760 -17.563  1.00 82.82           C  
ANISOU 1666  CB  GLN A 787    12677  13188   5602   2503   -691   1680       C  
ATOM   1667  CG  GLN A 787       9.812   7.157 -18.712  1.00 79.03           C  
ANISOU 1667  CG  GLN A 787    12493  12626   4908   2476   -517   1846       C  
ATOM   1668  CD  GLN A 787       9.039   7.670 -19.904  1.00 90.83           C  
ANISOU 1668  CD  GLN A 787    14035  14413   6063   2732   -666   1988       C  
ATOM   1669  OE1 GLN A 787       9.494   8.567 -20.612  1.00 95.60           O  
ANISOU 1669  OE1 GLN A 787    14910  14878   6537   2851   -529   2245       O  
ATOM   1670  NE2 GLN A 787       7.863   7.098 -20.138  1.00 95.98           N  
ANISOU 1670  NE2 GLN A 787    14420  15484   6565   2812   -941   1815       N  
ATOM   1671  N   GLN A 788       5.927   6.815 -16.459  1.00 81.96           N  
ANISOU 1671  N   GLN A 788    11932  13621   5590   2893  -1197   1511       N  
ATOM   1672  CA  GLN A 788       5.042   6.007 -15.625  1.00 84.39           C  
ANISOU 1672  CA  GLN A 788    11882  14154   6030   2795  -1365   1245       C  
ATOM   1673  C   GLN A 788       5.510   4.553 -15.698  1.00 74.97           C  
ANISOU 1673  C   GLN A 788    10610  13057   4816   2411  -1362    935       C  
ATOM   1674  O   GLN A 788       4.874   3.669 -16.278  1.00 85.85           O  
ANISOU 1674  O   GLN A 788    11791  14807   6023   2288  -1522    692       O  
ATOM   1675  CB  GLN A 788       3.595   6.185 -16.067  1.00 96.65           C  
ANISOU 1675  CB  GLN A 788    13169  16147   7406   3035  -1607   1206       C  
ATOM   1676  CG  GLN A 788       3.036   7.558 -15.705  1.00 99.80           C  
ANISOU 1676  CG  GLN A 788    13614  16425   7882   3426  -1596   1471       C  
ATOM   1677  CD  GLN A 788       1.983   8.055 -16.675  1.00105.92           C  
ANISOU 1677  CD  GLN A 788    14290  17590   8366   3750  -1774   1553       C  
ATOM   1678  OE1 GLN A 788       1.234   7.271 -17.258  1.00110.31           O  
ANISOU 1678  OE1 GLN A 788    14581  18608   8726   3682  -1968   1337       O  
ATOM   1679  NE2 GLN A 788       1.926   9.369 -16.856  1.00110.53           N  
ANISOU 1679  NE2 GLN A 788    15092  17987   8916   4103  -1697   1859       N  
ATOM   1680  N   ALA A 789       6.683   4.336 -15.112  1.00 64.45           N  
ANISOU 1680  N   ALA A 789     9454  11366   3668   2218  -1155    940       N  
ATOM   1681  CA  ALA A 789       7.308   3.025 -15.054  1.00 63.21           C  
ANISOU 1681  CA  ALA A 789     9278  11211   3529   1874  -1095    662       C  
ATOM   1682  C   ALA A 789       6.556   2.094 -14.109  1.00 64.62           C  
ANISOU 1682  C   ALA A 789     9150  11533   3871   1708  -1221    376       C  
ATOM   1683  O   ALA A 789       5.893   2.526 -13.163  1.00 62.70           O  
ANISOU 1683  O   ALA A 789     8744  11271   3808   1830  -1290    424       O  
ATOM   1684  CB  ALA A 789       8.755   3.151 -14.577  1.00 58.63           C  
ANISOU 1684  CB  ALA A 789     8948  10208   3119   1757   -822    761       C  
ATOM   1685  N   THR A 790       6.676   0.793 -14.372  1.00 69.76           N  
ANISOU 1685  N   THR A 790     9733  12307   4465   1410  -1230     63       N  
ATOM   1686  CA  THR A 790       6.350  -0.201 -13.361  1.00 57.46           C  
ANISOU 1686  CA  THR A 790     7966  10751   3115   1169  -1258   -216       C  
ATOM   1687  C   THR A 790       7.465  -0.233 -12.328  1.00 57.05           C  
ANISOU 1687  C   THR A 790     8074  10303   3300   1092  -1052   -159       C  
ATOM   1688  O   THR A 790       8.653  -0.132 -12.662  1.00 53.54           O  
ANISOU 1688  O   THR A 790     7887   9630   2825   1073   -862    -62       O  
ATOM   1689  CB  THR A 790       6.173  -1.597 -13.964  1.00 65.94           C  
ANISOU 1689  CB  THR A 790     8958  12010   4085    856  -1292   -582       C  
ATOM   1690  OG1 THR A 790       7.407  -2.032 -14.550  1.00 71.57           O  
ANISOU 1690  OG1 THR A 790     9947  12527   4720    733  -1104   -615       O  
ATOM   1691  CG2 THR A 790       5.071  -1.606 -15.017  1.00 73.12           C  
ANISOU 1691  CG2 THR A 790     9695  13344   4744    922  -1496   -658       C  
ATOM   1692  N   LYS A 791       7.076  -0.356 -11.064  1.00 53.48           N  
ANISOU 1692  N   LYS A 791     7455   9785   3081   1051  -1082   -221       N  
ATOM   1693  CA  LYS A 791       8.022  -0.514  -9.974  1.00 49.55           C  
ANISOU 1693  CA  LYS A 791     7068   8931   2830    960   -901   -206       C  
ATOM   1694  C   LYS A 791       7.633  -1.746  -9.179  1.00 57.78           C  
ANISOU 1694  C   LYS A 791     7911   9944   4098    646   -907   -519       C  
ATOM   1695  O   LYS A 791       6.450  -1.960  -8.888  1.00 62.86           O  
ANISOU 1695  O   LYS A 791     8293  10872   4719    610  -1080   -657       O  
ATOM   1696  CB  LYS A 791       8.054   0.719  -9.076  1.00 50.61           C  
ANISOU 1696  CB  LYS A 791     7235   8827   3170   1191   -861     85       C  
ATOM   1697  CG  LYS A 791       9.057   0.659  -7.937  1.00 50.51           C  
ANISOU 1697  CG  LYS A 791     7304   8341   3546   1049   -644    117       C  
ATOM   1698  CD  LYS A 791       9.057   1.986  -7.194  1.00 60.35           C  
ANISOU 1698  CD  LYS A 791     8606   9380   4943   1279   -606    388       C  
ATOM   1699  CE  LYS A 791       9.488   1.842  -5.755  1.00 62.78           C  
ANISOU 1699  CE  LYS A 791     8857   9362   5637   1134   -486    348       C  
ATOM   1700  NZ  LYS A 791       9.157   3.078  -4.990  1.00 73.46           N  
ANISOU 1700  NZ  LYS A 791    10214  10583   7113   1352   -488    551       N  
ATOM   1701  N   LYS A 792       8.623  -2.567  -8.859  1.00 46.62           N  
ANISOU 1701  N   LYS A 792     6626   8201   2888    425   -708   -632       N  
ATOM   1702  CA  LYS A 792       8.424  -3.749  -8.037  1.00 50.37           C  
ANISOU 1702  CA  LYS A 792     6990   8549   3599    136   -660   -889       C  
ATOM   1703  C   LYS A 792       9.542  -3.782  -7.015  1.00 41.50           C  
ANISOU 1703  C   LYS A 792     5994   6960   2814    106   -450   -780       C  
ATOM   1704  O   LYS A 792      10.714  -3.653  -7.378  1.00 43.94           O  
ANISOU 1704  O   LYS A 792     6499   7072   3125    152   -296   -688       O  
ATOM   1705  CB  LYS A 792       8.425  -5.034  -8.879  1.00 55.47           C  
ANISOU 1705  CB  LYS A 792     7675   9314   4086   -117   -638  -1210       C  
ATOM   1706  CG  LYS A 792       8.581  -6.318  -8.065  1.00 56.13           C  
ANISOU 1706  CG  LYS A 792     7766   9120   4441   -413   -501  -1443       C  
ATOM   1707  CD  LYS A 792       7.372  -7.211  -8.210  1.00 61.49           C  
ANISOU 1707  CD  LYS A 792     8258  10081   5026   -677   -617  -1766       C  
ATOM   1708  CE  LYS A 792       7.647  -8.606  -7.682  1.00 55.58           C  
ANISOU 1708  CE  LYS A 792     7611   9012   4493   -989   -433  -2012       C  
ATOM   1709  NZ  LYS A 792       8.259  -8.558  -6.335  1.00 45.73           N  
ANISOU 1709  NZ  LYS A 792     6429   7346   3599   -943   -288  -1833       N  
ATOM   1710  N   LEU A 793       9.180  -3.908  -5.748  1.00 38.57           N  
ANISOU 1710  N   LEU A 793     5498   6450   2708     38   -445   -790       N  
ATOM   1711  CA  LEU A 793      10.148  -4.042  -4.673  1.00 38.25           C  
ANISOU 1711  CA  LEU A 793     5546   6016   2972      4   -271   -712       C  
ATOM   1712  C   LEU A 793      10.256  -5.495  -4.239  1.00 38.89           C  
ANISOU 1712  C   LEU A 793     5647   5934   3194   -252   -172   -946       C  
ATOM   1713  O   LEU A 793       9.287  -6.254  -4.290  1.00 39.27           O  
ANISOU 1713  O   LEU A 793     5585   6144   3193   -437   -245  -1158       O  
ATOM   1714  CB  LEU A 793       9.767  -3.181  -3.467  1.00 36.36           C  
ANISOU 1714  CB  LEU A 793     5188   5702   2924    116   -309   -548       C  
ATOM   1715  CG  LEU A 793       9.723  -1.677  -3.716  1.00 40.83           C  
ANISOU 1715  CG  LEU A 793     5781   6333   3398    387   -366   -296       C  
ATOM   1716  CD1 LEU A 793       9.501  -0.896  -2.412  1.00 42.41           C  
ANISOU 1716  CD1 LEU A 793     5897   6394   3823    480   -361   -165       C  
ATOM   1717  CD2 LEU A 793      10.994  -1.232  -4.396  1.00 37.14           C  
ANISOU 1717  CD2 LEU A 793     5537   5703   2870    465   -226   -159       C  
ATOM   1718  N   ASP A 794      11.455  -5.881  -3.827  1.00 35.71           N  
ANISOU 1718  N   ASP A 794     5392   5214   2961   -258      6   -909       N  
ATOM   1719  CA  ASP A 794      11.682  -7.200  -3.271  1.00 40.71           C  
ANISOU 1719  CA  ASP A 794     6093   5621   3754   -440    128  -1078       C  
ATOM   1720  C   ASP A 794      12.627  -7.065  -2.089  1.00 41.94           C  
ANISOU 1720  C   ASP A 794     6291   5480   4163   -350    248   -921       C  
ATOM   1721  O   ASP A 794      13.466  -6.164  -2.047  1.00 38.92           O  
ANISOU 1721  O   ASP A 794     5931   5050   3808   -186    283   -741       O  
ATOM   1722  CB  ASP A 794      12.253  -8.162  -4.314  1.00 40.77           C  
ANISOU 1722  CB  ASP A 794     6269   5585   3637   -529    233  -1265       C  
ATOM   1723  CG  ASP A 794      11.215  -8.602  -5.314  1.00 53.25           C  
ANISOU 1723  CG  ASP A 794     7797   7460   4975   -689    119  -1495       C  
ATOM   1724  OD1 ASP A 794      10.245  -9.265  -4.892  1.00 58.82           O  
ANISOU 1724  OD1 ASP A 794     8409   8211   5728   -895     77  -1665       O  
ATOM   1725  OD2 ASP A 794      11.349  -8.260  -6.510  1.00 44.65           O  
ANISOU 1725  OD2 ASP A 794     6750   6582   3634   -620     73  -1510       O  
ATOM   1726  N   LEU A 795      12.465  -7.956  -1.119  1.00 41.44           N  
ANISOU 1726  N   LEU A 795     6241   5233   4273   -469    314   -994       N  
ATOM   1727  CA  LEU A 795      13.305  -7.955   0.067  1.00 32.58           C  
ANISOU 1727  CA  LEU A 795     5152   3864   3363   -378    413   -857       C  
ATOM   1728  C   LEU A 795      14.515  -8.836  -0.201  1.00 30.04           C  
ANISOU 1728  C   LEU A 795     5006   3325   3081   -336    578   -910       C  
ATOM   1729  O   LEU A 795      14.361  -9.991  -0.601  1.00 36.30           O  
ANISOU 1729  O   LEU A 795     5925   4022   3847   -462    655  -1091       O  
ATOM   1730  CB  LEU A 795      12.522  -8.464   1.278  1.00 30.60           C  
ANISOU 1730  CB  LEU A 795     4847   3529   3252   -500    412   -881       C  
ATOM   1731  CG  LEU A 795      11.286  -7.638   1.669  1.00 35.36           C  
ANISOU 1731  CG  LEU A 795     5244   4360   3830   -529    263   -844       C  
ATOM   1732  CD1 LEU A 795      10.515  -8.299   2.818  1.00 44.45           C  
ANISOU 1732  CD1 LEU A 795     6351   5434   5106   -690    298   -895       C  
ATOM   1733  CD2 LEU A 795      11.700  -6.220   2.047  1.00 30.60           C  
ANISOU 1733  CD2 LEU A 795     4563   3801   3263   -319    208   -634       C  
ATOM   1734  N   TRP A 796      15.713  -8.285  -0.004  1.00 27.47           N  
ANISOU 1734  N   TRP A 796     4684   2934   2818   -162    642   -768       N  
ATOM   1735  CA  TRP A 796      16.942  -9.042  -0.199  1.00 28.52           C  
ANISOU 1735  CA  TRP A 796     4942   2901   2994    -73    798   -808       C  
ATOM   1736  C   TRP A 796      17.552  -9.524   1.111  1.00 28.41           C  
ANISOU 1736  C   TRP A 796     4941   2685   3170     21    872   -727       C  
ATOM   1737  O   TRP A 796      17.833 -10.716   1.245  1.00 37.24           O  
ANISOU 1737  O   TRP A 796     6206   3604   4339     32    985   -810       O  
ATOM   1738  CB  TRP A 796      17.982  -8.222  -0.979  1.00 26.76           C  
ANISOU 1738  CB  TRP A 796     4697   2781   2689     51    845   -736       C  
ATOM   1739  CG  TRP A 796      19.231  -9.035  -1.180  1.00 33.27           C  
ANISOU 1739  CG  TRP A 796     5613   3473   3555    159   1012   -797       C  
ATOM   1740  CD1 TRP A 796      20.374  -8.987  -0.432  1.00 32.06           C  
ANISOU 1740  CD1 TRP A 796     5399   3247   3534    313   1091   -706       C  
ATOM   1741  CD2 TRP A 796      19.442 -10.055  -2.165  1.00 38.65           C  
ANISOU 1741  CD2 TRP A 796     6450   4095   4140    135   1120   -980       C  
ATOM   1742  NE1 TRP A 796      21.291  -9.905  -0.904  1.00 34.18           N  
ANISOU 1742  NE1 TRP A 796     5765   3424   3798    418   1242   -807       N  
ATOM   1743  CE2 TRP A 796      20.741 -10.575  -1.963  1.00 33.95           C  
ANISOU 1743  CE2 TRP A 796     5886   3378   3636    309   1272   -978       C  
ATOM   1744  CE3 TRP A 796      18.657 -10.587  -3.197  1.00 35.93           C  
ANISOU 1744  CE3 TRP A 796     6213   3808   3631    -15   1104  -1164       C  
ATOM   1745  CZ2 TRP A 796      21.271 -11.593  -2.754  1.00 32.53           C  
ANISOU 1745  CZ2 TRP A 796     5860   3099   3400    356   1423  -1145       C  
ATOM   1746  CZ3 TRP A 796      19.196 -11.597  -3.994  1.00 40.54           C  
ANISOU 1746  CZ3 TRP A 796     6960   4292   4152     -1   1254  -1347       C  
ATOM   1747  CH2 TRP A 796      20.489 -12.084  -3.768  1.00 35.28           C  
ANISOU 1747  CH2 TRP A 796     6342   3473   3592    192   1419  -1332       C  
ATOM   1748  N   SER A 797      17.770  -8.626   2.079  1.00 34.18           N  
ANISOU 1748  N   SER A 797     5536   3460   3990    101    814   -566       N  
ATOM   1749  CA  SER A 797      18.293  -9.035   3.379  1.00 38.23           C  
ANISOU 1749  CA  SER A 797     6045   3834   4646    200    859   -482       C  
ATOM   1750  C   SER A 797      17.652  -8.207   4.484  1.00 34.52           C  
ANISOU 1750  C   SER A 797     5442   3435   4238    167    752   -372       C  
ATOM   1751  O   SER A 797      17.388  -7.018   4.313  1.00 33.51           O  
ANISOU 1751  O   SER A 797     5201   3457   4076    152    669   -318       O  
ATOM   1752  CB  SER A 797      19.813  -8.893   3.471  1.00 41.58           C  
ANISOU 1752  CB  SER A 797     6424   4264   5111    394    941   -424       C  
ATOM   1753  OG  SER A 797      20.211  -7.569   3.197  1.00 54.03           O  
ANISOU 1753  OG  SER A 797     7860   6013   6656    403    900   -357       O  
ATOM   1754  N   LEU A 798      17.415  -8.861   5.635  1.00 33.50           N  
ANISOU 1754  N   LEU A 798     5352   3183   4194    168    772   -333       N  
ATOM   1755  CA  LEU A 798      16.702  -8.262   6.763  1.00 34.94           C  
ANISOU 1755  CA  LEU A 798     5426   3425   4424    123    691   -251       C  
ATOM   1756  C   LEU A 798      17.630  -8.049   7.952  1.00 36.79           C  
ANISOU 1756  C   LEU A 798     5601   3649   4729    279    702   -131       C  
ATOM   1757  O   LEU A 798      18.508  -8.881   8.198  1.00 30.81           O  
ANISOU 1757  O   LEU A 798     4929   2782   3994    414    783   -108       O  
ATOM   1758  CB  LEU A 798      15.541  -9.166   7.180  1.00 28.12           C  
ANISOU 1758  CB  LEU A 798     4649   2462   3572    -40    713   -308       C  
ATOM   1759  CG  LEU A 798      14.544  -9.436   6.047  1.00 40.33           C  
ANISOU 1759  CG  LEU A 798     6219   4071   5035   -227    689   -466       C  
ATOM   1760  CD1 LEU A 798      13.475 -10.406   6.491  1.00 40.56           C  
ANISOU 1760  CD1 LEU A 798     6326   4001   5084   -433    742   -552       C  
ATOM   1761  CD2 LEU A 798      13.931  -8.116   5.576  1.00 38.45           C  
ANISOU 1761  CD2 LEU A 798     5800   4083   4727   -239    549   -453       C  
ATOM   1762  N   PRO A 799      17.458  -6.968   8.717  1.00 31.46           N  
ANISOU 1762  N   PRO A 799     4780   3097   4076    279    623    -63       N  
ATOM   1763  CA  PRO A 799      18.367  -6.698   9.826  1.00 25.34           C  
ANISOU 1763  CA  PRO A 799     3925   2363   3341    410    621     22       C  
ATOM   1764  C   PRO A 799      18.012  -7.517  11.056  1.00 31.49           C  
ANISOU 1764  C   PRO A 799     4777   3055   4135    432    640     85       C  
ATOM   1765  O   PRO A 799      16.893  -8.048  11.169  1.00 30.00           O  
ANISOU 1765  O   PRO A 799     4674   2782   3943    298    656     63       O  
ATOM   1766  CB  PRO A 799      18.157  -5.207  10.091  1.00 19.67           C  
ANISOU 1766  CB  PRO A 799     3055   1788   2631    363    545     38       C  
ATOM   1767  CG  PRO A 799      16.672  -5.014   9.792  1.00 18.78           C  
ANISOU 1767  CG  PRO A 799     2957   1680   2497    228    495      5       C  
ATOM   1768  CD  PRO A 799      16.427  -5.924   8.582  1.00 20.01           C  
ANISOU 1768  CD  PRO A 799     3232   1766   2606    175    534    -72       C  
ATOM   1769  N   PRO A 800      18.948  -7.626  12.012  1.00 30.49           N  
ANISOU 1769  N   PRO A 800     4608   2967   4008    594    642    164       N  
ATOM   1770  CA  PRO A 800      18.604  -8.178  13.335  1.00 30.55           C  
ANISOU 1770  CA  PRO A 800     4680   2929   3998    629    650    256       C  
ATOM   1771  C   PRO A 800      17.344  -7.588  13.942  1.00 27.50           C  
ANISOU 1771  C   PRO A 800     4241   2597   3611    458    606    250       C  
ATOM   1772  O   PRO A 800      16.577  -8.326  14.568  1.00 31.31           O  
ANISOU 1772  O   PRO A 800     4840   2977   4078    390    658    290       O  
ATOM   1773  CB  PRO A 800      19.835  -7.832  14.183  1.00 36.47           C  
ANISOU 1773  CB  PRO A 800     5299   3839   4718    825    606    318       C  
ATOM   1774  CG  PRO A 800      20.983  -7.815  13.177  1.00 36.42           C  
ANISOU 1774  CG  PRO A 800     5235   3876   4729    933    632    263       C  
ATOM   1775  CD  PRO A 800      20.386  -7.305  11.888  1.00 32.13           C  
ANISOU 1775  CD  PRO A 800     4701   3293   4214    755    642    167       C  
ATOM   1776  N   VAL A 801      17.107  -6.285  13.797  1.00 25.45           N  
ANISOU 1776  N   VAL A 801     3820   2483   3365    390    530    201       N  
ATOM   1777  CA  VAL A 801      15.888  -5.662  14.301  1.00 25.23           C  
ANISOU 1777  CA  VAL A 801     3728   2520   3340    260    493    182       C  
ATOM   1778  C   VAL A 801      15.139  -5.058  13.128  1.00 28.31           C  
ANISOU 1778  C   VAL A 801     4074   2938   3744    159    458    101       C  
ATOM   1779  O   VAL A 801      15.575  -4.063  12.531  1.00 28.21           O  
ANISOU 1779  O   VAL A 801     3990   2989   3740    195    422     82       O  
ATOM   1780  CB  VAL A 801      16.164  -4.609  15.388  1.00 33.41           C  
ANISOU 1780  CB  VAL A 801     4629   3701   4365    304    441    200       C  
ATOM   1781  CG1 VAL A 801      14.847  -3.984  15.863  1.00 26.82           C  
ANISOU 1781  CG1 VAL A 801     3730   2927   3533    192    421    167       C  
ATOM   1782  CG2 VAL A 801      16.856  -5.259  16.572  1.00 28.90           C  
ANISOU 1782  CG2 VAL A 801     4092   3151   3737    421    457    285       C  
ATOM   1783  N   LEU A 802      13.998  -5.639  12.821  1.00 21.79           N  
ANISOU 1783  N   LEU A 802     3292   2080   2908     30    475     54       N  
ATOM   1784  CA  LEU A 802      13.162  -5.233  11.702  1.00 24.59           C  
ANISOU 1784  CA  LEU A 802     3594   2507   3242    -53    425    -28       C  
ATOM   1785  C   LEU A 802      12.070  -4.304  12.203  1.00 25.91           C  
ANISOU 1785  C   LEU A 802     3616   2817   3410    -89    367    -43       C  
ATOM   1786  O   LEU A 802      11.216  -4.711  13.006  1.00 31.84           O  
ANISOU 1786  O   LEU A 802     4338   3596   4164   -183    395    -57       O  
ATOM   1787  CB  LEU A 802      12.571  -6.471  11.029  1.00 24.54           C  
ANISOU 1787  CB  LEU A 802     3693   2420   3211   -190    477   -110       C  
ATOM   1788  CG  LEU A 802      11.625  -6.213   9.860  1.00 27.12           C  
ANISOU 1788  CG  LEU A 802     3947   2878   3481   -287    410   -218       C  
ATOM   1789  CD1 LEU A 802      12.346  -5.415   8.771  1.00 22.64           C  
ANISOU 1789  CD1 LEU A 802     3373   2358   2872   -165    358   -201       C  
ATOM   1790  CD2 LEU A 802      11.072  -7.543   9.352  1.00 29.32           C  
ANISOU 1790  CD2 LEU A 802     4331   3077   3733   -471    478   -337       C  
ATOM   1791  N   VAL A 803      12.107  -3.058  11.762  1.00 26.95           N  
ANISOU 1791  N   VAL A 803     3670   3031   3540     -7    304    -35       N  
ATOM   1792  CA  VAL A 803      11.116  -2.076  12.157  1.00 28.74           C  
ANISOU 1792  CA  VAL A 803     3770   3380   3770     13    255    -49       C  
ATOM   1793  C   VAL A 803      10.125  -1.927  11.014  1.00 34.70           C  
ANISOU 1793  C   VAL A 803     4464   4255   4464     -2    186   -104       C  
ATOM   1794  O   VAL A 803      10.524  -1.702   9.866  1.00 35.69           O  
ANISOU 1794  O   VAL A 803     4645   4373   4542     50    157    -93       O  
ATOM   1795  CB  VAL A 803      11.782  -0.740  12.515  1.00 36.99           C  
ANISOU 1795  CB  VAL A 803     4797   4408   4849    129    249     -3       C  
ATOM   1796  CG1 VAL A 803      10.734   0.294  12.885  1.00 33.36           C  
ANISOU 1796  CG1 VAL A 803     4234   4045   4397    184    215    -22       C  
ATOM   1797  CG2 VAL A 803      12.794  -0.963  13.653  1.00 30.17           C  
ANISOU 1797  CG2 VAL A 803     3959   3487   4016    134    298     25       C  
ATOM   1798  N   VAL A 804       8.836  -2.061  11.331  1.00 26.64           N  
ANISOU 1798  N   VAL A 804     3316   3379   3428    -72    161   -168       N  
ATOM   1799  CA  VAL A 804       7.750  -2.141  10.361  1.00 27.52           C  
ANISOU 1799  CA  VAL A 804     3320   3678   3461   -108     83   -251       C  
ATOM   1800  C   VAL A 804       6.792  -0.986  10.630  1.00 36.97           C  
ANISOU 1800  C   VAL A 804     4348   5052   4648     28     18   -246       C  
ATOM   1801  O   VAL A 804       6.091  -0.966  11.650  1.00 30.17           O  
ANISOU 1801  O   VAL A 804     3371   4269   3824    -15     50   -282       O  
ATOM   1802  CB  VAL A 804       7.020  -3.491  10.432  1.00 39.47           C  
ANISOU 1802  CB  VAL A 804     4802   5237   4956   -343    127   -368       C  
ATOM   1803  CG1 VAL A 804       5.923  -3.544   9.388  1.00 41.37           C  
ANISOU 1803  CG1 VAL A 804     4891   5732   5095   -397     30   -488       C  
ATOM   1804  CG2 VAL A 804       8.007  -4.658  10.256  1.00 32.13           C  
ANISOU 1804  CG2 VAL A 804     4083   4078   4046   -442    219   -364       C  
ATOM   1805  N   HIS A 805       6.773  -0.021   9.727  1.00 27.57           N  
ANISOU 1805  N   HIS A 805     3159   3917   3401    208    -60   -195       N  
ATOM   1806  CA  HIS A 805       5.915   1.146   9.811  1.00 28.37           C  
ANISOU 1806  CA  HIS A 805     3134   4162   3483    403   -120   -172       C  
ATOM   1807  C   HIS A 805       4.668   0.899   8.971  1.00 38.27           C  
ANISOU 1807  C   HIS A 805     4198   5724   4617    413   -235   -260       C  
ATOM   1808  O   HIS A 805       4.763   0.776   7.751  1.00 34.78           O  
ANISOU 1808  O   HIS A 805     3800   5352   4063    444   -308   -254       O  
ATOM   1809  CB  HIS A 805       6.672   2.376   9.307  1.00 27.18           C  
ANISOU 1809  CB  HIS A 805     3138   3860   3328    613   -117    -43       C  
ATOM   1810  CG  HIS A 805       5.805   3.566   9.047  1.00 36.88           C  
ANISOU 1810  CG  HIS A 805     4295   5209   4510    869   -181      5       C  
ATOM   1811  ND1 HIS A 805       5.999   4.405   7.970  1.00 41.70           N  
ANISOU 1811  ND1 HIS A 805     5028   5785   5032   1069   -219    120       N  
ATOM   1812  CD2 HIS A 805       4.750   4.068   9.729  1.00 38.75           C  
ANISOU 1812  CD2 HIS A 805     4361   5594   4769    984   -200    -36       C  
ATOM   1813  CE1 HIS A 805       5.091   5.365   7.993  1.00 46.22           C  
ANISOU 1813  CE1 HIS A 805     5522   6466   5573   1320   -266    159       C  
ATOM   1814  NE2 HIS A 805       4.321   5.184   9.051  1.00 40.04           N  
ANISOU 1814  NE2 HIS A 805     4547   5804   4861   1277   -257     56       N  
ATOM   1815  N   LEU A 806       3.505   0.839   9.618  1.00 27.73           N  
ANISOU 1815  N   LEU A 806     2638   4609   3291    384   -250   -352       N  
ATOM   1816  CA  LEU A 806       2.232   0.732   8.912  1.00 32.83           C  
ANISOU 1816  CA  LEU A 806     3037   5622   3817    410   -370   -457       C  
ATOM   1817  C   LEU A 806       1.786   2.116   8.446  1.00 36.01           C  
ANISOU 1817  C   LEU A 806     3382   6150   4151    778   -469   -358       C  
ATOM   1818  O   LEU A 806       1.585   3.019   9.261  1.00 47.37           O  
ANISOU 1818  O   LEU A 806     4795   7536   5666    955   -425   -307       O  
ATOM   1819  CB  LEU A 806       1.176   0.099   9.816  1.00 38.13           C  
ANISOU 1819  CB  LEU A 806     3465   6499   4525    214   -324   -607       C  
ATOM   1820  CG  LEU A 806       1.545  -1.277  10.376  1.00 39.88           C  
ANISOU 1820  CG  LEU A 806     3785   6557   4811   -143   -195   -683       C  
ATOM   1821  CD1 LEU A 806       0.503  -1.725  11.388  1.00 39.41           C  
ANISOU 1821  CD1 LEU A 806     3508   6679   4787   -329   -113   -805       C  
ATOM   1822  CD2 LEU A 806       1.684  -2.320   9.264  1.00 37.40           C  
ANISOU 1822  CD2 LEU A 806     3531   6266   4414   -343   -229   -779       C  
ATOM   1823  N   LYS A 807       1.642   2.283   7.135  1.00 40.43           N  
ANISOU 1823  N   LYS A 807     3942   6865   4553    908   -594   -328       N  
ATOM   1824  CA  LYS A 807       1.418   3.593   6.525  1.00 33.13           C  
ANISOU 1824  CA  LYS A 807     3052   5998   3539   1297   -677   -182       C  
ATOM   1825  C   LYS A 807      -0.028   4.016   6.755  1.00 36.94           C  
ANISOU 1825  C   LYS A 807     3208   6860   3966   1491   -773   -254       C  
ATOM   1826  O   LYS A 807      -0.904   3.800   5.923  1.00 41.96           O  
ANISOU 1826  O   LYS A 807     3622   7888   4432   1555   -925   -330       O  
ATOM   1827  CB  LYS A 807       1.751   3.541   5.037  1.00 44.94           C  
ANISOU 1827  CB  LYS A 807     4666   7560   4848   1370   -776   -116       C  
ATOM   1828  CG  LYS A 807       1.714   4.888   4.343  1.00 52.78           C  
ANISOU 1828  CG  LYS A 807     5785   8538   5730   1781   -832     86       C  
ATOM   1829  CD  LYS A 807       2.359   4.785   2.979  1.00 61.49           C  
ANISOU 1829  CD  LYS A 807     7085   9623   6657   1804   -879    175       C  
ATOM   1830  CE  LYS A 807       1.781   3.617   2.197  1.00 67.45           C  
ANISOU 1830  CE  LYS A 807     7635  10749   7244   1602  -1012    -13       C  
ATOM   1831  NZ  LYS A 807       2.739   3.129   1.167  1.00 69.60           N  
ANISOU 1831  NZ  LYS A 807     8134  10904   7405   1476   -989     13       N  
ATOM   1832  N   ARG A 808      -0.291   4.634   7.903  1.00 43.96           N  
ANISOU 1832  N   ARG A 808     4047   7667   4989   1592   -685   -247       N  
ATOM   1833  CA  ARG A 808      -1.646   5.084   8.180  1.00 43.63           C  
ANISOU 1833  CA  ARG A 808     3680   7992   4904   1806   -757   -322       C  
ATOM   1834  C   ARG A 808      -1.882   6.527   7.766  1.00 42.61           C  
ANISOU 1834  C   ARG A 808     3669   7802   4717   2258   -791   -151       C  
ATOM   1835  O   ARG A 808      -3.033   6.909   7.520  1.00 46.06           O  
ANISOU 1835  O   ARG A 808     3939   8499   5061   2408   -854   -187       O  
ATOM   1836  CB  ARG A 808      -1.966   4.907   9.670  1.00 43.06           C  
ANISOU 1836  CB  ARG A 808     3480   7890   4989   1650   -620   -433       C  
ATOM   1837  CG  ARG A 808      -1.911   3.459  10.124  1.00 35.74           C  
ANISOU 1837  CG  ARG A 808     2475   6996   4107   1181   -551   -589       C  
ATOM   1838  CD  ARG A 808      -2.272   3.316  11.603  1.00 39.87           C  
ANISOU 1838  CD  ARG A 808     2886   7510   4752   1042   -405   -678       C  
ATOM   1839  NE  ARG A 808      -2.283   1.913  12.009  1.00 34.70           N  
ANISOU 1839  NE  ARG A 808     2187   6873   4124    602   -321   -806       N  
ATOM   1840  CZ  ARG A 808      -3.299   1.082  11.785  1.00 40.43           C  
ANISOU 1840  CZ  ARG A 808     2619   7960   4781    382   -352   -986       C  
ATOM   1841  NH1 ARG A 808      -4.390   1.525  11.172  1.00 40.92           N  
ANISOU 1841  NH1 ARG A 808     2399   8415   4732    573   -483  -1057       N  
ATOM   1842  NH2 ARG A 808      -3.226  -0.187  12.177  1.00 43.97           N  
ANISOU 1842  NH2 ARG A 808     3098   8345   5265    -34   -237  -1088       N  
ATOM   1843  N   PHE A 809      -0.833   7.336   7.683  1.00 48.84           N  
ANISOU 1843  N   PHE A 809     4801   8193   5562   2417   -712     30       N  
ATOM   1844  CA  PHE A 809      -0.952   8.719   7.242  1.00 56.94           C  
ANISOU 1844  CA  PHE A 809     6052   9037   6544   2744   -684    201       C  
ATOM   1845  C   PHE A 809      -0.397   8.837   5.829  1.00 63.41           C  
ANISOU 1845  C   PHE A 809     7086   9806   7202   2831   -752    352       C  
ATOM   1846  O   PHE A 809       0.734   8.414   5.565  1.00 71.01           O  
ANISOU 1846  O   PHE A 809     8232  10569   8180   2691   -720    407       O  
ATOM   1847  CB  PHE A 809      -0.217   9.667   8.192  1.00 49.06           C  
ANISOU 1847  CB  PHE A 809     5319   7595   5728   2804   -501    275       C  
ATOM   1848  CG  PHE A 809      -0.544   9.440   9.637  1.00 52.55           C  
ANISOU 1848  CG  PHE A 809     5581   8065   6320   2678   -415    120       C  
ATOM   1849  CD1 PHE A 809      -1.604  10.099  10.229  1.00 60.66           C  
ANISOU 1849  CD1 PHE A 809     6475   9206   7368   2832   -392     65       C  
ATOM   1850  CD2 PHE A 809       0.207   8.557  10.402  1.00 54.80           C  
ANISOU 1850  CD2 PHE A 809     5851   8259   6713   2381   -343     29       C  
ATOM   1851  CE1 PHE A 809      -1.911   9.891  11.563  1.00 56.93           C  
ANISOU 1851  CE1 PHE A 809     5847   8769   7013   2706   -298    -79       C  
ATOM   1852  CE2 PHE A 809      -0.093   8.343  11.733  1.00 51.53           C  
ANISOU 1852  CE2 PHE A 809     5296   7874   6409   2239   -248   -108       C  
ATOM   1853  CZ  PHE A 809      -1.157   9.012  12.314  1.00 58.29           C  
ANISOU 1853  CZ  PHE A 809     5999   8871   7278   2425   -226   -164       C  
ATOM   1854  N   SER A 810      -1.195   9.405   4.931  1.00 68.44           N  
ANISOU 1854  N   SER A 810     7698  10634   7671   3068   -839    418       N  
ATOM   1855  CA  SER A 810      -0.829   9.552   3.523  1.00 78.62           C  
ANISOU 1855  CA  SER A 810     9172  11929   8770   3168   -903    557       C  
ATOM   1856  C   SER A 810      -0.365   8.226   2.922  1.00 74.73           C  
ANISOU 1856  C   SER A 810     8592  11618   8184   2897  -1000    464       C  
ATOM   1857  O   SER A 810       0.189   8.190   1.826  1.00 78.94           O  
ANISOU 1857  O   SER A 810     9308  12118   8568   2917  -1031    567       O  
ATOM   1858  CB  SER A 810       0.257  10.622   3.353  1.00 76.58           C  
ANISOU 1858  CB  SER A 810     9346  11179   8570   3279   -743    771       C  
ATOM   1859  OG  SER A 810       1.468  10.239   3.980  1.00 80.18           O  
ANISOU 1859  OG  SER A 810     9954  11325   9186   3043   -628    762       O  
ATOM   1860  N   ASP A 817      -7.019  11.530   5.498  1.00 85.97           N  
ANISOU 1860  N   ASP A 817     8938  14114   9613   4033  -1061    179       N  
ATOM   1861  CA  ASP A 817      -6.870  11.348   6.935  1.00 84.34           C  
ANISOU 1861  CA  ASP A 817     8675  13743   9626   3837   -933     67       C  
ATOM   1862  C   ASP A 817      -6.250   9.981   7.224  1.00 80.20           C  
ANISOU 1862  C   ASP A 817     8052  13248   9171   3401   -931    -68       C  
ATOM   1863  O   ASP A 817      -5.769   9.300   6.317  1.00 85.55           O  
ANISOU 1863  O   ASP A 817     8766  13991   9748   3266  -1014    -54       O  
ATOM   1864  CB  ASP A 817      -8.225  11.492   7.641  1.00 90.41           C  
ANISOU 1864  CB  ASP A 817     9119  14837  10397   3933   -940    -78       C  
ATOM   1865  CG  ASP A 817      -8.105  12.108   9.034  1.00 98.75           C  
ANISOU 1865  CG  ASP A 817    10256  15603  11661   3954   -773    -98       C  
ATOM   1866  OD1 ASP A 817      -7.333  11.588   9.870  1.00 93.55           O  
ANISOU 1866  OD1 ASP A 817     9660  14727  11157   3666   -671   -158       O  
ATOM   1867  OD2 ASP A 817      -8.786  13.124   9.289  1.00105.11           O  
ANISOU 1867  OD2 ASP A 817    11065  16405  12467   4269   -740    -59       O  
ATOM   1868  N   LYS A 818      -6.279   9.590   8.493  1.00 62.63           N  
ANISOU 1868  N   LYS A 818     5711  10977   7110   3188   -827   -198       N  
ATOM   1869  CA  LYS A 818      -5.650   8.359   8.940  1.00 55.78           C  
ANISOU 1869  CA  LYS A 818     4779  10089   6327   2785   -792   -315       C  
ATOM   1870  C   LYS A 818      -6.501   7.141   8.589  1.00 50.69           C  
ANISOU 1870  C   LYS A 818     3791   9899   5572   2516   -888   -514       C  
ATOM   1871  O   LYS A 818      -7.731   7.166   8.699  1.00 60.07           O  
ANISOU 1871  O   LYS A 818     4710  11426   6690   2565   -922   -629       O  
ATOM   1872  CB  LYS A 818      -5.412   8.431  10.451  1.00 53.21           C  
ANISOU 1872  CB  LYS A 818     4466   9556   6197   2663   -628   -378       C  
ATOM   1873  CG  LYS A 818      -4.787   7.206  11.075  1.00 49.80           C  
ANISOU 1873  CG  LYS A 818     3975   9091   5854   2262   -563   -491       C  
ATOM   1874  CD  LYS A 818      -4.769   7.351  12.586  1.00 51.60           C  
ANISOU 1874  CD  LYS A 818     4190   9182   6234   2173   -398   -560       C  
ATOM   1875  CE  LYS A 818      -4.313   6.074  13.251  1.00 49.91           C  
ANISOU 1875  CE  LYS A 818     3898   8980   6085   1765   -319   -674       C  
ATOM   1876  NZ  LYS A 818      -4.423   6.160  14.739  1.00 55.52           N  
ANISOU 1876  NZ  LYS A 818     4582   9612   6903   1667   -154   -747       N  
ATOM   1877  N   LEU A 819      -5.834   6.078   8.149  1.00 50.70           N  
ANISOU 1877  N   LEU A 819     3811   9900   5555   2220   -920   -565       N  
ATOM   1878  CA  LEU A 819      -6.467   4.775   7.969  1.00 58.04           C  
ANISOU 1878  CA  LEU A 819     4464  11171   6416   1857   -961   -784       C  
ATOM   1879  C   LEU A 819      -6.469   4.038   9.306  1.00 48.59           C  
ANISOU 1879  C   LEU A 819     3170   9910   5380   1520   -808   -918       C  
ATOM   1880  O   LEU A 819      -5.404   3.802   9.881  1.00 48.70           O  
ANISOU 1880  O   LEU A 819     3362   9616   5526   1389   -716   -865       O  
ATOM   1881  CB  LEU A 819      -5.715   3.957   6.918  1.00 58.96           C  
ANISOU 1881  CB  LEU A 819     4680  11278   6444   1670  -1043   -789       C  
ATOM   1882  CG  LEU A 819      -5.293   4.658   5.623  1.00 58.44           C  
ANISOU 1882  CG  LEU A 819     4816  11164   6226   1979  -1161   -609       C  
ATOM   1883  CD1 LEU A 819      -4.416   3.748   4.776  1.00 62.30           C  
ANISOU 1883  CD1 LEU A 819     5421  11606   6643   1743  -1215   -633       C  
ATOM   1884  CD2 LEU A 819      -6.506   5.115   4.832  1.00 59.69           C  
ANISOU 1884  CD2 LEU A 819     4788  11696   6194   2215  -1275   -635       C  
ATOM   1885  N   ASP A 820      -7.652   3.674   9.803  1.00 53.48           N  
ANISOU 1885  N   ASP A 820     3516  10826   5979   1379   -772  -1088       N  
ATOM   1886  CA  ASP A 820      -7.769   2.982  11.082  1.00 57.54           C  
ANISOU 1886  CA  ASP A 820     3955  11288   6621   1053   -606  -1206       C  
ATOM   1887  C   ASP A 820      -7.874   1.473  10.921  1.00 53.91           C  
ANISOU 1887  C   ASP A 820     3408  10937   6137    567   -563  -1382       C  
ATOM   1888  O   ASP A 820      -8.335   0.792  11.844  1.00 52.28           O  
ANISOU 1888  O   ASP A 820     3106  10769   5989    270   -422  -1505       O  
ATOM   1889  CB  ASP A 820      -8.973   3.506  11.868  1.00 63.05           C  
ANISOU 1889  CB  ASP A 820     4439  12200   7317   1173   -554  -1282       C  
ATOM   1890  CG  ASP A 820      -8.571   4.446  12.980  1.00 68.96           C  
ANISOU 1890  CG  ASP A 820     5333  12665   8202   1379   -441  -1171       C  
ATOM   1891  OD1 ASP A 820      -7.396   4.398  13.399  1.00 74.65           O  
ANISOU 1891  OD1 ASP A 820     6287  13043   9033   1313   -365  -1080       O  
ATOM   1892  OD2 ASP A 820      -9.429   5.227  13.442  1.00 78.24           O  
ANISOU 1892  OD2 ASP A 820     6386  13971   9370   1604   -423  -1190       O  
ATOM   1893  N   THR A 821      -7.472   0.950   9.763  1.00 56.00           N  
ANISOU 1893  N   THR A 821     3732  11234   6310    479   -668  -1397       N  
ATOM   1894  CA  THR A 821      -7.482  -0.485   9.494  1.00 57.41           C  
ANISOU 1894  CA  THR A 821     3890  11456   6469     12   -613  -1569       C  
ATOM   1895  C   THR A 821      -6.903  -1.277  10.657  1.00 49.86           C  
ANISOU 1895  C   THR A 821     3067  10205   5672   -332   -413  -1587       C  
ATOM   1896  O   THR A 821      -5.862  -0.918  11.206  1.00 49.49           O  
ANISOU 1896  O   THR A 821     3210   9855   5740   -239   -362  -1441       O  
ATOM   1897  CB  THR A 821      -6.660  -0.768   8.237  1.00 58.94           C  
ANISOU 1897  CB  THR A 821     4238  11578   6578      8   -733  -1530       C  
ATOM   1898  OG1 THR A 821      -7.038   0.148   7.206  1.00 73.19           O  
ANISOU 1898  OG1 THR A 821     5980  13602   8225    394   -910  -1451       O  
ATOM   1899  CG2 THR A 821      -6.874  -2.197   7.764  1.00 57.12           C  
ANISOU 1899  CG2 THR A 821     3984  11421   6297   -449   -682  -1738       C  
ATOM   1900  N   LEU A 822      -7.582  -2.360  11.030  1.00 48.88           N  
ANISOU 1900  N   LEU A 822     2858  10169   5545   -725   -285  -1762       N  
ATOM   1901  CA  LEU A 822      -7.015  -3.317  11.974  1.00 49.08           C  
ANISOU 1901  CA  LEU A 822     3074   9882   5692  -1086    -78  -1768       C  
ATOM   1902  C   LEU A 822      -6.047  -4.212  11.211  1.00 51.05           C  
ANISOU 1902  C   LEU A 822     3553   9895   5946  -1311    -78  -1776       C  
ATOM   1903  O   LEU A 822      -6.460  -4.963  10.319  1.00 56.73           O  
ANISOU 1903  O   LEU A 822     4236  10750   6571  -1510   -109  -1926       O  
ATOM   1904  CB  LEU A 822      -8.113  -4.140  12.644  1.00 53.20           C  
ANISOU 1904  CB  LEU A 822     3470  10546   6198  -1412     78  -1935       C  
ATOM   1905  CG  LEU A 822      -7.700  -5.259  13.606  1.00 54.09           C  
ANISOU 1905  CG  LEU A 822     3816  10331   6404  -1798    317  -1935       C  
ATOM   1906  CD1 LEU A 822      -6.841  -4.725  14.745  1.00 51.32           C  
ANISOU 1906  CD1 LEU A 822     3630   9699   6169  -1658    406  -1745       C  
ATOM   1907  CD2 LEU A 822      -8.941  -5.974  14.158  1.00 54.21           C  
ANISOU 1907  CD2 LEU A 822     3685  10536   6375  -2090    460  -2107       C  
ATOM   1908  N   VAL A 823      -4.761  -4.110  11.530  1.00 46.77           N  
ANISOU 1908  N   VAL A 823     3248   9015   5509  -1272    -39  -1628       N  
ATOM   1909  CA  VAL A 823      -3.738  -4.981  10.962  1.00 44.24           C  
ANISOU 1909  CA  VAL A 823     3186   8415   5209  -1491    -10  -1630       C  
ATOM   1910  C   VAL A 823      -3.378  -6.015  12.021  1.00 39.90           C  
ANISOU 1910  C   VAL A 823     2870   7523   4767  -1823    240  -1615       C  
ATOM   1911  O   VAL A 823      -2.851  -5.673  13.082  1.00 42.53           O  
ANISOU 1911  O   VAL A 823     3353   7623   5184  -1706    338  -1450       O  
ATOM   1912  CB  VAL A 823      -2.498  -4.197  10.508  1.00 43.23           C  
ANISOU 1912  CB  VAL A 823     3336   8000   5091  -1136   -110  -1405       C  
ATOM   1913  CG1 VAL A 823      -1.450  -5.154   9.952  1.00 48.90           C  
ANISOU 1913  CG1 VAL A 823     4395   8365   5820  -1315    -51  -1386       C  
ATOM   1914  CG2 VAL A 823      -2.859  -3.162   9.438  1.00 38.52           C  
ANISOU 1914  CG2 VAL A 823     2553   7715   4366   -790   -340  -1389       C  
ATOM   1915  N   ASP A 824      -3.691  -7.275  11.746  1.00 47.18           N  
ANISOU 1915  N   ASP A 824     3909   8356   5660  -2163    353  -1746       N  
ATOM   1916  CA  ASP A 824      -3.335  -8.376  12.631  1.00 45.36           C  
ANISOU 1916  CA  ASP A 824     3974   7752   5509  -2446    599  -1706       C  
ATOM   1917  C   ASP A 824      -1.902  -8.807  12.334  1.00 46.71           C  
ANISOU 1917  C   ASP A 824     4498   7509   5742  -2460    636  -1597       C  
ATOM   1918  O   ASP A 824      -1.562  -9.096  11.183  1.00 55.25           O  
ANISOU 1918  O   ASP A 824     5650   8568   6774  -2485    546  -1676       O  
ATOM   1919  CB  ASP A 824      -4.312  -9.541  12.426  1.00 55.55           C  
ANISOU 1919  CB  ASP A 824     5260   9108   6738  -2777    719  -1897       C  
ATOM   1920  CG  ASP A 824      -4.170 -10.636  13.475  1.00 59.39           C  
ANISOU 1920  CG  ASP A 824     6043   9237   7285  -3031    984  -1842       C  
ATOM   1921  OD1 ASP A 824      -3.696 -10.353  14.590  1.00 64.02           O  
ANISOU 1921  OD1 ASP A 824     6745   9643   7937  -2938   1070  -1666       O  
ATOM   1922  OD2 ASP A 824      -4.542 -11.790  13.175  1.00 69.44           O  
ANISOU 1922  OD2 ASP A 824     7443  10415   8527  -3313   1112  -1974       O  
ATOM   1923  N   PHE A 825      -1.062  -8.832  13.360  1.00 43.52           N  
ANISOU 1923  N   PHE A 825     4352   6766   5416  -2370    758  -1392       N  
ATOM   1924  CA  PHE A 825       0.341  -9.194  13.251  1.00 35.24           C  
ANISOU 1924  CA  PHE A 825     3692   5289   4408  -2242    790  -1224       C  
ATOM   1925  C   PHE A 825       0.701 -10.162  14.372  1.00 44.21           C  
ANISOU 1925  C   PHE A 825     5120   6081   5598  -2416   1032  -1119       C  
ATOM   1926  O   PHE A 825       0.031 -10.195  15.407  1.00 45.33           O  
ANISOU 1926  O   PHE A 825     5170   6311   5744  -2543   1155  -1114       O  
ATOM   1927  CB  PHE A 825       1.249  -7.957  13.316  1.00 34.36           C  
ANISOU 1927  CB  PHE A 825     3608   5138   4310  -1813    639  -1028       C  
ATOM   1928  CG  PHE A 825       0.978  -7.054  14.492  1.00 39.08           C  
ANISOU 1928  CG  PHE A 825     4071   5847   4930  -1655    649   -932       C  
ATOM   1929  CD1 PHE A 825       0.058  -6.012  14.389  1.00 37.03           C  
ANISOU 1929  CD1 PHE A 825     3478   5952   4639  -1519    530  -1005       C  
ATOM   1930  CD2 PHE A 825       1.669  -7.223  15.691  1.00 30.65           C  
ANISOU 1930  CD2 PHE A 825     3214   4532   3899  -1613    775   -771       C  
ATOM   1931  CE1 PHE A 825      -0.186  -5.158  15.470  1.00 36.55           C  
ANISOU 1931  CE1 PHE A 825     3308   5980   4600  -1362    555   -937       C  
ATOM   1932  CE2 PHE A 825       1.431  -6.359  16.790  1.00 30.72           C  
ANISOU 1932  CE2 PHE A 825     3103   4658   3910  -1473    787   -705       C  
ATOM   1933  CZ  PHE A 825       0.502  -5.331  16.670  1.00 30.18           C  
ANISOU 1933  CZ  PHE A 825     2714   4926   3826  -1355    686   -797       C  
ATOM   1934  N   PRO A 826       1.735 -10.972  14.181  1.00 42.29           N  
ANISOU 1934  N   PRO A 826     5233   5452   5382  -2409   1115  -1031       N  
ATOM   1935  CA  PRO A 826       2.072 -11.967  15.202  1.00 41.41           C  
ANISOU 1935  CA  PRO A 826     5437   4996   5301  -2539   1352   -909       C  
ATOM   1936  C   PRO A 826       2.915 -11.373  16.314  1.00 42.19           C  
ANISOU 1936  C   PRO A 826     5637   4989   5403  -2233   1340   -657       C  
ATOM   1937  O   PRO A 826       3.698 -10.442  16.113  1.00 36.55           O  
ANISOU 1937  O   PRO A 826     4874   4321   4692  -1912   1169   -563       O  
ATOM   1938  CB  PRO A 826       2.849 -13.033  14.414  1.00 44.40           C  
ANISOU 1938  CB  PRO A 826     6143   5039   5689  -2545   1407   -917       C  
ATOM   1939  CG  PRO A 826       3.449 -12.301  13.286  1.00 51.69           C  
ANISOU 1939  CG  PRO A 826     6975   6057   6608  -2353   1209   -954       C  
ATOM   1940  CD  PRO A 826       2.498 -11.179  12.936  1.00 53.65           C  
ANISOU 1940  CD  PRO A 826     6808   6766   6811  -2319   1022  -1068       C  
ATOM   1941  N   ILE A 827       2.689 -11.893  17.526  1.00 41.13           N  
ANISOU 1941  N   ILE A 827     5634   4739   5252  -2356   1532   -559       N  
ATOM   1942  CA  ILE A 827       3.575 -11.601  18.649  1.00 33.76           C  
ANISOU 1942  CA  ILE A 827     4860   3679   4290  -2092   1546   -319       C  
ATOM   1943  C   ILE A 827       4.879 -12.379  18.512  1.00 33.46           C  
ANISOU 1943  C   ILE A 827     5190   3264   4261  -1931   1591   -164       C  
ATOM   1944  O   ILE A 827       5.965 -11.856  18.760  1.00 37.92           O  
ANISOU 1944  O   ILE A 827     5804   3793   4811  -1609   1480    -17       O  
ATOM   1945  CB  ILE A 827       2.873 -11.939  19.983  1.00 47.50           C  
ANISOU 1945  CB  ILE A 827     6627   5451   5971  -2230   1717   -257       C  
ATOM   1946  CG1 ILE A 827       1.485 -11.297  20.053  1.00 43.04           C  
ANISOU 1946  CG1 ILE A 827     5680   5275   5400  -2394   1689   -442       C  
ATOM   1947  CG2 ILE A 827       3.739 -11.484  21.152  1.00 41.66           C  
ANISOU 1947  CG2 ILE A 827     6010   4653   5167  -1977   1726    -27       C  
ATOM   1948  CD1 ILE A 827       1.535  -9.755  20.009  1.00 38.53           C  
ANISOU 1948  CD1 ILE A 827     4804   5001   4835  -2148   1499   -458       C  
ATOM   1949  N   ASN A 828       4.780 -13.649  18.151  1.00 36.33           N  
ANISOU 1949  N   ASN A 828     5774   3397   4631  -2067   1707   -213       N  
ATOM   1950  CA  ASN A 828       5.915 -14.555  18.095  1.00 44.07           C  
ANISOU 1950  CA  ASN A 828     7094   4041   5610  -1871   1758    -78       C  
ATOM   1951  C   ASN A 828       5.970 -15.194  16.721  1.00 47.35           C  
ANISOU 1951  C   ASN A 828     7573   4351   6066  -1962   1750   -248       C  
ATOM   1952  O   ASN A 828       4.939 -15.372  16.069  1.00 58.10           O  
ANISOU 1952  O   ASN A 828     8788   5855   7431  -2237   1761   -464       O  
ATOM   1953  CB  ASN A 828       5.799 -15.666  19.172  1.00 41.06           C  
ANISOU 1953  CB  ASN A 828     6968   3459   5172  -1895   1936     46       C  
ATOM   1954  CG  ASN A 828       5.832 -15.115  20.582  1.00 43.65           C  
ANISOU 1954  CG  ASN A 828     7264   3893   5428  -1784   1948    227       C  
ATOM   1955  OD1 ASN A 828       6.696 -14.309  20.922  1.00 53.23           O  
ANISOU 1955  OD1 ASN A 828     8444   5168   6615  -1529   1844    364       O  
ATOM   1956  ND2 ASN A 828       4.893 -15.550  21.411  1.00 55.16           N  
ANISOU 1956  ND2 ASN A 828     8733   5387   6840  -1982   2083    220       N  
ATOM   1957  N   ASP A 829       7.187 -15.522  16.280  1.00 46.50           N  
ANISOU 1957  N   ASP A 829     7664   4032   5973  -1716   1725   -162       N  
ATOM   1958  CA  ASP A 829       7.403 -16.448  15.166  1.00 40.74           C  
ANISOU 1958  CA  ASP A 829     7082   3136   5261  -1766   1771   -290       C  
ATOM   1959  C   ASP A 829       6.897 -15.898  13.832  1.00 46.34           C  
ANISOU 1959  C   ASP A 829     7571   4049   5986  -1934   1656   -523       C  
ATOM   1960  O   ASP A 829       6.328 -16.634  13.023  1.00 50.36           O  
ANISOU 1960  O   ASP A 829     8105   4547   6481  -2150   1715   -712       O  
ATOM   1961  CB  ASP A 829       6.767 -17.812  15.452  1.00 50.35           C  
ANISOU 1961  CB  ASP A 829     8503   4173   6455  -1972   1973   -341       C  
ATOM   1962  CG  ASP A 829       7.470 -18.564  16.561  1.00 64.34           C  
ANISOU 1962  CG  ASP A 829    10557   5692   8196  -1761   2092   -109       C  
ATOM   1963  OD1 ASP A 829       8.711 -18.462  16.656  1.00 67.82           O  
ANISOU 1963  OD1 ASP A 829    11096   6038   8633  -1425   2029     49       O  
ATOM   1964  OD2 ASP A 829       6.780 -19.261  17.337  1.00 70.89           O  
ANISOU 1964  OD2 ASP A 829    11502   6438   8994  -1926   2248    -88       O  
ATOM   1965  N   LEU A 830       7.109 -14.608  13.592  1.00 46.11           N  
ANISOU 1965  N   LEU A 830     7330   4216   5973  -1835   1493   -515       N  
ATOM   1966  CA  LEU A 830       6.935 -14.058  12.253  1.00 40.70           C  
ANISOU 1966  CA  LEU A 830     6477   3705   5284  -1909   1360   -706       C  
ATOM   1967  C   LEU A 830       8.028 -14.624  11.350  1.00 50.25           C  
ANISOU 1967  C   LEU A 830     7903   4697   6493  -1738   1371   -709       C  
ATOM   1968  O   LEU A 830       9.214 -14.348  11.554  1.00 47.20           O  
ANISOU 1968  O   LEU A 830     7618   4187   6129  -1440   1343   -545       O  
ATOM   1969  CB  LEU A 830       6.987 -12.532  12.301  1.00 33.83           C  
ANISOU 1969  CB  LEU A 830     5291   3175   4389  -1676   1134   -639       C  
ATOM   1970  CG  LEU A 830       7.076 -11.806  10.956  1.00 31.45           C  
ANISOU 1970  CG  LEU A 830     4819   3090   4042  -1587    951   -750       C  
ATOM   1971  CD1 LEU A 830       5.859 -12.145  10.077  1.00 42.73           C  
ANISOU 1971  CD1 LEU A 830     6102   4719   5414  -1898    935  -1008       C  
ATOM   1972  CD2 LEU A 830       7.219 -10.313  11.163  1.00 36.41           C  
ANISOU 1972  CD2 LEU A 830     5211   3966   4657  -1336    774   -643       C  
ATOM   1973  N   ASP A 831       7.638 -15.429  10.357  1.00 49.29           N  
ANISOU 1973  N   ASP A 831     7829   4562   6337  -1915   1415   -900       N  
ATOM   1974  CA  ASP A 831       8.580 -16.068   9.438  1.00 46.56           C  
ANISOU 1974  CA  ASP A 831     7679   4031   5983  -1777   1448   -929       C  
ATOM   1975  C   ASP A 831       8.611 -15.264   8.143  1.00 45.63           C  
ANISOU 1975  C   ASP A 831     7400   4125   5811  -1788   1290  -1092       C  
ATOM   1976  O   ASP A 831       7.645 -15.271   7.375  1.00 54.04           O  
ANISOU 1976  O   ASP A 831     8311   5414   6809  -2034   1235  -1306       O  
ATOM   1977  CB  ASP A 831       8.177 -17.519   9.185  1.00 52.25           C  
ANISOU 1977  CB  ASP A 831     8586   4580   6688  -1966   1621  -1038       C  
ATOM   1978  CG  ASP A 831       9.130 -18.256   8.244  1.00 56.19           C  
ANISOU 1978  CG  ASP A 831     9288   4884   7179  -1829   1677  -1077       C  
ATOM   1979  OD1 ASP A 831      10.233 -17.756   7.952  1.00 66.56           O  
ANISOU 1979  OD1 ASP A 831    10617   6172   8501  -1548   1599   -985       O  
ATOM   1980  OD2 ASP A 831       8.760 -19.355   7.794  1.00 62.31           O  
ANISOU 1980  OD2 ASP A 831    10202   5536   7936  -2012   1811  -1211       O  
ATOM   1981  N   MET A 832       9.712 -14.569   7.902  1.00 49.00           N  
ANISOU 1981  N   MET A 832     7845   4529   6244  -1504   1209   -986       N  
ATOM   1982  CA  MET A 832       9.815 -13.716   6.732  1.00 47.76           C  
ANISOU 1982  CA  MET A 832     7500   4650   5996  -1420   1035  -1067       C  
ATOM   1983  C   MET A 832      10.386 -14.446   5.522  1.00 53.31           C  
ANISOU 1983  C   MET A 832     8393   5214   6650  -1433   1105  -1220       C  
ATOM   1984  O   MET A 832      10.541 -13.833   4.460  1.00 50.38           O  
ANISOU 1984  O   MET A 832     7905   5061   6177  -1364    981  -1287       O  
ATOM   1985  CB  MET A 832      10.674 -12.490   7.053  1.00 41.13           C  
ANISOU 1985  CB  MET A 832     6523   3935   5169  -1091    905   -855       C  
ATOM   1986  CG  MET A 832      10.046 -11.499   8.050  1.00 41.26           C  
ANISOU 1986  CG  MET A 832     6312   4155   5209  -1066    805   -741       C  
ATOM   1987  SD  MET A 832       8.647 -10.634   7.321  1.00 43.97           S  
ANISOU 1987  SD  MET A 832     6347   4907   5452  -1212    633   -889       S  
ATOM   1988  CE  MET A 832       9.502  -9.580   6.144  1.00 47.23           C  
ANISOU 1988  CE  MET A 832     6708   5458   5780   -955    494   -834       C  
ATOM   1989  N   SER A 833      10.683 -15.739   5.654  1.00 53.43           N  
ANISOU 1989  N   SER A 833     8641   4950   6712  -1456   1277  -1219       N  
ATOM   1990  CA  SER A 833      11.483 -16.425   4.644  1.00 53.33           C  
ANISOU 1990  CA  SER A 833     8781   4819   6665  -1358   1340  -1291       C  
ATOM   1991  C   SER A 833      10.772 -16.497   3.299  1.00 55.99           C  
ANISOU 1991  C   SER A 833     9034   5360   6879  -1588   1280  -1554       C  
ATOM   1992  O   SER A 833      11.430 -16.465   2.252  1.00 60.74           O  
ANISOU 1992  O   SER A 833     9681   5991   7408  -1483   1262  -1629       O  
ATOM   1993  CB  SER A 833      11.850 -17.824   5.139  1.00 42.78           C  
ANISOU 1993  CB  SER A 833     7687   3172   5396  -1318   1529  -1217       C  
ATOM   1994  OG  SER A 833      10.689 -18.518   5.548  1.00 56.54           O  
ANISOU 1994  OG  SER A 833     9450   4887   7145  -1614   1616  -1299       O  
ATOM   1995  N   GLU A 834       9.439 -16.576   3.298  1.00 46.99           N  
ANISOU 1995  N   GLU A 834     7748   4406   5699  -1890   1242  -1699       N  
ATOM   1996  CA  GLU A 834       8.702 -16.639   2.039  1.00 54.90           C  
ANISOU 1996  CA  GLU A 834     8626   5674   6560  -2098   1159  -1950       C  
ATOM   1997  C   GLU A 834       8.776 -15.343   1.240  1.00 52.38           C  
ANISOU 1997  C   GLU A 834     8119   5688   6095  -1989    949  -1992       C  
ATOM   1998  O   GLU A 834       8.491 -15.361   0.036  1.00 62.49           O  
ANISOU 1998  O   GLU A 834     9330   7193   7221  -2067    868  -2167       O  
ATOM   1999  CB  GLU A 834       7.236 -16.988   2.299  1.00 65.89           C  
ANISOU 1999  CB  GLU A 834     9851   7247   7937  -2427   1162  -2088       C  
ATOM   2000  CG  GLU A 834       6.564 -16.070   3.307  1.00 70.17           C  
ANISOU 2000  CG  GLU A 834    10172   7975   8515  -2446   1066  -1991       C  
ATOM   2001  CD  GLU A 834       5.061 -16.247   3.351  1.00 76.51           C  
ANISOU 2001  CD  GLU A 834    10730   9071   9269  -2751   1041  -2157       C  
ATOM   2002  OE1 GLU A 834       4.430 -16.272   2.271  1.00 79.40           O  
ANISOU 2002  OE1 GLU A 834    10936   9731   9501  -2884    943  -2362       O  
ATOM   2003  OE2 GLU A 834       4.514 -16.366   4.467  1.00 73.55           O  
ANISOU 2003  OE2 GLU A 834    10316   8652   8977  -2845   1123  -2081       O  
ATOM   2004  N   PHE A 835       9.149 -14.226   1.868  1.00 55.79           N  
ANISOU 2004  N   PHE A 835     8466   6176   6556  -1789    858  -1815       N  
ATOM   2005  CA  PHE A 835       9.216 -12.941   1.182  1.00 56.21           C  
ANISOU 2005  CA  PHE A 835     8301   6577   6478  -1588    652  -1729       C  
ATOM   2006  C   PHE A 835      10.616 -12.580   0.708  1.00 52.88           C  
ANISOU 2006  C   PHE A 835     8004   6045   6045  -1296    677  -1591       C  
ATOM   2007  O   PHE A 835      10.767 -11.613  -0.041  1.00 68.51           O  
ANISOU 2007  O   PHE A 835     9864   8272   7895  -1150    545  -1532       O  
ATOM   2008  CB  PHE A 835       8.702 -11.815   2.095  1.00 42.79           C  
ANISOU 2008  CB  PHE A 835     6355   5072   4831  -1476    520  -1538       C  
ATOM   2009  CG  PHE A 835       7.291 -12.010   2.563  1.00 49.84           C  
ANISOU 2009  CG  PHE A 835     7065   6148   5725  -1740    486  -1669       C  
ATOM   2010  CD1 PHE A 835       6.225 -11.902   1.674  1.00 48.36           C  
ANISOU 2010  CD1 PHE A 835     6671   6336   5369  -1909    353  -1880       C  
ATOM   2011  CD2 PHE A 835       7.027 -12.298   3.893  1.00 51.45           C  
ANISOU 2011  CD2 PHE A 835     7285   6183   6081  -1819    590  -1585       C  
ATOM   2012  CE1 PHE A 835       4.914 -12.092   2.109  1.00 47.70           C  
ANISOU 2012  CE1 PHE A 835     6371   6469   5285  -2168    328  -2025       C  
ATOM   2013  CE2 PHE A 835       5.726 -12.489   4.332  1.00 57.66           C  
ANISOU 2013  CE2 PHE A 835     7887   7154   6866  -2086    585  -1716       C  
ATOM   2014  CZ  PHE A 835       4.666 -12.386   3.437  1.00 53.37           C  
ANISOU 2014  CZ  PHE A 835     7109   7000   6171  -2267    456  -1946       C  
ATOM   2015  N   LEU A 836      11.637 -13.294   1.155  1.00 46.98           N  
ANISOU 2015  N   LEU A 836     7483   4945   5422  -1193    849  -1527       N  
ATOM   2016  CA  LEU A 836      13.011 -12.986   0.790  1.00 41.28           C  
ANISOU 2016  CA  LEU A 836     6840   4143   4699   -918    889  -1409       C  
ATOM   2017  C   LEU A 836      13.343 -13.643  -0.540  1.00 39.85           C  
ANISOU 2017  C   LEU A 836     6811   3944   4387   -972    964  -1618       C  
ATOM   2018  O   LEU A 836      12.928 -14.774  -0.802  1.00 51.99           O  
ANISOU 2018  O   LEU A 836     8483   5344   5928  -1168   1062  -1806       O  
ATOM   2019  CB  LEU A 836      13.971 -13.485   1.870  1.00 46.64           C  
ANISOU 2019  CB  LEU A 836     7666   4503   5553   -745   1029  -1254       C  
ATOM   2020  CG  LEU A 836      14.064 -12.657   3.140  1.00 48.49           C  
ANISOU 2020  CG  LEU A 836     7752   4781   5890   -611    955  -1020       C  
ATOM   2021  CD1 LEU A 836      14.796 -13.441   4.187  1.00 56.73           C  
ANISOU 2021  CD1 LEU A 836     8965   5523   7066   -480   1096   -907       C  
ATOM   2022  CD2 LEU A 836      14.803 -11.365   2.839  1.00 54.26           C  
ANISOU 2022  CD2 LEU A 836     8323   5713   6580   -405    852   -884       C  
ATOM   2023  N   ILE A 837      14.079 -12.929  -1.393  1.00 39.30           N  
ANISOU 2023  N   ILE A 837     6698   4030   4205   -798    919  -1565       N  
ATOM   2024  CA  ILE A 837      14.507 -13.532  -2.657  1.00 48.67           C  
ANISOU 2024  CA  ILE A 837     8035   5207   5250   -825   1007  -1761       C  
ATOM   2025  C   ILE A 837      15.967 -13.963  -2.627  1.00 43.46           C  
ANISOU 2025  C   ILE A 837     7527   4305   4681   -593   1180  -1696       C  
ATOM   2026  O   ILE A 837      16.420 -14.643  -3.560  1.00 56.68           O  
ANISOU 2026  O   ILE A 837     9286   5953   6296   -577   1255  -1810       O  
ATOM   2027  CB  ILE A 837      14.251 -12.598  -3.860  1.00 54.74           C  
ANISOU 2027  CB  ILE A 837     8674   6348   5775   -815    861  -1784       C  
ATOM   2028  CG1 ILE A 837      15.117 -11.338  -3.781  1.00 49.14           C  
ANISOU 2028  CG1 ILE A 837     7863   5737   5072   -559    818  -1521       C  
ATOM   2029  CG2 ILE A 837      12.777 -12.245  -3.947  1.00 57.25           C  
ANISOU 2029  CG2 ILE A 837     8813   6955   5984  -1008    676  -1862       C  
ATOM   2030  CD1 ILE A 837      15.143 -10.558  -5.085  1.00 44.03           C  
ANISOU 2030  CD1 ILE A 837     7179   5383   4169   -513    740  -1523       C  
ATOM   2031  N   ASN A 838      16.708 -13.589  -1.601  1.00 43.13           N  
ANISOU 2031  N   ASN A 838     7438   4154   4796   -389   1202  -1477       N  
ATOM   2032  CA  ASN A 838      18.067 -14.037  -1.363  1.00 38.67           C  
ANISOU 2032  CA  ASN A 838     6947   3409   4338   -142   1338  -1390       C  
ATOM   2033  C   ASN A 838      18.055 -15.480  -0.869  1.00 45.57           C  
ANISOU 2033  C   ASN A 838     7959   4012   5344   -159   1435  -1405       C  
ATOM   2034  O   ASN A 838      17.541 -15.745   0.228  1.00 47.87           O  
ANISOU 2034  O   ASN A 838     8267   4178   5744   -212   1426  -1314       O  
ATOM   2035  CB  ASN A 838      18.700 -13.088  -0.346  1.00 40.03           C  
ANISOU 2035  CB  ASN A 838     6967   3631   4613     50   1289  -1155       C  
ATOM   2036  CG  ASN A 838      20.092 -13.491   0.083  1.00 37.57           C  
ANISOU 2036  CG  ASN A 838     6673   3196   4407    320   1404  -1061       C  
ATOM   2037  OD1 ASN A 838      20.682 -14.434  -0.426  1.00 42.82           O  
ANISOU 2037  OD1 ASN A 838     7424   3768   5077    393   1496  -1128       O  
ATOM   2038  ND2 ASN A 838      20.629 -12.746   1.042  1.00 39.35           N  
ANISOU 2038  ND2 ASN A 838     6752   3482   4716    469   1359   -883       N  
ATOM   2039  N   PRO A 839      18.573 -16.442  -1.638  1.00 47.74           N  
ANISOU 2039  N   PRO A 839     8352   4187   5599   -120   1540  -1513       N  
ATOM   2040  CA  PRO A 839      18.566 -17.837  -1.171  1.00 47.69           C  
ANISOU 2040  CA  PRO A 839     8517   3898   5705   -125   1654  -1518       C  
ATOM   2041  C   PRO A 839      19.559 -18.115  -0.055  1.00 54.67           C  
ANISOU 2041  C   PRO A 839     9415   4632   6724    160   1708  -1303       C  
ATOM   2042  O   PRO A 839      19.503 -19.199   0.538  1.00 62.37           O  
ANISOU 2042  O   PRO A 839    10549   5371   7779    175   1801  -1261       O  
ATOM   2043  CB  PRO A 839      18.906 -18.632  -2.433  1.00 46.51           C  
ANISOU 2043  CB  PRO A 839     8484   3712   5478   -143   1747  -1712       C  
ATOM   2044  CG  PRO A 839      19.640 -17.692  -3.302  1.00 46.26           C  
ANISOU 2044  CG  PRO A 839     8327   3920   5328    -17   1709  -1730       C  
ATOM   2045  CD  PRO A 839      19.104 -16.307  -3.003  1.00 40.79           C  
ANISOU 2045  CD  PRO A 839     7470   3452   4576    -84   1568  -1645       C  
ATOM   2046  N   ASN A 840      20.449 -17.177   0.258  1.00 60.61           N  
ANISOU 2046  N   ASN A 840    10007   5533   7489    380   1656  -1166       N  
ATOM   2047  CA  ASN A 840      21.442 -17.354   1.307  1.00 61.95           C  
ANISOU 2047  CA  ASN A 840    10140   5639   7759    662   1678   -974       C  
ATOM   2048  C   ASN A 840      21.095 -16.593   2.574  1.00 65.63           C  
ANISOU 2048  C   ASN A 840    10493   6165   8278    669   1579   -802       C  
ATOM   2049  O   ASN A 840      21.927 -16.509   3.482  1.00 78.55           O  
ANISOU 2049  O   ASN A 840    12052   7825   9969    903   1564   -641       O  
ATOM   2050  CB  ASN A 840      22.817 -16.932   0.799  1.00 58.37           C  
ANISOU 2050  CB  ASN A 840     9552   5342   7283    909   1702   -963       C  
ATOM   2051  CG  ASN A 840      23.214 -17.686  -0.441  1.00 56.70           C  
ANISOU 2051  CG  ASN A 840     9447   5082   7015    920   1809  -1137       C  
ATOM   2052  OD1 ASN A 840      23.069 -18.905  -0.503  1.00 68.60           O  
ANISOU 2052  OD1 ASN A 840    11149   6362   8556    909   1899  -1197       O  
ATOM   2053  ND2 ASN A 840      23.691 -16.965  -1.452  1.00 57.54           N  
ANISOU 2053  ND2 ASN A 840     9441   5397   7024    930   1813  -1224       N  
ATOM   2054  N   ALA A 841      19.897 -16.024   2.649  1.00 56.87           N  
ANISOU 2054  N   ALA A 841     9359   5106   7141    422   1504   -844       N  
ATOM   2055  CA  ALA A 841      19.417 -15.509   3.914  1.00 52.91           C  
ANISOU 2055  CA  ALA A 841     8785   4620   6696    405   1429   -697       C  
ATOM   2056  C   ALA A 841      19.217 -16.671   4.882  1.00 56.53           C  
ANISOU 2056  C   ALA A 841     9401   4862   7218    420   1503   -606       C  
ATOM   2057  O   ALA A 841      19.041 -17.824   4.478  1.00 71.93           O  
ANISOU 2057  O   ALA A 841    11535   6630   9166    348   1612   -693       O  
ATOM   2058  CB  ALA A 841      18.119 -14.724   3.720  1.00 48.39           C  
ANISOU 2058  CB  ALA A 841     8155   4152   6077    133   1342   -787       C  
ATOM   2059  N   GLY A 842      19.271 -16.362   6.173  1.00 68.28           N  
ANISOU 2059  N   GLY A 842    10828   6369   8746    518   1455   -429       N  
ATOM   2060  CA  GLY A 842      19.211 -17.381   7.195  1.00 65.25           C  
ANISOU 2060  CA  GLY A 842    10599   5803   8391    576   1532   -310       C  
ATOM   2061  C   GLY A 842      17.799 -17.852   7.471  1.00 71.01           C  
ANISOU 2061  C   GLY A 842    11445   6412   9124    266   1581   -369       C  
ATOM   2062  O   GLY A 842      16.942 -17.882   6.581  1.00 71.38           O  
ANISOU 2062  O   GLY A 842    11505   6466   9148      2   1591   -552       O  
ATOM   2063  N   PRO A 843      17.533 -18.245   8.721  1.00 65.36           N  
ANISOU 2063  N   PRO A 843    10806   5607   8421    289   1617   -222       N  
ATOM   2064  CA  PRO A 843      16.164 -18.665   9.067  1.00 64.19           C  
ANISOU 2064  CA  PRO A 843    10747   5367   8275    -25   1682   -280       C  
ATOM   2065  C   PRO A 843      15.160 -17.523   9.030  1.00 64.43           C  
ANISOU 2065  C   PRO A 843    10580   5597   8304   -255   1566   -355       C  
ATOM   2066  O   PRO A 843      14.010 -17.733   8.620  1.00 74.73           O  
ANISOU 2066  O   PRO A 843    11890   6907   9598   -569   1597   -512       O  
ATOM   2067  CB  PRO A 843      16.325 -19.246  10.481  1.00 62.43           C  
ANISOU 2067  CB  PRO A 843    10649   5026   8047    113   1750    -78       C  
ATOM   2068  CG  PRO A 843      17.564 -18.590  11.023  1.00 66.05           C  
ANISOU 2068  CG  PRO A 843    10976   5627   8494    465   1644     85       C  
ATOM   2069  CD  PRO A 843      18.473 -18.407   9.844  1.00 66.15           C  
ANISOU 2069  CD  PRO A 843    10918   5701   8515    598   1612    -11       C  
ATOM   2070  N   CYS A 844      15.565 -16.324   9.456  1.00 52.94           N  
ANISOU 2070  N   CYS A 844     8940   4319   6855   -107   1437   -254       N  
ATOM   2071  CA  CYS A 844      14.726 -15.120   9.449  1.00 57.81           C  
ANISOU 2071  CA  CYS A 844     9373   5120   7474   -279   1326   -309       C  
ATOM   2072  C   CYS A 844      13.360 -15.336  10.115  1.00 49.11           C  
ANISOU 2072  C   CYS A 844     8273   4009   6376   -566   1366   -339       C  
ATOM   2073  O   CYS A 844      12.307 -15.039   9.546  1.00 57.10           O  
ANISOU 2073  O   CYS A 844     9189   5132   7372   -840   1332   -508       O  
ATOM   2074  CB  CYS A 844      14.565 -14.582   8.028  1.00 65.92           C  
ANISOU 2074  CB  CYS A 844    10321   6260   8467   -385   1265   -500       C  
ATOM   2075  SG  CYS A 844      15.980 -13.572   7.475  1.00 94.04           S  
ANISOU 2075  SG  CYS A 844    13744   9977  12011    -76   1172   -437       S  
ATOM   2076  N   ARG A 845      13.380 -15.837  11.342  1.00 52.13           N  
ANISOU 2076  N   ARG A 845     8748   4296   6762   -500   1436   -182       N  
ATOM   2077  CA  ARG A 845      12.197 -15.827  12.195  1.00 46.12           C  
ANISOU 2077  CA  ARG A 845     7955   3569   5999   -735   1474   -175       C  
ATOM   2078  C   ARG A 845      12.332 -14.690  13.194  1.00 37.38           C  
ANISOU 2078  C   ARG A 845     6699   2611   4895   -614   1377    -26       C  
ATOM   2079  O   ARG A 845      13.429 -14.425  13.689  1.00 39.05           O  
ANISOU 2079  O   ARG A 845     6915   2828   5095   -315   1331    129       O  
ATOM   2080  CB  ARG A 845      12.021 -17.157  12.927  1.00 47.02           C  
ANISOU 2080  CB  ARG A 845     8298   3473   6094   -769   1642   -106       C  
ATOM   2081  CG  ARG A 845      11.839 -18.324  11.995  1.00 64.73           C  
ANISOU 2081  CG  ARG A 845    10711   5546   8337   -910   1765   -260       C  
ATOM   2082  CD  ARG A 845      12.103 -19.656  12.677  1.00 71.92           C  
ANISOU 2082  CD  ARG A 845    11904   6189   9231   -832   1943   -151       C  
ATOM   2083  NE  ARG A 845      10.946 -20.139  13.423  1.00 77.73           N  
ANISOU 2083  NE  ARG A 845    12704   6877   9953  -1104   2065   -169       N  
ATOM   2084  CZ  ARG A 845       9.870 -20.679  12.861  1.00 80.30           C  
ANISOU 2084  CZ  ARG A 845    13045   7184  10280  -1456   2162   -373       C  
ATOM   2085  NH1 ARG A 845       8.865 -21.099  13.616  1.00 84.33           N  
ANISOU 2085  NH1 ARG A 845    13600   7667  10774  -1696   2282   -385       N  
ATOM   2086  NH2 ARG A 845       9.792 -20.790  11.543  1.00 75.94           N  
ANISOU 2086  NH2 ARG A 845    12454   6665   9736  -1574   2139   -574       N  
ATOM   2087  N   TYR A 846      11.211 -14.025  13.489  1.00 35.82           N  
ANISOU 2087  N   TYR A 846     6342   2568   4701   -848   1346    -85       N  
ATOM   2088  CA  TYR A 846      11.207 -12.822  14.308  1.00 34.75           C  
ANISOU 2088  CA  TYR A 846     5961   2701   4542   -726   1207     16       C  
ATOM   2089  C   TYR A 846      10.138 -12.903  15.395  1.00 36.36           C  
ANISOU 2089  C   TYR A 846     6136   2953   4725   -920   1286     46       C  
ATOM   2090  O   TYR A 846       9.069 -13.490  15.199  1.00 35.58           O  
ANISOU 2090  O   TYR A 846     6068   2815   4636  -1226   1392    -81       O  
ATOM   2091  CB  TYR A 846      10.955 -11.569  13.472  1.00 30.86           C  
ANISOU 2091  CB  TYR A 846     5173   2504   4047   -723   1022    -96       C  
ATOM   2092  CG  TYR A 846      12.118 -11.129  12.603  1.00 36.63           C  
ANISOU 2092  CG  TYR A 846     5883   3253   4781   -502    933    -89       C  
ATOM   2093  CD1 TYR A 846      12.384 -11.762  11.400  1.00 40.93           C  
ANISOU 2093  CD1 TYR A 846     6547   3681   5324   -538    975   -200       C  
ATOM   2094  CD2 TYR A 846      12.929 -10.065  12.977  1.00 33.95           C  
ANISOU 2094  CD2 TYR A 846     5401   3059   4439   -284    824     10       C  
ATOM   2095  CE1 TYR A 846      13.437 -11.366  10.595  1.00 35.73           C  
ANISOU 2095  CE1 TYR A 846     5862   3056   4657   -348    915   -198       C  
ATOM   2096  CE2 TYR A 846      13.992  -9.663  12.181  1.00 31.94           C  
ANISOU 2096  CE2 TYR A 846     5118   2832   4187   -119    769      6       C  
ATOM   2097  CZ  TYR A 846      14.235 -10.323  10.983  1.00 37.54           C  
ANISOU 2097  CZ  TYR A 846     5943   3431   4890   -146    818    -90       C  
ATOM   2098  OH  TYR A 846      15.286  -9.936  10.166  1.00 32.62           O  
ANISOU 2098  OH  TYR A 846     5288   2850   4258      7    786    -98       O  
ATOM   2099  N   ASN A 847      10.440 -12.277  16.532  1.00 41.45           N  
ANISOU 2099  N   ASN A 847     6705   3713   5331   -756   1236    195       N  
ATOM   2100  CA  ASN A 847       9.523 -12.116  17.658  1.00 33.09           C  
ANISOU 2100  CA  ASN A 847     5580   2762   4232   -897   1296    233       C  
ATOM   2101  C   ASN A 847       9.350 -10.632  17.945  1.00 28.76           C  
ANISOU 2101  C   ASN A 847     4718   2538   3672   -804   1126    207       C  
ATOM   2102  O   ASN A 847      10.320  -9.870  17.916  1.00 32.18           O  
ANISOU 2102  O   ASN A 847     5078   3048   4103   -565   1000    261       O  
ATOM   2103  CB  ASN A 847      10.038 -12.819  18.919  1.00 30.88           C  
ANISOU 2103  CB  ASN A 847     5548   2304   3879   -774   1423    448       C  
ATOM   2104  CG  ASN A 847      10.060 -14.310  18.784  1.00 36.99           C  
ANISOU 2104  CG  ASN A 847     6617   2781   4657   -836   1584    465       C  
ATOM   2105  OD1 ASN A 847       9.475 -14.865  17.855  1.00 41.65           O  
ANISOU 2105  OD1 ASN A 847     7224   3302   5300  -1047   1633    294       O  
ATOM   2106  ND2 ASN A 847      10.741 -14.984  19.717  1.00 41.76           N  
ANISOU 2106  ND2 ASN A 847     7413   3268   5186   -621   1636    648       N  
ATOM   2107  N   LEU A 848       8.108 -10.223  18.195  1.00 29.23           N  
ANISOU 2107  N   LEU A 848     4593   2786   3728  -1001   1136    109       N  
ATOM   2108  CA  LEU A 848       7.811  -8.825  18.473  1.00 29.61           C  
ANISOU 2108  CA  LEU A 848     4364   3115   3770   -907   1001     72       C  
ATOM   2109  C   LEU A 848       8.484  -8.381  19.770  1.00 30.28           C  
ANISOU 2109  C   LEU A 848     4478   3235   3791   -723    993    215       C  
ATOM   2110  O   LEU A 848       8.474  -9.110  20.766  1.00 31.74           O  
ANISOU 2110  O   LEU A 848     4827   3327   3908   -759   1120    327       O  
ATOM   2111  CB  LEU A 848       6.288  -8.648  18.586  1.00 31.27           C  
ANISOU 2111  CB  LEU A 848     4374   3527   3980  -1141   1044    -63       C  
ATOM   2112  CG  LEU A 848       5.729  -7.235  18.680  1.00 35.49           C  
ANISOU 2112  CG  LEU A 848     4614   4351   4519  -1045    918   -135       C  
ATOM   2113  CD1 LEU A 848       5.829  -6.537  17.336  1.00 26.70           C  
ANISOU 2113  CD1 LEU A 848     3378   3321   3446   -944    760   -220       C  
ATOM   2114  CD2 LEU A 848       4.286  -7.271  19.200  1.00 33.89           C  
ANISOU 2114  CD2 LEU A 848     4228   4352   4295  -1258   1008   -239       C  
ATOM   2115  N   ILE A 849       9.034  -7.165  19.780  1.00 26.49           N  
ANISOU 2115  N   ILE A 849     3848   2898   3321   -538    852    206       N  
ATOM   2116  CA  ILE A 849       9.598  -6.618  21.009  1.00 30.38           C  
ANISOU 2116  CA  ILE A 849     4327   3478   3738   -393    831    292       C  
ATOM   2117  C   ILE A 849       9.008  -5.268  21.388  1.00 25.06           C  
ANISOU 2117  C   ILE A 849     3428   3025   3070   -377    767    196       C  
ATOM   2118  O   ILE A 849       9.067  -4.896  22.581  1.00 30.70           O  
ANISOU 2118  O   ILE A 849     4121   3841   3701   -330    788    229       O  
ATOM   2119  CB  ILE A 849      11.142  -6.529  20.951  1.00 35.29           C  
ANISOU 2119  CB  ILE A 849     5021   4043   4344   -171    752    374       C  
ATOM   2120  CG1 ILE A 849      11.607  -5.601  19.822  1.00 30.59           C  
ANISOU 2120  CG1 ILE A 849     4300   3487   3835   -101    633    282       C  
ATOM   2121  CG2 ILE A 849      11.761  -7.931  20.857  1.00 31.83           C  
ANISOU 2121  CG2 ILE A 849     4831   3383   3880   -125    838    495       C  
ATOM   2122  CD1 ILE A 849      13.137  -5.276  19.836  1.00 22.54           C  
ANISOU 2122  CD1 ILE A 849     3284   2479   2802     91    559    328       C  
ATOM   2123  N   ALA A 850       8.415  -4.532  20.449  1.00 24.96           N  
ANISOU 2123  N   ALA A 850     3259   3092   3135   -398    696     80       N  
ATOM   2124  CA  ALA A 850       7.822  -3.251  20.840  1.00 23.10           C  
ANISOU 2124  CA  ALA A 850     2836   3034   2906   -344    655     -4       C  
ATOM   2125  C   ALA A 850       6.843  -2.812  19.767  1.00 28.98           C  
ANISOU 2125  C   ALA A 850     3425   3872   3714   -378    603   -111       C  
ATOM   2126  O   ALA A 850       6.909  -3.262  18.618  1.00 26.30           O  
ANISOU 2126  O   ALA A 850     3119   3467   3405   -415    564   -125       O  
ATOM   2127  CB  ALA A 850       8.873  -2.160  21.080  1.00 22.06           C  
ANISOU 2127  CB  ALA A 850     2696   2907   2780   -171    574      1       C  
ATOM   2128  N   VAL A 851       5.896  -1.977  20.182  1.00 25.92           N  
ANISOU 2128  N   VAL A 851     2863   3660   3326   -353    607   -191       N  
ATOM   2129  CA  VAL A 851       4.848  -1.442  19.315  1.00 24.04           C  
ANISOU 2129  CA  VAL A 851     2436   3574   3122   -330    547   -290       C  
ATOM   2130  C   VAL A 851       4.627   0.012  19.706  1.00 31.21           C  
ANISOU 2130  C   VAL A 851     3238   4572   4050   -138    515   -333       C  
ATOM   2131  O   VAL A 851       4.310   0.304  20.862  1.00 29.01           O  
ANISOU 2131  O   VAL A 851     2910   4372   3739   -138    591   -363       O  
ATOM   2132  CB  VAL A 851       3.520  -2.210  19.442  1.00 27.46           C  
ANISOU 2132  CB  VAL A 851     2726   4179   3530   -534    626   -376       C  
ATOM   2133  CG1 VAL A 851       2.434  -1.529  18.626  1.00 29.11           C  
ANISOU 2133  CG1 VAL A 851     2686   4621   3752   -461    541   -488       C  
ATOM   2134  CG2 VAL A 851       3.670  -3.667  19.047  1.00 31.78           C  
ANISOU 2134  CG2 VAL A 851     3414   4595   4065   -755    691   -355       C  
ATOM   2135  N   SER A 852       4.801   0.919  18.762  1.00 26.44           N  
ANISOU 2135  N   SER A 852     2620   3939   3487     29    421   -335       N  
ATOM   2136  CA  SER A 852       4.352   2.292  18.919  1.00 26.09           C  
ANISOU 2136  CA  SER A 852     2486   3959   3469    228    405   -382       C  
ATOM   2137  C   SER A 852       2.898   2.387  18.481  1.00 28.53           C  
ANISOU 2137  C   SER A 852     2562   4516   3763    272    376   -462       C  
ATOM   2138  O   SER A 852       2.550   1.948  17.375  1.00 30.84           O  
ANISOU 2138  O   SER A 852     2794   4886   4036    244    298   -465       O  
ATOM   2139  CB  SER A 852       5.224   3.230  18.078  1.00 33.06           C  
ANISOU 2139  CB  SER A 852     3500   4669   4394    392    341   -326       C  
ATOM   2140  OG  SER A 852       4.759   4.562  18.137  1.00 34.68           O  
ANISOU 2140  OG  SER A 852     3663   4885   4628    602    345   -362       O  
ATOM   2141  N   ASN A 853       2.062   2.975  19.344  1.00 26.85           N  
ANISOU 2141  N   ASN A 853     2202   4453   3546    347    438   -540       N  
ATOM   2142  CA  ASN A 853       0.638   3.175  19.106  1.00 31.47           C  
ANISOU 2142  CA  ASN A 853     2514   5330   4113    423    420   -635       C  
ATOM   2143  C   ASN A 853       0.339   4.641  18.869  1.00 32.79           C  
ANISOU 2143  C   ASN A 853     2644   5504   4310    762    380   -643       C  
ATOM   2144  O   ASN A 853       0.944   5.519  19.489  1.00 35.92           O  
ANISOU 2144  O   ASN A 853     3192   5711   4746    879    437   -630       O  
ATOM   2145  CB  ASN A 853      -0.219   2.741  20.308  1.00 34.27           C  
ANISOU 2145  CB  ASN A 853     2702   5885   4434    273    550   -731       C  
ATOM   2146  CG  ASN A 853       0.188   1.418  20.862  1.00 36.87           C  
ANISOU 2146  CG  ASN A 853     3146   6134   4727    -39    640   -695       C  
ATOM   2147  OD1 ASN A 853       0.044   0.387  20.200  1.00 34.10           O  
ANISOU 2147  OD1 ASN A 853     2787   5805   4365   -233    623   -695       O  
ATOM   2148  ND2 ASN A 853       0.701   1.425  22.093  1.00 37.54           N  
ANISOU 2148  ND2 ASN A 853     3357   6124   4782    -84    743   -665       N  
ATOM   2149  N   HIS A 854      -0.669   4.890  18.039  1.00 34.48           N  
ANISOU 2149  N   HIS A 854     2649   5956   4497    919    293   -679       N  
ATOM   2150  CA  HIS A 854      -1.213   6.223  17.852  1.00 31.95           C  
ANISOU 2150  CA  HIS A 854     2266   5682   4190   1289    267   -683       C  
ATOM   2151  C   HIS A 854      -2.727   6.169  17.983  1.00 40.99           C  
ANISOU 2151  C   HIS A 854     3043   7241   5291   1368    259   -807       C  
ATOM   2152  O   HIS A 854      -3.376   5.292  17.406  1.00 42.19           O  
ANISOU 2152  O   HIS A 854     3001   7647   5383   1201    187   -856       O  
ATOM   2153  CB  HIS A 854      -0.832   6.816  16.493  1.00 42.65           C  
ANISOU 2153  CB  HIS A 854     3758   6917   5529   1515    143   -561       C  
ATOM   2154  CG  HIS A 854      -1.443   8.158  16.249  1.00 42.90           C  
ANISOU 2154  CG  HIS A 854     3759   6978   5563   1933    126   -537       C  
ATOM   2155  ND1 HIS A 854      -2.621   8.320  15.555  1.00 47.94           N  
ANISOU 2155  ND1 HIS A 854     4209   7883   6121   2078     16   -538       N  
ATOM   2156  CD2 HIS A 854      -1.068   9.395  16.648  1.00 45.15           C  
ANISOU 2156  CD2 HIS A 854     4273   6968   5915   2134    212   -492       C  
ATOM   2157  CE1 HIS A 854      -2.933   9.603  15.517  1.00 47.87           C  
ANISOU 2157  CE1 HIS A 854     4321   7739   6129   2376     34   -474       C  
ATOM   2158  NE2 HIS A 854      -2.007  10.279  16.171  1.00 47.98           N  
ANISOU 2158  NE2 HIS A 854     4595   7394   6241   2400    160   -448       N  
ATOM   2159  N   TYR A 855      -3.279   7.112  18.746  1.00 42.29           N  
ANISOU 2159  N   TYR A 855     3205   7384   5480   1544    330   -839       N  
ATOM   2160  CA  TYR A 855      -4.702   7.206  19.021  1.00 45.45           C  
ANISOU 2160  CA  TYR A 855     3357   8073   5838   1582    330   -926       C  
ATOM   2161  C   TYR A 855      -5.220   8.553  18.545  1.00 49.65           C  
ANISOU 2161  C   TYR A 855     3928   8562   6375   1977    272   -869       C  
ATOM   2162  O   TYR A 855      -4.522   9.571  18.652  1.00 51.87           O  
ANISOU 2162  O   TYR A 855     4462   8525   6721   2177    319   -796       O  
ATOM   2163  CB  TYR A 855      -5.012   7.058  20.533  1.00 46.48           C  
ANISOU 2163  CB  TYR A 855     3433   8244   5982   1425    499  -1027       C  
ATOM   2164  CG  TYR A 855      -4.512   5.780  21.156  1.00 43.63           C  
ANISOU 2164  CG  TYR A 855     3084   7892   5602   1038    589  -1059       C  
ATOM   2165  CD1 TYR A 855      -5.305   4.638  21.176  1.00 42.39           C  
ANISOU 2165  CD1 TYR A 855     2730   7986   5389    747    606  -1130       C  
ATOM   2166  CD2 TYR A 855      -3.238   5.708  21.708  1.00 44.99           C  
ANISOU 2166  CD2 TYR A 855     3484   7809   5802    956    667  -1017       C  
ATOM   2167  CE1 TYR A 855      -4.846   3.460  21.734  1.00 40.30           C  
ANISOU 2167  CE1 TYR A 855     2533   7676   5105    390    713  -1132       C  
ATOM   2168  CE2 TYR A 855      -2.769   4.534  22.269  1.00 39.43           C  
ANISOU 2168  CE2 TYR A 855     2817   7102   5063    622    757  -1020       C  
ATOM   2169  CZ  TYR A 855      -3.577   3.417  22.284  1.00 43.81           C  
ANISOU 2169  CZ  TYR A 855     3212   7865   5570    343    787  -1063       C  
ATOM   2170  OH  TYR A 855      -3.114   2.253  22.851  1.00 54.55           O  
ANISOU 2170  OH  TYR A 855     4670   9163   6892     13    901  -1036       O  
ATOM   2171  N   GLY A 856      -6.438   8.533  18.003  1.00 49.26           N  
ANISOU 2171  N   GLY A 856     3638   8830   6249   2071    178   -909       N  
ATOM   2172  CA  GLY A 856      -7.264   9.710  17.813  1.00 68.82           C  
ANISOU 2172  CA  GLY A 856     6081  11354   8713   2434    149   -885       C  
ATOM   2173  C   GLY A 856      -6.657  10.870  17.053  1.00 72.67           C  
ANISOU 2173  C   GLY A 856     6853  11533   9224   2760    105   -726       C  
ATOM   2174  O   GLY A 856      -6.819  12.026  17.455  1.00 81.87           O  
ANISOU 2174  O   GLY A 856     8138  12521  10447   3014    183   -704       O  
ATOM   2175  N   GLY A 857      -5.981  10.588  15.947  1.00 71.99           N  
ANISOU 2175  N   GLY A 857     6891  11370   9091   2748     -5   -617       N  
ATOM   2176  CA  GLY A 857      -5.380  11.647  15.156  1.00 80.20           C  
ANISOU 2176  CA  GLY A 857     8232  12105  10136   3024    -31   -449       C  
ATOM   2177  C   GLY A 857      -6.315  12.274  14.145  1.00 88.69           C  
ANISOU 2177  C   GLY A 857     9235  13371  11091   3342   -154   -373       C  
ATOM   2178  O   GLY A 857      -5.989  12.356  12.962  1.00 92.94           O  
ANISOU 2178  O   GLY A 857     9899  13877  11537   3443   -258   -244       O  
ATOM   2179  N   GLY A 860      -6.607  15.456  18.364  1.00 80.48           N  
ANISOU 2179  N   GLY A 860     8513  11581  10482   3678    454   -627       N  
ATOM   2180  CA  GLY A 860      -6.257  14.881  19.649  1.00 76.85           C  
ANISOU 2180  CA  GLY A 860     8001  11117  10082   3388    583   -774       C  
ATOM   2181  C   GLY A 860      -5.405  13.633  19.531  1.00 80.65           C  
ANISOU 2181  C   GLY A 860     8471  11639  10532   3049    534   -768       C  
ATOM   2182  O   GLY A 860      -5.654  12.637  20.212  1.00 91.79           O  
ANISOU 2182  O   GLY A 860     9675  13289  11910   2795    560   -872       O  
ATOM   2183  N   GLY A 861      -4.396  13.688  18.662  1.00 73.14           N  
ANISOU 2183  N   GLY A 861     7756  10448   9587   3040    476   -641       N  
ATOM   2184  CA  GLY A 861      -3.536  12.534  18.442  1.00 61.68           C  
ANISOU 2184  CA  GLY A 861     6306   9021   8108   2754    427   -626       C  
ATOM   2185  C   GLY A 861      -2.545  12.346  19.582  1.00 64.40           C  
ANISOU 2185  C   GLY A 861     6787   9165   8519   2528    570   -714       C  
ATOM   2186  O   GLY A 861      -2.006  13.305  20.134  1.00 67.15           O  
ANISOU 2186  O   GLY A 861     7362   9209   8943   2595    689   -743       O  
ATOM   2187  N   HIS A 862      -2.313  11.086  19.936  1.00 53.18           N  
ANISOU 2187  N   HIS A 862     5225   7926   7054   2245    560   -769       N  
ATOM   2188  CA  HIS A 862      -1.414  10.781  21.042  1.00 44.03           C  
ANISOU 2188  CA  HIS A 862     4171   6643   5915   2027    680   -852       C  
ATOM   2189  C   HIS A 862      -0.738   9.443  20.777  1.00 39.25           C  
ANISOU 2189  C   HIS A 862     3517   6130   5266   1764    625   -831       C  
ATOM   2190  O   HIS A 862      -1.379   8.506  20.304  1.00 46.26           O  
ANISOU 2190  O   HIS A 862     4188   7284   6103   1654    547   -825       O  
ATOM   2191  CB  HIS A 862      -2.171  10.748  22.375  1.00 46.70           C  
ANISOU 2191  CB  HIS A 862     4360   7153   6231   1951    799   -988       C  
ATOM   2192  CG  HIS A 862      -1.291  10.526  23.566  1.00 55.95           C  
ANISOU 2192  CG  HIS A 862     5652   8225   7383   1744    917  -1075       C  
ATOM   2193  ND1 HIS A 862      -0.220  11.342  23.862  1.00 60.06           N  
ANISOU 2193  ND1 HIS A 862     6443   8430   7948   1781    984  -1103       N  
ATOM   2194  CD2 HIS A 862      -1.325   9.583  24.537  1.00 55.24           C  
ANISOU 2194  CD2 HIS A 862     5458   8317   7215   1484    982  -1140       C  
ATOM   2195  CE1 HIS A 862       0.373  10.907  24.960  1.00 57.17           C  
ANISOU 2195  CE1 HIS A 862     6109   8091   7520   1563   1062  -1197       C  
ATOM   2196  NE2 HIS A 862      -0.278   9.841  25.389  1.00 56.17           N  
ANISOU 2196  NE2 HIS A 862     5771   8257   7315   1391   1064  -1202       N  
ATOM   2197  N   TYR A 863       0.554   9.354  21.084  1.00 31.56           N  
ANISOU 2197  N   TYR A 863     2794   4884   4313   1579    656   -794       N  
ATOM   2198  CA  TYR A 863       1.299   8.120  20.908  1.00 31.01           C  
ANISOU 2198  CA  TYR A 863     2769   4804   4210   1272    602   -725       C  
ATOM   2199  C   TYR A 863       1.682   7.504  22.247  1.00 34.71           C  
ANISOU 2199  C   TYR A 863     3253   5302   4632   1029    695   -788       C  
ATOM   2200  O   TYR A 863       1.949   8.208  23.226  1.00 42.58           O  
ANISOU 2200  O   TYR A 863     4330   6220   5630   1064    790   -873       O  
ATOM   2201  CB  TYR A 863       2.574   8.329  20.104  1.00 44.48           C  
ANISOU 2201  CB  TYR A 863     4729   6219   5953   1251    548   -615       C  
ATOM   2202  CG  TYR A 863       2.381   8.938  18.741  1.00 40.93           C  
ANISOU 2202  CG  TYR A 863     4327   5704   5520   1485    465   -519       C  
ATOM   2203  CD1 TYR A 863       2.234  10.307  18.596  1.00 42.84           C  
ANISOU 2203  CD1 TYR A 863     4687   5781   5808   1772    516   -513       C  
ATOM   2204  CD2 TYR A 863       2.400   8.149  17.595  1.00 42.66           C  
ANISOU 2204  CD2 TYR A 863     4508   6005   5695   1422    348   -430       C  
ATOM   2205  CE1 TYR A 863       2.092  10.879  17.358  1.00 53.26           C  
ANISOU 2205  CE1 TYR A 863     6091   7027   7120   2011    449   -393       C  
ATOM   2206  CE2 TYR A 863       2.262   8.718  16.334  1.00 40.88           C  
ANISOU 2206  CE2 TYR A 863     4343   5740   5450   1647    268   -330       C  
ATOM   2207  CZ  TYR A 863       2.116  10.080  16.227  1.00 46.83           C  
ANISOU 2207  CZ  TYR A 863     5221   6333   6239   1948    318   -297       C  
ATOM   2208  OH  TYR A 863       1.971  10.658  14.990  1.00 58.65           O  
ANISOU 2208  OH  TYR A 863     6809   7783   7691   2200    248   -167       O  
ATOM   2209  N   THR A 864       1.743   6.174  22.257  1.00 35.08           N  
ANISOU 2209  N   THR A 864     3250   5452   4628    784    673   -742       N  
ATOM   2210  CA  THR A 864       2.169   5.402  23.426  1.00 34.70           C  
ANISOU 2210  CA  THR A 864     3251   5425   4507    560    754   -751       C  
ATOM   2211  C   THR A 864       3.000   4.233  22.933  1.00 33.98           C  
ANISOU 2211  C   THR A 864     3278   5235   4399    370    695   -633       C  
ATOM   2212  O   THR A 864       3.232   4.089  21.729  1.00 30.27           O  
ANISOU 2212  O   THR A 864     2840   4686   3974    401    600   -569       O  
ATOM   2213  CB  THR A 864       0.982   4.878  24.234  1.00 28.36           C  
ANISOU 2213  CB  THR A 864     2240   4896   3639    464    856   -831       C  
ATOM   2214  OG1 THR A 864       0.145   4.089  23.384  1.00 34.52           O  
ANISOU 2214  OG1 THR A 864     2848   5843   4427    381    811   -820       O  
ATOM   2215  CG2 THR A 864       0.173   6.022  24.842  1.00 30.32           C  
ANISOU 2215  CG2 THR A 864     2363   5259   3897    673    935   -966       C  
ATOM   2216  N   ALA A 865       3.419   3.356  23.850  1.00 24.60           N  
ANISOU 2216  N   ALA A 865     2161   4056   3131    190    758   -598       N  
ATOM   2217  CA  ALA A 865       4.150   2.171  23.407  1.00 24.57           C  
ANISOU 2217  CA  ALA A 865     2281   3944   3110     41    721   -482       C  
ATOM   2218  C   ALA A 865       3.817   0.952  24.251  1.00 28.00           C  
ANISOU 2218  C   ALA A 865     2728   4460   3450   -160    827   -443       C  
ATOM   2219  O   ALA A 865       3.635   1.069  25.461  1.00 33.75           O  
ANISOU 2219  O   ALA A 865     3448   5284   4092   -185    920   -473       O  
ATOM   2220  CB  ALA A 865       5.662   2.395  23.469  1.00 24.78           C  
ANISOU 2220  CB  ALA A 865     2493   3787   3136     82    669   -422       C  
ATOM   2221  N   PHE A 866       3.731  -0.208  23.611  1.00 30.82           N  
ANISOU 2221  N   PHE A 866     3127   4769   3815   -309    828   -379       N  
ATOM   2222  CA  PHE A 866       3.934  -1.491  24.285  1.00 32.62           C  
ANISOU 2222  CA  PHE A 866     3497   4941   3957   -489    933   -284       C  
ATOM   2223  C   PHE A 866       5.397  -1.865  24.129  1.00 29.47           C  
ANISOU 2223  C   PHE A 866     3315   4335   3545   -424    867   -161       C  
ATOM   2224  O   PHE A 866       5.990  -1.639  23.069  1.00 28.92           O  
ANISOU 2224  O   PHE A 866     3272   4159   3556   -343    761   -154       O  
ATOM   2225  CB  PHE A 866       3.100  -2.627  23.686  1.00 26.11           C  
ANISOU 2225  CB  PHE A 866     2637   4133   3151   -709   1001   -296       C  
ATOM   2226  CG  PHE A 866       1.622  -2.513  23.902  1.00 28.08           C  
ANISOU 2226  CG  PHE A 866     2640   4636   3395   -824   1087   -427       C  
ATOM   2227  CD1 PHE A 866       1.052  -2.817  25.136  1.00 29.78           C  
ANISOU 2227  CD1 PHE A 866     2835   4965   3515   -953   1255   -431       C  
ATOM   2228  CD2 PHE A 866       0.782  -2.168  22.853  1.00 30.14           C  
ANISOU 2228  CD2 PHE A 866     2675   5052   3725   -806   1006   -546       C  
ATOM   2229  CE1 PHE A 866      -0.325  -2.737  25.321  1.00 37.05           C  
ANISOU 2229  CE1 PHE A 866     3493   6153   4430  -1072   1351   -568       C  
ATOM   2230  CE2 PHE A 866      -0.597  -2.082  23.035  1.00 34.92           C  
ANISOU 2230  CE2 PHE A 866     3002   5948   4319   -901   1080   -683       C  
ATOM   2231  CZ  PHE A 866      -1.150  -2.364  24.267  1.00 39.23           C  
ANISOU 2231  CZ  PHE A 866     3510   6607   4788  -1043   1259   -702       C  
ATOM   2232  N   ALA A 867       5.984  -2.440  25.172  1.00 26.04           N  
ANISOU 2232  N   ALA A 867     3030   3867   2997   -444    933    -60       N  
ATOM   2233  CA  ALA A 867       7.334  -2.957  25.000  1.00 23.74           C  
ANISOU 2233  CA  ALA A 867     2921   3414   2684   -364    872     61       C  
ATOM   2234  C   ALA A 867       7.563  -4.129  25.932  1.00 27.20           C  
ANISOU 2234  C   ALA A 867     3550   3800   2987   -421    982    209       C  
ATOM   2235  O   ALA A 867       7.027  -4.181  27.045  1.00 28.90           O  
ANISOU 2235  O   ALA A 867     3763   4134   3085   -480   1085    222       O  
ATOM   2236  CB  ALA A 867       8.401  -1.889  25.243  1.00 26.26           C  
ANISOU 2236  CB  ALA A 867     3218   3766   2995   -194    763     27       C  
ATOM   2237  N   LYS A 868       8.362  -5.075  25.455  1.00 28.18           N  
ANISOU 2237  N   LYS A 868     3852   3737   3118   -389    973    328       N  
ATOM   2238  CA  LYS A 868       8.769  -6.228  26.235  1.00 27.94           C  
ANISOU 2238  CA  LYS A 868     4056   3606   2956   -379   1073    507       C  
ATOM   2239  C   LYS A 868      10.071  -5.914  26.970  1.00 30.67           C  
ANISOU 2239  C   LYS A 868     4443   4031   3179   -152    972    589       C  
ATOM   2240  O   LYS A 868      11.054  -5.500  26.355  1.00 27.42           O  
ANISOU 2240  O   LYS A 868     3981   3607   2829    -17    841    559       O  
ATOM   2241  CB  LYS A 868       8.941  -7.437  25.312  1.00 28.57           C  
ANISOU 2241  CB  LYS A 868     4322   3425   3109   -437   1129    582       C  
ATOM   2242  CG  LYS A 868       9.140  -8.734  26.041  1.00 30.74           C  
ANISOU 2242  CG  LYS A 868     4889   3531   3261   -441   1280    778       C  
ATOM   2243  CD  LYS A 868       9.382  -9.879  25.070  1.00 40.52           C  
ANISOU 2243  CD  LYS A 868     6337   4470   4587   -482   1348    828       C  
ATOM   2244  CE  LYS A 868       9.440 -11.197  25.840  1.00 58.98           C  
ANISOU 2244  CE  LYS A 868     9017   6587   6804   -492   1542   1037       C  
ATOM   2245  NZ  LYS A 868       9.339 -12.414  24.999  1.00 70.28           N  
ANISOU 2245  NZ  LYS A 868    10696   7681   8327   -612   1680   1057       N  
ATOM   2246  N   ASN A 869      10.080  -6.102  28.287  1.00 27.72           N  
ANISOU 2246  N   ASN A 869     4147   3770   2615   -118   1034    682       N  
ATOM   2247  CA  ASN A 869      11.270  -5.769  29.061  1.00 29.46           C  
ANISOU 2247  CA  ASN A 869     4369   4140   2683     95    921    735       C  
ATOM   2248  C   ASN A 869      12.288  -6.898  28.984  1.00 32.83           C  
ANISOU 2248  C   ASN A 869     5009   4425   3040    270    911    938       C  
ATOM   2249  O   ASN A 869      11.949  -8.067  29.206  1.00 34.37           O  
ANISOU 2249  O   ASN A 869     5443   4443   3174    237   1057   1107       O  
ATOM   2250  CB  ASN A 869      10.900  -5.493  30.520  1.00 37.94           C  
ANISOU 2250  CB  ASN A 869     5441   5433   3543     84    981    749       C  
ATOM   2251  CG  ASN A 869      12.113  -5.217  31.376  1.00 36.40           C  
ANISOU 2251  CG  ASN A 869     5237   5443   3150    295    854    792       C  
ATOM   2252  OD1 ASN A 869      12.729  -6.133  31.917  1.00 39.44           O  
ANISOU 2252  OD1 ASN A 869     5804   5820   3363    446    864    996       O  
ATOM   2253  ND2 ASN A 869      12.475  -3.947  31.489  1.00 33.97           N  
ANISOU 2253  ND2 ASN A 869     4721   5325   2861    312    736    593       N  
ATOM   2254  N   LYS A 870      13.547  -6.549  28.704  1.00 39.84           N  
ANISOU 2254  N   LYS A 870     5814   5391   3931    461    755    919       N  
ATOM   2255  CA  LYS A 870      14.545  -7.577  28.408  1.00 40.52           C  
ANISOU 2255  CA  LYS A 870     6067   5343   3985    666    738   1089       C  
ATOM   2256  C   LYS A 870      14.953  -8.385  29.627  1.00 45.19           C  
ANISOU 2256  C   LYS A 870     6850   6003   4317    855    776   1313       C  
ATOM   2257  O   LYS A 870      15.590  -9.433  29.468  1.00 54.41           O  
ANISOU 2257  O   LYS A 870     8219   7010   5444   1048    805   1495       O  
ATOM   2258  CB  LYS A 870      15.804  -6.961  27.788  1.00 32.69           C  
ANISOU 2258  CB  LYS A 870     4894   4468   3059    818    569    993       C  
ATOM   2259  CG  LYS A 870      16.632  -6.110  28.763  1.00 37.42           C  
ANISOU 2259  CG  LYS A 870     5312   5418   3488    937    430    926       C  
ATOM   2260  CD  LYS A 870      17.914  -5.591  28.088  1.00 43.61           C  
ANISOU 2260  CD  LYS A 870     5907   6318   4344   1051    289    819       C  
ATOM   2261  CE  LYS A 870      18.784  -4.768  29.033  1.00 42.91           C  
ANISOU 2261  CE  LYS A 870     5614   6607   4082   1132    153    715       C  
ATOM   2262  NZ  LYS A 870      19.162  -5.546  30.253  1.00 51.65           N  
ANISOU 2262  NZ  LYS A 870     6825   7896   4904   1352    126    902       N  
ATOM   2263  N   ASP A 871      14.620  -7.938  30.832  1.00 40.34           N  
ANISOU 2263  N   ASP A 871     6195   5620   3512    829    782   1311       N  
ATOM   2264  CA  ASP A 871      15.094  -8.618  32.027  1.00 42.00           C  
ANISOU 2264  CA  ASP A 871     6581   5947   3430   1043    795   1534       C  
ATOM   2265  C   ASP A 871      14.085  -9.610  32.583  1.00 46.93           C  
ANISOU 2265  C   ASP A 871     7507   6367   3958    929   1029   1726       C  
ATOM   2266  O   ASP A 871      14.488 -10.676  33.054  1.00 50.48           O  
ANISOU 2266  O   ASP A 871     8160   6692   4328   1078   1052   1908       O  
ATOM   2267  CB  ASP A 871      15.476  -7.595  33.100  1.00 48.89           C  
ANISOU 2267  CB  ASP A 871     7247   7235   4095   1101    661   1420       C  
ATOM   2268  CG  ASP A 871      16.707  -6.778  32.716  1.00 62.36           C  
ANISOU 2268  CG  ASP A 871     8686   9164   5845   1231    444   1256       C  
ATOM   2269  OD1 ASP A 871      17.618  -7.339  32.074  1.00 65.40           O  
ANISOU 2269  OD1 ASP A 871     9096   9468   6284   1423    380   1342       O  
ATOM   2270  OD2 ASP A 871      16.762  -5.573  33.044  1.00 63.23           O  
ANISOU 2270  OD2 ASP A 871     8563   9523   5939   1130    355   1028       O  
ATOM   2271  N   ASP A 872      12.781  -9.302  32.540  1.00 46.53           N  
ANISOU 2271  N   ASP A 872     7411   6265   4005    618   1164   1606       N  
ATOM   2272  CA  ASP A 872      11.763 -10.259  32.965  1.00 52.52           C  
ANISOU 2272  CA  ASP A 872     8412   6821   4722    434   1397   1738       C  
ATOM   2273  C   ASP A 872      10.943 -10.841  31.820  1.00 44.15           C  
ANISOU 2273  C   ASP A 872     7421   5433   3919    184   1538   1677       C  
ATOM   2274  O   ASP A 872      10.139 -11.746  32.061  1.00 51.22           O  
ANISOU 2274  O   ASP A 872     8468   6149   4843     -4   1698   1730       O  
ATOM   2275  CB  ASP A 872      10.820  -9.633  34.011  1.00 49.17           C  
ANISOU 2275  CB  ASP A 872     7896   6640   4145    262   1490   1666       C  
ATOM   2276  CG  ASP A 872      10.024  -8.432  33.485  1.00 44.44           C  
ANISOU 2276  CG  ASP A 872     6982   6173   3732     53   1460   1371       C  
ATOM   2277  OD1 ASP A 872       9.904  -8.223  32.255  1.00 35.81           O  
ANISOU 2277  OD1 ASP A 872     5769   4940   2898    -28   1405   1236       O  
ATOM   2278  OD2 ASP A 872       9.491  -7.691  34.341  1.00 38.48           O  
ANISOU 2278  OD2 ASP A 872     6097   5668   2856    -19   1487   1267       O  
ATOM   2279  N   GLY A 873      11.130 -10.361  30.591  1.00 38.45           N  
ANISOU 2279  N   GLY A 873     6538   4658   3413    159   1439   1518       N  
ATOM   2280  CA  GLY A 873      10.380 -10.855  29.453  1.00 42.95           C  
ANISOU 2280  CA  GLY A 873     7147   4967   4205    -79   1549   1431       C  
ATOM   2281  C   GLY A 873       8.903 -10.531  29.456  1.00 49.34           C  
ANISOU 2281  C   GLY A 873     7815   5848   5086   -417   1675   1272       C  
ATOM   2282  O   GLY A 873       8.163 -11.093  28.646  1.00 42.00           O  
ANISOU 2282  O   GLY A 873     6927   4729   4301   -652   1792   1201       O  
ATOM   2283  N   LYS A 874       8.441  -9.648  30.335  1.00 45.34           N  
ANISOU 2283  N   LYS A 874     7125   5628   4475   -450   1659   1195       N  
ATOM   2284  CA  LYS A 874       7.033  -9.287  30.370  1.00 38.43           C  
ANISOU 2284  CA  LYS A 874     6074   4867   3662   -737   1779   1032       C  
ATOM   2285  C   LYS A 874       6.775  -8.029  29.545  1.00 33.21           C  
ANISOU 2285  C   LYS A 874     5068   4372   3178   -739   1610    781       C  
ATOM   2286  O   LYS A 874       7.681  -7.248  29.254  1.00 31.82           O  
ANISOU 2286  O   LYS A 874     4790   4262   3038   -534   1416    733       O  
ATOM   2287  CB  LYS A 874       6.561  -9.068  31.809  1.00 39.80           C  
ANISOU 2287  CB  LYS A 874     6255   5255   3612   -772   1895   1082       C  
ATOM   2288  CG  LYS A 874       6.748 -10.273  32.720  1.00 44.22           C  
ANISOU 2288  CG  LYS A 874     7123   5675   4002   -739   2015   1331       C  
ATOM   2289  CD  LYS A 874       6.172 -10.006  34.097  1.00 43.34           C  
ANISOU 2289  CD  LYS A 874     6969   5812   3687   -787   2102   1351       C  
ATOM   2290  CE  LYS A 874       6.029 -11.297  34.878  1.00 49.68           C  
ANISOU 2290  CE  LYS A 874     8035   6455   4386   -821   2225   1564       C  
ATOM   2291  NZ  LYS A 874       7.355 -11.815  35.309  1.00 68.53           N  
ANISOU 2291  NZ  LYS A 874    10654   8764   6622   -514   2108   1783       N  
ATOM   2292  N   TRP A 875       5.505  -7.848  29.184  1.00 35.83           N  
ANISOU 2292  N   TRP A 875     5223   4780   3612   -976   1699    623       N  
ATOM   2293  CA  TRP A 875       5.045  -6.719  28.395  1.00 31.54           C  
ANISOU 2293  CA  TRP A 875     4368   4392   3223   -969   1567    404       C  
ATOM   2294  C   TRP A 875       4.548  -5.595  29.284  1.00 35.59           C  
ANISOU 2294  C   TRP A 875     4676   5184   3661   -923   1565    290       C  
ATOM   2295  O   TRP A 875       3.891  -5.832  30.304  1.00 33.70           O  
ANISOU 2295  O   TRP A 875     4457   5060   3287  -1038   1730    315       O  
ATOM   2296  CB  TRP A 875       3.924  -7.162  27.457  1.00 38.14           C  
ANISOU 2296  CB  TRP A 875     5094   5202   4195  -1222   1649    282       C  
ATOM   2297  CG  TRP A 875       4.411  -7.906  26.273  1.00 32.78           C  
ANISOU 2297  CG  TRP A 875     4550   4279   3627  -1245   1602    311       C  
ATOM   2298  CD1 TRP A 875       4.482  -9.262  26.122  1.00 39.86           C  
ANISOU 2298  CD1 TRP A 875     5717   4914   4513  -1395   1751    418       C  
ATOM   2299  CD2 TRP A 875       4.899  -7.335  25.063  1.00 34.04           C  
ANISOU 2299  CD2 TRP A 875     4602   4416   3916  -1113   1410    226       C  
ATOM   2300  NE1 TRP A 875       4.984  -9.571  24.879  1.00 34.80           N  
ANISOU 2300  NE1 TRP A 875     5130   4102   3992  -1361   1657    384       N  
ATOM   2301  CE2 TRP A 875       5.253  -8.400  24.211  1.00 30.59           C  
ANISOU 2301  CE2 TRP A 875     4360   3726   3536  -1189   1444    273       C  
ATOM   2302  CE3 TRP A 875       5.070  -6.022  24.614  1.00 30.36           C  
ANISOU 2302  CE3 TRP A 875     3918   4100   3517   -938   1232    119       C  
ATOM   2303  CZ2 TRP A 875       5.769  -8.195  22.930  1.00 28.11           C  
ANISOU 2303  CZ2 TRP A 875     4008   3342   3330  -1099   1299    210       C  
ATOM   2304  CZ3 TRP A 875       5.591  -5.814  23.333  1.00 26.30           C  
ANISOU 2304  CZ3 TRP A 875     3384   3498   3110   -851   1094     79       C  
ATOM   2305  CH2 TRP A 875       5.930  -6.897  22.506  1.00 32.78           C  
ANISOU 2305  CH2 TRP A 875     4380   4103   3972   -933   1124    122       C  
ATOM   2306  N   TYR A 876       4.835  -4.365  28.870  1.00 34.92           N  
ANISOU 2306  N   TYR A 876     4409   5194   3665   -761   1398    157       N  
ATOM   2307  CA  TYR A 876       4.488  -3.175  29.628  1.00 37.56           C  
ANISOU 2307  CA  TYR A 876     4571   5752   3947   -682   1389     25       C  
ATOM   2308  C   TYR A 876       3.966  -2.127  28.666  1.00 40.59           C  
ANISOU 2308  C   TYR A 876     4721   6192   4508   -619   1292   -153       C  
ATOM   2309  O   TYR A 876       4.269  -2.141  27.468  1.00 31.62           O  
ANISOU 2309  O   TYR A 876     3579   4929   3506   -583   1182   -154       O  
ATOM   2310  CB  TYR A 876       5.693  -2.625  30.403  1.00 34.50           C  
ANISOU 2310  CB  TYR A 876     4271   5401   3435   -496   1290     61       C  
ATOM   2311  CG  TYR A 876       6.199  -3.588  31.449  1.00 32.46           C  
ANISOU 2311  CG  TYR A 876     4238   5139   2958   -500   1371    252       C  
ATOM   2312  CD1 TYR A 876       7.154  -4.556  31.139  1.00 34.87           C  
ANISOU 2312  CD1 TYR A 876     4752   5257   3239   -433   1327    438       C  
ATOM   2313  CD2 TYR A 876       5.707  -3.543  32.751  1.00 33.04           C  
ANISOU 2313  CD2 TYR A 876     4324   5397   2831   -548   1502    256       C  
ATOM   2314  CE1 TYR A 876       7.608  -5.459  32.118  1.00 32.90           C  
ANISOU 2314  CE1 TYR A 876     4735   4999   2768   -387   1405    644       C  
ATOM   2315  CE2 TYR A 876       6.153  -4.433  33.727  1.00 36.23           C  
ANISOU 2315  CE2 TYR A 876     4960   5805   3000   -528   1581    460       C  
ATOM   2316  CZ  TYR A 876       7.102  -5.382  33.410  1.00 34.96           C  
ANISOU 2316  CZ  TYR A 876     5017   5449   2815   -434   1528    662       C  
ATOM   2317  OH  TYR A 876       7.541  -6.253  34.386  1.00 37.29           O  
ANISOU 2317  OH  TYR A 876     5563   5746   2860   -365   1606    890       O  
ATOM   2318  N   TYR A 877       3.181  -1.212  29.216  1.00 36.07           N  
ANISOU 2318  N   TYR A 877     3970   5816   3919   -586   1341   -296       N  
ATOM   2319  CA  TYR A 877       2.552  -0.127  28.478  1.00 34.61           C  
ANISOU 2319  CA  TYR A 877     3568   5706   3876   -477   1272   -456       C  
ATOM   2320  C   TYR A 877       3.126   1.191  28.981  1.00 35.84           C  
ANISOU 2320  C   TYR A 877     3723   5876   4017   -283   1213   -549       C  
ATOM   2321  O   TYR A 877       3.028   1.499  30.176  1.00 34.41           O  
ANISOU 2321  O   TYR A 877     3547   5824   3705   -280   1301   -602       O  
ATOM   2322  CB  TYR A 877       1.031  -0.171  28.660  1.00 41.10           C  
ANISOU 2322  CB  TYR A 877     4161   6755   4699   -585   1405   -568       C  
ATOM   2323  CG  TYR A 877       0.301   0.757  27.720  1.00 40.10           C  
ANISOU 2323  CG  TYR A 877     3801   6721   4713   -440   1321   -705       C  
ATOM   2324  CD1 TYR A 877       0.143   0.430  26.371  1.00 43.98           C  
ANISOU 2324  CD1 TYR A 877     4235   7161   5314   -461   1217   -692       C  
ATOM   2325  CD2 TYR A 877      -0.212   1.960  28.167  1.00 41.34           C  
ANISOU 2325  CD2 TYR A 877     3811   7019   4878   -260   1345   -845       C  
ATOM   2326  CE1 TYR A 877      -0.515   1.277  25.507  1.00 45.95           C  
ANISOU 2326  CE1 TYR A 877     4279   7522   5659   -290   1127   -794       C  
ATOM   2327  CE2 TYR A 877      -0.878   2.812  27.309  1.00 42.75           C  
ANISOU 2327  CE2 TYR A 877     3797   7275   5173    -74   1270   -945       C  
ATOM   2328  CZ  TYR A 877      -1.024   2.466  25.983  1.00 48.06           C  
ANISOU 2328  CZ  TYR A 877     4409   7917   5934    -82   1154   -908       C  
ATOM   2329  OH  TYR A 877      -1.681   3.311  25.132  1.00 60.31           O  
ANISOU 2329  OH  TYR A 877     5777   9572   7568    139   1068   -985       O  
ATOM   2330  N   PHE A 878       3.697   1.971  28.070  1.00 27.00           N  
ANISOU 2330  N   PHE A 878     2610   4624   3023   -141   1080   -580       N  
ATOM   2331  CA  PHE A 878       4.407   3.199  28.383  1.00 26.60           C  
ANISOU 2331  CA  PHE A 878     2602   4522   2983      5   1032   -675       C  
ATOM   2332  C   PHE A 878       3.622   4.369  27.811  1.00 34.56           C  
ANISOU 2332  C   PHE A 878     3477   5537   4118    162   1029   -805       C  
ATOM   2333  O   PHE A 878       3.543   4.529  26.581  1.00 33.81           O  
ANISOU 2333  O   PHE A 878     3357   5344   4146    235    944   -772       O  
ATOM   2334  CB  PHE A 878       5.805   3.179  27.775  1.00 25.64           C  
ANISOU 2334  CB  PHE A 878     2625   4216   2903     35    908   -597       C  
ATOM   2335  CG  PHE A 878       6.690   2.116  28.314  1.00 24.72           C  
ANISOU 2335  CG  PHE A 878     2640   4097   2657    -49    895   -463       C  
ATOM   2336  CD1 PHE A 878       6.587   0.804  27.879  1.00 24.50           C  
ANISOU 2336  CD1 PHE A 878     2673   4011   2624   -143    908   -316       C  
ATOM   2337  CD2 PHE A 878       7.643   2.436  29.264  1.00 25.05           C  
ANISOU 2337  CD2 PHE A 878     2749   4198   2572    -21    872   -493       C  
ATOM   2338  CE1 PHE A 878       7.434  -0.171  28.377  1.00 24.93           C  
ANISOU 2338  CE1 PHE A 878     2881   4035   2556   -169    905   -172       C  
ATOM   2339  CE2 PHE A 878       8.489   1.475  29.767  1.00 29.28           C  
ANISOU 2339  CE2 PHE A 878     3398   4761   2966    -43    845   -355       C  
ATOM   2340  CZ  PHE A 878       8.385   0.166  29.334  1.00 25.87           C  
ANISOU 2340  CZ  PHE A 878     3053   4242   2536    -98    866   -179       C  
ATOM   2341  N   ASP A 879       3.055   5.185  28.699  1.00 32.98           N  
ANISOU 2341  N   ASP A 879     3206   5453   3874    235   1125   -948       N  
ATOM   2342  CA  ASP A 879       2.258   6.350  28.344  1.00 37.56           C  
ANISOU 2342  CA  ASP A 879     3673   6040   4558    435   1149  -1076       C  
ATOM   2343  C   ASP A 879       2.887   7.568  29.009  1.00 34.31           C  
ANISOU 2343  C   ASP A 879     3382   5517   4137    535   1187  -1212       C  
ATOM   2344  O   ASP A 879       2.525   7.931  30.131  1.00 33.98           O  
ANISOU 2344  O   ASP A 879     3308   5605   4000    539   1300  -1343       O  
ATOM   2345  CB  ASP A 879       0.802   6.163  28.768  1.00 35.11           C  
ANISOU 2345  CB  ASP A 879     3135   5993   4210    437   1264  -1153       C  
ATOM   2346  CG  ASP A 879      -0.091   7.321  28.325  1.00 51.58           C  
ANISOU 2346  CG  ASP A 879     5089   8104   6403    701   1274  -1265       C  
ATOM   2347  OD1 ASP A 879       0.394   8.220  27.609  1.00 45.75           O  
ANISOU 2347  OD1 ASP A 879     4456   7157   5768    882   1207  -1269       O  
ATOM   2348  OD2 ASP A 879      -1.281   7.336  28.695  1.00 53.18           O  
ANISOU 2348  OD2 ASP A 879     5135   8482   6589    720   1329  -1302       O  
ATOM   2349  N   ASP A 880       3.807   8.215  28.290  1.00 30.71           N  
ANISOU 2349  N   ASP A 880     3068   4821   3779    598   1107  -1197       N  
ATOM   2350  CA  ASP A 880       4.612   9.328  28.806  1.00 36.33           C  
ANISOU 2350  CA  ASP A 880     3925   5385   4494    630   1145  -1339       C  
ATOM   2351  C   ASP A 880       5.177   8.896  30.157  1.00 34.39           C  
ANISOU 2351  C   ASP A 880     3707   5298   4061    467   1178  -1398       C  
ATOM   2352  O   ASP A 880       5.986   7.953  30.183  1.00 34.24           O  
ANISOU 2352  O   ASP A 880     3729   5316   3965    334   1095  -1272       O  
ATOM   2353  CB  ASP A 880       3.783  10.622  28.773  1.00 41.13           C  
ANISOU 2353  CB  ASP A 880     4521   5913   5194    854   1245  -1485       C  
ATOM   2354  CG  ASP A 880       3.542  11.114  27.340  1.00 38.64           C  
ANISOU 2354  CG  ASP A 880     4236   5409   5039   1043   1186  -1390       C  
ATOM   2355  OD1 ASP A 880       4.250  10.637  26.432  1.00 35.82           O  
ANISOU 2355  OD1 ASP A 880     3942   4947   4720    967   1077  -1247       O  
ATOM   2356  OD2 ASP A 880       2.662  11.973  27.126  1.00 42.89           O  
ANISOU 2356  OD2 ASP A 880     4738   5910   5647   1285   1251  -1454       O  
ATOM   2357  N   SER A 881       4.828   9.538  31.275  1.00 33.43           N  
ANISOU 2357  N   SER A 881     3575   5280   3849    489   1293  -1581       N  
ATOM   2358  CA  SER A 881       5.510   9.186  32.514  1.00 38.44           C  
ANISOU 2358  CA  SER A 881     4253   6081   4272    342   1304  -1635       C  
ATOM   2359  C   SER A 881       4.988   7.890  33.132  1.00 46.06           C  
ANISOU 2359  C   SER A 881     5138   7290   5072    246   1332  -1498       C  
ATOM   2360  O   SER A 881       5.651   7.332  34.009  1.00 39.74           O  
ANISOU 2360  O   SER A 881     4397   6630   4074    141   1312  -1464       O  
ATOM   2361  CB  SER A 881       5.376  10.313  33.536  1.00 37.79           C  
ANISOU 2361  CB  SER A 881     4219   6010   4131    373   1402  -1864       C  
ATOM   2362  OG  SER A 881       4.003  10.517  33.831  1.00 41.50           O  
ANISOU 2362  OG  SER A 881     4597   6548   4623    482   1495  -1874       O  
ATOM   2363  N   SER A 882       3.844   7.388  32.674  1.00 38.14           N  
ANISOU 2363  N   SER A 882     4009   6346   4135    276   1380  -1416       N  
ATOM   2364  CA  SER A 882       3.178   6.242  33.276  1.00 33.64           C  
ANISOU 2364  CA  SER A 882     3371   5989   3422    154   1460  -1312       C  
ATOM   2365  C   SER A 882       3.674   4.943  32.661  1.00 37.32           C  
ANISOU 2365  C   SER A 882     3905   6387   3890     39   1369  -1079       C  
ATOM   2366  O   SER A 882       3.755   4.812  31.434  1.00 37.63           O  
ANISOU 2366  O   SER A 882     3931   6270   4095     70   1276  -1002       O  
ATOM   2367  CB  SER A 882       1.662   6.372  33.100  1.00 43.96           C  
ANISOU 2367  CB  SER A 882     4503   7380   4820    211   1543  -1346       C  
ATOM   2368  OG  SER A 882       1.040   5.107  33.084  1.00 55.08           O  
ANISOU 2368  OG  SER A 882     5840   8913   6174     54   1594  -1209       O  
ATOM   2369  N   VAL A 883       4.001   3.979  33.512  1.00 34.94           N  
ANISOU 2369  N   VAL A 883     3692   6194   3388    -80   1405   -962       N  
ATOM   2370  CA  VAL A 883       4.351   2.636  33.071  1.00 36.49           C  
ANISOU 2370  CA  VAL A 883     3983   6312   3568   -181   1363   -735       C  
ATOM   2371  C   VAL A 883       3.417   1.665  33.771  1.00 35.29           C  
ANISOU 2371  C   VAL A 883     3821   6309   3279   -326   1533   -652       C  
ATOM   2372  O   VAL A 883       3.205   1.778  34.984  1.00 35.36           O  
ANISOU 2372  O   VAL A 883     3845   6500   3090   -351   1644   -699       O  
ATOM   2373  CB  VAL A 883       5.821   2.302  33.378  1.00 40.73           C  
ANISOU 2373  CB  VAL A 883     4686   6802   3985   -157   1247   -631       C  
ATOM   2374  CG1 VAL A 883       6.177   0.943  32.775  1.00 33.90           C  
ANISOU 2374  CG1 VAL A 883     3938   5806   3135   -215   1212   -397       C  
ATOM   2375  CG2 VAL A 883       6.741   3.381  32.814  1.00 40.94           C  
ANISOU 2375  CG2 VAL A 883     4706   6714   4136    -57   1113   -754       C  
ATOM   2376  N   SER A 884       2.848   0.722  33.021  1.00 35.56           N  
ANISOU 2376  N   SER A 884     3835   6272   3406   -444   1571   -542       N  
ATOM   2377  CA  SER A 884       1.968  -0.249  33.661  1.00 41.83           C  
ANISOU 2377  CA  SER A 884     4636   7182   4075   -633   1765   -466       C  
ATOM   2378  C   SER A 884       2.163  -1.620  33.035  1.00 37.54           C  
ANISOU 2378  C   SER A 884     4244   6455   3564   -775   1777   -268       C  
ATOM   2379  O   SER A 884       2.718  -1.754  31.946  1.00 33.28           O  
ANISOU 2379  O   SER A 884     3739   5731   3174   -725   1637   -226       O  
ATOM   2380  CB  SER A 884       0.507   0.202  33.583  1.00 42.18           C  
ANISOU 2380  CB  SER A 884     4432   7372   4223   -667   1855   -623       C  
ATOM   2381  OG  SER A 884       0.236   0.732  32.306  1.00 64.87           O  
ANISOU 2381  OG  SER A 884     7135  10205   7306   -584   1754   -720       O  
ATOM   2382  N   THR A 885       1.731  -2.653  33.750  1.00 39.03           N  
ANISOU 2382  N   THR A 885     4551   6678   3602   -957   1965   -145       N  
ATOM   2383  CA  THR A 885       1.824  -3.992  33.187  1.00 40.79           C  
ANISOU 2383  CA  THR A 885     4952   6685   3861  -1113   2019     30       C  
ATOM   2384  C   THR A 885       0.798  -4.163  32.076  1.00 41.08           C  
ANISOU 2384  C   THR A 885     4788   6708   4113  -1263   2032    -88       C  
ATOM   2385  O   THR A 885      -0.274  -3.552  32.084  1.00 43.65           O  
ANISOU 2385  O   THR A 885     4857   7213   4516  -1273   2043   -256       O  
ATOM   2386  CB  THR A 885       1.606  -5.070  34.253  1.00 40.40           C  
ANISOU 2386  CB  THR A 885     5125   6591   3637  -1227   2187    215       C  
ATOM   2387  OG1 THR A 885       0.362  -4.831  34.909  1.00 46.27           O  
ANISOU 2387  OG1 THR A 885     5695   7510   4376  -1320   2301    101       O  
ATOM   2388  CG2 THR A 885       2.739  -5.057  35.269  1.00 47.49           C  
ANISOU 2388  CG2 THR A 885     6244   7520   4280  -1057   2155    365       C  
ATOM   2389  N   ALA A 886       1.139  -5.018  31.120  1.00 39.18           N  
ANISOU 2389  N   ALA A 886     4673   6247   3966  -1353   2007     -1       N  
ATOM   2390  CA  ALA A 886       0.313  -5.275  29.957  1.00 43.28           C  
ANISOU 2390  CA  ALA A 886     5019   6757   4667  -1502   1991   -118       C  
ATOM   2391  C   ALA A 886       0.340  -6.772  29.691  1.00 47.51           C  
ANISOU 2391  C   ALA A 886     5804   7034   5215  -1705   2085     17       C  
ATOM   2392  O   ALA A 886       1.195  -7.495  30.213  1.00 45.11           O  
ANISOU 2392  O   ALA A 886     5813   6526   4801  -1666   2136    220       O  
ATOM   2393  CB  ALA A 886       0.820  -4.490  28.729  1.00 34.24           C  
ANISOU 2393  CB  ALA A 886     3759   5568   3682  -1309   1759   -200       C  
ATOM   2394  N   SER A 887      -0.597  -7.236  28.864  1.00 49.42           N  
ANISOU 2394  N   SER A 887     5909   7285   5584  -1899   2096   -106       N  
ATOM   2395  CA  SER A 887      -0.606  -8.610  28.383  1.00 53.82           C  
ANISOU 2395  CA  SER A 887     6689   7577   6183  -2100   2172    -38       C  
ATOM   2396  C   SER A 887      -0.625  -8.639  26.859  1.00 56.67           C  
ANISOU 2396  C   SER A 887     6941   7899   6693  -2149   2051   -165       C  
ATOM   2397  O   SER A 887      -1.157  -7.728  26.210  1.00 54.66           O  
ANISOU 2397  O   SER A 887     6367   7891   6512  -2096   1934   -338       O  
ATOM   2398  CB  SER A 887      -1.803  -9.380  28.920  1.00 57.84           C  
ANISOU 2398  CB  SER A 887     7175   8134   6669  -2353   2336    -90       C  
ATOM   2399  OG  SER A 887      -2.997  -8.872  28.365  1.00 66.01           O  
ANISOU 2399  OG  SER A 887     7846   9448   7788  -2452   2288   -328       O  
ATOM   2400  N   GLU A 888      -0.049  -9.713  26.299  1.00 56.58           N  
ANISOU 2400  N   GLU A 888     7207   7576   6715  -2227   2079    -78       N  
ATOM   2401  CA  GLU A 888       0.084  -9.854  24.849  1.00 49.66           C  
ANISOU 2401  CA  GLU A 888     6281   6631   5957  -2272   1972   -188       C  
ATOM   2402  C   GLU A 888      -1.244  -9.675  24.126  1.00 42.00           C  
ANISOU 2402  C   GLU A 888     4975   5933   5051  -2447   1928   -437       C  
ATOM   2403  O   GLU A 888      -1.278  -9.187  22.991  1.00 54.75           O  
ANISOU 2403  O   GLU A 888     6402   7663   6737  -2403   1781   -560       O  
ATOM   2404  CB  GLU A 888       0.654 -11.231  24.500  1.00 54.44           C  
ANISOU 2404  CB  GLU A 888     7249   6856   6578  -2358   2049    -89       C  
ATOM   2405  CG  GLU A 888       1.994 -11.575  25.122  1.00 67.05           C  
ANISOU 2405  CG  GLU A 888     9193   8179   8102  -2138   2073    168       C  
ATOM   2406  CD  GLU A 888       2.529 -12.916  24.626  1.00 73.88           C  
ANISOU 2406  CD  GLU A 888    10394   8674   9002  -2169   2134    240       C  
ATOM   2407  OE1 GLU A 888       3.627 -13.324  25.062  1.00 82.52           O  
ANISOU 2407  OE1 GLU A 888    11770   9545  10038  -1950   2140    449       O  
ATOM   2408  OE2 GLU A 888       1.853 -13.558  23.792  1.00 69.27           O  
ANISOU 2408  OE2 GLU A 888     9783   8043   8494  -2393   2171     72       O  
ATOM   2409  N   ASP A 889      -2.343 -10.053  24.760  1.00 43.35           N  
ANISOU 2409  N   ASP A 889     5060   6229   5183  -2633   2049   -512       N  
ATOM   2410  CA  ASP A 889      -3.626 -10.065  24.068  1.00 47.60           C  
ANISOU 2410  CA  ASP A 889     5298   7031   5759  -2813   2015   -753       C  
ATOM   2411  C   ASP A 889      -4.228  -8.678  23.867  1.00 44.49           C  
ANISOU 2411  C   ASP A 889     4497   7028   5380  -2627   1862   -884       C  
ATOM   2412  O   ASP A 889      -5.319  -8.590  23.304  1.00 53.85           O  
ANISOU 2412  O   ASP A 889     5405   8481   6575  -2723   1811  -1079       O  
ATOM   2413  CB  ASP A 889      -4.599 -10.960  24.831  1.00 54.86           C  
ANISOU 2413  CB  ASP A 889     6265   7954   6625  -3085   2214   -797       C  
ATOM   2414  CG  ASP A 889      -4.098 -12.390  24.943  1.00 72.38           C  
ANISOU 2414  CG  ASP A 889     8899   9769   8832  -3254   2373   -681       C  
ATOM   2415  OD1 ASP A 889      -3.347 -12.831  24.046  1.00 71.71           O  
ANISOU 2415  OD1 ASP A 889     8992   9455   8798  -3226   2314   -660       O  
ATOM   2416  OD2 ASP A 889      -4.450 -13.076  25.925  1.00 78.00           O  
ANISOU 2416  OD2 ASP A 889     9771  10385   9482  -3398   2563   -608       O  
ATOM   2417  N   GLN A 890      -3.584  -7.600  24.315  1.00 52.56           N  
ANISOU 2417  N   GLN A 890     5478   8098   6393  -2349   1791   -791       N  
ATOM   2418  CA  GLN A 890      -4.047  -6.257  23.989  1.00 53.03           C  
ANISOU 2418  CA  GLN A 890     5194   8475   6482  -2116   1637   -908       C  
ATOM   2419  C   GLN A 890      -3.123  -5.545  23.014  1.00 49.53           C  
ANISOU 2419  C   GLN A 890     4735   7984   6099  -1892   1465   -881       C  
ATOM   2420  O   GLN A 890      -3.429  -4.427  22.589  1.00 55.63           O  
ANISOU 2420  O   GLN A 890     5255   8982   6901  -1656   1324   -963       O  
ATOM   2421  CB  GLN A 890      -4.227  -5.416  25.261  1.00 61.16           C  
ANISOU 2421  CB  GLN A 890     6153   9632   7453  -1954   1696   -874       C  
ATOM   2422  CG  GLN A 890      -2.979  -5.178  26.085  1.00 62.77           C  
ANISOU 2422  CG  GLN A 890     6612   9636   7602  -1812   1741   -695       C  
ATOM   2423  CD  GLN A 890      -3.299  -4.646  27.489  1.00 67.10           C  
ANISOU 2423  CD  GLN A 890     7130  10309   8056  -1731   1839   -680       C  
ATOM   2424  OE1 GLN A 890      -2.745  -5.116  28.482  1.00 61.87           O  
ANISOU 2424  OE1 GLN A 890     6714   9504   7289  -1775   1959   -535       O  
ATOM   2425  NE2 GLN A 890      -4.189  -3.661  27.566  1.00 65.28           N  
ANISOU 2425  NE2 GLN A 890     6608  10346   7849  -1590   1785   -826       N  
ATOM   2426  N   ILE A 891      -2.025  -6.185  22.622  1.00 40.14           N  
ANISOU 2426  N   ILE A 891     3823   6500   4930  -1947   1480   -766       N  
ATOM   2427  CA  ILE A 891      -1.032  -5.538  21.768  1.00 42.70           C  
ANISOU 2427  CA  ILE A 891     4216   6704   5305  -1676   1282   -707       C  
ATOM   2428  C   ILE A 891      -1.602  -5.232  20.385  1.00 43.11           C  
ANISOU 2428  C   ILE A 891     4025   6954   5401  -1648   1121   -856       C  
ATOM   2429  O   ILE A 891      -1.400  -4.136  19.844  1.00 46.80           O  
ANISOU 2429  O   ILE A 891     4389   7501   5891  -1349    944   -854       O  
ATOM   2430  CB  ILE A 891       0.225  -6.421  21.675  1.00 45.86           C  
ANISOU 2430  CB  ILE A 891     5003   6715   5705  -1696   1308   -543       C  
ATOM   2431  CG1 ILE A 891       0.842  -6.594  23.061  1.00 44.96           C  
ANISOU 2431  CG1 ILE A 891     5114   6456   5514  -1650   1431   -376       C  
ATOM   2432  CG2 ILE A 891       1.217  -5.822  20.691  1.00 41.68           C  
ANISOU 2432  CG2 ILE A 891     4540   6069   5228  -1432   1103   -497       C  
ATOM   2433  CD1 ILE A 891       2.146  -7.339  23.058  1.00 43.20           C  
ANISOU 2433  CD1 ILE A 891     5248   5891   5276  -1582   1438   -197       C  
ATOM   2434  N   VAL A 892      -2.305  -6.189  19.787  1.00 38.77           N  
ANISOU 2434  N   VAL A 892     3397   6486   4849  -1962   1185   -989       N  
ATOM   2435  CA  VAL A 892      -2.830  -6.048  18.432  1.00 45.30           C  
ANISOU 2435  CA  VAL A 892     4008   7525   5679  -1954   1020  -1140       C  
ATOM   2436  C   VAL A 892      -4.072  -5.167  18.487  1.00 49.25           C  
ANISOU 2436  C   VAL A 892     4151   8418   6142  -1799    927  -1260       C  
ATOM   2437  O   VAL A 892      -5.105  -5.571  19.020  1.00 51.40           O  
ANISOU 2437  O   VAL A 892     4326   8830   6374  -1963   1021  -1351       O  
ATOM   2438  CB  VAL A 892      -3.156  -7.413  17.815  1.00 53.63           C  
ANISOU 2438  CB  VAL A 892     5194   8471   6714  -2279   1085  -1240       C  
ATOM   2439  CG1 VAL A 892      -3.856  -7.245  16.468  1.00 54.04           C  
ANISOU 2439  CG1 VAL A 892     4995   8816   6724  -2268    908  -1420       C  
ATOM   2440  CG2 VAL A 892      -1.894  -8.281  17.687  1.00 37.69           C  
ANISOU 2440  CG2 VAL A 892     3571   6018   4733  -2373   1173  -1112       C  
ATOM   2441  N   SER A 893      -3.989  -3.965  17.929  1.00 47.39           N  
ANISOU 2441  N   SER A 893     3738   8352   5916  -1465    751  -1255       N  
ATOM   2442  CA  SER A 893      -5.156  -3.093  17.930  1.00 50.12           C  
ANISOU 2442  CA  SER A 893     3786   9038   6220  -1259    660  -1347       C  
ATOM   2443  C   SER A 893      -5.081  -2.165  16.732  1.00 47.80           C  
ANISOU 2443  C   SER A 893     3362   8891   5908   -936    436  -1344       C  
ATOM   2444  O   SER A 893      -4.035  -2.029  16.098  1.00 40.05           O  
ANISOU 2444  O   SER A 893     2535   7728   4956   -838    358  -1253       O  
ATOM   2445  CB  SER A 893      -5.253  -2.276  19.219  1.00 44.30           C  
ANISOU 2445  CB  SER A 893     3031   8299   5501  -1082    748  -1287       C  
ATOM   2446  OG  SER A 893      -4.308  -1.218  19.197  1.00 47.66           O  
ANISOU 2446  OG  SER A 893     3537   8598   5974   -757    676  -1175       O  
ATOM   2447  N   LYS A 894      -6.206  -1.505  16.441  1.00 46.18           N  
ANISOU 2447  N   LYS A 894     2906   9000   5641   -745    333  -1426       N  
ATOM   2448  CA  LYS A 894      -6.224  -0.510  15.375  1.00 47.94           C  
ANISOU 2448  CA  LYS A 894     3041   9355   5821   -375    127  -1387       C  
ATOM   2449  C   LYS A 894      -5.205   0.597  15.600  1.00 49.10           C  
ANISOU 2449  C   LYS A 894     3348   9268   6040    -31    100  -1222       C  
ATOM   2450  O   LYS A 894      -4.832   1.287  14.638  1.00 41.13           O  
ANISOU 2450  O   LYS A 894     2379   8247   5003    251    -52  -1143       O  
ATOM   2451  CB  LYS A 894      -7.616   0.106  15.251  1.00 47.47           C  
ANISOU 2451  CB  LYS A 894     2712   9647   5679   -188     53  -1479       C  
ATOM   2452  CG  LYS A 894      -8.654  -0.825  14.706  1.00 49.14           C  
ANISOU 2452  CG  LYS A 894     2731  10151   5789   -467     39  -1663       C  
ATOM   2453  CD  LYS A 894     -10.017  -0.178  14.771  1.00 59.67           C  
ANISOU 2453  CD  LYS A 894     3777  11851   7043   -274    -13  -1757       C  
ATOM   2454  CE  LYS A 894     -11.068  -1.086  14.174  1.00 67.92           C  
ANISOU 2454  CE  LYS A 894     4604  13229   7972   -553    -28  -1964       C  
ATOM   2455  NZ  LYS A 894     -12.366  -0.373  14.009  1.00 73.31           N  
ANISOU 2455  NZ  LYS A 894     4976  14324   8553   -312   -115  -2056       N  
ATOM   2456  N   ALA A 895      -4.756   0.777  16.849  1.00 37.89           N  
ANISOU 2456  N   ALA A 895     2042   7659   4695    -51    253  -1171       N  
ATOM   2457  CA  ALA A 895      -3.826   1.838  17.213  1.00 40.91           C  
ANISOU 2457  CA  ALA A 895     2615   7788   5140    248    256  -1040       C  
ATOM   2458  C   ALA A 895      -2.394   1.513  16.847  1.00 34.66           C  
ANISOU 2458  C   ALA A 895     2199   6592   4379    178    235   -896       C  
ATOM   2459  O   ALA A 895      -1.566   2.425  16.789  1.00 31.26           O  
ANISOU 2459  O   ALA A 895     1973   5920   3984    418    202   -781       O  
ATOM   2460  CB  ALA A 895      -3.892   2.121  18.718  1.00 40.94           C  
ANISOU 2460  CB  ALA A 895     2637   7737   5180    230    426  -1055       C  
ATOM   2461  N   ALA A 896      -2.079   0.241  16.633  1.00 34.32           N  
ANISOU 2461  N   ALA A 896     2254   6463   4323   -148    274   -911       N  
ATOM   2462  CA  ALA A 896      -0.714  -0.155  16.323  1.00 33.81           C  
ANISOU 2462  CA  ALA A 896     2526   6036   4285   -202    267   -784       C  
ATOM   2463  C   ALA A 896      -0.235   0.533  15.048  1.00 30.55           C  
ANISOU 2463  C   ALA A 896     2191   5566   3851     40    110   -712       C  
ATOM   2464  O   ALA A 896      -0.932   0.537  14.026  1.00 36.46           O  
ANISOU 2464  O   ALA A 896     2765   6560   4530     89     -7   -779       O  
ATOM   2465  CB  ALA A 896      -0.631  -1.675  16.178  1.00 42.72           C  
ANISOU 2465  CB  ALA A 896     3736   7098   5398   -567    343   -831       C  
ATOM   2466  N   TYR A 897       0.964   1.116  15.123  1.00 33.77           N  
ANISOU 2466  N   TYR A 897     2856   5670   4304    181    113   -580       N  
ATOM   2467  CA  TYR A 897       1.478   2.021  14.101  1.00 33.86           C  
ANISOU 2467  CA  TYR A 897     2976   5590   4300    435      6   -488       C  
ATOM   2468  C   TYR A 897       2.902   1.649  13.676  1.00 28.95           C  
ANISOU 2468  C   TYR A 897     2635   4668   3699    359     17   -391       C  
ATOM   2469  O   TYR A 897       3.193   1.561  12.476  1.00 32.81           O  
ANISOU 2469  O   TYR A 897     3188   5145   4133    397    -65   -357       O  
ATOM   2470  CB  TYR A 897       1.403   3.462  14.628  1.00 34.51           C  
ANISOU 2470  CB  TYR A 897     3067   5621   4425    726     25   -444       C  
ATOM   2471  CG  TYR A 897       1.962   4.506  13.702  1.00 44.80           C  
ANISOU 2471  CG  TYR A 897     4534   6771   5718    988    -41   -328       C  
ATOM   2472  CD1 TYR A 897       1.621   4.516  12.353  1.00 45.32           C  
ANISOU 2472  CD1 TYR A 897     4555   6978   5686   1100   -167   -295       C  
ATOM   2473  CD2 TYR A 897       2.821   5.490  14.172  1.00 40.81           C  
ANISOU 2473  CD2 TYR A 897     4237   5985   5284   1108     34   -257       C  
ATOM   2474  CE1 TYR A 897       2.127   5.468  11.496  1.00 49.17           C  
ANISOU 2474  CE1 TYR A 897     5226   7314   6143   1341   -206   -163       C  
ATOM   2475  CE2 TYR A 897       3.326   6.459  13.321  1.00 41.28           C  
ANISOU 2475  CE2 TYR A 897     4477   5872   5334   1320     10   -145       C  
ATOM   2476  CZ  TYR A 897       2.976   6.439  11.979  1.00 55.26           C  
ANISOU 2476  CZ  TYR A 897     6224   7770   7002   1444   -106    -83       C  
ATOM   2477  OH  TYR A 897       3.475   7.387  11.113  1.00 52.33           O  
ANISOU 2477  OH  TYR A 897     6063   7218   6600   1656   -112     54       O  
ATOM   2478  N   VAL A 898       3.805   1.424  14.624  1.00 26.52           N  
ANISOU 2478  N   VAL A 898     2479   4145   3450    265    115   -349       N  
ATOM   2479  CA  VAL A 898       5.152   0.961  14.278  1.00 23.35           C  
ANISOU 2479  CA  VAL A 898     2301   3505   3064    197    130   -273       C  
ATOM   2480  C   VAL A 898       5.451  -0.302  15.079  1.00 28.37           C  
ANISOU 2480  C   VAL A 898     3000   4067   3710    -27    222   -284       C  
ATOM   2481  O   VAL A 898       5.251  -0.322  16.291  1.00 30.17           O  
ANISOU 2481  O   VAL A 898     3197   4316   3951    -71    298   -294       O  
ATOM   2482  CB  VAL A 898       6.234   2.029  14.547  1.00 27.61           C  
ANISOU 2482  CB  VAL A 898     2991   3847   3654    346    153   -194       C  
ATOM   2483  CG1 VAL A 898       7.629   1.464  14.271  1.00 27.12           C  
ANISOU 2483  CG1 VAL A 898     3107   3595   3604    265    176   -135       C  
ATOM   2484  CG2 VAL A 898       6.011   3.259  13.668  1.00 25.41           C  
ANISOU 2484  CG2 VAL A 898     2720   3574   3362    573     93   -153       C  
ATOM   2485  N   LEU A 899       5.920  -1.356  14.412  1.00 26.22           N  
ANISOU 2485  N   LEU A 899     2838   3703   3421   -155    226   -279       N  
ATOM   2486  CA  LEU A 899       6.229  -2.633  15.055  1.00 27.88           C  
ANISOU 2486  CA  LEU A 899     3161   3796   3636   -341    329   -269       C  
ATOM   2487  C   LEU A 899       7.732  -2.876  15.042  1.00 29.82           C  
ANISOU 2487  C   LEU A 899     3610   3820   3902   -278    348   -172       C  
ATOM   2488  O   LEU A 899       8.363  -2.757  13.994  1.00 27.33           O  
ANISOU 2488  O   LEU A 899     3359   3442   3583   -213    297   -158       O  
ATOM   2489  CB  LEU A 899       5.540  -3.792  14.341  1.00 25.67           C  
ANISOU 2489  CB  LEU A 899     2864   3564   3324   -552    350   -363       C  
ATOM   2490  CG  LEU A 899       4.131  -3.554  13.795  1.00 39.72           C  
ANISOU 2490  CG  LEU A 899     4396   5634   5061   -607    285   -494       C  
ATOM   2491  CD1 LEU A 899       3.621  -4.824  13.137  1.00 32.72           C  
ANISOU 2491  CD1 LEU A 899     3515   4777   4139   -874    324   -619       C  
ATOM   2492  CD2 LEU A 899       3.212  -3.112  14.915  1.00 40.30           C  
ANISOU 2492  CD2 LEU A 899     4289   5876   5145   -614    334   -526       C  
ATOM   2493  N   PHE A 900       8.303  -3.243  16.184  1.00 27.12           N  
ANISOU 2493  N   PHE A 900     3356   3387   3562   -289    422   -107       N  
ATOM   2494  CA  PHE A 900       9.705  -3.636  16.282  1.00 22.47           C  
ANISOU 2494  CA  PHE A 900     2926   2635   2976   -217    440    -22       C  
ATOM   2495  C   PHE A 900       9.747  -5.139  16.501  1.00 28.24           C  
ANISOU 2495  C   PHE A 900     3809   3234   3685   -334    538     12       C  
ATOM   2496  O   PHE A 900       9.204  -5.628  17.513  1.00 26.05           O  
ANISOU 2496  O   PHE A 900     3554   2967   3378   -425    622     36       O  
ATOM   2497  CB  PHE A 900      10.432  -2.952  17.447  1.00 22.33           C  
ANISOU 2497  CB  PHE A 900     2900   2636   2947   -109    441     31       C  
ATOM   2498  CG  PHE A 900      10.802  -1.510  17.213  1.00 22.89           C  
ANISOU 2498  CG  PHE A 900     2893   2752   3050      5    376      1       C  
ATOM   2499  CD1 PHE A 900       9.854  -0.578  16.870  1.00 24.60           C  
ANISOU 2499  CD1 PHE A 900     3002   3056   3290     32    343    -58       C  
ATOM   2500  CD2 PHE A 900      12.119  -1.090  17.393  1.00 23.64           C  
ANISOU 2500  CD2 PHE A 900     3027   2805   3152     88    362     28       C  
ATOM   2501  CE1 PHE A 900      10.213   0.757  16.663  1.00 29.10           C  
ANISOU 2501  CE1 PHE A 900     3555   3610   3893    144    314    -72       C  
ATOM   2502  CE2 PHE A 900      12.476   0.250  17.217  1.00 24.55           C  
ANISOU 2502  CE2 PHE A 900     3098   2927   3302    149    337    -13       C  
ATOM   2503  CZ  PHE A 900      11.523   1.161  16.843  1.00 26.22           C  
ANISOU 2503  CZ  PHE A 900     3254   3165   3542    178    323    -54       C  
ATOM   2504  N   TYR A 901      10.434  -5.843  15.586  1.00 23.34           N  
ANISOU 2504  N   TYR A 901     3318   2476   3076   -323    547     18       N  
ATOM   2505  CA  TYR A 901      10.672  -7.281  15.624  1.00 23.98           C  
ANISOU 2505  CA  TYR A 901     3600   2364   3148   -396    657     52       C  
ATOM   2506  C   TYR A 901      12.168  -7.540  15.749  1.00 29.84           C  
ANISOU 2506  C   TYR A 901     4466   2985   3886   -200    661    154       C  
ATOM   2507  O   TYR A 901      12.970  -6.839  15.139  1.00 31.45           O  
ANISOU 2507  O   TYR A 901     4606   3238   4107    -79    585    144       O  
ATOM   2508  CB  TYR A 901      10.149  -7.955  14.358  1.00 24.51           C  
ANISOU 2508  CB  TYR A 901     3711   2379   3223   -546    676    -66       C  
ATOM   2509  CG  TYR A 901       8.654  -8.173  14.329  1.00 28.93           C  
ANISOU 2509  CG  TYR A 901     4164   3057   3772   -784    707   -184       C  
ATOM   2510  CD1 TYR A 901       8.096  -9.285  14.933  1.00 25.08           C  
ANISOU 2510  CD1 TYR A 901     3801   2447   3280   -984    859   -192       C  
ATOM   2511  CD2 TYR A 901       7.810  -7.300  13.656  1.00 29.83           C  
ANISOU 2511  CD2 TYR A 901     4053   3409   3870   -808    594   -288       C  
ATOM   2512  CE1 TYR A 901       6.733  -9.525  14.897  1.00 35.14           C  
ANISOU 2512  CE1 TYR A 901     4949   3857   4544  -1244    904   -327       C  
ATOM   2513  CE2 TYR A 901       6.435  -7.523  13.620  1.00 33.65           C  
ANISOU 2513  CE2 TYR A 901     4389   4061   4334  -1021    614   -417       C  
ATOM   2514  CZ  TYR A 901       5.907  -8.647  14.247  1.00 28.47           C  
ANISOU 2514  CZ  TYR A 901     3833   3301   3683  -1260    773   -449       C  
ATOM   2515  OH  TYR A 901       4.547  -8.892  14.228  1.00 32.83           O  
ANISOU 2515  OH  TYR A 901     4212   4048   4216  -1512    812   -601       O  
ATOM   2516  N   GLN A 902      12.554  -8.531  16.544  1.00 29.31           N  
ANISOU 2516  N   GLN A 902     4575   2775   3788   -159    758    257       N  
ATOM   2517  CA  GLN A 902      13.958  -8.910  16.674  1.00 33.76           C  
ANISOU 2517  CA  GLN A 902     5241   3252   4334     64    761    356       C  
ATOM   2518  C   GLN A 902      14.143 -10.338  16.184  1.00 34.91           C  
ANISOU 2518  C   GLN A 902     5640   3133   4490     57    887    376       C  
ATOM   2519  O   GLN A 902      13.356 -11.234  16.524  1.00 31.31           O  
ANISOU 2519  O   GLN A 902     5347   2524   4025    -96   1012    391       O  
ATOM   2520  CB  GLN A 902      14.479  -8.778  18.113  1.00 32.37           C  
ANISOU 2520  CB  GLN A 902     5062   3158   4081    210    750    486       C  
ATOM   2521  CG  GLN A 902      15.999  -8.975  18.210  1.00 38.10           C  
ANISOU 2521  CG  GLN A 902     5813   3890   4773    475    715    568       C  
ATOM   2522  CD  GLN A 902      16.533  -8.894  19.630  1.00 47.97           C  
ANISOU 2522  CD  GLN A 902     7045   5272   5910    635    685    689       C  
ATOM   2523  OE1 GLN A 902      15.774  -8.711  20.579  1.00 47.48           O  
ANISOU 2523  OE1 GLN A 902     6977   5274   5789    543    704    719       O  
ATOM   2524  NE2 GLN A 902      17.849  -9.046  19.782  1.00 51.81           N  
ANISOU 2524  NE2 GLN A 902     7508   5830   6349    883    637    751       N  
ATOM   2525  N   ARG A 903      15.183 -10.545  15.389  1.00 30.34           N  
ANISOU 2525  N   ARG A 903     5103   2492   3931    213    875    367       N  
ATOM   2526  CA  ARG A 903      15.403 -11.841  14.769  1.00 35.12           C  
ANISOU 2526  CA  ARG A 903     5959   2829   4556    225   1004    356       C  
ATOM   2527  C   ARG A 903      15.872 -12.841  15.815  1.00 34.70           C  
ANISOU 2527  C   ARG A 903     6135   2592   4457    394   1113    529       C  
ATOM   2528  O   ARG A 903      16.763 -12.541  16.613  1.00 40.55           O  
ANISOU 2528  O   ARG A 903     6808   3456   5143    638   1048    653       O  
ATOM   2529  CB  ARG A 903      16.437 -11.715  13.645  1.00 29.72           C  
ANISOU 2529  CB  ARG A 903     5238   2158   3895    372    969    292       C  
ATOM   2530  CG  ARG A 903      16.243 -12.732  12.522  1.00 42.44           C  
ANISOU 2530  CG  ARG A 903     7052   3541   5532    275   1085    177       C  
ATOM   2531  CD  ARG A 903      17.131 -12.399  11.321  1.00 48.11           C  
ANISOU 2531  CD  ARG A 903     7692   4332   6255    388   1045     91       C  
ATOM   2532  NE  ARG A 903      18.542 -12.285  11.677  1.00 43.35           N  
ANISOU 2532  NE  ARG A 903     7035   3792   5645    694   1026    194       N  
ATOM   2533  CZ  ARG A 903      19.397 -11.433  11.114  1.00 45.41           C  
ANISOU 2533  CZ  ARG A 903     7101   4249   5901    792    952    158       C  
ATOM   2534  NH1 ARG A 903      19.000 -10.595  10.158  1.00 38.41           N  
ANISOU 2534  NH1 ARG A 903     6096   3488   5011    631    893     51       N  
ATOM   2535  NH2 ARG A 903      20.658 -11.414  11.509  1.00 47.65           N  
ANISOU 2535  NH2 ARG A 903     7308   4622   6175   1053    944    232       N  
ATOM   2536  N   GLN A 904      15.275 -14.038  15.793  1.00 36.90           N  
ANISOU 2536  N   GLN A 904     6629   2655   4735    256   1252    512       N  
ATOM   2537  CA  GLN A 904      15.519 -15.028  16.840  1.00 43.50           C  
ANISOU 2537  CA  GLN A 904     7640   3386   5501    382   1337    659       C  
ATOM   2538  C   GLN A 904      16.994 -15.405  16.943  1.00 53.49           C  
ANISOU 2538  C   GLN A 904     8932   4666   6724    744   1304    760       C  
ATOM   2539  O   GLN A 904      17.513 -15.589  18.046  1.00 58.41           O  
ANISOU 2539  O   GLN A 904     9589   5345   7261    952   1291    920       O  
ATOM   2540  CB  GLN A 904      14.653 -16.265  16.599  1.00 46.12           C  
ANISOU 2540  CB  GLN A 904     8183   3491   5847    151   1500    585       C  
ATOM   2541  CG  GLN A 904      13.165 -15.971  16.726  1.00 43.81           C  
ANISOU 2541  CG  GLN A 904     7831   3239   5576   -211   1541    487       C  
ATOM   2542  CD  GLN A 904      12.278 -17.161  16.415  1.00 49.65           C  
ANISOU 2542  CD  GLN A 904     8748   3789   6329   -473   1705    377       C  
ATOM   2543  OE1 GLN A 904      12.759 -18.239  16.061  1.00 53.81           O  
ANISOU 2543  OE1 GLN A 904     9477   4116   6854   -389   1803    375       O  
ATOM   2544  NE2 GLN A 904      10.965 -16.967  16.541  1.00 46.27           N  
ANISOU 2544  NE2 GLN A 904     8232   3439   5910   -800   1745    272       N  
ATOM   2545  N   ASP A 905      17.700 -15.490  15.818  1.00 53.71           N  
ANISOU 2545  N   ASP A 905     8926   4680   6799    829   1286    664       N  
ATOM   2546  CA  ASP A 905      19.104 -15.877  15.913  1.00 52.97           C  
ANISOU 2546  CA  ASP A 905     8831   4632   6664   1169   1264    748       C  
ATOM   2547  C   ASP A 905      20.004 -14.771  16.453  1.00 55.93           C  
ANISOU 2547  C   ASP A 905     8958   5296   6998   1387   1113    817       C  
ATOM   2548  O   ASP A 905      21.189 -15.031  16.690  1.00 60.84           O  
ANISOU 2548  O   ASP A 905     9530   6021   7567   1675   1079    886       O  
ATOM   2549  CB  ASP A 905      19.616 -16.344  14.549  1.00 55.60           C  
ANISOU 2549  CB  ASP A 905     9201   4875   7051   1192   1309    619       C  
ATOM   2550  CG  ASP A 905      19.159 -15.452  13.427  1.00 75.42           C  
ANISOU 2550  CG  ASP A 905    11572   7456   9626    987   1256    452       C  
ATOM   2551  OD1 ASP A 905      18.014 -14.969  13.500  1.00 83.34           O  
ANISOU 2551  OD1 ASP A 905    12553   8461  10651    731   1245    400       O  
ATOM   2552  OD2 ASP A 905      19.937 -15.229  12.478  1.00 78.06           O  
ANISOU 2552  OD2 ASP A 905    11822   7857   9982   1086   1232    372       O  
ATOM   2553  N   THR A 906      19.488 -13.555  16.651  1.00 51.33           N  
ANISOU 2553  N   THR A 906     8210   4859   6434   1260   1026    792       N  
ATOM   2554  CA  THR A 906      20.268 -12.458  17.210  1.00 52.13           C  
ANISOU 2554  CA  THR A 906     8073   5242   6493   1441    892    839       C  
ATOM   2555  C   THR A 906      19.984 -12.214  18.690  1.00 57.41           C  
ANISOU 2555  C   THR A 906     8732   6029   7053   1484    849    979       C  
ATOM   2556  O   THR A 906      20.584 -11.312  19.283  1.00 60.32           O  
ANISOU 2556  O   THR A 906     8853   6708   7359   1571    715    972       O  
ATOM   2557  CB  THR A 906      20.006 -11.167  16.422  1.00 48.39           C  
ANISOU 2557  CB  THR A 906     7355   4940   6091   1235    800    675       C  
ATOM   2558  OG1 THR A 906      18.675 -10.703  16.690  1.00 56.64           O  
ANISOU 2558  OG1 THR A 906     8387   5982   7150    956    793    636       O  
ATOM   2559  CG2 THR A 906      20.180 -11.408  14.910  1.00 39.17           C  
ANISOU 2559  CG2 THR A 906     6230   3651   5003   1186    856    549       C  
ATOM   2560  N   PHE A 907      19.083 -12.983  19.292  1.00 57.28           N  
ANISOU 2560  N   PHE A 907     8927   5837   7000   1356    951   1051       N  
ATOM   2561  CA  PHE A 907      18.740 -12.784  20.694  1.00 56.88           C  
ANISOU 2561  CA  PHE A 907     8888   5900   6824   1379    932   1185       C  
ATOM   2562  C   PHE A 907      19.980 -12.885  21.571  1.00 58.13           C  
ANISOU 2562  C   PHE A 907     8963   6282   6842   1719    837   1299       C  
ATOM   2563  O   PHE A 907      20.807 -13.785  21.404  1.00 57.17           O  
ANISOU 2563  O   PHE A 907     8917   6103   6703   1920    866   1332       O  
ATOM   2564  CB  PHE A 907      17.703 -13.817  21.134  1.00 59.96           C  
ANISOU 2564  CB  PHE A 907     9531   6054   7198   1195   1088   1234       C  
ATOM   2565  CG  PHE A 907      16.326 -13.579  20.579  1.00 60.97           C  
ANISOU 2565  CG  PHE A 907     9678   6063   7424    825   1165   1112       C  
ATOM   2566  CD1 PHE A 907      15.977 -12.348  20.052  1.00 51.01           C  
ANISOU 2566  CD1 PHE A 907     8171   4980   6230    679   1062    975       C  
ATOM   2567  CD2 PHE A 907      15.374 -14.588  20.594  1.00 68.88           C  
ANISOU 2567  CD2 PHE A 907    10877   6846   8447    604   1319   1088       C  
ATOM   2568  CE1 PHE A 907      14.708 -12.122  19.548  1.00 48.13           C  
ANISOU 2568  CE1 PHE A 907     7756   4590   5942    352   1102    834       C  
ATOM   2569  CE2 PHE A 907      14.100 -14.368  20.088  1.00 63.87           C  
ANISOU 2569  CE2 PHE A 907    10208   6168   7892    253   1380    948       C  
ATOM   2570  CZ  PHE A 907      13.770 -13.123  19.563  1.00 48.18           C  
ANISOU 2570  CZ  PHE A 907     7993   4352   5962    139   1280    841       C  
ATOM   2571  N   SER A 908      20.118 -11.950  22.501  1.00 67.66           N  
ANISOU 2571  N   SER A 908    10000   7775   7935   1784    721   1347       N  
ATOM   2572  CA  SER A 908      21.234 -12.004  23.430  1.00 72.09           C  
ANISOU 2572  CA  SER A 908    10444   8616   8332   2082    612   1429       C  
ATOM   2573  C   SER A 908      21.062 -13.191  24.367  1.00 77.71           C  
ANISOU 2573  C   SER A 908    11404   9195   8927   2172    709   1584       C  
ATOM   2574  O   SER A 908      19.982 -13.405  24.925  1.00 82.68           O  
ANISOU 2574  O   SER A 908    12200   9686   9528   1985    805   1644       O  
ATOM   2575  CB  SER A 908      21.335 -10.706  24.228  1.00 77.37           C  
ANISOU 2575  CB  SER A 908    10835   9667   8897   2042    459   1368       C  
ATOM   2576  OG  SER A 908      22.496 -10.700  25.041  1.00 81.44           O  
ANISOU 2576  OG  SER A 908    11207  10506   9232   2352    334   1436       O  
ATOM   2577  N   GLY A 909      22.120 -13.981  24.512  1.00 77.33           N  
ANISOU 2577  N   GLY A 909    11382   9186   8813   2457    697   1647       N  
ATOM   2578  CA  GLY A 909      22.163 -15.009  25.525  1.00 79.94           C  
ANISOU 2578  CA  GLY A 909    11928   9442   9003   2615    768   1814       C  
ATOM   2579  C   GLY A 909      21.526 -16.334  25.170  1.00 80.78           C  
ANISOU 2579  C   GLY A 909    12385   9118   9190   2526    975   1869       C  
ATOM   2580  O   GLY A 909      21.603 -17.264  25.980  1.00 89.74           O  
ANISOU 2580  O   GLY A 909    13729  10158  10210   2678   1053   2021       O  
ATOM   2581  N   THR A 910      20.893 -16.465  24.005  1.00 73.63           N  
ANISOU 2581  N   THR A 910    11554   7957   8464   2282   1069   1744       N  
ATOM   2582  CA  THR A 910      20.343 -17.749  23.591  1.00 75.21           C  
ANISOU 2582  CA  THR A 910    12070   7771   8735   2179   1266   1757       C  
ATOM   2583  C   THR A 910      20.785 -18.077  22.171  1.00 72.08           C  
ANISOU 2583  C   THR A 910    11671   7238   8475   2182   1299   1623       C  
ATOM   2584  O   THR A 910      20.858 -17.195  21.309  1.00 81.67           O  
ANISOU 2584  O   THR A 910    12676   8567   9786   2079   1212   1482       O  
ATOM   2585  CB  THR A 910      18.803 -17.786  23.697  1.00 75.70           C  
ANISOU 2585  CB  THR A 910    12266   7641   8855   1793   1387   1720       C  
ATOM   2586  OG1 THR A 910      18.326 -19.077  23.298  1.00 87.56           O  
ANISOU 2586  OG1 THR A 910    14066   8786  10416   1684   1584   1711       O  
ATOM   2587  CG2 THR A 910      18.169 -16.745  22.820  1.00 68.58           C  
ANISOU 2587  CG2 THR A 910    11171   6804   8083   1517   1329   1545       C  
ATOM   2588  N   GLY A 911      21.096 -19.353  21.945  1.00 71.55           N  
ANISOU 2588  N   GLY A 911    11853   6926   8408   2311   1435   1671       N  
ATOM   2589  CA  GLY A 911      21.575 -19.813  20.658  1.00 72.17           C  
ANISOU 2589  CA  GLY A 911    11961   6869   8590   2341   1485   1554       C  
ATOM   2590  C   GLY A 911      20.647 -20.803  19.987  1.00 66.64           C  
ANISOU 2590  C   GLY A 911    11546   5791   7981   2083   1684   1475       C  
ATOM   2591  O   GLY A 911      20.380 -21.883  20.524  1.00 57.90           O  
ANISOU 2591  O   GLY A 911    10730   4446   6825   2116   1838   1580       O  
ATOM   2592  N   PHE A 912      20.164 -20.447  18.799  1.00 73.06           N  
ANISOU 2592  N   PHE A 912    12281   6558   8920   1825   1685   1284       N  
ATOM   2593  CA  PHE A 912      19.214 -21.273  18.061  1.00 76.73           C  
ANISOU 2593  CA  PHE A 912    12970   6719   9466   1532   1858   1163       C  
ATOM   2594  C   PHE A 912      19.917 -22.289  17.170  1.00 81.71           C  
ANISOU 2594  C   PHE A 912    13769   7151  10128   1680   1964   1115       C  
ATOM   2595  O   PHE A 912      19.309 -22.845  16.254  1.00 87.32           O  
ANISOU 2595  O   PHE A 912    14614   7651  10911   1442   2084    966       O  
ATOM   2596  CB  PHE A 912      18.292 -20.391  17.216  1.00 78.47           C  
ANISOU 2596  CB  PHE A 912    13014   7017   9782   1180   1801    970       C  
ATOM   2597  CG  PHE A 912      17.250 -19.666  18.015  1.00 76.80           C  
ANISOU 2597  CG  PHE A 912    12713   6913   9555    955   1762    992       C  
ATOM   2598  CD1 PHE A 912      17.606 -18.652  18.891  1.00 78.15           C  
ANISOU 2598  CD1 PHE A 912    12686   7344   9663   1101   1615   1101       C  
ATOM   2599  CD2 PHE A 912      15.911 -19.993  17.887  1.00 84.03           C  
ANISOU 2599  CD2 PHE A 912    13729   7689  10511    589   1879    890       C  
ATOM   2600  CE1 PHE A 912      16.647 -17.982  19.631  1.00 71.16           C  
ANISOU 2600  CE1 PHE A 912    11725   6556   8756    898   1591   1122       C  
ATOM   2601  CE2 PHE A 912      14.945 -19.323  18.623  1.00 84.13           C  
ANISOU 2601  CE2 PHE A 912    13640   7819  10505    381   1852    905       C  
ATOM   2602  CZ  PHE A 912      15.315 -18.314  19.494  1.00 76.91           C  
ANISOU 2602  CZ  PHE A 912    12547   7144   9529    542   1712   1027       C  
TER    2603      PHE A 912                                                      
HETATM 2604 ZN    ZN A1001      13.442   4.821 -21.236  1.00 60.03          ZN  
HETATM 2605  O   HOH A1101      22.422  14.698  28.000  1.00 39.66           O  
HETATM 2606  O   HOH A1102      23.157 -14.691  -1.749  1.00 39.48           O  
HETATM 2607  O   HOH A1103      23.124   9.262  32.465  1.00 44.58           O  
HETATM 2608  O   HOH A1104      10.194  -9.640  -1.320  1.00 56.42           O  
HETATM 2609  O   HOH A1105      33.301   0.794  -4.392  1.00 50.30           O  
HETATM 2610  O   HOH A1106      27.916  -1.620  10.107  1.00 39.64           O  
HETATM 2611  O   HOH A1107       4.123   8.519  25.175  1.00 33.91           O  
HETATM 2612  O   HOH A1108      19.231  -2.955 -14.659  1.00 60.26           O  
HETATM 2613  O   HOH A1109      11.434  -1.900  29.722  1.00 25.50           O  
HETATM 2614  O   HOH A1110      14.716  -4.834  34.264  1.00 48.12           O  
HETATM 2615  O   HOH A1111       5.657   6.966  36.489  1.00 51.61           O  
HETATM 2616  O   HOH A1112       1.120   3.122  31.533  1.00 38.17           O  
HETATM 2617  O   HOH A1113      16.562  -0.377  -4.467  1.00 48.43           O  
HETATM 2618  O   HOH A1114       3.406  -7.249  32.356  1.00 60.89           O  
HETATM 2619  O   HOH A1115       3.402  12.093  31.911  1.00 47.53           O  
HETATM 2620  O   HOH A1116       6.345  -0.118  -5.397  1.00 61.76           O  
HETATM 2621  O   HOH A1117     -14.404  -1.893  14.319  1.00 72.22           O  
HETATM 2622  O   HOH A1118      31.622  22.096  11.783  1.00 55.61           O  
HETATM 2623  O   HOH A1119      31.310   9.651   8.313  1.00 52.52           O  
HETATM 2624  O   HOH A1120      28.573   7.924  -3.535  1.00 51.93           O  
HETATM 2625  O   HOH A1121      -1.097 -11.790  17.113  1.00 57.70           O  
HETATM 2626  O   HOH A1122      -1.807  -1.479  19.836  1.00 45.69           O  
HETATM 2627  O   HOH A1123      18.460   1.880  23.139  1.00 28.04           O  
HETATM 2628  O   HOH A1124      20.314  13.095  27.783  1.00 27.41           O  
HETATM 2629  O   HOH A1125      24.267  -6.958  11.628  1.00 46.06           O  
HETATM 2630  O   HOH A1126      -3.277  -3.007  13.799  1.00 39.42           O  
HETATM 2631  O   HOH A1127      -2.797  -8.707  20.907  1.00 42.26           O  
HETATM 2632  O   HOH A1128      12.482  -5.830  -7.622  1.00 39.37           O  
HETATM 2633  O   HOH A1129      28.662  -7.697   0.923  1.00 57.51           O  
HETATM 2634  O   HOH A1130      16.634  22.041  19.623  1.00 43.36           O  
HETATM 2635  O   HOH A1131      28.885  13.166  14.100  1.00 32.93           O  
HETATM 2636  O   HOH A1132      29.019   2.684  15.780  1.00 33.66           O  
HETATM 2637  O   HOH A1133      13.100   2.132  -5.044  1.00 53.31           O  
HETATM 2638  O   HOH A1134      24.497  16.187  24.279  1.00 52.85           O  
HETATM 2639  O   HOH A1135      29.580  -8.223  -6.134  1.00 43.46           O  
HETATM 2640  O   HOH A1136       5.449   6.183  25.703  1.00 30.52           O  
HETATM 2641  O   HOH A1137       7.133  -0.077 -18.155  1.00 66.54           O  
HETATM 2642  O   HOH A1138      22.158  -4.981   9.454  1.00 37.14           O  
HETATM 2643  O   HOH A1139      20.703 -17.128  18.633  1.00 71.44           O  
HETATM 2644  O   HOH A1140      25.011  15.438  27.023  1.00 79.19           O  
HETATM 2645  O   HOH A1141      20.711  -8.131 -10.912  1.00 45.28           O  
HETATM 2646  O   HOH A1142      13.088  -5.956  24.650  1.00 28.91           O  
HETATM 2647  O   HOH A1143      24.946  -2.653  -6.569  1.00 46.20           O  
HETATM 2648  O   HOH A1144       6.545  12.474  22.702  1.00 36.04           O  
HETATM 2649  O   HOH A1145      15.827   4.085  36.209  1.00 34.45           O  
HETATM 2650  O   HOH A1146       8.817  -3.237 -12.557  1.00 51.73           O  
HETATM 2651  O   HOH A1147       1.928  11.909  22.246  1.00 44.64           O  
HETATM 2652  O   HOH A1148       6.412  -3.505  -5.347  1.00 46.25           O  
HETATM 2653  O   HOH A1149       7.549 -11.535  21.689  1.00 32.89           O  
HETATM 2654  O   HOH A1150      12.281   1.607  28.640  1.00 31.18           O  
HETATM 2655  O   HOH A1151      20.340   4.888   9.870  1.00 34.52           O  
HETATM 2656  O   HOH A1152      15.987   0.619  -9.820  1.00 39.50           O  
HETATM 2657  O   HOH A1153      20.812  -3.828  31.673  1.00 69.70           O  
HETATM 2658  O   HOH A1154      15.721 -16.358  12.742  1.00 45.18           O  
HETATM 2659  O   HOH A1155      22.589   2.893  34.144  1.00 52.27           O  
HETATM 2660  O   HOH A1156      23.879 -10.301   0.068  1.00 44.42           O  
HETATM 2661  O   HOH A1157       9.886 -13.409  34.314  1.00 54.09           O  
HETATM 2662  O   HOH A1158       4.150  11.737  23.840  1.00 55.06           O  
HETATM 2663  O   HOH A1159      14.531  -2.307  10.468  1.00 26.75           O  
HETATM 2664  O   HOH A1160      -2.789   3.826  14.593  1.00 35.84           O  
HETATM 2665  O   HOH A1161      -8.711  -2.282  17.589  1.00 55.99           O  
HETATM 2666  O   HOH A1162       8.659 -14.821  22.960  1.00 48.49           O  
HETATM 2667  O   HOH A1163       2.023   7.108   7.964  1.00 49.86           O  
HETATM 2668  O   HOH A1164      17.689  16.049  29.765  1.00 67.29           O  
HETATM 2669  O   HOH A1165      13.409   2.432  36.133  1.00 37.72           O  
HETATM 2670  O   HOH A1166      18.116 -10.014  23.245  1.00 50.56           O  
HETATM 2671  O   HOH A1167      25.051  -4.708  21.018  1.00 39.72           O  
HETATM 2672  O   HOH A1168      33.222  -0.567   6.543  1.00 42.77           O  
HETATM 2673  O   HOH A1169       8.793  14.377  25.335  1.00 52.09           O  
HETATM 2674  O   HOH A1170      25.485   7.012   1.965  1.00 42.57           O  
HETATM 2675  O   HOH A1171      10.991   2.703  -2.778  1.00 57.20           O  
HETATM 2676  O   HOH A1172      28.605  -3.030 -18.592  1.00 70.41           O  
HETATM 2677  O   HOH A1173       7.045   6.783  27.744  1.00 31.28           O  
HETATM 2678  O   HOH A1174      22.839  15.544   8.273  1.00 45.19           O  
HETATM 2679  O   HOH A1175       4.744 -15.726   9.988  1.00 56.48           O  
HETATM 2680  O   HOH A1176      35.595   3.853   3.418  1.00 44.26           O  
HETATM 2681  O   HOH A1177       7.703   3.835  36.658  1.00 94.96           O  
HETATM 2682  O   HOH A1178      32.413  12.348   5.125  1.00 36.42           O  
HETATM 2683  O   HOH A1179       0.500 -11.854   9.186  1.00 37.14           O  
HETATM 2684  O   HOH A1180      14.466   3.195   5.539  1.00 36.69           O  
HETATM 2685  O   HOH A1181       3.782  -8.456  -8.592  1.00 52.03           O  
HETATM 2686  O   HOH A1182      37.438   6.746   6.885  1.00 52.40           O  
HETATM 2687  O   HOH A1183      14.009  -4.286  26.850  1.00 26.29           O  
HETATM 2688  O   HOH A1184      24.529   1.009  -1.930  1.00 46.41           O  
HETATM 2689  O   HOH A1185      16.536  -3.319  25.843  1.00 26.99           O  
HETATM 2690  O   HOH A1186      -6.118   4.122  17.276  1.00 59.57           O  
HETATM 2691  O   HOH A1187       6.520 -12.090  24.046  1.00 40.22           O  
HETATM 2692  O   HOH A1188      32.997  -2.362   2.345  1.00 58.98           O  
HETATM 2693  O   HOH A1189      24.380   3.831   0.825  1.00 44.78           O  
HETATM 2694  O   HOH A1190      17.709  13.809  27.619  1.00 32.77           O  
HETATM 2695  O   HOH A1191      19.921  -8.985  21.952  1.00 53.72           O  
HETATM 2696  O   HOH A1192      25.464   9.513   3.267  1.00 46.10           O  
HETATM 2697  O   HOH A1193       0.341  -1.709  36.247  1.00 51.25           O  
HETATM 2698  O   HOH A1194      29.146   4.937  32.824  1.00 75.15           O  
HETATM 2699  O   HOH A1195      20.227  12.648  30.502  1.00 61.67           O  
HETATM 2700  O   HOH A1196       4.530  14.109  31.881  1.00 60.48           O  
HETATM 2701  O   HOH A1197       5.247   9.936  22.002  1.00 39.15           O  
HETATM 2702  O   HOH A1198      21.860  -9.439   9.524  1.00 55.45           O  
HETATM 2703  O   HOH A1199      19.767 -12.461 -11.337  1.00 47.53           O  
HETATM 2704  O   HOH A1200      18.678 -11.662   5.764  1.00 54.98           O  
HETATM 2705  O   HOH A1201      -9.017   8.524   6.197  1.00 50.64           O  
HETATM 2706  O   HOH A1202     -10.274   4.739   8.429  1.00 73.08           O  
HETATM 2707  O   HOH A1203      22.531  -1.330  -7.045  1.00 43.37           O  
HETATM 2708  O   HOH A1204      -3.797  -0.747  28.732  1.00 45.57           O  
HETATM 2709  O   HOH A1205      22.104  13.280   6.958  1.00 55.91           O  
HETATM 2710  O   HOH A1206       1.665 -14.861  18.059  1.00 42.91           O  
HETATM 2711  O   HOH A1207       8.253  14.693  40.640  1.00 76.11           O  
HETATM 2712  O   HOH A1208      35.554   5.477  -8.492  1.00 80.24           O  
HETATM 2713  O   HOH A1209      30.884  -0.632  -7.383  1.00 69.99           O  
HETATM 2714  O   HOH A1210      19.338  -5.879 -15.389  1.00 63.65           O  
HETATM 2715  O   HOH A1211      12.604 -10.102  26.707  1.00 48.50           O  
HETATM 2716  O   HOH A1212      20.091  16.242   8.911  1.00 49.47           O  
HETATM 2717  O   HOH A1213      14.187 -12.292  28.249  1.00 60.56           O  
HETATM 2718  O   HOH A1214      -1.204 -14.244   4.966  1.00 66.92           O  
HETATM 2719  O   HOH A1215      10.409   1.000   2.544  1.00 44.51           O  
HETATM 2720  O   HOH A1216      22.653   5.305   5.847  1.00 41.03           O  
HETATM 2721  O   HOH A1217      35.366   4.548  15.291  1.00 50.58           O  
HETATM 2722  O   HOH A1218      19.199   4.087   4.809  1.00 50.09           O  
HETATM 2723  O   HOH A1219      18.103  -2.351  40.421  1.00 61.32           O  
HETATM 2724  O   HOH A1220      36.127  -0.146  19.018  1.00 62.90           O  
HETATM 2725  O   HOH A1221      13.491  -8.561  24.628  1.00 31.85           O  
HETATM 2726  O   HOH A1222      16.272  11.127   6.959  1.00 90.37           O  
HETATM 2727  O   HOH A1223      26.599 -10.713  23.477  1.00 73.36           O  
HETATM 2728  O   HOH A1224      23.577  -6.862  16.851  1.00 57.16           O  
HETATM 2729  O   HOH A1225      32.200   7.374 -12.208  1.00 58.37           O  
HETATM 2730  O   HOH A1226      19.555  15.623  31.054  1.00 59.18           O  
HETATM 2731  O   HOH A1227      36.007   6.289  29.555  1.00 59.67           O  
HETATM 2732  O   HOH A1228      -6.433   6.881  29.261  1.00 69.36           O  
HETATM 2733  O   HOH A1229      25.912 -11.048  17.222  1.00 95.81           O  
HETATM 2734  O   HOH A1230      39.400   3.231  27.735  1.00 68.09           O  
HETATM 2735  O   HOH A1231       6.070   6.855 -28.846  1.00 74.35           O  
CONECT 1253 2604                                                                
CONECT 1271 2604                                                                
CONECT 1616 2604                                                                
CONECT 1637 2604                                                                
CONECT 2604 1253 1271 1616 1637                                                 
MASTER      335    0    1   12   22    0    1    6 2716    1    5   29          
END                                                                             



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elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Last modification: October 18th, 2018.