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Browse entries in the PDBbind-CN Database

HEADER    STRUCTURAL PROTEIN/DNA                  09-MAY-18   5ZVA              
TITLE     APOBEC3F CHIMERIC CATALYTIC DOMAIN IN COMPLEX WITH DNA(DC9)           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: APEBEC3F/SSDNA-C9;                                         
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: APOBEC-RELATED CYTIDINE DEAMINASE,ARCD,APOBEC-RELATED       
COMPND   5 PROTEIN 9,ARP-9,CEM-15,CEM15,DEOXYCYTIDINE DEAMINASE,A3G,            
COMPND   6 APOLIPOPROTEIN B MRNA-EDITING ENZYME CATALYTIC POLYPEPTIDE-LIKE 3F,  
COMPND   7 A3F;                                                                 
COMPND   8 EC: 3.5.4.-,3.5.4.-;                                                 
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 OTHER_DETAILS: ALL RESIDURES INCLUDES PURIFICATION TAG OF            
COMPND  11 A3F(6HIS+THROMBIN CLEAVAGE TAG+ CHIMERIC A3F) (REFERENCE: K. SIU, ET 
COMPND  12 AL. NAT. COMMUN. 2013, 4, 2593. PDB CODE:4J4J),ALL RESIDURES INCLUDES
COMPND  13 PURIFICATION TAG OF A3F(6HIS+THROMBIN CLEAVAGE TAG+ CHIMERIC A3F)    
COMPND  14 (REFERENCE: K. SIU, ET AL. NAT. COMMUN. 2013, 4, 2593. PDB           
COMPND  15 CODE:4J4J);                                                          
COMPND  16 MOL_ID: 2;                                                           
COMPND  17 MOLECULE: DNA (5'-D(*AP*TP*TP*TP*TP*CP*AP*AP*CP*T)-3');              
COMPND  18 CHAIN: C;                                                            
COMPND  19 ENGINEERED: YES;                                                     
COMPND  20 OTHER_DETAILS: CHEMICALLY SYNTHESIZED                                
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: APOBEC3G, MDS019, APOBEC3F;                                    
SOURCE   6 EXPRESSION_SYSTEM: PROKARYOTIC ENVIRONMENTAL SAMPLES;                
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 81490;                                      
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 SYNTHETIC: YES;                                                      
SOURCE  10 ORGANISM_SCIENTIFIC: DNA-BINDING VECTOR PODB80;                      
SOURCE  11 ORGANISM_TAXID: 62978                                                
KEYWDS    APOBEC3F, HIV-1, DEAMINATION, STRUCTURAL PROTEIN-DNA COMPLEX          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.CHENG,T.L.ZHANG,C.X.WANG,W.X.LAN,J.P.DING,C.Y.CAO                   
REVDAT   2   28-NOV-18 5ZVA    1       TITLE  COMPND JRNL                       
REVDAT   1   21-NOV-18 5ZVA    0                                                
JRNL        AUTH   C.CHENG,T.ZHANG,C.WANG,W.LAN,J.DING,C.CAO                    
JRNL        TITL   CRYSTAL STRUCTURE OF CYTIDINE DEAMINASE HUMAN APOBEC3F       
JRNL        TITL 2 CHIMERIC CATALYTIC DOMAIN IN COMPLEX WITH DNA                
JRNL        REF    CHIN.J.CHEM.                  V.  36  1241 2018              
JRNL        REFN                   ISSN 1001-604X                               
JRNL        DOI    10.1002/CJOC.201800508                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
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) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.68                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 21994                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.164                           
REMARK   3   R VALUE            (WORKING SET) : 0.161                           
REMARK   3   FREE R VALUE                     : 0.208                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1158                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : NULL                                          
REMARK   3   SHRINKAGE RADIUS   : NULL                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.147            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL             
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 50.96                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.71000                                             
REMARK   3    B22 (A**2) : 2.18000                                              
REMARK   3    B33 (A**2) : 0.53000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
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  : 3                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID -32 THROUGH 373 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -22.3506  -5.4280  -4.0854              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0739 T22:   0.0009                                     
REMARK   3      T33:   0.0390 T12:   0.0001                                     
REMARK   3      T13:  -0.0052 T23:  -0.0007                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0768 L22:   0.1379                                     
REMARK   3      L33:   0.0540 L12:   0.0152                                     
REMARK   3      L13:  -0.0574 L23:  -0.0488                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0052 S12:  -0.0045 S13:   0.0073                       
REMARK   3      S21:   0.0048 S22:  -0.0070 S23:  -0.0087                       
REMARK   3      S31:  -0.0018 S32:   0.0050 S33:   0.0018                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID -29 THROUGH 373 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.2109 -28.4956  28.9230              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0714 T22:   0.0005                                     
REMARK   3      T33:   0.0385 T12:  -0.0009                                     
REMARK   3      T13:   0.0003 T23:  -0.0021                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0350 L22:   0.0862                                     
REMARK   3      L33:   0.1690 L12:  -0.0547                                     
REMARK   3      L13:   0.0039 L23:  -0.0158                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0037 S12:  -0.0033 S13:  -0.0017                       
REMARK   3      S21:   0.0041 S22:   0.0057 S23:  -0.0002                       
REMARK   3      S31:   0.0025 S32:  -0.0016 S33:  -0.0020                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 1 THROUGH 10 )                    
REMARK   3    ORIGIN FOR THE GROUP (A): -30.9308 -26.9196  12.6758              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1752 T22:   0.0457                                     
REMARK   3      T33:   0.0367 T12:  -0.0354                                     
REMARK   3      T13:   0.0297 T23:  -0.0023                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.5691 L22:   0.2317                                     
REMARK   3      L33:   1.7847 L12:   0.5800                                     
REMARK   3      L13:   2.2116 L23:  -0.2378                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0359 S12:   0.0257 S13:  -0.3485                       
REMARK   3      S21:  -0.1495 S22:  -0.0081 S23:  -0.0676                       
REMARK   3      S31:   0.3715 S32:   0.0420 S33:  -0.0277                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: U VALUES : WITH TLS ADDED                 
REMARK   4                                                                      
REMARK   4 5ZVA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-MAY-18.                  
REMARK 100 THE DEPOSITION ID IS D_1300007691.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-JUL-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL17U1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9793                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 130 MM                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : ADDREF                             
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 23245                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 45.680                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.5                               
REMARK 200  DATA REDUNDANCY                : 13.20                              
REMARK 200  R MERGE                    (I) : 0.12100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.38                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.61900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: PHASES                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.92                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.05M SODIUM CACODYLATE, PH 6.5, AND     
REMARK 280  30%(V/V) 2-METHYL-2,4-PENTANEDIOL(MPD), VAPOR DIFFUSION, HANGING    
REMARK 280  DROP, TEMPERATURE 291K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-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       30.65600            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       45.67700            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       45.65200            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       45.67700            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       30.65600            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       45.65200            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1370 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 11810 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -42.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: 410 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 10140 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -34.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
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   -53                                                      
REMARK 465     ALA A   -52                                                      
REMARK 465     HIS A   -51                                                      
REMARK 465     HIS A   -50                                                      
REMARK 465     HIS A   -49                                                      
REMARK 465     HIS A   -48                                                      
REMARK 465     HIS A   -47                                                      
REMARK 465     HIS A   -46                                                      
REMARK 465     VAL A   -45                                                      
REMARK 465     ASP A   -44                                                      
REMARK 465     ASP A   -43                                                      
REMARK 465     ASP A   -42                                                      
REMARK 465     ASP A   -41                                                      
REMARK 465     LYS A   -40                                                      
REMARK 465     MET A   -39                                                      
REMARK 465     LEU A   -38                                                      
REMARK 465     VAL A   -37                                                      
REMARK 465     PRO A   -36                                                      
REMARK 465     ARG A   -35                                                      
REMARK 465     GLY A   -34                                                      
REMARK 465     SER A   -33                                                      
REMARK 465     VAL A   242                                                      
REMARK 465     ASP A   243                                                      
REMARK 465     PRO A   244                                                      
REMARK 465     GLU A   245                                                      
REMARK 465     MET B   -53                                                      
REMARK 465     ALA B   -52                                                      
REMARK 465     HIS B   -51                                                      
REMARK 465     HIS B   -50                                                      
REMARK 465     HIS B   -49                                                      
REMARK 465     HIS B   -48                                                      
REMARK 465     HIS B   -47                                                      
REMARK 465     HIS B   -46                                                      
REMARK 465     VAL B   -45                                                      
REMARK 465     ASP B   -44                                                      
REMARK 465     ASP B   -43                                                      
REMARK 465     ASP B   -42                                                      
REMARK 465     ASP B   -41                                                      
REMARK 465     LYS B   -40                                                      
REMARK 465     MET B   -39                                                      
REMARK 465     LEU B   -38                                                      
REMARK 465     VAL B   -37                                                      
REMARK 465     PRO B   -36                                                      
REMARK 465     ARG B   -35                                                      
REMARK 465     GLY B   -34                                                      
REMARK 465     SER B   -33                                                      
REMARK 465     GLU B   -32                                                      
REMARK 465     ASN B   -31                                                      
REMARK 465     LEU B   -30                                                      
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     THR A 246    OG1  CG2                                            
REMARK 470     GLN B 241    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 245    CG   CD   OE1  OE2                                  
REMARK 470     THR B 246    OG1  CG2                                            
REMARK 470      DT C  10    C5'  C4'  O4'  C3'  O3'  C2'  C1'                   
REMARK 470      DT C  10    N1   C2   O2   N3   C4   O4   C5                    
REMARK 470      DT C  10    C7   C6                                             
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    TYR B  -1   C     LEU B 218   N       0.167                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ARG A  -5       79.15   -102.83                                   
REMARK 500    CYS B 248      124.71   -177.93                                   
REMARK 500    ASN B 266       42.28    -99.90                                   
REMARK 500    TYR B 345       75.57    -69.09                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 401  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 249   ND1                                                    
REMARK 620 2 CYS A 280   SG  104.0                                              
REMARK 620 3 CYS A 283   SG  112.1 123.0                                        
REMARK 620 4 CAC A 402   O1  104.0  94.3 116.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 401  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 249   ND1                                                    
REMARK 620 2 CYS B 280   SG  108.5                                              
REMARK 620 3 CYS B 283   SG  109.9 119.2                                        
REMARK 620 4 CAC B 402   O1  111.4  99.3 108.0                                  
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 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CAC A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CAC B 402                 
DBREF  5ZVA A  -23    -1  UNP    Q9HC16   ABC3G_HUMAN    197    219             
DBREF  5ZVA A  218   373  UNP    Q8IUX4   ABC3F_HUMAN    218    373             
DBREF  5ZVA B  -23    -1  UNP    Q9HC16   ABC3G_HUMAN    197    219             
DBREF  5ZVA B  218   373  UNP    Q8IUX4   ABC3F_HUMAN    218    373             
DBREF  5ZVA C    1     9  PDB    5ZVA     5ZVA             1      9             
SEQADV 5ZVA MET A  -53  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVA ALA A  -52  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVA HIS A  -51  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVA HIS A  -50  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVA HIS A  -49  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVA HIS A  -48  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVA HIS A  -47  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVA HIS A  -46  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVA VAL A  -45  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVA ASP A  -44  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVA ASP A  -43  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVA ASP A  -42  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVA ASP A  -41  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVA LYS A  -40  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVA MET A  -39  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVA LEU A  -38  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVA VAL A  -37  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVA PRO A  -36  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVA ARG A  -35  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVA GLY A  -34  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVA SER A  -33  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVA GLU A  -32  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVA ASN A  -31  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVA LEU A  -30  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVA TYR A  -29  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVA PHE A  -28  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVA GLN A  -27  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVA GLY A  -26  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVA SER A  -25  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVA ALA A  -24  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVA MET B  -53  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVA ALA B  -52  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVA HIS B  -51  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVA HIS B  -50  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVA HIS B  -49  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVA HIS B  -48  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVA HIS B  -47  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVA HIS B  -46  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVA VAL B  -45  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVA ASP B  -44  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVA ASP B  -43  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVA ASP B  -42  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVA ASP B  -41  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVA LYS B  -40  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVA MET B  -39  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVA LEU B  -38  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVA VAL B  -37  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVA PRO B  -36  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVA ARG B  -35  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVA GLY B  -34  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVA SER B  -33  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVA GLU B  -32  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVA ASN B  -31  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVA LEU B  -30  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVA TYR B  -29  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVA PHE B  -28  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVA GLN B  -27  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVA GLY B  -26  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVA SER B  -25  UNP  Q9HC16              EXPRESSION TAG                 
SEQADV 5ZVA ALA B  -24  UNP  Q9HC16              EXPRESSION TAG                 
SEQRES   1 A  209  MET ALA HIS HIS HIS HIS HIS HIS VAL ASP ASP ASP ASP          
SEQRES   2 A  209  LYS MET LEU VAL PRO ARG GLY SER GLU ASN LEU TYR PHE          
SEQRES   3 A  209  GLN GLY SER ALA MET ASP PRO PRO THR PHE THR PHE ASN          
SEQRES   4 A  209  PHE ASN ASN GLU PRO TRP VAL ARG GLY ARG HIS GLU THR          
SEQRES   5 A  209  TYR LEU CYS PHE THR MET GLU VAL VAL LYS HIS HIS SER          
SEQRES   6 A  209  PRO VAL SER TRP LYS ARG GLY VAL PHE ARG ASN GLN VAL          
SEQRES   7 A  209  ASP PRO GLU THR HIS CYS HIS ALA GLU ARG CYS PHE LEU          
SEQRES   8 A  209  SER TRP PHE CYS ASP ASP ILE LEU SER PRO ASN THR ASN          
SEQRES   9 A  209  TYR GLU VAL THR TRP TYR THR SER TRP SER PRO CYS PRO          
SEQRES  10 A  209  GLU CYS ALA GLY GLU VAL ALA GLU PHE LEU ALA ARG HIS          
SEQRES  11 A  209  SER ASN VAL ASN LEU THR ILE PHE THR ALA ARG LEU TYR          
SEQRES  12 A  209  TYR PHE TRP ASP THR ASP TYR GLN GLU GLY LEU ARG SER          
SEQRES  13 A  209  LEU SER GLN GLU GLY ALA SER VAL GLU ILE MET GLY TYR          
SEQRES  14 A  209  LYS ASP PHE LYS TYR CYS TRP GLU ASN PHE VAL TYR ASN          
SEQRES  15 A  209  ASP ASP GLU PRO PHE LYS PRO TRP LYS GLY LEU LYS TYR          
SEQRES  16 A  209  ASN PHE LEU PHE LEU ASP SER LYS LEU GLN GLU ILE LEU          
SEQRES  17 A  209  GLU                                                          
SEQRES   1 B  209  MET ALA HIS HIS HIS HIS HIS HIS VAL ASP ASP ASP ASP          
SEQRES   2 B  209  LYS MET LEU VAL PRO ARG GLY SER GLU ASN LEU TYR PHE          
SEQRES   3 B  209  GLN GLY SER ALA MET ASP PRO PRO THR PHE THR PHE ASN          
SEQRES   4 B  209  PHE ASN ASN GLU PRO TRP VAL ARG GLY ARG HIS GLU THR          
SEQRES   5 B  209  TYR LEU CYS PHE THR MET GLU VAL VAL LYS HIS HIS SER          
SEQRES   6 B  209  PRO VAL SER TRP LYS ARG GLY VAL PHE ARG ASN GLN VAL          
SEQRES   7 B  209  ASP PRO GLU THR HIS CYS HIS ALA GLU ARG CYS PHE LEU          
SEQRES   8 B  209  SER TRP PHE CYS ASP ASP ILE LEU SER PRO ASN THR ASN          
SEQRES   9 B  209  TYR GLU VAL THR TRP TYR THR SER TRP SER PRO CYS PRO          
SEQRES  10 B  209  GLU CYS ALA GLY GLU VAL ALA GLU PHE LEU ALA ARG HIS          
SEQRES  11 B  209  SER ASN VAL ASN LEU THR ILE PHE THR ALA ARG LEU TYR          
SEQRES  12 B  209  TYR PHE TRP ASP THR ASP TYR GLN GLU GLY LEU ARG SER          
SEQRES  13 B  209  LEU SER GLN GLU GLY ALA SER VAL GLU ILE MET GLY TYR          
SEQRES  14 B  209  LYS ASP PHE LYS TYR CYS TRP GLU ASN PHE VAL TYR ASN          
SEQRES  15 B  209  ASP ASP GLU PRO PHE LYS PRO TRP LYS GLY LEU LYS TYR          
SEQRES  16 B  209  ASN PHE LEU PHE LEU ASP SER LYS LEU GLN GLU ILE LEU          
SEQRES  17 B  209  GLU                                                          
SEQRES   1 C   10   DA  DT  DT  DT  DT  DC  DA  DA  DC  DT                      
HET     ZN  A 401       1                                                       
HET    CAC  A 402       5                                                       
HET     ZN  B 401       1                                                       
HET    CAC  B 402       5                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     CAC CACODYLATE ION                                                   
HETSYN     CAC DIMETHYLARSINATE                                                 
FORMUL   4   ZN    2(ZN 2+)                                                     
FORMUL   5  CAC    2(C2 H6 AS O2 1-)                                            
FORMUL   8  HOH   *115(H2 O)                                                    
HELIX    1 AA1 ASP A  -22  ASN A  -13  1                                  10    
HELIX    2 AA2 HIS A  249  ILE A  262  1                                  14    
HELIX    3 AA3 CYS A  280  HIS A  294  1                                  15    
HELIX    4 AA4 ASP A  311  GLU A  324  1                                  14    
HELIX    5 AA5 GLY A  332  VAL A  344  1                                  13    
HELIX    6 AA6 GLY A  356  GLU A  373  1                                  18    
HELIX    7 AA7 ASP B  -22  ASN B  -13  1                                  10    
HELIX    8 AA8 HIS B  249  ILE B  262  1                                  14    
HELIX    9 AA9 CYS B  280  HIS B  294  1                                  15    
HELIX   10 AB1 ASP B  311  GLU B  324  1                                  14    
HELIX   11 AB2 GLY B  332  PHE B  343  1                                  12    
HELIX   12 AB3 GLY B  356  GLU B  373  1                                  18    
SHEET    1 AA1 6 PHE A -28  GLN A -27  0                                        
SHEET    2 AA1 6 SER A 232  PHE A 238  1  O  ARG A 235   N  GLN A -27           
SHEET    3 AA1 6 LEU A 218  LYS A 226 -1  N  VAL A 224   O  SER A 232           
SHEET    4 AA1 6 THR A 267  TRP A 277 -1  O  ASN A 268   N  VAL A 225           
SHEET    5 AA1 6 VAL A 297  ARG A 305  1  O  ASN A 298   N  VAL A 271           
SHEET    6 AA1 6 SER A 327  ILE A 330  1  O  SER A 327   N  ILE A 301           
SHEET    1 AA2 6 PHE B -28  GLN B -27  0                                        
SHEET    2 AA2 6 SER B 232  PHE B 238  1  O  ARG B 235   N  GLN B -27           
SHEET    3 AA2 6 LEU B 218  LYS B 226 -1  N  LEU B 218   O  PHE B 238           
SHEET    4 AA2 6 THR B 267  TRP B 277 -1  O  ASN B 268   N  VAL B 225           
SHEET    5 AA2 6 VAL B 297  ARG B 305  1  O  THR B 300   N  TRP B 273           
SHEET    6 AA2 6 SER B 327  ILE B 330  1  O  SER B 327   N  ILE B 301           
SSBOND   1 CYS B  248    CYS B  253                          1555   1555  2.42  
LINK         ND1 HIS A 249                ZN    ZN A 401     1555   1555  2.20  
LINK         SG  CYS A 280                ZN    ZN A 401     1555   1555  2.38  
LINK         SG  CYS A 283                ZN    ZN A 401     1555   1555  2.21  
LINK         ND1 HIS B 249                ZN    ZN B 401     1555   1555  2.09  
LINK         SG  CYS B 280                ZN    ZN B 401     1555   1555  2.27  
LINK         SG  CYS B 283                ZN    ZN B 401     1555   1555  2.18  
LINK        ZN    ZN A 401                 O1  CAC A 402     1555   1555  2.25  
LINK        ZN    ZN B 401                 O1  CAC B 402     1555   1555  2.11  
SITE     1 AC1  4 HIS A 249  CYS A 280  CYS A 283  CAC A 402                    
SITE     1 AC2  9 THR A  -2  ASN A 240  HIS A 249  GLU A 251                    
SITE     2 AC2  9 TRP A 277  SER A 278  PRO A 279  CYS A 280                    
SITE     3 AC2  9  ZN A 401                                                     
SITE     1 AC3  4 HIS B 249  CYS B 280  CYS B 283  CAC B 402                    
SITE     1 AC4  9 THR B  -2  ASN B 240  HIS B 249  GLU B 251                    
SITE     2 AC4  9 TRP B 277  SER B 278  CYS B 280  CYS B 283                    
SITE     3 AC4  9  ZN B 401                                                     
CRYST1   61.312   91.304   91.354  90.00  90.00  90.00 P 21 21 21    8          
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      0.016310  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010952  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010946        0.00000                         
ATOM      1  N   GLU A -32     -42.468   7.309  -5.079  1.00101.10           N  
ANISOU    1  N   GLU A -32    11676  13273  13462   2120   1970   -552       N  
ATOM      2  CA  GLU A -32     -41.725   7.793  -3.879  1.00106.09           C  
ANISOU    2  CA  GLU A -32    13207  12453  14648   1904   1074   -445       C  
ATOM      3  C   GLU A -32     -40.268   7.319  -3.940  1.00100.45           C  
ANISOU    3  C   GLU A -32    13318  11211  13636   1589   2000   -154       C  
ATOM      4  O   GLU A -32     -39.599   7.476  -4.967  1.00103.29           O  
ANISOU    4  O   GLU A -32    14399  11742  13103  -1242   1633    160       O  
ATOM      5  CB  GLU A -32     -42.403   7.327  -2.573  1.00103.42           C  
ANISOU    5  CB  GLU A -32    12844  11107  15342   2098   1486   -165       C  
ATOM      6  CG  GLU A -32     -43.854   7.752  -2.392  1.00108.47           C  
ANISOU    6  CG  GLU A -32    12990  12361  15862   1809   2677    639       C  
ATOM      7  CD  GLU A -32     -44.848   6.701  -2.862  1.00115.01           C  
ANISOU    7  CD  GLU A -32    15065  13165  15466   1530   2190   -688       C  
ATOM      8  OE1 GLU A -32     -44.678   6.139  -3.967  1.00110.32           O  
ANISOU    8  OE1 GLU A -32    14473  11552  15889   1196   2653   -868       O  
ATOM      9  OE2 GLU A -32     -45.816   6.439  -2.119  1.00126.97           O  
ANISOU    9  OE2 GLU A -32    15176  17246  15821   1744   2388    143       O  
ATOM     10  N   ASN A -31     -39.794   6.737  -2.838  1.00 90.96           N  
ANISOU   10  N   ASN A -31    12285   7142  15131   2143   1146   -715       N  
ATOM     11  CA  ASN A -31     -38.449   6.183  -2.727  1.00 81.95           C  
ANISOU   11  CA  ASN A -31    11443   6855  12838   1618   2171  -1464       C  
ATOM     12  C   ASN A -31     -38.404   4.697  -3.089  1.00 77.96           C  
ANISOU   12  C   ASN A -31    11138   6986  11495   1829   2445  -1311       C  
ATOM     13  O   ASN A -31     -37.512   3.971  -2.639  1.00 73.25           O  
ANISOU   13  O   ASN A -31    10729   8077   9025   1664   2937   -736       O  
ATOM     14  CB  ASN A -31     -37.908   6.410  -1.308  1.00 78.66           C  
ANISOU   14  CB  ASN A -31    10405   6414  13068   2340   2157  -1916       C  
ATOM     15  CG  ASN A -31     -37.745   7.881  -0.971  1.00 81.72           C  
ANISOU   15  CG  ASN A -31    12016   6562  12469   1469   1764  -1656       C  
ATOM     16  OD1 ASN A -31     -37.226   8.661  -1.770  1.00 77.50           O  
ANISOU   16  OD1 ASN A -31    11677   4416  13351   1575    970  -1550       O  
ATOM     17  ND2 ASN A -31     -38.189   8.266   0.220  1.00 79.35           N  
ANISOU   17  ND2 ASN A -31    12730   4625  12793    941   1369  -2929       N  
ATOM     18  N   LEU A -30     -39.371   4.257  -3.898  1.00 81.46           N  
ANISOU   18  N   LEU A -30    11013   8116  11819   1444   2355   -940       N  
ATOM     19  CA  LEU A -30     -39.460   2.867  -4.361  1.00 79.47           C  
ANISOU   19  CA  LEU A -30    10635   7980  11578   1439   2310   -743       C  
ATOM     20  C   LEU A -30     -38.820   2.663  -5.740  1.00 76.05           C  
ANISOU   20  C   LEU A -30    10912   6923  11059    938   1837   -607       C  
ATOM     21  O   LEU A -30     -38.909   1.565  -6.307  1.00 73.61           O  
ANISOU   21  O   LEU A -30     9565   6427  11975    144   1787   -316       O  
ATOM     22  CB  LEU A -30     -40.922   2.379  -4.362  1.00 84.52           C  
ANISOU   22  CB  LEU A -30    10753   8930  12430   1230   2028   -785       C  
ATOM     23  CG  LEU A -30     -41.682   2.186  -3.037  1.00 89.16           C  
ANISOU   23  CG  LEU A -30    11286   9729  12860   1080   2248     94       C  
ATOM     24  CD1 LEU A -30     -43.182   2.097  -3.291  1.00 86.79           C  
ANISOU   24  CD1 LEU A -30    10686   9563  12725   2730   3060   -410       C  
ATOM     25  CD2 LEU A -30     -41.196   0.969  -2.255  1.00 89.48           C  
ANISOU   25  CD2 LEU A -30    12251   8859  12886   1267   2396   -497       C  
ATOM     26  N   TYR A -29     -38.171   3.714  -6.260  1.00 71.00           N  
ANISOU   26  N   TYR A -29    10295   6616  10063   1689   2017   -400       N  
ATOM     27  CA  TYR A -29     -37.496   3.679  -7.563  1.00 60.93           C  
ANISOU   27  CA  TYR A -29     8116   5012  10022   2158   1604    469       C  
ATOM     28  C   TYR A -29     -36.513   2.511  -7.653  1.00 51.01           C  
ANISOU   28  C   TYR A -29     7956   3646   7775   1284   1325    -59       C  
ATOM     29  O   TYR A -29     -35.633   2.363  -6.798  1.00 53.64           O  
ANISOU   29  O   TYR A -29     8100   3632   8647   1839    959   -636       O  
ATOM     30  CB  TYR A -29     -36.769   5.004  -7.863  1.00 64.36           C  
ANISOU   30  CB  TYR A -29     8733   4746  10972   2152   1273     -2       C  
ATOM     31  CG  TYR A -29     -35.984   4.971  -9.167  1.00 81.14           C  
ANISOU   31  CG  TYR A -29    11141   8055  11632   1500   2299   1135       C  
ATOM     32  CD1 TYR A -29     -36.604   5.285 -10.387  1.00 86.68           C  
ANISOU   32  CD1 TYR A -29    11181   8395  13356   2912   1575   2338       C  
ATOM     33  CD2 TYR A -29     -34.624   4.596  -9.189  1.00 79.15           C  
ANISOU   33  CD2 TYR A -29    11113   6854  12105   1268   1350    884       C  
ATOM     34  CE1 TYR A -29     -35.897   5.239 -11.585  1.00 93.54           C  
ANISOU   34  CE1 TYR A -29    13059   9345  13134   2732   1907   2529       C  
ATOM     35  CE2 TYR A -29     -33.909   4.545 -10.383  1.00 76.92           C  
ANISOU   35  CE2 TYR A -29    10799   5105  13320   2911   2150     54       C  
ATOM     36  CZ  TYR A -29     -34.551   4.871 -11.575  1.00 94.33           C  
ANISOU   36  CZ  TYR A -29    12898   9386  13556   2315   1803   1338       C  
ATOM     37  OH  TYR A -29     -33.858   4.832 -12.762  1.00104.41           O  
ANISOU   37  OH  TYR A -29    14031  10978  14662   2550   2887    815       O  
ATOM     38  N   PHE A -28     -36.668   1.699  -8.696  1.00 40.93           N  
ANISOU   38  N   PHE A -28     5885   2983   6681   1610   1160    765       N  
ATOM     39  CA  PHE A -28     -35.825   0.526  -8.903  1.00 37.51           C  
ANISOU   39  CA  PHE A -28     6049   2527   5673   1251   1032    293       C  
ATOM     40  C   PHE A -28     -35.121   0.598 -10.258  1.00 35.58           C  
ANISOU   40  C   PHE A -28     5536   2191   5792   1314    923    626       C  
ATOM     41  O   PHE A -28     -35.769   0.738 -11.292  1.00 41.43           O  
ANISOU   41  O   PHE A -28     6713   3438   5589   1674   1006   1982       O  
ATOM     42  CB  PHE A -28     -36.665  -0.750  -8.785  1.00 36.55           C  
ANISOU   42  CB  PHE A -28     5666   2839   5380   1185   1070    259       C  
ATOM     43  CG  PHE A -28     -35.860  -2.000  -8.520  1.00 35.96           C  
ANISOU   43  CG  PHE A -28     5412   2955   5295   1135    725    212       C  
ATOM     44  CD1 PHE A -28     -35.275  -2.718  -9.573  1.00 34.03           C  
ANISOU   44  CD1 PHE A -28     5028   2944   4957    995    859    466       C  
ATOM     45  CD2 PHE A -28     -35.716  -2.489  -7.217  1.00 35.84           C  
ANISOU   45  CD2 PHE A -28     5416   3015   5186    937    386     83       C  
ATOM     46  CE1 PHE A -28     -34.540  -3.879  -9.331  1.00 32.87           C  
ANISOU   46  CE1 PHE A -28     5311   2633   4542    856    481    165       C  
ATOM     47  CE2 PHE A -28     -34.983  -3.652  -6.974  1.00 33.16           C  
ANISOU   47  CE2 PHE A -28     4944   2883   4773    774    701    -14       C  
ATOM     48  CZ  PHE A -28     -34.399  -4.347  -8.032  1.00 31.14           C  
ANISOU   48  CZ  PHE A -28     4975   2302   4553    900    338     26       C  
ATOM     49  N   GLN A -27     -33.795   0.505 -10.238  1.00 33.63           N  
ANISOU   49  N   GLN A -27     5484   1562   5729   1266    943    520       N  
ATOM     50  CA  GLN A -27     -32.980   0.476 -11.449  1.00 36.33           C  
ANISOU   50  CA  GLN A -27     5800   2558   5443   1035    854    980       C  
ATOM     51  C   GLN A -27     -32.725  -0.971 -11.898  1.00 37.27           C  
ANISOU   51  C   GLN A -27     6173   2734   5252    867    779    603       C  
ATOM     52  O   GLN A -27     -32.225  -1.782 -11.125  1.00 37.40           O  
ANISOU   52  O   GLN A -27     6430   2783   4996    614    853    729       O  
ATOM     53  CB  GLN A -27     -31.658   1.221 -11.201  1.00 37.67           C  
ANISOU   53  CB  GLN A -27     6142   2336   5835    747    939   1007       C  
ATOM     54  CG  GLN A -27     -30.700   1.287 -12.387  1.00 40.60           C  
ANISOU   54  CG  GLN A -27     6401   2743   6279    907   1293    941       C  
ATOM     55  CD  GLN A -27     -31.249   2.073 -13.570  1.00 45.39           C  
ANISOU   55  CD  GLN A -27     6796   3496   6953   1155    652   1105       C  
ATOM     56  OE1 GLN A -27     -32.003   3.036 -13.406  1.00 46.36           O  
ANISOU   56  OE1 GLN A -27     7011   2949   7653    870    575    722       O  
ATOM     57  NE2 GLN A -27     -30.865   1.662 -14.775  1.00 51.67           N  
ANISOU   57  NE2 GLN A -27     7616   4833   7183     59   1399    718       N  
ATOM     58  N   GLY A -26     -33.058  -1.283 -13.149  1.00 38.23           N  
ANISOU   58  N   GLY A -26     6241   3065   5219    648    367   1035       N  
ATOM     59  CA  GLY A -26     -32.893  -2.645 -13.695  1.00 35.92           C  
ANISOU   59  CA  GLY A -26     5709   3202   4737   1059    443   1068       C  
ATOM     60  C   GLY A -26     -34.028  -3.584 -13.300  1.00 35.85           C  
ANISOU   60  C   GLY A -26     5324   3576   4720   1079    614    681       C  
ATOM     61  O   GLY A -26     -35.120  -3.139 -12.947  1.00 35.18           O  
ANISOU   61  O   GLY A -26     5016   3896   4452    976    492    825       O  
ATOM     62  N   SER A -25     -33.765  -4.887 -13.362  1.00 37.71           N  
ANISOU   62  N   SER A -25     6368   3543   4416    922    364    802       N  
ATOM     63  CA  SER A -25     -34.763  -5.911 -13.032  1.00 39.60           C  
ANISOU   63  CA  SER A -25     6208   4084   4750    699    256    705       C  
ATOM     64  C   SER A -25     -34.390  -6.639 -11.746  1.00 33.21           C  
ANISOU   64  C   SER A -25     4906   3422   4287    716    378     92       C  
ATOM     65  O   SER A -25     -33.219  -6.942 -11.524  1.00 33.96           O  
ANISOU   65  O   SER A -25     5246   3009   4645   1027     28   -718       O  
ATOM     66  CB  SER A -25     -34.887  -6.929 -14.171  1.00 44.29           C  
ANISOU   66  CB  SER A -25     7014   4304   5507    343   -354    322       C  
ATOM     67  OG  SER A -25     -35.292  -6.311 -15.382  1.00 49.52           O  
ANISOU   67  OG  SER A -25     8232   4583   5998    600   -156    982       O  
ATOM     68  N   ALA A -24     -35.387  -6.918 -10.907  1.00 31.21           N  
ANISOU   68  N   ALA A -24     4699   3067   4093    720    142    130       N  
ATOM     69  CA  ALA A -24     -35.223  -7.818  -9.760  1.00 30.54           C  
ANISOU   69  CA  ALA A -24     4550   3096   3954    764    413     71       C  
ATOM     70  C   ALA A -24     -34.947  -9.245 -10.253  1.00 33.19           C  
ANISOU   70  C   ALA A -24     5028   3195   4388    802     27   -199       C  
ATOM     71  O   ALA A -24     -35.308  -9.586 -11.384  1.00 34.62           O  
ANISOU   71  O   ALA A -24     5503   3268   4383    809     48   -328       O  
ATOM     72  CB  ALA A -24     -36.465  -7.790  -8.888  1.00 28.13           C  
ANISOU   72  CB  ALA A -24     4371   2475   3841    690    303   -351       C  
ATOM     73  N   MET A -23     -34.287 -10.051  -9.420  1.00 31.93           N  
ANISOU   73  N   MET A -23     5233   3172   3725    408    153     -2       N  
ATOM     74  CA  MET A -23     -34.004 -11.457  -9.734  1.00 30.67           C  
ANISOU   74  CA  MET A -23     4553   3235   3864    487    178     69       C  
ATOM     75  C   MET A -23     -35.221 -12.329  -9.408  1.00 30.30           C  
ANISOU   75  C   MET A -23     4429   3196   3888    486     56   -239       C  
ATOM     76  O   MET A -23     -35.945 -12.047  -8.449  1.00 32.03           O  
ANISOU   76  O   MET A -23     4406   3994   3769    397     35   -455       O  
ATOM     77  CB  MET A -23     -32.804 -11.951  -8.915  1.00 30.21           C  
ANISOU   77  CB  MET A -23     4373   3153   3952    432    250     31       C  
ATOM     78  CG  MET A -23     -31.452 -11.389  -9.340  1.00 26.74           C  
ANISOU   78  CG  MET A -23     4064   2676   3420    490   -466    255       C  
ATOM     79  SD  MET A -23     -30.108 -11.710  -8.172  1.00 19.70           S  
ANISOU   79  SD  MET A -23     3637   1706   2141    307     67    -96       S  
ATOM     80  CE  MET A -23     -30.435 -10.434  -6.976  1.00 21.57           C  
ANISOU   80  CE  MET A -23     3816   1403   2977    416     49   -276       C  
ATOM     81  N   ASP A -22     -35.458 -13.385 -10.186  1.00 30.26           N  
ANISOU   81  N   ASP A -22     4311   3095   4090    424    -37   -196       N  
ATOM     82  CA  ASP A -22     -36.377 -14.432  -9.711  1.00 29.96           C  
ANISOU   82  CA  ASP A -22     4104   3246   4029    361   -108   -185       C  
ATOM     83  C   ASP A -22     -35.698 -15.252  -8.581  1.00 26.95           C  
ANISOU   83  C   ASP A -22     3947   2373   3917     55     62   -277       C  
ATOM     84  O   ASP A -22     -34.463 -15.237  -8.484  1.00 25.70           O  
ANISOU   84  O   ASP A -22     3938   1926   3899     45     -4   -506       O  
ATOM     85  CB  ASP A -22     -36.964 -15.278 -10.856  1.00 35.93           C  
ANISOU   85  CB  ASP A -22     4901   4119   4629   -246   -460   -439       C  
ATOM     86  CG  ASP A -22     -35.911 -15.902 -11.758  1.00 46.22           C  
ANISOU   86  CG  ASP A -22     5860   5392   6309    384    346   -482       C  
ATOM     87  OD1 ASP A -22     -35.079 -16.701 -11.265  1.00 48.04           O  
ANISOU   87  OD1 ASP A -22     6338   5836   6076    477   -351   -577       O  
ATOM     88  OD2 ASP A -22     -35.954 -15.622 -12.985  1.00 54.60           O  
ANISOU   88  OD2 ASP A -22     7141   6852   6753  -1568    120    286       O  
ATOM     89  N   PRO A -21     -36.488 -15.915  -7.689  1.00 27.35           N  
ANISOU   89  N   PRO A -21     3927   2716   3746    158     58   -166       N  
ATOM     90  CA  PRO A -21     -35.838 -16.658  -6.583  1.00 26.87           C  
ANISOU   90  CA  PRO A -21     3607   2896   3704   -132   -196   -174       C  
ATOM     91  C   PRO A -21     -34.737 -17.665  -6.988  1.00 26.81           C  
ANISOU   91  C   PRO A -21     4163   2500   3524    -28   -267   -274       C  
ATOM     92  O   PRO A -21     -33.671 -17.631  -6.375  1.00 28.71           O  
ANISOU   92  O   PRO A -21     4253   2689   3965   -155   -381   -252       O  
ATOM     93  CB  PRO A -21     -37.013 -17.352  -5.870  1.00 26.28           C  
ANISOU   93  CB  PRO A -21     3615   2627   3742   -164   -394     66       C  
ATOM     94  CG  PRO A -21     -38.184 -16.481  -6.163  1.00 26.62           C  
ANISOU   94  CG  PRO A -21     3356   2931   3825    -93   -162     21       C  
ATOM     95  CD  PRO A -21     -37.962 -15.954  -7.563  1.00 27.56           C  
ANISOU   95  CD  PRO A -21     3789   2922   3758     93   -242   -101       C  
ATOM     96  N   PRO A -20     -34.958 -18.527  -8.017  1.00 28.63           N  
ANISOU   96  N   PRO A -20     4337   2496   4042    -98   -446   -545       N  
ATOM     97  CA  PRO A -20     -33.846 -19.467  -8.337  1.00 28.77           C  
ANISOU   97  CA  PRO A -20     4302   2658   3972      4   -478   -457       C  
ATOM     98  C   PRO A -20     -32.548 -18.803  -8.834  1.00 28.27           C  
ANISOU   98  C   PRO A -20     4328   2509   3904    200   -339   -331       C  
ATOM     99  O   PRO A -20     -31.469 -19.327  -8.578  1.00 27.00           O  
ANISOU   99  O   PRO A -20     4621   1916   3721    323   -374   -121       O  
ATOM    100  CB  PRO A -20     -34.443 -20.372  -9.425  1.00 28.31           C  
ANISOU  100  CB  PRO A -20     4423   1926   4405    466   -388   -760       C  
ATOM    101  CG  PRO A -20     -35.922 -20.277  -9.216  1.00 30.62           C  
ANISOU  101  CG  PRO A -20     4382   2659   4592     88   -541   -764       C  
ATOM    102  CD  PRO A -20     -36.151 -18.834  -8.833  1.00 27.88           C  
ANISOU  102  CD  PRO A -20     4015   2516   4062    210   -469   -393       C  
ATOM    103  N   THR A -19     -32.656 -17.656  -9.512  1.00 29.66           N  
ANISOU  103  N   THR A -19     4764   2883   3623    125   -200    -73       N  
ATOM    104  CA  THR A -19     -31.482 -16.891  -9.960  1.00 29.13           C  
ANISOU  104  CA  THR A -19     4634   2903   3529     51   -195   -239       C  
ATOM    105  C   THR A -19     -30.703 -16.324  -8.777  1.00 26.68           C  
ANISOU  105  C   THR A -19     4425   2579   3131    283     28   -125       C  
ATOM    106  O   THR A -19     -29.466 -16.346  -8.782  1.00 26.93           O  
ANISOU  106  O   THR A -19     4473   2800   2956   -220    311   -366       O  
ATOM    107  CB  THR A -19     -31.871 -15.751 -10.932  1.00 31.86           C  
ANISOU  107  CB  THR A -19     4927   3260   3918    151   -207     36       C  
ATOM    108  OG1 THR A -19     -32.585 -16.297 -12.047  1.00 36.41           O  
ANISOU  108  OG1 THR A -19     5532   4109   4192   -338   -566     85       O  
ATOM    109  CG2 THR A -19     -30.641 -15.006 -11.461  1.00 31.24           C  
ANISOU  109  CG2 THR A -19     5329   2709   3830      8   -162    198       C  
ATOM    110  N   PHE A -18     -31.425 -15.829  -7.771  1.00 25.91           N  
ANISOU  110  N   PHE A -18     4433   2207   3205    400     -9    -93       N  
ATOM    111  CA  PHE A -18     -30.804 -15.299  -6.550  1.00 26.64           C  
ANISOU  111  CA  PHE A -18     4305   2605   3210    254    131   -266       C  
ATOM    112  C   PHE A -18     -30.057 -16.405  -5.802  1.00 26.00           C  
ANISOU  112  C   PHE A -18     4057   2432   3390     71    120   -260       C  
ATOM    113  O   PHE A -18     -28.881 -16.274  -5.473  1.00 28.11           O  
ANISOU  113  O   PHE A -18     4154   3095   3430     72    -49   -216       O  
ATOM    114  CB  PHE A -18     -31.841 -14.642  -5.611  1.00 25.47           C  
ANISOU  114  CB  PHE A -18     4220   2132   3322    251    130   -224       C  
ATOM    115  CG  PHE A -18     -31.268 -14.258  -4.259  1.00 26.10           C  
ANISOU  115  CG  PHE A -18     4129   2526   3262     86    204   -146       C  
ATOM    116  CD1 PHE A -18     -30.482 -13.115  -4.116  1.00 26.34           C  
ANISOU  116  CD1 PHE A -18     4292   2332   3384    144     73    -17       C  
ATOM    117  CD2 PHE A -18     -31.478 -15.062  -3.139  1.00 27.82           C  
ANISOU  117  CD2 PHE A -18     4414   2706   3447     50    211     12       C  
ATOM    118  CE1 PHE A -18     -29.937 -12.773  -2.879  1.00 28.44           C  
ANISOU  118  CE1 PHE A -18     4572   2680   3551     95   -101     43       C  
ATOM    119  CE2 PHE A -18     -30.935 -14.722  -1.898  1.00 28.44           C  
ANISOU  119  CE2 PHE A -18     4218   2869   3718   -113      2     51       C  
ATOM    120  CZ  PHE A -18     -30.166 -13.575  -1.767  1.00 27.46           C  
ANISOU  120  CZ  PHE A -18     4135   2874   3423    -89     24    -49       C  
ATOM    121  N   THR A -17     -30.765 -17.493  -5.541  1.00 28.43           N  
ANISOU  121  N   THR A -17     4604   2546   3651    -92    208    -69       N  
ATOM    122  CA  THR A -17     -30.232 -18.615  -4.783  1.00 31.17           C  
ANISOU  122  CA  THR A -17     4747   2714   4381      8    172    215       C  
ATOM    123  C   THR A -17     -28.988 -19.223  -5.452  1.00 31.25           C  
ANISOU  123  C   THR A -17     4819   2871   4184    107     12    -17       C  
ATOM    124  O   THR A -17     -28.018 -19.555  -4.769  1.00 33.35           O  
ANISOU  124  O   THR A -17     4882   2873   4914    291   -225     -2       O  
ATOM    125  CB  THR A -17     -31.355 -19.628  -4.525  1.00 33.55           C  
ANISOU  125  CB  THR A -17     4855   3095   4795   -144    395    661       C  
ATOM    126  OG1 THR A -17     -32.369 -18.959  -3.769  1.00 35.92           O  
ANISOU  126  OG1 THR A -17     5346   2889   5410   -298    940    751       O  
ATOM    127  CG2 THR A -17     -30.864 -20.839  -3.738  1.00 34.55           C  
ANISOU  127  CG2 THR A -17     5336   2840   4951     80    600    573       C  
ATOM    128  N   PHE A -16     -29.016 -19.318  -6.781  1.00 29.20           N  
ANISOU  128  N   PHE A -16     4605   2370   4117    150    343      2       N  
ATOM    129  CA  PHE A -16     -27.877 -19.795  -7.555  1.00 27.07           C  
ANISOU  129  CA  PHE A -16     4469   2249   3564    169    118     94       C  
ATOM    130  C   PHE A -16     -26.699 -18.822  -7.462  1.00 26.74           C  
ANISOU  130  C   PHE A -16     4450   2220   3490    204    299      1       C  
ATOM    131  O   PHE A -16     -25.574 -19.237  -7.150  1.00 27.59           O  
ANISOU  131  O   PHE A -16     4243   2781   3456     27    639    510       O  
ATOM    132  CB  PHE A -16     -28.292 -20.026  -9.014  1.00 27.52           C  
ANISOU  132  CB  PHE A -16     4771   1967   3716    383    103   -500       C  
ATOM    133  CG  PHE A -16     -27.193 -20.561  -9.891  1.00 28.79           C  
ANISOU  133  CG  PHE A -16     4933   2298   3706    550    183   -421       C  
ATOM    134  CD1 PHE A -16     -26.908 -21.930  -9.922  1.00 28.47           C  
ANISOU  134  CD1 PHE A -16     4917   2280   3619    576     22   -330       C  
ATOM    135  CD2 PHE A -16     -26.463 -19.701 -10.715  1.00 29.32           C  
ANISOU  135  CD2 PHE A -16     4858   2430   3851    573    207   -269       C  
ATOM    136  CE1 PHE A -16     -25.903 -22.427 -10.748  1.00 30.32           C  
ANISOU  136  CE1 PHE A -16     5027   2713   3777    492    137   -566       C  
ATOM    137  CE2 PHE A -16     -25.459 -20.190 -11.545  1.00 30.73           C  
ANISOU  137  CE2 PHE A -16     5083   2682   3910    696    294   -391       C  
ATOM    138  CZ  PHE A -16     -25.176 -21.552 -11.556  1.00 31.04           C  
ANISOU  138  CZ  PHE A -16     5354   2722   3717    731    426   -524       C  
ATOM    139  N   ASN A -15     -26.958 -17.538  -7.710  1.00 26.02           N  
ANISOU  139  N   ASN A -15     4556   2167   3161    175    472    -15       N  
ATOM    140  CA  ASN A -15     -25.875 -16.548  -7.784  1.00 26.82           C  
ANISOU  140  CA  ASN A -15     4439   2291   3460    234    386     99       C  
ATOM    141  C   ASN A -15     -25.302 -16.078  -6.462  1.00 27.28           C  
ANISOU  141  C   ASN A -15     4393   2577   3395    307    305    312       C  
ATOM    142  O   ASN A -15     -24.132 -15.686  -6.402  1.00 32.03           O  
ANISOU  142  O   ASN A -15     4562   2897   4710     29    321    706       O  
ATOM    143  CB  ASN A -15     -26.278 -15.349  -8.635  1.00 25.30           C  
ANISOU  143  CB  ASN A -15     4313   2271   3028    255    599     44       C  
ATOM    144  CG  ASN A -15     -26.198 -15.656 -10.105  1.00 26.08           C  
ANISOU  144  CG  ASN A -15     4519   2315   3072    313    378     16       C  
ATOM    145  OD1 ASN A -15     -25.110 -15.674 -10.693  1.00 28.80           O  
ANISOU  145  OD1 ASN A -15     4944   2707   3290    669    808    257       O  
ATOM    146  ND2 ASN A -15     -27.346 -15.916 -10.710  1.00 25.87           N  
ANISOU  146  ND2 ASN A -15     4649   2152   3028   -131    380     52       N  
ATOM    147  N   PHE A -14     -26.111 -16.103  -5.410  1.00 25.92           N  
ANISOU  147  N   PHE A -14     4182   2345   3320    121    209    344       N  
ATOM    148  CA  PHE A -14     -25.630 -15.624  -4.121  1.00 27.83           C  
ANISOU  148  CA  PHE A -14     4438   2616   3518     20    169     35       C  
ATOM    149  C   PHE A -14     -25.186 -16.710  -3.154  1.00 28.99           C  
ANISOU  149  C   PHE A -14     4498   2738   3775    -49    110    234       C  
ATOM    150  O   PHE A -14     -24.781 -16.419  -2.029  1.00 30.39           O  
ANISOU  150  O   PHE A -14     4862   2778   3905   -539   -231    587       O  
ATOM    151  CB  PHE A -14     -26.599 -14.601  -3.518  1.00 27.09           C  
ANISOU  151  CB  PHE A -14     4186   2602   3504     11     39     42       C  
ATOM    152  CG  PHE A -14     -26.486 -13.245  -4.162  1.00 28.25           C  
ANISOU  152  CG  PHE A -14     4387   2625   3720    -99    212     66       C  
ATOM    153  CD1 PHE A -14     -27.142 -12.970  -5.373  1.00 28.09           C  
ANISOU  153  CD1 PHE A -14     4451   2571   3649    131    343     58       C  
ATOM    154  CD2 PHE A -14     -25.682 -12.256  -3.596  1.00 28.17           C  
ANISOU  154  CD2 PHE A -14     4398   2766   3539    -45    143    -45       C  
ATOM    155  CE1 PHE A -14     -27.021 -11.724  -5.981  1.00 28.58           C  
ANISOU  155  CE1 PHE A -14     4559   2744   3555    -14    436    207       C  
ATOM    156  CE2 PHE A -14     -25.558 -11.008  -4.202  1.00 29.77           C  
ANISOU  156  CE2 PHE A -14     4751   2830   3730   -190    221     14       C  
ATOM    157  CZ  PHE A -14     -26.227 -10.743  -5.392  1.00 28.96           C  
ANISOU  157  CZ  PHE A -14     4493   2689   3821     71    310    204       C  
ATOM    158  N   ASN A -13     -25.236 -17.959  -3.615  1.00 29.79           N  
ANISOU  158  N   ASN A -13     4540   2777   4000    173    230    101       N  
ATOM    159  CA  ASN A -13     -24.621 -19.081  -2.898  1.00 31.74           C  
ANISOU  159  CA  ASN A -13     4415   3167   4478    114     15    408       C  
ATOM    160  C   ASN A -13     -23.173 -18.738  -2.580  1.00 32.24           C  
ANISOU  160  C   ASN A -13     4331   3575   4343    200     87    382       C  
ATOM    161  O   ASN A -13     -22.409 -18.355  -3.472  1.00 32.49           O  
ANISOU  161  O   ASN A -13     4773   3147   4422    174    198    448       O  
ATOM    162  CB  ASN A -13     -24.685 -20.367  -3.717  1.00 34.47           C  
ANISOU  162  CB  ASN A -13     4823   2885   5386    237    112    357       C  
ATOM    163  CG  ASN A -13     -24.194 -21.567  -2.931  1.00 39.78           C  
ANISOU  163  CG  ASN A -13     5341   3393   6380    315    124    968       C  
ATOM    164  OD1 ASN A -13     -22.995 -21.850  -2.889  1.00 41.22           O  
ANISOU  164  OD1 ASN A -13     5527   3032   7102    817   -258    962       O  
ATOM    165  ND2 ASN A -13     -25.121 -22.265  -2.280  1.00 39.53           N  
ANISOU  165  ND2 ASN A -13     6079   2915   6024    259    344   1084       N  
ATOM    166  N   ASN A -12     -22.808 -18.857  -1.308  1.00 32.53           N  
ANISOU  166  N   ASN A -12     4331   3625   4401   -127    -23    416       N  
ATOM    167  CA  ASN A -12     -21.503 -18.385  -0.861  1.00 32.21           C  
ANISOU  167  CA  ASN A -12     4322   3571   4343   -115    -74    489       C  
ATOM    168  C   ASN A -12     -20.449 -19.461  -0.611  1.00 33.02           C  
ANISOU  168  C   ASN A -12     4273   3597   4675   -150     42    799       C  
ATOM    169  O   ASN A -12     -19.485 -19.217   0.118  1.00 37.06           O  
ANISOU  169  O   ASN A -12     4425   4485   5169   -763   -142   1137       O  
ATOM    170  CB  ASN A -12     -21.644 -17.440   0.346  1.00 29.51           C  
ANISOU  170  CB  ASN A -12     4054   3095   4062   -344    102    728       C  
ATOM    171  CG  ASN A -12     -22.123 -18.140   1.604  1.00 27.38           C  
ANISOU  171  CG  ASN A -12     3716   3039   3645   -180   -229    600       C  
ATOM    172  OD1 ASN A -12     -22.749 -19.204   1.554  1.00 31.03           O  
ANISOU  172  OD1 ASN A -12     3969   3226   4592   -383    -76    220       O  
ATOM    173  ND2 ASN A -12     -21.842 -17.531   2.749  1.00 24.60           N  
ANISOU  173  ND2 ASN A -12     3247   2314   3785   -511   -514    843       N  
ATOM    174  N   GLU A -11     -20.620 -20.639  -1.207  1.00 31.83           N  
ANISOU  174  N   GLU A -11     4261   3691   4139    -40     57    848       N  
ATOM    175  CA  GLU A -11     -19.525 -21.614  -1.225  1.00 34.64           C  
ANISOU  175  CA  GLU A -11     4640   3931   4590    245     30   1254       C  
ATOM    176  C   GLU A -11     -18.318 -20.951  -1.897  1.00 36.77           C  
ANISOU  176  C   GLU A -11     4277   4640   5052    321    173   1043       C  
ATOM    177  O   GLU A -11     -18.460 -20.405  -2.998  1.00 38.00           O  
ANISOU  177  O   GLU A -11     4714   4027   5698    506    847   1740       O  
ATOM    178  CB  GLU A -11     -19.925 -22.919  -1.901  1.00 38.56           C  
ANISOU  178  CB  GLU A -11     5251   3888   5511    462   -128    863       C  
ATOM    179  CG  GLU A -11     -19.940 -24.108  -0.951  1.00 52.64           C  
ANISOU  179  CG  GLU A -11     7893   5018   7088   -162   -172   2044       C  
ATOM    180  CD  GLU A -11     -21.267 -24.849  -0.931  1.00 69.33           C  
ANISOU  180  CD  GLU A -11     9050   6729  10560  -1394   -253   1530       C  
ATOM    181  OE1 GLU A -11     -21.775 -25.221  -2.019  1.00 82.35           O  
ANISOU  181  OE1 GLU A -11    11644   9069  10574  -1203   -964   1151       O  
ATOM    182  OE2 GLU A -11     -21.801 -25.068   0.185  1.00 74.86           O  
ANISOU  182  OE2 GLU A -11    11572   6889   9981  -2215   -910   3074       O  
ATOM    183  N   PRO A -10     -17.149 -20.946  -1.211  1.00 36.01           N  
ANISOU  183  N   PRO A -10     4135   4307   5238    278    180   1061       N  
ATOM    184  CA  PRO A -10     -15.949 -20.204  -1.645  1.00 35.46           C  
ANISOU  184  CA  PRO A -10     4104   4049   5317    348    174   1119       C  
ATOM    185  C   PRO A -10     -15.470 -20.541  -3.058  1.00 38.06           C  
ANISOU  185  C   PRO A -10     4464   4357   5639    147    553   1158       C  
ATOM    186  O   PRO A -10     -14.909 -19.671  -3.732  1.00 37.78           O  
ANISOU  186  O   PRO A -10     4453   4612   5288     67    684   1062       O  
ATOM    187  CB  PRO A -10     -14.883 -20.609  -0.622  1.00 35.08           C  
ANISOU  187  CB  PRO A -10     3820   4123   5385    288    215    999       C  
ATOM    188  CG  PRO A -10     -15.644 -21.084   0.568  1.00 36.89           C  
ANISOU  188  CG  PRO A -10     4094   4507   5415      4    345    807       C  
ATOM    189  CD  PRO A -10     -16.918 -21.672   0.052  1.00 35.41           C  
ANISOU  189  CD  PRO A -10     4046   3954   5452      8    327   1253       C  
ATOM    190  N   TRP A  -9     -15.699 -21.779  -3.503  1.00 38.44           N  
ANISOU  190  N   TRP A  -9     4573   4023   6008    850    905   1136       N  
ATOM    191  CA  TRP A  -9     -15.269 -22.204  -4.826  1.00 37.47           C  
ANISOU  191  CA  TRP A  -9     4591   3608   6037   1240    740    971       C  
ATOM    192  C   TRP A  -9     -16.378 -22.713  -5.760  1.00 42.05           C  
ANISOU  192  C   TRP A  -9     5051   4322   6604   1099    278    999       C  
ATOM    193  O   TRP A  -9     -16.098 -23.546  -6.625  1.00 51.24           O  
ANISOU  193  O   TRP A  -9     7528   5129   6811    948    332    530       O  
ATOM    194  CB  TRP A  -9     -14.183 -23.279  -4.713  1.00 37.70           C  
ANISOU  194  CB  TRP A  -9     4142   3949   6232   1125    387   1458       C  
ATOM    195  CG  TRP A  -9     -12.949 -22.917  -3.934  1.00 36.69           C  
ANISOU  195  CG  TRP A  -9     3918   3704   6318   1277    599   1627       C  
ATOM    196  CD1 TRP A  -9     -11.850 -22.251  -4.400  1.00 36.99           C  
ANISOU  196  CD1 TRP A  -9     3848   3690   6514   1233    679   1310       C  
ATOM    197  CD2 TRP A  -9     -12.666 -23.256  -2.570  1.00 37.18           C  
ANISOU  197  CD2 TRP A  -9     3855   3812   6458   1409    258   1643       C  
ATOM    198  NE1 TRP A  -9     -10.906 -22.140  -3.410  1.00 37.12           N  
ANISOU  198  NE1 TRP A  -9     4023   3710   6369   1511    571   1565       N  
ATOM    199  CE2 TRP A  -9     -11.376 -22.749  -2.275  1.00 38.51           C  
ANISOU  199  CE2 TRP A  -9     4249   3586   6795    702    711   1518       C  
ATOM    200  CE3 TRP A  -9     -13.379 -23.942  -1.564  1.00 38.22           C  
ANISOU  200  CE3 TRP A  -9     4103   3937   6479   1304    520   1402       C  
ATOM    201  CZ2 TRP A  -9     -10.768 -22.906  -1.008  1.00 42.89           C  
ANISOU  201  CZ2 TRP A  -9     4768   4850   6676    512    658   1262       C  
ATOM    202  CZ3 TRP A  -9     -12.779 -24.097  -0.296  1.00 38.39           C  
ANISOU  202  CZ3 TRP A  -9     4363   3773   6448    571    573   1470       C  
ATOM    203  CH2 TRP A  -9     -11.481 -23.580  -0.035  1.00 42.46           C  
ANISOU  203  CH2 TRP A  -9     4604   4111   7415    237    286   1610       C  
ATOM    204  N   VAL A  -8     -17.613 -22.232  -5.621  1.00 43.02           N  
ANISOU  204  N   VAL A  -8     5370   4782   6191   1284    699    551       N  
ATOM    205  CA  VAL A  -8     -18.710 -22.678  -6.526  1.00 46.19           C  
ANISOU  205  CA  VAL A  -8     6163   5130   6257    946    458    368       C  
ATOM    206  C   VAL A  -8     -18.354 -22.631  -8.012  1.00 45.27           C  
ANISOU  206  C   VAL A  -8     6141   4703   6356    824    726     88       C  
ATOM    207  O   VAL A  -8     -17.661 -21.714  -8.470  1.00 44.56           O  
ANISOU  207  O   VAL A  -8     7102   4605   5222    763    486    474       O  
ATOM    208  CB  VAL A  -8     -20.026 -21.882  -6.378  1.00 45.33           C  
ANISOU  208  CB  VAL A  -8     6341   4581   6302    976    391    275       C  
ATOM    209  CG1 VAL A  -8     -20.811 -22.347  -5.176  1.00 51.40           C  
ANISOU  209  CG1 VAL A  -8     6904   6014   6610    897    449   1059       C  
ATOM    210  CG2 VAL A  -8     -19.784 -20.380  -6.375  1.00 42.61           C  
ANISOU  210  CG2 VAL A  -8     6024   4395   5770   1008    -47   -907       C  
ATOM    211  N   ARG A  -7     -18.841 -23.617  -8.755  1.00 43.76           N  
ANISOU  211  N   ARG A  -7     6060   4412   6154   1356    928    -64       N  
ATOM    212  CA  ARG A  -7     -18.648 -23.633 -10.195  1.00 44.38           C  
ANISOU  212  CA  ARG A  -7     6471   4327   6062   1517    727   -123       C  
ATOM    213  C   ARG A  -7     -19.884 -23.181 -10.972  1.00 40.60           C  
ANISOU  213  C   ARG A  -7     6143   3749   5532   1269    949   -525       C  
ATOM    214  O   ARG A  -7     -21.013 -23.293 -10.485  1.00 35.19           O  
ANISOU  214  O   ARG A  -7     5822   2234   5313   1560    588   -855       O  
ATOM    215  CB  ARG A  -7     -18.106 -24.983 -10.681  1.00 52.97           C  
ANISOU  215  CB  ARG A  -7     8024   4797   7306   2005   1197   -484       C  
ATOM    216  CG  ARG A  -7     -18.863 -26.242 -10.281  1.00 58.45           C  
ANISOU  216  CG  ARG A  -7     8886   5290   8029   1693   1365   -285       C  
ATOM    217  CD  ARG A  -7     -18.114 -27.495 -10.741  1.00 63.89           C  
ANISOU  217  CD  ARG A  -7     9095   6339   8839   2366   1771   -792       C  
ATOM    218  NE  ARG A  -7     -17.858 -27.488 -12.188  1.00 62.16           N  
ANISOU  218  NE  ARG A  -7     8741   5939   8935   3332   2051  -1014       N  
ATOM    219  CZ  ARG A  -7     -16.701 -27.153 -12.765  1.00 60.72           C  
ANISOU  219  CZ  ARG A  -7     9024   5984   8062   2346   1594  -1120       C  
ATOM    220  NH1 ARG A  -7     -16.597 -27.173 -14.089  1.00 52.36           N  
ANISOU  220  NH1 ARG A  -7     8233   3684   7975   2186   1875  -2012       N  
ATOM    221  NH2 ARG A  -7     -15.647 -26.795 -12.034  1.00 62.26           N  
ANISOU  221  NH2 ARG A  -7     9042   4842   9769   2137   1412  -1798       N  
ATOM    222  N   GLY A  -6     -19.640 -22.649 -12.170  1.00 41.53           N  
ANISOU  222  N   GLY A  -6     6367   3669   5740   1258    759   -208       N  
ATOM    223  CA  GLY A  -6     -20.687 -22.274 -13.113  1.00 39.12           C  
ANISOU  223  CA  GLY A  -6     6286   3499   5079   1456    955   -387       C  
ATOM    224  C   GLY A  -6     -21.400 -20.965 -12.826  1.00 39.18           C  
ANISOU  224  C   GLY A  -6     6354   3505   5026   1426    930   -459       C  
ATOM    225  O   GLY A  -6     -22.516 -20.767 -13.315  1.00 43.79           O  
ANISOU  225  O   GLY A  -6     6266   4897   5472   1166    987    -37       O  
ATOM    226  N   ARG A  -5     -20.777 -20.082 -12.038  1.00 36.80           N  
ANISOU  226  N   ARG A  -5     5947   3445   4590   1200    878   -259       N  
ATOM    227  CA  ARG A  -5     -21.326 -18.733 -11.773  1.00 33.72           C  
ANISOU  227  CA  ARG A  -5     5372   3392   4048   1170    680     90       C  
ATOM    228  C   ARG A  -5     -20.587 -17.686 -12.593  1.00 37.00           C  
ANISOU  228  C   ARG A  -5     5754   3615   4687   1005    833    291       C  
ATOM    229  O   ARG A  -5     -19.712 -16.980 -12.077  1.00 39.78           O  
ANISOU  229  O   ARG A  -5     5451   4123   5541   1172    366    236       O  
ATOM    230  CB  ARG A  -5     -21.284 -18.371 -10.276  1.00 31.19           C  
ANISOU  230  CB  ARG A  -5     4931   2793   4127    873    736    -76       C  
ATOM    231  CG  ARG A  -5     -22.489 -18.820  -9.461  1.00 32.42           C  
ANISOU  231  CG  ARG A  -5     5049   3152   4115    767    805    -68       C  
ATOM    232  CD  ARG A  -5     -22.533 -20.337  -9.257  1.00 34.06           C  
ANISOU  232  CD  ARG A  -5     5520   3173   4249   1087    445    280       C  
ATOM    233  NE  ARG A  -5     -23.583 -20.711  -8.314  1.00 34.44           N  
ANISOU  233  NE  ARG A  -5     5421   2854   4810    661    371    342       N  
ATOM    234  CZ  ARG A  -5     -23.896 -21.956  -7.964  1.00 34.11           C  
ANISOU  234  CZ  ARG A  -5     5335   2838   4788    552    625    -32       C  
ATOM    235  NH1 ARG A  -5     -23.255 -22.998  -8.489  1.00 34.29           N  
ANISOU  235  NH1 ARG A  -5     5609   2469   4948    645    914    450       N  
ATOM    236  NH2 ARG A  -5     -24.868 -22.162  -7.086  1.00 30.18           N  
ANISOU  236  NH2 ARG A  -5     4622   2148   4695    514    222    -46       N  
ATOM    237  N   HIS A  -4     -20.948 -17.591 -13.872  1.00 37.11           N  
ANISOU  237  N   HIS A  -4     6116   3534   4448   1413   1040     89       N  
ATOM    238  CA  HIS A  -4     -20.245 -16.722 -14.813  1.00 39.39           C  
ANISOU  238  CA  HIS A  -4     6226   4493   4246   1460   1284    223       C  
ATOM    239  C   HIS A  -4     -20.707 -15.260 -14.749  1.00 40.22           C  
ANISOU  239  C   HIS A  -4     5947   4447   4885   1249   1189    198       C  
ATOM    240  O   HIS A  -4     -19.978 -14.359 -15.164  1.00 43.19           O  
ANISOU  240  O   HIS A  -4     6451   5115   4842   1150    949   1305       O  
ATOM    241  CB  HIS A  -4     -20.366 -17.278 -16.233  1.00 39.93           C  
ANISOU  241  CB  HIS A  -4     6162   4499   4508   1543   1465   -142       C  
ATOM    242  CG  HIS A  -4     -19.857 -18.678 -16.368  1.00 45.17           C  
ANISOU  242  CG  HIS A  -4     6871   4864   5427   1998   1706   -521       C  
ATOM    243  ND1 HIS A  -4     -18.538 -18.965 -16.645  1.00 50.87           N  
ANISOU  243  ND1 HIS A  -4     7095   5796   6436   2245   2138   -470       N  
ATOM    244  CD2 HIS A  -4     -20.483 -19.872 -16.239  1.00 46.09           C  
ANISOU  244  CD2 HIS A  -4     7255   5079   5177   1741   1538   -628       C  
ATOM    245  CE1 HIS A  -4     -18.376 -20.276 -16.697  1.00 53.73           C  
ANISOU  245  CE1 HIS A  -4     7568   5767   7079   2047   1946   -269       C  
ATOM    246  NE2 HIS A  -4     -19.541 -20.849 -16.454  1.00 52.61           N  
ANISOU  246  NE2 HIS A  -4     7474   5402   7114   1991   1444   -775       N  
ATOM    247  N   GLU A  -3     -21.911 -15.035 -14.226  1.00 38.56           N  
ANISOU  247  N   GLU A  -3     6108   4318   4223   1278   1152   -295       N  
ATOM    248  CA  GLU A  -3     -22.471 -13.692 -14.107  1.00 37.75           C  
ANISOU  248  CA  GLU A  -3     6143   3943   4254   1014    926    335       C  
ATOM    249  C   GLU A  -3     -21.985 -13.033 -12.817  1.00 36.29           C  
ANISOU  249  C   GLU A  -3     5863   3603   4320    674   1016    393       C  
ATOM    250  O   GLU A  -3     -21.660 -13.717 -11.846  1.00 35.90           O  
ANISOU  250  O   GLU A  -3     6267   2782   4591    434    903    264       O  
ATOM    251  CB  GLU A  -3     -24.010 -13.752 -14.162  1.00 42.08           C  
ANISOU  251  CB  GLU A  -3     6290   4734   4962    811    390    761       C  
ATOM    252  CG  GLU A  -3     -24.735 -12.409 -14.279  1.00 46.63           C  
ANISOU  252  CG  GLU A  -3     6880   5132   5704   1290    528    455       C  
ATOM    253  CD  GLU A  -3     -24.358 -11.619 -15.520  1.00 51.54           C  
ANISOU  253  CD  GLU A  -3     8022   5412   6147   1321    619    955       C  
ATOM    254  OE1 GLU A  -3     -23.475 -10.744 -15.406  1.00 51.56           O  
ANISOU  254  OE1 GLU A  -3     8096   5433   6059   1310    614   1242       O  
ATOM    255  OE2 GLU A  -3     -24.932 -11.875 -16.603  1.00 56.83           O  
ANISOU  255  OE2 GLU A  -3     9002   5905   6684   1519    701  -1059       O  
ATOM    256  N   THR A  -2     -22.064 -11.703 -12.802  1.00 35.07           N  
ANISOU  256  N   THR A  -2     5406   3655   4263    584    970    748       N  
ATOM    257  CA  THR A  -2     -21.725 -10.874 -11.651  1.00 34.50           C  
ANISOU  257  CA  THR A  -2     5062   3604   4441    553   1066    668       C  
ATOM    258  C   THR A  -2     -22.948  -9.989 -11.386  1.00 35.29           C  
ANISOU  258  C   THR A  -2     5078   3728   4600    535   1251    631       C  
ATOM    259  O   THR A  -2     -23.306  -9.158 -12.221  1.00 37.69           O  
ANISOU  259  O   THR A  -2     5731   3694   4896    661    710    514       O  
ATOM    260  CB  THR A  -2     -20.496  -9.991 -11.924  1.00 37.84           C  
ANISOU  260  CB  THR A  -2     5295   4172   4910    212    915    722       C  
ATOM    261  OG1 THR A  -2     -19.343 -10.819 -12.118  1.00 41.51           O  
ANISOU  261  OG1 THR A  -2     5255   4419   6098    339   1200   1602       O  
ATOM    262  CG2 THR A  -2     -20.247  -9.049 -10.756  1.00 39.85           C  
ANISOU  262  CG2 THR A  -2     5982   4147   5010   -236    489    790       C  
ATOM    263  N   TYR A  -1     -23.576 -10.176 -10.230  1.00 31.92           N  
ANISOU  263  N   TYR A  -1     4973   3246   3907    480    837    304       N  
ATOM    264  CA  TYR A  -1     -24.752  -9.396  -9.862  1.00 30.59           C  
ANISOU  264  CA  TYR A  -1     4722   3149   3750    286    844    425       C  
ATOM    265  C   TYR A  -1     -24.399  -8.311  -8.850  1.00 32.91           C  
ANISOU  265  C   TYR A  -1     4993   2849   4659     24    950    161       C  
ATOM    266  O   TYR A  -1     -23.918  -8.603  -7.755  1.00 38.47           O  
ANISOU  266  O   TYR A  -1     5183   4344   5089    -11    556    -85       O  
ATOM    267  CB  TYR A  -1     -25.843 -10.307  -9.297  1.00 28.15           C  
ANISOU  267  CB  TYR A  -1     4495   2258   3942    378    783   -164       C  
ATOM    268  CG  TYR A  -1     -26.668 -11.004 -10.355  1.00 28.81           C  
ANISOU  268  CG  TYR A  -1     4643   2700   3602    548    660     27       C  
ATOM    269  CD1 TYR A  -1     -27.801 -10.403 -10.888  1.00 30.34           C  
ANISOU  269  CD1 TYR A  -1     4852   3014   3660    756    609     52       C  
ATOM    270  CD2 TYR A  -1     -26.315 -12.263 -10.822  1.00 27.80           C  
ANISOU  270  CD2 TYR A  -1     5067   2628   2866    199    926     37       C  
ATOM    271  CE1 TYR A  -1     -28.559 -11.036 -11.855  1.00 32.97           C  
ANISOU  271  CE1 TYR A  -1     5339   3290   3896    650    499   -273       C  
ATOM    272  CE2 TYR A  -1     -27.066 -12.904 -11.789  1.00 29.50           C  
ANISOU  272  CE2 TYR A  -1     4942   2924   3342    344    704   -136       C  
ATOM    273  CZ  TYR A  -1     -28.187 -12.286 -12.301  1.00 32.21           C  
ANISOU  273  CZ  TYR A  -1     5317   3065   3854    608    526      6       C  
ATOM    274  OH  TYR A  -1     -28.938 -12.920 -13.264  1.00 37.97           O  
ANISOU  274  OH  TYR A  -1     6398   3298   4729   -583    490   -225       O  
ATOM    275  N   LEU A 218     -24.690  -6.919  -9.124  1.00 31.18           N  
ANISOU  275  N   LEU A 218     4853   2539   4454     79    519     60       N  
ATOM    276  CA  LEU A 218     -24.435  -5.892  -8.169  1.00 29.59           C  
ANISOU  276  CA  LEU A 218     4496   2279   4468     40    222    225       C  
ATOM    277  C   LEU A 218     -25.809  -5.354  -7.847  1.00 30.32           C  
ANISOU  277  C   LEU A 218     4608   2400   4511    -83    632     27       C  
ATOM    278  O   LEU A 218     -26.428  -4.663  -8.661  1.00 34.53           O  
ANISOU  278  O   LEU A 218     5263   2657   5200    408    110   -176       O  
ATOM    279  CB  LEU A 218     -23.524  -4.843  -8.803  1.00 32.49           C  
ANISOU  279  CB  LEU A 218     4864   2578   4900   -207    598    135       C  
ATOM    280  CG  LEU A 218     -22.920  -3.742  -7.935  1.00 34.49           C  
ANISOU  280  CG  LEU A 218     5088   2565   5450   -243    780   -165       C  
ATOM    281  CD1 LEU A 218     -21.721  -3.184  -8.666  1.00 36.69           C  
ANISOU  281  CD1 LEU A 218     5548   2627   5766   -671    868     53       C  
ATOM    282  CD2 LEU A 218     -23.919  -2.642  -7.626  1.00 32.43           C  
ANISOU  282  CD2 LEU A 218     5648   1982   4690   -110    252   -402       C  
ATOM    283  N   CYS A 219     -26.300  -5.735  -6.678  1.00 28.71           N  
ANISOU  283  N   CYS A 219     4652   1677   4580   -258    420    306       N  
ATOM    284  CA  CYS A 219     -27.462  -5.100  -6.073  1.00 30.56           C  
ANISOU  284  CA  CYS A 219     4519   2241   4849    -46    372    313       C  
ATOM    285  C   CYS A 219     -26.957  -3.873  -5.326  1.00 31.93           C  
ANISOU  285  C   CYS A 219     4877   2413   4840   -135    426    194       C  
ATOM    286  O   CYS A 219     -25.829  -3.862  -4.842  1.00 32.04           O  
ANISOU  286  O   CYS A 219     4774   2148   5249    478    435   -377       O  
ATOM    287  CB  CYS A 219     -28.151  -6.063  -5.112  1.00 30.44           C  
ANISOU  287  CB  CYS A 219     4444   2554   4566    107    336    465       C  
ATOM    288  SG  CYS A 219     -28.588  -7.649  -5.865  1.00 38.17           S  
ANISOU  288  SG  CYS A 219     5851   2603   6047   -273    -52    460       S  
ATOM    289  N   PHE A 220     -27.775  -2.831  -5.244  1.00 32.62           N  
ANISOU  289  N   PHE A 220     5133   2521   4737    -28    662    216       N  
ATOM    290  CA  PHE A 220     -27.358  -1.617  -4.550  1.00 32.50           C  
ANISOU  290  CA  PHE A 220     5342   2458   4547     -5    736    296       C  
ATOM    291  C   PHE A 220     -28.521  -0.917  -3.868  1.00 32.32           C  
ANISOU  291  C   PHE A 220     5444   2407   4426   -164    940    402       C  
ATOM    292  O   PHE A 220     -29.663  -1.015  -4.317  1.00 33.85           O  
ANISOU  292  O   PHE A 220     5283   2757   4822     58    861    728       O  
ATOM    293  CB  PHE A 220     -26.621  -0.649  -5.502  1.00 32.36           C  
ANISOU  293  CB  PHE A 220     5324   2446   4525     10    841    177       C  
ATOM    294  CG  PHE A 220     -27.527   0.081  -6.461  1.00 35.25           C  
ANISOU  294  CG  PHE A 220     6069   2711   4613    294    694    312       C  
ATOM    295  CD1 PHE A 220     -27.836  -0.466  -7.711  1.00 34.76           C  
ANISOU  295  CD1 PHE A 220     6039   2283   4885    246    547    125       C  
ATOM    296  CD2 PHE A 220     -28.075   1.324  -6.119  1.00 33.52           C  
ANISOU  296  CD2 PHE A 220     5812   2488   4433    -61    821    235       C  
ATOM    297  CE1 PHE A 220     -28.672   0.214  -8.597  1.00 32.85           C  
ANISOU  297  CE1 PHE A 220     5765   2026   4691    173    644     21       C  
ATOM    298  CE2 PHE A 220     -28.920   1.998  -6.998  1.00 32.64           C  
ANISOU  298  CE2 PHE A 220     5966   1715   4719    168    912    185       C  
ATOM    299  CZ  PHE A 220     -29.221   1.442  -8.237  1.00 31.05           C  
ANISOU  299  CZ  PHE A 220     5427   1942   4428    192    903    421       C  
ATOM    300  N   THR A 221     -28.220  -0.228  -2.774  1.00 33.26           N  
ANISOU  300  N   THR A 221     6113   2251   4272   -370   1106    436       N  
ATOM    301  CA  THR A 221     -29.119   0.797  -2.253  1.00 36.07           C  
ANISOU  301  CA  THR A 221     6129   2895   4680   -157   1233    237       C  
ATOM    302  C   THR A 221     -28.312   2.064  -2.097  1.00 38.05           C  
ANISOU  302  C   THR A 221     6721   2836   4900   -202   1208   -101       C  
ATOM    303  O   THR A 221     -27.106   2.024  -1.808  1.00 39.92           O  
ANISOU  303  O   THR A 221     6893   3312   4962    136   1049   -329       O  
ATOM    304  CB  THR A 221     -29.769   0.443  -0.902  1.00 37.34           C  
ANISOU  304  CB  THR A 221     6589   2890   4708   -563   1202    454       C  
ATOM    305  OG1 THR A 221     -28.773   0.468   0.123  1.00 46.56           O  
ANISOU  305  OG1 THR A 221     7880   4893   4918   -702    805   -371       O  
ATOM    306  CG2 THR A 221     -30.413  -0.919  -0.952  1.00 32.08           C  
ANISOU  306  CG2 THR A 221     5921   2500   3765      9   1145    166       C  
ATOM    307  N   MET A 222     -28.996   3.184  -2.281  1.00 38.13           N  
ANISOU  307  N   MET A 222     6551   3141   4793   -111   1103    257       N  
ATOM    308  CA  MET A 222     -28.375   4.485  -2.304  1.00 40.04           C  
ANISOU  308  CA  MET A 222     7289   2871   5052    -78   1192   -136       C  
ATOM    309  C   MET A 222     -29.258   5.446  -1.528  1.00 42.46           C  
ANISOU  309  C   MET A 222     7382   3091   5659      3   1633    -34       C  
ATOM    310  O   MET A 222     -30.452   5.562  -1.811  1.00 42.81           O  
ANISOU  310  O   MET A 222     7290   2842   6131    -54   1706   -743       O  
ATOM    311  CB  MET A 222     -28.215   4.927  -3.759  1.00 39.82           C  
ANISOU  311  CB  MET A 222     7134   2922   5073   -237   1559   -283       C  
ATOM    312  CG  MET A 222     -27.470   6.230  -3.984  1.00 40.09           C  
ANISOU  312  CG  MET A 222     7326   2665   5240    -23   2033   -385       C  
ATOM    313  SD  MET A 222     -27.192   6.503  -5.738  1.00 42.32           S  
ANISOU  313  SD  MET A 222     7693   2926   5461   -328   1572    793       S  
ATOM    314  CE  MET A 222     -28.827   6.893  -6.312  1.00 33.36           C  
ANISOU  314  CE  MET A 222     7113   1116   4444    -78   2318     10       C  
ATOM    315  N   GLU A 223     -28.666   6.101  -0.531  1.00 46.27           N  
ANISOU  315  N   GLU A 223     8168   3400   6010   -320   1679   -252       N  
ATOM    316  CA  GLU A 223     -29.297   7.220   0.149  1.00 50.39           C  
ANISOU  316  CA  GLU A 223     9040   3805   6301   -233   1916   -672       C  
ATOM    317  C   GLU A 223     -28.776   8.528  -0.452  1.00 51.45           C  
ANISOU  317  C   GLU A 223     9143   3621   6781   -112   1747   -620       C  
ATOM    318  O   GLU A 223     -27.568   8.804  -0.425  1.00 51.82           O  
ANISOU  318  O   GLU A 223     9379   3498   6813   -633   1818  -1256       O  
ATOM    319  CB  GLU A 223     -29.044   7.160   1.657  1.00 57.40           C  
ANISOU  319  CB  GLU A 223     9974   5276   6558   -711   1207   -571       C  
ATOM    320  CG  GLU A 223     -29.809   8.218   2.444  1.00 66.90           C  
ANISOU  320  CG  GLU A 223    11050   6165   8201      8   1837   -913       C  
ATOM    321  CD  GLU A 223     -29.597   8.155   3.949  1.00 74.24           C  
ANISOU  321  CD  GLU A 223    12295   7752   8159     43   2011  -1410       C  
ATOM    322  OE1 GLU A 223     -30.496   8.623   4.681  1.00 73.07           O  
ANISOU  322  OE1 GLU A 223    11988   6028   9747    -81   2331  -1572       O  
ATOM    323  OE2 GLU A 223     -28.544   7.652   4.408  1.00 82.93           O  
ANISOU  323  OE2 GLU A 223    12853  10503   8152    218   1146   -853       O  
ATOM    324  N   VAL A 224     -29.700   9.309  -1.006  1.00 49.82           N  
ANISOU  324  N   VAL A 224     8927   3217   6783    297   2229   -805       N  
ATOM    325  CA  VAL A 224     -29.393  10.598  -1.618  1.00 51.44           C  
ANISOU  325  CA  VAL A 224     9388   3575   6579    300   1983   -445       C  
ATOM    326  C   VAL A 224     -29.728  11.705  -0.615  1.00 56.27           C  
ANISOU  326  C   VAL A 224    10353   3540   7484    497   2117   -744       C  
ATOM    327  O   VAL A 224     -30.904  11.918  -0.283  1.00 55.15           O  
ANISOU  327  O   VAL A 224    10300   3169   7483    507   2199    269       O  
ATOM    328  CB  VAL A 224     -30.171  10.792  -2.939  1.00 50.35           C  
ANISOU  328  CB  VAL A 224     9273   3290   6567    600   2255   -323       C  
ATOM    329  CG1 VAL A 224     -29.869  12.149  -3.564  1.00 47.05           C  
ANISOU  329  CG1 VAL A 224     8126   2701   7048    841   2811   -870       C  
ATOM    330  CG2 VAL A 224     -29.868   9.659  -3.917  1.00 47.60           C  
ANISOU  330  CG2 VAL A 224     8166   2797   7120    761   1966   -268       C  
ATOM    331  N   VAL A 225     -28.684  12.391  -0.141  1.00 56.99           N  
ANISOU  331  N   VAL A 225    10724   3372   7554     25   2363   -625       N  
ATOM    332  CA  VAL A 225     -28.799  13.418   0.903  1.00 58.77           C  
ANISOU  332  CA  VAL A 225    11240   3800   7291   -400   2077   -842       C  
ATOM    333  C   VAL A 225     -28.426  14.796   0.350  1.00 61.43           C  
ANISOU  333  C   VAL A 225    11639   3677   8023    -57   2590   -828       C  
ATOM    334  O   VAL A 225     -27.260  15.065   0.044  1.00 63.17           O  
ANISOU  334  O   VAL A 225    11770   3990   8240   -164   2780   -668       O  
ATOM    335  CB  VAL A 225     -27.952  13.066   2.159  1.00 57.64           C  
ANISOU  335  CB  VAL A 225    11500   3240   7158   -458   1752  -1523       C  
ATOM    336  CG1 VAL A 225     -27.979  14.190   3.188  1.00 55.18           C  
ANISOU  336  CG1 VAL A 225    11412   3068   6485   -553   3492  -1128       C  
ATOM    337  CG2 VAL A 225     -28.441  11.773   2.803  1.00 61.32           C  
ANISOU  337  CG2 VAL A 225    11537   4309   7451  -1159   1231   -798       C  
ATOM    338  N   LYS A 226     -29.434  15.655   0.227  1.00 66.83           N  
ANISOU  338  N   LYS A 226    11795   4316   9281    396   2813   -725       N  
ATOM    339  CA  LYS A 226     -29.257  17.034  -0.224  1.00 68.10           C  
ANISOU  339  CA  LYS A 226    12165   4290   9420    309   2871   -748       C  
ATOM    340  C   LYS A 226     -29.765  17.986   0.863  1.00 70.70           C  
ANISOU  340  C   LYS A 226    13179   4326   9355    288   2435  -1116       C  
ATOM    341  O   LYS A 226     -30.861  17.790   1.392  1.00 69.15           O  
ANISOU  341  O   LYS A 226    13535   3310   9425   -855   2311   -544       O  
ATOM    342  CB  LYS A 226     -29.992  17.247  -1.551  1.00 71.29           C  
ANISOU  342  CB  LYS A 226    12983   3975  10128    984   2208   -869       C  
ATOM    343  CG  LYS A 226     -29.519  18.454  -2.341  1.00 77.74           C  
ANISOU  343  CG  LYS A 226    13534   5225  10777   1546   3259    187       C  
ATOM    344  CD  LYS A 226     -30.211  18.537  -3.695  1.00 78.41           C  
ANISOU  344  CD  LYS A 226    14338   5394  10058   1604   3922   -145       C  
ATOM    345  CE  LYS A 226     -30.529  19.978  -4.084  1.00 81.28           C  
ANISOU  345  CE  LYS A 226    14506   5530  10846    590   4518   1326       C  
ATOM    346  NZ  LYS A 226     -29.364  20.909  -4.032  1.00 79.19           N  
ANISOU  346  NZ  LYS A 226    14574   6461   9052    -45   5526   2033       N  
ATOM    347  N   HIS A 227     -28.974  19.014   1.179  1.00 76.66           N  
ANISOU  347  N   HIS A 227    14127   4540  10458   -119   2251  -1408       N  
ATOM    348  CA  HIS A 227     -29.166  19.824   2.401  1.00 87.92           C  
ANISOU  348  CA  HIS A 227    16226   5925  11251    -73   2359  -2377       C  
ATOM    349  C   HIS A 227     -30.559  20.450   2.639  1.00 88.37           C  
ANISOU  349  C   HIS A 227    16102   5374  12101    -21   1586  -1858       C  
ATOM    350  O   HIS A 227     -30.991  20.549   3.793  1.00 98.11           O  
ANISOU  350  O   HIS A 227    17940   6469  12869  -1191   2900  -2200       O  
ATOM    351  CB  HIS A 227     -28.053  20.878   2.551  1.00 99.01           C  
ANISOU  351  CB  HIS A 227    17222   6780  13617   -734   1921  -2510       C  
ATOM    352  CG  HIS A 227     -27.984  21.501   3.917  1.00112.70           C  
ANISOU  352  CG  HIS A 227    20548   8832  13440   -526    617  -2603       C  
ATOM    353  ND1 HIS A 227     -28.189  22.849   4.132  1.00117.45           N  
ANISOU  353  ND1 HIS A 227    21894   8442  14289    317     85   -970       N  
ATOM    354  CD2 HIS A 227     -27.746  20.959   5.136  1.00116.37           C  
ANISOU  354  CD2 HIS A 227    21130   9215  13869   -777   -330  -2213       C  
ATOM    355  CE1 HIS A 227     -28.074  23.111   5.423  1.00117.37           C  
ANISOU  355  CE1 HIS A 227    21795   7748  15051   1036    186  -3561       C  
ATOM    356  NE2 HIS A 227     -27.807  21.982   6.054  1.00118.20           N  
ANISOU  356  NE2 HIS A 227    21988  10150  12770    243   -952  -2240       N  
ATOM    357  N   HIS A 228     -31.256  20.851   1.573  1.00 85.56           N  
ANISOU  357  N   HIS A 228    15515   4663  12329   1022   1800  -1700       N  
ATOM    358  CA  HIS A 228     -32.580  21.497   1.714  1.00 80.75           C  
ANISOU  358  CA  HIS A 228    15370   4421  10890    856   2477  -1570       C  
ATOM    359  C   HIS A 228     -33.744  20.710   1.096  1.00 74.48           C  
ANISOU  359  C   HIS A 228    13621   4347  10328   1099   3777  -1215       C  
ATOM    360  O   HIS A 228     -34.855  21.233   0.940  1.00 74.23           O  
ANISOU  360  O   HIS A 228    13436   5370   9397   1549   5232   -457       O  
ATOM    361  CB  HIS A 228     -32.545  22.926   1.164  1.00 79.46           C  
ANISOU  361  CB  HIS A 228    15199   3903  11087   1366   2376  -2019       C  
ATOM    362  CG  HIS A 228     -31.459  23.769   1.750  1.00 82.15           C  
ANISOU  362  CG  HIS A 228    15835   3150  12225   1381   1701  -1683       C  
ATOM    363  ND1 HIS A 228     -31.589  24.416   2.960  1.00 87.53           N  
ANISOU  363  ND1 HIS A 228    16198   5114  11945   1540   2189  -1724       N  
ATOM    364  CD2 HIS A 228     -30.216  24.058   1.298  1.00 79.00           C  
ANISOU  364  CD2 HIS A 228    16130   1299  12585   1994   2453  -1891       C  
ATOM    365  CE1 HIS A 228     -30.475  25.077   3.224  1.00 96.37           C  
ANISOU  365  CE1 HIS A 228    16820   5901  13894    715   2060   -778       C  
ATOM    366  NE2 HIS A 228     -29.627  24.878   2.229  1.00 91.13           N  
ANISOU  366  NE2 HIS A 228    16599   4893  13132    117   1413  -1563       N  
ATOM    367  N   SER A 229     -33.476  19.452   0.761  1.00 73.94           N  
ANISOU  367  N   SER A 229    14338   4297   9459    996   3165  -1320       N  
ATOM    368  CA  SER A 229     -34.456  18.569   0.137  1.00 78.58           C  
ANISOU  368  CA  SER A 229    13354   5864  10638    371   2923   -478       C  
ATOM    369  C   SER A 229     -34.778  17.389   1.054  1.00 72.11           C  
ANISOU  369  C   SER A 229    12429   5642   9327   1393   2600   -651       C  
ATOM    370  O   SER A 229     -33.995  17.095   1.965  1.00 68.06           O  
ANISOU  370  O   SER A 229    11991   4489   9378   2714   3517    705       O  
ATOM    371  CB  SER A 229     -33.921  18.058  -1.205  1.00 83.22           C  
ANISOU  371  CB  SER A 229    13803   7086  10730    150   2611  -1319       C  
ATOM    372  OG  SER A 229     -33.707  19.132  -2.104  1.00 91.85           O  
ANISOU  372  OG  SER A 229    14680   9480  10739    493   2185     49       O  
ATOM    373  N   PRO A 230     -35.939  16.725   0.839  1.00 70.24           N  
ANISOU  373  N   PRO A 230    12509   4818   9361   1323   3247   -788       N  
ATOM    374  CA  PRO A 230     -36.138  15.418   1.460  1.00 70.35           C  
ANISOU  374  CA  PRO A 230    12134   4844   9751   1499   3368   -613       C  
ATOM    375  C   PRO A 230     -35.101  14.410   0.970  1.00 66.03           C  
ANISOU  375  C   PRO A 230    11807   4756   8525   1221   3160   -511       C  
ATOM    376  O   PRO A 230     -34.728  14.410  -0.214  1.00 61.21           O  
ANISOU  376  O   PRO A 230    11737   3176   8344   -194   3024   -986       O  
ATOM    377  CB  PRO A 230     -37.542  15.002   0.990  1.00 70.36           C  
ANISOU  377  CB  PRO A 230    12167   4792   9771    704   3942      3       C  
ATOM    378  CG  PRO A 230     -37.889  15.927  -0.128  1.00 74.48           C  
ANISOU  378  CG  PRO A 230    13401   4915   9981   1604   3619   -222       C  
ATOM    379  CD  PRO A 230     -37.180  17.204   0.203  1.00 74.33           C  
ANISOU  379  CD  PRO A 230    12791   5756   9693   1254   3100   -211       C  
ATOM    380  N   VAL A 231     -34.623  13.590   1.902  1.00 61.63           N  
ANISOU  380  N   VAL A 231    10568   4280   8565   1104   3471   -465       N  
ATOM    381  CA  VAL A 231     -33.757  12.461   1.599  1.00 57.83           C  
ANISOU  381  CA  VAL A 231    10735   3735   7501    816   3382   -540       C  
ATOM    382  C   VAL A 231     -34.519  11.483   0.696  1.00 61.72           C  
ANISOU  382  C   VAL A 231    10455   5191   7803    773   2753   -635       C  
ATOM    383  O   VAL A 231     -35.673  11.138   0.974  1.00 64.49           O  
ANISOU  383  O   VAL A 231    10200   5622   8681   1656   3199   -708       O  
ATOM    384  CB  VAL A 231     -33.188  11.806   2.899  1.00 60.94           C  
ANISOU  384  CB  VAL A 231    11143   4350   7661    945   3099   -404       C  
ATOM    385  CG1 VAL A 231     -34.226  11.742   4.018  1.00 61.37           C  
ANISOU  385  CG1 VAL A 231    11483   4364   7470   1631   3059    453       C  
ATOM    386  CG2 VAL A 231     -32.602  10.428   2.634  1.00 60.99           C  
ANISOU  386  CG2 VAL A 231    11221   4007   7945    569   3148   -241       C  
ATOM    387  N   SER A 232     -33.880  11.089  -0.407  1.00 60.58           N  
ANISOU  387  N   SER A 232    10539   5204   7273    776   2289   -688       N  
ATOM    388  CA  SER A 232     -34.444  10.103  -1.324  1.00 56.12           C  
ANISOU  388  CA  SER A 232     9500   4094   7728    993   2322   -351       C  
ATOM    389  C   SER A 232     -33.588   8.842  -1.432  1.00 51.86           C  
ANISOU  389  C   SER A 232     8783   3795   7125    479   2399   -261       C  
ATOM    390  O   SER A 232     -32.401   8.838  -1.089  1.00 52.22           O  
ANISOU  390  O   SER A 232     8980   4212   6648    -27   2115   -769       O  
ATOM    391  CB  SER A 232     -34.718  10.710  -2.709  1.00 55.37           C  
ANISOU  391  CB  SER A 232     9485   3993   7557    980   3189   -179       C  
ATOM    392  OG  SER A 232     -33.533  11.201  -3.290  1.00 55.80           O  
ANISOU  392  OG  SER A 232    10460   4339   6399   1000   3239   1190       O  
ATOM    393  N   TRP A 233     -34.217   7.774  -1.907  1.00 50.31           N  
ANISOU  393  N   TRP A 233     8667   3953   6495    766   2622   -693       N  
ATOM    394  CA  TRP A 233     -33.607   6.459  -1.962  1.00 48.72           C  
ANISOU  394  CA  TRP A 233     8160   3940   6411    725   2207   -290       C  
ATOM    395  C   TRP A 233     -33.729   5.861  -3.349  1.00 50.32           C  
ANISOU  395  C   TRP A 233     8228   4316   6574    873   1785   -449       C  
ATOM    396  O   TRP A 233     -34.767   6.004  -4.008  1.00 56.84           O  
ANISOU  396  O   TRP A 233     8364   5771   7461   1074   1473   -578       O  
ATOM    397  CB  TRP A 233     -34.271   5.531  -0.951  1.00 50.73           C  
ANISOU  397  CB  TRP A 233     8891   3966   6417    521   2379   -363       C  
ATOM    398  CG  TRP A 233     -33.994   5.890   0.477  1.00 52.56           C  
ANISOU  398  CG  TRP A 233     8863   4559   6549    543   1938   -214       C  
ATOM    399  CD1 TRP A 233     -34.675   6.795   1.250  1.00 52.37           C  
ANISOU  399  CD1 TRP A 233     9124   4327   6445    396   2401     80       C  
ATOM    400  CD2 TRP A 233     -32.966   5.344   1.307  1.00 50.84           C  
ANISOU  400  CD2 TRP A 233     8805   4328   6183    293   1893    -78       C  
ATOM    401  NE1 TRP A 233     -34.129   6.848   2.510  1.00 53.97           N  
ANISOU  401  NE1 TRP A 233     9193   4592   6720    391   1953    338       N  
ATOM    402  CE2 TRP A 233     -33.081   5.965   2.577  1.00 51.65           C  
ANISOU  402  CE2 TRP A 233     8608   4668   6346    204   2041   -389       C  
ATOM    403  CE3 TRP A 233     -31.953   4.386   1.103  1.00 50.02           C  
ANISOU  403  CE3 TRP A 233     8236   4597   6170     40   1916   -191       C  
ATOM    404  CZ2 TRP A 233     -32.222   5.659   3.648  1.00 51.80           C  
ANISOU  404  CZ2 TRP A 233     8669   4539   6473     32   1987   -524       C  
ATOM    405  CZ3 TRP A 233     -31.094   4.080   2.169  1.00 53.61           C  
ANISOU  405  CZ3 TRP A 233     8802   5473   6094    -34   1585   -426       C  
ATOM    406  CH2 TRP A 233     -31.238   4.721   3.428  1.00 52.17           C  
ANISOU  406  CH2 TRP A 233     8844   4574   6405    210   1475   -550       C  
ATOM    407  N   LYS A 234     -32.657   5.208  -3.791  1.00 46.63           N  
ANISOU  407  N   LYS A 234     7719   3950   6045    769   1490     61       N  
ATOM    408  CA  LYS A 234     -32.685   4.402  -5.014  1.00 45.29           C  
ANISOU  408  CA  LYS A 234     7779   3314   6113    712   1226    194       C  
ATOM    409  C   LYS A 234     -32.093   3.035  -4.741  1.00 41.23           C  
ANISOU  409  C   LYS A 234     6807   3277   5578    530   1047   -218       C  
ATOM    410  O   LYS A 234     -31.172   2.889  -3.937  1.00 44.62           O  
ANISOU  410  O   LYS A 234     7009   4111   5833    487    819   -297       O  
ATOM    411  CB  LYS A 234     -31.944   5.081  -6.173  1.00 45.83           C  
ANISOU  411  CB  LYS A 234     7782   3639   5989    832   1476    -24       C  
ATOM    412  CG  LYS A 234     -32.537   6.425  -6.584  1.00 52.18           C  
ANISOU  412  CG  LYS A 234     9247   3779   6800    829    812    487       C  
ATOM    413  CD  LYS A 234     -32.035   6.912  -7.933  1.00 54.70           C  
ANISOU  413  CD  LYS A 234     8920   4304   7558    486   1581    597       C  
ATOM    414  CE  LYS A 234     -32.322   8.399  -8.111  1.00 64.04           C  
ANISOU  414  CE  LYS A 234     9774   5049   9508   1729   1049   1453       C  
ATOM    415  NZ  LYS A 234     -33.774   8.739  -8.085  1.00 61.45           N  
ANISOU  415  NZ  LYS A 234    10266   4191   8890   2681    675   2184       N  
ATOM    416  N   ARG A 235     -32.654   2.032  -5.398  1.00 37.09           N  
ANISOU  416  N   ARG A 235     6372   2905   4814    642   1108    237       N  
ATOM    417  CA  ARG A 235     -32.076   0.705  -5.400  1.00 37.22           C  
ANISOU  417  CA  ARG A 235     6051   2878   5211    600    760    383       C  
ATOM    418  C   ARG A 235     -32.148   0.084  -6.790  1.00 37.62           C  
ANISOU  418  C   ARG A 235     5921   2888   5482    658    673    238       C  
ATOM    419  O   ARG A 235     -32.865   0.574  -7.672  1.00 35.95           O  
ANISOU  419  O   ARG A 235     6079   2336   5241   1001   1226    541       O  
ATOM    420  CB  ARG A 235     -32.714  -0.184  -4.326  1.00 37.96           C  
ANISOU  420  CB  ARG A 235     5901   2477   6043    347    960    372       C  
ATOM    421  CG  ARG A 235     -34.201  -0.387  -4.453  1.00 44.35           C  
ANISOU  421  CG  ARG A 235     5968   3363   7519    401   1029    180       C  
ATOM    422  CD  ARG A 235     -34.833  -0.635  -3.092  1.00 52.18           C  
ANISOU  422  CD  ARG A 235     7812   4514   7498    703   1544    189       C  
ATOM    423  NE  ARG A 235     -36.271  -0.376  -3.167  1.00 60.43           N  
ANISOU  423  NE  ARG A 235     7791   6008   9159    602   1673    127       N  
ATOM    424  CZ  ARG A 235     -37.214  -1.299  -3.363  1.00 59.92           C  
ANISOU  424  CZ  ARG A 235     7746   5852   9168    565   2002   -173       C  
ATOM    425  NH1 ARG A 235     -38.481  -0.920  -3.430  1.00 63.26           N  
ANISOU  425  NH1 ARG A 235     7378   6466  10190   -118   1293    265       N  
ATOM    426  NH2 ARG A 235     -36.907  -2.591  -3.483  1.00 54.03           N  
ANISOU  426  NH2 ARG A 235     7327   5566   7633     54   1385   -564       N  
ATOM    427  N   GLY A 236     -31.374  -0.974  -6.994  1.00 35.04           N  
ANISOU  427  N   GLY A 236     5710   2602   4999    346    772    130       N  
ATOM    428  CA  GLY A 236     -31.439  -1.704  -8.236  1.00 32.57           C  
ANISOU  428  CA  GLY A 236     5157   2367   4851    428    586    250       C  
ATOM    429  C   GLY A 236     -30.459  -2.841  -8.359  1.00 31.34           C  
ANISOU  429  C   GLY A 236     4822   2458   4624    363    255      8       C  
ATOM    430  O   GLY A 236     -29.810  -3.231  -7.389  1.00 30.39           O  
ANISOU  430  O   GLY A 236     5353   1964   4227    370    347    -61       O  
ATOM    431  N   VAL A 237     -30.378  -3.377  -9.573  1.00 30.51           N  
ANISOU  431  N   VAL A 237     4716   2216   4660    514    417     29       N  
ATOM    432  CA  VAL A 237     -29.548  -4.535  -9.876  1.00 29.97           C  
ANISOU  432  CA  VAL A 237     4940   2052   4395    453    338   -100       C  
ATOM    433  C   VAL A 237     -28.815  -4.252 -11.184  1.00 29.25           C  
ANISOU  433  C   VAL A 237     4936   1787   4387    573    285     69       C  
ATOM    434  O   VAL A 237     -29.437  -3.874 -12.172  1.00 32.24           O  
ANISOU  434  O   VAL A 237     5481   2556   4213    746    158    -13       O  
ATOM    435  CB  VAL A 237     -30.395  -5.842  -9.989  1.00 30.78           C  
ANISOU  435  CB  VAL A 237     4715   2255   4725    363    337   -153       C  
ATOM    436  CG1 VAL A 237     -29.517  -7.054 -10.305  1.00 32.27           C  
ANISOU  436  CG1 VAL A 237     4818   2438   5005    407    361   -440       C  
ATOM    437  CG2 VAL A 237     -31.185  -6.118  -8.712  1.00 30.09           C  
ANISOU  437  CG2 VAL A 237     4375   2299   4759    239    435   -702       C  
ATOM    438  N   PHE A 238     -27.494  -4.409 -11.166  1.00 30.77           N  
ANISOU  438  N   PHE A 238     4912   2016   4762    322    350     38       N  
ATOM    439  CA  PHE A 238     -26.682  -4.435 -12.384  1.00 33.04           C  
ANISOU  439  CA  PHE A 238     5446   2482   4624    507    438     20       C  
ATOM    440  C   PHE A 238     -26.080  -5.823 -12.599  1.00 33.28           C  
ANISOU  440  C   PHE A 238     5618   2511   4513    550    195    -69       C  
ATOM    441  O   PHE A 238     -25.827  -6.558 -11.637  1.00 30.83           O  
ANISOU  441  O   PHE A 238     5943   1378   4391    386    210   -409       O  
ATOM    442  CB  PHE A 238     -25.561  -3.389 -12.317  1.00 34.42           C  
ANISOU  442  CB  PHE A 238     5700   2544   4833    384    574    113       C  
ATOM    443  CG  PHE A 238     -26.043  -1.969 -12.490  1.00 34.30           C  
ANISOU  443  CG  PHE A 238     5772   2756   4501    707    575     20       C  
ATOM    444  CD1 PHE A 238     -26.188  -1.413 -13.771  1.00 34.84           C  
ANISOU  444  CD1 PHE A 238     6101   2623   4514    569    736     79       C  
ATOM    445  CD2 PHE A 238     -26.350  -1.183 -11.375  1.00 31.93           C  
ANISOU  445  CD2 PHE A 238     5588   2159   4384    456    476    124       C  
ATOM    446  CE1 PHE A 238     -26.644  -0.105 -13.935  1.00 34.71           C  
ANISOU  446  CE1 PHE A 238     6317   2449   4421    333   1019    113       C  
ATOM    447  CE2 PHE A 238     -26.800   0.124 -11.535  1.00 31.58           C  
ANISOU  447  CE2 PHE A 238     5802   2046   4150    328    632     98       C  
ATOM    448  CZ  PHE A 238     -26.949   0.664 -12.810  1.00 32.45           C  
ANISOU  448  CZ  PHE A 238     5996   2092   4241    325    857    256       C  
ATOM    449  N   ARG A 239     -25.879  -6.168 -13.869  1.00 34.21           N  
ANISOU  449  N   ARG A 239     5705   2876   4416    610    107    -27       N  
ATOM    450  CA  ARG A 239     -25.108  -7.339 -14.286  1.00 37.27           C  
ANISOU  450  CA  ARG A 239     5942   3241   4975    755    416   -296       C  
ATOM    451  C   ARG A 239     -24.044  -6.879 -15.282  1.00 38.35           C  
ANISOU  451  C   ARG A 239     6147   3118   5305    793    668   -273       C  
ATOM    452  O   ARG A 239     -23.957  -5.682 -15.595  1.00 39.52           O  
ANISOU  452  O   ARG A 239     6366   3406   5243    636    918    326       O  
ATOM    453  CB  ARG A 239     -25.990  -8.377 -14.976  1.00 41.87           C  
ANISOU  453  CB  ARG A 239     6521   3358   6028    563    152   -551       C  
ATOM    454  CG  ARG A 239     -27.201  -8.871 -14.212  1.00 45.35           C  
ANISOU  454  CG  ARG A 239     6616   4146   6466    938    324   -135       C  
ATOM    455  CD  ARG A 239     -27.957  -9.886 -15.060  1.00 54.81           C  
ANISOU  455  CD  ARG A 239     7736   5003   8085    694   -446   -794       C  
ATOM    456  NE  ARG A 239     -28.298  -9.350 -16.378  1.00 66.76           N  
ANISOU  456  NE  ARG A 239     9921   7167   8276   -165   -387    -33       N  
ATOM    457  CZ  ARG A 239     -28.699 -10.070 -17.425  1.00 78.20           C  
ANISOU  457  CZ  ARG A 239    12001   8005   9704   -576   -795   -995       C  
ATOM    458  NH1 ARG A 239     -28.832 -11.394 -17.336  1.00 86.09           N  
ANISOU  458  NH1 ARG A 239    13134   8107  11467   -423    362    728       N  
ATOM    459  NH2 ARG A 239     -28.972  -9.450 -18.572  1.00 68.92           N  
ANISOU  459  NH2 ARG A 239    12110   3905  10171  -3451   2507   1103       N  
ATOM    460  N   ASN A 240     -23.251  -7.829 -15.782  1.00 37.49           N  
ANISOU  460  N   ASN A 240     6272   2909   5061    749    709   -265       N  
ATOM    461  CA  ASN A 240     -22.274  -7.560 -16.833  1.00 41.82           C  
ANISOU  461  CA  ASN A 240     6816   3733   5340   1088   1119    -83       C  
ATOM    462  C   ASN A 240     -22.927  -7.167 -18.170  1.00 45.30           C  
ANISOU  462  C   ASN A 240     7193   4574   5443    902    644   -204       C  
ATOM    463  O   ASN A 240     -24.009  -7.660 -18.507  1.00 40.85           O  
ANISOU  463  O   ASN A 240     7263   3850   4406   1328    205   -415       O  
ATOM    464  CB  ASN A 240     -21.347  -8.767 -17.045  1.00 42.16           C  
ANISOU  464  CB  ASN A 240     6973   3330   5715    829   1237   -379       C  
ATOM    465  CG  ASN A 240     -20.511  -9.115 -15.815  1.00 45.04           C  
ANISOU  465  CG  ASN A 240     7317   3820   5975    710    981   -129       C  
ATOM    466  OD1 ASN A 240     -20.175  -8.259 -14.990  1.00 47.28           O  
ANISOU  466  OD1 ASN A 240     7449   4183   6329    170   1787   -550       O  
ATOM    467  ND2 ASN A 240     -20.158 -10.388 -15.701  1.00 45.90           N  
ANISOU  467  ND2 ASN A 240     7132   4013   6293    965    427   -139       N  
ATOM    468  N   GLN A 241     -22.247  -6.272 -18.895  1.00 49.24           N  
ANISOU  468  N   GLN A 241     8242   4775   5690    802    852    133       N  
ATOM    469  CA  GLN A 241     -22.569  -5.818 -20.270  1.00 50.77           C  
ANISOU  469  CA  GLN A 241     9392   4277   5618   1195    343   -329       C  
ATOM    470  C   GLN A 241     -23.934  -5.147 -20.364  1.00 55.77           C  
ANISOU  470  C   GLN A 241     9327   5918   5942   1388    388    443       C  
ATOM    471  O   GLN A 241     -24.179  -4.149 -19.685  1.00 60.08           O  
ANISOU  471  O   GLN A 241    11044   6396   5387    235   -641   -384       O  
ATOM    472  CB  GLN A 241     -22.395  -6.949 -21.290  1.00 51.04           C  
ANISOU  472  CB  GLN A 241     9930   4044   5418   1404   1129     -9       C  
ATOM    473  CG  GLN A 241     -22.561  -6.577 -22.753  1.00 56.46           C  
ANISOU  473  CG  GLN A 241    10938   4898   5613    975   1626    113       C  
ATOM    474  CD  GLN A 241     -22.171  -7.700 -23.707  1.00 63.76           C  
ANISOU  474  CD  GLN A 241    11718   6258   6249    926   1686   -939       C  
ATOM    475  OE1 GLN A 241     -22.220  -8.891 -23.358  1.00 64.45           O  
ANISOU  475  OE1 GLN A 241    10797   5955   7735    327   2051   -883       O  
ATOM    476  NE2 GLN A 241     -21.782  -7.324 -24.928  1.00 63.87           N  
ANISOU  476  NE2 GLN A 241    11305   6761   6198    202   1117   -356       N  
ATOM    477  N   THR A 246     -20.060  -0.845 -25.835  1.00 80.41           N  
ANISOU  477  N   THR A 246    14015   9244   7292   -199   1744  -1264       N  
ATOM    478  CA  THR A 246     -20.917  -0.704 -24.655  1.00 80.37           C  
ANISOU  478  CA  THR A 246    13586   9328   7620   1468   1829   -110       C  
ATOM    479  C   THR A 246     -20.743  -1.826 -23.611  1.00 81.57           C  
ANISOU  479  C   THR A 246    13562   8861   8569   1710   2531    172       C  
ATOM    480  O   THR A 246     -21.484  -1.870 -22.615  1.00 83.26           O  
ANISOU  480  O   THR A 246    13439   9270   8925   1483   2780    281       O  
ATOM    481  CB  THR A 246     -22.379  -0.563 -25.073  1.00 77.06           C  
ANISOU  481  CB  THR A 246    13554   8511   7211   2643   1664  -1725       C  
ATOM    482  N   HIS A 247     -19.765  -2.713 -23.837  1.00 79.25           N  
ANISOU  482  N   HIS A 247    12868   8927   8316   1534   2690    676       N  
ATOM    483  CA  HIS A 247     -19.419  -3.798 -22.896  1.00 74.17           C  
ANISOU  483  CA  HIS A 247    12127   8511   7540    927   2973    446       C  
ATOM    484  C   HIS A 247     -18.901  -3.242 -21.566  1.00 68.61           C  
ANISOU  484  C   HIS A 247    11504   7162   7401   1087   2441   1200       C  
ATOM    485  O   HIS A 247     -18.211  -2.214 -21.543  1.00 71.36           O  
ANISOU  485  O   HIS A 247    12281   7375   7455    619   2353    475       O  
ATOM    486  CB  HIS A 247     -18.408  -4.783 -23.509  1.00 80.50           C  
ANISOU  486  CB  HIS A 247    13137   8561   8886   1801   3303    892       C  
ATOM    487  CG  HIS A 247     -17.009  -4.249 -23.593  1.00 91.60           C  
ANISOU  487  CG  HIS A 247    13369  10576  10858   1530   2913    972       C  
ATOM    488  ND1 HIS A 247     -16.114  -4.339 -22.546  1.00 94.82           N  
ANISOU  488  ND1 HIS A 247    14542  10901  10581   2187   2784   1720       N  
ATOM    489  CD2 HIS A 247     -16.353  -3.617 -24.595  1.00 96.25           C  
ANISOU  489  CD2 HIS A 247    14671  11223  10677   1649   3123   1456       C  
ATOM    490  CE1 HIS A 247     -14.969  -3.784 -22.900  1.00 96.47           C  
ANISOU  490  CE1 HIS A 247    14907  10802  10945   1657   3024   1377       C  
ATOM    491  NE2 HIS A 247     -15.086  -3.339 -24.139  1.00 93.80           N  
ANISOU  491  NE2 HIS A 247    14200  10322  11117    417   4433   2119       N  
ATOM    492  N   CYS A 248     -19.223  -3.932 -20.470  1.00 55.53           N  
ANISOU  492  N   CYS A 248     9331   5714   6054   2517   2066    198       N  
ATOM    493  CA  CYS A 248     -19.014  -3.392 -19.129  1.00 52.15           C  
ANISOU  493  CA  CYS A 248     8704   5224   5884    856   1989    856       C  
ATOM    494  C   CYS A 248     -19.193  -4.460 -18.039  1.00 43.39           C  
ANISOU  494  C   CYS A 248     7191   4124   5169   1060   1680     71       C  
ATOM    495  O   CYS A 248     -20.230  -5.113 -17.996  1.00 42.48           O  
ANISOU  495  O   CYS A 248     7729   3759   4652    799   1099    163       O  
ATOM    496  CB  CYS A 248     -20.039  -2.276 -18.913  1.00 56.67           C  
ANISOU  496  CB  CYS A 248    10389   4818   6323   1708   2016   2856       C  
ATOM    497  SG  CYS A 248     -19.405  -0.824 -18.084  1.00 89.89           S  
ANISOU  497  SG  CYS A 248    14774   9718   9662    704   1023   -414       S  
ATOM    498  N   HIS A 249     -18.205  -4.634 -17.156  1.00 42.00           N  
ANISOU  498  N   HIS A 249     6487   4103   5367    576   1825    207       N  
ATOM    499  CA  HIS A 249     -18.423  -5.401 -15.908  1.00 41.79           C  
ANISOU  499  CA  HIS A 249     6182   4075   5620    587   1883    361       C  
ATOM    500  C   HIS A 249     -19.434  -4.652 -15.036  1.00 36.91           C  
ANISOU  500  C   HIS A 249     6081   3098   4845    329   1451    336       C  
ATOM    501  O   HIS A 249     -19.498  -3.426 -15.091  1.00 38.81           O  
ANISOU  501  O   HIS A 249     6478   3089   5177    367   1528    225       O  
ATOM    502  CB  HIS A 249     -17.127  -5.575 -15.118  1.00 41.85           C  
ANISOU  502  CB  HIS A 249     5995   4176   5729    515   2143    401       C  
ATOM    503  CG  HIS A 249     -16.161  -6.552 -15.711  1.00 45.63           C  
ANISOU  503  CG  HIS A 249     6795   3596   6943    854   2302    503       C  
ATOM    504  ND1 HIS A 249     -14.994  -6.912 -15.070  1.00 45.64           N  
ANISOU  504  ND1 HIS A 249     6757   3451   7131    178   2140    985       N  
ATOM    505  CD2 HIS A 249     -16.182  -7.250 -16.874  1.00 48.17           C  
ANISOU  505  CD2 HIS A 249     7167   4630   6504    585   1412    563       C  
ATOM    506  CE1 HIS A 249     -14.332  -7.778 -15.820  1.00 51.29           C  
ANISOU  506  CE1 HIS A 249     7307   4755   7425    900   1889    382       C  
ATOM    507  NE2 HIS A 249     -15.033  -8.005 -16.917  1.00 48.70           N  
ANISOU  507  NE2 HIS A 249     7840   3873   6790    754   2155    226       N  
ATOM    508  N   ALA A 250     -20.203  -5.392 -14.234  1.00 34.82           N  
ANISOU  508  N   ALA A 250     5594   2815   4819    415   1327    201       N  
ATOM    509  CA  ALA A 250     -21.283  -4.828 -13.397  1.00 34.05           C  
ANISOU  509  CA  ALA A 250     5573   2574   4790    390   1306    268       C  
ATOM    510  C   ALA A 250     -20.879  -3.598 -12.574  1.00 35.52           C  
ANISOU  510  C   ALA A 250     5730   2748   5015    -39   1093    377       C  
ATOM    511  O   ALA A 250     -21.644  -2.630 -12.487  1.00 38.16           O  
ANISOU  511  O   ALA A 250     5655   3290   5552    192   1627    144       O  
ATOM    512  CB  ALA A 250     -21.874  -5.898 -12.487  1.00 30.34           C  
ANISOU  512  CB  ALA A 250     5292   1925   4308    330   1145   -317       C  
ATOM    513  N   GLU A 251     -19.680  -3.643 -11.990  1.00 39.81           N  
ANISOU  513  N   GLU A 251     5770   3561   5795   -344    855    969       N  
ATOM    514  CA  GLU A 251     -19.151  -2.550 -11.156  1.00 43.86           C  
ANISOU  514  CA  GLU A 251     7073   3362   6226    -97    953    607       C  
ATOM    515  C   GLU A 251     -18.953  -1.280 -11.984  1.00 42.35           C  
ANISOU  515  C   GLU A 251     6869   3485   5734   -223   1423    437       C  
ATOM    516  O   GLU A 251     -19.285  -0.193 -11.528  1.00 42.77           O  
ANISOU  516  O   GLU A 251     7173   3714   5361    156   1450    622       O  
ATOM    517  CB  GLU A 251     -17.845  -2.960 -10.442  1.00 48.12           C  
ANISOU  517  CB  GLU A 251     7164   4282   6836   -117    626    300       C  
ATOM    518  CG  GLU A 251     -17.950  -4.182  -9.515  1.00 52.53           C  
ANISOU  518  CG  GLU A 251     7637   4490   7830    236    847    915       C  
ATOM    519  CD  GLU A 251     -17.678  -5.528 -10.208  1.00 61.38           C  
ANISOU  519  CD  GLU A 251     9401   5518   8400    232   1174     49       C  
ATOM    520  OE1 GLU A 251     -17.664  -5.598 -11.464  1.00 50.53           O  
ANISOU  520  OE1 GLU A 251     9044   2250   7905    119   2085   2092       O  
ATOM    521  OE2 GLU A 251     -17.477  -6.540  -9.485  1.00 69.36           O  
ANISOU  521  OE2 GLU A 251     9122   6531  10700   1767     74    818       O  
ATOM    522  N   ARG A 252     -18.445  -1.439 -13.206  1.00 43.28           N  
ANISOU  522  N   ARG A 252     6678   3732   6032   -135   1824    520       N  
ATOM    523  CA  ARG A 252     -18.308  -0.332 -14.161  1.00 43.81           C  
ANISOU  523  CA  ARG A 252     7048   3785   5810    779   1799    561       C  
ATOM    524  C   ARG A 252     -19.653   0.158 -14.717  1.00 41.10           C  
ANISOU  524  C   ARG A 252     6950   3262   5401    369   1736    223       C  
ATOM    525  O   ARG A 252     -19.808   1.356 -14.956  1.00 43.02           O  
ANISOU  525  O   ARG A 252     7539   3433   5372    464   1917    736       O  
ATOM    526  CB  ARG A 252     -17.390  -0.715 -15.319  1.00 49.85           C  
ANISOU  526  CB  ARG A 252     7578   5332   6029    719   2404    751       C  
ATOM    527  CG  ARG A 252     -15.899  -0.636 -15.037  1.00 62.52           C  
ANISOU  527  CG  ARG A 252     8126   7433   8194    189   1898    862       C  
ATOM    528  CD  ARG A 252     -15.094  -1.254 -16.179  1.00 76.71           C  
ANISOU  528  CD  ARG A 252     8944  10401   9802    972   3970   1604       C  
ATOM    529  NE  ARG A 252     -15.270  -0.545 -17.453  1.00 81.56           N  
ANISOU  529  NE  ARG A 252    11131   9622  10235   -330   3719   1877       N  
ATOM    530  CZ  ARG A 252     -14.385  -0.523 -18.452  1.00 76.04           C  
ANISOU  530  CZ  ARG A 252    11019   7214  10657     95   3847   2716       C  
ATOM    531  NH1 ARG A 252     -13.219  -1.152 -18.356  1.00 71.50           N  
ANISOU  531  NH1 ARG A 252     9988   5961  11215   -968   5144   3385       N  
ATOM    532  NH2 ARG A 252     -14.667   0.146 -19.560  1.00 80.14           N  
ANISOU  532  NH2 ARG A 252    12036   8387  10027   1019   4410   2585       N  
ATOM    533  N   CYS A 253     -20.601  -0.762 -14.943  1.00 40.17           N  
ANISOU  533  N   CYS A 253     6392   3305   5563    407   2126    325       N  
ATOM    534  CA  CYS A 253     -21.961  -0.403 -15.388  1.00 39.34           C  
ANISOU  534  CA  CYS A 253     6712   3114   5120    452   1656    391       C  
ATOM    535  C   CYS A 253     -22.612   0.513 -14.363  1.00 37.21           C  
ANISOU  535  C   CYS A 253     6388   3074   4675    396   1157    372       C  
ATOM    536  O   CYS A 253     -23.213   1.525 -14.736  1.00 39.09           O  
ANISOU  536  O   CYS A 253     6429   2636   5786    421   1065    -68       O  
ATOM    537  CB  CYS A 253     -22.854  -1.629 -15.579  1.00 41.66           C  
ANISOU  537  CB  CYS A 253     6692   3656   5480     93   1324    453       C  
ATOM    538  SG  CYS A 253     -22.317  -2.820 -16.815  1.00 56.32           S  
ANISOU  538  SG  CYS A 253     9306   4592   7498    942    -46  -1344       S  
ATOM    539  N   PHE A 254     -22.484   0.153 -13.082  1.00 34.97           N  
ANISOU  539  N   PHE A 254     5875   3026   4384   -188   1304    243       N  
ATOM    540  CA  PHE A 254     -22.968   1.003 -11.996  1.00 35.01           C  
ANISOU  540  CA  PHE A 254     6101   2682   4517     44   1286    446       C  
ATOM    541  C   PHE A 254     -22.359   2.404 -12.038  1.00 37.18           C  
ANISOU  541  C   PHE A 254     6524   2630   4970     12   1160    708       C  
ATOM    542  O   PHE A 254     -23.103   3.387 -11.982  1.00 39.05           O  
ANISOU  542  O   PHE A 254     6972   2917   4949    365    708    492       O  
ATOM    543  CB  PHE A 254     -22.739   0.383 -10.603  1.00 34.41           C  
ANISOU  543  CB  PHE A 254     6028   2581   4465    -37   1341    484       C  
ATOM    544  CG  PHE A 254     -23.195   1.274  -9.480  1.00 34.45           C  
ANISOU  544  CG  PHE A 254     5959   2629   4500     72   1067    373       C  
ATOM    545  CD1 PHE A 254     -22.353   2.271  -8.967  1.00 35.63           C  
ANISOU  545  CD1 PHE A 254     6148   2535   4852   -108   1029    518       C  
ATOM    546  CD2 PHE A 254     -24.488   1.159  -8.964  1.00 36.40           C  
ANISOU  546  CD2 PHE A 254     6177   2942   4711    -38   1386    613       C  
ATOM    547  CE1 PHE A 254     -22.788   3.121  -7.949  1.00 37.39           C  
ANISOU  547  CE1 PHE A 254     6167   3472   4564    -18   1286    480       C  
ATOM    548  CE2 PHE A 254     -24.924   2.004  -7.944  1.00 37.54           C  
ANISOU  548  CE2 PHE A 254     6516   2727   5019    -71   1077    276       C  
ATOM    549  CZ  PHE A 254     -24.073   2.981  -7.437  1.00 35.36           C  
ANISOU  549  CZ  PHE A 254     5935   2814   4686    202   1196    184       C  
ATOM    550  N   LEU A 255     -21.025   2.483 -12.112  1.00 38.09           N  
ANISOU  550  N   LEU A 255     6522   2814   5133    101   1557    739       N  
ATOM    551  CA  LEU A 255     -20.301   3.768 -12.080  1.00 43.05           C  
ANISOU  551  CA  LEU A 255     7266   3060   6029   -235   1506    738       C  
ATOM    552  C   LEU A 255     -20.696   4.661 -13.236  1.00 45.10           C  
ANISOU  552  C   LEU A 255     7923   3546   5665   -154   1911    943       C  
ATOM    553  O   LEU A 255     -20.895   5.863 -13.058  1.00 50.29           O  
ANISOU  553  O   LEU A 255     8658   3721   6729   -146   1643    379       O  
ATOM    554  CB  LEU A 255     -18.778   3.572 -12.091  1.00 47.29           C  
ANISOU  554  CB  LEU A 255     7251   4197   6519   -249   1715    647       C  
ATOM    555  CG  LEU A 255     -18.051   2.894 -10.922  1.00 50.13           C  
ANISOU  555  CG  LEU A 255     7564   4791   6693   -344   1268    564       C  
ATOM    556  CD1 LEU A 255     -16.548   3.025 -11.130  1.00 51.17           C  
ANISOU  556  CD1 LEU A 255     7357   4477   7606    373   1284    779       C  
ATOM    557  CD2 LEU A 255     -18.464   3.461  -9.567  1.00 45.68           C  
ANISOU  557  CD2 LEU A 255     7445   3471   6437   -948   1766   1283       C  
ATOM    558  N   SER A 256     -20.816   4.044 -14.409  1.00 44.69           N  
ANISOU  558  N   SER A 256     7848   3373   5759    179   1958    855       N  
ATOM    559  CA  SER A 256     -21.194   4.711 -15.650  1.00 47.69           C  
ANISOU  559  CA  SER A 256     8338   3822   5958    463   1477    929       C  
ATOM    560  C   SER A 256     -22.624   5.262 -15.577  1.00 45.76           C  
ANISOU  560  C   SER A 256     8314   3454   5616    317   1759   1135       C  
ATOM    561  O   SER A 256     -22.879   6.373 -16.029  1.00 48.09           O  
ANISOU  561  O   SER A 256     8881   3521   5869    274   1384   1255       O  
ATOM    562  CB  SER A 256     -21.029   3.741 -16.821  1.00 50.74           C  
ANISOU  562  CB  SER A 256     9164   4093   6019    602   2120    836       C  
ATOM    563  OG  SER A 256     -21.349   4.356 -18.045  1.00 64.15           O  
ANISOU  563  OG  SER A 256    11573   5985   6813     63   1534   1730       O  
ATOM    564  N   TRP A 257     -23.540   4.489 -14.991  1.00 43.50           N  
ANISOU  564  N   TRP A 257     7699   3145   5681    476   1747    765       N  
ATOM    565  CA  TRP A 257     -24.916   4.936 -14.763  1.00 41.75           C  
ANISOU  565  CA  TRP A 257     7534   3076   5251    505   1293    693       C  
ATOM    566  C   TRP A 257     -25.009   6.025 -13.684  1.00 41.04           C  
ANISOU  566  C   TRP A 257     7537   2675   5380    285   1210    821       C  
ATOM    567  O   TRP A 257     -25.794   6.965 -13.816  1.00 41.90           O  
ANISOU  567  O   TRP A 257     7655   3022   5242    544   1169    432       O  
ATOM    568  CB  TRP A 257     -25.824   3.748 -14.415  1.00 39.77           C  
ANISOU  568  CB  TRP A 257     7363   2507   5240    771   1287    353       C  
ATOM    569  CG  TRP A 257     -27.134   4.150 -13.807  1.00 39.58           C  
ANISOU  569  CG  TRP A 257     6895   2954   5189    277   1127    554       C  
ATOM    570  CD1 TRP A 257     -28.250   4.567 -14.472  1.00 39.45           C  
ANISOU  570  CD1 TRP A 257     7235   2680   5073    523   1034    586       C  
ATOM    571  CD2 TRP A 257     -27.456   4.203 -12.406  1.00 39.68           C  
ANISOU  571  CD2 TRP A 257     7015   2968   5092    405    949    390       C  
ATOM    572  NE1 TRP A 257     -29.253   4.863 -13.577  1.00 38.89           N  
ANISOU  572  NE1 TRP A 257     7184   2557   5035    899    835    317       N  
ATOM    573  CE2 TRP A 257     -28.795   4.652 -12.303  1.00 38.70           C  
ANISOU  573  CE2 TRP A 257     7206   2635   4862    693    993    342       C  
ATOM    574  CE3 TRP A 257     -26.744   3.913 -11.229  1.00 37.72           C  
ANISOU  574  CE3 TRP A 257     6939   2436   4954    344   1128    627       C  
ATOM    575  CZ2 TRP A 257     -29.447   4.809 -11.069  1.00 38.72           C  
ANISOU  575  CZ2 TRP A 257     7136   2584   4990    600   1014    140       C  
ATOM    576  CZ3 TRP A 257     -27.388   4.077  -9.995  1.00 38.80           C  
ANISOU  576  CZ3 TRP A 257     6845   2793   5105    592   1094    208       C  
ATOM    577  CH2 TRP A 257     -28.730   4.522  -9.929  1.00 38.80           C  
ANISOU  577  CH2 TRP A 257     7019   2466   5257    778    863    108       C  
ATOM    578  N   PHE A 258     -24.224   5.876 -12.619  1.00 39.70           N  
ANISOU  578  N   PHE A 258     7489   2364   5228    128   1295    684       N  
ATOM    579  CA  PHE A 258     -24.193   6.839 -11.522  1.00 39.09           C  
ANISOU  579  CA  PHE A 258     7267   2161   5425    326   1648    575       C  
ATOM    580  C   PHE A 258     -23.698   8.209 -11.991  1.00 41.34           C  
ANISOU  580  C   PHE A 258     7450   2502   5755     19   1673    811       C  
ATOM    581  O   PHE A 258     -24.298   9.227 -11.656  1.00 45.82           O  
ANISOU  581  O   PHE A 258     7555   2712   7139     29   1310     31       O  
ATOM    582  CB  PHE A 258     -23.341   6.315 -10.357  1.00 38.09           C  
ANISOU  582  CB  PHE A 258     7558   1449   5463    150   1796   1084       C  
ATOM    583  CG  PHE A 258     -23.297   7.238  -9.168  1.00 46.56           C  
ANISOU  583  CG  PHE A 258     8481   3133   6074   -168   1656    249       C  
ATOM    584  CD1 PHE A 258     -24.301   7.203  -8.201  1.00 49.31           C  
ANISOU  584  CD1 PHE A 258     8618   3621   6495   -388   1904    443       C  
ATOM    585  CD2 PHE A 258     -22.252   8.148  -9.011  1.00 51.75           C  
ANISOU  585  CD2 PHE A 258     8235   3992   7434   -364   1488    247       C  
ATOM    586  CE1 PHE A 258     -24.262   8.054  -7.101  1.00 50.07           C  
ANISOU  586  CE1 PHE A 258     9091   3026   6906   -536   2220    327       C  
ATOM    587  CE2 PHE A 258     -22.212   9.004  -7.915  1.00 59.34           C  
ANISOU  587  CE2 PHE A 258     8965   6087   7495   -150   1539   -507       C  
ATOM    588  CZ  PHE A 258     -23.216   8.951  -6.956  1.00 57.19           C  
ANISOU  588  CZ  PHE A 258     8606   5043   8078   -899   1630    -13       C  
ATOM    589  N   CYS A 259     -22.612   8.226 -12.763  1.00 41.63           N  
ANISOU  589  N   CYS A 259     7895   2623   5300     23   1802    781       N  
ATOM    590  CA  CYS A 259     -22.027   9.478 -13.244  1.00 45.18           C  
ANISOU  590  CA  CYS A 259     8648   2672   5846     22   1877   1106       C  
ATOM    591  C   CYS A 259     -22.883  10.149 -14.317  1.00 46.04           C  
ANISOU  591  C   CYS A 259     8526   2848   6118    427   1824    907       C  
ATOM    592  O   CYS A 259     -23.019  11.378 -14.321  1.00 45.28           O  
ANISOU  592  O   CYS A 259     8793   2706   5704   -407   1999   1250       O  
ATOM    593  CB  CYS A 259     -20.604   9.254 -13.763  1.00 52.76           C  
ANISOU  593  CB  CYS A 259     8565   4145   7334    139   1731    517       C  
ATOM    594  SG  CYS A 259     -19.434   8.706 -12.498  1.00 56.71           S  
ANISOU  594  SG  CYS A 259     9047   4356   8143    -14   1204    560       S  
ATOM    595  N   ASP A 260     -23.458   9.343 -15.211  1.00 43.55           N  
ANISOU  595  N   ASP A 260     8537   1966   6042    429   1868   1181       N  
ATOM    596  CA  ASP A 260     -24.226   9.854 -16.349  1.00 48.65           C  
ANISOU  596  CA  ASP A 260     9166   3125   6191    638   1557   1301       C  
ATOM    597  C   ASP A 260     -25.656  10.268 -16.003  1.00 50.22           C  
ANISOU  597  C   ASP A 260     9244   3700   6137    519   1670   1229       C  
ATOM    598  O   ASP A 260     -26.208  11.166 -16.646  1.00 50.34           O  
ANISOU  598  O   ASP A 260     9922   2485   6717     43   1371    982       O  
ATOM    599  CB  ASP A 260     -24.240   8.847 -17.510  1.00 48.83           C  
ANISOU  599  CB  ASP A 260     9795   2861   5896    453   1599   1689       C  
ATOM    600  CG  ASP A 260     -22.898   8.750 -18.236  1.00 57.12           C  
ANISOU  600  CG  ASP A 260    10258   4617   6825    834   2046   1547       C  
ATOM    601  OD1 ASP A 260     -21.941   9.478 -17.884  1.00 61.77           O  
ANISOU  601  OD1 ASP A 260    11184   5331   6954    598   1166   1170       O  
ATOM    602  OD2 ASP A 260     -22.803   7.934 -19.176  1.00 67.89           O  
ANISOU  602  OD2 ASP A 260    11656   5890   8246   -539    829    -27       O  
ATOM    603  N   ASP A 261     -26.258   9.615 -15.009  1.00 51.90           N  
ANISOU  603  N   ASP A 261     9918   3762   6037    468   1752   1312       N  
ATOM    604  CA  ASP A 261     -27.670   9.858 -14.684  1.00 57.02           C  
ANISOU  604  CA  ASP A 261    10081   4453   7131    739   1697   1584       C  
ATOM    605  C   ASP A 261     -27.959  10.430 -13.285  1.00 57.69           C  
ANISOU  605  C   ASP A 261    10403   3543   7971   1075   1569    746       C  
ATOM    606  O   ASP A 261     -28.986  11.084 -13.094  1.00 67.96           O  
ANISOU  606  O   ASP A 261    10134   6080   9607   1528   1874    317       O  
ATOM    607  CB  ASP A 261     -28.503   8.584 -14.905  1.00 61.19           C  
ANISOU  607  CB  ASP A 261    10573   4735   7938    459   1407   1044       C  
ATOM    608  CG  ASP A 261     -28.629   8.188 -16.378  1.00 66.65           C  
ANISOU  608  CG  ASP A 261    11620   5944   7760    917   1015   1597       C  
ATOM    609  OD1 ASP A 261     -28.059   8.851 -17.271  1.00 70.07           O  
ANISOU  609  OD1 ASP A 261    11354   4614  10654  -1193   1421   1198       O  
ATOM    610  OD2 ASP A 261     -29.319   7.184 -16.647  1.00 73.37           O  
ANISOU  610  OD2 ASP A 261    11408   6736   9732    666    999   1372       O  
ATOM    611  N   ILE A 262     -27.068  10.194 -12.321  1.00 55.49           N  
ANISOU  611  N   ILE A 262    10199   3016   7867    386   1517    572       N  
ATOM    612  CA  ILE A 262     -27.373  10.471 -10.909  1.00 55.80           C  
ANISOU  612  CA  ILE A 262     9886   3390   7925    390   1821    838       C  
ATOM    613  C   ILE A 262     -26.578  11.618 -10.282  1.00 56.66           C  
ANISOU  613  C   ILE A 262    10158   2819   8550    737   1949    640       C  
ATOM    614  O   ILE A 262     -27.182  12.562  -9.772  1.00 61.18           O  
ANISOU  614  O   ILE A 262     9933   3015  10296   1014   2155    537       O  
ATOM    615  CB  ILE A 262     -27.272   9.183 -10.033  1.00 55.26           C  
ANISOU  615  CB  ILE A 262     9890   3382   7721    243   1564    738       C  
ATOM    616  CG1 ILE A 262     -28.195   8.064 -10.555  1.00 55.76           C  
ANISOU  616  CG1 ILE A 262     9874   3205   8107    556   1520    401       C  
ATOM    617  CG2 ILE A 262     -27.533   9.477  -8.555  1.00 52.81           C  
ANISOU  617  CG2 ILE A 262     9807   2595   7661    410   1421    716       C  
ATOM    618  CD1 ILE A 262     -29.670   8.415 -10.716  1.00 56.18           C  
ANISOU  618  CD1 ILE A 262     9604   3020   8721   -167   1554    872       C  
ATOM    619  N   LEU A 263     -25.244  11.527 -10.325  1.00 57.88           N  
ANISOU  619  N   LEU A 263    10271   2682   9036    873   2324    665       N  
ATOM    620  CA  LEU A 263     -24.342  12.409  -9.564  1.00 62.71           C  
ANISOU  620  CA  LEU A 263    10691   3337   9799     11   2533    536       C  
ATOM    621  C   LEU A 263     -24.634  13.888  -9.783  1.00 63.09           C  
ANISOU  621  C   LEU A 263    10970   3532   9468    180   2913   1096       C  
ATOM    622  O   LEU A 263     -24.460  14.397 -10.884  1.00 63.89           O  
ANISOU  622  O   LEU A 263    11837   2379  10058     93   3185   1461       O  
ATOM    623  CB  LEU A 263     -22.869  12.098  -9.882  1.00 65.52           C  
ANISOU  623  CB  LEU A 263    10812   3831  10251     29   2866    516       C  
ATOM    624  CG  LEU A 263     -21.803  13.045  -9.304  1.00 71.09           C  
ANISOU  624  CG  LEU A 263    11211   5362  10436   -114   2152    321       C  
ATOM    625  CD1 LEU A 263     -21.348  12.619  -7.915  1.00 70.26           C  
ANISOU  625  CD1 LEU A 263    11285   5487   9920   -391   3663   1426       C  
ATOM    626  CD2 LEU A 263     -20.618  13.165 -10.252  1.00 78.31           C  
ANISOU  626  CD2 LEU A 263    11941   7026  10787    643   2809    -64       C  
ATOM    627  N   SER A 264     -25.068  14.556  -8.714  1.00 68.77           N  
ANISOU  627  N   SER A 264    11939   4155  10035    170   3069    436       N  
ATOM    628  CA  SER A 264     -25.480  15.965  -8.745  1.00 67.80           C  
ANISOU  628  CA  SER A 264    12141   3877   9742   -227   2943   1157       C  
ATOM    629  C   SER A 264     -24.586  16.852  -7.864  1.00 73.52           C  
ANISOU  629  C   SER A 264    13487   4417  10028   -102   2467    536       C  
ATOM    630  O   SER A 264     -23.910  16.334  -6.969  1.00 70.05           O  
ANISOU  630  O   SER A 264    15450   2451   8713   -362   2215    202       O  
ATOM    631  CB  SER A 264     -26.941  16.088  -8.305  1.00 67.88           C  
ANISOU  631  CB  SER A 264    11889   4199   9701     61   2467    714       C  
ATOM    632  OG  SER A 264     -27.798  15.448  -9.229  1.00 65.77           O  
ANISOU  632  OG  SER A 264    12147   5270   7573    569   2042   1685       O  
ATOM    633  N   PRO A 265     -24.562  18.186  -8.125  1.00 79.92           N  
ANISOU  633  N   PRO A 265    14278   4272  11814   -118   3046    154       N  
ATOM    634  CA  PRO A 265     -23.835  19.096  -7.228  1.00 83.73           C  
ANISOU  634  CA  PRO A 265    14186   5112  12514   -617   3038   -176       C  
ATOM    635  C   PRO A 265     -24.486  19.235  -5.851  1.00 84.34           C  
ANISOU  635  C   PRO A 265    14130   5604  12310  -1058   2821   -636       C  
ATOM    636  O   PRO A 265     -25.713  19.114  -5.729  1.00 78.82           O  
ANISOU  636  O   PRO A 265    14243   3368  12334   -374   3402  -1553       O  
ATOM    637  CB  PRO A 265     -23.879  20.440  -7.970  1.00 89.06           C  
ANISOU  637  CB  PRO A 265    14410   5694  13731   -251   2798    613       C  
ATOM    638  CG  PRO A 265     -25.025  20.327  -8.918  1.00 86.44           C  
ANISOU  638  CG  PRO A 265    13876   4955  14010    534   2923    -51       C  
ATOM    639  CD  PRO A 265     -25.032  18.890  -9.337  1.00 82.42           C  
ANISOU  639  CD  PRO A 265    14213   4640  12463    191   2804    544       C  
ATOM    640  N   ASN A 266     -23.648  19.473  -4.837  1.00 82.25           N  
ANISOU  640  N   ASN A 266    13032   5710  12507  -2166   3274  -1277       N  
ATOM    641  CA  ASN A 266     -24.061  19.735  -3.442  1.00 81.01           C  
ANISOU  641  CA  ASN A 266    13559   4741  12480  -1083   3172   -778       C  
ATOM    642  C   ASN A 266     -24.876  18.613  -2.777  1.00 79.34           C  
ANISOU  642  C   ASN A 266    14384   3760  12000   -951   2901  -1002       C  
ATOM    643  O   ASN A 266     -25.697  18.868  -1.883  1.00 76.08           O  
ANISOU  643  O   ASN A 266    15077   2543  11285  -2305   3170   -880       O  
ATOM    644  CB  ASN A 266     -24.784  21.097  -3.320  1.00 88.72           C  
ANISOU  644  CB  ASN A 266    14708   4566  14432   -794   3143   -644       C  
ATOM    645  CG  ASN A 266     -24.003  22.241  -3.947  1.00 89.54           C  
ANISOU  645  CG  ASN A 266    14753   5199  14068   -831   2938   -212       C  
ATOM    646  OD1 ASN A 266     -22.924  22.610  -3.476  1.00 92.25           O  
ANISOU  646  OD1 ASN A 266    15442   4950  14656  -1230   2702  -2065       O  
ATOM    647  ND2 ASN A 266     -24.554  22.816  -5.011  1.00 91.91           N  
ANISOU  647  ND2 ASN A 266    16055   4835  14029   -369   3364    448       N  
ATOM    648  N   THR A 267     -24.631  17.376  -3.211  1.00 71.22           N  
ANISOU  648  N   THR A 267    12569   3814  10675   -541   3381   -484       N  
ATOM    649  CA  THR A 267     -25.368  16.202  -2.735  1.00 64.62           C  
ANISOU  649  CA  THR A 267    11895   3167   9489   -187   2805   -791       C  
ATOM    650  C   THR A 267     -24.403  15.133  -2.213  1.00 64.06           C  
ANISOU  650  C   THR A 267    11292   3461   9588   -594   2392   -822       C  
ATOM    651  O   THR A 267     -23.378  14.848  -2.840  1.00 65.40           O  
ANISOU  651  O   THR A 267    11069   3694  10086  -1746   3032   -188       O  
ATOM    652  CB  THR A 267     -26.278  15.606  -3.845  1.00 62.34           C  
ANISOU  652  CB  THR A 267    11422   2710   9551   -267   2816   -226       C  
ATOM    653  OG1 THR A 267     -27.069  16.641  -4.442  1.00 66.53           O  
ANISOU  653  OG1 THR A 267    12377   3763   9138    564   3707    552       O  
ATOM    654  CG2 THR A 267     -27.222  14.556  -3.283  1.00 56.95           C  
ANISOU  654  CG2 THR A 267    10600   2518   8520     40   2714   -693       C  
ATOM    655  N   ASN A 268     -24.744  14.564  -1.057  1.00 64.62           N  
ANISOU  655  N   ASN A 268    11287   3928   9337   -500   2247   -897       N  
ATOM    656  CA  ASN A 268     -24.044  13.407  -0.498  1.00 61.90           C  
ANISOU  656  CA  ASN A 268    10724   3188   9607   -846   1843  -1552       C  
ATOM    657  C   ASN A 268     -24.755  12.096  -0.807  1.00 54.48           C  
ANISOU  657  C   ASN A 268     9643   2719   8338   -267   2124  -1304       C  
ATOM    658  O   ASN A 268     -25.987  12.045  -0.897  1.00 53.18           O  
ANISOU  658  O   ASN A 268     9681   2072   8450   -228   2287  -1408       O  
ATOM    659  CB  ASN A 268     -23.832  13.565   1.013  1.00 71.58           C  
ANISOU  659  CB  ASN A 268    12358   5049   9789   -868   1569  -1529       C  
ATOM    660  CG  ASN A 268     -22.629  14.437   1.351  1.00 78.41           C  
ANISOU  660  CG  ASN A 268    13395   5399  10997  -2072   1374   -501       C  
ATOM    661  OD1 ASN A 268     -22.340  15.418   0.667  1.00 80.28           O  
ANISOU  661  OD1 ASN A 268    13710   4359  12432  -3507    -56   -728       O  
ATOM    662  ND2 ASN A 268     -21.926  14.080   2.420  1.00 85.30           N  
ANISOU  662  ND2 ASN A 268    13966   6816  11627  -1311    583  -1080       N  
ATOM    663  N   TYR A 269     -23.959  11.043  -0.963  1.00 49.87           N  
ANISOU  663  N   TYR A 269     8893   2172   7880   -760   1678  -1148       N  
ATOM    664  CA  TYR A 269     -24.449   9.745  -1.387  1.00 44.55           C  
ANISOU  664  CA  TYR A 269     8286   1918   6720   -551   1830   -771       C  
ATOM    665  C   TYR A 269     -23.914   8.659  -0.471  1.00 46.38           C  
ANISOU  665  C   TYR A 269     8698   2313   6610   -716   1500   -678       C  
ATOM    666  O   TYR A 269     -22.698   8.516  -0.312  1.00 48.53           O  
ANISOU  666  O   TYR A 269     8872   1603   7964  -1147    753   -648       O  
ATOM    667  CB  TYR A 269     -24.048   9.468  -2.845  1.00 43.62           C  
ANISOU  667  CB  TYR A 269     8050   1797   6726   -118   2060   -715       C  
ATOM    668  CG  TYR A 269     -24.635  10.438  -3.847  1.00 43.49           C  
ANISOU  668  CG  TYR A 269     8364   1677   6481     39   2399   -785       C  
ATOM    669  CD1 TYR A 269     -25.900  10.218  -4.407  1.00 44.61           C  
ANISOU  669  CD1 TYR A 269     8591   2112   6246     92   2109   -730       C  
ATOM    670  CD2 TYR A 269     -23.930  11.587  -4.239  1.00 45.69           C  
ANISOU  670  CD2 TYR A 269     8435   2153   6770   -173   2464   -496       C  
ATOM    671  CE1 TYR A 269     -26.449  11.114  -5.325  1.00 48.62           C  
ANISOU  671  CE1 TYR A 269     9409   2050   7012     23   2115    -92       C  
ATOM    672  CE2 TYR A 269     -24.468  12.488  -5.155  1.00 49.21           C  
ANISOU  672  CE2 TYR A 269     9204   2349   7145     56   2552    -36       C  
ATOM    673  CZ  TYR A 269     -25.732  12.245  -5.699  1.00 50.09           C  
ANISOU  673  CZ  TYR A 269     9511   2255   7263     -5   2082    266       C  
ATOM    674  OH  TYR A 269     -26.274  13.133  -6.612  1.00 51.98           O  
ANISOU  674  OH  TYR A 269    10687   1273   7788    229   2421    478       O  
ATOM    675  N   GLU A 270     -24.837   7.919   0.141  1.00 45.66           N  
ANISOU  675  N   GLU A 270     8894   2577   5876   -935   1688  -1215       N  
ATOM    676  CA  GLU A 270     -24.515   6.732   0.926  1.00 49.10           C  
ANISOU  676  CA  GLU A 270     8988   2783   6881   -835    993   -936       C  
ATOM    677  C   GLU A 270     -24.898   5.521   0.097  1.00 43.67           C  
ANISOU  677  C   GLU A 270     8191   2711   5689   -356   1143   -672       C  
ATOM    678  O   GLU A 270     -26.085   5.227  -0.072  1.00 41.56           O  
ANISOU  678  O   GLU A 270     8507   2235   5047   -596    345   -263       O  
ATOM    679  CB  GLU A 270     -25.270   6.731   2.262  1.00 58.13           C  
ANISOU  679  CB  GLU A 270     9969   4557   7559   -380   1775  -1202       C  
ATOM    680  CG  GLU A 270     -24.641   7.597   3.345  1.00 76.53           C  
ANISOU  680  CG  GLU A 270    12521   7793   8761  -1073    522  -2179       C  
ATOM    681  CD  GLU A 270     -23.396   6.979   3.968  1.00 89.63           C  
ANISOU  681  CD  GLU A 270    13742   8847  11464   -333    148   -911       C  
ATOM    682  OE1 GLU A 270     -22.470   7.749   4.307  1.00105.39           O  
ANISOU  682  OE1 GLU A 270    15967  10303  13770  -1911   -173  -2022       O  
ATOM    683  OE2 GLU A 270     -23.338   5.735   4.122  1.00 91.32           O  
ANISOU  683  OE2 GLU A 270    14711   8684  11302   -592    750   -725       O  
ATOM    684  N   VAL A 271     -23.885   4.836  -0.426  1.00 43.87           N  
ANISOU  684  N   VAL A 271     7735   3111   5819   -484   1054   -729       N  
ATOM    685  CA  VAL A 271     -24.077   3.725  -1.361  1.00 40.27           C  
ANISOU  685  CA  VAL A 271     7171   2666   5462   -492   1222   -370       C  
ATOM    686  C   VAL A 271     -23.652   2.394  -0.730  1.00 40.30           C  
ANISOU  686  C   VAL A 271     7239   2791   5281   -675    936   -282       C  
ATOM    687  O   VAL A 271     -22.563   2.277  -0.157  1.00 40.90           O  
ANISOU  687  O   VAL A 271     7390   3489   4659  -1124    809   -349       O  
ATOM    688  CB  VAL A 271     -23.334   3.975  -2.702  1.00 37.59           C  
ANISOU  688  CB  VAL A 271     7376   1737   5169   -497   1014   -212       C  
ATOM    689  CG1 VAL A 271     -23.613   2.867  -3.706  1.00 36.59           C  
ANISOU  689  CG1 VAL A 271     7196   1619   5085   -255    585    -54       C  
ATOM    690  CG2 VAL A 271     -23.747   5.310  -3.309  1.00 37.92           C  
ANISOU  690  CG2 VAL A 271     7048   1558   5802   -308   1314   -343       C  
ATOM    691  N   THR A 272     -24.535   1.405  -0.837  1.00 38.81           N  
ANISOU  691  N   THR A 272     6912   2585   5247   -470    995    -82       N  
ATOM    692  CA  THR A 272     -24.245   0.039  -0.420  1.00 34.96           C  
ANISOU  692  CA  THR A 272     6230   2550   4504   -267    797   -402       C  
ATOM    693  C   THR A 272     -24.383  -0.890  -1.626  1.00 33.33           C  
ANISOU  693  C   THR A 272     5952   2444   4266   -137    783   -245       C  
ATOM    694  O   THR A 272     -25.402  -0.860  -2.319  1.00 32.56           O  
ANISOU  694  O   THR A 272     6445   2385   3540    -87    745    257       O  
ATOM    695  CB  THR A 272     -25.169  -0.416   0.732  1.00 34.80           C  
ANISOU  695  CB  THR A 272     6631   2378   4210    -96    783   -316       C  
ATOM    696  OG1 THR A 272     -25.138   0.561   1.779  1.00 39.45           O  
ANISOU  696  OG1 THR A 272     7458   2468   5062   -471     56   -744       O  
ATOM    697  CG2 THR A 272     -24.723  -1.759   1.305  1.00 32.03           C  
ANISOU  697  CG2 THR A 272     6166   1945   4056   -592    807   -455       C  
ATOM    698  N   TRP A 273     -23.347  -1.695  -1.866  1.00 31.02           N  
ANISOU  698  N   TRP A 273     5674   2015   4094   -339    623   -106       N  
ATOM    699  CA  TRP A 273     -23.353  -2.731  -2.900  1.00 29.57           C  
ANISOU  699  CA  TRP A 273     5508   2081   3644   -100    671     87       C  
ATOM    700  C   TRP A 273     -23.442  -4.111  -2.278  1.00 29.11           C  
ANISOU  700  C   TRP A 273     5308   2119   3631    -48    475    129       C  
ATOM    701  O   TRP A 273     -22.815  -4.370  -1.250  1.00 30.20           O  
ANISOU  701  O   TRP A 273     5424   2150   3897    543    572    677       O  
ATOM    702  CB  TRP A 273     -22.052  -2.704  -3.683  1.00 29.44           C  
ANISOU  702  CB  TRP A 273     5422   1982   3779   -248    644     65       C  
ATOM    703  CG  TRP A 273     -21.895  -1.615  -4.679  1.00 31.31           C  
ANISOU  703  CG  TRP A 273     5711   2046   4138   -280    774    212       C  
ATOM    704  CD1 TRP A 273     -22.738  -0.556  -4.916  1.00 31.33           C  
ANISOU  704  CD1 TRP A 273     6049   1975   3878   -217    577    171       C  
ATOM    705  CD2 TRP A 273     -20.781  -1.447  -5.553  1.00 33.75           C  
ANISOU  705  CD2 TRP A 273     5923   2627   4272   -206    964    311       C  
ATOM    706  NE1 TRP A 273     -22.216   0.247  -5.903  1.00 33.79           N  
ANISOU  706  NE1 TRP A 273     6077   2234   4528   -399   1203    143       N  
ATOM    707  CE2 TRP A 273     -21.015  -0.273  -6.311  1.00 35.00           C  
ANISOU  707  CE2 TRP A 273     6100   2278   4918   -166   1083    293       C  
ATOM    708  CE3 TRP A 273     -19.600  -2.182  -5.778  1.00 34.09           C  
ANISOU  708  CE3 TRP A 273     5852   2479   4619   -201    870    395       C  
ATOM    709  CZ2 TRP A 273     -20.113   0.185  -7.285  1.00 36.29           C  
ANISOU  709  CZ2 TRP A 273     6283   2482   5022   -289   1226    210       C  
ATOM    710  CZ3 TRP A 273     -18.703  -1.725  -6.743  1.00 35.97           C  
ANISOU  710  CZ3 TRP A 273     5650   3094   4921    107   1154    393       C  
ATOM    711  CH2 TRP A 273     -18.966  -0.549  -7.486  1.00 37.17           C  
ANISOU  711  CH2 TRP A 273     6194   2664   5261   -293   1270    379       C  
ATOM    712  N   TYR A 274     -24.208  -4.988  -2.917  1.00 28.21           N  
ANISOU  712  N   TYR A 274     5243   1981   3493    221    608   -115       N  
ATOM    713  CA  TYR A 274     -24.226  -6.405  -2.595  1.00 28.70           C  
ANISOU  713  CA  TYR A 274     5089   2154   3660    -91    483    242       C  
ATOM    714  C   TYR A 274     -23.888  -7.115  -3.893  1.00 31.15           C  
ANISOU  714  C   TYR A 274     5384   2745   3706    -43    305     34       C  
ATOM    715  O   TYR A 274     -24.706  -7.170  -4.817  1.00 34.49           O  
ANISOU  715  O   TYR A 274     5704   3569   3830   -355    104   -190       O  
ATOM    716  CB  TYR A 274     -25.591  -6.839  -2.081  1.00 26.87           C  
ANISOU  716  CB  TYR A 274     4903   2307   2998     52    303    237       C  
ATOM    717  CG  TYR A 274     -26.052  -6.086  -0.865  1.00 29.68           C  
ANISOU  717  CG  TYR A 274     5547   2517   3213    117    402     34       C  
ATOM    718  CD1 TYR A 274     -26.794  -4.905  -0.989  1.00 31.22           C  
ANISOU  718  CD1 TYR A 274     5562   2593   3705    184    634    269       C  
ATOM    719  CD2 TYR A 274     -25.759  -6.555   0.421  1.00 29.36           C  
ANISOU  719  CD2 TYR A 274     5522   2491   3142    -89    516     89       C  
ATOM    720  CE1 TYR A 274     -27.219  -4.207   0.139  1.00 34.13           C  
ANISOU  720  CE1 TYR A 274     6078   3143   3747   -146    276   -309       C  
ATOM    721  CE2 TYR A 274     -26.180  -5.864   1.549  1.00 30.55           C  
ANISOU  721  CE2 TYR A 274     5641   2765   3198   -165    676      0       C  
ATOM    722  CZ  TYR A 274     -26.909  -4.695   1.403  1.00 33.34           C  
ANISOU  722  CZ  TYR A 274     5891   2901   3875    -13    576    -15       C  
ATOM    723  OH  TYR A 274     -27.325  -4.011   2.524  1.00 38.87           O  
ANISOU  723  OH  TYR A 274     6589   4000   4180     -6    407   -721       O  
ATOM    724  N   THR A 275     -22.662  -7.615  -3.971  1.00 31.96           N  
ANISOU  724  N   THR A 275     5431   2678   4035    119    308    343       N  
ATOM    725  CA  THR A 275     -22.161  -8.219  -5.191  1.00 31.82           C  
ANISOU  725  CA  THR A 275     5204   2766   4118    131    282    369       C  
ATOM    726  C   THR A 275     -22.031  -9.720  -4.967  1.00 30.22           C  
ANISOU  726  C   THR A 275     5079   2805   3596     15     -1    533       C  
ATOM    727  O   THR A 275     -21.732 -10.154  -3.858  1.00 28.76           O  
ANISOU  727  O   THR A 275     5017   2747   3163   -299    498    466       O  
ATOM    728  CB  THR A 275     -20.799  -7.627  -5.595  1.00 32.00           C  
ANISOU  728  CB  THR A 275     5295   2559   4305     86    252    757       C  
ATOM    729  OG1 THR A 275     -19.845  -7.923  -4.574  1.00 36.37           O  
ANISOU  729  OG1 THR A 275     5529   3761   4529    -83   -165    263       O  
ATOM    730  CG2 THR A 275     -20.880  -6.114  -5.752  1.00 31.78           C  
ANISOU  730  CG2 THR A 275     5802   2494   3778   -139     57    569       C  
ATOM    731  N   SER A 276     -22.260 -10.506  -6.016  1.00 29.16           N  
ANISOU  731  N   SER A 276     4707   2626   3743    255     25    448       N  
ATOM    732  CA  SER A 276     -22.171 -11.961  -5.906  1.00 29.07           C  
ANISOU  732  CA  SER A 276     4849   2632   3560    367      7    293       C  
ATOM    733  C   SER A 276     -20.708 -12.400  -5.975  1.00 31.47           C  
ANISOU  733  C   SER A 276     4896   3261   3799    454    349    460       C  
ATOM    734  O   SER A 276     -20.307 -13.337  -5.281  1.00 33.16           O  
ANISOU  734  O   SER A 276     5171   3266   4160    147     44    657       O  
ATOM    735  CB  SER A 276     -23.018 -12.644  -6.975  1.00 26.35           C  
ANISOU  735  CB  SER A 276     4684   2396   2928    336    353    446       C  
ATOM    736  OG  SER A 276     -22.594 -12.273  -8.270  1.00 27.67           O  
ANISOU  736  OG  SER A 276     5157   2488   2865    255    -21    870       O  
ATOM    737  N   TRP A 277     -19.929 -11.708  -6.811  1.00 32.02           N  
ANISOU  737  N   TRP A 277     4994   3040   4132    437    525    441       N  
ATOM    738  CA  TRP A 277     -18.476 -11.870  -6.887  1.00 32.08           C  
ANISOU  738  CA  TRP A 277     4907   3235   4044    245    368    567       C  
ATOM    739  C   TRP A 277     -17.828 -10.552  -6.491  1.00 33.59           C  
ANISOU  739  C   TRP A 277     5158   3118   4485    195    462    701       C  
ATOM    740  O   TRP A 277     -18.346  -9.498  -6.834  1.00 35.89           O  
ANISOU  740  O   TRP A 277     6162   3190   4284    254    730   1088       O  
ATOM    741  CB  TRP A 277     -18.029 -12.200  -8.317  1.00 29.50           C  
ANISOU  741  CB  TRP A 277     4706   2568   3931    551    406    974       C  
ATOM    742  CG  TRP A 277     -18.193 -13.626  -8.793  1.00 27.78           C  
ANISOU  742  CG  TRP A 277     4323   2686   3544    652    442    819       C  
ATOM    743  CD1 TRP A 277     -18.907 -14.038  -9.883  1.00 27.72           C  
ANISOU  743  CD1 TRP A 277     3964   2714   3854    301    414    913       C  
ATOM    744  CD2 TRP A 277     -17.584 -14.814  -8.237  1.00 27.09           C  
ANISOU  744  CD2 TRP A 277     4301   2541   3450    348    374    996       C  
ATOM    745  NE1 TRP A 277     -18.799 -15.405 -10.034  1.00 28.56           N  
ANISOU  745  NE1 TRP A 277     4330   2771   3749    513    405    842       N  
ATOM    746  CE2 TRP A 277     -17.995 -15.909  -9.045  1.00 28.51           C  
ANISOU  746  CE2 TRP A 277     4435   2767   3629    373    310    864       C  
ATOM    747  CE3 TRP A 277     -16.736 -15.058  -7.140  1.00 24.88           C  
ANISOU  747  CE3 TRP A 277     3989   2142   3323    213    457    882       C  
ATOM    748  CZ2 TRP A 277     -17.598 -17.246  -8.783  1.00 28.64           C  
ANISOU  748  CZ2 TRP A 277     4256   2852   3774    525    218    717       C  
ATOM    749  CZ3 TRP A 277     -16.336 -16.393  -6.871  1.00 25.11           C  
ANISOU  749  CZ3 TRP A 277     3703   2438   3399    479     59    946       C  
ATOM    750  CH2 TRP A 277     -16.770 -17.469  -7.696  1.00 26.56           C  
ANISOU  750  CH2 TRP A 277     4159   2328   3604    363    368    859       C  
ATOM    751  N   SER A 278     -16.699 -10.615  -5.786  1.00 32.64           N  
ANISOU  751  N   SER A 278     4859   3097   4442    -40    661    710       N  
ATOM    752  CA  SER A 278     -15.876  -9.435  -5.509  1.00 36.13           C  
ANISOU  752  CA  SER A 278     5242   3366   5118   -245    504    716       C  
ATOM    753  C   SER A 278     -15.193  -8.931  -6.809  1.00 37.46           C  
ANISOU  753  C   SER A 278     5638   3260   5334   -224    664    837       C  
ATOM    754  O   SER A 278     -15.067  -9.707  -7.767  1.00 39.25           O  
ANISOU  754  O   SER A 278     6013   3170   5729    162    543    658       O  
ATOM    755  CB  SER A 278     -14.847  -9.748  -4.411  1.00 38.19           C  
ANISOU  755  CB  SER A 278     5341   3621   5548     24    488   1336       C  
ATOM    756  OG  SER A 278     -13.880 -10.671  -4.870  1.00 42.52           O  
ANISOU  756  OG  SER A 278     4992   4579   6583    451    158    977       O  
ATOM    757  N   PRO A 279     -14.761  -7.643  -6.854  1.00 35.25           N  
ANISOU  757  N   PRO A 279     5459   2986   4947     42    658    877       N  
ATOM    758  CA  PRO A 279     -14.247  -7.050  -8.105  1.00 34.66           C  
ANISOU  758  CA  PRO A 279     5269   2784   5113   -219    874    741       C  
ATOM    759  C   PRO A 279     -12.921  -7.617  -8.608  1.00 38.81           C  
ANISOU  759  C   PRO A 279     5227   3396   6121   -112   1117   1263       C  
ATOM    760  O   PRO A 279     -12.070  -7.978  -7.803  1.00 41.11           O  
ANISOU  760  O   PRO A 279     5691   3109   6819     -8   1011   2082       O  
ATOM    761  CB  PRO A 279     -14.030  -5.570  -7.733  1.00 35.18           C  
ANISOU  761  CB  PRO A 279     5609   2653   5103   -453    860   1067       C  
ATOM    762  CG  PRO A 279     -14.883  -5.333  -6.536  1.00 36.88           C  
ANISOU  762  CG  PRO A 279     6407   2617   4987   -507    868    417       C  
ATOM    763  CD  PRO A 279     -14.841  -6.629  -5.780  1.00 38.22           C  
ANISOU  763  CD  PRO A 279     6550   3206   4765   -276    447    802       C  
ATOM    764  N   CYS A 280     -12.754  -7.667  -9.931  1.00 43.32           N  
ANISOU  764  N   CYS A 280     5896   4400   6163   -646   1253   1189       N  
ATOM    765  CA  CYS A 280     -11.442  -7.866 -10.569  1.00 46.24           C  
ANISOU  765  CA  CYS A 280     6329   4480   6758   -146   1560   1202       C  
ATOM    766  C   CYS A 280     -10.555  -6.609 -10.336  1.00 49.28           C  
ANISOU  766  C   CYS A 280     6399   4776   7548   -308   1468    906       C  
ATOM    767  O   CYS A 280     -11.093  -5.554  -9.969  1.00 46.43           O  
ANISOU  767  O   CYS A 280     6140   3888   7612   -536    522   1267       O  
ATOM    768  CB  CYS A 280     -11.622  -8.139 -12.070  1.00 44.63           C  
ANISOU  768  CB  CYS A 280     6455   3867   6633     91   1648   1060       C  
ATOM    769  SG  CYS A 280     -12.009  -6.664 -13.055  1.00 50.81           S  
ANISOU  769  SG  CYS A 280     7807   4439   7056   -687   1632   2011       S  
ATOM    770  N   PRO A 281      -9.210  -6.711 -10.542  1.00 51.14           N  
ANISOU  770  N   PRO A 281     6504   5125   7799   -581   1950    805       N  
ATOM    771  CA  PRO A 281      -8.336  -5.542 -10.301  1.00 49.88           C  
ANISOU  771  CA  PRO A 281     6098   4529   8324   -439   2549   1362       C  
ATOM    772  C   PRO A 281      -8.616  -4.293 -11.155  1.00 50.80           C  
ANISOU  772  C   PRO A 281     6495   4581   8223   -222   2327   1230       C  
ATOM    773  O   PRO A 281      -8.437  -3.177 -10.658  1.00 55.99           O  
ANISOU  773  O   PRO A 281     7593   4448   9231   -347   3100   1044       O  
ATOM    774  CB  PRO A 281      -6.920  -6.082 -10.572  1.00 48.95           C  
ANISOU  774  CB  PRO A 281     5616   4422   8557   -731   1877   1236       C  
ATOM    775  CG  PRO A 281      -7.105  -7.359 -11.309  1.00 50.63           C  
ANISOU  775  CG  PRO A 281     6022   5365   7851   -258   2332    450       C  
ATOM    776  CD  PRO A 281      -8.405  -7.918 -10.822  1.00 50.02           C  
ANISOU  776  CD  PRO A 281     6575   5151   7280   -413   2307   1303       C  
ATOM    777  N   GLU A 282      -9.040  -4.478 -12.409  1.00 53.23           N  
ANISOU  777  N   GLU A 282     6611   5133   8478    191   1921    954       N  
ATOM    778  CA  GLU A 282      -9.420  -3.358 -13.287  1.00 56.10           C  
ANISOU  778  CA  GLU A 282     7528   4510   9275   -588   2456   1471       C  
ATOM    779  C   GLU A 282     -10.644  -2.627 -12.746  1.00 55.53           C  
ANISOU  779  C   GLU A 282     7686   4587   8826   -395   2263   1497       C  
ATOM    780  O   GLU A 282     -10.663  -1.400 -12.720  1.00 59.68           O  
ANISOU  780  O   GLU A 282     8583   4598   9491   -158   2174   2057       O  
ATOM    781  CB  GLU A 282      -9.681  -3.826 -14.723  1.00 61.50           C  
ANISOU  781  CB  GLU A 282     8502   5562   9301   -350   2389   1637       C  
ATOM    782  CG  GLU A 282      -8.438  -3.970 -15.592  1.00 73.76           C  
ANISOU  782  CG  GLU A 282     9495   7508  11020  -1229   3712   1372       C  
ATOM    783  CD  GLU A 282      -7.611  -5.216 -15.295  1.00 85.94           C  
ANISOU  783  CD  GLU A 282    11161   8799  12693    124   3165    993       C  
ATOM    784  OE1 GLU A 282      -6.427  -5.238 -15.692  1.00 96.84           O  
ANISOU  784  OE1 GLU A 282    11653  11037  14103  -2010   4331    109       O  
ATOM    785  OE2 GLU A 282      -8.127  -6.177 -14.675  1.00 91.97           O  
ANISOU  785  OE2 GLU A 282    11851  10481  12610   -848   4063    912       O  
ATOM    786  N   CYS A 283     -11.653  -3.386 -12.311  1.00 54.37           N  
ANISOU  786  N   CYS A 283     7295   4897   8463   -298   2260   1323       N  
ATOM    787  CA  CYS A 283     -12.833  -2.814 -11.663  1.00 52.12           C  
ANISOU  787  CA  CYS A 283     7262   4611   7928   -486   1966   1011       C  
ATOM    788  C   CYS A 283     -12.514  -2.187 -10.322  1.00 51.92           C  
ANISOU  788  C   CYS A 283     7360   4322   8044   -679   1778   1045       C  
ATOM    789  O   CYS A 283     -12.978  -1.084 -10.035  1.00 52.69           O  
ANISOU  789  O   CYS A 283     7276   4399   8344   -257   2306   1727       O  
ATOM    790  CB  CYS A 283     -13.921  -3.858 -11.478  1.00 51.86           C  
ANISOU  790  CB  CYS A 283     7564   4332   7806   -492   1460   1584       C  
ATOM    791  SG  CYS A 283     -15.007  -3.963 -12.902  1.00 49.86           S  
ANISOU  791  SG  CYS A 283     8141   3806   6996   -208   1826    318       S  
ATOM    792  N   ALA A 284     -11.722  -2.891  -9.513  1.00 51.57           N  
ANISOU  792  N   ALA A 284     7549   4111   7932  -1037   1641   1119       N  
ATOM    793  CA  ALA A 284     -11.294  -2.392  -8.206  1.00 53.26           C  
ANISOU  793  CA  ALA A 284     7225   4510   8498  -1109   1064    965       C  
ATOM    794  C   ALA A 284     -10.548  -1.054  -8.311  1.00 52.69           C  
ANISOU  794  C   ALA A 284     7231   4539   8248  -1166   1637    848       C  
ATOM    795  O   ALA A 284     -10.848  -0.126  -7.564  1.00 54.51           O  
ANISOU  795  O   ALA A 284     7570   4117   9021  -1118   2029    969       O  
ATOM    796  CB  ALA A 284     -10.456  -3.436  -7.488  1.00 51.77           C  
ANISOU  796  CB  ALA A 284     6951   3457   9260  -1550    929    866       C  
ATOM    797  N   GLY A 285      -9.610  -0.965  -9.258  1.00 53.67           N  
ANISOU  797  N   GLY A 285     7150   4275   8966  -1399   1832   1030       N  
ATOM    798  CA  GLY A 285      -8.843   0.258  -9.534  1.00 53.87           C  
ANISOU  798  CA  GLY A 285     7587   4160   8718  -1406   2169   1085       C  
ATOM    799  C   GLY A 285      -9.702   1.408 -10.030  1.00 56.91           C  
ANISOU  799  C   GLY A 285     7783   4668   9173  -1322   2319   1485       C  
ATOM    800  O   GLY A 285      -9.505   2.556  -9.617  1.00 64.68           O  
ANISOU  800  O   GLY A 285     9539   5442   9595  -1687   2208    725       O  
ATOM    801  N   GLU A 286     -10.654   1.097 -10.912  1.00 56.00           N  
ANISOU  801  N   GLU A 286     8215   4247   8813  -1336   2460   1126       N  
ATOM    802  CA  GLU A 286     -11.619   2.075 -11.427  1.00 59.47           C  
ANISOU  802  CA  GLU A 286     8366   5000   9230   -723   2809   1257       C  
ATOM    803  C   GLU A 286     -12.563   2.618 -10.354  1.00 54.54           C  
ANISOU  803  C   GLU A 286     8394   3772   8556  -1079   2351   1103       C  
ATOM    804  O   GLU A 286     -12.863   3.814 -10.350  1.00 55.27           O  
ANISOU  804  O   GLU A 286     8263   4076   8660   -479   2349   2318       O  
ATOM    805  CB  GLU A 286     -12.426   1.489 -12.586  1.00 67.77           C  
ANISOU  805  CB  GLU A 286     9641   6093  10014   -392   1887   1031       C  
ATOM    806  CG  GLU A 286     -11.802   1.731 -13.949  1.00 81.57           C  
ANISOU  806  CG  GLU A 286    12089   8722  10182    931   2151   2346       C  
ATOM    807  CD  GLU A 286     -12.459   0.916 -15.044  1.00 92.53           C  
ANISOU  807  CD  GLU A 286    14434   8919  11801   1030   1357   1523       C  
ATOM    808  OE1 GLU A 286     -12.201  -0.301 -15.116  1.00 87.65           O  
ANISOU  808  OE1 GLU A 286    15608   8128   9566    468    812   5397       O  
ATOM    809  OE2 GLU A 286     -13.221   1.496 -15.845  1.00106.00           O  
ANISOU  809  OE2 GLU A 286    14189  12127  13958   2914    706   1060       O  
ATOM    810  N   VAL A 287     -13.024   1.742  -9.456  1.00 48.24           N  
ANISOU  810  N   VAL A 287     7269   3173   7886   -813   2044    641       N  
ATOM    811  CA  VAL A 287     -13.892   2.143  -8.344  1.00 40.89           C  
ANISOU  811  CA  VAL A 287     6526   1886   7121  -1676   1991   1283       C  
ATOM    812  C   VAL A 287     -13.104   3.007  -7.341  1.00 48.79           C  
ANISOU  812  C   VAL A 287     7226   3897   7414  -1441   1578    709       C  
ATOM    813  O   VAL A 287     -13.578   4.078  -6.932  1.00 53.08           O  
ANISOU  813  O   VAL A 287     7936   4338   7894   -886   1641    511       O  
ATOM    814  CB  VAL A 287     -14.589   0.932  -7.671  1.00 40.50           C  
ANISOU  814  CB  VAL A 287     6311   2148   6928  -1685   1750   1143       C  
ATOM    815  CG1 VAL A 287     -15.423   1.375  -6.479  1.00 46.14           C  
ANISOU  815  CG1 VAL A 287     6268   4159   7103   -887   1759    764       C  
ATOM    816  CG2 VAL A 287     -15.495   0.203  -8.658  1.00 41.15           C  
ANISOU  816  CG2 VAL A 287     6162   2300   7171   -778   1631    100       C  
ATOM    817  N   ALA A 288     -11.898   2.557  -6.983  1.00 51.75           N  
ANISOU  817  N   ALA A 288     7055   4267   8339  -1369   1841   1026       N  
ATOM    818  CA  ALA A 288     -10.986   3.321  -6.118  1.00 60.14           C  
ANISOU  818  CA  ALA A 288     8350   4994   9505  -1731   1339    275       C  
ATOM    819  C   ALA A 288     -10.713   4.737  -6.643  1.00 64.18           C  
ANISOU  819  C   ALA A 288     8989   5183  10213  -2366   1602    308       C  
ATOM    820  O   ALA A 288     -10.747   5.701  -5.873  1.00 68.55           O  
ANISOU  820  O   ALA A 288     9567   5995  10484  -1779   1518   -266       O  
ATOM    821  CB  ALA A 288      -9.681   2.563  -5.909  1.00 64.64           C  
ANISOU  821  CB  ALA A 288     8080   6292  10186  -1478    937   -282       C  
ATOM    822  N   GLU A 289     -10.470   4.856  -7.951  1.00 64.75           N  
ANISOU  822  N   GLU A 289     8922   5149  10530  -2613   1764    630       N  
ATOM    823  CA  GLU A 289     -10.236   6.157  -8.582  1.00 68.51           C  
ANISOU  823  CA  GLU A 289     9851   4741  11437  -1616   1786    888       C  
ATOM    824  C   GLU A 289     -11.510   7.001  -8.669  1.00 67.26           C  
ANISOU  824  C   GLU A 289     9437   4913  11204  -1905   1773    477       C  
ATOM    825  O   GLU A 289     -11.441   8.233  -8.607  1.00 71.35           O  
ANISOU  825  O   GLU A 289     9970   4886  12254  -1871   1491    319       O  
ATOM    826  CB  GLU A 289      -9.593   6.011  -9.965  1.00 76.76           C  
ANISOU  826  CB  GLU A 289    10273   6641  12250  -1287   2737    966       C  
ATOM    827  CG  GLU A 289      -8.808   7.250 -10.401  1.00 89.95           C  
ANISOU  827  CG  GLU A 289    12628   7128  14418  -1740   3555   1803       C  
ATOM    828  CD  GLU A 289      -8.445   7.268 -11.880  1.00102.14           C  
ANISOU  828  CD  GLU A 289    15511   9162  14133  -1663   2801   1655       C  
ATOM    829  OE1 GLU A 289      -8.566   6.222 -12.561  1.00110.72           O  
ANISOU  829  OE1 GLU A 289    16547  11564  13956  -2346    -86    179       O  
ATOM    830  OE2 GLU A 289      -8.027   8.344 -12.364  1.00108.26           O  
ANISOU  830  OE2 GLU A 289    16546   8109  16478  -2182   2317   1139       O  
ATOM    831  N   PHE A 290     -12.662   6.344  -8.820  1.00 61.78           N  
ANISOU  831  N   PHE A 290     9177   3680  10615  -1572   2521   1414       N  
ATOM    832  CA  PHE A 290     -13.948   7.042  -8.788  1.00 58.34           C  
ANISOU  832  CA  PHE A 290     8774   4036   9357  -1646   2443   1119       C  
ATOM    833  C   PHE A 290     -14.199   7.667  -7.412  1.00 59.46           C  
ANISOU  833  C   PHE A 290     8769   4005   9817  -1473   2295    702       C  
ATOM    834  O   PHE A 290     -14.690   8.795  -7.324  1.00 65.55           O  
ANISOU  834  O   PHE A 290     9655   3490  11761  -1757   1882   1110       O  
ATOM    835  CB  PHE A 290     -15.097   6.111  -9.197  1.00 55.12           C  
ANISOU  835  CB  PHE A 290     8824   3547   8571  -1147   2156    728       C  
ATOM    836  CG  PHE A 290     -16.461   6.618  -8.806  1.00 56.82           C  
ANISOU  836  CG  PHE A 290     9205   3562   8822   -649   1955    327       C  
ATOM    837  CD1 PHE A 290     -17.171   7.476  -9.646  1.00 54.12           C  
ANISOU  837  CD1 PHE A 290     9595   3311   7655   -703   2392    297       C  
ATOM    838  CD2 PHE A 290     -17.038   6.240  -7.583  1.00 60.76           C  
ANISOU  838  CD2 PHE A 290     9484   4968   8634   -584   2007    136       C  
ATOM    839  CE1 PHE A 290     -18.425   7.947  -9.276  1.00 60.02           C  
ANISOU  839  CE1 PHE A 290     9308   4577   8920   -246   1981    958       C  
ATOM    840  CE2 PHE A 290     -18.289   6.712  -7.209  1.00 61.86           C  
ANISOU  840  CE2 PHE A 290     9644   5863   7994   -184   1905    271       C  
ATOM    841  CZ  PHE A 290     -18.981   7.567  -8.057  1.00 61.65           C  
ANISOU  841  CZ  PHE A 290     9597   4710   9116   -388   2267    778       C  
ATOM    842  N   LEU A 291     -13.863   6.929  -6.354  1.00 59.33           N  
ANISOU  842  N   LEU A 291     8585   4292   9664  -1597   2089    654       N  
ATOM    843  CA  LEU A 291     -14.069   7.383  -4.975  1.00 59.58           C  
ANISOU  843  CA  LEU A 291     8923   3994   9719  -1664   1617    173       C  
ATOM    844  C   LEU A 291     -13.118   8.502  -4.562  1.00 64.94           C  
ANISOU  844  C   LEU A 291     9331   4463  10878  -2137   1793    -74       C  
ATOM    845  O   LEU A 291     -13.488   9.363  -3.760  1.00 69.06           O  
ANISOU  845  O   LEU A 291     9206   5422  11610  -1381   2634   -220       O  
ATOM    846  CB  LEU A 291     -13.972   6.212  -3.992  1.00 57.12           C  
ANISOU  846  CB  LEU A 291     8591   3993   9116  -1949   1536     -9       C  
ATOM    847  CG  LEU A 291     -15.046   5.115  -4.054  1.00 53.89           C  
ANISOU  847  CG  LEU A 291     8030   3867   8576  -1621   1569     53       C  
ATOM    848  CD1 LEU A 291     -14.586   3.884  -3.286  1.00 51.82           C  
ANISOU  848  CD1 LEU A 291     7783   3601   8305  -1821   1240   -317       C  
ATOM    849  CD2 LEU A 291     -16.405   5.594  -3.553  1.00 50.55           C  
ANISOU  849  CD2 LEU A 291     8099   2872   8234  -1517   1753    632       C  
ATOM    850  N   ALA A 292     -11.900   8.480  -5.109  1.00 68.54           N  
ANISOU  850  N   ALA A 292     9707   4806  11530  -2254   2215     42       N  
ATOM    851  CA  ALA A 292     -10.908   9.545  -4.905  1.00 69.61           C  
ANISOU  851  CA  ALA A 292     9669   5044  11735  -2493   2224    491       C  
ATOM    852  C   ALA A 292     -11.356  10.843  -5.579  1.00 66.50           C  
ANISOU  852  C   ALA A 292     9189   4347  11730  -2522   2102   -274       C  
ATOM    853  O   ALA A 292     -11.143  11.933  -5.052  1.00 69.28           O  
ANISOU  853  O   ALA A 292     9502   5057  11762  -2989   2101   -836       O  
ATOM    854  CB  ALA A 292      -9.549   9.108  -5.434  1.00 67.35           C  
ANISOU  854  CB  ALA A 292     8732   4456  12403  -3428   1805    669       C  
ATOM    855  N   ARG A 293     -11.986  10.690  -6.743  1.00 69.12           N  
ANISOU  855  N   ARG A 293     9919   5088  11253  -1615   2229   -430       N  
ATOM    856  CA  ARG A 293     -12.557  11.775  -7.538  1.00 74.13           C  
ANISOU  856  CA  ARG A 293    11471   4196  12499  -2055   2385    214       C  
ATOM    857  C   ARG A 293     -13.799  12.399  -6.869  1.00 75.02           C  
ANISOU  857  C   ARG A 293    11403   4784  12316  -1828   2264    426       C  
ATOM    858  O   ARG A 293     -14.051  13.597  -7.026  1.00 76.15           O  
ANISOU  858  O   ARG A 293    11519   4608  12803  -2690   2316   1399       O  
ATOM    859  CB  ARG A 293     -12.891  11.226  -8.937  1.00 78.65           C  
ANISOU  859  CB  ARG A 293    12806   4455  12623  -1416   1838    570       C  
ATOM    860  CG  ARG A 293     -13.396  12.209  -9.980  1.00 87.62           C  
ANISOU  860  CG  ARG A 293    14107   5496  13687  -1709   1939   2084       C  
ATOM    861  CD  ARG A 293     -12.278  12.880 -10.766  1.00 97.76           C  
ANISOU  861  CD  ARG A 293    13107   9324  14711  -2459   2493    978       C  
ATOM    862  NE  ARG A 293     -12.817  13.774 -11.797  1.00102.70           N  
ANISOU  862  NE  ARG A 293    15475   8552  14995  -2375   1577    553       N  
ATOM    863  CZ  ARG A 293     -13.235  15.026 -11.594  1.00108.01           C  
ANISOU  863  CZ  ARG A 293    15992   9153  15894  -1178   2080   1090       C  
ATOM    864  NH1 ARG A 293     -13.183  15.586 -10.389  1.00111.49           N  
ANISOU  864  NH1 ARG A 293    16330   9406  16622   -124   2603    130       N  
ATOM    865  NH2 ARG A 293     -13.711  15.729 -12.610  1.00112.15           N  
ANISOU  865  NH2 ARG A 293    16465  10454  15693    -89   2239   1118       N  
ATOM    866  N   HIS A 294     -14.557  11.588  -6.124  1.00 74.07           N  
ANISOU  866  N   HIS A 294    10886   5392  11864  -1821   2604    -45       N  
ATOM    867  CA  HIS A 294     -15.804  12.035  -5.479  1.00 68.76           C  
ANISOU  867  CA  HIS A 294    10578   4763  10784  -1830   2142    150       C  
ATOM    868  C   HIS A 294     -15.840  11.778  -3.960  1.00 66.18           C  
ANISOU  868  C   HIS A 294    10602   4043  10499  -2056   2019   -618       C  
ATOM    869  O   HIS A 294     -16.198  10.678  -3.502  1.00 64.89           O  
ANISOU  869  O   HIS A 294    10171   3769  10713  -1389   1804   -264       O  
ATOM    870  CB  HIS A 294     -17.032  11.411  -6.164  1.00 64.01           C  
ANISOU  870  CB  HIS A 294    10602   3357  10359  -1548   2276    -41       C  
ATOM    871  CG  HIS A 294     -17.050  11.577  -7.651  1.00 66.16           C  
ANISOU  871  CG  HIS A 294    10862   3870  10407  -1303   1909    196       C  
ATOM    872  ND1 HIS A 294     -16.556  10.621  -8.512  1.00 67.91           N  
ANISOU  872  ND1 HIS A 294    10478   4662  10660   -229   1779    346       N  
ATOM    873  CD2 HIS A 294     -17.496  12.590  -8.430  1.00 71.45           C  
ANISOU  873  CD2 HIS A 294    11414   4966  10765   -427   1529    332       C  
ATOM    874  CE1 HIS A 294     -16.702  11.035  -9.758  1.00 70.93           C  
ANISOU  874  CE1 HIS A 294    11049   4946  10955   -423   1439    672       C  
ATOM    875  NE2 HIS A 294     -17.267  12.228  -9.736  1.00 71.10           N  
ANISOU  875  NE2 HIS A 294    11842   4559  10612   -644   1503    702       N  
ATOM    876  N   SER A 295     -15.475  12.813  -3.199  1.00 64.78           N  
ANISOU  876  N   SER A 295    10260   3476  10875  -2508   2557   -467       N  
ATOM    877  CA  SER A 295     -15.497  12.810  -1.726  1.00 66.73           C  
ANISOU  877  CA  SER A 295    10572   4087  10693  -2608   1690   -610       C  
ATOM    878  C   SER A 295     -16.913  12.720  -1.150  1.00 63.88           C  
ANISOU  878  C   SER A 295    10444   3427  10398  -2822   1434   -533       C  
ATOM    879  O   SER A 295     -17.103  12.226  -0.032  1.00 67.54           O  
ANISOU  879  O   SER A 295    11660   4272   9727  -2861   1331  -1086       O  
ATOM    880  CB  SER A 295     -14.827  14.075  -1.180  1.00 69.22           C  
ANISOU  880  CB  SER A 295    11030   4372  10898  -2886    990   -484       C  
ATOM    881  OG  SER A 295     -13.563  14.287  -1.777  1.00 76.69           O  
ANISOU  881  OG  SER A 295    11021   6055  12061  -1992   1186  -1161       O  
ATOM    882  N   ASN A 296     -17.890  13.215  -1.914  1.00 56.95           N  
ANISOU  882  N   ASN A 296     9902   1875   9860  -2567   1904   -939       N  
ATOM    883  CA  ASN A 296     -19.302  13.206  -1.522  1.00 56.72           C  
ANISOU  883  CA  ASN A 296     9815   2635   9099  -1607   1596  -1124       C  
ATOM    884  C   ASN A 296     -19.987  11.833  -1.615  1.00 54.72           C  
ANISOU  884  C   ASN A 296     9409   2657   8723  -1552   1805  -1061       C  
ATOM    885  O   ASN A 296     -21.142  11.694  -1.208  1.00 56.45           O  
ANISOU  885  O   ASN A 296     9737   2813   8896  -1502   2212  -2228       O  
ATOM    886  CB  ASN A 296     -20.086  14.267  -2.317  1.00 56.36           C  
ANISOU  886  CB  ASN A 296    10023   2090   9297  -1666   1758  -1076       C  
ATOM    887  CG  ASN A 296     -20.058  14.026  -3.822  1.00 59.15           C  
ANISOU  887  CG  ASN A 296    10256   2980   9236  -1316   2122   -427       C  
ATOM    888  OD1 ASN A 296     -19.027  13.665  -4.395  1.00 61.56           O  
ANISOU  888  OD1 ASN A 296    10529   3341   9521  -1116   2435   -286       O  
ATOM    889  ND2 ASN A 296     -21.197  14.237  -4.471  1.00 58.63           N  
ANISOU  889  ND2 ASN A 296     9890   3133   9251   -952   2431   -477       N  
ATOM    890  N   VAL A 297     -19.273  10.834  -2.145  1.00 53.10           N  
ANISOU  890  N   VAL A 297     8894   2746   8535  -1533   1716   -902       N  
ATOM    891  CA  VAL A 297     -19.776   9.456  -2.259  1.00 51.20           C  
ANISOU  891  CA  VAL A 297     8973   2632   7846  -1405   1919   -806       C  
ATOM    892  C   VAL A 297     -19.096   8.549  -1.229  1.00 53.95           C  
ANISOU  892  C   VAL A 297     9051   3441   8005  -1405   1550   -679       C  
ATOM    893  O   VAL A 297     -17.867   8.480  -1.158  1.00 56.14           O  
ANISOU  893  O   VAL A 297     9010   3489   8830  -1351   2089   -571       O  
ATOM    894  CB  VAL A 297     -19.596   8.864  -3.690  1.00 48.00           C  
ANISOU  894  CB  VAL A 297     8443   2206   7586  -1329   2035   -392       C  
ATOM    895  CG1 VAL A 297     -20.185   7.456  -3.783  1.00 43.58           C  
ANISOU  895  CG1 VAL A 297     7983   1862   6712   -877   2358   -293       C  
ATOM    896  CG2 VAL A 297     -20.228   9.763  -4.748  1.00 42.42           C  
ANISOU  896  CG2 VAL A 297     7992    916   7207  -1644   2827   -283       C  
ATOM    897  N   ASN A 298     -19.918   7.864  -0.437  1.00 55.65           N  
ANISOU  897  N   ASN A 298     9312   3263   8566  -1777   1757   -917       N  
ATOM    898  CA  ASN A 298     -19.459   6.886   0.540  1.00 59.30           C  
ANISOU  898  CA  ASN A 298     9455   4401   8676  -1444    947   -759       C  
ATOM    899  C   ASN A 298     -19.946   5.496   0.122  1.00 55.53           C  
ANISOU  899  C   ASN A 298     8758   4284   8053  -1216    969   -555       C  
ATOM    900  O   ASN A 298     -21.151   5.289  -0.068  1.00 53.59           O  
ANISOU  900  O   ASN A 298     9125   3609   7626  -2057    385   -564       O  
ATOM    901  CB  ASN A 298     -19.987   7.254   1.929  1.00 68.16           C  
ANISOU  901  CB  ASN A 298    10476   6410   9011  -1634   1341  -1191       C  
ATOM    902  CG  ASN A 298     -19.200   6.603   3.048  1.00 78.38           C  
ANISOU  902  CG  ASN A 298    11864   7607  10310  -1437    566   -744       C  
ATOM    903  OD1 ASN A 298     -18.111   7.057   3.402  1.00 89.59           O  
ANISOU  903  OD1 ASN A 298    12857   9706  11475  -2235    316  -2761       O  
ATOM    904  ND2 ASN A 298     -19.759   5.545   3.627  1.00 77.57           N  
ANISOU  904  ND2 ASN A 298    11701   6797  10972  -1803    505  -1558       N  
ATOM    905  N   LEU A 299     -19.011   4.557  -0.036  1.00 50.52           N  
ANISOU  905  N   LEU A 299     8637   3769   6787  -1485   1140   -847       N  
ATOM    906  CA  LEU A 299     -19.338   3.220  -0.530  1.00 47.73           C  
ANISOU  906  CA  LEU A 299     8009   3568   6555  -1321    870   -536       C  
ATOM    907  C   LEU A 299     -19.043   2.090   0.457  1.00 48.31           C  
ANISOU  907  C   LEU A 299     7953   4278   6123  -1326    736   -387       C  
ATOM    908  O   LEU A 299     -17.933   1.993   0.991  1.00 51.40           O  
ANISOU  908  O   LEU A 299     8016   4658   6853  -1588    503   -351       O  
ATOM    909  CB  LEU A 299     -18.654   2.949  -1.885  1.00 48.07           C  
ANISOU  909  CB  LEU A 299     7896   3638   6728  -1397   1044   -392       C  
ATOM    910  CG  LEU A 299     -18.863   1.591  -2.583  1.00 44.75           C  
ANISOU  910  CG  LEU A 299     7227   3437   6337   -873    924   -271       C  
ATOM    911  CD1 LEU A 299     -20.322   1.317  -2.928  1.00 42.14           C  
ANISOU  911  CD1 LEU A 299     7223   2355   6433   -956    976   -179       C  
ATOM    912  CD2 LEU A 299     -18.002   1.485  -3.828  1.00 42.83           C  
ANISOU  912  CD2 LEU A 299     6853   2922   6498   -828    951     43       C  
ATOM    913  N   THR A 300     -20.055   1.247   0.677  1.00 43.65           N  
ANISOU  913  N   THR A 300     7688   3159   5738   -957    463   -915       N  
ATOM    914  CA  THR A 300     -19.931   0.017   1.451  1.00 44.57           C  
ANISOU  914  CA  THR A 300     7606   3485   5843  -1172    452   -546       C  
ATOM    915  C   THR A 300     -20.170  -1.160   0.499  1.00 40.91           C  
ANISOU  915  C   THR A 300     6814   3233   5495   -893    161   -213       C  
ATOM    916  O   THR A 300     -21.215  -1.243  -0.145  1.00 39.99           O  
ANISOU  916  O   THR A 300     6553   2702   5939  -1016    224    342       O  
ATOM    917  CB  THR A 300     -20.932  -0.018   2.634  1.00 46.35           C  
ANISOU  917  CB  THR A 300     7854   3790   5964  -1031    556   -751       C  
ATOM    918  OG1 THR A 300     -20.678   1.081   3.513  1.00 51.51           O  
ANISOU  918  OG1 THR A 300     8756   4593   6221  -1434    395  -1236       O  
ATOM    919  CG2 THR A 300     -20.808  -1.308   3.436  1.00 47.23           C  
ANISOU  919  CG2 THR A 300     7903   4257   5784  -1205    563   -402       C  
ATOM    920  N   ILE A 301     -19.189  -2.053   0.402  1.00 39.23           N  
ANISOU  920  N   ILE A 301     6643   3155   5106   -996    112   -267       N  
ATOM    921  CA  ILE A 301     -19.305  -3.251  -0.433  1.00 36.30           C  
ANISOU  921  CA  ILE A 301     5925   3173   4693  -1003    125   -164       C  
ATOM    922  C   ILE A 301     -19.465  -4.504   0.436  1.00 37.22           C  
ANISOU  922  C   ILE A 301     6046   3228   4868   -874   -262    -32       C  
ATOM    923  O   ILE A 301     -18.579  -4.845   1.226  1.00 38.19           O  
ANISOU  923  O   ILE A 301     5649   3460   5400   -935   -496   -390       O  
ATOM    924  CB  ILE A 301     -18.114  -3.400  -1.418  1.00 35.66           C  
ANISOU  924  CB  ILE A 301     5585   2994   4970   -922     53     45       C  
ATOM    925  CG1 ILE A 301     -17.964  -2.134  -2.279  1.00 37.85           C  
ANISOU  925  CG1 ILE A 301     5859   3263   5259  -1208    401    246       C  
ATOM    926  CG2 ILE A 301     -18.285  -4.638  -2.303  1.00 35.75           C  
ANISOU  926  CG2 ILE A 301     5597   2799   5185   -419    -64     65       C  
ATOM    927  CD1 ILE A 301     -16.681  -2.057  -3.082  1.00 40.07           C  
ANISOU  927  CD1 ILE A 301     5762   3823   5637  -1188    447    223       C  
ATOM    928  N   PHE A 302     -20.620  -5.156   0.298  1.00 36.45           N  
ANISOU  928  N   PHE A 302     5690   3530   4628   -667   -282    192       N  
ATOM    929  CA  PHE A 302     -20.837  -6.508   0.807  1.00 34.84           C  
ANISOU  929  CA  PHE A 302     5468   3345   4423   -379    -37      3       C  
ATOM    930  C   PHE A 302     -20.747  -7.486  -0.361  1.00 34.38           C  
ANISOU  930  C   PHE A 302     5445   3558   4058   -315   -100    134       C  
ATOM    931  O   PHE A 302     -21.384  -7.271  -1.392  1.00 35.43           O  
ANISOU  931  O   PHE A 302     6282   3357   3820   -273    173    928       O  
ATOM    932  CB  PHE A 302     -22.204  -6.634   1.482  1.00 35.05           C  
ANISOU  932  CB  PHE A 302     5576   3848   3891   -420     -6   -354       C  
ATOM    933  CG  PHE A 302     -22.328  -5.878   2.773  1.00 35.24           C  
ANISOU  933  CG  PHE A 302     6035   3578   3774   -560      0   -204       C  
ATOM    934  CD1 PHE A 302     -21.794  -6.390   3.956  1.00 34.81           C  
ANISOU  934  CD1 PHE A 302     6031   3327   3865   -383   -192   -365       C  
ATOM    935  CD2 PHE A 302     -23.017  -4.665   2.816  1.00 36.43           C  
ANISOU  935  CD2 PHE A 302     6218   3475   4149   -654    107   -295       C  
ATOM    936  CE1 PHE A 302     -21.924  -5.698   5.157  1.00 40.58           C  
ANISOU  936  CE1 PHE A 302     7283   4088   4046   -330    -33   -689       C  
ATOM    937  CE2 PHE A 302     -23.156  -3.965   4.012  1.00 39.81           C  
ANISOU  937  CE2 PHE A 302     6858   4023   4245   -368    -39   -551       C  
ATOM    938  CZ  PHE A 302     -22.605  -4.480   5.186  1.00 42.29           C  
ANISOU  938  CZ  PHE A 302     7391   4339   4335   -148    -94   -418       C  
ATOM    939  N   THR A 303     -19.964  -8.555  -0.196  1.00 32.70           N  
ANISOU  939  N   THR A 303     5116   3099   4209   -626    -58     60       N  
ATOM    940  CA  THR A 303     -19.759  -9.534  -1.266  1.00 32.25           C  
ANISOU  940  CA  THR A 303     4930   3365   3957   -380     12    168       C  
ATOM    941  C   THR A 303     -20.053 -10.979  -0.827  1.00 32.02           C  
ANISOU  941  C   THR A 303     4947   3460   3757   -274   -303    379       C  
ATOM    942  O   THR A 303     -19.633 -11.409   0.252  1.00 32.41           O  
ANISOU  942  O   THR A 303     5165   2981   4168    736   -301    536       O  
ATOM    943  CB  THR A 303     -18.360  -9.404  -1.925  1.00 33.68           C  
ANISOU  943  CB  THR A 303     4826   3657   4312   -584    -91    421       C  
ATOM    944  OG1 THR A 303     -18.289 -10.260  -3.076  1.00 36.11           O  
ANISOU  944  OG1 THR A 303     4991   3866   4860   -705    399     97       O  
ATOM    945  CG2 THR A 303     -17.216  -9.747  -0.950  1.00 33.90           C  
ANISOU  945  CG2 THR A 303     4873   3749   4258   -474   -183    139       C  
ATOM    946  N   ALA A 304     -20.788 -11.711  -1.665  1.00 30.47           N  
ANISOU  946  N   ALA A 304     4404   3109   4061   -207   -121    249       N  
ATOM    947  CA  ALA A 304     -21.152 -13.096  -1.352  1.00 29.01           C  
ANISOU  947  CA  ALA A 304     4357   3149   3516    -36   -202    383       C  
ATOM    948  C   ALA A 304     -19.917 -13.982  -1.390  1.00 29.02           C  
ANISOU  948  C   ALA A 304     4524   3098   3402     61   -244    539       C  
ATOM    949  O   ALA A 304     -19.713 -14.790  -0.492  1.00 29.74           O  
ANISOU  949  O   ALA A 304     4903   2798   3597    152   -154    551       O  
ATOM    950  CB  ALA A 304     -22.235 -13.618  -2.297  1.00 25.06           C  
ANISOU  950  CB  ALA A 304     4365   2223   2934    -92    180    265       C  
ATOM    951  N   ARG A 305     -19.090 -13.792  -2.420  1.00 30.51           N  
ANISOU  951  N   ARG A 305     4245   3396   3951   -171    -59    593       N  
ATOM    952  CA  ARG A 305     -17.887 -14.595  -2.640  1.00 31.76           C  
ANISOU  952  CA  ARG A 305     4565   3480   4022     75    -46    612       C  
ATOM    953  C   ARG A 305     -16.685 -13.732  -3.027  1.00 35.47           C  
ANISOU  953  C   ARG A 305     4648   4007   4821   -185   -297    793       C  
ATOM    954  O   ARG A 305     -16.833 -12.612  -3.547  1.00 37.26           O  
ANISOU  954  O   ARG A 305     5129   3892   5134   -605   -541    922       O  
ATOM    955  CB  ARG A 305     -18.121 -15.615  -3.749  1.00 28.46           C  
ANISOU  955  CB  ARG A 305     4071   2923   3817    247    139    827       C  
ATOM    956  CG  ARG A 305     -19.164 -16.674  -3.456  1.00 28.85           C  
ANISOU  956  CG  ARG A 305     4322   3095   3542     96    148    704       C  
ATOM    957  CD  ARG A 305     -19.312 -17.604  -4.641  1.00 29.25           C  
ANISOU  957  CD  ARG A 305     4689   2701   3721    204     58    694       C  
ATOM    958  NE  ARG A 305     -19.567 -16.884  -5.893  1.00 30.68           N  
ANISOU  958  NE  ARG A 305     4736   3044   3876    568   -150    741       N  
ATOM    959  CZ  ARG A 305     -20.772 -16.558  -6.354  1.00 28.92           C  
ANISOU  959  CZ  ARG A 305     4694   2808   3484    478    -40    836       C  
ATOM    960  NH1 ARG A 305     -21.867 -16.891  -5.675  1.00 28.46           N  
ANISOU  960  NH1 ARG A 305     4524   2566   3723    352    -29    590       N  
ATOM    961  NH2 ARG A 305     -20.880 -15.892  -7.497  1.00 28.49           N  
ANISOU  961  NH2 ARG A 305     4740   2928   3156    289    141    695       N  
ATOM    962  N   LEU A 306     -15.499 -14.282  -2.790  1.00 35.60           N  
ANISOU  962  N   LEU A 306     4580   4274   4669   -117   -295    805       N  
ATOM    963  CA  LEU A 306     -14.256 -13.634  -3.162  1.00 37.49           C  
ANISOU  963  CA  LEU A 306     4807   4397   5038   -260   -104   1101       C  
ATOM    964  C   LEU A 306     -13.723 -14.215  -4.462  1.00 36.77           C  
ANISOU  964  C   LEU A 306     4758   3914   5297   -152     33   1051       C  
ATOM    965  O   LEU A 306     -13.383 -15.388  -4.542  1.00 39.74           O  
ANISOU  965  O   LEU A 306     4746   4208   6143    317    316   1226       O  
ATOM    966  CB  LEU A 306     -13.224 -13.752  -2.038  1.00 38.59           C  
ANISOU  966  CB  LEU A 306     4808   4492   5360   -564   -350    966       C  
ATOM    967  CG  LEU A 306     -13.513 -13.038  -0.712  1.00 36.85           C  
ANISOU  967  CG  LEU A 306     4388   4174   5436   -450   -381   1018       C  
ATOM    968  CD1 LEU A 306     -12.428 -13.368   0.311  1.00 37.38           C  
ANISOU  968  CD1 LEU A 306     4238   4438   5527   -258   -333   1049       C  
ATOM    969  CD2 LEU A 306     -13.659 -11.528  -0.894  1.00 37.07           C  
ANISOU  969  CD2 LEU A 306     4494   4313   5276      8   -456   1643       C  
ATOM    970  N   TYR A 307     -13.671 -13.371  -5.484  1.00 35.70           N  
ANISOU  970  N   TYR A 307     4687   3932   4946   -230    382    818       N  
ATOM    971  CA  TYR A 307     -13.221 -13.753  -6.808  1.00 31.79           C  
ANISOU  971  CA  TYR A 307     4202   3003   4873   -165    397   1013       C  
ATOM    972  C   TYR A 307     -11.697 -13.799  -6.803  1.00 34.61           C  
ANISOU  972  C   TYR A 307     4256   3640   5252     97    270    928       C  
ATOM    973  O   TYR A 307     -11.037 -12.804  -6.468  1.00 37.89           O  
ANISOU  973  O   TYR A 307     5082   2951   6364    -69    562   1387       O  
ATOM    974  CB  TYR A 307     -13.764 -12.728  -7.803  1.00 31.42           C  
ANISOU  974  CB  TYR A 307     4589   2521   4826     34    593    835       C  
ATOM    975  CG  TYR A 307     -13.623 -13.041  -9.269  1.00 32.80           C  
ANISOU  975  CG  TYR A 307     4945   2802   4713    345    899   1264       C  
ATOM    976  CD1 TYR A 307     -14.230 -14.167  -9.834  1.00 37.35           C  
ANISOU  976  CD1 TYR A 307     5572   3388   5229    -39    800    998       C  
ATOM    977  CD2 TYR A 307     -12.932 -12.172 -10.114  1.00 39.30           C  
ANISOU  977  CD2 TYR A 307     5540   3631   5761   -247   1365   1500       C  
ATOM    978  CE1 TYR A 307     -14.113 -14.439 -11.193  1.00 40.72           C  
ANISOU  978  CE1 TYR A 307     6548   3462   5460    335   1238    718       C  
ATOM    979  CE2 TYR A 307     -12.809 -12.433 -11.476  1.00 44.74           C  
ANISOU  979  CE2 TYR A 307     6795   4290   5915    387   1146   1042       C  
ATOM    980  CZ  TYR A 307     -13.404 -13.567 -12.010  1.00 44.74           C  
ANISOU  980  CZ  TYR A 307     6623   4260   6115    211   1657   1004       C  
ATOM    981  OH  TYR A 307     -13.288 -13.830 -13.356  1.00 52.44           O  
ANISOU  981  OH  TYR A 307     8247   5490   6188    312   1004    313       O  
ATOM    982  N   TYR A 308     -11.147 -14.972  -7.131  1.00 34.09           N  
ANISOU  982  N   TYR A 308     4026   3441   5483    -15    -70    966       N  
ATOM    983  CA  TYR A 308      -9.694 -15.214  -7.175  1.00 37.38           C  
ANISOU  983  CA  TYR A 308     4164   3893   6146    375    359   1355       C  
ATOM    984  C   TYR A 308      -8.967 -14.685  -5.935  1.00 39.73           C  
ANISOU  984  C   TYR A 308     4348   4532   6216     92    336   1377       C  
ATOM    985  O   TYR A 308      -7.981 -13.944  -6.059  1.00 43.61           O  
ANISOU  985  O   TYR A 308     4922   4819   6827   -281    572   1752       O  
ATOM    986  CB  TYR A 308      -9.054 -14.616  -8.445  1.00 42.23           C  
ANISOU  986  CB  TYR A 308     5249   4391   6403    337    662   1662       C  
ATOM    987  CG  TYR A 308      -9.361 -15.338  -9.736  1.00 46.74           C  
ANISOU  987  CG  TYR A 308     6173   4848   6736    323   1005   1196       C  
ATOM    988  CD1 TYR A 308      -8.803 -16.593 -10.014  1.00 49.70           C  
ANISOU  988  CD1 TYR A 308     6512   5139   7232    852   1206   1717       C  
ATOM    989  CD2 TYR A 308     -10.182 -14.751 -10.703  1.00 48.58           C  
ANISOU  989  CD2 TYR A 308     6301   4739   7417    701    938   1370       C  
ATOM    990  CE1 TYR A 308      -9.083 -17.257 -11.207  1.00 51.91           C  
ANISOU  990  CE1 TYR A 308     6821   5521   7380    356   1453   1549       C  
ATOM    991  CE2 TYR A 308     -10.461 -15.400 -11.902  1.00 50.11           C  
ANISOU  991  CE2 TYR A 308     6609   4986   7445    561   1232   1262       C  
ATOM    992  CZ  TYR A 308      -9.914 -16.650 -12.147  1.00 48.73           C  
ANISOU  992  CZ  TYR A 308     6475   5202   6836    498   1677   1015       C  
ATOM    993  OH  TYR A 308     -10.196 -17.291 -13.324  1.00 50.69           O  
ANISOU  993  OH  TYR A 308     7282   5721   6257  -1054   2795   1187       O  
ATOM    994  N   PHE A 309      -9.456 -15.061  -4.749  1.00 37.45           N  
ANISOU  994  N   PHE A 309     4268   3856   6103    218    -51   1707       N  
ATOM    995  CA  PHE A 309      -8.892 -14.571  -3.483  1.00 36.22           C  
ANISOU  995  CA  PHE A 309     3813   3802   6148   -102    -25   1603       C  
ATOM    996  C   PHE A 309      -7.426 -14.977  -3.242  1.00 41.64           C  
ANISOU  996  C   PHE A 309     3743   5127   6951    -70    -65   1334       C  
ATOM    997  O   PHE A 309      -6.714 -14.332  -2.464  1.00 45.91           O  
ANISOU  997  O   PHE A 309     4523   5424   7496   -695     94    997       O  
ATOM    998  CB  PHE A 309      -9.791 -14.943  -2.291  1.00 38.70           C  
ANISOU  998  CB  PHE A 309     4125   4734   5844   -252     56   1106       C  
ATOM    999  CG  PHE A 309      -9.934 -16.435  -2.042  1.00 41.12           C  
ANISOU  999  CG  PHE A 309     4529   4796   6299   -205   -178   1269       C  
ATOM   1000  CD1 PHE A 309      -8.973 -17.140  -1.302  1.00 43.96           C  
ANISOU 1000  CD1 PHE A 309     4705   5223   6773      0   -376   1298       C  
ATOM   1001  CD2 PHE A 309     -11.059 -17.129  -2.504  1.00 39.90           C  
ANISOU 1001  CD2 PHE A 309     4392   4743   6023    -63    154    963       C  
ATOM   1002  CE1 PHE A 309      -9.115 -18.505  -1.057  1.00 43.04           C  
ANISOU 1002  CE1 PHE A 309     4423   5210   6719   -138    -24   1014       C  
ATOM   1003  CE2 PHE A 309     -11.210 -18.493  -2.256  1.00 39.20           C  
ANISOU 1003  CE2 PHE A 309     4340   4758   5793    171   -154    933       C  
ATOM   1004  CZ  PHE A 309     -10.237 -19.181  -1.534  1.00 40.23           C  
ANISOU 1004  CZ  PHE A 309     4499   4835   5950     76   -223   1229       C  
ATOM   1005  N   TRP A 310      -6.994 -16.038  -3.928  1.00 42.89           N  
ANISOU 1005  N   TRP A 310     3991   5064   7238     22    137   1327       N  
ATOM   1006  CA  TRP A 310      -5.642 -16.589  -3.815  1.00 45.62           C  
ANISOU 1006  CA  TRP A 310     4056   5454   7824    164     88   1236       C  
ATOM   1007  C   TRP A 310      -4.629 -15.950  -4.776  1.00 49.72           C  
ANISOU 1007  C   TRP A 310     4328   5791   8770   -327    200   1405       C  
ATOM   1008  O   TRP A 310      -3.446 -16.287  -4.740  1.00 54.82           O  
ANISOU 1008  O   TRP A 310     4812   6403   9613    574   -146    873       O  
ATOM   1009  CB  TRP A 310      -5.692 -18.097  -4.066  1.00 46.59           C  
ANISOU 1009  CB  TRP A 310     4850   5381   7470    436   -181   1594       C  
ATOM   1010  CG  TRP A 310      -6.252 -18.452  -5.428  1.00 40.93           C  
ANISOU 1010  CG  TRP A 310     3873   4407   7269    457    324   1537       C  
ATOM   1011  CD1 TRP A 310      -5.550 -18.570  -6.601  1.00 39.38           C  
ANISOU 1011  CD1 TRP A 310     3702   3585   7673    846    703   1408       C  
ATOM   1012  CD2 TRP A 310      -7.627 -18.705  -5.753  1.00 38.03           C  
ANISOU 1012  CD2 TRP A 310     3607   4115   6726    793    479   1759       C  
ATOM   1013  NE1 TRP A 310      -6.404 -18.888  -7.634  1.00 38.53           N  
ANISOU 1013  NE1 TRP A 310     3535   3788   7314   1105   1026   1457       N  
ATOM   1014  CE2 TRP A 310      -7.683 -18.979  -7.145  1.00 37.78           C  
ANISOU 1014  CE2 TRP A 310     3434   3972   6945    867    832   1393       C  
ATOM   1015  CE3 TRP A 310      -8.819 -18.728  -5.005  1.00 36.98           C  
ANISOU 1015  CE3 TRP A 310     3881   4019   6149    696    466   1880       C  
ATOM   1016  CZ2 TRP A 310      -8.888 -19.279  -7.810  1.00 39.05           C  
ANISOU 1016  CZ2 TRP A 310     4088   4572   6177   1000    475   1309       C  
ATOM   1017  CZ3 TRP A 310     -10.030 -19.026  -5.668  1.00 37.32           C  
ANISOU 1017  CZ3 TRP A 310     3894   4033   6251   1005    474   1560       C  
ATOM   1018  CH2 TRP A 310     -10.048 -19.298  -7.060  1.00 39.36           C  
ANISOU 1018  CH2 TRP A 310     4023   4807   6121   1060    366   1811       C  
ATOM   1019  N   ASP A 311      -5.102 -15.055  -5.643  1.00 54.56           N  
ANISOU 1019  N   ASP A 311     5431   6342   8957   -401     43   1803       N  
ATOM   1020  CA  ASP A 311      -4.259 -14.349  -6.614  1.00 55.57           C  
ANISOU 1020  CA  ASP A 311     4805   6364   9944    -59    828   1707       C  
ATOM   1021  C   ASP A 311      -3.896 -12.976  -6.053  1.00 54.79           C  
ANISOU 1021  C   ASP A 311     4832   6645   9339   -624    811   1925       C  
ATOM   1022  O   ASP A 311      -4.777 -12.216  -5.644  1.00 57.64           O  
ANISOU 1022  O   ASP A 311     5249   6625  10025    -73     11   1645       O  
ATOM   1023  CB  ASP A 311      -5.006 -14.211  -7.948  1.00 58.27           C  
ANISOU 1023  CB  ASP A 311     6195   6353   9589   -457   1012   1797       C  
ATOM   1024  CG  ASP A 311      -4.106 -13.767  -9.097  1.00 63.55           C  
ANISOU 1024  CG  ASP A 311     6273   7490  10380    112   2112   1202       C  
ATOM   1025  OD1 ASP A 311      -3.552 -12.643  -9.062  1.00 61.53           O  
ANISOU 1025  OD1 ASP A 311     6119   7341   9917    328   1135   1898       O  
ATOM   1026  OD2 ASP A 311      -3.983 -14.544 -10.064  1.00 70.81           O  
ANISOU 1026  OD2 ASP A 311     8186   7711  11006    459   2389    771       O  
ATOM   1027  N   THR A 312      -2.600 -12.664  -6.051  1.00 58.46           N  
ANISOU 1027  N   THR A 312     4859   7010  10343   -618    863   1760       N  
ATOM   1028  CA  THR A 312      -2.079 -11.424  -5.445  1.00 60.76           C  
ANISOU 1028  CA  THR A 312     5018   7217  10850   -655    800   1425       C  
ATOM   1029  C   THR A 312      -2.518 -10.133  -6.149  1.00 62.09           C  
ANISOU 1029  C   THR A 312     5713   7158  10718   -696    971   1552       C  
ATOM   1030  O   THR A 312      -2.614  -9.087  -5.503  1.00 69.24           O  
ANISOU 1030  O   THR A 312     7459   7806  11042  -1162   1221    918       O  
ATOM   1031  CB  THR A 312      -0.542 -11.441  -5.297  1.00 63.11           C  
ANISOU 1031  CB  THR A 312     5090   7706  11183   -300    262   1539       C  
ATOM   1032  OG1 THR A 312       0.067 -11.659  -6.576  1.00 65.36           O  
ANISOU 1032  OG1 THR A 312     4992   8435  11406   -449    524   1900       O  
ATOM   1033  CG2 THR A 312      -0.104 -12.532  -4.320  1.00 61.38           C  
ANISOU 1033  CG2 THR A 312     4928   7190  11202   -683   -128   1313       C  
ATOM   1034  N   ASP A 313      -2.781 -10.211  -7.455  1.00 58.82           N  
ANISOU 1034  N   ASP A 313     4675   6865  10809   -521    776   1610       N  
ATOM   1035  CA  ASP A 313      -3.303  -9.071  -8.231  1.00 57.63           C  
ANISOU 1035  CA  ASP A 313     5338   5876  10683  -1062   1380   1579       C  
ATOM   1036  C   ASP A 313      -4.735  -8.694  -7.834  1.00 53.09           C  
ANISOU 1036  C   ASP A 313     5279   5428   9462  -1234   1241   1534       C  
ATOM   1037  O   ASP A 313      -5.100  -7.516  -7.854  1.00 60.94           O  
ANISOU 1037  O   ASP A 313     6880   5798  10475   -671   1067    653       O  
ATOM   1038  CB  ASP A 313      -3.241  -9.355  -9.739  1.00 63.04           C  
ANISOU 1038  CB  ASP A 313     6464   6817  10670   -827   1642   1675       C  
ATOM   1039  CG  ASP A 313      -1.817  -9.514 -10.260  1.00 67.90           C  
ANISOU 1039  CG  ASP A 313     6643   7047  12108   -200   1839   1131       C  
ATOM   1040  OD1 ASP A 313      -0.869  -8.976  -9.648  1.00 73.73           O  
ANISOU 1040  OD1 ASP A 313     7655   6639  13721   -923   1340    817       O  
ATOM   1041  OD2 ASP A 313      -1.649 -10.177 -11.304  1.00 74.06           O  
ANISOU 1041  OD2 ASP A 313     8203   6946  12988   1156    363    226       O  
ATOM   1042  N   TYR A 314      -5.534  -9.704  -7.491  1.00 45.98           N  
ANISOU 1042  N   TYR A 314     4375   4966   8130   -508   1160   1614       N  
ATOM   1043  CA  TYR A 314      -6.905  -9.518  -7.021  1.00 45.00           C  
ANISOU 1043  CA  TYR A 314     4332   4541   8224   -575   1050   1410       C  
ATOM   1044  C   TYR A 314      -6.937  -9.071  -5.555  1.00 47.72           C  
ANISOU 1044  C   TYR A 314     4744   5167   8218   -968    724   1271       C  
ATOM   1045  O   TYR A 314      -7.791  -8.266  -5.169  1.00 51.94           O  
ANISOU 1045  O   TYR A 314     4389   6227   9119   -941   1382   1424       O  
ATOM   1046  CB  TYR A 314      -7.722 -10.801  -7.239  1.00 44.97           C  
ANISOU 1046  CB  TYR A 314     4870   4475   7739   -556    674   1204       C  
ATOM   1047  CG  TYR A 314      -8.028 -11.080  -8.701  1.00 45.25           C  
ANISOU 1047  CG  TYR A 314     5164   4757   7270   -379   1277   1676       C  
ATOM   1048  CD1 TYR A 314      -7.024 -11.519  -9.588  1.00 45.80           C  
ANISOU 1048  CD1 TYR A 314     5344   4291   7768     -8   1464   1964       C  
ATOM   1049  CD2 TYR A 314      -9.323 -10.907  -9.203  1.00 44.86           C  
ANISOU 1049  CD2 TYR A 314     5004   4424   7616   -213   1484   1649       C  
ATOM   1050  CE1 TYR A 314      -7.306 -11.763 -10.932  1.00 51.92           C  
ANISOU 1050  CE1 TYR A 314     6424   5412   7891   -623   1666   1605       C  
ATOM   1051  CE2 TYR A 314      -9.617 -11.152 -10.542  1.00 48.87           C  
ANISOU 1051  CE2 TYR A 314     6231   4778   7556    -66   1529   1521       C  
ATOM   1052  CZ  TYR A 314      -8.612 -11.575 -11.404  1.00 54.08           C  
ANISOU 1052  CZ  TYR A 314     6434   5971   8140   -118   1796   1118       C  
ATOM   1053  OH  TYR A 314      -8.917 -11.813 -12.728  1.00 57.29           O  
ANISOU 1053  OH  TYR A 314     7811   6132   7825   -568   2101   1291       O  
ATOM   1054  N   GLN A 315      -6.000  -9.591  -4.757  1.00 49.23           N  
ANISOU 1054  N   GLN A 315     4480   5483   8738   -994    363    915       N  
ATOM   1055  CA  GLN A 315      -5.788  -9.161  -3.366  1.00 51.03           C  
ANISOU 1055  CA  GLN A 315     5128   5486   8772   -876    284    852       C  
ATOM   1056  C   GLN A 315      -5.450  -7.670  -3.294  1.00 52.82           C  
ANISOU 1056  C   GLN A 315     5242   5851   8975  -1816    426    959       C  
ATOM   1057  O   GLN A 315      -6.093  -6.930  -2.542  1.00 54.45           O  
ANISOU 1057  O   GLN A 315     5440   5145  10101  -1767    796   1244       O  
ATOM   1058  CB  GLN A 315      -4.675  -9.977  -2.700  1.00 51.27           C  
ANISOU 1058  CB  GLN A 315     4725   6250   8503  -1127    262   1281       C  
ATOM   1059  CG  GLN A 315      -5.023 -11.435  -2.440  1.00 52.29           C  
ANISOU 1059  CG  GLN A 315     4586   6145   9136   -936    242   1284       C  
ATOM   1060  CD  GLN A 315      -3.821 -12.299  -2.090  1.00 53.93           C  
ANISOU 1060  CD  GLN A 315     4772   6112   9605  -1062   -135   1793       C  
ATOM   1061  OE1 GLN A 315      -2.676 -11.841  -2.074  1.00 55.94           O  
ANISOU 1061  OE1 GLN A 315     5359   5801  10093  -1642  -1088   1903       O  
ATOM   1062  NE2 GLN A 315      -4.081 -13.567  -1.815  1.00 52.66           N  
ANISOU 1062  NE2 GLN A 315     4336   6301   9369  -1574     68   1741       N  
ATOM   1063  N   GLU A 316      -4.457  -7.248  -4.086  1.00 51.24           N  
ANISOU 1063  N   GLU A 316     4809   5671   8988  -1559    462    616       N  
ATOM   1064  CA  GLU A 316      -4.073  -5.833  -4.235  1.00 53.58           C  
ANISOU 1064  CA  GLU A 316     5215   5732   9408  -1757    533    664       C  
ATOM   1065  C   GLU A 316      -5.270  -4.955  -4.582  1.00 52.91           C  
ANISOU 1065  C   GLU A 316     5576   5196   9330  -1769    712    814       C  
ATOM   1066  O   GLU A 316      -5.438  -3.880  -4.004  1.00 60.80           O  
ANISOU 1066  O   GLU A 316     7423   5837   9841  -2042    758     57       O  
ATOM   1067  CB  GLU A 316      -2.995  -5.665  -5.310  1.00 61.35           C  
ANISOU 1067  CB  GLU A 316     5399   7086  10823  -2569   1245    744       C  
ATOM   1068  CG  GLU A 316      -1.576  -5.941  -4.836  1.00 74.91           C  
ANISOU 1068  CG  GLU A 316     6480   8941  13039  -1617    255   1379       C  
ATOM   1069  CD  GLU A 316      -0.537  -5.813  -5.945  1.00 84.94           C  
ANISOU 1069  CD  GLU A 316     8202   9950  14121  -1349   1509   1523       C  
ATOM   1070  OE1 GLU A 316       0.334  -6.706  -6.040  1.00 91.73           O  
ANISOU 1070  OE1 GLU A 316     9522   9713  15618   -716   1029   1417       O  
ATOM   1071  OE2 GLU A 316      -0.580  -4.827  -6.719  1.00 88.30           O  
ANISOU 1071  OE2 GLU A 316     9748  10287  13514   -246    829   1573       O  
ATOM   1072  N   GLY A 317      -6.094  -5.433  -5.518  1.00 50.35           N  
ANISOU 1072  N   GLY A 317     5088   5450   8592  -1552   1025   1070       N  
ATOM   1073  CA  GLY A 317      -7.315  -4.751  -5.943  1.00 50.72           C  
ANISOU 1073  CA  GLY A 317     5202   5300   8766  -1572    887   1116       C  
ATOM   1074  C   GLY A 317      -8.266  -4.478  -4.795  1.00 50.66           C  
ANISOU 1074  C   GLY A 317     5706   5126   8415  -1421    633    776       C  
ATOM   1075  O   GLY A 317      -8.771  -3.362  -4.657  1.00 53.92           O  
ANISOU 1075  O   GLY A 317     6897   4817   8772  -1241   -439   1303       O  
ATOM   1076  N   LEU A 318      -8.491  -5.494  -3.962  1.00 50.65           N  
ANISOU 1076  N   LEU A 318     5361   5586   8298  -1706    489    941       N  
ATOM   1077  CA  LEU A 318      -9.342  -5.357  -2.777  1.00 48.18           C  
ANISOU 1077  CA  LEU A 318     6123   4649   7532  -1429    183    903       C  
ATOM   1078  C   LEU A 318      -8.713  -4.457  -1.717  1.00 48.73           C  
ANISOU 1078  C   LEU A 318     5557   4635   8321  -2023    208    838       C  
ATOM   1079  O   LEU A 318      -9.420  -3.684  -1.064  1.00 55.11           O  
ANISOU 1079  O   LEU A 318     6970   5264   8702  -1477    686    799       O  
ATOM   1080  CB  LEU A 318      -9.693  -6.726  -2.180  1.00 43.65           C  
ANISOU 1080  CB  LEU A 318     4921   4295   7367  -1386    -12    553       C  
ATOM   1081  CG  LEU A 318     -10.508  -7.718  -3.009  1.00 41.98           C  
ANISOU 1081  CG  LEU A 318     4931   4164   6855  -1078   -105    623       C  
ATOM   1082  CD1 LEU A 318     -10.680  -9.017  -2.231  1.00 43.64           C  
ANISOU 1082  CD1 LEU A 318     5481   4360   6739  -1886   -125    619       C  
ATOM   1083  CD2 LEU A 318     -11.864  -7.153  -3.419  1.00 44.61           C  
ANISOU 1083  CD2 LEU A 318     5333   3946   7669   -419    -11    366       C  
ATOM   1084  N   ARG A 319      -7.392  -4.564  -1.562  1.00 48.25           N  
ANISOU 1084  N   ARG A 319     5446   4396   8488  -2104    446    783       N  
ATOM   1085  CA  ARG A 319      -6.623  -3.713  -0.649  1.00 54.80           C  
ANISOU 1085  CA  ARG A 319     5762   5569   9489  -2207    -81    228       C  
ATOM   1086  C   ARG A 319      -6.726  -2.230  -1.010  1.00 57.34           C  
ANISOU 1086  C   ARG A 319     6620   5576   9588  -2636    346    413       C  
ATOM   1087  O   ARG A 319      -6.958  -1.397  -0.131  1.00 65.62           O  
ANISOU 1087  O   ARG A 319     7714   6332  10886  -2820    888   -261       O  
ATOM   1088  CB  ARG A 319      -5.153  -4.142  -0.609  1.00 57.47           C  
ANISOU 1088  CB  ARG A 319     5672   6114  10048  -2122    221    688       C  
ATOM   1089  CG  ARG A 319      -4.896  -5.412   0.184  1.00 59.63           C  
ANISOU 1089  CG  ARG A 319     6262   6501   9892  -1850    -77    762       C  
ATOM   1090  CD  ARG A 319      -3.427  -5.815   0.164  1.00 63.20           C  
ANISOU 1090  CD  ARG A 319     5815   7541  10656  -2341  -1148   1009       C  
ATOM   1091  NE  ARG A 319      -2.582  -4.870   0.894  1.00 69.38           N  
ANISOU 1091  NE  ARG A 319     6573   7810  11977  -2442  -1326    403       N  
ATOM   1092  CZ  ARG A 319      -2.389  -4.870   2.214  1.00 74.21           C  
ANISOU 1092  CZ  ARG A 319     7344   8729  12124  -2885  -1327    697       C  
ATOM   1093  NH1 ARG A 319      -1.596  -3.954   2.758  1.00 80.25           N  
ANISOU 1093  NH1 ARG A 319     8198   8520  13772  -3207  -1416    254       N  
ATOM   1094  NH2 ARG A 319      -2.980  -5.773   2.996  1.00 71.49           N  
ANISOU 1094  NH2 ARG A 319     5665   8450  13046  -3291  -1011    199       N  
ATOM   1095  N   SER A 320      -6.572  -1.917  -2.298  1.00 54.93           N  
ANISOU 1095  N   SER A 320     6373   5263   9234  -2406    176     25       N  
ATOM   1096  CA  SER A 320      -6.638  -0.539  -2.792  1.00 60.71           C  
ANISOU 1096  CA  SER A 320     7702   5352  10012  -1942    129    162       C  
ATOM   1097  C   SER A 320      -8.037   0.053  -2.624  1.00 60.23           C  
ANISOU 1097  C   SER A 320     7368   5692   9823  -2219    396    298       C  
ATOM   1098  O   SER A 320      -8.175   1.232  -2.310  1.00 67.96           O  
ANISOU 1098  O   SER A 320     8688   5740  11392  -1755    859    406       O  
ATOM   1099  CB  SER A 320      -6.168  -0.448  -4.248  1.00 64.30           C  
ANISOU 1099  CB  SER A 320     8684   5161  10584  -2278    985    623       C  
ATOM   1100  OG  SER A 320      -7.061  -1.115  -5.122  1.00 67.59           O  
ANISOU 1100  OG  SER A 320     9023   6798   9857  -1566    864   -103       O  
ATOM   1101  N   LEU A 321      -9.061  -0.777  -2.818  1.00 57.31           N  
ANISOU 1101  N   LEU A 321     7089   5374   9311  -1909    628    392       N  
ATOM   1102  CA  LEU A 321     -10.451  -0.402  -2.552  1.00 55.87           C  
ANISOU 1102  CA  LEU A 321     7283   5048   8895  -1635    735    378       C  
ATOM   1103  C   LEU A 321     -10.664   0.036  -1.108  1.00 57.90           C  
ANISOU 1103  C   LEU A 321     7316   5895   8786  -1904    228    226       C  
ATOM   1104  O   LEU A 321     -11.264   1.086  -0.855  1.00 60.91           O  
ANISOU 1104  O   LEU A 321     7488   6039   9616  -1888     93     78       O  
ATOM   1105  CB  LEU A 321     -11.398  -1.556  -2.886  1.00 55.60           C  
ANISOU 1105  CB  LEU A 321     6862   5455   8809  -1683    701    351       C  
ATOM   1106  CG  LEU A 321     -12.192  -1.519  -4.190  1.00 57.11           C  
ANISOU 1106  CG  LEU A 321     7398   5470   8832  -1298    608     47       C  
ATOM   1107  CD1 LEU A 321     -12.977  -2.814  -4.326  1.00 56.59           C  
ANISOU 1107  CD1 LEU A 321     7332   5337   8832  -1219    906   -192       C  
ATOM   1108  CD2 LEU A 321     -13.131  -0.322  -4.229  1.00 55.88           C  
ANISOU 1108  CD2 LEU A 321     7543   4938   8751  -1511    984    428       C  
ATOM   1109  N   SER A 322     -10.153  -0.769  -0.176  1.00 56.82           N  
ANISOU 1109  N   SER A 322     7100   5526   8960  -2058     43    134       N  
ATOM   1110  CA  SER A 322     -10.224  -0.482   1.256  1.00 59.66           C  
ANISOU 1110  CA  SER A 322     7626   6000   9041  -2256    -29   -233       C  
ATOM   1111  C   SER A 322      -9.473   0.799   1.637  1.00 61.16           C  
ANISOU 1111  C   SER A 322     7896   6281   9058  -2511   -172   -366       C  
ATOM   1112  O   SER A 322      -9.989   1.614   2.405  1.00 64.69           O  
ANISOU 1112  O   SER A 322     9225   7318   8035  -2495  -1053  -1197       O  
ATOM   1113  CB  SER A 322      -9.707  -1.675   2.063  1.00 63.49           C  
ANISOU 1113  CB  SER A 322     7709   6759   9656  -1812   -509    129       C  
ATOM   1114  OG  SER A 322     -10.002  -1.523   3.440  1.00 69.62           O  
ANISOU 1114  OG  SER A 322     9312   7025  10115   -563    405    758       O  
ATOM   1115  N   GLN A 323      -8.280   0.977   1.071  1.00 63.29           N  
ANISOU 1115  N   GLN A 323     7519   6247  10278  -2580   -285   -229       N  
ATOM   1116  CA  GLN A 323      -7.426   2.145   1.341  1.00 71.66           C  
ANISOU 1116  CA  GLN A 323     8824   6782  11621  -3331   -267   -562       C  
ATOM   1117  C   GLN A 323      -7.982   3.478   0.817  1.00 70.02           C  
ANISOU 1117  C   GLN A 323     8563   6852  11187  -3202   -138   -855       C  
ATOM   1118  O   GLN A 323      -7.594   4.541   1.302  1.00 78.34           O  
ANISOU 1118  O   GLN A 323     9713   7025  13027  -4309    132   -815       O  
ATOM   1119  CB  GLN A 323      -6.011   1.906   0.803  1.00 80.65           C  
ANISOU 1119  CB  GLN A 323     9148   8479  13013  -2964    433    192       C  
ATOM   1120  CG  GLN A 323      -5.132   1.066   1.724  1.00 92.22           C  
ANISOU 1120  CG  GLN A 323    10377  10665  13998  -2323   -201    937       C  
ATOM   1121  CD  GLN A 323      -4.085   0.243   0.985  1.00 94.71           C  
ANISOU 1121  CD  GLN A 323    10122  10819  15041  -2427   -256    697       C  
ATOM   1122  OE1 GLN A 323      -3.444   0.714   0.041  1.00 95.82           O  
ANISOU 1122  OE1 GLN A 323     7562  13074  15768  -2328   -273   1068       O  
ATOM   1123  NE2 GLN A 323      -3.900  -0.997   1.424  1.00 98.31           N  
ANISOU 1123  NE2 GLN A 323    10602  10720  16028  -1937  -1738    437       N  
ATOM   1124  N   GLU A 324      -8.884   3.412  -0.161  1.00 69.35           N  
ANISOU 1124  N   GLU A 324     8951   6544  10854  -2894   -190   -534       N  
ATOM   1125  CA  GLU A 324      -9.544   4.603  -0.712  1.00 69.33           C  
ANISOU 1125  CA  GLU A 324     9516   5496  11327  -3550    388   -141       C  
ATOM   1126  C   GLU A 324     -10.921   4.881  -0.081  1.00 69.94           C  
ANISOU 1126  C   GLU A 324    10092   5899  10580  -2327    157   -435       C  
ATOM   1127  O   GLU A 324     -11.702   5.689  -0.604  1.00 67.52           O  
ANISOU 1127  O   GLU A 324    11768   4080   9806  -3433    297    833       O  
ATOM   1128  CB  GLU A 324      -9.645   4.515  -2.244  1.00 73.41           C  
ANISOU 1128  CB  GLU A 324    10448   5855  11589  -3914   -113   -469       C  
ATOM   1129  CG  GLU A 324      -8.307   4.512  -2.986  1.00 82.45           C  
ANISOU 1129  CG  GLU A 324    10555   7684  13087  -3117    162    338       C  
ATOM   1130  CD  GLU A 324      -7.595   5.855  -2.974  1.00 94.07           C  
ANISOU 1130  CD  GLU A 324    12471   8292  14979  -4145    234    704       C  
ATOM   1131  OE1 GLU A 324      -8.245   6.885  -3.262  1.00100.34           O  
ANISOU 1131  OE1 GLU A 324    13208   9354  15562  -3463   -700    707       O  
ATOM   1132  OE2 GLU A 324      -6.376   5.875  -2.687  1.00108.59           O  
ANISOU 1132  OE2 GLU A 324    12667  11413  17178  -2692   -348    831       O  
ATOM   1133  N   GLY A 325     -11.214   4.206   1.033  1.00 65.20           N  
ANISOU 1133  N   GLY A 325     9483   4914  10376  -2367   -364   -774       N  
ATOM   1134  CA  GLY A 325     -12.354   4.557   1.886  1.00 63.96           C  
ANISOU 1134  CA  GLY A 325     8976   5345   9978  -2871   -465   -539       C  
ATOM   1135  C   GLY A 325     -13.565   3.647   1.850  1.00 58.16           C  
ANISOU 1135  C   GLY A 325     8674   4532   8891  -2325    -82   -723       C  
ATOM   1136  O   GLY A 325     -14.437   3.752   2.714  1.00 63.92           O  
ANISOU 1136  O   GLY A 325     9108   5418   9758  -1653    574    422       O  
ATOM   1137  N   ALA A 326     -13.631   2.771   0.851  1.00 52.52           N  
ANISOU 1137  N   ALA A 326     7693   4027   8233  -2186   -593   -146       N  
ATOM   1138  CA  ALA A 326     -14.701   1.786   0.765  1.00 51.44           C  
ANISOU 1138  CA  ALA A 326     7412   4226   7905  -2092   -218   -591       C  
ATOM   1139  C   ALA A 326     -14.497   0.706   1.819  1.00 54.87           C  
ANISOU 1139  C   ALA A 326     8007   4469   8371  -1697   -439   -448       C  
ATOM   1140  O   ALA A 326     -13.398   0.170   1.956  1.00 61.09           O  
ANISOU 1140  O   ALA A 326     8204   5432   9574  -1339   -291   -297       O  
ATOM   1141  CB  ALA A 326     -14.764   1.174  -0.626  1.00 47.02           C  
ANISOU 1141  CB  ALA A 326     6655   3649   7559  -1774    -76   -218       C  
ATOM   1142  N   SER A 327     -15.544   0.419   2.587  1.00 54.22           N  
ANISOU 1142  N   SER A 327     7703   4580   8315  -2077   -776   -687       N  
ATOM   1143  CA  SER A 327     -15.514  -0.723   3.489  1.00 54.70           C  
ANISOU 1143  CA  SER A 327     7973   5199   7611  -1581   -990   -673       C  
ATOM   1144  C   SER A 327     -15.937  -1.968   2.711  1.00 54.77           C  
ANISOU 1144  C   SER A 327     7556   4854   8398  -1660  -1023   -537       C  
ATOM   1145  O   SER A 327     -17.041  -2.030   2.162  1.00 58.31           O  
ANISOU 1145  O   SER A 327     8449   5922   7781  -1488  -1691   -739       O  
ATOM   1146  CB  SER A 327     -16.378  -0.493   4.735  1.00 58.10           C  
ANISOU 1146  CB  SER A 327     8589   6439   7044  -1552  -1077   -832       C  
ATOM   1147  OG  SER A 327     -17.730  -0.267   4.400  1.00 57.74           O  
ANISOU 1147  OG  SER A 327     8814   6273   6850  -1250   -526   -495       O  
ATOM   1148  N   VAL A 328     -15.024  -2.932   2.637  1.00 49.32           N  
ANISOU 1148  N   VAL A 328     6735   4537   7465  -2174   -755   -563       N  
ATOM   1149  CA  VAL A 328     -15.267  -4.209   1.976  1.00 45.12           C  
ANISOU 1149  CA  VAL A 328     6324   4298   6521  -1557   -589   -364       C  
ATOM   1150  C   VAL A 328     -15.531  -5.273   3.044  1.00 44.88           C  
ANISOU 1150  C   VAL A 328     6276   4526   6248  -1594   -520   -345       C  
ATOM   1151  O   VAL A 328     -14.742  -5.428   3.982  1.00 46.76           O  
ANISOU 1151  O   VAL A 328     6984   4593   6187  -1762   -569    374       O  
ATOM   1152  CB  VAL A 328     -14.083  -4.626   1.069  1.00 46.76           C  
ANISOU 1152  CB  VAL A 328     6386   4524   6857  -1508   -366   -212       C  
ATOM   1153  CG1 VAL A 328     -14.440  -5.853   0.240  1.00 45.58           C  
ANISOU 1153  CG1 VAL A 328     6600   4010   6705   -908   -184   -157       C  
ATOM   1154  CG2 VAL A 328     -13.669  -3.482   0.152  1.00 49.47           C  
ANISOU 1154  CG2 VAL A 328     6910   4374   7512  -1184     80    -28       C  
ATOM   1155  N   GLU A 329     -16.649  -5.985   2.890  1.00 41.78           N  
ANISOU 1155  N   GLU A 329     6056   4324   5492  -1362   -550   -276       N  
ATOM   1156  CA  GLU A 329     -17.099  -7.015   3.833  1.00 42.28           C  
ANISOU 1156  CA  GLU A 329     6335   4307   5420  -1280   -824   -152       C  
ATOM   1157  C   GLU A 329     -17.697  -8.232   3.122  1.00 40.56           C  
ANISOU 1157  C   GLU A 329     6136   4075   5199   -948   -394   -286       C  
ATOM   1158  O   GLU A 329     -18.133  -8.145   1.971  1.00 43.62           O  
ANISOU 1158  O   GLU A 329     6420   4965   5187   -569   -381   -149       O  
ATOM   1159  CB  GLU A 329     -18.147  -6.440   4.791  1.00 46.68           C  
ANISOU 1159  CB  GLU A 329     7019   5014   5701  -1163   -366   -313       C  
ATOM   1160  CG  GLU A 329     -17.590  -5.566   5.899  1.00 59.11           C  
ANISOU 1160  CG  GLU A 329     9252   5971   7237  -1577   -835  -1287       C  
ATOM   1161  CD  GLU A 329     -18.684  -4.836   6.651  1.00 74.83           C  
ANISOU 1161  CD  GLU A 329    10757   8019   9655   -256    313  -1137       C  
ATOM   1162  OE1 GLU A 329     -18.988  -3.682   6.271  1.00 88.51           O  
ANISOU 1162  OE1 GLU A 329    12813   9063  11754    569    -18    179       O  
ATOM   1163  OE2 GLU A 329     -19.246  -5.419   7.608  1.00 77.27           O  
ANISOU 1163  OE2 GLU A 329    13040   5819  10497   -343   -202     98       O  
ATOM   1164  N   ILE A 330     -17.722  -9.359   3.826  1.00 40.18           N  
ANISOU 1164  N   ILE A 330     5894   4266   5106   -873   -614   -166       N  
ATOM   1165  CA  ILE A 330     -18.412 -10.555   3.361  1.00 39.40           C  
ANISOU 1165  CA  ILE A 330     5738   3947   5282   -825   -210      4       C  
ATOM   1166  C   ILE A 330     -19.893 -10.454   3.745  1.00 35.53           C  
ANISOU 1166  C   ILE A 330     5695   3313   4490   -651   -460    102       C  
ATOM   1167  O   ILE A 330     -20.220 -10.018   4.850  1.00 38.68           O  
ANISOU 1167  O   ILE A 330     6859   3147   4691  -1078     56     59       O  
ATOM   1168  CB  ILE A 330     -17.755 -11.846   3.936  1.00 38.93           C  
ANISOU 1168  CB  ILE A 330     5423   4078   5291   -909   -321     28       C  
ATOM   1169  CG1 ILE A 330     -16.233 -11.880   3.656  1.00 39.56           C  
ANISOU 1169  CG1 ILE A 330     5413   4497   5119   -823   -532     15       C  
ATOM   1170  CG2 ILE A 330     -18.440 -13.110   3.420  1.00 35.32           C  
ANISOU 1170  CG2 ILE A 330     5212   3292   4913   -691    533    261       C  
ATOM   1171  CD1 ILE A 330     -15.796 -11.851   2.196  1.00 38.01           C  
ANISOU 1171  CD1 ILE A 330     5003   3951   5485  -1164     91    191       C  
ATOM   1172  N   MET A 331     -20.776 -10.833   2.821  1.00 33.42           N  
ANISOU 1172  N   MET A 331     5287   3144   4266   -756   -221    356       N  
ATOM   1173  CA  MET A 331     -22.206 -10.926   3.099  1.00 31.77           C  
ANISOU 1173  CA  MET A 331     5179   3194   3696   -695   -361     42       C  
ATOM   1174  C   MET A 331     -22.438 -12.036   4.125  1.00 32.30           C  
ANISOU 1174  C   MET A 331     5347   3325   3600   -431   -410    100       C  
ATOM   1175  O   MET A 331     -21.954 -13.162   3.961  1.00 32.47           O  
ANISOU 1175  O   MET A 331     5104   3431   3799   -153   -965    610       O  
ATOM   1176  CB  MET A 331     -23.006 -11.226   1.825  1.00 29.12           C  
ANISOU 1176  CB  MET A 331     5058   2693   3313   -680   -180    361       C  
ATOM   1177  CG  MET A 331     -23.110 -10.087   0.810  1.00 23.83           C  
ANISOU 1177  CG  MET A 331     4302   1997   2754   -495   -688   -308       C  
ATOM   1178  SD  MET A 331     -24.025 -10.507  -0.697  1.00 16.32           S  
ANISOU 1178  SD  MET A 331     3216   1043   1942   -403    -43    245       S  
ATOM   1179  CE  MET A 331     -25.691 -10.463  -0.071  1.00 18.56           C  
ANISOU 1179  CE  MET A 331     3452   1364   2236   -310    212    182       C  
ATOM   1180  N   GLY A 332     -23.143 -11.695   5.199  1.00 32.37           N  
ANISOU 1180  N   GLY A 332     5157   3442   3698   -259   -407    149       N  
ATOM   1181  CA  GLY A 332     -23.611 -12.669   6.182  1.00 34.07           C  
ANISOU 1181  CA  GLY A 332     5439   3763   3741   -336   -291    208       C  
ATOM   1182  C   GLY A 332     -25.116 -12.834   6.079  1.00 33.12           C  
ANISOU 1182  C   GLY A 332     5469   3590   3525   -562     90    157       C  
ATOM   1183  O   GLY A 332     -25.760 -12.256   5.187  1.00 34.73           O  
ANISOU 1183  O   GLY A 332     5545   3666   3985   -316   -191     64       O  
ATOM   1184  N   TYR A 333     -25.675 -13.610   7.001  1.00 30.18           N  
ANISOU 1184  N   TYR A 333     5031   3249   3184   -189    136    -28       N  
ATOM   1185  CA  TYR A 333     -27.111 -13.884   7.035  1.00 29.67           C  
ANISOU 1185  CA  TYR A 333     5042   3387   2842   -121    146     72       C  
ATOM   1186  C   TYR A 333     -27.976 -12.641   6.785  1.00 30.89           C  
ANISOU 1186  C   TYR A 333     5371   3270   3096    -65    141     24       C  
ATOM   1187  O   TYR A 333     -28.786 -12.636   5.861  1.00 31.20           O  
ANISOU 1187  O   TYR A 333     5589   3080   3186   -267     99   -619       O  
ATOM   1188  CB  TYR A 333     -27.515 -14.577   8.350  1.00 28.78           C  
ANISOU 1188  CB  TYR A 333     4873   3276   2783     61    273     25       C  
ATOM   1189  CG  TYR A 333     -29.014 -14.730   8.497  1.00 31.44           C  
ANISOU 1189  CG  TYR A 333     4905   3778   3260    -41    286    310       C  
ATOM   1190  CD1 TYR A 333     -29.695 -15.772   7.851  1.00 31.15           C  
ANISOU 1190  CD1 TYR A 333     5009   3349   3475    101    284    462       C  
ATOM   1191  CD2 TYR A 333     -29.764 -13.815   9.260  1.00 32.27           C  
ANISOU 1191  CD2 TYR A 333     5222   3747   3292     25    250    222       C  
ATOM   1192  CE1 TYR A 333     -31.075 -15.908   7.968  1.00 32.95           C  
ANISOU 1192  CE1 TYR A 333     5035   3699   3785   -111    383    663       C  
ATOM   1193  CE2 TYR A 333     -31.144 -13.945   9.382  1.00 34.89           C  
ANISOU 1193  CE2 TYR A 333     5191   4118   3946    314    305    300       C  
ATOM   1194  CZ  TYR A 333     -31.790 -14.992   8.735  1.00 36.15           C  
ANISOU 1194  CZ  TYR A 333     5406   4062   4266     53    490    319       C  
ATOM   1195  OH  TYR A 333     -33.149 -15.130   8.851  1.00 39.53           O  
ANISOU 1195  OH  TYR A 333     5373   4798   4847     62    100    657       O  
ATOM   1196  N   LYS A 334     -27.787 -11.600   7.599  1.00 33.01           N  
ANISOU 1196  N   LYS A 334     5603   3398   3538   -280    169   -149       N  
ATOM   1197  CA  LYS A 334     -28.586 -10.364   7.521  1.00 34.40           C  
ANISOU 1197  CA  LYS A 334     6030   3522   3518    -32    151   -169       C  
ATOM   1198  C   LYS A 334     -28.530  -9.702   6.139  1.00 31.99           C  
ANISOU 1198  C   LYS A 334     5471   3546   3134    -56   -104   -537       C  
ATOM   1199  O   LYS A 334     -29.495  -9.076   5.715  1.00 36.33           O  
ANISOU 1199  O   LYS A 334     5876   3789   4136    242     -7   -155       O  
ATOM   1200  CB  LYS A 334     -28.172  -9.360   8.621  1.00 39.60           C  
ANISOU 1200  CB  LYS A 334     6499   4426   4119   -328    -97   -749       C  
ATOM   1201  CG  LYS A 334     -26.739  -8.841   8.508  1.00 46.83           C  
ANISOU 1201  CG  LYS A 334     7042   5246   5504  -1071   -149   -781       C  
ATOM   1202  CD  LYS A 334     -26.451  -7.655   9.418  1.00 51.31           C  
ANISOU 1202  CD  LYS A 334     8243   6124   5129  -1773   -598   -928       C  
ATOM   1203  CE  LYS A 334     -24.961  -7.327   9.427  1.00 56.24           C  
ANISOU 1203  CE  LYS A 334     8555   7490   5322  -2193   -782  -1075       C  
ATOM   1204  NZ  LYS A 334     -24.381  -6.992   8.090  1.00 60.81           N  
ANISOU 1204  NZ  LYS A 334     9274   7766   6064  -4066   -644   -247       N  
ATOM   1205  N   ASP A 335     -27.400  -9.863   5.450  1.00 29.87           N  
ANISOU 1205  N   ASP A 335     5064   3192   3090   -432   -336   -260       N  
ATOM   1206  CA  ASP A 335     -27.174  -9.273   4.135  1.00 30.46           C  
ANISOU 1206  CA  ASP A 335     5220   3176   3175   -226   -219   -181       C  
ATOM   1207  C   ASP A 335     -27.883 -10.074   3.039  1.00 29.77           C  
ANISOU 1207  C   ASP A 335     5311   2712   3288   -175     22   -316       C  
ATOM   1208  O   ASP A 335     -28.509  -9.483   2.150  1.00 30.20           O  
ANISOU 1208  O   ASP A 335     5652   2439   3382   -175    -66   -263       O  
ATOM   1209  CB  ASP A 335     -25.675  -9.120   3.853  1.00 31.62           C  
ANISOU 1209  CB  ASP A 335     5325   3142   3546   -394      3   -134       C  
ATOM   1210  CG  ASP A 335     -24.919  -8.467   5.017  1.00 36.40           C  
ANISOU 1210  CG  ASP A 335     6173   3636   4020   -573   -157   -554       C  
ATOM   1211  OD1 ASP A 335     -25.236  -7.314   5.396  1.00 37.50           O  
ANISOU 1211  OD1 ASP A 335     6582   3774   3891   -200    135   -586       O  
ATOM   1212  OD2 ASP A 335     -23.998  -9.117   5.560  1.00 42.25           O  
ANISOU 1212  OD2 ASP A 335     6483   4435   5134   -431   -358     58       O  
ATOM   1213  N   PHE A 336     -27.806 -11.408   3.111  1.00 28.96           N  
ANISOU 1213  N   PHE A 336     4755   2669   3580   -443    253   -279       N  
ATOM   1214  CA  PHE A 336     -28.566 -12.270   2.193  1.00 26.88           C  
ANISOU 1214  CA  PHE A 336     4624   2305   3284   -154    187   -106       C  
ATOM   1215  C   PHE A 336     -30.075 -12.067   2.373  1.00 27.17           C  
ANISOU 1215  C   PHE A 336     4641   2522   3161   -102     59     20       C  
ATOM   1216  O   PHE A 336     -30.819 -12.017   1.396  1.00 28.61           O  
ANISOU 1216  O   PHE A 336     4953   2688   3229     31    -48   -196       O  
ATOM   1217  CB  PHE A 336     -28.197 -13.749   2.377  1.00 25.93           C  
ANISOU 1217  CB  PHE A 336     4346   2198   3306   -386    165    -53       C  
ATOM   1218  CG  PHE A 336     -26.786 -14.092   1.966  1.00 25.77           C  
ANISOU 1218  CG  PHE A 336     4403   2284   3102   -275    111    148       C  
ATOM   1219  CD1 PHE A 336     -26.400 -14.054   0.625  1.00 25.45           C  
ANISOU 1219  CD1 PHE A 336     4434   2137   3096   -237    164     13       C  
ATOM   1220  CD2 PHE A 336     -25.842 -14.478   2.923  1.00 26.04           C  
ANISOU 1220  CD2 PHE A 336     4359   2322   3210   -282     37    112       C  
ATOM   1221  CE1 PHE A 336     -25.095 -14.372   0.254  1.00 24.16           C  
ANISOU 1221  CE1 PHE A 336     4181   1775   3223   -469    -43    212       C  
ATOM   1222  CE2 PHE A 336     -24.540 -14.798   2.557  1.00 24.86           C  
ANISOU 1222  CE2 PHE A 336     4377   1993   3075   -473    147     49       C  
ATOM   1223  CZ  PHE A 336     -24.164 -14.745   1.218  1.00 23.96           C  
ANISOU 1223  CZ  PHE A 336     4533   1618   2951   -455    -64    175       C  
ATOM   1224  N   LYS A 337     -30.509 -11.933   3.625  1.00 27.61           N  
ANISOU 1224  N   LYS A 337     4896   2290   3302    144    249   -116       N  
ATOM   1225  CA  LYS A 337     -31.910 -11.688   3.962  1.00 31.69           C  
ANISOU 1225  CA  LYS A 337     5000   3138   3900    202    328    148       C  
ATOM   1226  C   LYS A 337     -32.386 -10.341   3.398  1.00 31.60           C  
ANISOU 1226  C   LYS A 337     5076   2911   4016   -255    277    223       C  
ATOM   1227  O   LYS A 337     -33.456 -10.260   2.777  1.00 30.91           O  
ANISOU 1227  O   LYS A 337     5084   2564   4096    -75    274    193       O  
ATOM   1228  CB  LYS A 337     -32.095 -11.747   5.481  1.00 33.89           C  
ANISOU 1228  CB  LYS A 337     5842   3178   3856    125    412    231       C  
ATOM   1229  CG  LYS A 337     -33.506 -11.505   5.985  1.00 37.32           C  
ANISOU 1229  CG  LYS A 337     5822   3791   4564    169    478   -204       C  
ATOM   1230  CD  LYS A 337     -33.618 -11.975   7.432  1.00 46.86           C  
ANISOU 1230  CD  LYS A 337     7519   5487   4795    347    617    290       C  
ATOM   1231  CE  LYS A 337     -34.443 -11.025   8.289  1.00 51.94           C  
ANISOU 1231  CE  LYS A 337     7499   6941   5292    797    883     87       C  
ATOM   1232  NZ  LYS A 337     -35.869 -10.964   7.875  1.00 51.95           N  
ANISOU 1232  NZ  LYS A 337     7270   7449   5019    192   1014    -35       N  
ATOM   1233  N   TYR A 338     -31.578  -9.303   3.602  1.00 28.55           N  
ANISOU 1233  N   TYR A 338     5260   2214   3371    133    475   -381       N  
ATOM   1234  CA  TYR A 338     -31.853  -7.995   3.023  1.00 29.79           C  
ANISOU 1234  CA  TYR A 338     5355   2528   3435     80    217    -69       C  
ATOM   1235  C   TYR A 338     -32.044  -8.052   1.492  1.00 30.10           C  
ANISOU 1235  C   TYR A 338     5460   2464   3513    -51    150   -362       C  
ATOM   1236  O   TYR A 338     -33.028  -7.507   0.967  1.00 32.59           O  
ANISOU 1236  O   TYR A 338     5713   2310   4359     43     82   -314       O  
ATOM   1237  CB  TYR A 338     -30.768  -6.975   3.418  1.00 31.74           C  
ANISOU 1237  CB  TYR A 338     5695   2646   3717    -61    208   -492       C  
ATOM   1238  CG  TYR A 338     -31.105  -5.581   2.966  1.00 34.82           C  
ANISOU 1238  CG  TYR A 338     6137   2838   4255     19     54   -277       C  
ATOM   1239  CD1 TYR A 338     -31.880  -4.728   3.773  1.00 38.02           C  
ANISOU 1239  CD1 TYR A 338     6382   3477   4587    258    224   -453       C  
ATOM   1240  CD2 TYR A 338     -30.674  -5.111   1.715  1.00 35.21           C  
ANISOU 1240  CD2 TYR A 338     5679   3448   4250      9    184   -351       C  
ATOM   1241  CE1 TYR A 338     -32.203  -3.442   3.350  1.00 40.13           C  
ANISOU 1241  CE1 TYR A 338     6960   3274   5013    302    176   -642       C  
ATOM   1242  CE2 TYR A 338     -30.993  -3.829   1.283  1.00 39.27           C  
ANISOU 1242  CE2 TYR A 338     6330   3446   5143    -22    311    -80       C  
ATOM   1243  CZ  TYR A 338     -31.759  -2.999   2.104  1.00 42.89           C  
ANISOU 1243  CZ  TYR A 338     7379   3649   5267     57    386   -547       C  
ATOM   1244  OH  TYR A 338     -32.081  -1.730   1.672  1.00 47.90           O  
ANISOU 1244  OH  TYR A 338     7533   3965   6699   -491   -228    463       O  
ATOM   1245  N   CYS A 339     -31.123  -8.714   0.789  1.00 28.25           N  
ANISOU 1245  N   CYS A 339     5082   2153   3496   -113    124     30       N  
ATOM   1246  CA  CYS A 339     -31.206  -8.852  -0.672  1.00 29.57           C  
ANISOU 1246  CA  CYS A 339     5197   2509   3529   -122    166    -92       C  
ATOM   1247  C   CYS A 339     -32.430  -9.620  -1.145  1.00 28.89           C  
ANISOU 1247  C   CYS A 339     4971   2396   3609    -18    243    185       C  
ATOM   1248  O   CYS A 339     -33.057  -9.247  -2.150  1.00 31.18           O  
ANISOU 1248  O   CYS A 339     5042   2876   3926     85      1    234       O  
ATOM   1249  CB  CYS A 339     -29.947  -9.493  -1.232  1.00 33.68           C  
ANISOU 1249  CB  CYS A 339     5187   3121   4489    528     73    447       C  
ATOM   1250  SG  CYS A 339     -28.549  -8.380  -1.083  1.00 39.72           S  
ANISOU 1250  SG  CYS A 339     6187   3464   5441      2    538    397       S  
ATOM   1251  N   TRP A 340     -32.752 -10.693  -0.420  1.00 26.16           N  
ANISOU 1251  N   TRP A 340     4458   2098   3382    -43    226    -82       N  
ATOM   1252  CA  TRP A 340     -33.951 -11.480  -0.677  1.00 25.84           C  
ANISOU 1252  CA  TRP A 340     4294   2207   3317     34    166    195       C  
ATOM   1253  C   TRP A 340     -35.189 -10.580  -0.618  1.00 27.63           C  
ANISOU 1253  C   TRP A 340     4516   2409   3571    252    111    129       C  
ATOM   1254  O   TRP A 340     -36.071 -10.662  -1.484  1.00 28.29           O  
ANISOU 1254  O   TRP A 340     4653   2588   3508    474     19     33       O  
ATOM   1255  CB  TRP A 340     -34.053 -12.651   0.318  1.00 24.70           C  
ANISOU 1255  CB  TRP A 340     4080   1942   3361     -1     49     95       C  
ATOM   1256  CG  TRP A 340     -35.303 -13.466   0.158  1.00 26.36           C  
ANISOU 1256  CG  TRP A 340     4204   2144   3667   -131     -9    279       C  
ATOM   1257  CD1 TRP A 340     -36.456 -13.350   0.889  1.00 27.07           C  
ANISOU 1257  CD1 TRP A 340     4087   2264   3933    -85     16    400       C  
ATOM   1258  CD2 TRP A 340     -35.533 -14.516  -0.793  1.00 25.63           C  
ANISOU 1258  CD2 TRP A 340     3995   2286   3457    -73   -300    274       C  
ATOM   1259  NE1 TRP A 340     -37.385 -14.267   0.456  1.00 26.70           N  
ANISOU 1259  NE1 TRP A 340     4240   2238   3666    -57   -130    257       N  
ATOM   1260  CE2 TRP A 340     -36.848 -14.997  -0.572  1.00 26.57           C  
ANISOU 1260  CE2 TRP A 340     4105   2330   3660   -147   -140    202       C  
ATOM   1261  CE3 TRP A 340     -34.754 -15.102  -1.808  1.00 25.68           C  
ANISOU 1261  CE3 TRP A 340     4131   2274   3352    -68   -362    255       C  
ATOM   1262  CZ2 TRP A 340     -37.418 -16.041  -1.341  1.00 25.94           C  
ANISOU 1262  CZ2 TRP A 340     3920   1905   4029    -11   -116    264       C  
ATOM   1263  CZ3 TRP A 340     -35.314 -16.145  -2.574  1.00 25.23           C  
ANISOU 1263  CZ3 TRP A 340     3974   1939   3672   -208    -28    314       C  
ATOM   1264  CH2 TRP A 340     -36.640 -16.596  -2.333  1.00 25.03           C  
ANISOU 1264  CH2 TRP A 340     4017   1769   3721   -308   -182    203       C  
ATOM   1265  N   GLU A 341     -35.218  -9.703   0.387  1.00 28.51           N  
ANISOU 1265  N   GLU A 341     4832   2426   3573     48    464    139       N  
ATOM   1266  CA  GLU A 341     -36.361  -8.824   0.629  1.00 31.18           C  
ANISOU 1266  CA  GLU A 341     5186   2830   3831    397    550    151       C  
ATOM   1267  C   GLU A 341     -36.497  -7.678  -0.367  1.00 31.95           C  
ANISOU 1267  C   GLU A 341     5324   3126   3689    400    210    224       C  
ATOM   1268  O   GLU A 341     -37.611  -7.237  -0.629  1.00 33.67           O  
ANISOU 1268  O   GLU A 341     5391   3561   3840    506    185    179       O  
ATOM   1269  CB  GLU A 341     -36.333  -8.291   2.065  1.00 33.23           C  
ANISOU 1269  CB  GLU A 341     5692   3013   3919    279    268    -95       C  
ATOM   1270  CG  GLU A 341     -36.743  -9.347   3.085  1.00 40.52           C  
ANISOU 1270  CG  GLU A 341     6272   4337   4784   -243    918    525       C  
ATOM   1271  CD  GLU A 341     -36.288  -9.056   4.507  1.00 49.66           C  
ANISOU 1271  CD  GLU A 341     7529   5876   5463     20   -117    423       C  
ATOM   1272  OE1 GLU A 341     -35.653  -8.007   4.762  1.00 51.30           O  
ANISOU 1272  OE1 GLU A 341     8705   4656   6131    234    517   1068       O  
ATOM   1273  OE2 GLU A 341     -36.571  -9.899   5.387  1.00 56.42           O  
ANISOU 1273  OE2 GLU A 341     8663   6246   6527    198     74   1178       O  
ATOM   1274  N   ASN A 342     -35.374  -7.217  -0.926  1.00 32.33           N  
ANISOU 1274  N   ASN A 342     5780   2971   3534    104    358     31       N  
ATOM   1275  CA  ASN A 342     -35.339  -5.969  -1.714  1.00 32.25           C  
ANISOU 1275  CA  ASN A 342     5765   2693   3793    321    224    -71       C  
ATOM   1276  C   ASN A 342     -35.025  -6.088  -3.209  1.00 31.35           C  
ANISOU 1276  C   ASN A 342     5579   2506   3825    426    274     65       C  
ATOM   1277  O   ASN A 342     -35.339  -5.168  -3.979  1.00 32.41           O  
ANISOU 1277  O   ASN A 342     5548   2713   4052    418    532    367       O  
ATOM   1278  CB  ASN A 342     -34.371  -4.974  -1.065  1.00 32.26           C  
ANISOU 1278  CB  ASN A 342     5999   2431   3826    383    276   -152       C  
ATOM   1279  CG  ASN A 342     -34.889  -4.447   0.250  1.00 33.51           C  
ANISOU 1279  CG  ASN A 342     6433   2453   3846    446   -201   -667       C  
ATOM   1280  OD1 ASN A 342     -35.742  -3.566   0.276  1.00 42.88           O  
ANISOU 1280  OD1 ASN A 342     6825   3703   5762   1173   -171   -898       O  
ATOM   1281  ND2 ASN A 342     -34.388  -4.991   1.350  1.00 30.12           N  
ANISOU 1281  ND2 ASN A 342     6461   1247   3737    618    386   -612       N  
ATOM   1282  N   PHE A 343     -34.416  -7.202  -3.618  1.00 28.15           N  
ANISOU 1282  N   PHE A 343     4822   2349   3523    261    245    266       N  
ATOM   1283  CA  PHE A 343     -33.940  -7.350  -5.000  1.00 28.66           C  
ANISOU 1283  CA  PHE A 343     5079   2306   3504    228    159    140       C  
ATOM   1284  C   PHE A 343     -34.454  -8.603  -5.702  1.00 30.44           C  
ANISOU 1284  C   PHE A 343     5131   2525   3910      1     -3     97       C  
ATOM   1285  O   PHE A 343     -34.046  -8.909  -6.827  1.00 33.23           O  
ANISOU 1285  O   PHE A 343     5738   3018   3869    277    106    209       O  
ATOM   1286  CB  PHE A 343     -32.404  -7.299  -5.048  1.00 26.21           C  
ANISOU 1286  CB  PHE A 343     5023   1740   3195     60    286    124       C  
ATOM   1287  CG  PHE A 343     -31.816  -6.111  -4.342  1.00 27.79           C  
ANISOU 1287  CG  PHE A 343     5404   1683   3471     90    253      6       C  
ATOM   1288  CD1 PHE A 343     -31.967  -4.822  -4.861  1.00 27.23           C  
ANISOU 1288  CD1 PHE A 343     5256   1606   3483    322    340   -119       C  
ATOM   1289  CD2 PHE A 343     -31.112  -6.278  -3.147  1.00 29.94           C  
ANISOU 1289  CD2 PHE A 343     5602   2175   3599    318    147     -7       C  
ATOM   1290  CE1 PHE A 343     -31.424  -3.725  -4.198  1.00 30.24           C  
ANISOU 1290  CE1 PHE A 343     5468   2083   3938    -28    171   -263       C  
ATOM   1291  CE2 PHE A 343     -30.562  -5.185  -2.482  1.00 32.12           C  
ANISOU 1291  CE2 PHE A 343     5774   2686   3742   -153     90    -37       C  
ATOM   1292  CZ  PHE A 343     -30.722  -3.906  -3.006  1.00 32.33           C  
ANISOU 1292  CZ  PHE A 343     5710   2603   3968   -210    104    -21       C  
ATOM   1293  N   VAL A 344     -35.343  -9.323  -5.025  1.00 27.74           N  
ANISOU 1293  N   VAL A 344     4775   2131   3633    183   -228     90       N  
ATOM   1294  CA  VAL A 344     -35.854 -10.598  -5.502  1.00 25.46           C  
ANISOU 1294  CA  VAL A 344     4403   2075   3196    308   -280    167       C  
ATOM   1295  C   VAL A 344     -37.373 -10.530  -5.546  1.00 27.55           C  
ANISOU 1295  C   VAL A 344     4410   2570   3487    340   -388    124       C  
ATOM   1296  O   VAL A 344     -38.000  -9.898  -4.695  1.00 29.46           O  
ANISOU 1296  O   VAL A 344     4846   2557   3791    684   -227    157       O  
ATOM   1297  CB  VAL A 344     -35.386 -11.767  -4.590  1.00 23.80           C  
ANISOU 1297  CB  VAL A 344     4067   1827   3149    103   -409     20       C  
ATOM   1298  CG1 VAL A 344     -35.945 -13.114  -5.040  1.00 23.43           C  
ANISOU 1298  CG1 VAL A 344     4050   1661   3188    -60    -30    245       C  
ATOM   1299  CG2 VAL A 344     -33.869 -11.826  -4.545  1.00 21.77           C  
ANISOU 1299  CG2 VAL A 344     4004   1591   2676    424   -264   -193       C  
ATOM   1300  N   TYR A 345     -37.957 -11.172  -6.550  1.00 28.43           N  
ANISOU 1300  N   TYR A 345     4553   2537   3710    139   -310    -34       N  
ATOM   1301  CA  TYR A 345     -39.390 -11.414  -6.568  1.00 31.59           C  
ANISOU 1301  CA  TYR A 345     4553   3111   4338    301   -598    290       C  
ATOM   1302  C   TYR A 345     -39.709 -12.542  -5.582  1.00 33.73           C  
ANISOU 1302  C   TYR A 345     4915   3373   4527      2   -522    395       C  
ATOM   1303  O   TYR A 345     -39.974 -13.682  -5.983  1.00 36.67           O  
ANISOU 1303  O   TYR A 345     5224   3545   5160    357   -671   -165       O  
ATOM   1304  CB  TYR A 345     -39.848 -11.785  -7.974  1.00 33.18           C  
ANISOU 1304  CB  TYR A 345     4763   3378   4465    465   -903    277       C  
ATOM   1305  CG  TYR A 345     -39.738 -10.681  -9.003  1.00 36.26           C  
ANISOU 1305  CG  TYR A 345     5425   3692   4660    539  -1044    520       C  
ATOM   1306  CD1 TYR A 345     -40.523  -9.521  -8.904  1.00 36.62           C  
ANISOU 1306  CD1 TYR A 345     6062   3291   4561    466  -1099    161       C  
ATOM   1307  CD2 TYR A 345     -38.880 -10.812 -10.107  1.00 37.35           C  
ANISOU 1307  CD2 TYR A 345     5337   4052   4802    288   -986    401       C  
ATOM   1308  CE1 TYR A 345     -40.442  -8.522  -9.864  1.00 38.48           C  
ANISOU 1308  CE1 TYR A 345     6388   3016   5216    -16   -761    259       C  
ATOM   1309  CE2 TYR A 345     -38.794  -9.812 -11.070  1.00 38.30           C  
ANISOU 1309  CE2 TYR A 345     5847   3911   4794    142   -610    286       C  
ATOM   1310  CZ  TYR A 345     -39.578  -8.678 -10.941  1.00 41.08           C  
ANISOU 1310  CZ  TYR A 345     6177   3823   5606    199   -655    212       C  
ATOM   1311  OH  TYR A 345     -39.502  -7.689 -11.883  1.00 49.14           O  
ANISOU 1311  OH  TYR A 345     7119   6082   5470    668  -1390   1241       O  
ATOM   1312  N   ASN A 346     -39.670 -12.218  -4.289  1.00 32.57           N  
ANISOU 1312  N   ASN A 346     4601   3397   4376     36   -396    490       N  
ATOM   1313  CA  ASN A 346     -39.807 -13.226  -3.227  1.00 30.49           C  
ANISOU 1313  CA  ASN A 346     4095   3027   4460     -1   -236    289       C  
ATOM   1314  C   ASN A 346     -41.241 -13.700  -2.989  1.00 32.27           C  
ANISOU 1314  C   ASN A 346     4007   3201   5050     95   -218    379       C  
ATOM   1315  O   ASN A 346     -41.457 -14.683  -2.272  1.00 34.92           O  
ANISOU 1315  O   ASN A 346     4545   3578   5144    231     28    602       O  
ATOM   1316  CB  ASN A 346     -39.201 -12.711  -1.914  1.00 31.31           C  
ANISOU 1316  CB  ASN A 346     4415   3084   4396    368   -209     92       C  
ATOM   1317  CG  ASN A 346     -39.768 -11.364  -1.493  1.00 31.65           C  
ANISOU 1317  CG  ASN A 346     4395   3116   4511    370    -40     25       C  
ATOM   1318  OD1 ASN A 346     -40.981 -11.193  -1.382  1.00 32.05           O  
ANISOU 1318  OD1 ASN A 346     4587   2973   4618   1088   -231   -382       O  
ATOM   1319  ND2 ASN A 346     -38.886 -10.406  -1.250  1.00 30.96           N  
ANISOU 1319  ND2 ASN A 346     4643   2876   4242    388    122     32       N  
ATOM   1320  N   ASP A 347     -42.207 -12.976  -3.562  1.00 34.43           N  
ANISOU 1320  N   ASP A 347     4291   3828   4962    176   -372    699       N  
ATOM   1321  CA  ASP A 347     -43.638 -13.300  -3.471  1.00 39.77           C  
ANISOU 1321  CA  ASP A 347     4436   4699   5975   -171   -336    896       C  
ATOM   1322  C   ASP A 347     -44.114 -13.445  -2.004  1.00 39.95           C  
ANISOU 1322  C   ASP A 347     4655   4428   6094   -112   -124    959       C  
ATOM   1323  O   ASP A 347     -44.965 -14.283  -1.686  1.00 39.60           O  
ANISOU 1323  O   ASP A 347     4901   4224   5920   -166   -569   1549       O  
ATOM   1324  CB  ASP A 347     -43.945 -14.550  -4.328  1.00 45.90           C  
ANISOU 1324  CB  ASP A 347     6023   5057   6359    148   -515    502       C  
ATOM   1325  CG  ASP A 347     -45.432 -14.821  -4.484  1.00 58.30           C  
ANISOU 1325  CG  ASP A 347     6441   7276   8431   -574  -1047   1001       C  
ATOM   1326  OD1 ASP A 347     -46.255 -13.875  -4.439  1.00 64.22           O  
ANISOU 1326  OD1 ASP A 347     7763   6913   9724   -178  -1352   2193       O  
ATOM   1327  OD2 ASP A 347     -45.778 -16.007  -4.651  1.00 68.49           O  
ANISOU 1327  OD2 ASP A 347     9303   6702  10017    192  -1308    950       O  
ATOM   1328  N   ASP A 348     -43.539 -12.612  -1.128  1.00 40.25           N  
ANISOU 1328  N   ASP A 348     5078   4036   6177    268      2    777       N  
ATOM   1329  CA  ASP A 348     -43.833 -12.571   0.322  1.00 43.18           C  
ANISOU 1329  CA  ASP A 348     5191   4888   6325    521    -88    911       C  
ATOM   1330  C   ASP A 348     -43.392 -13.797   1.128  1.00 43.49           C  
ANISOU 1330  C   ASP A 348     5358   4565   6601    387    173    931       C  
ATOM   1331  O   ASP A 348     -43.824 -13.986   2.270  1.00 47.03           O  
ANISOU 1331  O   ASP A 348     6584   4576   6708    328    412    974       O  
ATOM   1332  CB  ASP A 348     -45.310 -12.207   0.606  1.00 47.77           C  
ANISOU 1332  CB  ASP A 348     4829   5812   7509    166   -120    796       C  
ATOM   1333  CG  ASP A 348     -45.671 -10.805   0.134  1.00 55.94           C  
ANISOU 1333  CG  ASP A 348     6245   5888   9118    713    132    703       C  
ATOM   1334  OD1 ASP A 348     -44.889  -9.857   0.374  1.00 58.01           O  
ANISOU 1334  OD1 ASP A 348     6489   6360   9190    623     54   -124       O  
ATOM   1335  OD2 ASP A 348     -46.751 -10.645  -0.474  1.00 65.63           O  
ANISOU 1335  OD2 ASP A 348     7488   7635   9813    126  -1193    184       O  
ATOM   1336  N   GLU A 349     -42.527 -14.620   0.539  1.00 39.82           N  
ANISOU 1336  N   GLU A 349     5032   4072   6025    -44     92    854       N  
ATOM   1337  CA  GLU A 349     -41.941 -15.751   1.257  1.00 39.27           C  
ANISOU 1337  CA  GLU A 349     4885   4271   5765    -77      6    808       C  
ATOM   1338  C   GLU A 349     -40.695 -15.268   2.000  1.00 35.52           C  
ANISOU 1338  C   GLU A 349     4635   3919   4941     92    447    839       C  
ATOM   1339  O   GLU A 349     -39.936 -14.457   1.461  1.00 35.62           O  
ANISOU 1339  O   GLU A 349     5156   3188   5188    -57    847     48       O  
ATOM   1340  CB  GLU A 349     -41.613 -16.925   0.320  1.00 37.98           C  
ANISOU 1340  CB  GLU A 349     4997   3679   5752   -203    206   1118       C  
ATOM   1341  CG  GLU A 349     -42.778 -17.418  -0.557  1.00 48.56           C  
ANISOU 1341  CG  GLU A 349     5572   5768   7109   -348   -529    586       C  
ATOM   1342  CD  GLU A 349     -43.946 -18.070   0.199  1.00 57.37           C  
ANISOU 1342  CD  GLU A 349     6475   6343   8979   -719    -39   1329       C  
ATOM   1343  OE1 GLU A 349     -43.809 -18.415   1.397  1.00 63.52           O  
ANISOU 1343  OE1 GLU A 349     7791   7437   8905   -913   -546   1034       O  
ATOM   1344  OE2 GLU A 349     -45.022 -18.255  -0.421  1.00 58.52           O  
ANISOU 1344  OE2 GLU A 349     6782   5791   9660    615   -804    631       O  
ATOM   1345  N   PRO A 350     -40.499 -15.727   3.253  1.00 32.79           N  
ANISOU 1345  N   PRO A 350     4049   3513   4897     26    558    951       N  
ATOM   1346  CA  PRO A 350     -39.271 -15.387   3.982  1.00 32.02           C  
ANISOU 1346  CA  PRO A 350     4230   3437   4499   -161    578    961       C  
ATOM   1347  C   PRO A 350     -38.026 -15.997   3.356  1.00 31.85           C  
ANISOU 1347  C   PRO A 350     4126   3293   4680    -53    228    746       C  
ATOM   1348  O   PRO A 350     -38.103 -17.025   2.666  1.00 31.85           O  
ANISOU 1348  O   PRO A 350     4686   3445   3968    326   -142    913       O  
ATOM   1349  CB  PRO A 350     -39.493 -15.994   5.375  1.00 32.37           C  
ANISOU 1349  CB  PRO A 350     4270   3490   4537   -189    121   1272       C  
ATOM   1350  CG  PRO A 350     -40.613 -16.967   5.208  1.00 32.68           C  
ANISOU 1350  CG  PRO A 350     4326   3482   4609   -264    386   1364       C  
ATOM   1351  CD  PRO A 350     -41.477 -16.408   4.121  1.00 31.64           C  
ANISOU 1351  CD  PRO A 350     3867   3223   4931     42    393   1041       C  
ATOM   1352  N   PHE A 351     -36.895 -15.342   3.593  1.00 29.16           N  
ANISOU 1352  N   PHE A 351     4101   2941   4035     19    156   1043       N  
ATOM   1353  CA  PHE A 351     -35.589 -15.860   3.230  1.00 29.56           C  
ANISOU 1353  CA  PHE A 351     4238   2956   4035   -150    409    687       C  
ATOM   1354  C   PHE A 351     -35.328 -17.215   3.883  1.00 32.22           C  
ANISOU 1354  C   PHE A 351     4861   3176   4205     35     81    827       C  
ATOM   1355  O   PHE A 351     -35.570 -17.384   5.080  1.00 33.75           O  
ANISOU 1355  O   PHE A 351     5302   3361   4159     72    255    720       O  
ATOM   1356  CB  PHE A 351     -34.505 -14.854   3.637  1.00 30.01           C  
ANISOU 1356  CB  PHE A 351     4286   3186   3930   -160    340    430       C  
ATOM   1357  CG  PHE A 351     -33.107 -15.334   3.377  1.00 27.09           C  
ANISOU 1357  CG  PHE A 351     4359   2525   3407     -1    167    425       C  
ATOM   1358  CD1 PHE A 351     -32.713 -15.710   2.087  1.00 25.47           C  
ANISOU 1358  CD1 PHE A 351     4027   2508   3142   -189    114    648       C  
ATOM   1359  CD2 PHE A 351     -32.179 -15.404   4.419  1.00 25.71           C  
ANISOU 1359  CD2 PHE A 351     4416   2046   3304     64    183    702       C  
ATOM   1360  CE1 PHE A 351     -31.421 -16.163   1.845  1.00 27.29           C  
ANISOU 1360  CE1 PHE A 351     4101   2847   3417   -125    245    704       C  
ATOM   1361  CE2 PHE A 351     -30.880 -15.845   4.178  1.00 27.60           C  
ANISOU 1361  CE2 PHE A 351     4311   2792   3381   -128    413    853       C  
ATOM   1362  CZ  PHE A 351     -30.506 -16.235   2.892  1.00 27.32           C  
ANISOU 1362  CZ  PHE A 351     4244   2733   3404   -241    189    566       C  
ATOM   1363  N   LYS A 352     -34.864 -18.175   3.080  1.00 34.94           N  
ANISOU 1363  N   LYS A 352     4905   3648   4723    340   -286    396       N  
ATOM   1364  CA  LYS A 352     -34.499 -19.509   3.575  1.00 36.32           C  
ANISOU 1364  CA  LYS A 352     5126   3513   5160   -174     60    880       C  
ATOM   1365  C   LYS A 352     -32.996 -19.684   3.387  1.00 33.84           C  
ANISOU 1365  C   LYS A 352     5198   3091   4567    -35     71    434       C  
ATOM   1366  O   LYS A 352     -32.550 -19.926   2.264  1.00 36.48           O  
ANISOU 1366  O   LYS A 352     5481   3527   4851    108    740    986       O  
ATOM   1367  CB  LYS A 352     -35.243 -20.638   2.842  1.00 37.79           C  
ANISOU 1367  CB  LYS A 352     5491   3303   5563    -19   -357    920       C  
ATOM   1368  CG  LYS A 352     -36.655 -20.351   2.371  1.00 42.35           C  
ANISOU 1368  CG  LYS A 352     5308   3813   6967    210      4   1466       C  
ATOM   1369  CD  LYS A 352     -37.703 -20.413   3.473  1.00 42.73           C  
ANISOU 1369  CD  LYS A 352     6346   3750   6138     78     11   2100       C  
ATOM   1370  CE  LYS A 352     -39.100 -20.536   2.865  1.00 53.76           C  
ANISOU 1370  CE  LYS A 352     6690   5540   8194   -948   -499   1448       C  
ATOM   1371  NZ  LYS A 352     -39.339 -19.709   1.630  1.00 54.47           N  
ANISOU 1371  NZ  LYS A 352     7391   5014   8289  -1606  -2422    943       N  
ATOM   1372  N   PRO A 353     -32.208 -19.535   4.476  1.00 31.92           N  
ANISOU 1372  N   PRO A 353     4741   3218   4167    334    248    820       N  
ATOM   1373  CA  PRO A 353     -30.755 -19.645   4.359  1.00 29.96           C  
ANISOU 1373  CA  PRO A 353     4645   3050   3686     58    276    688       C  
ATOM   1374  C   PRO A 353     -30.371 -21.081   4.018  1.00 30.02           C  
ANISOU 1374  C   PRO A 353     4794   2977   3632   -187    225    565       C  
ATOM   1375  O   PRO A 353     -31.013 -22.009   4.499  1.00 32.40           O  
ANISOU 1375  O   PRO A 353     4929   3212   4167   -365    400    557       O  
ATOM   1376  CB  PRO A 353     -30.263 -19.262   5.760  1.00 29.74           C  
ANISOU 1376  CB  PRO A 353     4317   3249   3733     59    354    498       C  
ATOM   1377  CG  PRO A 353     -31.410 -19.573   6.671  1.00 29.66           C  
ANISOU 1377  CG  PRO A 353     4327   3249   3690    -77    269    465       C  
ATOM   1378  CD  PRO A 353     -32.625 -19.228   5.861  1.00 31.58           C  
ANISOU 1378  CD  PRO A 353     4490   3500   4008    -24    176    839       C  
ATOM   1379  N   TRP A 354     -29.362 -21.255   3.172  1.00 29.19           N  
ANISOU 1379  N   TRP A 354     4639   2957   3495   -112     26    346       N  
ATOM   1380  CA  TRP A 354     -28.905 -22.593   2.762  1.00 29.28           C  
ANISOU 1380  CA  TRP A 354     4600   2578   3948   -351    259    782       C  
ATOM   1381  C   TRP A 354     -27.916 -23.137   3.784  1.00 30.16           C  
ANISOU 1381  C   TRP A 354     4629   2697   4130   -302    172    784       C  
ATOM   1382  O   TRP A 354     -27.285 -22.375   4.514  1.00 30.64           O  
ANISOU 1382  O   TRP A 354     4614   2574   4452   -193    273    394       O  
ATOM   1383  CB  TRP A 354     -28.261 -22.549   1.367  1.00 27.02           C  
ANISOU 1383  CB  TRP A 354     4473   2131   3660   -169     33    302       C  
ATOM   1384  CG  TRP A 354     -27.287 -21.411   1.234  1.00 29.04           C  
ANISOU 1384  CG  TRP A 354     4655   2477   3900   -355    237    739       C  
ATOM   1385  CD1 TRP A 354     -25.962 -21.433   1.539  1.00 30.77           C  
ANISOU 1385  CD1 TRP A 354     4881   2998   3813   -175    -65    454       C  
ATOM   1386  CD2 TRP A 354     -27.577 -20.074   0.791  1.00 28.31           C  
ANISOU 1386  CD2 TRP A 354     4568   2328   3859   -214      5    308       C  
ATOM   1387  NE1 TRP A 354     -25.398 -20.202   1.300  1.00 32.44           N  
ANISOU 1387  NE1 TRP A 354     5111   3032   4180    -79     63    641       N  
ATOM   1388  CE2 TRP A 354     -26.366 -19.347   0.843  1.00 28.74           C  
ANISOU 1388  CE2 TRP A 354     4685   2509   3723   -376    205    492       C  
ATOM   1389  CE3 TRP A 354     -28.745 -19.421   0.352  1.00 26.22           C  
ANISOU 1389  CE3 TRP A 354     4644   1990   3329   -297    -65    273       C  
ATOM   1390  CZ2 TRP A 354     -26.281 -17.993   0.475  1.00 27.56           C  
ANISOU 1390  CZ2 TRP A 354     4495   2274   3700   -164    103    132       C  
ATOM   1391  CZ3 TRP A 354     -28.658 -18.071  -0.025  1.00 25.95           C  
ANISOU 1391  CZ3 TRP A 354     4374   1851   3631   -226     83     38       C  
ATOM   1392  CH2 TRP A 354     -27.433 -17.378   0.040  1.00 26.68           C  
ANISOU 1392  CH2 TRP A 354     4360   2012   3764   -267    148    -48       C  
ATOM   1393  N   LYS A 355     -27.791 -24.460   3.831  1.00 32.38           N  
ANISOU 1393  N   LYS A 355     4976   2783   4544     19    265    817       N  
ATOM   1394  CA  LYS A 355     -26.801 -25.129   4.669  1.00 33.73           C  
ANISOU 1394  CA  LYS A 355     5039   3040   4737    105    225    958       C  
ATOM   1395  C   LYS A 355     -25.390 -24.655   4.299  1.00 33.06           C  
ANISOU 1395  C   LYS A 355     5077   2907   4576     24    126   1030       C  
ATOM   1396  O   LYS A 355     -25.068 -24.513   3.121  1.00 33.69           O  
ANISOU 1396  O   LYS A 355     5373   3026   4400    587     37    622       O  
ATOM   1397  CB  LYS A 355     -26.939 -26.642   4.497  1.00 36.05           C  
ANISOU 1397  CB  LYS A 355     5369   3068   5256   -179    -11    927       C  
ATOM   1398  CG  LYS A 355     -26.064 -27.481   5.403  1.00 40.59           C  
ANISOU 1398  CG  LYS A 355     5997   3621   5802    213    202   1645       C  
ATOM   1399  CD  LYS A 355     -26.173 -28.955   5.029  1.00 46.39           C  
ANISOU 1399  CD  LYS A 355     6804   3932   6888   -276     96   1260       C  
ATOM   1400  CE  LYS A 355     -25.159 -29.815   5.784  1.00 49.18           C  
ANISOU 1400  CE  LYS A 355     7178   4688   6819    -99    280   1960       C  
ATOM   1401  NZ  LYS A 355     -25.353 -29.784   7.261  1.00 53.13           N  
ANISOU 1401  NZ  LYS A 355     8276   5331   6578  -1054   -379   2284       N  
ATOM   1402  N   GLY A 356     -24.566 -24.388   5.308  1.00 32.59           N  
ANISOU 1402  N   GLY A 356     5127   2292   4964    -73    -22    846       N  
ATOM   1403  CA  GLY A 356     -23.191 -23.939   5.081  1.00 33.78           C  
ANISOU 1403  CA  GLY A 356     4871   3336   4626     87     13   1109       C  
ATOM   1404  C   GLY A 356     -22.987 -22.426   4.966  1.00 33.48           C  
ANISOU 1404  C   GLY A 356     4829   3359   4530     76   -149    920       C  
ATOM   1405  O   GLY A 356     -21.841 -21.964   4.927  1.00 33.62           O  
ANISOU 1405  O   GLY A 356     4794   3163   4814    108    185   1086       O  
ATOM   1406  N   LEU A 357     -24.081 -21.656   4.928  1.00 31.61           N  
ANISOU 1406  N   LEU A 357     4851   3041   4117     25   -195    732       N  
ATOM   1407  CA  LEU A 357     -24.017 -20.193   4.774  1.00 30.01           C  
ANISOU 1407  CA  LEU A 357     4574   3012   3815     21   -104    629       C  
ATOM   1408  C   LEU A 357     -23.077 -19.533   5.796  1.00 29.28           C  
ANISOU 1408  C   LEU A 357     4582   3426   3117     98    -56    974       C  
ATOM   1409  O   LEU A 357     -22.242 -18.701   5.416  1.00 35.22           O  
ANISOU 1409  O   LEU A 357     4563   3823   4994    -57    101   1082       O  
ATOM   1410  CB  LEU A 357     -25.427 -19.571   4.834  1.00 27.72           C  
ANISOU 1410  CB  LEU A 357     4474   2719   3340   -157   -262    344       C  
ATOM   1411  CG  LEU A 357     -25.656 -18.061   4.603  1.00 27.24           C  
ANISOU 1411  CG  LEU A 357     4500   2799   3050    -74   -294    463       C  
ATOM   1412  CD1 LEU A 357     -27.105 -17.825   4.200  1.00 27.07           C  
ANISOU 1412  CD1 LEU A 357     4404   2625   3254   -228   -330    245       C  
ATOM   1413  CD2 LEU A 357     -25.292 -17.194   5.813  1.00 24.38           C  
ANISOU 1413  CD2 LEU A 357     4057   1917   3288   -440    -32    544       C  
ATOM   1414  N   LYS A 358     -23.217 -19.899   7.073  1.00 26.17           N  
ANISOU 1414  N   LYS A 358     4111   2883   2947    283   -183    796       N  
ATOM   1415  CA  LYS A 358     -22.385 -19.337   8.135  1.00 28.01           C  
ANISOU 1415  CA  LYS A 358     4400   3381   2861    184   -140    644       C  
ATOM   1416  C   LYS A 358     -20.941 -19.843   8.077  1.00 30.12           C  
ANISOU 1416  C   LYS A 358     4399   3566   3476     98    -58    664       C  
ATOM   1417  O   LYS A 358     -20.008 -19.044   8.196  1.00 33.64           O  
ANISOU 1417  O   LYS A 358     5074   3901   3806   -314   -325    275       O  
ATOM   1418  CB  LYS A 358     -22.996 -19.575   9.525  1.00 30.39           C  
ANISOU 1418  CB  LYS A 358     4989   3641   2915    247    141    552       C  
ATOM   1419  CG  LYS A 358     -22.201 -18.922  10.656  1.00 34.22           C  
ANISOU 1419  CG  LYS A 358     4912   4643   3444    174   -427    689       C  
ATOM   1420  CD  LYS A 358     -23.014 -18.709  11.928  1.00 40.61           C  
ANISOU 1420  CD  LYS A 358     6427   5366   3637     55    232    834       C  
ATOM   1421  CE  LYS A 358     -23.233 -20.008  12.686  1.00 43.55           C  
ANISOU 1421  CE  LYS A 358     6584   5597   4364    397    249   1347       C  
ATOM   1422  NZ  LYS A 358     -23.912 -19.790  13.988  1.00 46.60           N  
ANISOU 1422  NZ  LYS A 358     7613   5304   4786    -31   1102   1653       N  
ATOM   1423  N   TYR A 359     -20.753 -21.152   7.893  1.00 29.79           N  
ANISOU 1423  N   TYR A 359     4308   3459   3550    252   -192    894       N  
ATOM   1424  CA  TYR A 359     -19.403 -21.703   7.741  1.00 29.51           C  
ANISOU 1424  CA  TYR A 359     4201   3436   3575     50   -162    935       C  
ATOM   1425  C   TYR A 359     -18.652 -21.035   6.591  1.00 29.42           C  
ANISOU 1425  C   TYR A 359     4355   3240   3581     16   -182    931       C  
ATOM   1426  O   TYR A 359     -17.486 -20.667   6.743  1.00 30.99           O  
ANISOU 1426  O   TYR A 359     4147   3864   3764    236   -137    997       O  
ATOM   1427  CB  TYR A 359     -19.417 -23.221   7.541  1.00 29.53           C  
ANISOU 1427  CB  TYR A 359     4535   3231   3450    131    -91   1393       C  
ATOM   1428  CG  TYR A 359     -19.629 -24.047   8.797  1.00 30.96           C  
ANISOU 1428  CG  TYR A 359     4635   3539   3590    258   -308   1682       C  
ATOM   1429  CD1 TYR A 359     -18.905 -23.793   9.971  1.00 31.26           C  
ANISOU 1429  CD1 TYR A 359     4551   3828   3499    357   -201   1740       C  
ATOM   1430  CD2 TYR A 359     -20.524 -25.120   8.798  1.00 29.78           C  
ANISOU 1430  CD2 TYR A 359     4356   3617   3339    272   -137   1830       C  
ATOM   1431  CE1 TYR A 359     -19.090 -24.571  11.113  1.00 30.84           C  
ANISOU 1431  CE1 TYR A 359     4463   3902   3349    468    -79   1676       C  
ATOM   1432  CE2 TYR A 359     -20.715 -25.905   9.932  1.00 31.21           C  
ANISOU 1432  CE2 TYR A 359     4708   3887   3261    406   -135   1907       C  
ATOM   1433  CZ  TYR A 359     -19.999 -25.624  11.087  1.00 31.24           C  
ANISOU 1433  CZ  TYR A 359     4414   4000   3453    484   -156   1927       C  
ATOM   1434  OH  TYR A 359     -20.187 -26.405  12.215  1.00 33.11           O  
ANISOU 1434  OH  TYR A 359     4707   4252   3619    486     37   2083       O  
ATOM   1435  N   ASN A 360     -19.336 -20.871   5.455  1.00 29.03           N  
ANISOU 1435  N   ASN A 360     4511   2831   3688    256   -211   1025       N  
ATOM   1436  CA  ASN A 360     -18.758 -20.226   4.276  1.00 30.84           C  
ANISOU 1436  CA  ASN A 360     4586   3283   3847   -118    -70   1019       C  
ATOM   1437  C   ASN A 360     -18.399 -18.784   4.567  1.00 31.66           C  
ANISOU 1437  C   ASN A 360     4693   3286   4050     -5   -167    873       C  
ATOM   1438  O   ASN A 360     -17.315 -18.329   4.194  1.00 34.62           O  
ANISOU 1438  O   ASN A 360     4545   3856   4752      8    -31    366       O  
ATOM   1439  CB  ASN A 360     -19.710 -20.304   3.082  1.00 30.13           C  
ANISOU 1439  CB  ASN A 360     4472   3114   3862    -86    -56    961       C  
ATOM   1440  CG  ASN A 360     -19.987 -21.732   2.638  1.00 30.54           C  
ANISOU 1440  CG  ASN A 360     4413   3214   3977     81   -197    733       C  
ATOM   1441  OD1 ASN A 360     -19.185 -22.638   2.863  1.00 32.36           O  
ANISOU 1441  OD1 ASN A 360     4925   2873   4497    251    -58    540       O  
ATOM   1442  ND2 ASN A 360     -21.138 -21.939   2.014  1.00 27.83           N  
ANISOU 1442  ND2 ASN A 360     4094   3029   3451   -188    248    537       N  
ATOM   1443  N   PHE A 361     -19.300 -18.081   5.255  1.00 31.19           N  
ANISOU 1443  N   PHE A 361     4455   3530   3864   -328   -101    762       N  
ATOM   1444  CA  PHE A 361     -19.061 -16.697   5.668  1.00 33.29           C  
ANISOU 1444  CA  PHE A 361     4731   4006   3911   -379   -331    100       C  
ATOM   1445  C   PHE A 361     -17.791 -16.610   6.523  1.00 34.92           C  
ANISOU 1445  C   PHE A 361     4846   4346   4076   -480   -442    504       C  
ATOM   1446  O   PHE A 361     -16.964 -15.727   6.300  1.00 35.36           O  
ANISOU 1446  O   PHE A 361     4850   4480   4104   -706   -360    -55       O  
ATOM   1447  CB  PHE A 361     -20.269 -16.105   6.416  1.00 33.22           C  
ANISOU 1447  CB  PHE A 361     4634   3819   4167    -95   -482    174       C  
ATOM   1448  CG  PHE A 361     -19.932 -14.876   7.223  1.00 34.34           C  
ANISOU 1448  CG  PHE A 361     4997   4181   3868   -456   -725    251       C  
ATOM   1449  CD1 PHE A 361     -19.951 -13.608   6.633  1.00 34.72           C  
ANISOU 1449  CD1 PHE A 361     4954   4064   4173   -339   -518    252       C  
ATOM   1450  CD2 PHE A 361     -19.556 -14.986   8.570  1.00 35.01           C  
ANISOU 1450  CD2 PHE A 361     5387   4365   3550   -225   -291    411       C  
ATOM   1451  CE1 PHE A 361     -19.610 -12.473   7.370  1.00 37.31           C  
ANISOU 1451  CE1 PHE A 361     5896   4398   3881   -671   -310    141       C  
ATOM   1452  CE2 PHE A 361     -19.209 -13.856   9.307  1.00 38.69           C  
ANISOU 1452  CE2 PHE A 361     6226   4405   4069   -182   -398    213       C  
ATOM   1453  CZ  PHE A 361     -19.238 -12.598   8.707  1.00 38.40           C  
ANISOU 1453  CZ  PHE A 361     6289   4320   3979   -530   -479    151       C  
ATOM   1454  N   LEU A 362     -17.653 -17.528   7.484  1.00 36.50           N  
ANISOU 1454  N   LEU A 362     4969   4633   4267   -228   -570    746       N  
ATOM   1455  CA  LEU A 362     -16.511 -17.543   8.404  1.00 38.41           C  
ANISOU 1455  CA  LEU A 362     4944   4996   4654   -387   -693    848       C  
ATOM   1456  C   LEU A 362     -15.195 -17.823   7.680  1.00 39.31           C  
ANISOU 1456  C   LEU A 362     4973   5180   4781   -437   -673    612       C  
ATOM   1457  O   LEU A 362     -14.186 -17.162   7.968  1.00 39.57           O  
ANISOU 1457  O   LEU A 362     4852   4872   5311   -395   -754    814       O  
ATOM   1458  CB  LEU A 362     -16.727 -18.521   9.573  1.00 38.18           C  
ANISOU 1458  CB  LEU A 362     5069   5210   4227   -537   -895    767       C  
ATOM   1459  CG  LEU A 362     -17.769 -18.153  10.640  1.00 40.45           C  
ANISOU 1459  CG  LEU A 362     5748   5528   4092   -559   -725    701       C  
ATOM   1460  CD1 LEU A 362     -18.124 -19.364  11.499  1.00 40.30           C  
ANISOU 1460  CD1 LEU A 362     5794   5625   3890   -473  -1283    908       C  
ATOM   1461  CD2 LEU A 362     -17.316 -16.988  11.519  1.00 40.26           C  
ANISOU 1461  CD2 LEU A 362     5422   5358   4513   -842   -740    835       C  
ATOM   1462  N   PHE A 363     -15.210 -18.776   6.738  1.00 35.73           N  
ANISOU 1462  N   PHE A 363     4541   4436   4599   -291   -591    938       N  
ATOM   1463  CA  PHE A 363     -14.050 -19.003   5.875  1.00 37.44           C  
ANISOU 1463  CA  PHE A 363     4519   4671   5035    144   -429   1066       C  
ATOM   1464  C   PHE A 363     -13.667 -17.724   5.113  1.00 39.23           C  
ANISOU 1464  C   PHE A 363     4827   4857   5221   -126   -364   1098       C  
ATOM   1465  O   PHE A 363     -12.511 -17.287   5.169  1.00 42.54           O  
ANISOU 1465  O   PHE A 363     4891   5750   5521   -426    239   1523       O  
ATOM   1466  CB  PHE A 363     -14.270 -20.171   4.896  1.00 37.75           C  
ANISOU 1466  CB  PHE A 363     4292   4864   5185    -39   -379   1119       C  
ATOM   1467  CG  PHE A 363     -13.114 -20.385   3.940  1.00 41.19           C  
ANISOU 1467  CG  PHE A 363     4766   5416   5465    502   -128   1073       C  
ATOM   1468  CD1 PHE A 363     -12.031 -21.193   4.300  1.00 39.49           C  
ANISOU 1468  CD1 PHE A 363     4742   4859   5402    335   -123    983       C  
ATOM   1469  CD2 PHE A 363     -13.092 -19.753   2.691  1.00 40.83           C  
ANISOU 1469  CD2 PHE A 363     4726   5000   5785    641   -220   1314       C  
ATOM   1470  CE1 PHE A 363     -10.960 -21.379   3.428  1.00 42.11           C  
ANISOU 1470  CE1 PHE A 363     4798   5243   5957    458    155   1490       C  
ATOM   1471  CE2 PHE A 363     -12.028 -19.934   1.815  1.00 43.35           C  
ANISOU 1471  CE2 PHE A 363     4879   5701   5891    432    -73   1493       C  
ATOM   1472  CZ  PHE A 363     -10.961 -20.751   2.182  1.00 42.62           C  
ANISOU 1472  CZ  PHE A 363     4993   5221   5978    475    151   1436       C  
ATOM   1473  N   LEU A 364     -14.645 -17.131   4.424  1.00 39.46           N  
ANISOU 1473  N   LEU A 364     5057   4756   5177   -179   -554    941       N  
ATOM   1474  CA  LEU A 364     -14.427 -15.956   3.558  1.00 38.82           C  
ANISOU 1474  CA  LEU A 364     4773   4454   5522   -404   -490    845       C  
ATOM   1475  C   LEU A 364     -13.989 -14.707   4.319  1.00 38.57           C  
ANISOU 1475  C   LEU A 364     4825   4649   5179   -464   -802    917       C  
ATOM   1476  O   LEU A 364     -13.091 -13.987   3.866  1.00 42.02           O  
ANISOU 1476  O   LEU A 364     5442   4554   5968   -775  -1011   1349       O  
ATOM   1477  CB  LEU A 364     -15.669 -15.662   2.706  1.00 33.82           C  
ANISOU 1477  CB  LEU A 364     4822   3599   4426   -718   -222   1070       C  
ATOM   1478  CG  LEU A 364     -15.988 -16.685   1.615  1.00 34.75           C  
ANISOU 1478  CG  LEU A 364     4689   3877   4637   -571   -141    871       C  
ATOM   1479  CD1 LEU A 364     -17.396 -16.475   1.090  1.00 34.11           C  
ANISOU 1479  CD1 LEU A 364     4645   4109   4203    -92    125   1365       C  
ATOM   1480  CD2 LEU A 364     -14.969 -16.676   0.481  1.00 35.32           C  
ANISOU 1480  CD2 LEU A 364     4864   3609   4947  -1034    182   1121       C  
ATOM   1481  N   ASP A 365     -14.619 -14.465   5.467  1.00 38.03           N  
ANISOU 1481  N   ASP A 365     4887   4682   4878   -762   -940    917       N  
ATOM   1482  CA  ASP A 365     -14.256 -13.357   6.350  1.00 43.28           C  
ANISOU 1482  CA  ASP A 365     5457   5166   5821   -814   -966    280       C  
ATOM   1483  C   ASP A 365     -12.818 -13.466   6.858  1.00 47.01           C  
ANISOU 1483  C   ASP A 365     5485   5804   6569   -668  -1050    363       C  
ATOM   1484  O   ASP A 365     -12.108 -12.462   6.917  1.00 50.48           O  
ANISOU 1484  O   ASP A 365     5523   6115   7541   -868   -953   -269       O  
ATOM   1485  CB  ASP A 365     -15.233 -13.243   7.521  1.00 46.36           C  
ANISOU 1485  CB  ASP A 365     5963   5991   5658   -692   -838    138       C  
ATOM   1486  CG  ASP A 365     -15.018 -11.980   8.336  1.00 55.58           C  
ANISOU 1486  CG  ASP A 365     7596   6512   7008  -1135   -914   -479       C  
ATOM   1487  OD1 ASP A 365     -14.942 -10.883   7.742  1.00 58.67           O  
ANISOU 1487  OD1 ASP A 365     8012   6719   7559   -890   -319   -364       O  
ATOM   1488  OD2 ASP A 365     -14.923 -12.090   9.573  1.00 63.33           O  
ANISOU 1488  OD2 ASP A 365     9521   7434   7107  -1078  -1386   -421       O  
ATOM   1489  N   SER A 366     -12.402 -14.684   7.206  1.00 48.45           N  
ANISOU 1489  N   SER A 366     5766   6279   6361   -641   -959   1394       N  
ATOM   1490  CA  SER A 366     -11.017 -14.967   7.582  1.00 51.90           C  
ANISOU 1490  CA  SER A 366     5648   6720   7351  -1123  -1290   1437       C  
ATOM   1491  C   SER A 366     -10.018 -14.675   6.450  1.00 51.91           C  
ANISOU 1491  C   SER A 366     5641   6806   7273   -883  -1191    940       C  
ATOM   1492  O   SER A 366      -8.982 -14.045   6.693  1.00 53.64           O  
ANISOU 1492  O   SER A 366     5395   7371   7611   -983   -891   1109       O  
ATOM   1493  CB  SER A 366     -10.874 -16.408   8.062  1.00 55.13           C  
ANISOU 1493  CB  SER A 366     6086   7105   7756   -359  -1202   1995       C  
ATOM   1494  OG  SER A 366      -9.529 -16.679   8.390  1.00 61.05           O  
ANISOU 1494  OG  SER A 366     6668   7925   8604   -521  -2112   3160       O  
ATOM   1495  N   LYS A 367     -10.332 -15.122   5.228  1.00 49.56           N  
ANISOU 1495  N   LYS A 367     5735   5862   7232   -952   -583    770       N  
ATOM   1496  CA  LYS A 367      -9.488 -14.841   4.060  1.00 47.59           C  
ANISOU 1496  CA  LYS A 367     5040   5756   7285  -1097   -902   1044       C  
ATOM   1497  C   LYS A 367      -9.461 -13.352   3.753  1.00 45.55           C  
ANISOU 1497  C   LYS A 367     4780   5753   6773   -874   -989    987       C  
ATOM   1498  O   LYS A 367      -8.407 -12.827   3.421  1.00 47.56           O  
ANISOU 1498  O   LYS A 367     5089   5623   7359   -991   -774    959       O  
ATOM   1499  CB  LYS A 367      -9.903 -15.638   2.812  1.00 46.30           C  
ANISOU 1499  CB  LYS A 367     4802   5915   6872   -374  -1020   1136       C  
ATOM   1500  CG  LYS A 367      -9.632 -17.139   2.875  1.00 52.05           C  
ANISOU 1500  CG  LYS A 367     5987   6254   7535     94   -466    955       C  
ATOM   1501  CD  LYS A 367      -8.148 -17.515   2.830  1.00 59.16           C  
ANISOU 1501  CD  LYS A 367     5864   8197   8415    167  -1187    822       C  
ATOM   1502  CE  LYS A 367      -7.962 -18.980   3.218  1.00 63.44           C  
ANISOU 1502  CE  LYS A 367     6675   8078   9351    340  -1303    295       C  
ATOM   1503  NZ  LYS A 367      -6.547 -19.411   3.408  1.00 64.51           N  
ANISOU 1503  NZ  LYS A 367     7011   8455   9042   1077   -974    930       N  
ATOM   1504  N   LEU A 368     -10.604 -12.677   3.889  1.00 44.40           N  
ANISOU 1504  N   LEU A 368     5107   5467   6293   -835   -909    513       N  
ATOM   1505  CA  LEU A 368     -10.667 -11.225   3.686  1.00 46.23           C  
ANISOU 1505  CA  LEU A 368     5251   5455   6858   -937   -916    505       C  
ATOM   1506  C   LEU A 368      -9.804 -10.444   4.685  1.00 48.09           C  
ANISOU 1506  C   LEU A 368     5365   5650   7255  -1086   -937    281       C  
ATOM   1507  O   LEU A 368      -9.075  -9.537   4.278  1.00 54.05           O  
ANISOU 1507  O   LEU A 368     6073   5581   8880  -1079   -704    747       O  
ATOM   1508  CB  LEU A 368     -12.115 -10.708   3.678  1.00 43.75           C  
ANISOU 1508  CB  LEU A 368     5124   5048   6449  -1181   -951    656       C  
ATOM   1509  CG  LEU A 368     -12.335  -9.224   3.331  1.00 44.02           C  
ANISOU 1509  CG  LEU A 368     5261   4949   6516  -1217  -1043    542       C  
ATOM   1510  CD1 LEU A 368     -11.856  -8.866   1.924  1.00 41.14           C  
ANISOU 1510  CD1 LEU A 368     4905   4283   6441  -1260  -1419    675       C  
ATOM   1511  CD2 LEU A 368     -13.797  -8.851   3.509  1.00 43.45           C  
ANISOU 1511  CD2 LEU A 368     5213   4943   6353  -1585   -561    461       C  
ATOM   1512  N   GLN A 369      -9.873 -10.805   5.968  1.00 49.65           N  
ANISOU 1512  N   GLN A 369     5837   5789   7236  -1288  -1157    370       N  
ATOM   1513  CA  GLN A 369      -9.058 -10.146   7.004  1.00 55.23           C  
ANISOU 1513  CA  GLN A 369     6020   6584   8378  -1914  -1460     12       C  
ATOM   1514  C   GLN A 369      -7.557 -10.354   6.801  1.00 57.30           C  
ANISOU 1514  C   GLN A 369     6070   7474   8225  -1436  -1480    664       C  
ATOM   1515  O   GLN A 369      -6.773  -9.453   7.098  1.00 67.05           O  
ANISOU 1515  O   GLN A 369     6916   8922   9639  -2335  -1594    282       O  
ATOM   1516  CB  GLN A 369      -9.468 -10.548   8.435  1.00 58.80           C  
ANISOU 1516  CB  GLN A 369     7346   6738   8255  -1924  -1535   -139       C  
ATOM   1517  CG  GLN A 369     -10.919 -10.270   8.850  1.00 66.43           C  
ANISOU 1517  CG  GLN A 369     7716   8194   9330  -1525  -1260   -392       C  
ATOM   1518  CD  GLN A 369     -11.476  -8.917   8.410  1.00 72.41           C  
ANISOU 1518  CD  GLN A 369     8843   8556  10112  -1369  -1940      9       C  
ATOM   1519  OE1 GLN A 369     -10.879  -7.866   8.660  1.00 78.87           O  
ANISOU 1519  OE1 GLN A 369     9848   8783  11336  -1808  -2284    -30       O  
ATOM   1520  NE2 GLN A 369     -12.644  -8.942   7.766  1.00 62.87           N  
ANISOU 1520  NE2 GLN A 369     8175   5559  10151   -339  -1482    612       N  
ATOM   1521  N   GLU A 370      -7.171 -11.526   6.289  1.00 53.46           N  
ANISOU 1521  N   GLU A 370     5335   7050   7925  -2134  -1631    947       N  
ATOM   1522  CA  GLU A 370      -5.774 -11.820   5.917  1.00 56.40           C  
ANISOU 1522  CA  GLU A 370     5403   7603   8421  -2004  -1489    866       C  
ATOM   1523  C   GLU A 370      -5.300 -10.950   4.755  1.00 53.44           C  
ANISOU 1523  C   GLU A 370     4653   6980   8671  -1843  -1205    589       C  
ATOM   1524  O   GLU A 370      -4.147 -10.532   4.725  1.00 53.61           O  
ANISOU 1524  O   GLU A 370     4788   6347   9233  -1890   -443    357       O  
ATOM   1525  CB  GLU A 370      -5.590 -13.298   5.560  1.00 61.44           C  
ANISOU 1525  CB  GLU A 370     6675   7689   8978  -1805  -1511    638       C  
ATOM   1526  CG  GLU A 370      -5.436 -14.221   6.759  1.00 75.63           C  
ANISOU 1526  CG  GLU A 370     8539  10317   9878   -718  -2195   1739       C  
ATOM   1527  CD  GLU A 370      -5.498 -15.703   6.404  1.00 86.91           C  
ANISOU 1527  CD  GLU A 370     9878  10770  12371   -240  -1839   1057       C  
ATOM   1528  OE1 GLU A 370      -4.814 -16.496   7.085  1.00 96.69           O  
ANISOU 1528  OE1 GLU A 370    10301  12903  13533    534  -2275   1847       O  
ATOM   1529  OE2 GLU A 370      -6.229 -16.088   5.462  1.00 92.07           O  
ANISOU 1529  OE2 GLU A 370    10967  12337  11678   -636  -1863   1142       O  
ATOM   1530  N   ILE A 371      -6.201 -10.692   3.808  1.00 52.52           N  
ANISOU 1530  N   ILE A 371     5352   6389   8212  -1568  -1084    931       N  
ATOM   1531  CA  ILE A 371      -5.932  -9.829   2.660  1.00 52.70           C  
ANISOU 1531  CA  ILE A 371     5148   6417   8456  -1942   -960   1050       C  
ATOM   1532  C   ILE A 371      -5.836  -8.357   3.085  1.00 55.76           C  
ANISOU 1532  C   ILE A 371     5488   6895   8801  -1852  -1132    303       C  
ATOM   1533  O   ILE A 371      -4.928  -7.645   2.651  1.00 58.89           O  
ANISOU 1533  O   ILE A 371     5966   7110   9299  -2054   -927    352       O  
ATOM   1534  CB  ILE A 371      -6.984 -10.045   1.538  1.00 49.56           C  
ANISOU 1534  CB  ILE A 371     5142   5688   7998  -1876   -702   1006       C  
ATOM   1535  CG1 ILE A 371      -6.788 -11.423   0.893  1.00 47.78           C  
ANISOU 1535  CG1 ILE A 371     4967   5206   7981  -1495   -360   1538       C  
ATOM   1536  CG2 ILE A 371      -6.913  -8.952   0.472  1.00 49.07           C  
ANISOU 1536  CG2 ILE A 371     5106   5662   7876  -1732   -670    940       C  
ATOM   1537  CD1 ILE A 371      -8.007 -11.958   0.167  1.00 47.05           C  
ANISOU 1537  CD1 ILE A 371     5270   4814   7793  -1293   -835   2133       C  
ATOM   1538  N   LEU A 372      -6.750  -7.913   3.946  1.00 55.28           N  
ANISOU 1538  N   LEU A 372     5689   6642   8670  -1884   -971    563       N  
ATOM   1539  CA  LEU A 372      -6.809  -6.499   4.345  1.00 57.52           C  
ANISOU 1539  CA  LEU A 372     6008   6788   9058  -2059  -1092    282       C  
ATOM   1540  C   LEU A 372      -5.852  -6.105   5.479  1.00 63.12           C  
ANISOU 1540  C   LEU A 372     6439   7911   9632  -2273  -1614    321       C  
ATOM   1541  O   LEU A 372      -5.798  -4.934   5.869  1.00 68.57           O  
ANISOU 1541  O   LEU A 372     7863   8073  10115  -2513  -1285    125       O  
ATOM   1542  CB  LEU A 372      -8.249  -6.084   4.678  1.00 53.91           C  
ANISOU 1542  CB  LEU A 372     6004   6135   8344  -2060  -1177    268       C  
ATOM   1543  CG  LEU A 372      -9.323  -6.187   3.592  1.00 51.51           C  
ANISOU 1543  CG  LEU A 372     5803   5424   8342  -1876  -1112    505       C  
ATOM   1544  CD1 LEU A 372     -10.665  -5.746   4.154  1.00 51.27           C  
ANISOU 1544  CD1 LEU A 372     6395   4935   8148  -1691   -570    831       C  
ATOM   1545  CD2 LEU A 372      -8.973  -5.388   2.345  1.00 54.21           C  
ANISOU 1545  CD2 LEU A 372     6192   5824   8581  -1714   -554    595       C  
ATOM   1546  N   GLU A 373      -5.099  -7.084   5.985  1.00 66.77           N  
ANISOU 1546  N   GLU A 373     6609   8359  10399  -1724  -1563    387       N  
ATOM   1547  CA  GLU A 373      -4.135  -6.898   7.073  1.00 74.40           C  
ANISOU 1547  CA  GLU A 373     7343   9539  11385  -2465  -2319    -60       C  
ATOM   1548  C   GLU A 373      -2.922  -6.087   6.610  1.00 80.31           C  
ANISOU 1548  C   GLU A 373     8108  10195  12210  -2775  -2008    860       C  
ATOM   1549  O   GLU A 373      -2.397  -5.249   7.349  1.00 86.75           O  
ANISOU 1549  O   GLU A 373     9585  10881  12493  -2495  -1818   -183       O  
ATOM   1550  CB  GLU A 373      -3.682  -8.264   7.598  1.00 76.87           C  
ANISOU 1550  CB  GLU A 373     7746  10075  11384  -2631  -2847    485       C  
ATOM   1551  CG  GLU A 373      -3.315  -8.297   9.074  1.00 85.75           C  
ANISOU 1551  CG  GLU A 373     9018  12067  11495  -2026  -2802   1015       C  
ATOM   1552  CD  GLU A 373      -3.092  -9.708   9.599  1.00 91.39           C  
ANISOU 1552  CD  GLU A 373     9324  11964  13436  -2032  -2793    923       C  
ATOM   1553  OE1 GLU A 373      -2.097  -9.919  10.325  1.00 97.62           O  
ANISOU 1553  OE1 GLU A 373     9642  14205  13245  -1467  -3137   -432       O  
ATOM   1554  OE2 GLU A 373      -3.906 -10.609   9.292  1.00 95.58           O  
ANISOU 1554  OE2 GLU A 373     9967  13098  13250  -2636  -3157    375       O  
TER    1555      GLU A 373                                                      
ATOM   1556  N   TYR B -29      10.575 -32.786  31.471  1.00 65.55           N  
ANISOU 1556  N   TYR B -29     8712   9037   7156   1794  -5035   1146       N  
ATOM   1557  CA  TYR B -29      10.288 -31.320  31.574  1.00 72.35           C  
ANISOU 1557  CA  TYR B -29     9751   8643   9093    346  -3513    798       C  
ATOM   1558  C   TYR B -29       8.939 -30.953  30.932  1.00 66.65           C  
ANISOU 1558  C   TYR B -29     9893   8692   6736     -8  -3361    430       C  
ATOM   1559  O   TYR B -29       7.983 -30.608  31.643  1.00 69.23           O  
ANISOU 1559  O   TYR B -29     9379   8798   8127    882  -4003   -273       O  
ATOM   1560  CB  TYR B -29      11.441 -30.490  30.977  1.00 79.74           C  
ANISOU 1560  CB  TYR B -29    10427  10120   9748   -128  -2902   1216       C  
ATOM   1561  CG  TYR B -29      11.245 -28.985  31.076  1.00 85.16           C  
ANISOU 1561  CG  TYR B -29    11759  10350  10245     79  -2896   1063       C  
ATOM   1562  CD1 TYR B -29      11.523 -28.298  32.269  1.00 91.31           C  
ANISOU 1562  CD1 TYR B -29    12709  11483  10502    -80  -2487    324       C  
ATOM   1563  CD2 TYR B -29      10.785 -28.242  29.974  1.00 83.56           C  
ANISOU 1563  CD2 TYR B -29    11948  10451   9348   -816  -2746    930       C  
ATOM   1564  CE1 TYR B -29      11.342 -26.921  32.364  1.00 90.24           C  
ANISOU 1564  CE1 TYR B -29    13372  11106   9808  -1046  -2770    780       C  
ATOM   1565  CE2 TYR B -29      10.598 -26.864  30.061  1.00 84.70           C  
ANISOU 1565  CE2 TYR B -29    12514  10148   9518  -1630  -1817   1707       C  
ATOM   1566  CZ  TYR B -29      10.880 -26.211  31.255  1.00 87.17           C  
ANISOU 1566  CZ  TYR B -29    13239   9852  10027   -985  -1772   1152       C  
ATOM   1567  OH  TYR B -29      10.701 -24.853  31.348  1.00 86.70           O  
ANISOU 1567  OH  TYR B -29    12513   9358  11072   -527    -74   4353       O  
ATOM   1568  N   PHE B -28       8.884 -31.013  29.599  1.00 52.97           N  
ANISOU 1568  N   PHE B -28     7882   5856   6386    -46  -2422   1037       N  
ATOM   1569  CA  PHE B -28       7.648 -30.842  28.842  1.00 48.11           C  
ANISOU 1569  CA  PHE B -28     7420   5418   5440    106  -1745   1072       C  
ATOM   1570  C   PHE B -28       7.125 -32.222  28.445  1.00 51.89           C  
ANISOU 1570  C   PHE B -28     7819   5447   6449    168  -1753    890       C  
ATOM   1571  O   PHE B -28       7.807 -32.976  27.736  1.00 51.88           O  
ANISOU 1571  O   PHE B -28     7613   4907   7192    351  -1962    896       O  
ATOM   1572  CB  PHE B -28       7.906 -29.990  27.593  1.00 42.72           C  
ANISOU 1572  CB  PHE B -28     6705   4151   5373     19  -1722    587       C  
ATOM   1573  CG  PHE B -28       6.658 -29.477  26.918  1.00 44.51           C  
ANISOU 1573  CG  PHE B -28     6563   4989   5359     62  -1742    468       C  
ATOM   1574  CD1 PHE B -28       5.970 -30.262  25.977  1.00 43.26           C  
ANISOU 1574  CD1 PHE B -28     6910   4351   5176    127  -1398    395       C  
ATOM   1575  CD2 PHE B -28       6.183 -28.183  27.186  1.00 41.96           C  
ANISOU 1575  CD2 PHE B -28     6194   4846   4902   -192  -1611    509       C  
ATOM   1576  CE1 PHE B -28       4.822 -29.779  25.342  1.00 40.42           C  
ANISOU 1576  CE1 PHE B -28     6533   4537   4288   -229  -1479   -411       C  
ATOM   1577  CE2 PHE B -28       5.040 -27.696  26.551  1.00 38.20           C  
ANISOU 1577  CE2 PHE B -28     6089   4024   4398   -212  -1241    646       C  
ATOM   1578  CZ  PHE B -28       4.358 -28.495  25.625  1.00 39.77           C  
ANISOU 1578  CZ  PHE B -28     6550   4251   4309    -93  -1232    355       C  
ATOM   1579  N   GLN B -27       5.921 -32.547  28.913  1.00 50.99           N  
ANISOU 1579  N   GLN B -27     7650   5245   6476    589  -1780    991       N  
ATOM   1580  CA  GLN B -27       5.263 -33.804  28.575  1.00 50.79           C  
ANISOU 1580  CA  GLN B -27     7942   5515   5840    356  -1476    829       C  
ATOM   1581  C   GLN B -27       4.516 -33.668  27.239  1.00 50.47           C  
ANISOU 1581  C   GLN B -27     8365   5380   5428    859  -1183    770       C  
ATOM   1582  O   GLN B -27       3.660 -32.801  27.086  1.00 53.47           O  
ANISOU 1582  O   GLN B -27     8590   5535   6191    869  -1320   1262       O  
ATOM   1583  CB  GLN B -27       4.323 -34.228  29.710  1.00 51.58           C  
ANISOU 1583  CB  GLN B -27     8911   5425   5261    878  -1511   1618       C  
ATOM   1584  CG  GLN B -27       3.649 -35.584  29.529  1.00 59.17           C  
ANISOU 1584  CG  GLN B -27    10425   6028   6028    -19   -747   1117       C  
ATOM   1585  CD  GLN B -27       4.596 -36.774  29.664  1.00 66.61           C  
ANISOU 1585  CD  GLN B -27    10622   7572   7114    829  -1252   1727       C  
ATOM   1586  OE1 GLN B -27       5.608 -36.714  30.371  1.00 65.11           O  
ANISOU 1586  OE1 GLN B -27    11402   7609   5727    -12  -1322   1951       O  
ATOM   1587  NE2 GLN B -27       4.260 -37.872  28.986  1.00 74.18           N  
ANISOU 1587  NE2 GLN B -27    12263   7475   8447     26   -889   1631       N  
ATOM   1588  N   GLY B -26       4.854 -34.528  26.280  1.00 45.52           N  
ANISOU 1588  N   GLY B -26     7714   4476   5105    931  -1520   1082       N  
ATOM   1589  CA  GLY B -26       4.240 -34.506  24.952  1.00 40.22           C  
ANISOU 1589  CA  GLY B -26     6820   3627   4834    831  -1087    473       C  
ATOM   1590  C   GLY B -26       4.946 -33.596  23.960  1.00 42.08           C  
ANISOU 1590  C   GLY B -26     6923   4051   5014    563   -838    366       C  
ATOM   1591  O   GLY B -26       6.138 -33.294  24.108  1.00 43.79           O  
ANISOU 1591  O   GLY B -26     6577   4922   5136   1051   -472    334       O  
ATOM   1592  N   SER B -25       4.204 -33.164  22.943  1.00 42.16           N  
ANISOU 1592  N   SER B -25     7144   3766   5108   1123   -775    183       N  
ATOM   1593  CA  SER B -25       4.741 -32.296  21.897  1.00 47.13           C  
ANISOU 1593  CA  SER B -25     7664   4479   5763    590   -594    445       C  
ATOM   1594  C   SER B -25       4.020 -30.957  21.899  1.00 43.06           C  
ANISOU 1594  C   SER B -25     6773   4519   5067    336   -559     96       C  
ATOM   1595  O   SER B -25       2.782 -30.911  21.920  1.00 43.47           O  
ANISOU 1595  O   SER B -25     6860   4545   5109   1249   -332    -44       O  
ATOM   1596  CB  SER B -25       4.604 -32.944  20.515  1.00 51.41           C  
ANISOU 1596  CB  SER B -25     8258   5452   5823   1537      5    -55       C  
ATOM   1597  OG  SER B -25       5.010 -34.302  20.527  1.00 59.32           O  
ANISOU 1597  OG  SER B -25     9462   5962   7112   2464    490    542       O  
ATOM   1598  N   ALA B -24       4.798 -29.873  21.884  1.00 40.68           N  
ANISOU 1598  N   ALA B -24     6660   4344   4451    408   -577    631       N  
ATOM   1599  CA  ALA B -24       4.254 -28.535  21.674  1.00 39.02           C  
ANISOU 1599  CA  ALA B -24     6027   4027   4771    -18   -718    128       C  
ATOM   1600  C   ALA B -24       3.661 -28.445  20.260  1.00 39.74           C  
ANISOU 1600  C   ALA B -24     6007   4483   4609    436   -498    -55       C  
ATOM   1601  O   ALA B -24       4.120 -29.136  19.347  1.00 40.43           O  
ANISOU 1601  O   ALA B -24     6578   4922   3861    563   -594    109       O  
ATOM   1602  CB  ALA B -24       5.325 -27.475  21.894  1.00 35.20           C  
ANISOU 1602  CB  ALA B -24     5761   4045   3567     -7   -815    238       C  
ATOM   1603  N   MET B -23       2.622 -27.625  20.108  1.00 36.62           N  
ANISOU 1603  N   MET B -23     6061   3793   4060    207   -569     39       N  
ATOM   1604  CA  MET B -23       1.874 -27.505  18.861  1.00 32.24           C  
ANISOU 1604  CA  MET B -23     5317   3226   3707    151   -245   -406       C  
ATOM   1605  C   MET B -23       2.574 -26.566  17.875  1.00 32.48           C  
ANISOU 1605  C   MET B -23     5161   3263   3916    213   -594    -43       C  
ATOM   1606  O   MET B -23       3.240 -25.608  18.277  1.00 33.26           O  
ANISOU 1606  O   MET B -23     4830   3568   4238    -47  -1000    502       O  
ATOM   1607  CB  MET B -23       0.453 -26.993  19.136  1.00 31.96           C  
ANISOU 1607  CB  MET B -23     5404   3118   3620     76    -59   -239       C  
ATOM   1608  CG  MET B -23      -0.480 -27.946  19.888  1.00 31.91           C  
ANISOU 1608  CG  MET B -23     4691   2913   4516     93    233   -736       C  
ATOM   1609  SD  MET B -23      -2.085 -27.229  20.350  1.00 23.02           S  
ANISOU 1609  SD  MET B -23     4479   1189   3077   -243     86   -804       S  
ATOM   1610  CE  MET B -23      -1.612 -26.348  21.815  1.00 27.34           C  
ANISOU 1610  CE  MET B -23     5326   2463   2599   -536    -41   -666       C  
ATOM   1611  N   ASP B -22       2.428 -26.861  16.584  1.00 33.14           N  
ANISOU 1611  N   ASP B -22     5216   3544   3830    -90   -183    -81       N  
ATOM   1612  CA  ASP B -22       2.722 -25.906  15.509  1.00 32.83           C  
ANISOU 1612  CA  ASP B -22     5118   3419   3937    250     98    -98       C  
ATOM   1613  C   ASP B -22       1.724 -24.742  15.581  1.00 30.69           C  
ANISOU 1613  C   ASP B -22     5033   3134   3490     60    -38   -262       C  
ATOM   1614  O   ASP B -22       0.559 -24.963  15.942  1.00 29.53           O  
ANISOU 1614  O   ASP B -22     4983   3047   3188    352     -9   -286       O  
ATOM   1615  CB  ASP B -22       2.624 -26.592  14.136  1.00 35.29           C  
ANISOU 1615  CB  ASP B -22     5885   3700   3823    144    109    -72       C  
ATOM   1616  CG  ASP B -22       3.585 -27.776  13.988  1.00 40.54           C  
ANISOU 1616  CG  ASP B -22     6315   4364   4723    532    212   -290       C  
ATOM   1617  OD1 ASP B -22       4.669 -27.767  14.612  1.00 47.77           O  
ANISOU 1617  OD1 ASP B -22     6769   5508   5872     29   -474    535       O  
ATOM   1618  OD2 ASP B -22       3.257 -28.723  13.236  1.00 44.63           O  
ANISOU 1618  OD2 ASP B -22     7219   5105   4633    527   -156   -800       O  
ATOM   1619  N   PRO B -21       2.167 -23.504  15.250  1.00 31.05           N  
ANISOU 1619  N   PRO B -21     4859   3138   3801    -69   -167   -337       N  
ATOM   1620  CA  PRO B -21       1.248 -22.348  15.303  1.00 32.11           C  
ANISOU 1620  CA  PRO B -21     5004   3174   4021     -7     45   -160       C  
ATOM   1621  C   PRO B -21      -0.077 -22.529  14.519  1.00 32.60           C  
ANISOU 1621  C   PRO B -21     5280   3318   3787   -108     12   -366       C  
ATOM   1622  O   PRO B -21      -1.138 -22.279  15.108  1.00 33.75           O  
ANISOU 1622  O   PRO B -21     5521   2851   4449    -31    372    -20       O  
ATOM   1623  CB  PRO B -21       2.079 -21.181  14.742  1.00 31.75           C  
ANISOU 1623  CB  PRO B -21     4776   3020   4265   -252    -23   -627       C  
ATOM   1624  CG  PRO B -21       3.493 -21.602  14.882  1.00 34.04           C  
ANISOU 1624  CG  PRO B -21     4756   3408   4768   -345   -165   -423       C  
ATOM   1625  CD  PRO B -21       3.549 -23.101  14.919  1.00 32.51           C  
ANISOU 1625  CD  PRO B -21     4904   3459   3989     39    159   -585       C  
ATOM   1626  N   PRO B -20      -0.033 -22.971  13.226  1.00 33.30           N  
ANISOU 1626  N   PRO B -20     5264   3652   3734   -184     83   -505       N  
ATOM   1627  CA  PRO B -20      -1.313 -23.201  12.538  1.00 32.42           C  
ANISOU 1627  CA  PRO B -20     5154   3677   3484     11    115   -311       C  
ATOM   1628  C   PRO B -20      -2.192 -24.278  13.187  1.00 30.82           C  
ANISOU 1628  C   PRO B -20     5125   3327   3257    157     13   -488       C  
ATOM   1629  O   PRO B -20      -3.419 -24.166  13.119  1.00 30.00           O  
ANISOU 1629  O   PRO B -20     5098   3165   3132   -237    -39   -789       O  
ATOM   1630  CB  PRO B -20      -0.880 -23.641  11.126  1.00 32.38           C  
ANISOU 1630  CB  PRO B -20     5046   3814   3442    -43   -183   -560       C  
ATOM   1631  CG  PRO B -20       0.450 -22.998  10.935  1.00 32.00           C  
ANISOU 1631  CG  PRO B -20     5036   3947   3174    122    418   -438       C  
ATOM   1632  CD  PRO B -20       1.095 -23.163  12.284  1.00 32.45           C  
ANISOU 1632  CD  PRO B -20     4874   3734   3719   -123    -79   -383       C  
ATOM   1633  N   THR B -19      -1.575 -25.289  13.813  1.00 30.30           N  
ANISOU 1633  N   THR B -19     5524   2781   3206     81     -4   -661       N  
ATOM   1634  CA  THR B -19      -2.315 -26.351  14.506  1.00 30.64           C  
ANISOU 1634  CA  THR B -19     5342   2839   3459    145    -42   -489       C  
ATOM   1635  C   THR B -19      -3.108 -25.791  15.686  1.00 30.87           C  
ANISOU 1635  C   THR B -19     5357   2900   3469    126   -129   -562       C  
ATOM   1636  O   THR B -19      -4.285 -26.144  15.869  1.00 32.58           O  
ANISOU 1636  O   THR B -19     5526   2593   4257    -47     -3   -140       O  
ATOM   1637  CB  THR B -19      -1.399 -27.500  14.994  1.00 29.78           C  
ANISOU 1637  CB  THR B -19     5087   2942   3286    135    -63   -596       C  
ATOM   1638  OG1 THR B -19      -0.586 -27.966  13.913  1.00 30.34           O  
ANISOU 1638  OG1 THR B -19     5016   2629   3884    472    -66   -974       O  
ATOM   1639  CG2 THR B -19      -2.224 -28.666  15.529  1.00 30.99           C  
ANISOU 1639  CG2 THR B -19     5804   2669   3302    354    -65   -159       C  
ATOM   1640  N   PHE B -18      -2.454 -24.928  16.471  1.00 30.16           N  
ANISOU 1640  N   PHE B -18     5496   2652   3308     -7    -90   -362       N  
ATOM   1641  CA  PHE B -18      -3.082 -24.232  17.594  1.00 29.18           C  
ANISOU 1641  CA  PHE B -18     5084   2825   3175   -123   -298   -532       C  
ATOM   1642  C   PHE B -18      -4.245 -23.372  17.122  1.00 29.52           C  
ANISOU 1642  C   PHE B -18     5104   2842   3271   -130   -284   -519       C  
ATOM   1643  O   PHE B -18      -5.360 -23.502  17.624  1.00 33.02           O  
ANISOU 1643  O   PHE B -18     5449   3430   3666     70     59   -974       O  
ATOM   1644  CB  PHE B -18      -2.056 -23.353  18.337  1.00 27.75           C  
ANISOU 1644  CB  PHE B -18     4893   2698   2952   -136    -46   -515       C  
ATOM   1645  CG  PHE B -18      -2.665 -22.477  19.409  1.00 25.58           C  
ANISOU 1645  CG  PHE B -18     4617   2229   2870   -271   -199   -429       C  
ATOM   1646  CD1 PHE B -18      -3.007 -23.012  20.657  1.00 26.13           C  
ANISOU 1646  CD1 PHE B -18     4706   2688   2530    148   -381   -489       C  
ATOM   1647  CD2 PHE B -18      -2.915 -21.122  19.170  1.00 25.80           C  
ANISOU 1647  CD2 PHE B -18     4636   2204   2961   -308   -115   -491       C  
ATOM   1648  CE1 PHE B -18      -3.574 -22.214  21.645  1.00 27.16           C  
ANISOU 1648  CE1 PHE B -18     5044   2449   2825    202   -251   -527       C  
ATOM   1649  CE2 PHE B -18      -3.484 -20.316  20.157  1.00 27.20           C  
ANISOU 1649  CE2 PHE B -18     4760   2560   3014   -328    158   -504       C  
ATOM   1650  CZ  PHE B -18      -3.808 -20.864  21.397  1.00 27.13           C  
ANISOU 1650  CZ  PHE B -18     5124   2373   2809    -72   -176   -493       C  
ATOM   1651  N   THR B -17      -3.967 -22.503  16.153  1.00 30.74           N  
ANISOU 1651  N   THR B -17     5216   2966   3499    -41   -367   -267       N  
ATOM   1652  CA  THR B -17      -4.930 -21.529  15.655  1.00 31.20           C  
ANISOU 1652  CA  THR B -17     5128   3027   3698    103   -264   -207       C  
ATOM   1653  C   THR B -17      -6.184 -22.233  15.129  1.00 30.77           C  
ANISOU 1653  C   THR B -17     5048   2854   3788    -18    178   -355       C  
ATOM   1654  O   THR B -17      -7.299 -21.814  15.436  1.00 32.85           O  
ANISOU 1654  O   THR B -17     5194   3016   4271    413     18    -44       O  
ATOM   1655  CB  THR B -17      -4.268 -20.606  14.601  1.00 33.91           C  
ANISOU 1655  CB  THR B -17     5204   3341   4338     66    -35     93       C  
ATOM   1656  OG1 THR B -17      -3.158 -19.929  15.208  1.00 37.23           O  
ANISOU 1656  OG1 THR B -17     5981   3668   4496    -89   -414   -397       O  
ATOM   1657  CG2 THR B -17      -5.254 -19.556  14.036  1.00 32.64           C  
ANISOU 1657  CG2 THR B -17     5608   3035   3756    117    371    519       C  
ATOM   1658  N   PHE B -16      -5.994 -23.322  14.380  1.00 29.89           N  
ANISOU 1658  N   PHE B -16     5013   2884   3456   -144     68   -333       N  
ATOM   1659  CA  PHE B -16      -7.106 -24.136  13.889  1.00 29.36           C  
ANISOU 1659  CA  PHE B -16     5057   2927   3170    -12    -73   -511       C  
ATOM   1660  C   PHE B -16      -7.905 -24.778  15.035  1.00 28.95           C  
ANISOU 1660  C   PHE B -16     4753   3126   3120     63   -200   -538       C  
ATOM   1661  O   PHE B -16      -9.135 -24.623  15.113  1.00 28.98           O  
ANISOU 1661  O   PHE B -16     4713   3214   3082   -204   -365   -919       O  
ATOM   1662  CB  PHE B -16      -6.579 -25.215  12.939  1.00 29.21           C  
ANISOU 1662  CB  PHE B -16     4941   3233   2922      0   -268   -625       C  
ATOM   1663  CG  PHE B -16      -7.654 -26.043  12.297  1.00 29.75           C  
ANISOU 1663  CG  PHE B -16     5068   3190   3044     27   -285   -750       C  
ATOM   1664  CD1 PHE B -16      -8.452 -25.510  11.275  1.00 30.86           C  
ANISOU 1664  CD1 PHE B -16     4815   3705   3206     85   -369   -667       C  
ATOM   1665  CD2 PHE B -16      -7.860 -27.370  12.693  1.00 29.51           C  
ANISOU 1665  CD2 PHE B -16     4872   3350   2991      9   -331   -423       C  
ATOM   1666  CE1 PHE B -16      -9.435 -26.285  10.669  1.00 31.78           C  
ANISOU 1666  CE1 PHE B -16     5222   3658   3194   -138   -620   -416       C  
ATOM   1667  CE2 PHE B -16      -8.843 -28.148  12.088  1.00 31.86           C  
ANISOU 1667  CE2 PHE B -16     5124   3769   3211   -139   -444   -665       C  
ATOM   1668  CZ  PHE B -16      -9.633 -27.603  11.076  1.00 31.79           C  
ANISOU 1668  CZ  PHE B -16     5212   3414   3451    122   -428   -645       C  
ATOM   1669  N   ASN B -15      -7.196 -25.469  15.928  1.00 27.11           N  
ANISOU 1669  N   ASN B -15     4841   2516   2941    113    -15   -525       N  
ATOM   1670  CA  ASN B -15      -7.827 -26.275  16.967  1.00 27.20           C  
ANISOU 1670  CA  ASN B -15     4731   2289   3313   -108   -122   -497       C  
ATOM   1671  C   ASN B -15      -8.421 -25.526  18.147  1.00 29.53           C  
ANISOU 1671  C   ASN B -15     5041   2873   3303    -71     32   -533       C  
ATOM   1672  O   ASN B -15      -9.376 -26.001  18.768  1.00 29.22           O  
ANISOU 1672  O   ASN B -15     5190   2436   3473     33    -44     45       O  
ATOM   1673  CB  ASN B -15      -6.865 -27.359  17.449  1.00 27.29           C  
ANISOU 1673  CB  ASN B -15     4760   2342   3266   -146   -330   -543       C  
ATOM   1674  CG  ASN B -15      -6.803 -28.520  16.488  1.00 28.00           C  
ANISOU 1674  CG  ASN B -15     5071   2315   3250    -89   -358   -524       C  
ATOM   1675  OD1 ASN B -15      -7.748 -29.294  16.393  1.00 32.56           O  
ANISOU 1675  OD1 ASN B -15     5430   2727   4212   -434   -509   -417       O  
ATOM   1676  ND2 ASN B -15      -5.702 -28.640  15.761  1.00 26.77           N  
ANISOU 1676  ND2 ASN B -15     5043   1913   3214   -516   -326   -339       N  
ATOM   1677  N   PHE B -14      -7.871 -24.350  18.436  1.00 31.47           N  
ANISOU 1677  N   PHE B -14     5490   2882   3584    -93   -288   -652       N  
ATOM   1678  CA  PHE B -14      -8.353 -23.556  19.556  1.00 33.89           C  
ANISOU 1678  CA  PHE B -14     5704   3383   3789    126     -3   -696       C  
ATOM   1679  C   PHE B -14      -9.283 -22.403  19.171  1.00 34.08           C  
ANISOU 1679  C   PHE B -14     5852   3286   3809     73    232   -484       C  
ATOM   1680  O   PHE B -14      -9.713 -21.637  20.042  1.00 32.59           O  
ANISOU 1680  O   PHE B -14     6022   2698   3660    -59    446   -169       O  
ATOM   1681  CB  PHE B -14      -7.183 -23.108  20.434  1.00 33.13           C  
ANISOU 1681  CB  PHE B -14     5643   3152   3793    147    -65   -564       C  
ATOM   1682  CG  PHE B -14      -6.704 -24.181  21.364  1.00 32.89           C  
ANISOU 1682  CG  PHE B -14     5661   3183   3652   -115     66   -410       C  
ATOM   1683  CD1 PHE B -14      -5.855 -25.195  20.908  1.00 32.08           C  
ANISOU 1683  CD1 PHE B -14     5698   2898   3593   -244    -40   -502       C  
ATOM   1684  CD2 PHE B -14      -7.126 -24.204  22.697  1.00 32.87           C  
ANISOU 1684  CD2 PHE B -14     5934   3067   3484   -254   -154   -542       C  
ATOM   1685  CE1 PHE B -14      -5.422 -26.197  21.775  1.00 33.23           C  
ANISOU 1685  CE1 PHE B -14     6093   3111   3420   -265     66   -355       C  
ATOM   1686  CE2 PHE B -14      -6.696 -25.207  23.567  1.00 31.03           C  
ANISOU 1686  CE2 PHE B -14     6092   2702   2995   -335   -293   -879       C  
ATOM   1687  CZ  PHE B -14      -5.842 -26.199  23.105  1.00 31.85           C  
ANISOU 1687  CZ  PHE B -14     5825   2950   3327    -52    -33   -233       C  
ATOM   1688  N   ASN B -13      -9.617 -22.309  17.879  1.00 34.24           N  
ANISOU 1688  N   ASN B -13     5627   3365   4017   -108      0    311       N  
ATOM   1689  CA  ASN B -13     -10.637 -21.373  17.399  1.00 31.98           C  
ANISOU 1689  CA  ASN B -13     5385   3120   3644   -271    126    358       C  
ATOM   1690  C   ASN B -13     -11.910 -21.556  18.219  1.00 30.57           C  
ANISOU 1690  C   ASN B -13     5346   2514   3753   -293     63    316       C  
ATOM   1691  O   ASN B -13     -12.355 -22.681  18.442  1.00 29.19           O  
ANISOU 1691  O   ASN B -13     5239   2371   3481     -6   -278    534       O  
ATOM   1692  CB  ASN B -13     -10.924 -21.579  15.908  1.00 29.94           C  
ANISOU 1692  CB  ASN B -13     5215   2555   3604   -400     80    706       C  
ATOM   1693  CG  ASN B -13     -11.935 -20.582  15.366  1.00 33.15           C  
ANISOU 1693  CG  ASN B -13     5644   2806   4145   -212     46    966       C  
ATOM   1694  OD1 ASN B -13     -13.120 -20.881  15.285  1.00 38.31           O  
ANISOU 1694  OD1 ASN B -13     5758   3377   5420   -170   -419   1020       O  
ATOM   1695  ND2 ASN B -13     -11.475 -19.387  15.024  1.00 31.53           N  
ANISOU 1695  ND2 ASN B -13     5529   2521   3931    226   -160   1110       N  
ATOM   1696  N   ASN B -12     -12.478 -20.454  18.691  1.00 30.46           N  
ANISOU 1696  N   ASN B -12     5549   2638   3384    -88    -30    334       N  
ATOM   1697  CA  ASN B -12     -13.567 -20.563  19.642  1.00 30.54           C  
ANISOU 1697  CA  ASN B -12     5640   2535   3429   -142     32    279       C  
ATOM   1698  C   ASN B -12     -14.952 -20.231  19.089  1.00 31.90           C  
ANISOU 1698  C   ASN B -12     5770   2744   3606    157     64    362       C  
ATOM   1699  O   ASN B -12     -15.861 -19.914  19.855  1.00 30.91           O  
ANISOU 1699  O   ASN B -12     6238   2453   3053    137     59    118       O  
ATOM   1700  CB  ASN B -12     -13.244 -19.793  20.929  1.00 30.63           C  
ANISOU 1700  CB  ASN B -12     5940   2333   3362    -76    130    281       C  
ATOM   1701  CG  ASN B -12     -13.245 -18.287  20.738  1.00 33.34           C  
ANISOU 1701  CG  ASN B -12     6335   2353   3978   -215    171    374       C  
ATOM   1702  OD1 ASN B -12     -13.212 -17.776  19.610  1.00 35.31           O  
ANISOU 1702  OD1 ASN B -12     6774   3172   3471   -297    258     -4       O  
ATOM   1703  ND2 ASN B -12     -13.291 -17.558  21.855  1.00 31.77           N  
ANISOU 1703  ND2 ASN B -12     6275   2637   3157   -240    170    900       N  
ATOM   1704  N   GLU B -11     -15.120 -20.329  17.767  1.00 33.39           N  
ANISOU 1704  N   GLU B -11     6036   3044   3606    114    -42    674       N  
ATOM   1705  CA  GLU B -11     -16.464 -20.346  17.183  1.00 34.43           C  
ANISOU 1705  CA  GLU B -11     6100   3416   3565    516   -116    722       C  
ATOM   1706  C   GLU B -11     -17.243 -21.461  17.874  1.00 33.78           C  
ANISOU 1706  C   GLU B -11     5606   3405   3822    388     78    260       C  
ATOM   1707  O   GLU B -11     -16.701 -22.544  18.078  1.00 36.60           O  
ANISOU 1707  O   GLU B -11     6185   3672   4047    607     59    509       O  
ATOM   1708  CB  GLU B -11     -16.432 -20.572  15.669  1.00 36.24           C  
ANISOU 1708  CB  GLU B -11     6652   3492   3625    590   -225    462       C  
ATOM   1709  CG  GLU B -11     -15.991 -19.363  14.842  1.00 40.39           C  
ANISOU 1709  CG  GLU B -11     7559   4146   3642     79   -590    881       C  
ATOM   1710  CD  GLU B -11     -16.893 -18.141  14.989  1.00 49.21           C  
ANISOU 1710  CD  GLU B -11     8563   5184   4949   1072   -607   1121       C  
ATOM   1711  OE1 GLU B -11     -16.351 -17.016  15.124  1.00 58.41           O  
ANISOU 1711  OE1 GLU B -11    10686   6175   5332   -232  -1303    856       O  
ATOM   1712  OE2 GLU B -11     -18.138 -18.295  14.967  1.00 55.20           O  
ANISOU 1712  OE2 GLU B -11     8775   6283   5914    283   -401   1025       O  
ATOM   1713  N   PRO B -10     -18.497 -21.196  18.283  1.00 35.03           N  
ANISOU 1713  N   PRO B -10     5600   3786   3922    668    -28    509       N  
ATOM   1714  CA  PRO B -10     -19.233 -22.242  19.009  1.00 35.71           C  
ANISOU 1714  CA  PRO B -10     5516   3709   4341    480   -113    519       C  
ATOM   1715  C   PRO B -10     -19.464 -23.503  18.159  1.00 35.50           C  
ANISOU 1715  C   PRO B -10     5590   4155   3742    575   -121    394       C  
ATOM   1716  O   PRO B -10     -19.561 -24.617  18.702  1.00 36.44           O  
ANISOU 1716  O   PRO B -10     5721   3949   4175    666   -139    359       O  
ATOM   1717  CB  PRO B -10     -20.556 -21.556  19.370  1.00 37.86           C  
ANISOU 1717  CB  PRO B -10     5805   3922   4657    542    404    480       C  
ATOM   1718  CG  PRO B -10     -20.266 -20.091  19.295  1.00 38.64           C  
ANISOU 1718  CG  PRO B -10     6188   3885   4607    495    435    420       C  
ATOM   1719  CD  PRO B -10     -19.283 -19.953  18.173  1.00 35.83           C  
ANISOU 1719  CD  PRO B -10     6137   3457   4019    707    137    152       C  
ATOM   1720  N   TRP B  -9     -19.535 -23.319  16.842  1.00 32.99           N  
ANISOU 1720  N   TRP B  -9     5078   3751   3705    191    -15    490       N  
ATOM   1721  CA  TRP B  -9     -19.626 -24.432  15.906  1.00 32.09           C  
ANISOU 1721  CA  TRP B  -9     4564   4119   3507    552   -226    295       C  
ATOM   1722  C   TRP B  -9     -18.450 -24.366  14.958  1.00 32.52           C  
ANISOU 1722  C   TRP B  -9     4749   3863   3742    312   -118    357       C  
ATOM   1723  O   TRP B  -9     -18.182 -23.315  14.378  1.00 34.20           O  
ANISOU 1723  O   TRP B  -9     5115   3766   4114    884   -107    711       O  
ATOM   1724  CB  TRP B  -9     -20.948 -24.402  15.138  1.00 32.50           C  
ANISOU 1724  CB  TRP B  -9     4742   4061   3545    411   -410    -10       C  
ATOM   1725  CG  TRP B  -9     -22.138 -24.432  16.040  1.00 37.09           C  
ANISOU 1725  CG  TRP B  -9     4658   5028   4404    616   -257    221       C  
ATOM   1726  CD1 TRP B  -9     -22.742 -25.541  16.570  1.00 37.79           C  
ANISOU 1726  CD1 TRP B  -9     4820   4933   4604    570   -566    241       C  
ATOM   1727  CD2 TRP B  -9     -22.852 -23.301  16.552  1.00 39.76           C  
ANISOU 1727  CD2 TRP B  -9     5186   5147   4773   1016   -505    224       C  
ATOM   1728  NE1 TRP B  -9     -23.799 -25.169  17.369  1.00 39.62           N  
ANISOU 1728  NE1 TRP B  -9     4955   5625   4473    643   -523    345       N  
ATOM   1729  CE2 TRP B  -9     -23.890 -23.802  17.377  1.00 42.05           C  
ANISOU 1729  CE2 TRP B  -9     5400   5596   4978    914   -405    313       C  
ATOM   1730  CE3 TRP B  -9     -22.726 -21.910  16.384  1.00 42.65           C  
ANISOU 1730  CE3 TRP B  -9     5815   5211   5177    744   -439     35       C  
ATOM   1731  CZ2 TRP B  -9     -24.801 -22.960  18.036  1.00 46.94           C  
ANISOU 1731  CZ2 TRP B  -9     6210   6166   5459   1205     25    222       C  
ATOM   1732  CZ3 TRP B  -9     -23.630 -21.069  17.043  1.00 45.47           C  
ANISOU 1732  CZ3 TRP B  -9     6124   5587   5565   1253   -355    202       C  
ATOM   1733  CH2 TRP B  -9     -24.655 -21.600  17.859  1.00 48.90           C  
ANISOU 1733  CH2 TRP B  -9     6470   6086   6024   1200    -61    209       C  
ATOM   1734  N   VAL B  -8     -17.732 -25.485  14.843  1.00 32.99           N  
ANISOU 1734  N   VAL B  -8     4824   3725   3983    281   -324    166       N  
ATOM   1735  CA  VAL B  -8     -16.613 -25.643  13.903  1.00 31.33           C  
ANISOU 1735  CA  VAL B  -8     4908   3368   3627   -112   -271    354       C  
ATOM   1736  C   VAL B  -8     -16.692 -27.011  13.223  1.00 31.19           C  
ANISOU 1736  C   VAL B  -8     4821   3754   3275     40    -97     70       C  
ATOM   1737  O   VAL B  -8     -17.291 -27.954  13.767  1.00 32.16           O  
ANISOU 1737  O   VAL B  -8     4687   3492   4039     58    111     19       O  
ATOM   1738  CB  VAL B  -8     -15.219 -25.504  14.584  1.00 33.42           C  
ANISOU 1738  CB  VAL B  -8     5069   3769   3857     -1   -440    408       C  
ATOM   1739  CG1 VAL B  -8     -14.960 -24.080  15.079  1.00 33.97           C  
ANISOU 1739  CG1 VAL B  -8     5098   3577   4232     -6   -243    492       C  
ATOM   1740  CG2 VAL B  -8     -15.041 -26.512  15.715  1.00 32.02           C  
ANISOU 1740  CG2 VAL B  -8     4892   3405   3868    270    -31    340       C  
ATOM   1741  N   ARG B  -7     -16.081 -27.112  12.046  1.00 31.19           N  
ANISOU 1741  N   ARG B  -7     4723   4013   3114   -392   -140    265       N  
ATOM   1742  CA  ARG B  -7     -15.972 -28.377  11.319  1.00 34.46           C  
ANISOU 1742  CA  ARG B  -7     5212   4207   3671   -289   -193    -68       C  
ATOM   1743  C   ARG B  -7     -14.533 -28.833  11.231  1.00 34.20           C  
ANISOU 1743  C   ARG B  -7     5365   3977   3651   -149   -115   -166       C  
ATOM   1744  O   ARG B  -7     -13.614 -28.003  11.186  1.00 34.31           O  
ANISOU 1744  O   ARG B  -7     5476   3815   3744   -222    -71   -412       O  
ATOM   1745  CB  ARG B  -7     -16.524 -28.244   9.905  1.00 39.92           C  
ANISOU 1745  CB  ARG B  -7     6402   5146   3619   -478   -450   -321       C  
ATOM   1746  CG  ARG B  -7     -18.038 -28.218   9.845  1.00 49.43           C  
ANISOU 1746  CG  ARG B  -7     6634   6375   5773    227   -471   -316       C  
ATOM   1747  CD  ARG B  -7     -18.573 -29.191   8.812  1.00 60.98           C  
ANISOU 1747  CD  ARG B  -7     9027   8370   5769   -184  -1086   -928       C  
ATOM   1748  NE  ARG B  -7     -18.102 -28.887   7.465  1.00 64.37           N  
ANISOU 1748  NE  ARG B  -7     9723   9122   5613    229  -1391   -376       N  
ATOM   1749  CZ  ARG B  -7     -17.821 -29.801   6.539  1.00 68.32           C  
ANISOU 1749  CZ  ARG B  -7    10420   8300   7238   1149   -678   -358       C  
ATOM   1750  NH1 ARG B  -7     -17.413 -29.405   5.343  1.00 74.18           N  
ANISOU 1750  NH1 ARG B  -7    10295   9909   7980    896    196   -112       N  
ATOM   1751  NH2 ARG B  -7     -17.943 -31.102   6.797  1.00 60.20           N  
ANISOU 1751  NH2 ARG B  -7     9012   8398   5463   2008  -1607   1307       N  
ATOM   1752  N   GLY B  -6     -14.346 -30.153  11.193  1.00 32.57           N  
ANISOU 1752  N   GLY B  -6     5128   3853   3393   -442     48   -488       N  
ATOM   1753  CA  GLY B  -6     -13.029 -30.750  10.997  1.00 31.26           C  
ANISOU 1753  CA  GLY B  -6     5341   3077   3459   -295     78   -490       C  
ATOM   1754  C   GLY B  -6     -12.099 -30.706  12.196  1.00 31.85           C  
ANISOU 1754  C   GLY B  -6     5318   3199   3585   -384     78   -242       C  
ATOM   1755  O   GLY B  -6     -10.892 -30.897  12.042  1.00 37.77           O  
ANISOU 1755  O   GLY B  -6     5418   3825   5106   -160   -100   -130       O  
ATOM   1756  N   ARG B  -5     -12.638 -30.454  13.387  1.00 29.48           N  
ANISOU 1756  N   ARG B  -5     5426   2364   3409   -472     70     -6       N  
ATOM   1757  CA  ARG B  -5     -11.821 -30.535  14.597  1.00 31.71           C  
ANISOU 1757  CA  ARG B  -5     5108   3264   3674   -307     23   -182       C  
ATOM   1758  C   ARG B  -5     -11.993 -31.915  15.222  1.00 32.79           C  
ANISOU 1758  C   ARG B  -5     5128   3322   4009    -19     96    -25       C  
ATOM   1759  O   ARG B  -5     -12.693 -32.096  16.225  1.00 34.56           O  
ANISOU 1759  O   ARG B  -5     5254   3865   4012    592    221    316       O  
ATOM   1760  CB  ARG B  -5     -12.120 -29.381  15.568  1.00 29.39           C  
ANISOU 1760  CB  ARG B  -5     4846   2961   3360   -321    157    150       C  
ATOM   1761  CG  ARG B  -5     -11.379 -28.081  15.249  1.00 27.61           C  
ANISOU 1761  CG  ARG B  -5     4617   2869   3002   -371   -152    -66       C  
ATOM   1762  CD  ARG B  -5     -11.901 -27.368  13.998  1.00 26.81           C  
ANISOU 1762  CD  ARG B  -5     4698   2642   2845   -297    138    -13       C  
ATOM   1763  NE  ARG B  -5     -11.297 -26.048  13.869  1.00 26.88           N  
ANISOU 1763  NE  ARG B  -5     4561   2942   2707   -381     88    434       N  
ATOM   1764  CZ  ARG B  -5     -11.615 -25.122  12.962  1.00 28.28           C  
ANISOU 1764  CZ  ARG B  -5     4709   2783   3253   -446     65    627       C  
ATOM   1765  NH1 ARG B  -5     -12.545 -25.333  12.028  1.00 28.39           N  
ANISOU 1765  NH1 ARG B  -5     5177   2477   3129   -533    -71    848       N  
ATOM   1766  NH2 ARG B  -5     -10.977 -23.969  12.985  1.00 26.79           N  
ANISOU 1766  NH2 ARG B  -5     4256   2476   3446   -136   -202    845       N  
ATOM   1767  N   HIS B  -4     -11.351 -32.891  14.586  1.00 35.91           N  
ANISOU 1767  N   HIS B  -4     5386   3633   4624     57    337   -267       N  
ATOM   1768  CA  HIS B  -4     -11.462 -34.308  14.958  1.00 36.54           C  
ANISOU 1768  CA  HIS B  -4     5716   3556   4610   -416    378   -401       C  
ATOM   1769  C   HIS B  -4     -10.634 -34.663  16.195  1.00 37.52           C  
ANISOU 1769  C   HIS B  -4     5650   3651   4954   -319    243   -148       C  
ATOM   1770  O   HIS B  -4     -10.941 -35.620  16.892  1.00 43.48           O  
ANISOU 1770  O   HIS B  -4     6883   4037   5597   -442     92    267       O  
ATOM   1771  CB  HIS B  -4     -11.090 -35.194  13.766  1.00 34.72           C  
ANISOU 1771  CB  HIS B  -4     5743   2834   4612   -622    460   -251       C  
ATOM   1772  CG  HIS B  -4     -11.883 -34.895  12.529  1.00 40.65           C  
ANISOU 1772  CG  HIS B  -4     6183   4351   4909   -506     93   -394       C  
ATOM   1773  ND1 HIS B  -4     -13.182 -35.323  12.354  1.00 43.82           N  
ANISOU 1773  ND1 HIS B  -4     6469   5034   5143   -943    -82   -468       N  
ATOM   1774  CD2 HIS B  -4     -11.570 -34.189  11.416  1.00 42.05           C  
ANISOU 1774  CD2 HIS B  -4     6872   4568   4533   -475    117   -613       C  
ATOM   1775  CE1 HIS B  -4     -13.633 -34.901  11.187  1.00 43.02           C  
ANISOU 1775  CE1 HIS B  -4     6734   5119   4492   -936    139   -855       C  
ATOM   1776  NE2 HIS B  -4     -12.675 -34.211  10.598  1.00 43.10           N  
ANISOU 1776  NE2 HIS B  -4     6778   5183   4414   -797    210   -835       N  
ATOM   1777  N   GLU B  -3      -9.596 -33.880  16.464  1.00 37.30           N  
ANISOU 1777  N   GLU B  -3     5577   3650   4944   -390    382    219       N  
ATOM   1778  CA  GLU B  -3      -8.739 -34.069  17.636  1.00 40.71           C  
ANISOU 1778  CA  GLU B  -3     6173   4156   5139    139    264    244       C  
ATOM   1779  C   GLU B  -3      -9.220 -33.258  18.831  1.00 36.91           C  
ANISOU 1779  C   GLU B  -3     5400   3664   4957   -251     84    286       C  
ATOM   1780  O   GLU B  -3      -9.908 -32.255  18.668  1.00 38.36           O  
ANISOU 1780  O   GLU B  -3     5794   3223   5558   -229    348   -500       O  
ATOM   1781  CB  GLU B  -3      -7.291 -33.678  17.310  1.00 46.42           C  
ANISOU 1781  CB  GLU B  -3     6308   5130   6199    182    407    932       C  
ATOM   1782  CG  GLU B  -3      -6.420 -34.827  16.818  1.00 57.20           C  
ANISOU 1782  CG  GLU B  -3     7858   6243   7629    848    808    148       C  
ATOM   1783  CD  GLU B  -3      -5.805 -35.665  17.937  1.00 63.41           C  
ANISOU 1783  CD  GLU B  -3     8933   7017   8139    918    138    417       C  
ATOM   1784  OE1 GLU B  -3      -6.285 -35.611  19.101  1.00 54.22           O  
ANISOU 1784  OE1 GLU B  -3     9512   3263   7825   1392   -209  -1246       O  
ATOM   1785  OE2 GLU B  -3      -4.830 -36.396  17.639  1.00 69.03           O  
ANISOU 1785  OE2 GLU B  -3     8586   9450   8191    844    839  -1276       O  
ATOM   1786  N   THR B  -2      -8.871 -33.717  20.029  1.00 35.09           N  
ANISOU 1786  N   THR B  -2     5466   3110   4755   -390     -5      1       N  
ATOM   1787  CA  THR B  -2      -8.970 -32.895  21.231  1.00 34.44           C  
ANISOU 1787  CA  THR B  -2     5073   3284   4727   -337    155      5       C  
ATOM   1788  C   THR B  -2      -7.556 -32.611  21.728  1.00 32.97           C  
ANISOU 1788  C   THR B  -2     5157   2857   4512    -81   -150    172       C  
ATOM   1789  O   THR B  -2      -6.770 -33.537  21.954  1.00 32.26           O  
ANISOU 1789  O   THR B  -2     5262   2872   4124   -109   -622     -3       O  
ATOM   1790  CB  THR B  -2      -9.818 -33.555  22.342  1.00 35.73           C  
ANISOU 1790  CB  THR B  -2     5597   3052   4926   -328    215    319       C  
ATOM   1791  OG1 THR B  -2     -11.145 -33.774  21.858  1.00 36.46           O  
ANISOU 1791  OG1 THR B  -2     5645   2880   5328   -170     99    349       O  
ATOM   1792  CG2 THR B  -2      -9.898 -32.655  23.586  1.00 37.83           C  
ANISOU 1792  CG2 THR B  -2     6179   3492   4704   -249    448    394       C  
ATOM   1793  N   TYR B  -1      -7.236 -31.332  21.897  1.00 33.75           N  
ANISOU 1793  N   TYR B  -1     6356   2932   3534   -239   -189   -338       N  
ATOM   1794  CA  TYR B  -1      -5.917 -30.928  22.367  1.00 33.68           C  
ANISOU 1794  CA  TYR B  -1     6696   2495   3604   -379   -322   -316       C  
ATOM   1795  C   TYR B  -1      -5.967 -30.455  23.816  1.00 34.91           C  
ANISOU 1795  C   TYR B  -1     6745   3120   3399   -343   -538   -283       C  
ATOM   1796  O   TYR B  -1      -6.685 -29.511  24.146  1.00 40.40           O  
ANISOU 1796  O   TYR B  -1     7524   4517   3309   -135    283   -580       O  
ATOM   1797  CB  TYR B  -1      -5.343 -29.827  21.473  1.00 34.09           C  
ANISOU 1797  CB  TYR B  -1     7097   2545   3309   -347   -466    -97       C  
ATOM   1798  CG  TYR B  -1      -4.746 -30.336  20.181  1.00 33.53           C  
ANISOU 1798  CG  TYR B  -1     7128   2131   3481   -501   -537   -362       C  
ATOM   1799  CD1 TYR B  -1      -3.409 -30.703  20.108  1.00 37.00           C  
ANISOU 1799  CD1 TYR B  -1     7398   2294   4366     -6   -306   -356       C  
ATOM   1800  CD2 TYR B  -1      -5.519 -30.450  19.033  1.00 30.89           C  
ANISOU 1800  CD2 TYR B  -1     6993   1434   3310   -429   -474   -338       C  
ATOM   1801  CE1 TYR B  -1      -2.859 -31.169  18.929  1.00 39.80           C  
ANISOU 1801  CE1 TYR B  -1     7364   3615   4141   -148   -242   -297       C  
ATOM   1802  CE2 TYR B  -1      -4.978 -30.915  17.850  1.00 35.59           C  
ANISOU 1802  CE2 TYR B  -1     7417   2752   3351   -364    -11   -188       C  
ATOM   1803  CZ  TYR B  -1      -3.648 -31.273  17.803  1.00 39.16           C  
ANISOU 1803  CZ  TYR B  -1     7327   3383   4167   -377   -230    -92       C  
ATOM   1804  OH  TYR B  -1      -3.104 -31.737  16.627  1.00 42.51           O  
ANISOU 1804  OH  TYR B  -1     7813   3271   5068    116    696    -83       O  
ATOM   1805  N   LEU B 218      -5.085 -31.150  24.815  1.00 32.80           N  
ANISOU 1805  N   LEU B 218     6971   2155   3333   -299   -187     11       N  
ATOM   1806  CA  LEU B 218      -5.288 -30.918  26.240  1.00 32.49           C  
ANISOU 1806  CA  LEU B 218     6748   2281   3314     97   -433    -45       C  
ATOM   1807  C   LEU B 218      -4.021 -30.380  26.897  1.00 32.68           C  
ANISOU 1807  C   LEU B 218     6804   2225   3385     38   -591   -213       C  
ATOM   1808  O   LEU B 218      -3.225 -31.141  27.448  1.00 36.51           O  
ANISOU 1808  O   LEU B 218     6922   3027   3920    309   -867    -99       O  
ATOM   1809  CB  LEU B 218      -5.734 -32.206  26.934  1.00 32.79           C  
ANISOU 1809  CB  LEU B 218     7020   2335   3104      0   -438     -6       C  
ATOM   1810  CG  LEU B 218      -6.276 -32.055  28.357  1.00 33.92           C  
ANISOU 1810  CG  LEU B 218     7181   2641   3062    155   -479    -19       C  
ATOM   1811  CD1 LEU B 218      -7.085 -33.279  28.757  1.00 35.73           C  
ANISOU 1811  CD1 LEU B 218     7304   3021   3249    -60    -52   -153       C  
ATOM   1812  CD2 LEU B 218      -5.141 -31.813  29.342  1.00 36.24           C  
ANISOU 1812  CD2 LEU B 218     6803   3273   3692    173   -489    104       C  
ATOM   1813  N   CYS B 219      -3.840 -29.065  26.834  1.00 31.38           N  
ANISOU 1813  N   CYS B 219     6961   2177   2785    229  -1026      9       N  
ATOM   1814  CA  CYS B 219      -2.671 -28.424  27.422  1.00 35.19           C  
ANISOU 1814  CA  CYS B 219     6954   2793   3621     16  -1070   -265       C  
ATOM   1815  C   CYS B 219      -2.852 -28.425  28.934  1.00 36.31           C  
ANISOU 1815  C   CYS B 219     7064   3114   3616    201  -1122   -285       C  
ATOM   1816  O   CYS B 219      -3.970 -28.252  29.423  1.00 38.42           O  
ANISOU 1816  O   CYS B 219     7429   3831   3337    236   -723   -796       O  
ATOM   1817  CB  CYS B 219      -2.543 -26.998  26.912  1.00 35.18           C  
ANISOU 1817  CB  CYS B 219     6653   2734   3979    360  -1166   -202       C  
ATOM   1818  SG  CYS B 219      -2.439 -26.895  25.119  1.00 40.35           S  
ANISOU 1818  SG  CYS B 219     7614   3558   4158    357   -800    -16       S  
ATOM   1819  N   PHE B 220      -1.769 -28.632  29.676  1.00 35.67           N  
ANISOU 1819  N   PHE B 220     7390   2756   3405    212  -1209     80       N  
ATOM   1820  CA  PHE B 220      -1.862 -28.611  31.127  1.00 35.95           C  
ANISOU 1820  CA  PHE B 220     7394   2872   3390    693  -1276   -154       C  
ATOM   1821  C   PHE B 220      -0.692 -27.911  31.804  1.00 39.00           C  
ANISOU 1821  C   PHE B 220     7507   3361   3949    554  -1333   -269       C  
ATOM   1822  O   PHE B 220       0.423 -27.909  31.278  1.00 40.62           O  
ANISOU 1822  O   PHE B 220     7946   3629   3858    668   -747    -94       O  
ATOM   1823  CB  PHE B 220      -2.041 -30.036  31.688  1.00 35.22           C  
ANISOU 1823  CB  PHE B 220     6840   3008   3532    728  -1034     -8       C  
ATOM   1824  CG  PHE B 220      -0.765 -30.826  31.783  1.00 34.39           C  
ANISOU 1824  CG  PHE B 220     7089   2730   3249    875  -1116    222       C  
ATOM   1825  CD1 PHE B 220       0.037 -30.758  32.930  1.00 34.97           C  
ANISOU 1825  CD1 PHE B 220     7082   3080   3125    810  -1045    267       C  
ATOM   1826  CD2 PHE B 220      -0.360 -31.649  30.730  1.00 36.01           C  
ANISOU 1826  CD2 PHE B 220     7174   2883   3625    772   -986    -42       C  
ATOM   1827  CE1 PHE B 220       1.222 -31.489  33.020  1.00 35.49           C  
ANISOU 1827  CE1 PHE B 220     7286   2907   3291   1020   -682    451       C  
ATOM   1828  CE2 PHE B 220       0.821 -32.388  30.818  1.00 36.14           C  
ANISOU 1828  CE2 PHE B 220     7102   2880   3748    799  -1105   -164       C  
ATOM   1829  CZ  PHE B 220       1.610 -32.306  31.962  1.00 36.44           C  
ANISOU 1829  CZ  PHE B 220     7279   3030   3535   1058  -1076    128       C  
ATOM   1830  N   THR B 221      -0.971 -27.311  32.964  1.00 41.20           N  
ANISOU 1830  N   THR B 221     8071   3876   3705    986  -1527   -219       N  
ATOM   1831  CA  THR B 221       0.063 -26.934  33.928  1.00 44.45           C  
ANISOU 1831  CA  THR B 221     8562   4313   4011    928  -1740   -678       C  
ATOM   1832  C   THR B 221      -0.258 -27.612  35.258  1.00 46.57           C  
ANISOU 1832  C   THR B 221     8711   4724   4256   1146  -1787   -357       C  
ATOM   1833  O   THR B 221      -1.427 -27.884  35.565  1.00 44.43           O  
ANISOU 1833  O   THR B 221     8801   4068   4012   1438  -1227   -833       O  
ATOM   1834  CB  THR B 221       0.185 -25.411  34.137  1.00 45.43           C  
ANISOU 1834  CB  THR B 221     8716   4231   4313    915  -1432   -537       C  
ATOM   1835  OG1 THR B 221      -1.049 -24.896  34.646  1.00 44.64           O  
ANISOU 1835  OG1 THR B 221     9684   3150   4124    943   -757   -921       O  
ATOM   1836  CG2 THR B 221       0.544 -24.699  32.833  1.00 45.58           C  
ANISOU 1836  CG2 THR B 221     9134   4450   3734   1022  -1254  -1064       C  
ATOM   1837  N   MET B 222       0.786 -27.881  36.037  1.00 48.08           N  
ANISOU 1837  N   MET B 222     8793   4742   4733   1264  -1992   -281       N  
ATOM   1838  CA  MET B 222       0.657 -28.613  37.282  1.00 50.14           C  
ANISOU 1838  CA  MET B 222     9283   5459   4307   1733  -1976   -401       C  
ATOM   1839  C   MET B 222       1.576 -28.011  38.331  1.00 55.32           C  
ANISOU 1839  C   MET B 222    10013   6027   4976   1477  -2240   -886       C  
ATOM   1840  O   MET B 222       2.797 -27.980  38.152  1.00 60.53           O  
ANISOU 1840  O   MET B 222    10187   7004   5806   1601  -2081   -802       O  
ATOM   1841  CB  MET B 222       0.997 -30.086  37.053  1.00 51.40           C  
ANISOU 1841  CB  MET B 222     9714   5258   4556   1612  -2025    -52       C  
ATOM   1842  CG  MET B 222       0.865 -30.980  38.279  1.00 53.28           C  
ANISOU 1842  CG  MET B 222    10431   5180   4631   2049  -1420   -129       C  
ATOM   1843  SD  MET B 222       1.186 -32.717  37.916  1.00 48.84           S  
ANISOU 1843  SD  MET B 222    10389   4402   3762   1189  -1682    361       S  
ATOM   1844  CE  MET B 222      -0.179 -33.034  36.810  1.00 44.11           C  
ANISOU 1844  CE  MET B 222     8873   3142   4743   1455  -1340    788       C  
ATOM   1845  N   GLU B 223       0.970 -27.526  39.412  1.00 54.53           N  
ANISOU 1845  N   GLU B 223     9881   5769   5066   1871  -2314   -810       N  
ATOM   1846  CA  GLU B 223       1.699 -27.081  40.589  1.00 57.12           C  
ANISOU 1846  CA  GLU B 223    10608   6577   4516   2047  -2437   -558       C  
ATOM   1847  C   GLU B 223       1.790 -28.271  41.546  1.00 56.69           C  
ANISOU 1847  C   GLU B 223    10411   6144   4983   2025  -2183   -592       C  
ATOM   1848  O   GLU B 223       0.763 -28.805  41.982  1.00 52.81           O  
ANISOU 1848  O   GLU B 223    10145   5633   4287   2636  -1668   -591       O  
ATOM   1849  CB  GLU B 223       1.003 -25.873  41.236  1.00 63.75           C  
ANISOU 1849  CB  GLU B 223    12120   6741   5361   2138  -2105  -1145       C  
ATOM   1850  CG  GLU B 223       1.731 -25.300  42.447  1.00 76.14           C  
ANISOU 1850  CG  GLU B 223    13629   8873   6428   1412  -3159  -1452       C  
ATOM   1851  CD  GLU B 223       1.003 -24.132  43.094  1.00 88.05           C  
ANISOU 1851  CD  GLU B 223    15615   9517   8321   2609  -2399  -1199       C  
ATOM   1852  OE1 GLU B 223       0.925 -23.050  42.469  1.00 98.69           O  
ANISOU 1852  OE1 GLU B 223    17891   9922   9682    919   -775    -83       O  
ATOM   1853  OE2 GLU B 223       0.519 -24.290  44.236  1.00 79.50           O  
ANISOU 1853  OE2 GLU B 223    16832   7919   5455   3697  -5239  -1173       O  
ATOM   1854  N   VAL B 224       3.024 -28.684  41.839  1.00 59.46           N  
ANISOU 1854  N   VAL B 224    10718   6946   4926   2269  -2715   -578       N  
ATOM   1855  CA  VAL B 224       3.306 -29.821  42.728  1.00 62.10           C  
ANISOU 1855  CA  VAL B 224    10778   7510   5307   2596  -2772   -274       C  
ATOM   1856  C   VAL B 224       3.729 -29.294  44.109  1.00 64.40           C  
ANISOU 1856  C   VAL B 224    11197   8105   5165   2696  -2521   -472       C  
ATOM   1857  O   VAL B 224       4.752 -28.607  44.248  1.00 65.87           O  
ANISOU 1857  O   VAL B 224    11305   8147   5575   2980  -3875  -1233       O  
ATOM   1858  CB  VAL B 224       4.356 -30.793  42.112  1.00 57.81           C  
ANISOU 1858  CB  VAL B 224    10641   6771   4553   2303  -2987   -134       C  
ATOM   1859  CG1 VAL B 224       4.707 -31.924  43.064  1.00 56.40           C  
ANISOU 1859  CG1 VAL B 224    10326   7005   4097   2411  -3453   -298       C  
ATOM   1860  CG2 VAL B 224       3.854 -31.366  40.796  1.00 54.39           C  
ANISOU 1860  CG2 VAL B 224     9863   6445   4357   2385  -2212   -538       C  
ATOM   1861  N   VAL B 225       2.916 -29.609  45.115  1.00 63.97           N  
ANISOU 1861  N   VAL B 225    11976   7522   4807   2780  -2439     43       N  
ATOM   1862  CA  VAL B 225       3.104 -29.090  46.470  1.00 67.80           C  
ANISOU 1862  CA  VAL B 225    12442   8144   5175   2596  -2776   -422       C  
ATOM   1863  C   VAL B 225       3.421 -30.238  47.428  1.00 70.45           C  
ANISOU 1863  C   VAL B 225    12350   8681   5736   2983  -2891    -30       C  
ATOM   1864  O   VAL B 225       2.554 -31.059  47.749  1.00 66.10           O  
ANISOU 1864  O   VAL B 225    12518   8218   4376   3467  -1816    -61       O  
ATOM   1865  CB  VAL B 225       1.876 -28.270  46.960  1.00 71.48           C  
ANISOU 1865  CB  VAL B 225    13027   8623   5509   2978  -2442   -405       C  
ATOM   1866  CG1 VAL B 225       2.128 -27.687  48.350  1.00 74.74           C  
ANISOU 1866  CG1 VAL B 225    13245   9705   5447   2631  -2798   -374       C  
ATOM   1867  CG2 VAL B 225       1.522 -27.158  45.973  1.00 69.04           C  
ANISOU 1867  CG2 VAL B 225    12997   8743   4489   3241  -1164   -441       C  
ATOM   1868  N   LYS B 226       4.676 -30.276  47.868  1.00 76.07           N  
ANISOU 1868  N   LYS B 226    12594  10030   6278   2863  -3341   -107       N  
ATOM   1869  CA  LYS B 226       5.177 -31.311  48.766  1.00 79.57           C  
ANISOU 1869  CA  LYS B 226    13829  10575   5826   2742  -3298    268       C  
ATOM   1870  C   LYS B 226       5.739 -30.642  50.017  1.00 79.90           C  
ANISOU 1870  C   LYS B 226    14342  10130   5886   3248  -3624    354       C  
ATOM   1871  O   LYS B 226       6.605 -29.762  49.917  1.00 79.77           O  
ANISOU 1871  O   LYS B 226    14469   9961   5876   3451  -3501     75       O  
ATOM   1872  CB  LYS B 226       6.255 -32.136  48.056  1.00 82.46           C  
ANISOU 1872  CB  LYS B 226    14287  10813   6227   2975  -3179    336       C  
ATOM   1873  CG  LYS B 226       6.444 -33.540  48.597  1.00 91.03           C  
ANISOU 1873  CG  LYS B 226    14452  10795   9340   4147  -3688    245       C  
ATOM   1874  CD  LYS B 226       7.018 -34.459  47.530  1.00 99.40           C  
ANISOU 1874  CD  LYS B 226    15453  12851   9463   4308  -2452     98       C  
ATOM   1875  CE  LYS B 226       6.986 -35.910  47.986  1.00106.08           C  
ANISOU 1875  CE  LYS B 226    16509  12765  11032   5475  -2668    317       C  
ATOM   1876  NZ  LYS B 226       7.298 -36.862  46.883  1.00105.10           N  
ANISOU 1876  NZ  LYS B 226    16839  12543  10549   6253  -2303    998       N  
ATOM   1877  N   HIS B 227       5.235 -31.053  51.184  1.00 84.16           N  
ANISOU 1877  N   HIS B 227    15469  10809   5695   2871  -3826    872       N  
ATOM   1878  CA  HIS B 227       5.707 -30.542  52.476  1.00 90.48           C  
ANISOU 1878  CA  HIS B 227    15417  12389   6569   2927  -4372     69       C  
ATOM   1879  C   HIS B 227       7.216 -30.760  52.616  1.00 91.99           C  
ANISOU 1879  C   HIS B 227    15473  12132   7344   3451  -4591    405       C  
ATOM   1880  O   HIS B 227       7.738 -31.801  52.201  1.00 92.93           O  
ANISOU 1880  O   HIS B 227    14424  12787   8097   4532  -4392   1128       O  
ATOM   1881  CB  HIS B 227       4.940 -31.197  53.637  1.00100.48           C  
ANISOU 1881  CB  HIS B 227    17184  14258   6735   2946  -3734    599       C  
ATOM   1882  CG  HIS B 227       4.864 -30.351  54.875  1.00113.58           C  
ANISOU 1882  CG  HIS B 227    19382  15041   8732   3642  -2933   -717       C  
ATOM   1883  ND1 HIS B 227       5.256 -30.808  56.116  1.00118.27           N  
ANISOU 1883  ND1 HIS B 227    19088  16202   9647   4401  -3258    -97       N  
ATOM   1884  CD2 HIS B 227       4.437 -29.078  55.063  1.00116.50           C  
ANISOU 1884  CD2 HIS B 227    20140  15298   8824   4318  -2990   -110       C  
ATOM   1885  CE1 HIS B 227       5.076 -29.855  57.014  1.00115.94           C  
ANISOU 1885  CE1 HIS B 227    18878  16777   8395   3493  -3105   -250       C  
ATOM   1886  NE2 HIS B 227       4.582 -28.794  56.401  1.00116.78           N  
ANISOU 1886  NE2 HIS B 227    20354  14724   9290   3768  -2694  -1472       N  
ATOM   1887  N   HIS B 228       7.898 -29.747  53.158  1.00 94.39           N  
ANISOU 1887  N   HIS B 228    15459  12928   7477   3367  -5242    353       N  
ATOM   1888  CA  HIS B 228       9.371 -29.700  53.321  1.00 98.78           C  
ANISOU 1888  CA  HIS B 228    15370  13924   8239   3777  -4505    134       C  
ATOM   1889  C   HIS B 228      10.189 -29.605  52.013  1.00 94.17           C  
ANISOU 1889  C   HIS B 228    15119  12944   7717   3689  -4846   -836       C  
ATOM   1890  O   HIS B 228      11.427 -29.594  52.047  1.00 85.58           O  
ANISOU 1890  O   HIS B 228    14980   9896   7637   3207  -4887  -2769       O  
ATOM   1891  CB  HIS B 228       9.886 -30.840  54.222  1.00103.89           C  
ANISOU 1891  CB  HIS B 228    16142  14745   8586   4541  -4716    481       C  
ATOM   1892  CG  HIS B 228       9.460 -30.722  55.653  1.00109.19           C  
ANISOU 1892  CG  HIS B 228    17199  15870   8417   5193  -5229    634       C  
ATOM   1893  ND1 HIS B 228       8.384 -31.412  56.170  1.00114.64           N  
ANISOU 1893  ND1 HIS B 228    17920  16350   9286   4653  -5916   1205       N  
ATOM   1894  CD2 HIS B 228       9.973 -30.003  56.680  1.00108.71           C  
ANISOU 1894  CD2 HIS B 228    16739  14678   9889   5185  -5977    587       C  
ATOM   1895  CE1 HIS B 228       8.249 -31.119  57.451  1.00117.87           C  
ANISOU 1895  CE1 HIS B 228    19575  15954   9256   4067  -5161   1297       C  
ATOM   1896  NE2 HIS B 228       9.202 -30.268  57.786  1.00117.85           N  
ANISOU 1896  NE2 HIS B 228    18943  15519  10313   4758  -4918    -63       N  
ATOM   1897  N   SER B 229       9.494 -29.519  50.879  1.00 94.07           N  
ANISOU 1897  N   SER B 229    14710  13080   7950   3648  -4988  -1426       N  
ATOM   1898  CA  SER B 229      10.123 -29.362  49.565  1.00 99.78           C  
ANISOU 1898  CA  SER B 229    14855  13754   9302   2555  -4037   -199       C  
ATOM   1899  C   SER B 229       9.719 -28.039  48.903  1.00 96.90           C  
ANISOU 1899  C   SER B 229    14554  12762   9498   1989  -3823   -849       C  
ATOM   1900  O   SER B 229       8.616 -27.540  49.159  1.00 95.32           O  
ANISOU 1900  O   SER B 229    15611  10953   9651   2016  -2947  -2492       O  
ATOM   1901  CB  SER B 229       9.757 -30.535  48.647  1.00 99.79           C  
ANISOU 1901  CB  SER B 229    14608  13231  10077   2589  -4347    -56       C  
ATOM   1902  OG  SER B 229      10.441 -31.717  49.024  1.00100.33           O  
ANISOU 1902  OG  SER B 229    12797  13746  11576   3305  -4381  -1144       O  
ATOM   1903  N   PRO B 230      10.612 -27.458  48.063  1.00 91.84           N  
ANISOU 1903  N   PRO B 230    14329  12344   8220   1675  -4758   -681       N  
ATOM   1904  CA  PRO B 230      10.178 -26.333  47.233  1.00 87.71           C  
ANISOU 1904  CA  PRO B 230    13487  12027   7810   1497  -4817   -977       C  
ATOM   1905  C   PRO B 230       9.164 -26.781  46.183  1.00 84.09           C  
ANISOU 1905  C   PRO B 230    13352  11248   7350   1725  -4550   -864       C  
ATOM   1906  O   PRO B 230       9.241 -27.911  45.684  1.00 83.93           O  
ANISOU 1906  O   PRO B 230    13439  11143   7308   1843  -5174   -805       O  
ATOM   1907  CB  PRO B 230      11.473 -25.856  46.561  1.00 88.40           C  
ANISOU 1907  CB  PRO B 230    13670  12210   7707   1016  -4948  -1205       C  
ATOM   1908  CG  PRO B 230      12.411 -27.010  46.651  1.00 93.43           C  
ANISOU 1908  CG  PRO B 230    13901  12902   8693   1409  -4393   -717       C  
ATOM   1909  CD  PRO B 230      12.064 -27.696  47.937  1.00 94.99           C  
ANISOU 1909  CD  PRO B 230    14193  13419   8480   1112  -4456   -792       C  
ATOM   1910  N   VAL B 231       8.214 -25.896  45.886  1.00 81.18           N  
ANISOU 1910  N   VAL B 231    13315  10654   6874   1605  -4167  -1035       N  
ATOM   1911  CA  VAL B 231       7.195 -26.110  44.856  1.00 78.01           C  
ANISOU 1911  CA  VAL B 231    12901   9500   7237   1458  -4052  -1141       C  
ATOM   1912  C   VAL B 231       7.840 -26.365  43.480  1.00 78.30           C  
ANISOU 1912  C   VAL B 231    12901   9469   7377   1195  -3739   -764       C  
ATOM   1913  O   VAL B 231       8.820 -25.708  43.116  1.00 80.06           O  
ANISOU 1913  O   VAL B 231    13184   9476   7757    223  -4459  -1061       O  
ATOM   1914  CB  VAL B 231       6.155 -24.946  44.840  1.00 80.38           C  
ANISOU 1914  CB  VAL B 231    12956   9863   7721   1671  -3833  -1680       C  
ATOM   1915  CG1 VAL B 231       6.823 -23.578  44.710  1.00 88.18           C  
ANISOU 1915  CG1 VAL B 231    13944  10151   9407   1399  -3636  -1308       C  
ATOM   1916  CG2 VAL B 231       5.106 -25.138  43.755  1.00 76.57           C  
ANISOU 1916  CG2 VAL B 231    12357   9495   7241   3337  -3547  -1803       C  
ATOM   1917  N   SER B 232       7.308 -27.349  42.752  1.00 76.42           N  
ANISOU 1917  N   SER B 232    12167   9364   7504   1837  -3930   -946       N  
ATOM   1918  CA  SER B 232       7.769 -27.676  41.397  1.00 73.19           C  
ANISOU 1918  CA  SER B 232    11402   9210   7195   1468  -3967   -239       C  
ATOM   1919  C   SER B 232       6.621 -27.640  40.390  1.00 66.78           C  
ANISOU 1919  C   SER B 232    11179   7836   6356   1554  -3453    272       C  
ATOM   1920  O   SER B 232       5.459 -27.866  40.748  1.00 65.81           O  
ANISOU 1920  O   SER B 232    10974   7686   6343   2006  -3555     30       O  
ATOM   1921  CB  SER B 232       8.479 -29.038  41.366  1.00 80.85           C  
ANISOU 1921  CB  SER B 232    11751   9651   9315   1896  -3766   -850       C  
ATOM   1922  OG  SER B 232       7.665 -30.067  41.902  1.00 81.99           O  
ANISOU 1922  OG  SER B 232    12386   8474  10292   2687  -3847   -140       O  
ATOM   1923  N   TRP B 233       6.958 -27.352  39.134  1.00 64.13           N  
ANISOU 1923  N   TRP B 233    10573   7666   6124   1010  -3321   -390       N  
ATOM   1924  CA  TRP B 233       5.964 -27.235  38.070  1.00 60.63           C  
ANISOU 1924  CA  TRP B 233     9942   7309   5784   1007  -2868   -381       C  
ATOM   1925  C   TRP B 233       6.158 -28.266  36.961  1.00 57.21           C  
ANISOU 1925  C   TRP B 233     9378   6692   5667    917  -3055    -42       C  
ATOM   1926  O   TRP B 233       7.289 -28.656  36.648  1.00 59.38           O  
ANISOU 1926  O   TRP B 233     9362   7565   5633   1068  -3057    476       O  
ATOM   1927  CB  TRP B 233       5.959 -25.819  37.484  1.00 64.66           C  
ANISOU 1927  CB  TRP B 233    10640   7386   6541    572  -2750   -189       C  
ATOM   1928  CG  TRP B 233       5.462 -24.767  38.439  1.00 73.88           C  
ANISOU 1928  CG  TRP B 233    12204   8218   7647    563  -2707  -1134       C  
ATOM   1929  CD1 TRP B 233       4.160 -24.392  38.643  1.00 74.27           C  
ANISOU 1929  CD1 TRP B 233    12400   7807   8011    878  -2716  -1072       C  
ATOM   1930  CD2 TRP B 233       6.257 -23.953  39.315  1.00 80.41           C  
ANISOU 1930  CD2 TRP B 233    13283   9804   7464    586  -3837  -1199       C  
ATOM   1931  NE1 TRP B 233       4.096 -23.399  39.593  1.00 76.39           N  
ANISOU 1931  NE1 TRP B 233    12909   8858   7255   1109  -2724  -1288       N  
ATOM   1932  CE2 TRP B 233       5.366 -23.107  40.022  1.00 84.08           C  
ANISOU 1932  CE2 TRP B 233    13211  10378   8357   1081  -3528  -1004       C  
ATOM   1933  CE3 TRP B 233       7.638 -23.853  39.573  1.00 90.92           C  
ANISOU 1933  CE3 TRP B 233    13235  11382   9926    180  -3361  -1056       C  
ATOM   1934  CZ2 TRP B 233       5.810 -22.168  40.978  1.00 94.08           C  
ANISOU 1934  CZ2 TRP B 233    14641  10649  10455    746  -3729  -1911       C  
ATOM   1935  CZ3 TRP B 233       8.084 -22.917  40.528  1.00 96.44           C  
ANISOU 1935  CZ3 TRP B 233    13784  12120  10737   -164  -3795  -1478       C  
ATOM   1936  CH2 TRP B 233       7.166 -22.088  41.216  1.00 97.96           C  
ANISOU 1936  CH2 TRP B 233    14827  11658  10733     81  -4282  -2152       C  
ATOM   1937  N   LYS B 234       5.039 -28.705  36.389  1.00 52.66           N  
ANISOU 1937  N   LYS B 234     8876   5786   5343   1339  -2874    232       N  
ATOM   1938  CA  LYS B 234       5.024 -29.551  35.193  1.00 52.39           C  
ANISOU 1938  CA  LYS B 234     8687   5882   5336   1534  -1967    163       C  
ATOM   1939  C   LYS B 234       4.048 -28.997  34.159  1.00 47.77           C  
ANISOU 1939  C   LYS B 234     7816   5459   4875    832  -1579    177       C  
ATOM   1940  O   LYS B 234       3.024 -28.401  34.511  1.00 44.53           O  
ANISOU 1940  O   LYS B 234     8330   3308   5279    759  -2057   -261       O  
ATOM   1941  CB  LYS B 234       4.647 -30.996  35.538  1.00 55.28           C  
ANISOU 1941  CB  LYS B 234     8947   6169   5887   1609  -1592    789       C  
ATOM   1942  CG  LYS B 234       5.747 -31.786  36.228  1.00 59.78           C  
ANISOU 1942  CG  LYS B 234     9251   6903   6558   2213  -1839    648       C  
ATOM   1943  CD  LYS B 234       5.246 -33.157  36.647  1.00 65.60           C  
ANISOU 1943  CD  LYS B 234    10291   7282   7351   2138  -1471   1371       C  
ATOM   1944  CE  LYS B 234       6.261 -33.871  37.528  1.00 72.87           C  
ANISOU 1944  CE  LYS B 234    10457   9208   8020   2754  -1923   1191       C  
ATOM   1945  NZ  LYS B 234       7.422 -34.400  36.758  1.00 77.02           N  
ANISOU 1945  NZ  LYS B 234    10421   9239   9602   2165  -1189    337       N  
ATOM   1946  N   ARG B 235       4.378 -29.182  32.884  1.00 45.08           N  
ANISOU 1946  N   ARG B 235     7582   4935   4609    337  -2179   -222       N  
ATOM   1947  CA  ARG B 235       3.493 -28.778  31.803  1.00 43.09           C  
ANISOU 1947  CA  ARG B 235     7296   4812   4265    474  -1829   -328       C  
ATOM   1948  C   ARG B 235       3.601 -29.727  30.622  1.00 40.15           C  
ANISOU 1948  C   ARG B 235     6884   4059   4311    714  -1548     35       C  
ATOM   1949  O   ARG B 235       4.555 -30.499  30.512  1.00 40.01           O  
ANISOU 1949  O   ARG B 235     6578   4311   4311    769  -1753   1124       O  
ATOM   1950  CB  ARG B 235       3.707 -27.301  31.385  1.00 47.00           C  
ANISOU 1950  CB  ARG B 235     7949   4839   5067    319  -2163   -321       C  
ATOM   1951  CG  ARG B 235       4.916 -26.993  30.506  1.00 53.22           C  
ANISOU 1951  CG  ARG B 235     8557   6190   5472    254  -1765   -161       C  
ATOM   1952  CD  ARG B 235       6.063 -26.413  31.317  1.00 62.37           C  
ANISOU 1952  CD  ARG B 235     8946   7801   6948     39  -2425   -302       C  
ATOM   1953  NE  ARG B 235       6.846 -27.458  31.974  1.00 68.03           N  
ANISOU 1953  NE  ARG B 235     9557   8828   7461    622  -2475    143       N  
ATOM   1954  CZ  ARG B 235       7.593 -27.290  33.065  1.00 67.79           C  
ANISOU 1954  CZ  ARG B 235     9759   8439   7557    521  -2594    -63       C  
ATOM   1955  NH1 ARG B 235       7.676 -26.107  33.670  1.00 66.38           N  
ANISOU 1955  NH1 ARG B 235    10111   7837   7272     84  -3085    623       N  
ATOM   1956  NH2 ARG B 235       8.256 -28.326  33.558  1.00 66.68           N  
ANISOU 1956  NH2 ARG B 235    10430   8754   6149    383  -2631    522       N  
ATOM   1957  N   GLY B 236       2.604 -29.669  29.751  1.00 37.99           N  
ANISOU 1957  N   GLY B 236     6825   3895   3713    338  -1304   -125       N  
ATOM   1958  CA  GLY B 236       2.638 -30.406  28.507  1.00 35.64           C  
ANISOU 1958  CA  GLY B 236     6402   3122   4018    740  -1057   -158       C  
ATOM   1959  C   GLY B 236       1.310 -30.418  27.798  1.00 36.64           C  
ANISOU 1959  C   GLY B 236     6794   3512   3613    312  -1272   -233       C  
ATOM   1960  O   GLY B 236       0.402 -29.635  28.126  1.00 38.84           O  
ANISOU 1960  O   GLY B 236     6945   3345   4465    413  -1215     52       O  
ATOM   1961  N   VAL B 237       1.216 -31.320  26.824  1.00 36.12           N  
ANISOU 1961  N   VAL B 237     6702   3104   3915    611   -791   -317       N  
ATOM   1962  CA  VAL B 237       0.087 -31.419  25.898  1.00 34.73           C  
ANISOU 1962  CA  VAL B 237     6843   2837   3513    588   -789   -180       C  
ATOM   1963  C   VAL B 237      -0.255 -32.893  25.676  1.00 33.88           C  
ANISOU 1963  C   VAL B 237     6541   2961   3371    552   -869   -459       C  
ATOM   1964  O   VAL B 237       0.623 -33.692  25.347  1.00 35.54           O  
ANISOU 1964  O   VAL B 237     7162   2347   3993    751   -932   -656       O  
ATOM   1965  CB  VAL B 237       0.409 -30.746  24.528  1.00 34.24           C  
ANISOU 1965  CB  VAL B 237     6605   3008   3394     97   -906   -282       C  
ATOM   1966  CG1 VAL B 237      -0.719 -30.961  23.522  1.00 30.51           C  
ANISOU 1966  CG1 VAL B 237     6250   2661   2679    261   -565    -37       C  
ATOM   1967  CG2 VAL B 237       0.680 -29.250  24.686  1.00 34.46           C  
ANISOU 1967  CG2 VAL B 237     7021   3084   2987   -145   -580   -399       C  
ATOM   1968  N   PHE B 238      -1.525 -33.242  25.864  1.00 33.79           N  
ANISOU 1968  N   PHE B 238     6818   2873   3144    320   -578   -419       N  
ATOM   1969  CA  PHE B 238      -2.041 -34.560  25.475  1.00 33.90           C  
ANISOU 1969  CA  PHE B 238     6813   2594   3471    336   -393   -114       C  
ATOM   1970  C   PHE B 238      -3.000 -34.450  24.288  1.00 32.56           C  
ANISOU 1970  C   PHE B 238     6823   2391   3154    229   -209   -153       C  
ATOM   1971  O   PHE B 238      -3.699 -33.447  24.144  1.00 31.89           O  
ANISOU 1971  O   PHE B 238     6773   2615   2725    270   -603    174       O  
ATOM   1972  CB  PHE B 238      -2.740 -35.233  26.654  1.00 33.74           C  
ANISOU 1972  CB  PHE B 238     6966   2503   3349    350   -485    -83       C  
ATOM   1973  CG  PHE B 238      -1.798 -35.805  27.668  1.00 37.29           C  
ANISOU 1973  CG  PHE B 238     7214   2924   4027    887   -514     43       C  
ATOM   1974  CD1 PHE B 238      -1.324 -35.018  28.725  1.00 40.32           C  
ANISOU 1974  CD1 PHE B 238     7883   3217   4218    694   -656    -86       C  
ATOM   1975  CD2 PHE B 238      -1.382 -37.137  27.577  1.00 37.84           C  
ANISOU 1975  CD2 PHE B 238     7503   2815   4059    744   -331    -13       C  
ATOM   1976  CE1 PHE B 238      -0.448 -35.548  29.664  1.00 41.62           C  
ANISOU 1976  CE1 PHE B 238     7802   3654   4355   1164   -429     55       C  
ATOM   1977  CE2 PHE B 238      -0.510 -37.671  28.514  1.00 42.77           C  
ANISOU 1977  CE2 PHE B 238     7800   3727   4722   1021   -651    221       C  
ATOM   1978  CZ  PHE B 238      -0.046 -36.876  29.560  1.00 43.67           C  
ANISOU 1978  CZ  PHE B 238     7810   3773   5007   1267   -441   -211       C  
ATOM   1979  N   ARG B 239      -3.006 -35.486  23.452  1.00 35.39           N  
ANISOU 1979  N   ARG B 239     7423   2472   3549    254     54   -355       N  
ATOM   1980  CA  ARG B 239      -3.930 -35.657  22.320  1.00 40.41           C  
ANISOU 1980  CA  ARG B 239     7952   3169   4229   -183   -405   -442       C  
ATOM   1981  C   ARG B 239      -4.677 -36.964  22.550  1.00 41.84           C  
ANISOU 1981  C   ARG B 239     8439   3333   4124   -353   -201   -362       C  
ATOM   1982  O   ARG B 239      -4.290 -37.748  23.422  1.00 44.27           O  
ANISOU 1982  O   ARG B 239     9074   3319   4427   -330   -103    -51       O  
ATOM   1983  CB  ARG B 239      -3.148 -35.781  21.005  1.00 41.21           C  
ANISOU 1983  CB  ARG B 239     8633   3258   3765   -438   -594   -748       C  
ATOM   1984  CG  ARG B 239      -2.648 -34.471  20.414  1.00 50.54           C  
ANISOU 1984  CG  ARG B 239     9338   4022   5842   -155   -325    587       C  
ATOM   1985  CD  ARG B 239      -1.443 -34.649  19.486  1.00 60.37           C  
ANISOU 1985  CD  ARG B 239    10494   6138   6305   -558    552   -155       C  
ATOM   1986  NE  ARG B 239      -1.633 -35.664  18.441  1.00 71.25           N  
ANISOU 1986  NE  ARG B 239    11806   7626   7640  -1951    276  -1170       N  
ATOM   1987  CZ  ARG B 239      -1.676 -35.435  17.123  1.00 73.39           C  
ANISOU 1987  CZ  ARG B 239    13062   6851   7970  -2046   -208   -629       C  
ATOM   1988  NH1 ARG B 239      -1.850 -36.456  16.288  1.00 78.85           N  
ANISOU 1988  NH1 ARG B 239    13529   8568   7862  -4540  -1319  -1149       N  
ATOM   1989  NH2 ARG B 239      -1.536 -34.210  16.623  1.00 65.42           N  
ANISOU 1989  NH2 ARG B 239    13041   6573   5240   -687   -307   -731       N  
ATOM   1990  N   ASN B 240      -5.733 -37.205  21.772  1.00 43.86           N  
ANISOU 1990  N   ASN B 240     8598   4074   3992   -467   -233   -635       N  
ATOM   1991  CA  ASN B 240      -6.344 -38.534  21.704  1.00 44.42           C  
ANISOU 1991  CA  ASN B 240     8871   3743   4261   -271    -67   -395       C  
ATOM   1992  C   ASN B 240      -5.308 -39.556  21.246  1.00 43.86           C  
ANISOU 1992  C   ASN B 240     9112   3565   3986   -405     63   -509       C  
ATOM   1993  O   ASN B 240      -4.501 -39.268  20.353  1.00 44.31           O  
ANISOU 1993  O   ASN B 240     9667   3311   3856   -612    283   -851       O  
ATOM   1994  CB  ASN B 240      -7.549 -38.554  20.748  1.00 44.76           C  
ANISOU 1994  CB  ASN B 240     9335   3480   4191   -607   -343   -865       C  
ATOM   1995  CG  ASN B 240      -8.681 -37.628  21.186  1.00 45.44           C  
ANISOU 1995  CG  ASN B 240     8484   4890   3891   -624   -300   -611       C  
ATOM   1996  OD1 ASN B 240      -8.815 -37.277  22.364  1.00 45.68           O  
ANISOU 1996  OD1 ASN B 240     8780   4700   3874   -699    151   -440       O  
ATOM   1997  ND2 ASN B 240      -9.507 -37.229  20.229  1.00 45.65           N  
ANISOU 1997  ND2 ASN B 240     8348   4887   4109  -1168   -437   -108       N  
ATOM   1998  N   GLN B 241      -5.299 -40.715  21.905  1.00 45.05           N  
ANISOU 1998  N   GLN B 241     9029   3536   4551   -301    258   -353       N  
ATOM   1999  CA  GLN B 241      -4.577 -41.890  21.425  1.00 47.94           C  
ANISOU 1999  CA  GLN B 241    10113   3208   4895   -145    603   -240       C  
ATOM   2000  C   GLN B 241      -5.596 -42.737  20.670  1.00 49.12           C  
ANISOU 2000  C   GLN B 241    10392   3177   5095      6    325   -307       C  
ATOM   2001  O   GLN B 241      -6.727 -42.922  21.131  1.00 47.71           O  
ANISOU 2001  O   GLN B 241    10474   2866   4786   -404     18   -870       O  
ATOM   2002  CB  GLN B 241      -3.941 -42.665  22.582  1.00 50.94           C  
ANISOU 2002  CB  GLN B 241     9645   4590   5120    677    694   -174       C  
ATOM   2003  N   VAL B 242      -5.182 -43.248  19.514  1.00 53.19           N  
ANISOU 2003  N   VAL B 242    11333   3285   5589   -400    984   -516       N  
ATOM   2004  CA  VAL B 242      -6.108 -43.681  18.465  1.00 56.07           C  
ANISOU 2004  CA  VAL B 242    11728   3703   5870   -705    785   -701       C  
ATOM   2005  C   VAL B 242      -5.961 -45.172  18.058  1.00 58.92           C  
ANISOU 2005  C   VAL B 242    12176   4007   6202   -263   1278   -930       C  
ATOM   2006  O   VAL B 242      -6.890 -45.757  17.481  1.00 64.29           O  
ANISOU 2006  O   VAL B 242    12523   5354   6548   -762    721   -611       O  
ATOM   2007  CB  VAL B 242      -6.063 -42.639  17.299  1.00 54.18           C  
ANISOU 2007  CB  VAL B 242    11745   3579   5260   -614    563  -1144       C  
ATOM   2008  CG1 VAL B 242      -5.860 -43.247  15.919  1.00 51.76           C  
ANISOU 2008  CG1 VAL B 242    12281   1670   5714  -1157   -169  -1663       C  
ATOM   2009  CG2 VAL B 242      -7.269 -41.699  17.355  1.00 51.52           C  
ANISOU 2009  CG2 VAL B 242    11204   2941   5430  -1051    543    440       C  
ATOM   2010  N   ASP B 243      -4.816 -45.778  18.395  1.00 60.82           N  
ANISOU 2010  N   ASP B 243    12343   3607   7159    254   2182    -39       N  
ATOM   2011  CA  ASP B 243      -4.560 -47.209  18.164  1.00 68.79           C  
ANISOU 2011  CA  ASP B 243    14007   3747   8382     17   1838  -1186       C  
ATOM   2012  C   ASP B 243      -5.557 -48.062  18.969  1.00 71.81           C  
ANISOU 2012  C   ASP B 243    13916   4671   8697    -45   2011  -1121       C  
ATOM   2013  O   ASP B 243      -5.694 -47.852  20.182  1.00 73.91           O  
ANISOU 2013  O   ASP B 243    14332   5172   8577    624   2103   -648       O  
ATOM   2014  CB  ASP B 243      -3.104 -47.573  18.516  1.00 74.19           C  
ANISOU 2014  CB  ASP B 243    13827   4597   9762     16   1996   -883       C  
ATOM   2015  CG  ASP B 243      -2.737 -49.022  18.144  1.00 82.59           C  
ANISOU 2015  CG  ASP B 243    15319   5413  10645   1526   2112   -903       C  
ATOM   2016  OD1 ASP B 243      -3.104 -49.955  18.896  1.00 87.90           O  
ANISOU 2016  OD1 ASP B 243    16358   5606  11430   1630   2281   -321       O  
ATOM   2017  OD2 ASP B 243      -2.061 -49.230  17.109  1.00 87.37           O  
ANISOU 2017  OD2 ASP B 243    16305   5986  10905   2378   2296  -1959       O  
ATOM   2018  N   PRO B 244      -6.255 -49.016  18.296  1.00 74.94           N  
ANISOU 2018  N   PRO B 244    14676   4583   9213   -266   1848  -1285       N  
ATOM   2019  CA  PRO B 244      -7.288 -49.879  18.901  1.00 76.60           C  
ANISOU 2019  CA  PRO B 244    14793   5093   9216   -258   1832   -878       C  
ATOM   2020  C   PRO B 244      -6.905 -50.554  20.224  1.00 81.99           C  
ANISOU 2020  C   PRO B 244    15346   5070  10734    301   1639    557       C  
ATOM   2021  O   PRO B 244      -7.774 -50.742  21.078  1.00 84.71           O  
ANISOU 2021  O   PRO B 244    15364   5920  10899    932   1363   2420       O  
ATOM   2022  CB  PRO B 244      -7.552 -50.946  17.820  1.00 79.31           C  
ANISOU 2022  CB  PRO B 244    15017   4994  10121   -105   1539  -1306       C  
ATOM   2023  CG  PRO B 244      -6.511 -50.736  16.766  1.00 79.41           C  
ANISOU 2023  CG  PRO B 244    15417   4679  10074   -802   1575  -1750       C  
ATOM   2024  CD  PRO B 244      -6.136 -49.290  16.852  1.00 76.01           C  
ANISOU 2024  CD  PRO B 244    14973   4555   9351   -584   1652  -1650       C  
ATOM   2025  N   GLU B 245      -5.626 -50.898  20.387  1.00 76.73           N  
ANISOU 2025  N   GLU B 245    15354   3630  10170    387   2253    724       N  
ATOM   2026  CA  GLU B 245      -5.131 -51.540  21.611  1.00 81.56           C  
ANISOU 2026  CA  GLU B 245    15796   5222   9971    651   1641    273       C  
ATOM   2027  C   GLU B 245      -4.904 -50.574  22.781  1.00 79.03           C  
ANISOU 2027  C   GLU B 245    15957   5031   9039   1163   1764    724       C  
ATOM   2028  O   GLU B 245      -5.082 -50.959  23.935  1.00 80.01           O  
ANISOU 2028  O   GLU B 245    17036   4051   9312   3085    939   1968       O  
ATOM   2029  CB  GLU B 245      -3.857 -52.349  21.330  1.00 79.43           C  
ANISOU 2029  CB  GLU B 245    15786   5648   8745   1238   1189   1808       C  
ATOM   2030  N   THR B 246      -4.530 -49.328  22.477  1.00 78.07           N  
ANISOU 2030  N   THR B 246    15844   4508   9310   1218   1832   -402       N  
ATOM   2031  CA  THR B 246      -4.122 -48.350  23.498  1.00 75.69           C  
ANISOU 2031  CA  THR B 246    14303   4858   9595    788   1242   -273       C  
ATOM   2032  C   THR B 246      -4.905 -47.017  23.462  1.00 70.86           C  
ANISOU 2032  C   THR B 246    13427   5218   8278    760    725      9       C  
ATOM   2033  O   THR B 246      -4.406 -45.979  23.934  1.00 65.70           O  
ANISOU 2033  O   THR B 246    13162   5195   6603    171   1475    862       O  
ATOM   2034  CB  THR B 246      -2.601 -48.083  23.412  1.00 72.84           C  
ANISOU 2034  CB  THR B 246    13722   4163   9791   1571    865  -1991       C  
ATOM   2035  N   HIS B 247      -6.133 -47.055  22.937  1.00 65.27           N  
ANISOU 2035  N   HIS B 247    12849   3849   8101     57   1164   -552       N  
ATOM   2036  CA  HIS B 247      -6.927 -45.835  22.714  1.00 62.87           C  
ANISOU 2036  CA  HIS B 247    12257   4214   7413    -32   1051    -87       C  
ATOM   2037  C   HIS B 247      -7.460 -45.187  23.998  1.00 57.71           C  
ANISOU 2037  C   HIS B 247    11844   3371   6712   -432    511    302       C  
ATOM   2038  O   HIS B 247      -7.857 -45.871  24.943  1.00 60.24           O  
ANISOU 2038  O   HIS B 247    11861   3928   7097    -51    -59   1265       O  
ATOM   2039  CB  HIS B 247      -8.063 -46.068  21.698  1.00 60.55           C  
ANISOU 2039  CB  HIS B 247    12496   2906   7603   -199   1025   -503       C  
ATOM   2040  CG  HIS B 247      -9.157 -46.958  22.199  1.00 71.32           C  
ANISOU 2040  CG  HIS B 247    13050   4403   9644  -1140    988    -98       C  
ATOM   2041  ND1 HIS B 247      -9.172 -48.320  21.977  1.00 76.31           N  
ANISOU 2041  ND1 HIS B 247    13732   4675  10585   -492   1064   -930       N  
ATOM   2042  CD2 HIS B 247     -10.274 -46.682  22.916  1.00 71.01           C  
ANISOU 2042  CD2 HIS B 247    13361   4009   9610   -489    687  -1106       C  
ATOM   2043  CE1 HIS B 247     -10.249 -48.844  22.538  1.00 79.87           C  
ANISOU 2043  CE1 HIS B 247    14463   4533  11350  -1129   1053   -255       C  
ATOM   2044  NE2 HIS B 247     -10.934 -47.871  23.114  1.00 77.90           N  
ANISOU 2044  NE2 HIS B 247    13451   5668  10477  -1410   2220     -7       N  
ATOM   2045  N   CYS B 248      -7.561 -43.857  23.979  1.00 51.65           N  
ANISOU 2045  N   CYS B 248    10943   3379   5300   -541   -194   -273       N  
ATOM   2046  CA  CYS B 248      -8.087 -43.094  25.115  1.00 50.60           C  
ANISOU 2046  CA  CYS B 248    10428   3259   5535    -82    281    304       C  
ATOM   2047  C   CYS B 248      -8.157 -41.582  24.848  1.00 44.57           C  
ANISOU 2047  C   CYS B 248     9495   3288   4150   -518     71    241       C  
ATOM   2048  O   CYS B 248      -7.149 -40.967  24.500  1.00 45.09           O  
ANISOU 2048  O   CYS B 248     9767   2867   4497   -676      5    505       O  
ATOM   2049  CB  CYS B 248      -7.255 -43.366  26.371  1.00 54.98           C  
ANISOU 2049  CB  CYS B 248    11655   3419   5812    412   -329     38       C  
ATOM   2050  SG  CYS B 248      -5.505 -42.936  26.215  1.00 70.80           S  
ANISOU 2050  SG  CYS B 248    11703   6449   8748   1220  -1376    207       S  
ATOM   2051  N   HIS B 249      -9.340 -40.985  25.012  1.00 44.47           N  
ANISOU 2051  N   HIS B 249     8648   3546   4700   -768     -1    536       N  
ATOM   2052  CA  HIS B 249      -9.496 -39.553  24.800  1.00 43.70           C  
ANISOU 2052  CA  HIS B 249     8739   3529   4334   -753   -491    137       C  
ATOM   2053  C   HIS B 249      -8.460 -38.829  25.652  1.00 39.44           C  
ANISOU 2053  C   HIS B 249     8162   3283   3541   -438   -112    241       C  
ATOM   2054  O   HIS B 249      -8.079 -39.325  26.721  1.00 39.56           O  
ANISOU 2054  O   HIS B 249     8088   3300   3639    184    213    400       O  
ATOM   2055  CB  HIS B 249     -10.906 -39.078  25.154  1.00 44.49           C  
ANISOU 2055  CB  HIS B 249     9117   3511   4277   -634   -366    -97       C  
ATOM   2056  CG  HIS B 249     -11.978 -39.605  24.250  1.00 51.09           C  
ANISOU 2056  CG  HIS B 249     9667   4422   5320  -1732   -497   -243       C  
ATOM   2057  ND1 HIS B 249     -13.314 -39.563  24.588  1.00 50.17           N  
ANISOU 2057  ND1 HIS B 249    10011   4451   4599  -1700    117    433       N  
ATOM   2058  CD2 HIS B 249     -11.918 -40.192  23.029  1.00 56.11           C  
ANISOU 2058  CD2 HIS B 249    10190   5959   5170  -1559    -54   -393       C  
ATOM   2059  CE1 HIS B 249     -14.030 -40.097  23.613  1.00 57.05           C  
ANISOU 2059  CE1 HIS B 249    10587   5764   5324  -1897   -310   -169       C  
ATOM   2060  NE2 HIS B 249     -13.206 -40.489  22.657  1.00 56.15           N  
ANISOU 2060  NE2 HIS B 249    10709   5474   5148  -1881   -510   -531       N  
ATOM   2061  N   ALA B 250      -8.011 -37.669  25.169  1.00 37.85           N  
ANISOU 2061  N   ALA B 250     7717   2795   3869   -349   -289   -103       N  
ATOM   2062  CA  ALA B 250      -6.955 -36.861  25.811  1.00 39.71           C  
ANISOU 2062  CA  ALA B 250     7686   3116   4286   -483   -860    405       C  
ATOM   2063  C   ALA B 250      -7.068 -36.754  27.340  1.00 40.99           C  
ANISOU 2063  C   ALA B 250     7847   3421   4304   -844   -602    745       C  
ATOM   2064  O   ALA B 250      -6.062 -36.913  28.048  1.00 40.46           O  
ANISOU 2064  O   ALA B 250     7691   3548   4131  -1006   -410    942       O  
ATOM   2065  CB  ALA B 250      -6.888 -35.471  25.176  1.00 36.10           C  
ANISOU 2065  CB  ALA B 250     6997   2762   3954   -448  -1247    -31       C  
ATOM   2066  N   GLU B 251      -8.290 -36.507  27.825  1.00 42.19           N  
ANISOU 2066  N   GLU B 251     7678   3122   5229   -650   -645   1023       N  
ATOM   2067  CA  GLU B 251      -8.616 -36.446  29.265  1.00 45.96           C  
ANISOU 2067  CA  GLU B 251     8298   3768   5393   -604   -415    824       C  
ATOM   2068  C   GLU B 251      -8.227 -37.731  30.001  1.00 43.67           C  
ANISOU 2068  C   GLU B 251     8188   3574   4828   -656   -565    504       C  
ATOM   2069  O   GLU B 251      -7.562 -37.667  31.036  1.00 41.42           O  
ANISOU 2069  O   GLU B 251     8440   2761   4534   -217   -375    142       O  
ATOM   2070  CB  GLU B 251     -10.108 -36.140  29.502  1.00 47.48           C  
ANISOU 2070  CB  GLU B 251     8383   4385   5271   -295   -344    824       C  
ATOM   2071  CG  GLU B 251     -10.660 -34.923  28.770  1.00 50.74           C  
ANISOU 2071  CG  GLU B 251     8635   4401   6241   -222   -434   1053       C  
ATOM   2072  CD  GLU B 251     -11.230 -35.246  27.389  1.00 57.00           C  
ANISOU 2072  CD  GLU B 251     9213   5508   6936   -405   -729     56       C  
ATOM   2073  OE1 GLU B 251     -10.655 -36.070  26.647  1.00 54.85           O  
ANISOU 2073  OE1 GLU B 251     9164   5586   6088   -303   -597    467       O  
ATOM   2074  OE2 GLU B 251     -12.267 -34.659  27.031  1.00 61.66           O  
ANISOU 2074  OE2 GLU B 251     9944   6428   7055   -371  -1480    758       O  
ATOM   2075  N   ARG B 252      -8.638 -38.876  29.448  1.00 43.39           N  
ANISOU 2075  N   ARG B 252     8137   3147   5201  -1003    -78    791       N  
ATOM   2076  CA  ARG B 252      -8.303 -40.199  29.974  1.00 48.49           C  
ANISOU 2076  CA  ARG B 252     9507   3374   5540   -406   -645    642       C  
ATOM   2077  C   ARG B 252      -6.798 -40.448  29.955  1.00 51.65           C  
ANISOU 2077  C   ARG B 252     9434   4170   6019   -976   -734    311       C  
ATOM   2078  O   ARG B 252      -6.244 -40.963  30.933  1.00 54.88           O  
ANISOU 2078  O   ARG B 252    10351   4121   6378   -513    -95   1181       O  
ATOM   2079  CB  ARG B 252      -8.977 -41.288  29.143  1.00 60.36           C  
ANISOU 2079  CB  ARG B 252    11024   3687   8224  -1687  -1031    364       C  
ATOM   2080  CG  ARG B 252     -10.432 -41.580  29.460  1.00 72.08           C  
ANISOU 2080  CG  ARG B 252    11241   5851  10295   -939   -449    795       C  
ATOM   2081  CD  ARG B 252     -10.888 -42.822  28.697  1.00 88.08           C  
ANISOU 2081  CD  ARG B 252    13917   6393  13154  -1757  -1045    -57       C  
ATOM   2082  NE  ARG B 252     -10.119 -44.024  29.056  1.00 89.70           N  
ANISOU 2082  NE  ARG B 252    16206   6435  11439  -1856  -1274   2147       N  
ATOM   2083  CZ  ARG B 252     -10.037 -45.139  28.324  1.00 94.16           C  
ANISOU 2083  CZ  ARG B 252    16317   7305  12154  -1061  -1907   1507       C  
ATOM   2084  NH1 ARG B 252      -9.304 -46.155  28.761  1.00 99.38           N  
ANISOU 2084  NH1 ARG B 252    15878   7393  14489   -749   -655   2001       N  
ATOM   2085  NH2 ARG B 252     -10.674 -45.256  27.162  1.00 91.06           N  
ANISOU 2085  NH2 ARG B 252    15766   6244  12587   -774  -2459   1780       N  
ATOM   2086  N   CYS B 253      -6.152 -40.092  28.838  1.00 50.90           N  
ANISOU 2086  N   CYS B 253     9345   4122   5870  -1206   -974    331       N  
ATOM   2087  CA  CYS B 253      -4.699 -40.247  28.670  1.00 51.58           C  
ANISOU 2087  CA  CYS B 253     9453   4521   5622   -385  -1199    -40       C  
ATOM   2088  C   CYS B 253      -3.920 -39.410  29.694  1.00 43.52           C  
ANISOU 2088  C   CYS B 253     8793   3101   4639     71   -735    485       C  
ATOM   2089  O   CYS B 253      -2.885 -39.850  30.190  1.00 43.97           O  
ANISOU 2089  O   CYS B 253     9129   3498   4078    349   -889    -52       O  
ATOM   2090  CB  CYS B 253      -4.246 -39.899  27.243  1.00 56.79           C  
ANISOU 2090  CB  CYS B 253    10563   4829   6184    240   -549    572       C  
ATOM   2091  SG  CYS B 253      -5.249 -40.555  25.879  1.00 70.01           S  
ANISOU 2091  SG  CYS B 253    12035   6810   7753    -48  -1751    568       S  
ATOM   2092  N   PHE B 254      -4.416 -38.213  30.009  1.00 42.92           N  
ANISOU 2092  N   PHE B 254     8616   3234   4455    -95   -824    156       N  
ATOM   2093  CA  PHE B 254      -3.831 -37.416  31.090  1.00 42.21           C  
ANISOU 2093  CA  PHE B 254     8626   3045   4365    134   -959    277       C  
ATOM   2094  C   PHE B 254      -3.985 -38.143  32.428  1.00 43.25           C  
ANISOU 2094  C   PHE B 254     8944   2847   4641     25   -835    403       C  
ATOM   2095  O   PHE B 254      -3.011 -38.268  33.178  1.00 46.77           O  
ANISOU 2095  O   PHE B 254     9464   3320   4986    -59  -1312   -159       O  
ATOM   2096  CB  PHE B 254      -4.419 -35.995  31.177  1.00 38.34           C  
ANISOU 2096  CB  PHE B 254     8180   2794   3592   -136  -1128    600       C  
ATOM   2097  CG  PHE B 254      -3.892 -35.206  32.347  1.00 37.31           C  
ANISOU 2097  CG  PHE B 254     8269   2091   3814     91   -853    404       C  
ATOM   2098  CD1 PHE B 254      -4.479 -35.333  33.625  1.00 38.62           C  
ANISOU 2098  CD1 PHE B 254     8562   1927   4182     87   -337     49       C  
ATOM   2099  CD2 PHE B 254      -2.781 -34.373  32.199  1.00 36.42           C  
ANISOU 2099  CD2 PHE B 254     8142   2276   3420     71   -733    590       C  
ATOM   2100  CE1 PHE B 254      -3.974 -34.637  34.719  1.00 37.09           C  
ANISOU 2100  CE1 PHE B 254     8276   1845   3970    603   -229    -40       C  
ATOM   2101  CE2 PHE B 254      -2.282 -33.663  33.286  1.00 39.51           C  
ANISOU 2101  CE2 PHE B 254     8317   2745   3949   -280   -916    350       C  
ATOM   2102  CZ  PHE B 254      -2.877 -33.795  34.544  1.00 40.13           C  
ANISOU 2102  CZ  PHE B 254     8039   2858   4348    344   -327   -512       C  
ATOM   2103  N   LEU B 255      -5.205 -38.607  32.714  1.00 43.85           N  
ANISOU 2103  N   LEU B 255     8933   2935   4792   -159   -928    688       N  
ATOM   2104  CA  LEU B 255      -5.506 -39.324  33.953  1.00 47.90           C  
ANISOU 2104  CA  LEU B 255     9379   4037   4783     96   -814   1067       C  
ATOM   2105  C   LEU B 255      -4.635 -40.552  34.168  1.00 49.27           C  
ANISOU 2105  C   LEU B 255     9959   3594   5164    151   -585    842       C  
ATOM   2106  O   LEU B 255      -4.079 -40.713  35.254  1.00 54.18           O  
ANISOU 2106  O   LEU B 255    10609   4544   5432    893   -804   1260       O  
ATOM   2107  CB  LEU B 255      -6.989 -39.696  34.051  1.00 51.23           C  
ANISOU 2107  CB  LEU B 255     9582   4641   5240   -327   -762   1238       C  
ATOM   2108  CG  LEU B 255      -8.012 -38.608  34.409  1.00 56.27           C  
ANISOU 2108  CG  LEU B 255    10131   5163   6086   -364    185    551       C  
ATOM   2109  CD1 LEU B 255      -9.337 -39.273  34.758  1.00 58.19           C  
ANISOU 2109  CD1 LEU B 255    10485   5161   6463   -424   1046    575       C  
ATOM   2110  CD2 LEU B 255      -7.557 -37.695  35.548  1.00 54.32           C  
ANISOU 2110  CD2 LEU B 255    10625   4398   5613   -488    442   1044       C  
ATOM   2111  N   SER B 256      -4.505 -41.394  33.138  1.00 48.70           N  
ANISOU 2111  N   SER B 256     9810   3312   5381   -190   -820    669       N  
ATOM   2112  CA  SER B 256      -3.640 -42.586  33.197  1.00 50.00           C  
ANISOU 2112  CA  SER B 256    10308   3090   5598   -151   -880    590       C  
ATOM   2113  C   SER B 256      -2.191 -42.221  33.511  1.00 49.38           C  
ANISOU 2113  C   SER B 256    10131   3470   5161    775  -1132    807       C  
ATOM   2114  O   SER B 256      -1.595 -42.807  34.408  1.00 54.58           O  
ANISOU 2114  O   SER B 256    11400   3703   5635   1149  -1256   1292       O  
ATOM   2115  CB  SER B 256      -3.695 -43.376  31.890  1.00 49.91           C  
ANISOU 2115  CB  SER B 256    10675   2331   5958   -807   -980    488       C  
ATOM   2116  OG  SER B 256      -5.019 -43.762  31.595  1.00 59.68           O  
ANISOU 2116  OG  SER B 256    10745   3989   7941   -977   -815    654       O  
ATOM   2117  N   TRP B 257      -1.649 -41.243  32.779  1.00 47.91           N  
ANISOU 2117  N   TRP B 257     9746   2991   5466    350   -882     83       N  
ATOM   2118  CA  TRP B 257      -0.280 -40.763  32.977  1.00 46.52           C  
ANISOU 2118  CA  TRP B 257     9367   3493   4812    804  -1170    408       C  
ATOM   2119  C   TRP B 257      -0.052 -40.258  34.401  1.00 48.42           C  
ANISOU 2119  C   TRP B 257     9756   3882   4757    711  -1161    403       C  
ATOM   2120  O   TRP B 257       0.933 -40.626  35.035  1.00 54.41           O  
ANISOU 2120  O   TRP B 257     9992   5024   5656    564  -1470    847       O  
ATOM   2121  CB  TRP B 257       0.066 -39.671  31.958  1.00 43.46           C  
ANISOU 2121  CB  TRP B 257     8637   3509   4366    765   -948    103       C  
ATOM   2122  CG  TRP B 257       1.326 -38.908  32.285  1.00 44.94           C  
ANISOU 2122  CG  TRP B 257     8727   3825   4522    822  -1312     79       C  
ATOM   2123  CD1 TRP B 257       2.615 -39.334  32.106  1.00 43.70           C  
ANISOU 2123  CD1 TRP B 257     8742   4027   3833    877  -1424    249       C  
ATOM   2124  CD2 TRP B 257       1.414 -37.593  32.854  1.00 43.10           C  
ANISOU 2124  CD2 TRP B 257     8504   3654   4217    726  -1396    334       C  
ATOM   2125  NE1 TRP B 257       3.497 -38.367  32.526  1.00 44.40           N  
ANISOU 2125  NE1 TRP B 257     8766   3802   4301    786  -1206    417       N  
ATOM   2126  CE2 TRP B 257       2.789 -37.288  32.989  1.00 45.25           C  
ANISOU 2126  CE2 TRP B 257     8587   4032   4572    735  -1186    197       C  
ATOM   2127  CE3 TRP B 257       0.464 -36.643  33.267  1.00 42.45           C  
ANISOU 2127  CE3 TRP B 257     8331   3530   4266    600  -1526    425       C  
ATOM   2128  CZ2 TRP B 257       3.245 -36.060  33.510  1.00 46.35           C  
ANISOU 2128  CZ2 TRP B 257     8728   4434   4448    751  -1379   -144       C  
ATOM   2129  CZ3 TRP B 257       0.916 -35.418  33.792  1.00 42.11           C  
ANISOU 2129  CZ3 TRP B 257     8164   3967   3869    482  -1690    317       C  
ATOM   2130  CH2 TRP B 257       2.297 -35.145  33.911  1.00 42.06           C  
ANISOU 2130  CH2 TRP B 257     8183   4108   3690    460  -1560    325       C  
ATOM   2131  N   PHE B 258      -0.973 -39.431  34.890  1.00 49.24           N  
ANISOU 2131  N   PHE B 258     9595   4233   4879    783  -1176    452       N  
ATOM   2132  CA  PHE B 258      -0.884 -38.839  36.226  1.00 52.28           C  
ANISOU 2132  CA  PHE B 258    10388   4877   4597    564  -1309    673       C  
ATOM   2133  C   PHE B 258      -0.894 -39.898  37.329  1.00 54.33           C  
ANISOU 2133  C   PHE B 258    10958   4656   5029    614   -840    794       C  
ATOM   2134  O   PHE B 258      -0.113 -39.810  38.279  1.00 59.86           O  
ANISOU 2134  O   PHE B 258    11633   6305   4805     79   -704     -8       O  
ATOM   2135  CB  PHE B 258      -2.008 -37.811  36.423  1.00 55.00           C  
ANISOU 2135  CB  PHE B 258    10635   4927   5333    497   -973    304       C  
ATOM   2136  CG  PHE B 258      -2.013 -37.153  37.775  1.00 59.13           C  
ANISOU 2136  CG  PHE B 258    11316   6144   5005    549   -919    370       C  
ATOM   2137  CD1 PHE B 258      -1.111 -36.132  38.076  1.00 60.04           C  
ANISOU 2137  CD1 PHE B 258    11515   6034   5264    627   -944    360       C  
ATOM   2138  CD2 PHE B 258      -2.929 -37.543  38.750  1.00 64.13           C  
ANISOU 2138  CD2 PHE B 258    11521   7043   5800    880   -297    637       C  
ATOM   2139  CE1 PHE B 258      -1.117 -35.519  39.326  1.00 62.30           C  
ANISOU 2139  CE1 PHE B 258    11946   6456   5270    558  -1214    213       C  
ATOM   2140  CE2 PHE B 258      -2.938 -36.933  40.003  1.00 69.35           C  
ANISOU 2140  CE2 PHE B 258    11844   8148   6358    -22   -702   -192       C  
ATOM   2141  CZ  PHE B 258      -2.033 -35.919  40.290  1.00 64.79           C  
ANISOU 2141  CZ  PHE B 258    12192   7007   5418    459   -741   -270       C  
ATOM   2142  N   CYS B 259      -1.758 -40.901  37.182  1.00 54.93           N  
ANISOU 2142  N   CYS B 259    10823   5047   4999    511  -1685    974       N  
ATOM   2143  CA  CYS B 259      -1.876 -41.998  38.153  1.00 61.57           C  
ANISOU 2143  CA  CYS B 259    12152   5516   5724    376  -1075   1452       C  
ATOM   2144  C   CYS B 259      -0.686 -42.953  38.180  1.00 64.55           C  
ANISOU 2144  C   CYS B 259    12768   5404   6354    753  -1316   1400       C  
ATOM   2145  O   CYS B 259      -0.249 -43.364  39.254  1.00 68.07           O  
ANISOU 2145  O   CYS B 259    13102   6080   6679    492  -1383   1882       O  
ATOM   2146  CB  CYS B 259      -3.164 -42.780  37.920  1.00 65.10           C  
ANISOU 2146  CB  CYS B 259    12373   5926   6434   -128   -944   1722       C  
ATOM   2147  SG  CYS B 259      -4.633 -41.799  38.275  1.00 71.63           S  
ANISOU 2147  SG  CYS B 259    13233   6801   7182    -78    627   1608       S  
ATOM   2148  N   ASP B 260      -0.172 -43.300  37.002  1.00 67.85           N  
ANISOU 2148  N   ASP B 260    13222   5997   6557    971  -1397    905       N  
ATOM   2149  CA  ASP B 260       0.903 -44.286  36.871  1.00 71.22           C  
ANISOU 2149  CA  ASP B 260    13436   5855   7767   1229  -1994   1223       C  
ATOM   2150  C   ASP B 260       2.291 -43.717  37.177  1.00 67.29           C  
ANISOU 2150  C   ASP B 260    13526   5869   6172   1468  -2146    715       C  
ATOM   2151  O   ASP B 260       3.118 -44.394  37.790  1.00 70.68           O  
ANISOU 2151  O   ASP B 260    13954   5883   7016   1673  -2633    493       O  
ATOM   2152  CB  ASP B 260       0.891 -44.916  35.468  1.00 77.48           C  
ANISOU 2152  CB  ASP B 260    14492   6461   8483   1346  -1911    429       C  
ATOM   2153  CG  ASP B 260      -0.406 -45.669  35.155  1.00 84.09           C  
ANISOU 2153  CG  ASP B 260    15209   6959   9782    426  -1497   1081       C  
ATOM   2154  OD1 ASP B 260      -1.146 -46.055  36.089  1.00 90.09           O  
ANISOU 2154  OD1 ASP B 260    17003   7307   9920   -311   -825   1258       O  
ATOM   2155  OD2 ASP B 260      -0.683 -45.879  33.955  1.00 90.86           O  
ANISOU 2155  OD2 ASP B 260    16326   7969  10225    989  -2676   1035       O  
ATOM   2156  N   ASP B 261       2.537 -42.480  36.747  1.00 67.52           N  
ANISOU 2156  N   ASP B 261    13184   5987   6483   1156  -2107    657       N  
ATOM   2157  CA  ASP B 261       3.875 -41.883  36.802  1.00 67.61           C  
ANISOU 2157  CA  ASP B 261    12874   6161   6654   1367  -2123    790       C  
ATOM   2158  C   ASP B 261       4.047 -40.827  37.897  1.00 65.45           C  
ANISOU 2158  C   ASP B 261    12606   6516   5746   1938  -1873   1004       C  
ATOM   2159  O   ASP B 261       5.131 -40.707  38.472  1.00 73.21           O  
ANISOU 2159  O   ASP B 261    12260   7807   7748   1594  -1673    494       O  
ATOM   2160  CB  ASP B 261       4.245 -41.266  35.441  1.00 68.14           C  
ANISOU 2160  CB  ASP B 261    12566   6596   6726   1708  -1789    808       C  
ATOM   2161  CG  ASP B 261       4.309 -42.292  34.301  1.00 75.44           C  
ANISOU 2161  CG  ASP B 261    13572   6994   8098   1827  -1603     75       C  
ATOM   2162  OD1 ASP B 261       3.750 -43.406  34.417  1.00 77.24           O  
ANISOU 2162  OD1 ASP B 261    14343   7224   7779   1491   -675    529       O  
ATOM   2163  OD2 ASP B 261       4.921 -41.966  33.260  1.00 80.53           O  
ANISOU 2163  OD2 ASP B 261    13393   8450   8755   2318  -1607   1092       O  
ATOM   2164  N   ILE B 262       2.985 -40.074  38.186  1.00 62.40           N  
ANISOU 2164  N   ILE B 262    12239   6638   4831   1787  -2008    842       N  
ATOM   2165  CA  ILE B 262       3.119 -38.816  38.939  1.00 62.29           C  
ANISOU 2165  CA  ILE B 262    11930   6541   5194   1940  -1705    934       C  
ATOM   2166  C   ILE B 262       2.601 -38.865  40.380  1.00 64.71           C  
ANISOU 2166  C   ILE B 262    12190   6923   5473   2202  -1304    641       C  
ATOM   2167  O   ILE B 262       3.338 -38.515  41.310  1.00 65.42           O  
ANISOU 2167  O   ILE B 262    11658   7029   6166   3042  -1544    178       O  
ATOM   2168  CB  ILE B 262       2.503 -37.611  38.160  1.00 60.12           C  
ANISOU 2168  CB  ILE B 262    11574   6246   5022   1756  -1250    935       C  
ATOM   2169  CG1 ILE B 262       3.034 -37.539  36.710  1.00 54.95           C  
ANISOU 2169  CG1 ILE B 262    10657   5625   4596   1775  -1709    309       C  
ATOM   2170  CG2 ILE B 262       2.698 -36.290  38.909  1.00 61.81           C  
ANISOU 2170  CG2 ILE B 262    11872   7082   4529   1646   -801    255       C  
ATOM   2171  CD1 ILE B 262       4.549 -37.468  36.545  1.00 53.25           C  
ANISOU 2171  CD1 ILE B 262    10747   5356   4127   1675  -1390    456       C  
ATOM   2172  N   LEU B 263       1.350 -39.301  40.547  1.00 61.35           N  
ANISOU 2172  N   LEU B 263    12420   5734   5155   1977  -1538   1631       N  
ATOM   2173  CA  LEU B 263       0.651 -39.281  41.835  1.00 64.72           C  
ANISOU 2173  CA  LEU B 263    13047   6260   5284   1810  -1167   1328       C  
ATOM   2174  C   LEU B 263       1.444 -39.951  42.964  1.00 69.02           C  
ANISOU 2174  C   LEU B 263    13382   6974   5867   2297  -1281   1680       C  
ATOM   2175  O   LEU B 263       1.805 -41.126  42.875  1.00 70.24           O  
ANISOU 2175  O   LEU B 263    13074   7021   6592   2929  -1448   3577       O  
ATOM   2176  CB  LEU B 263      -0.749 -39.900  41.690  1.00 72.30           C  
ANISOU 2176  CB  LEU B 263    13080   7458   6931   1815   -909    428       C  
ATOM   2177  CG  LEU B 263      -1.720 -39.946  42.878  1.00 79.86           C  
ANISOU 2177  CG  LEU B 263    13570   8912   7860   1504   -195    314       C  
ATOM   2178  CD1 LEU B 263      -2.245 -38.563  43.247  1.00 83.44           C  
ANISOU 2178  CD1 LEU B 263    13543   8738   9419   1065   -820   -227       C  
ATOM   2179  CD2 LEU B 263      -2.873 -40.889  42.566  1.00 78.19           C  
ANISOU 2179  CD2 LEU B 263    14420   6668   8620   1315    968    634       C  
ATOM   2180  N   SER B 264       1.721 -39.164  44.003  1.00 75.62           N  
ANISOU 2180  N   SER B 264    14430   8030   6270   1736  -1521   1319       N  
ATOM   2181  CA  SER B 264       2.456 -39.592  45.194  1.00 81.13           C  
ANISOU 2181  CA  SER B 264    15015   9190   6618   2513  -1559   1799       C  
ATOM   2182  C   SER B 264       1.623 -39.311  46.457  1.00 83.36           C  
ANISOU 2182  C   SER B 264    15567   9956   6149   2210  -1536   2095       C  
ATOM   2183  O   SER B 264       0.800 -38.386  46.446  1.00 82.42           O  
ANISOU 2183  O   SER B 264    15692   9805   5817   2253  -2979   2233       O  
ATOM   2184  CB  SER B 264       3.804 -38.868  45.264  1.00 88.51           C  
ANISOU 2184  CB  SER B 264    15348   9669   8610   2199  -1203   2537       C  
ATOM   2185  OG  SER B 264       4.658 -39.289  44.215  1.00 90.45           O  
ANISOU 2185  OG  SER B 264    16456   7843  10066   2905   -781   2034       O  
ATOM   2186  N   PRO B 265       1.833 -40.098  47.544  1.00 86.88           N  
ANISOU 2186  N   PRO B 265    16628   9933   6448   2478  -1599   2302       N  
ATOM   2187  CA  PRO B 265       0.974 -40.016  48.744  1.00 89.35           C  
ANISOU 2187  CA  PRO B 265    16300  10361   7288   2772  -1218   2285       C  
ATOM   2188  C   PRO B 265       0.883 -38.644  49.435  1.00 88.57           C  
ANISOU 2188  C   PRO B 265    15586  11011   7054   2560  -1314   1570       C  
ATOM   2189  O   PRO B 265      -0.224 -38.135  49.631  1.00 92.41           O  
ANISOU 2189  O   PRO B 265    15707  11929   7476   2437    -73   1472       O  
ATOM   2190  CB  PRO B 265       1.590 -41.058  49.696  1.00 92.45           C  
ANISOU 2190  CB  PRO B 265    17370  10178   7579   2258   -327   3374       C  
ATOM   2191  CG  PRO B 265       2.978 -41.281  49.190  1.00 88.99           C  
ANISOU 2191  CG  PRO B 265    17107   9598   7107   2853   -986   3928       C  
ATOM   2192  CD  PRO B 265       2.860 -41.148  47.701  1.00 87.12           C  
ANISOU 2192  CD  PRO B 265    16547   9785   6767   2451   -936   2352       C  
ATOM   2193  N   ASN B 266       2.029 -38.053  49.771  1.00 83.64           N  
ANISOU 2193  N   ASN B 266    16070  10133   5573   2819  -2381   1716       N  
ATOM   2194  CA  ASN B 266       2.086 -36.871  50.639  1.00 85.81           C  
ANISOU 2194  CA  ASN B 266    16490  10230   5881   2246  -1734   1616       C  
ATOM   2195  C   ASN B 266       2.253 -35.567  49.855  1.00 81.89           C  
ANISOU 2195  C   ASN B 266    15597  10294   5223   1477  -1879   1195       C  
ATOM   2196  O   ASN B 266       3.008 -34.665  50.247  1.00 81.02           O  
ANISOU 2196  O   ASN B 266    17513   9802   3469   1887   -722  -1675       O  
ATOM   2197  CB  ASN B 266       3.196 -37.050  51.681  1.00 93.71           C  
ANISOU 2197  CB  ASN B 266    17088  11769   6747   2490  -2319   2214       C  
ATOM   2198  CG  ASN B 266       3.054 -38.343  52.463  1.00100.69           C  
ANISOU 2198  CG  ASN B 266    17824  12646   7786   1889  -1226   2970       C  
ATOM   2199  OD1 ASN B 266       2.266 -38.429  53.406  1.00104.64           O  
ANISOU 2199  OD1 ASN B 266    19132  12986   7640    893   -848   3949       O  
ATOM   2200  ND2 ASN B 266       3.817 -39.361  52.069  1.00102.27           N  
ANISOU 2200  ND2 ASN B 266    18537  10990   9330   2300  -1655   4379       N  
ATOM   2201  N   THR B 267       1.511 -35.475  48.755  1.00 77.63           N  
ANISOU 2201  N   THR B 267    15028   9627   4842   1783  -1410   1183       N  
ATOM   2202  CA  THR B 267       1.669 -34.406  47.782  1.00 73.77           C  
ANISOU 2202  CA  THR B 267    14341   8474   5213   1772  -1609    815       C  
ATOM   2203  C   THR B 267       0.297 -33.857  47.385  1.00 69.79           C  
ANISOU 2203  C   THR B 267    13707   8336   4471   1629   -931   -390       C  
ATOM   2204  O   THR B 267      -0.645 -34.623  47.164  1.00 70.13           O  
ANISOU 2204  O   THR B 267    14111   7475   5060   1598   -458    -41       O  
ATOM   2205  CB  THR B 267       2.432 -34.918  46.532  1.00 73.59           C  
ANISOU 2205  CB  THR B 267    14112   8142   5705   1649  -1586    589       C  
ATOM   2206  OG1 THR B 267       3.553 -35.721  46.934  1.00 77.62           O  
ANISOU 2206  OG1 THR B 267    14469   9462   5560   1163  -3336   1456       O  
ATOM   2207  CG2 THR B 267       2.936 -33.767  45.676  1.00 73.09           C  
ANISOU 2207  CG2 THR B 267    14413   8752   4605   1504  -1270    424       C  
ATOM   2208  N   ASN B 268       0.194 -32.528  47.328  1.00 69.36           N  
ANISOU 2208  N   ASN B 268    13503   8418   4431   2145  -1341     -8       N  
ATOM   2209  CA  ASN B 268      -0.978 -31.843  46.778  1.00 66.81           C  
ANISOU 2209  CA  ASN B 268    13662   7791   3929   1659  -1216    792       C  
ATOM   2210  C   ASN B 268      -0.705 -31.393  45.348  1.00 64.28           C  
ANISOU 2210  C   ASN B 268    13059   7566   3797   2088  -1308    716       C  
ATOM   2211  O   ASN B 268       0.439 -31.080  45.001  1.00 63.80           O  
ANISOU 2211  O   ASN B 268    12461   7841   3938   2624  -1831    255       O  
ATOM   2212  CB  ASN B 268      -1.390 -30.650  47.655  1.00 69.52           C  
ANISOU 2212  CB  ASN B 268    14286   8485   3643   2058  -1403    440       C  
ATOM   2213  CG  ASN B 268      -2.142 -31.069  48.917  1.00 78.43           C  
ANISOU 2213  CG  ASN B 268    14327   9654   5817   1782     55    641       C  
ATOM   2214  OD1 ASN B 268      -1.913 -32.143  49.481  1.00 83.79           O  
ANISOU 2214  OD1 ASN B 268    15190  10478   6167   1945   -186   1547       O  
ATOM   2215  ND2 ASN B 268      -3.042 -30.205  49.372  1.00 85.59           N  
ANISOU 2215  ND2 ASN B 268    14639  10781   7098   2053    -22   -686       N  
ATOM   2216  N   TYR B 269      -1.756 -31.371  44.526  1.00 61.56           N  
ANISOU 2216  N   TYR B 269    12433   7159   3795   1382   -920    542       N  
ATOM   2217  CA  TYR B 269      -1.645 -31.018  43.103  1.00 56.30           C  
ANISOU 2217  CA  TYR B 269    11618   6212   3559   1237  -1324    157       C  
ATOM   2218  C   TYR B 269      -2.660 -29.954  42.689  1.00 53.19           C  
ANISOU 2218  C   TYR B 269    11293   6229   2687   1011  -1266    120       C  
ATOM   2219  O   TYR B 269      -3.862 -30.109  42.916  1.00 60.08           O  
ANISOU 2219  O   TYR B 269    11443   7611   3771    930  -1207   -317       O  
ATOM   2220  CB  TYR B 269      -1.794 -32.267  42.220  1.00 54.67           C  
ANISOU 2220  CB  TYR B 269    11163   5862   3746   1283  -1240    393       C  
ATOM   2221  CG  TYR B 269      -0.788 -33.361  42.524  1.00 55.09           C  
ANISOU 2221  CG  TYR B 269    11209   6031   3692   1282  -1202    686       C  
ATOM   2222  CD1 TYR B 269      -1.042 -34.321  43.514  1.00 55.45           C  
ANISOU 2222  CD1 TYR B 269    11495   6119   3451   1290  -1495    772       C  
ATOM   2223  CD2 TYR B 269       0.422 -33.433  41.826  1.00 54.97           C  
ANISOU 2223  CD2 TYR B 269    11313   6183   3390   1484  -1259    142       C  
ATOM   2224  CE1 TYR B 269      -0.115 -35.316  43.800  1.00 59.59           C  
ANISOU 2224  CE1 TYR B 269    11939   6249   4452   1613  -1477    397       C  
ATOM   2225  CE2 TYR B 269       1.351 -34.427  42.100  1.00 53.76           C  
ANISOU 2225  CE2 TYR B 269    11487   6432   2504   1395  -1837    503       C  
ATOM   2226  CZ  TYR B 269       1.076 -35.364  43.085  1.00 57.56           C  
ANISOU 2226  CZ  TYR B 269    11904   5730   4236   1373  -1574    959       C  
ATOM   2227  OH  TYR B 269       2.003 -36.337  43.355  1.00 60.06           O  
ANISOU 2227  OH  TYR B 269    12199   6279   4340   1792  -2505    530       O  
ATOM   2228  N   GLU B 270      -2.161 -28.869  42.101  1.00 53.47           N  
ANISOU 2228  N   GLU B 270    11602   5635   3079   1037  -1245   -239       N  
ATOM   2229  CA  GLU B 270      -3.011 -27.855  41.477  1.00 56.07           C  
ANISOU 2229  CA  GLU B 270    11571   6320   3413   1387  -1061    -20       C  
ATOM   2230  C   GLU B 270      -2.836 -27.948  39.961  1.00 50.67           C  
ANISOU 2230  C   GLU B 270    10859   4899   3495   1047  -1085   -489       C  
ATOM   2231  O   GLU B 270      -1.800 -27.558  39.412  1.00 56.15           O  
ANISOU 2231  O   GLU B 270    10791   5876   4665   1297   -740   -177       O  
ATOM   2232  CB  GLU B 270      -2.708 -26.447  42.021  1.00 65.60           C  
ANISOU 2232  CB  GLU B 270    13319   6892   4715   1201  -1773   -977       C  
ATOM   2233  CG  GLU B 270      -3.310 -26.186  43.403  1.00 80.14           C  
ANISOU 2233  CG  GLU B 270    14873   9407   6167   1938     85   -366       C  
ATOM   2234  CD  GLU B 270      -2.965 -24.819  43.988  1.00 91.17           C  
ANISOU 2234  CD  GLU B 270    16800  10350   7489   1610  -1299   -959       C  
ATOM   2235  OE1 GLU B 270      -2.523 -24.778  45.156  1.00 91.40           O  
ANISOU 2235  OE1 GLU B 270    17887  10603   6238   2634   -254    615       O  
ATOM   2236  OE2 GLU B 270      -3.140 -23.786  43.298  1.00100.13           O  
ANISOU 2236  OE2 GLU B 270    16352  10262  11430   3621  -1781   -207       O  
ATOM   2237  N   VAL B 271      -3.852 -28.497  39.300  1.00 46.38           N  
ANISOU 2237  N   VAL B 271    10153   4732   2735   1374   -828     35       N  
ATOM   2238  CA  VAL B 271      -3.790 -28.815  37.873  1.00 43.28           C  
ANISOU 2238  CA  VAL B 271     9362   4420   2662    986   -498    163       C  
ATOM   2239  C   VAL B 271      -4.718 -27.886  37.089  1.00 42.65           C  
ANISOU 2239  C   VAL B 271     9240   4583   2382    817   -578     -3       C  
ATOM   2240  O   VAL B 271      -5.875 -27.664  37.476  1.00 43.29           O  
ANISOU 2240  O   VAL B 271     9660   4218   2567   1092   -522  -1215       O  
ATOM   2241  CB  VAL B 271      -4.148 -30.297  37.593  1.00 42.42           C  
ANISOU 2241  CB  VAL B 271     9269   4452   2394    971   -677    214       C  
ATOM   2242  CG1 VAL B 271      -3.847 -30.676  36.149  1.00 44.54           C  
ANISOU 2242  CG1 VAL B 271     9200   5177   2544   1095    -16    334       C  
ATOM   2243  CG2 VAL B 271      -3.391 -31.235  38.521  1.00 45.95           C  
ANISOU 2243  CG2 VAL B 271     9956   4797   2704   1419   -877    222       C  
ATOM   2244  N   THR B 272      -4.199 -27.337  35.995  1.00 38.43           N  
ANISOU 2244  N   THR B 272     8789   3564   2245    615   -759   -311       N  
ATOM   2245  CA  THR B 272      -5.009 -26.556  35.085  1.00 37.41           C  
ANISOU 2245  CA  THR B 272     8611   3464   2136    708   -386   -152       C  
ATOM   2246  C   THR B 272      -4.988 -27.199  33.706  1.00 35.24           C  
ANISOU 2246  C   THR B 272     8117   2968   2303    258   -794   -212       C  
ATOM   2247  O   THR B 272      -3.918 -27.517  33.178  1.00 38.98           O  
ANISOU 2247  O   THR B 272     8161   2996   3651    266   -509   -229       O  
ATOM   2248  CB  THR B 272      -4.539 -25.091  35.026  1.00 40.14           C  
ANISOU 2248  CB  THR B 272     8904   3605   2740    480   -716   -278       C  
ATOM   2249  OG1 THR B 272      -4.398 -24.585  36.362  1.00 44.72           O  
ANISOU 2249  OG1 THR B 272     9652   4402   2937    490   -258   -807       O  
ATOM   2250  CG2 THR B 272      -5.549 -24.232  34.274  1.00 39.07           C  
ANISOU 2250  CG2 THR B 272     8783   3478   2583    373   -641   -272       C  
ATOM   2251  N   TRP B 273      -6.177 -27.411  33.146  1.00 33.53           N  
ANISOU 2251  N   TRP B 273     7709   2786   2245    455   -504     54       N  
ATOM   2252  CA  TRP B 273      -6.328 -27.857  31.762  1.00 33.39           C  
ANISOU 2252  CA  TRP B 273     7367   3089   2231    492   -291   -103       C  
ATOM   2253  C   TRP B 273      -6.782 -26.714  30.864  1.00 34.02           C  
ANISOU 2253  C   TRP B 273     7467   3111   2345    566   -328   -150       C  
ATOM   2254  O   TRP B 273      -7.630 -25.898  31.251  1.00 37.98           O  
ANISOU 2254  O   TRP B 273     7774   3391   3264    881   -277   -192       O  
ATOM   2255  CB  TRP B 273      -7.345 -28.997  31.640  1.00 32.97           C  
ANISOU 2255  CB  TRP B 273     7312   2990   2225    566   -477   -121       C  
ATOM   2256  CG  TRP B 273      -6.948 -30.325  32.222  1.00 35.20           C  
ANISOU 2256  CG  TRP B 273     7556   3119   2698    616   -433    107       C  
ATOM   2257  CD1 TRP B 273      -5.737 -30.677  32.750  1.00 37.29           C  
ANISOU 2257  CD1 TRP B 273     7551   3695   2920    368   -628    265       C  
ATOM   2258  CD2 TRP B 273      -7.765 -31.501  32.283  1.00 39.43           C  
ANISOU 2258  CD2 TRP B 273     7702   3663   3617    308   -113    366       C  
ATOM   2259  NE1 TRP B 273      -5.758 -31.993  33.159  1.00 40.70           N  
ANISOU 2259  NE1 TRP B 273     8023   3398   4043    463   -576    -61       N  
ATOM   2260  CE2 TRP B 273      -6.990 -32.522  32.886  1.00 40.87           C  
ANISOU 2260  CE2 TRP B 273     7906   3576   4044    507   -334     94       C  
ATOM   2261  CE3 TRP B 273      -9.084 -31.792  31.892  1.00 39.36           C  
ANISOU 2261  CE3 TRP B 273     7622   3528   3803    460    -30    467       C  
ATOM   2262  CZ2 TRP B 273      -7.492 -33.813  33.114  1.00 43.23           C  
ANISOU 2262  CZ2 TRP B 273     8148   4080   4197    106    310    395       C  
ATOM   2263  CZ3 TRP B 273      -9.583 -33.077  32.117  1.00 39.30           C  
ANISOU 2263  CZ3 TRP B 273     7854   3488   3588    353    186    211       C  
ATOM   2264  CH2 TRP B 273      -8.784 -34.071  32.721  1.00 42.67           C  
ANISOU 2264  CH2 TRP B 273     8030   3843   4337    460    196    707       C  
ATOM   2265  N   TYR B 274      -6.210 -26.670  29.664  1.00 31.77           N  
ANISOU 2265  N   TYR B 274     6951   2733   2386    381   -385   -132       N  
ATOM   2266  CA  TYR B 274      -6.721 -25.858  28.581  1.00 30.61           C  
ANISOU 2266  CA  TYR B 274     6580   2778   2270    342   -404   -216       C  
ATOM   2267  C   TYR B 274      -7.055 -26.816  27.445  1.00 30.94           C  
ANISOU 2267  C   TYR B 274     6313   2846   2595    317   -358   -372       C  
ATOM   2268  O   TYR B 274      -6.160 -27.347  26.775  1.00 33.68           O  
ANISOU 2268  O   TYR B 274     6375   3309   3112    497    -78   -311       O  
ATOM   2269  CB  TYR B 274      -5.691 -24.813  28.154  1.00 31.67           C  
ANISOU 2269  CB  TYR B 274     6666   2963   2403    153   -630   -383       C  
ATOM   2270  CG  TYR B 274      -5.185 -23.930  29.288  1.00 33.26           C  
ANISOU 2270  CG  TYR B 274     6995   3058   2584     71   -682   -507       C  
ATOM   2271  CD1 TYR B 274      -4.066 -24.301  30.042  1.00 34.05           C  
ANISOU 2271  CD1 TYR B 274     7119   3238   2581    279   -692   -455       C  
ATOM   2272  CD2 TYR B 274      -5.819 -22.719  29.598  1.00 35.59           C  
ANISOU 2272  CD2 TYR B 274     7658   3349   2515    437   -440   -545       C  
ATOM   2273  CE1 TYR B 274      -3.592 -23.495  31.074  1.00 39.59           C  
ANISOU 2273  CE1 TYR B 274     8034   4237   2770    219   -407  -1193       C  
ATOM   2274  CE2 TYR B 274      -5.351 -21.902  30.624  1.00 37.90           C  
ANISOU 2274  CE2 TYR B 274     8113   3398   2887     29   -775   -458       C  
ATOM   2275  CZ  TYR B 274      -4.239 -22.296  31.358  1.00 40.33           C  
ANISOU 2275  CZ  TYR B 274     8216   3743   3364    173   -909   -632       C  
ATOM   2276  OH  TYR B 274      -3.774 -21.502  32.377  1.00 45.26           O  
ANISOU 2276  OH  TYR B 274     9714   4414   3068     89   -971   -842       O  
ATOM   2277  N   THR B 275      -8.351 -27.058  27.254  1.00 32.66           N  
ANISOU 2277  N   THR B 275     6321   2939   3146     54   -203     15       N  
ATOM   2278  CA  THR B 275      -8.821 -28.009  26.256  1.00 32.96           C  
ANISOU 2278  CA  THR B 275     6217   3208   3096     66    -82   -161       C  
ATOM   2279  C   THR B 275      -9.464 -27.304  25.068  1.00 31.24           C  
ANISOU 2279  C   THR B 275     6010   3012   2848    -77    320    -40       C  
ATOM   2280  O   THR B 275     -10.130 -26.281  25.233  1.00 33.01           O  
ANISOU 2280  O   THR B 275     5924   3466   3151    161    312    -58       O  
ATOM   2281  CB  THR B 275      -9.830 -29.018  26.849  1.00 35.99           C  
ANISOU 2281  CB  THR B 275     6466   3830   3376     69    156    337       C  
ATOM   2282  OG1 THR B 275     -10.964 -28.312  27.373  1.00 39.52           O  
ANISOU 2282  OG1 THR B 275     7387   3530   4097    521    440    105       O  
ATOM   2283  CG2 THR B 275      -9.192 -29.855  27.957  1.00 35.22           C  
ANISOU 2283  CG2 THR B 275     6564   2627   4191    340   -630   -261       C  
ATOM   2284  N   SER B 276      -9.265 -27.861  23.877  1.00 29.94           N  
ANISOU 2284  N   SER B 276     5717   2775   2883     71    203    -55       N  
ATOM   2285  CA  SER B 276      -9.858 -27.317  22.655  1.00 28.99           C  
ANISOU 2285  CA  SER B 276     4968   2992   3054    -16    -35   -267       C  
ATOM   2286  C   SER B 276     -11.350 -27.644  22.569  1.00 31.78           C  
ANISOU 2286  C   SER B 276     5027   3320   3728   -309     61   -120       C  
ATOM   2287  O   SER B 276     -12.140 -26.808  22.111  1.00 35.17           O  
ANISOU 2287  O   SER B 276     5603   3089   4671   -228    -12    148       O  
ATOM   2288  CB  SER B 276      -9.103 -27.799  21.410  1.00 28.12           C  
ANISOU 2288  CB  SER B 276     5116   2856   2712   -163   -157   -252       C  
ATOM   2289  OG  SER B 276      -9.159 -29.211  21.294  1.00 30.58           O  
ANISOU 2289  OG  SER B 276     5367   2966   3285     39   -468   -689       O  
ATOM   2290  N   TRP B 277     -11.718 -28.855  23.001  1.00 29.71           N  
ANISOU 2290  N   TRP B 277     4890   3387   3010    -95     79    159       N  
ATOM   2291  CA  TRP B 277     -13.117 -29.264  23.164  1.00 31.36           C  
ANISOU 2291  CA  TRP B 277     5012   3230   3672   -245    322     83       C  
ATOM   2292  C   TRP B 277     -13.374 -29.610  24.638  1.00 34.08           C  
ANISOU 2292  C   TRP B 277     5548   3558   3841   -267    414    229       C  
ATOM   2293  O   TRP B 277     -12.494 -30.150  25.314  1.00 36.28           O  
ANISOU 2293  O   TRP B 277     6461   3384   3936   -446     -4    845       O  
ATOM   2294  CB  TRP B 277     -13.418 -30.524  22.357  1.00 31.74           C  
ANISOU 2294  CB  TRP B 277     5030   3101   3928   -153    385     53       C  
ATOM   2295  CG  TRP B 277     -13.679 -30.419  20.870  1.00 34.27           C  
ANISOU 2295  CG  TRP B 277     4921   4037   4060   -459    344    238       C  
ATOM   2296  CD1 TRP B 277     -12.972 -31.043  19.878  1.00 35.40           C  
ANISOU 2296  CD1 TRP B 277     4949   4037   4464   -359    431    110       C  
ATOM   2297  CD2 TRP B 277     -14.756 -29.729  20.213  1.00 34.44           C  
ANISOU 2297  CD2 TRP B 277     4688   3970   4425   -480    610    489       C  
ATOM   2298  NE1 TRP B 277     -13.521 -30.765  18.649  1.00 34.46           N  
ANISOU 2298  NE1 TRP B 277     5111   3656   4326   -415    562    153       N  
ATOM   2299  CE2 TRP B 277     -14.617 -29.965  18.822  1.00 34.71           C  
ANISOU 2299  CE2 TRP B 277     4521   4251   4416   -506    470    504       C  
ATOM   2300  CE3 TRP B 277     -15.814 -28.925  20.660  1.00 34.99           C  
ANISOU 2300  CE3 TRP B 277     4931   3942   4419   -423    759    376       C  
ATOM   2301  CZ2 TRP B 277     -15.493 -29.423  17.873  1.00 34.38           C  
ANISOU 2301  CZ2 TRP B 277     4285   4469   4306   -701    493    471       C  
ATOM   2302  CZ3 TRP B 277     -16.694 -28.385  19.713  1.00 36.30           C  
ANISOU 2302  CZ3 TRP B 277     4788   4735   4269   -897    500    275       C  
ATOM   2303  CH2 TRP B 277     -16.524 -28.637  18.337  1.00 34.58           C  
ANISOU 2303  CH2 TRP B 277     4381   4462   4296   -756    819    572       C  
ATOM   2304  N   SER B 278     -14.581 -29.333  25.125  1.00 34.21           N  
ANISOU 2304  N   SER B 278     5680   3398   3919   -668    787    159       N  
ATOM   2305  CA  SER B 278     -14.983 -29.760  26.466  1.00 38.15           C  
ANISOU 2305  CA  SER B 278     6183   4240   4072   -219    841    606       C  
ATOM   2306  C   SER B 278     -15.253 -31.294  26.498  1.00 41.34           C  
ANISOU 2306  C   SER B 278     7003   4196   4509     -7    257    659       C  
ATOM   2307  O   SER B 278     -15.549 -31.879  25.457  1.00 40.29           O  
ANISOU 2307  O   SER B 278     6493   4660   4153    177    374    669       O  
ATOM   2308  CB  SER B 278     -16.197 -28.951  26.933  1.00 36.26           C  
ANISOU 2308  CB  SER B 278     6157   3443   4176   -207    642    589       C  
ATOM   2309  OG  SER B 278     -17.332 -29.257  26.155  1.00 37.76           O  
ANISOU 2309  OG  SER B 278     5492   4530   4322    490    698    535       O  
ATOM   2310  N   PRO B 279     -15.147 -31.947  27.684  1.00 42.40           N  
ANISOU 2310  N   PRO B 279     7343   4202   4563   -288    722    831       N  
ATOM   2311  CA  PRO B 279     -15.206 -33.428  27.738  1.00 42.03           C  
ANISOU 2311  CA  PRO B 279     7135   4185   4648   -395    623    969       C  
ATOM   2312  C   PRO B 279     -16.526 -34.064  27.281  1.00 43.97           C  
ANISOU 2312  C   PRO B 279     6875   4515   5316   -450    772   1162       C  
ATOM   2313  O   PRO B 279     -17.582 -33.458  27.442  1.00 46.42           O  
ANISOU 2313  O   PRO B 279     6901   4789   5944   -535   1198   1119       O  
ATOM   2314  CB  PRO B 279     -14.989 -33.734  29.228  1.00 41.85           C  
ANISOU 2314  CB  PRO B 279     7541   3729   4632   -275    721    940       C  
ATOM   2315  CG  PRO B 279     -14.340 -32.518  29.795  1.00 40.93           C  
ANISOU 2315  CG  PRO B 279     7509   3871   4170   -133    713    722       C  
ATOM   2316  CD  PRO B 279     -14.919 -31.371  29.025  1.00 42.13           C  
ANISOU 2316  CD  PRO B 279     7672   3924   4410     62    801    779       C  
ATOM   2317  N   CYS B 280     -16.449 -35.272  26.713  1.00 45.14           N  
ANISOU 2317  N   CYS B 280     7186   4472   5491   -579    774   1207       N  
ATOM   2318  CA  CYS B 280     -17.628 -36.126  26.483  1.00 46.49           C  
ANISOU 2318  CA  CYS B 280     7256   4322   6085   -627    961   1371       C  
ATOM   2319  C   CYS B 280     -18.114 -36.655  27.847  1.00 47.52           C  
ANISOU 2319  C   CYS B 280     7104   4606   6344   -896   1077   1550       C  
ATOM   2320  O   CYS B 280     -17.330 -36.634  28.804  1.00 46.57           O  
ANISOU 2320  O   CYS B 280     7585   3954   6152   -417    988   1590       O  
ATOM   2321  CB  CYS B 280     -17.283 -37.280  25.528  1.00 46.61           C  
ANISOU 2321  CB  CYS B 280     7496   4342   5869   -228    430   1423       C  
ATOM   2322  SG  CYS B 280     -16.296 -38.625  26.245  1.00 46.48           S  
ANISOU 2322  SG  CYS B 280     8323   3846   5491   -105    186   1123       S  
ATOM   2323  N   PRO B 281     -19.391 -37.124  27.954  1.00 51.02           N  
ANISOU 2323  N   PRO B 281     7418   5281   6686  -1567    660   1805       N  
ATOM   2324  CA  PRO B 281     -19.897 -37.539  29.282  1.00 55.16           C  
ANISOU 2324  CA  PRO B 281     8077   5684   7196  -1773   1157   2253       C  
ATOM   2325  C   PRO B 281     -19.141 -38.700  29.941  1.00 57.23           C  
ANISOU 2325  C   PRO B 281     8918   5667   7156  -1384   1061   2043       C  
ATOM   2326  O   PRO B 281     -19.104 -38.776  31.174  1.00 59.35           O  
ANISOU 2326  O   PRO B 281     9924   5424   7202  -1096    172   2977       O  
ATOM   2327  CB  PRO B 281     -21.366 -37.918  29.017  1.00 55.13           C  
ANISOU 2327  CB  PRO B 281     7678   6445   6824  -1762   2069   2064       C  
ATOM   2328  CG  PRO B 281     -21.480 -38.097  27.544  1.00 42.71           C  
ANISOU 2328  CG  PRO B 281     5241   4084   6900  -2401   1738   2634       C  
ATOM   2329  CD  PRO B 281     -20.456 -37.196  26.931  1.00 40.38           C  
ANISOU 2329  CD  PRO B 281     5324   3774   6243  -2251   1670   2419       C  
ATOM   2330  N   GLU B 282     -18.547 -39.576  29.126  1.00 58.24           N  
ANISOU 2330  N   GLU B 282     8669   5769   7690  -1462   1024   1724       N  
ATOM   2331  CA  GLU B 282     -17.716 -40.680  29.618  1.00 59.13           C  
ANISOU 2331  CA  GLU B 282     8872   5935   7657  -1500    939   2164       C  
ATOM   2332  C   GLU B 282     -16.446 -40.150  30.276  1.00 55.65           C  
ANISOU 2332  C   GLU B 282     8952   5001   7188  -1289   1215   2006       C  
ATOM   2333  O   GLU B 282     -16.106 -40.574  31.382  1.00 63.69           O  
ANISOU 2333  O   GLU B 282    10085   6307   7805   -321    623   2274       O  
ATOM   2334  CB  GLU B 282     -17.373 -41.671  28.497  1.00 63.00           C  
ANISOU 2334  CB  GLU B 282     9208   6549   8179  -1528   1354   1760       C  
ATOM   2335  CG  GLU B 282     -18.468 -42.687  28.175  1.00 79.82           C  
ANISOU 2335  CG  GLU B 282    11305   8127  10894  -2877    585   1119       C  
ATOM   2336  CD  GLU B 282     -19.677 -42.094  27.450  1.00 87.15           C  
ANISOU 2336  CD  GLU B 282    11917   9055  12141  -2184    815   1943       C  
ATOM   2337  OE1 GLU B 282     -20.807 -42.563  27.717  1.00 95.40           O  
ANISOU 2337  OE1 GLU B 282    13130   8837  14280  -3622   1387   2025       O  
ATOM   2338  OE2 GLU B 282     -19.509 -41.167  26.619  1.00 87.85           O  
ANISOU 2338  OE2 GLU B 282    13166   8574  11636  -3269   1148   1255       O  
ATOM   2339  N   CYS B 283     -15.769 -39.217  29.597  1.00 48.53           N  
ANISOU 2339  N   CYS B 283     8570   3787   6080   -702    792   1565       N  
ATOM   2340  CA  CYS B 283     -14.565 -38.558  30.117  1.00 47.09           C  
ANISOU 2340  CA  CYS B 283     8306   3977   5609   -460    793   1335       C  
ATOM   2341  C   CYS B 283     -14.863 -37.729  31.356  1.00 45.10           C  
ANISOU 2341  C   CYS B 283     8358   3399   5378   -432    961   1765       C  
ATOM   2342  O   CYS B 283     -14.109 -37.773  32.326  1.00 46.16           O  
ANISOU 2342  O   CYS B 283     8860   2886   5790   -677    603    882       O  
ATOM   2343  CB  CYS B 283     -13.915 -37.667  29.054  1.00 46.81           C  
ANISOU 2343  CB  CYS B 283     8147   4470   5166   -875    539   1147       C  
ATOM   2344  SG  CYS B 283     -12.837 -38.548  27.899  1.00 52.39           S  
ANISOU 2344  SG  CYS B 283     7864   4774   7265   -495    282     74       S  
ATOM   2345  N   ALA B 284     -15.969 -36.989  31.317  1.00 46.65           N  
ANISOU 2345  N   ALA B 284     8167   4273   5281   -210   1059   1838       N  
ATOM   2346  CA  ALA B 284     -16.369 -36.118  32.420  1.00 50.13           C  
ANISOU 2346  CA  ALA B 284     8404   5397   5245    -82   1342   1778       C  
ATOM   2347  C   ALA B 284     -16.694 -36.929  33.672  1.00 51.55           C  
ANISOU 2347  C   ALA B 284     8573   5097   5916   -380   1473   2097       C  
ATOM   2348  O   ALA B 284     -16.342 -36.525  34.784  1.00 56.13           O  
ANISOU 2348  O   ALA B 284     9280   6073   5973   -168   1203   1836       O  
ATOM   2349  CB  ALA B 284     -17.542 -35.239  32.012  1.00 47.41           C  
ANISOU 2349  CB  ALA B 284     8319   4964   4727   -177   1348   1516       C  
ATOM   2350  N   GLY B 285     -17.342 -38.078  33.470  1.00 50.62           N  
ANISOU 2350  N   GLY B 285     8721   4910   5600   -490   1470   2669       N  
ATOM   2351  CA  GLY B 285     -17.640 -39.037  34.539  1.00 52.95           C  
ANISOU 2351  CA  GLY B 285     9532   5060   5524   -490   1561   2732       C  
ATOM   2352  C   GLY B 285     -16.390 -39.620  35.179  1.00 55.24           C  
ANISOU 2352  C   GLY B 285     9334   5544   6108   -771   1424   2622       C  
ATOM   2353  O   GLY B 285     -16.316 -39.723  36.406  1.00 57.80           O  
ANISOU 2353  O   GLY B 285     9668   6094   6198  -1165   1366   2532       O  
ATOM   2354  N   GLU B 286     -15.414 -39.993  34.347  1.00 54.70           N  
ANISOU 2354  N   GLU B 286     9367   5496   5918   -912   1369   2484       N  
ATOM   2355  CA  GLU B 286     -14.122 -40.519  34.815  1.00 57.61           C  
ANISOU 2355  CA  GLU B 286    10096   5467   6322   -458    939   2476       C  
ATOM   2356  C   GLU B 286     -13.304 -39.484  35.595  1.00 54.15           C  
ANISOU 2356  C   GLU B 286    10224   4851   5500    -23   1252   2361       C  
ATOM   2357  O   GLU B 286     -12.664 -39.828  36.589  1.00 54.98           O  
ANISOU 2357  O   GLU B 286    10631   4240   6017    199   1146   2962       O  
ATOM   2358  CB  GLU B 286     -13.286 -41.053  33.650  1.00 62.42           C  
ANISOU 2358  CB  GLU B 286    11423   5798   6493    101    966   1932       C  
ATOM   2359  CG  GLU B 286     -13.755 -42.372  33.068  1.00 75.48           C  
ANISOU 2359  CG  GLU B 286    12781   5966   9930   -229    -26   1586       C  
ATOM   2360  CD  GLU B 286     -12.958 -42.772  31.838  1.00 85.42           C  
ANISOU 2360  CD  GLU B 286    13544   8017  10892   1162    203   1371       C  
ATOM   2361  OE1 GLU B 286     -11.779 -43.158  31.986  1.00 97.69           O  
ANISOU 2361  OE1 GLU B 286    13781   9538  13796   1629   -734   1433       O  
ATOM   2362  OE2 GLU B 286     -13.514 -42.703  30.721  1.00 90.62           O  
ANISOU 2362  OE2 GLU B 286    15312   7978  11139    418   -526   1364       O  
ATOM   2363  N   VAL B 287     -13.325 -38.230  35.138  1.00 52.26           N  
ANISOU 2363  N   VAL B 287    10005   4529   5322   -125   1342   1898       N  
ATOM   2364  CA  VAL B 287     -12.594 -37.140  35.802  1.00 52.52           C  
ANISOU 2364  CA  VAL B 287    10203   4738   5012     19   1081   1802       C  
ATOM   2365  C   VAL B 287     -13.256 -36.782  37.150  1.00 54.08           C  
ANISOU 2365  C   VAL B 287    10002   5316   5228    280   1333   2124       C  
ATOM   2366  O   VAL B 287     -12.564 -36.627  38.165  1.00 54.69           O  
ANISOU 2366  O   VAL B 287    10186   5483   5110    731   1380   1458       O  
ATOM   2367  CB  VAL B 287     -12.405 -35.908  34.867  1.00 49.91           C  
ANISOU 2367  CB  VAL B 287     9793   4822   4349   -147   1078   1572       C  
ATOM   2368  CG1 VAL B 287     -11.729 -34.752  35.588  1.00 45.83           C  
ANISOU 2368  CG1 VAL B 287     9867   3699   3844    368   1015   2025       C  
ATOM   2369  CG2 VAL B 287     -11.566 -36.278  33.659  1.00 50.14           C  
ANISOU 2369  CG2 VAL B 287     9923   5061   4064   -553    861    974       C  
ATOM   2370  N   ALA B 288     -14.588 -36.686  37.151  1.00 55.56           N  
ANISOU 2370  N   ALA B 288    10057   5173   5877    764   1933   2630       N  
ATOM   2371  CA  ALA B 288     -15.371 -36.455  38.372  1.00 58.99           C  
ANISOU 2371  CA  ALA B 288    10891   6379   5141    594   1750   2556       C  
ATOM   2372  C   ALA B 288     -15.192 -37.575  39.398  1.00 61.48           C  
ANISOU 2372  C   ALA B 288    11283   6393   5681    499   1900   2851       C  
ATOM   2373  O   ALA B 288     -15.027 -37.294  40.592  1.00 64.93           O  
ANISOU 2373  O   ALA B 288    11707   6875   6089    441    903   2618       O  
ATOM   2374  CB  ALA B 288     -16.844 -36.268  38.039  1.00 58.56           C  
ANISOU 2374  CB  ALA B 288    10495   7197   4555    386   2568   1781       C  
ATOM   2375  N   GLU B 289     -15.221 -38.827  38.924  1.00 60.23           N  
ANISOU 2375  N   GLU B 289    11022   6291   5570    536   2055   2958       N  
ATOM   2376  CA  GLU B 289     -14.974 -40.014  39.763  1.00 66.72           C  
ANISOU 2376  CA  GLU B 289    12043   6656   6652    513   1685   3538       C  
ATOM   2377  C   GLU B 289     -13.557 -39.997  40.348  1.00 67.55           C  
ANISOU 2377  C   GLU B 289    12408   6635   6621    558   1434   3075       C  
ATOM   2378  O   GLU B 289     -13.365 -40.305  41.527  1.00 73.73           O  
ANISOU 2378  O   GLU B 289    13294   7787   6930    692    982   3460       O  
ATOM   2379  CB  GLU B 289     -15.275 -41.313  38.981  1.00 73.42           C  
ANISOU 2379  CB  GLU B 289    12747   7834   7313   -202   1870   2549       C  
ATOM   2380  CG  GLU B 289     -14.462 -42.563  39.336  1.00 86.18           C  
ANISOU 2380  CG  GLU B 289    13822   8899  10024    424   1403   3161       C  
ATOM   2381  CD  GLU B 289     -14.852 -43.238  40.648  1.00 98.43           C  
ANISOU 2381  CD  GLU B 289    15633  10611  11153   -653   1575   4247       C  
ATOM   2382  OE1 GLU B 289     -14.203 -44.252  40.988  1.00111.30           O  
ANISOU 2382  OE1 GLU B 289    16051  10565  15672    155   1681   3709       O  
ATOM   2383  OE2 GLU B 289     -15.789 -42.782  41.346  1.00103.47           O  
ANISOU 2383  OE2 GLU B 289    14614  10394  14303   -934   1564   2957       O  
ATOM   2384  N   PHE B 290     -12.587 -39.612  39.519  1.00 63.34           N  
ANISOU 2384  N   PHE B 290    11868   5588   6610    757   1467   2046       N  
ATOM   2385  CA  PHE B 290     -11.195 -39.449  39.933  1.00 62.27           C  
ANISOU 2385  CA  PHE B 290    11877   5778   6001   1357   1133   2401       C  
ATOM   2386  C   PHE B 290     -11.017 -38.378  41.023  1.00 64.53           C  
ANISOU 2386  C   PHE B 290    12011   6601   5904   1148   1194   2135       C  
ATOM   2387  O   PHE B 290     -10.330 -38.616  42.024  1.00 65.76           O  
ANISOU 2387  O   PHE B 290    12019   6787   6179   1763   1170   1853       O  
ATOM   2388  CB  PHE B 290     -10.322 -39.150  38.707  1.00 61.08           C  
ANISOU 2388  CB  PHE B 290    11989   5526   5693   1187    993   2231       C  
ATOM   2389  CG  PHE B 290      -8.913 -38.756  39.037  1.00 64.68           C  
ANISOU 2389  CG  PHE B 290    12309   6565   5699    835    718   1734       C  
ATOM   2390  CD1 PHE B 290      -7.954 -39.728  39.328  1.00 66.24           C  
ANISOU 2390  CD1 PHE B 290    12549   6581   6037    894    314   1834       C  
ATOM   2391  CD2 PHE B 290      -8.539 -37.410  39.046  1.00 64.59           C  
ANISOU 2391  CD2 PHE B 290    12277   6659   5602    698    853    755       C  
ATOM   2392  CE1 PHE B 290      -6.652 -39.364  39.634  1.00 69.68           C  
ANISOU 2392  CE1 PHE B 290    12653   6757   7062   1090     17   1052       C  
ATOM   2393  CE2 PHE B 290      -7.236 -37.042  39.349  1.00 72.97           C  
ANISOU 2393  CE2 PHE B 290    12542   7823   7358    801     23    810       C  
ATOM   2394  CZ  PHE B 290      -6.293 -38.023  39.643  1.00 74.60           C  
ANISOU 2394  CZ  PHE B 290    13272   7126   7945    492   -300   1514       C  
ATOM   2395  N   LEU B 291     -11.639 -37.215  40.822  1.00 61.82           N  
ANISOU 2395  N   LEU B 291    11810   6372   5306    882   1649   2214       N  
ATOM   2396  CA  LEU B 291     -11.550 -36.095  41.768  1.00 62.21           C  
ANISOU 2396  CA  LEU B 291    12022   6628   4987   1047   1320   2335       C  
ATOM   2397  C   LEU B 291     -12.213 -36.364  43.120  1.00 62.01           C  
ANISOU 2397  C   LEU B 291    11732   7075   4752   1663   1100   2506       C  
ATOM   2398  O   LEU B 291     -11.779 -35.820  44.137  1.00 65.80           O  
ANISOU 2398  O   LEU B 291    11846   8486   4667   2464    331   2526       O  
ATOM   2399  CB  LEU B 291     -12.121 -34.815  41.151  1.00 61.22           C  
ANISOU 2399  CB  LEU B 291    11905   6566   4789    919   1265   2271       C  
ATOM   2400  CG  LEU B 291     -11.369 -34.158  39.989  1.00 59.04           C  
ANISOU 2400  CG  LEU B 291    11651   6175   4607    661   1121   2000       C  
ATOM   2401  CD1 LEU B 291     -12.240 -33.068  39.389  1.00 58.14           C  
ANISOU 2401  CD1 LEU B 291    11259   6685   4145    932   1692   2117       C  
ATOM   2402  CD2 LEU B 291     -10.021 -33.598  40.425  1.00 61.36           C  
ANISOU 2402  CD2 LEU B 291    11229   7117   4965    513   1587   3016       C  
ATOM   2403  N   ALA B 292     -13.261 -37.189  43.114  1.00 61.45           N  
ANISOU 2403  N   ALA B 292    12395   6159   4794   1409    920   3743       N  
ATOM   2404  CA  ALA B 292     -13.932 -37.643  44.336  1.00 70.22           C  
ANISOU 2404  CA  ALA B 292    12757   8527   5393   1005   2041   3143       C  
ATOM   2405  C   ALA B 292     -13.032 -38.583  45.136  1.00 77.55           C  
ANISOU 2405  C   ALA B 292    14138   8669   6657   1291   1272   3443       C  
ATOM   2406  O   ALA B 292     -13.029 -38.545  46.368  1.00 82.70           O  
ANISOU 2406  O   ALA B 292    14258  10439   6725    154    610   3091       O  
ATOM   2407  CB  ALA B 292     -15.250 -38.329  44.000  1.00 67.17           C  
ANISOU 2407  CB  ALA B 292    11490   9094   4936   1140   3259   3298       C  
ATOM   2408  N   ARG B 293     -12.270 -39.410  44.417  1.00 78.69           N  
ANISOU 2408  N   ARG B 293    14399   9072   6427   1354   1139   3219       N  
ATOM   2409  CA  ARG B 293     -11.367 -40.406  45.004  1.00 79.62           C  
ANISOU 2409  CA  ARG B 293    14647   8638   6967   1154    787   3269       C  
ATOM   2410  C   ARG B 293     -10.013 -39.832  45.439  1.00 80.01           C  
ANISOU 2410  C   ARG B 293    14277   9099   7023   1661    907   3129       C  
ATOM   2411  O   ARG B 293      -9.304 -40.451  46.239  1.00 81.25           O  
ANISOU 2411  O   ARG B 293    14515   8275   8079   1787    962   3710       O  
ATOM   2412  CB  ARG B 293     -11.177 -41.587  44.035  1.00 70.87           C  
ANISOU 2412  CB  ARG B 293    14043   7297   5585   1113    855   4724       C  
ATOM   2413  CG  ARG B 293     -12.085 -42.786  44.294  1.00 79.57           C  
ANISOU 2413  CG  ARG B 293    14679   7815   7736    462   1027   4646       C  
ATOM   2414  CD  ARG B 293     -13.555 -42.539  43.964  1.00 83.14           C  
ANISOU 2414  CD  ARG B 293    15060   8601   7925    921    747   4672       C  
ATOM   2415  NE  ARG B 293     -14.442 -43.467  44.673  1.00 96.29           N  
ANISOU 2415  NE  ARG B 293    15845  10116  10622   -863   2064   3381       N  
ATOM   2416  CZ  ARG B 293     -15.108 -43.196  45.799  1.00100.64           C  
ANISOU 2416  CZ  ARG B 293    16248  11248  10740   -289   2365   3830       C  
ATOM   2417  NH1 ARG B 293     -15.879 -44.129  46.345  1.00 96.33           N  
ANISOU 2417  NH1 ARG B 293    14890  10640  11070    489   2886   3442       N  
ATOM   2418  NH2 ARG B 293     -15.017 -42.004  46.385  1.00103.65           N  
ANISOU 2418  NH2 ARG B 293    16630  10936  11816   1151   2775   3513       N  
ATOM   2419  N   HIS B 294      -9.668 -38.650  44.920  1.00 78.79           N  
ANISOU 2419  N   HIS B 294    14608   8545   6783   1717   1313   2315       N  
ATOM   2420  CA  HIS B 294      -8.391 -37.998  45.230  1.00 74.91           C  
ANISOU 2420  CA  HIS B 294    14307   8516   5638   2114    963   1827       C  
ATOM   2421  C   HIS B 294      -8.572 -36.541  45.665  1.00 74.00           C  
ANISOU 2421  C   HIS B 294    14531   8657   4928   1601    528   1563       C  
ATOM   2422  O   HIS B 294      -8.583 -35.623  44.835  1.00 73.52           O  
ANISOU 2422  O   HIS B 294    14638   8764   4530   1227    853   1413       O  
ATOM   2423  CB  HIS B 294      -7.420 -38.127  44.051  1.00 73.25           C  
ANISOU 2423  CB  HIS B 294    14006   8215   5609   2020    924   2837       C  
ATOM   2424  CG  HIS B 294      -7.130 -39.545  43.667  1.00 79.41           C  
ANISOU 2424  CG  HIS B 294    14205   8999   6968   2439   1408   1906       C  
ATOM   2425  ND1 HIS B 294      -7.815 -40.199  42.665  1.00 81.64           N  
ANISOU 2425  ND1 HIS B 294    14594   8977   7448   2059    547   2617       N  
ATOM   2426  CD2 HIS B 294      -6.250 -40.444  44.169  1.00 82.39           C  
ANISOU 2426  CD2 HIS B 294    14490   8762   8050   2562   1871   2783       C  
ATOM   2427  CE1 HIS B 294      -7.357 -41.433  42.553  1.00 86.20           C  
ANISOU 2427  CE1 HIS B 294    14854   9480   8417   2689    532   1904       C  
ATOM   2428  NE2 HIS B 294      -6.408 -41.607  43.455  1.00 86.45           N  
ANISOU 2428  NE2 HIS B 294    14934   9415   8496   3219    577   2289       N  
ATOM   2429  N   SER B 295      -8.714 -36.359  46.980  1.00 74.18           N  
ANISOU 2429  N   SER B 295    14685   8643   4856   1250    496   1755       N  
ATOM   2430  CA  SER B 295      -8.927 -35.053  47.628  1.00 74.66           C  
ANISOU 2430  CA  SER B 295    14543   9129   4693   2049   1078   1562       C  
ATOM   2431  C   SER B 295      -7.742 -34.105  47.465  1.00 68.06           C  
ANISOU 2431  C   SER B 295    14343   8217   3300   2563    904   1650       C  
ATOM   2432  O   SER B 295      -7.928 -32.890  47.407  1.00 75.26           O  
ANISOU 2432  O   SER B 295    16308   8329   3955   3115    292    387       O  
ATOM   2433  CB  SER B 295      -9.209 -35.236  49.124  1.00 76.62           C  
ANISOU 2433  CB  SER B 295    14288   9790   5031   2439   2289   1115       C  
ATOM   2434  OG  SER B 295     -10.211 -36.209  49.351  1.00 87.30           O  
ANISOU 2434  OG  SER B 295    14864  11456   6849   1653   2276   1492       O  
ATOM   2435  N   ASN B 296      -6.536 -34.675  47.398  1.00 63.11           N  
ANISOU 2435  N   ASN B 296    13963   7695   2318   2315    651   2126       N  
ATOM   2436  CA  ASN B 296      -5.277 -33.932  47.233  1.00 62.97           C  
ANISOU 2436  CA  ASN B 296    13285   7122   3516   2677    -55   1286       C  
ATOM   2437  C   ASN B 296      -5.051 -33.304  45.841  1.00 61.86           C  
ANISOU 2437  C   ASN B 296    12697   7304   3502   2701   -171   1339       C  
ATOM   2438  O   ASN B 296      -4.023 -32.659  45.610  1.00 59.57           O  
ANISOU 2438  O   ASN B 296    12433   7034   3166   3158   -595   1825       O  
ATOM   2439  CB  ASN B 296      -4.081 -34.822  47.627  1.00 63.51           C  
ANISOU 2439  CB  ASN B 296    13075   7709   3347   2665     54   1530       C  
ATOM   2440  CG  ASN B 296      -3.926 -36.048  46.730  1.00 65.69           C  
ANISOU 2440  CG  ASN B 296    13331   7704   3924   2415    -34   1279       C  
ATOM   2441  OD1 ASN B 296      -4.908 -36.684  46.339  1.00 64.70           O  
ANISOU 2441  OD1 ASN B 296    13561   7181   3839   2418   -143   1470       O  
ATOM   2442  ND2 ASN B 296      -2.682 -36.391  46.414  1.00 64.99           N  
ANISOU 2442  ND2 ASN B 296    13059   7629   4002   2101   -283   1468       N  
ATOM   2443  N   VAL B 297      -6.008 -33.495  44.929  1.00 59.81           N  
ANISOU 2443  N   VAL B 297    12104   7109   3511   2697    148   1210       N  
ATOM   2444  CA  VAL B 297      -5.949 -32.916  43.579  1.00 57.14           C  
ANISOU 2444  CA  VAL B 297    11728   6690   3290   2518    255    840       C  
ATOM   2445  C   VAL B 297      -7.067 -31.886  43.360  1.00 58.93           C  
ANISOU 2445  C   VAL B 297    12019   6724   3645   2589   -123    891       C  
ATOM   2446  O   VAL B 297      -8.252 -32.188  43.556  1.00 59.21           O  
ANISOU 2446  O   VAL B 297    11476   7119   3902   3255  -1133    511       O  
ATOM   2447  CB  VAL B 297      -5.984 -34.010  42.476  1.00 53.65           C  
ANISOU 2447  CB  VAL B 297    10933   6188   3264   2405      0   1093       C  
ATOM   2448  CG1 VAL B 297      -5.953 -33.392  41.084  1.00 50.39           C  
ANISOU 2448  CG1 VAL B 297    10849   5173   3124   2097   -686    765       C  
ATOM   2449  CG2 VAL B 297      -4.822 -34.983  42.638  1.00 52.18           C  
ANISOU 2449  CG2 VAL B 297    11730   4940   3155   2452   -133   1662       C  
ATOM   2450  N   ASN B 298      -6.664 -30.676  42.967  1.00 58.99           N  
ANISOU 2450  N   ASN B 298    11889   6748   3775   2361    451    607       N  
ATOM   2451  CA  ASN B 298      -7.572 -29.599  42.566  1.00 61.48           C  
ANISOU 2451  CA  ASN B 298    12086   7349   3923   2522    171   1012       C  
ATOM   2452  C   ASN B 298      -7.410 -29.321  41.071  1.00 55.99           C  
ANISOU 2452  C   ASN B 298    11046   6382   3846   2033    -59    645       C  
ATOM   2453  O   ASN B 298      -6.295 -29.078  40.588  1.00 53.30           O  
ANISOU 2453  O   ASN B 298    11163   5652   3437   1977    352   1088       O  
ATOM   2454  CB  ASN B 298      -7.306 -28.331  43.393  1.00 68.49           C  
ANISOU 2454  CB  ASN B 298    13041   7816   5165   2179    396    417       C  
ATOM   2455  CG  ASN B 298      -8.264 -27.195  43.064  1.00 75.52           C  
ANISOU 2455  CG  ASN B 298    13722   8724   6245   2586    359   1171       C  
ATOM   2456  OD1 ASN B 298      -9.443 -27.235  43.418  1.00 85.60           O  
ANISOU 2456  OD1 ASN B 298    13909  10856   7757   1825    681   1158       O  
ATOM   2457  ND2 ASN B 298      -7.753 -26.167  42.397  1.00 76.42           N  
ANISOU 2457  ND2 ASN B 298    14682   8666   5688   2005    258    905       N  
ATOM   2458  N   LEU B 299      -8.528 -29.368  40.348  1.00 51.99           N  
ANISOU 2458  N   LEU B 299    11225   5330   3198   2076     25    800       N  
ATOM   2459  CA  LEU B 299      -8.525 -29.222  38.900  1.00 48.00           C  
ANISOU 2459  CA  LEU B 299     9987   5186   3062   1988    -50    309       C  
ATOM   2460  C   LEU B 299      -9.301 -27.993  38.439  1.00 46.76           C  
ANISOU 2460  C   LEU B 299     9784   5226   2754   2030     95    200       C  
ATOM   2461  O   LEU B 299     -10.440 -27.772  38.855  1.00 46.82           O  
ANISOU 2461  O   LEU B 299    10383   5186   2219   2079    749   -158       O  
ATOM   2462  CB  LEU B 299      -9.068 -30.491  38.225  1.00 45.73           C  
ANISOU 2462  CB  LEU B 299     9784   4925   2664   2095    450    223       C  
ATOM   2463  CG  LEU B 299      -9.056 -30.557  36.688  1.00 44.69           C  
ANISOU 2463  CG  LEU B 299     9336   5009   2634   1484    151    475       C  
ATOM   2464  CD1 LEU B 299      -7.651 -30.666  36.119  1.00 44.72           C  
ANISOU 2464  CD1 LEU B 299     9523   5359   2108   1586     75    -41       C  
ATOM   2465  CD2 LEU B 299      -9.887 -31.726  36.204  1.00 43.05           C  
ANISOU 2465  CD2 LEU B 299     9123   4866   2367   1540    174    661       C  
ATOM   2466  N   THR B 300      -8.658 -27.205  37.577  1.00 43.21           N  
ANISOU 2466  N   THR B 300     9368   4594   2455   1846   -542     46       N  
ATOM   2467  CA  THR B 300      -9.290 -26.082  36.885  1.00 42.79           C  
ANISOU 2467  CA  THR B 300     9161   4667   2427   1896   -420    140       C  
ATOM   2468  C   THR B 300      -9.291 -26.401  35.389  1.00 40.31           C  
ANISOU 2468  C   THR B 300     8932   3920   2461   1472   -295    182       C  
ATOM   2469  O   THR B 300      -8.241 -26.711  34.816  1.00 38.92           O  
ANISOU 2469  O   THR B 300     8927   3580   2281   1040   -214    -36       O  
ATOM   2470  CB  THR B 300      -8.560 -24.750  37.176  1.00 43.83           C  
ANISOU 2470  CB  THR B 300     9317   4572   2763   1835   -573    433       C  
ATOM   2471  OG1 THR B 300      -8.519 -24.530  38.592  1.00 46.11           O  
ANISOU 2471  OG1 THR B 300     9626   4956   2935   1609   -327     85       O  
ATOM   2472  CG2 THR B 300      -9.281 -23.569  36.534  1.00 45.14           C  
ANISOU 2472  CG2 THR B 300     9242   5006   2900   2341   -397    244       C  
ATOM   2473  N   ILE B 301     -10.474 -26.353  34.776  1.00 39.75           N  
ANISOU 2473  N   ILE B 301     8804   3905   2390   1162   -210    403       N  
ATOM   2474  CA  ILE B 301     -10.630 -26.629  33.345  1.00 40.80           C  
ANISOU 2474  CA  ILE B 301     8762   4341   2396   1318   -181    275       C  
ATOM   2475  C   ILE B 301     -11.038 -25.358  32.606  1.00 41.80           C  
ANISOU 2475  C   ILE B 301     8823   4171   2888   1256   -172    313       C  
ATOM   2476  O   ILE B 301     -12.070 -24.752  32.908  1.00 49.06           O  
ANISOU 2476  O   ILE B 301     8565   5715   4357   1326   -209    380       O  
ATOM   2477  CB  ILE B 301     -11.658 -27.757  33.050  1.00 41.32           C  
ANISOU 2477  CB  ILE B 301     8889   4404   2406   1151     91    386       C  
ATOM   2478  CG1 ILE B 301     -11.275 -29.054  33.776  1.00 43.59           C  
ANISOU 2478  CG1 ILE B 301     8932   4642   2987   1437     66    589       C  
ATOM   2479  CG2 ILE B 301     -11.792 -27.999  31.541  1.00 39.26           C  
ANISOU 2479  CG2 ILE B 301     8421   4090   2406    799   -109    531       C  
ATOM   2480  CD1 ILE B 301     -12.357 -30.116  33.780  1.00 46.62           C  
ANISOU 2480  CD1 ILE B 301     9056   5311   3345    966    406   1299       C  
ATOM   2481  N   PHE B 302     -10.200 -24.961  31.656  1.00 38.57           N  
ANISOU 2481  N   PHE B 302     8263   3732   2660   1492   -304     51       N  
ATOM   2482  CA  PHE B 302     -10.540 -23.938  30.677  1.00 38.73           C  
ANISOU 2482  CA  PHE B 302     8053   4035   2626   1333   -540    148       C  
ATOM   2483  C   PHE B 302     -10.761 -24.638  29.349  1.00 37.60           C  
ANISOU 2483  C   PHE B 302     7663   3856   2765   1069   -725    234       C  
ATOM   2484  O   PHE B 302      -9.932 -25.452  28.923  1.00 41.30           O  
ANISOU 2484  O   PHE B 302     8113   4087   3489   1071   -146     91       O  
ATOM   2485  CB  PHE B 302      -9.419 -22.908  30.543  1.00 40.89           C  
ANISOU 2485  CB  PHE B 302     8706   4000   2827    912   -904     70       C  
ATOM   2486  CG  PHE B 302      -9.269 -22.004  31.737  1.00 42.40           C  
ANISOU 2486  CG  PHE B 302     8537   4642   2929   1501   -752   -342       C  
ATOM   2487  CD1 PHE B 302     -10.061 -20.860  31.871  1.00 46.26           C  
ANISOU 2487  CD1 PHE B 302     8806   4949   3819   1776  -1017   -549       C  
ATOM   2488  CD2 PHE B 302      -8.314 -22.280  32.715  1.00 41.85           C  
ANISOU 2488  CD2 PHE B 302     8855   4056   2989   1772   -796   -108       C  
ATOM   2489  CE1 PHE B 302      -9.921 -20.021  32.977  1.00 47.63           C  
ANISOU 2489  CE1 PHE B 302     9516   4749   3829   1265  -1324   -330       C  
ATOM   2490  CE2 PHE B 302      -8.163 -21.446  33.817  1.00 45.93           C  
ANISOU 2490  CE2 PHE B 302     9415   4666   3371   1498   -939   -468       C  
ATOM   2491  CZ  PHE B 302      -8.968 -20.314  33.949  1.00 46.48           C  
ANISOU 2491  CZ  PHE B 302     9310   4817   3531   1549   -948   -335       C  
ATOM   2492  N   THR B 303     -11.881 -24.335  28.702  1.00 35.39           N  
ANISOU 2492  N   THR B 303     6928   3722   2794    725   -310    257       N  
ATOM   2493  CA  THR B 303     -12.179 -24.920  27.401  1.00 34.86           C  
ANISOU 2493  CA  THR B 303     6720   3584   2939    926   -359     83       C  
ATOM   2494  C   THR B 303     -12.435 -23.852  26.338  1.00 35.90           C  
ANISOU 2494  C   THR B 303     6872   3570   3196    772   -437    226       C  
ATOM   2495  O   THR B 303     -13.119 -22.861  26.602  1.00 39.87           O  
ANISOU 2495  O   THR B 303     6549   4128   4470    984   -246     26       O  
ATOM   2496  CB  THR B 303     -13.314 -25.974  27.480  1.00 35.98           C  
ANISOU 2496  CB  THR B 303     6486   4070   3113    854   -103    168       C  
ATOM   2497  OG1 THR B 303     -13.412 -26.664  26.228  1.00 39.59           O  
ANISOU 2497  OG1 THR B 303     7476   3964   3600    530     32   -168       O  
ATOM   2498  CG2 THR B 303     -14.671 -25.351  27.845  1.00 35.43           C  
ANISOU 2498  CG2 THR B 303     6524   3989   2949   1087   -525     28       C  
ATOM   2499  N   ALA B 304     -11.854 -24.047  25.153  1.00 34.30           N  
ANISOU 2499  N   ALA B 304     6517   3327   3186    477   -491     71       N  
ATOM   2500  CA  ALA B 304     -12.058 -23.130  24.022  1.00 33.43           C  
ANISOU 2500  CA  ALA B 304     6086   3180   3437    306   -595    154       C  
ATOM   2501  C   ALA B 304     -13.494 -23.179  23.499  1.00 33.30           C  
ANISOU 2501  C   ALA B 304     6019   3192   3442    484   -491    173       C  
ATOM   2502  O   ALA B 304     -14.090 -22.138  23.240  1.00 33.50           O  
ANISOU 2502  O   ALA B 304     6122   3171   3436    526   -388    118       O  
ATOM   2503  CB  ALA B 304     -11.063 -23.410  22.900  1.00 30.79           C  
ANISOU 2503  CB  ALA B 304     6112   2722   2862     92   -731    329       C  
ATOM   2504  N   ARG B 305     -14.038 -24.389  23.363  1.00 33.62           N  
ANISOU 2504  N   ARG B 305     5729   3427   3615    194   -221    275       N  
ATOM   2505  CA  ARG B 305     -15.384 -24.613  22.834  1.00 33.10           C  
ANISOU 2505  CA  ARG B 305     5633   3410   3532    352   -144    392       C  
ATOM   2506  C   ARG B 305     -16.137 -25.597  23.719  1.00 34.50           C  
ANISOU 2506  C   ARG B 305     5741   3503   3865    277    -15    475       C  
ATOM   2507  O   ARG B 305     -15.517 -26.393  24.429  1.00 34.24           O  
ANISOU 2507  O   ARG B 305     6386   3137   3486    372    512    586       O  
ATOM   2508  CB  ARG B 305     -15.313 -25.200  21.425  1.00 33.95           C  
ANISOU 2508  CB  ARG B 305     5939   3413   3546    267   -263    320       C  
ATOM   2509  CG  ARG B 305     -14.744 -24.283  20.347  1.00 32.00           C  
ANISOU 2509  CG  ARG B 305     5685   2738   3735    187   -149      3       C  
ATOM   2510  CD  ARG B 305     -14.769 -24.973  18.987  1.00 29.02           C  
ANISOU 2510  CD  ARG B 305     5208   2434   3384    -50   -246    345       C  
ATOM   2511  NE  ARG B 305     -14.088 -26.271  19.047  1.00 27.41           N  
ANISOU 2511  NE  ARG B 305     4770   2511   3131    -82   -277    234       N  
ATOM   2512  CZ  ARG B 305     -12.784 -26.461  18.852  1.00 26.50           C  
ANISOU 2512  CZ  ARG B 305     4797   2291   2980   -249    -35    124       C  
ATOM   2513  NH1 ARG B 305     -12.270 -27.687  18.962  1.00 25.47           N  
ANISOU 2513  NH1 ARG B 305     5039   2550   2087    -59    -65    731       N  
ATOM   2514  NH2 ARG B 305     -11.994 -25.440  18.542  1.00 25.90           N  
ANISOU 2514  NH2 ARG B 305     4785   2148   2907   -255   -277    187       N  
ATOM   2515  N   LEU B 306     -17.466 -25.545  23.671  1.00 32.73           N  
ANISOU 2515  N   LEU B 306     5698   3132   3606    222     51    539       N  
ATOM   2516  CA  LEU B 306     -18.299 -26.535  24.345  1.00 34.45           C  
ANISOU 2516  CA  LEU B 306     5776   3648   3664    237    487    617       C  
ATOM   2517  C   LEU B 306     -18.761 -27.617  23.371  1.00 35.56           C  
ANISOU 2517  C   LEU B 306     5901   3502   4106    -61    509    693       C  
ATOM   2518  O   LEU B 306     -19.483 -27.338  22.410  1.00 37.18           O  
ANISOU 2518  O   LEU B 306     6300   4089   3735   -529    490    738       O  
ATOM   2519  CB  LEU B 306     -19.493 -25.874  25.038  1.00 36.02           C  
ANISOU 2519  CB  LEU B 306     6053   3778   3854    459    580    578       C  
ATOM   2520  CG  LEU B 306     -19.221 -24.886  26.180  1.00 36.38           C  
ANISOU 2520  CG  LEU B 306     6115   4042   3663    739    808    511       C  
ATOM   2521  CD1 LEU B 306     -20.519 -24.199  26.567  1.00 35.45           C  
ANISOU 2521  CD1 LEU B 306     6200   4085   3182   1061    584    728       C  
ATOM   2522  CD2 LEU B 306     -18.577 -25.551  27.395  1.00 37.41           C  
ANISOU 2522  CD2 LEU B 306     6613   3745   3855    737    956    822       C  
ATOM   2523  N   TYR B 307     -18.325 -28.848  23.631  1.00 36.57           N  
ANISOU 2523  N   TYR B 307     6231   3488   4175   -118    695    995       N  
ATOM   2524  CA  TYR B 307     -18.630 -30.010  22.801  1.00 36.22           C  
ANISOU 2524  CA  TYR B 307     6268   3548   3946   -343    743   1022       C  
ATOM   2525  C   TYR B 307     -20.038 -30.496  23.109  1.00 38.97           C  
ANISOU 2525  C   TYR B 307     6311   3840   4654   -470    631   1077       C  
ATOM   2526  O   TYR B 307     -20.327 -30.902  24.242  1.00 42.75           O  
ANISOU 2526  O   TYR B 307     7179   4301   4759    -30    453   1586       O  
ATOM   2527  CB  TYR B 307     -17.589 -31.114  23.057  1.00 37.98           C  
ANISOU 2527  CB  TYR B 307     6799   3441   4188   -284    780   1484       C  
ATOM   2528  CG  TYR B 307     -17.538 -32.251  22.042  1.00 45.07           C  
ANISOU 2528  CG  TYR B 307     7673   4247   5202   -681    740    686       C  
ATOM   2529  CD1 TYR B 307     -17.460 -31.993  20.663  1.00 46.67           C  
ANISOU 2529  CD1 TYR B 307     7790   4626   5313   -971    799    856       C  
ATOM   2530  CD2 TYR B 307     -17.517 -33.589  22.465  1.00 47.87           C  
ANISOU 2530  CD2 TYR B 307     7988   4522   5678   -931    923   1090       C  
ATOM   2531  CE1 TYR B 307     -17.395 -33.027  19.739  1.00 49.65           C  
ANISOU 2531  CE1 TYR B 307     8668   4545   5652  -1036    744    750       C  
ATOM   2532  CE2 TYR B 307     -17.455 -34.637  21.544  1.00 50.43           C  
ANISOU 2532  CE2 TYR B 307     8070   5014   6075   -313   1158    673       C  
ATOM   2533  CZ  TYR B 307     -17.391 -34.346  20.183  1.00 51.80           C  
ANISOU 2533  CZ  TYR B 307     8750   4732   6199   -539    595   1037       C  
ATOM   2534  OH  TYR B 307     -17.330 -35.361  19.254  1.00 51.98           O  
ANISOU 2534  OH  TYR B 307     8671   3531   7548  -1835    154    983       O  
ATOM   2535  N   TYR B 308     -20.911 -30.426  22.101  1.00 37.76           N  
ANISOU 2535  N   TYR B 308     6205   3837   4306   -585    856   1311       N  
ATOM   2536  CA  TYR B 308     -22.328 -30.835  22.202  1.00 39.31           C  
ANISOU 2536  CA  TYR B 308     6154   4049   4730   -565   1154   1586       C  
ATOM   2537  C   TYR B 308     -23.079 -30.158  23.349  1.00 37.57           C  
ANISOU 2537  C   TYR B 308     5789   4364   4121  -1440   1628   1906       C  
ATOM   2538  O   TYR B 308     -23.759 -30.836  24.130  1.00 42.73           O  
ANISOU 2538  O   TYR B 308     6473   4763   4997  -1450   2015   1952       O  
ATOM   2539  CB  TYR B 308     -22.478 -32.369  22.310  1.00 38.71           C  
ANISOU 2539  CB  TYR B 308     5927   4081   4698   -834   1242   1652       C  
ATOM   2540  CG  TYR B 308     -22.218 -33.133  21.040  1.00 40.87           C  
ANISOU 2540  CG  TYR B 308     6639   3733   5157  -1027    620   1161       C  
ATOM   2541  CD1 TYR B 308     -23.235 -33.327  20.096  1.00 42.14           C  
ANISOU 2541  CD1 TYR B 308     5961   4116   5932  -1412    682   1366       C  
ATOM   2542  CD2 TYR B 308     -20.956 -33.682  20.779  1.00 40.79           C  
ANISOU 2542  CD2 TYR B 308     6536   3924   5038   -906    204   1488       C  
ATOM   2543  CE1 TYR B 308     -22.998 -34.037  18.920  1.00 43.04           C  
ANISOU 2543  CE1 TYR B 308     6409   4155   5787  -1482    627   1355       C  
ATOM   2544  CE2 TYR B 308     -20.711 -34.396  19.612  1.00 42.08           C  
ANISOU 2544  CE2 TYR B 308     6722   3785   5480   -763    721   1302       C  
ATOM   2545  CZ  TYR B 308     -21.733 -34.569  18.689  1.00 44.17           C  
ANISOU 2545  CZ  TYR B 308     6860   4187   5736  -1081    647    928       C  
ATOM   2546  OH  TYR B 308     -21.484 -35.271  17.539  1.00 47.21           O  
ANISOU 2546  OH  TYR B 308     7530   4122   6284   -865    743    578       O  
ATOM   2547  N   PHE B 309     -22.979 -28.832  23.446  1.00 41.47           N  
ANISOU 2547  N   PHE B 309     6423   4388   4944  -1048   1316   1589       N  
ATOM   2548  CA  PHE B 309     -23.552 -28.109  24.596  1.00 45.40           C  
ANISOU 2548  CA  PHE B 309     6632   4867   5749   -284   1437   1310       C  
ATOM   2549  C   PHE B 309     -25.080 -28.192  24.711  1.00 46.85           C  
ANISOU 2549  C   PHE B 309     6701   4785   6314   -886   1293   1477       C  
ATOM   2550  O   PHE B 309     -25.633 -27.993  25.793  1.00 54.64           O  
ANISOU 2550  O   PHE B 309     7955   5905   6899   -257   1877   1270       O  
ATOM   2551  CB  PHE B 309     -23.063 -26.647  24.661  1.00 44.20           C  
ANISOU 2551  CB  PHE B 309     6295   4972   5525   -381   1141   1347       C  
ATOM   2552  CG  PHE B 309     -23.515 -25.785  23.512  1.00 42.69           C  
ANISOU 2552  CG  PHE B 309     5905   4838   5477   -331    970   1138       C  
ATOM   2553  CD1 PHE B 309     -24.796 -25.217  23.496  1.00 42.95           C  
ANISOU 2553  CD1 PHE B 309     5887   4940   5492   -312    903   1125       C  
ATOM   2554  CD2 PHE B 309     -22.647 -25.503  22.457  1.00 43.13           C  
ANISOU 2554  CD2 PHE B 309     5858   5319   5209   -220    884    889       C  
ATOM   2555  CE1 PHE B 309     -25.207 -24.411  22.440  1.00 40.80           C  
ANISOU 2555  CE1 PHE B 309     5593   4391   5518   -471    923   1036       C  
ATOM   2556  CE2 PHE B 309     -23.051 -24.690  21.397  1.00 40.30           C  
ANISOU 2556  CE2 PHE B 309     5459   4223   5627     77    828    584       C  
ATOM   2557  CZ  PHE B 309     -24.332 -24.149  21.388  1.00 39.50           C  
ANISOU 2557  CZ  PHE B 309     5298   4237   5470    -92    881    822       C  
ATOM   2558  N   TRP B 310     -25.736 -28.489  23.591  1.00 47.84           N  
ANISOU 2558  N   TRP B 310     6818   5457   5901   -812   1400   1481       N  
ATOM   2559  CA  TRP B 310     -27.196 -28.648  23.503  1.00 50.67           C  
ANISOU 2559  CA  TRP B 310     6760   6055   6437   -710   1407   1533       C  
ATOM   2560  C   TRP B 310     -27.682 -30.041  23.925  1.00 49.72           C  
ANISOU 2560  C   TRP B 310     6683   6500   5705   -936   2059   1651       C  
ATOM   2561  O   TRP B 310     -28.879 -30.245  24.124  1.00 55.96           O  
ANISOU 2561  O   TRP B 310     7024   7355   6881  -1915   2032   1860       O  
ATOM   2562  CB  TRP B 310     -27.656 -28.360  22.067  1.00 51.21           C  
ANISOU 2562  CB  TRP B 310     6902   5930   6624   -704    948   1272       C  
ATOM   2563  CG  TRP B 310     -26.971 -29.241  21.056  1.00 47.24           C  
ANISOU 2563  CG  TRP B 310     6039   5865   6045  -1237   1099   1601       C  
ATOM   2564  CD1 TRP B 310     -27.398 -30.460  20.608  1.00 48.84           C  
ANISOU 2564  CD1 TRP B 310     6403   5919   6235  -1195   1184   1435       C  
ATOM   2565  CD2 TRP B 310     -25.726 -28.986  20.399  1.00 43.79           C  
ANISOU 2565  CD2 TRP B 310     5760   5003   5874  -1172    755   1621       C  
ATOM   2566  NE1 TRP B 310     -26.503 -30.974  19.707  1.00 46.68           N  
ANISOU 2566  NE1 TRP B 310     6075   5485   6176  -1405    920   1347       N  
ATOM   2567  CE2 TRP B 310     -25.467 -30.091  19.557  1.00 44.83           C  
ANISOU 2567  CE2 TRP B 310     5904   5211   5917  -1264    801   1400       C  
ATOM   2568  CE3 TRP B 310     -24.799 -27.926  20.436  1.00 43.06           C  
ANISOU 2568  CE3 TRP B 310     5726   4766   5869  -1041   1054   1642       C  
ATOM   2569  CZ2 TRP B 310     -24.323 -30.172  18.760  1.00 42.17           C  
ANISOU 2569  CZ2 TRP B 310     5961   4616   5443  -1382    754   1498       C  
ATOM   2570  CZ3 TRP B 310     -23.662 -28.005  19.638  1.00 39.25           C  
ANISOU 2570  CZ3 TRP B 310     5196   4076   5638  -1312    693   1437       C  
ATOM   2571  CH2 TRP B 310     -23.436 -29.121  18.811  1.00 39.78           C  
ANISOU 2571  CH2 TRP B 310     5709   4487   4916  -1237    570   1356       C  
ATOM   2572  N   ASP B 311     -26.754 -30.992  24.025  1.00 50.20           N  
ANISOU 2572  N   ASP B 311     7028   6095   5948  -1058   1482   1749       N  
ATOM   2573  CA  ASP B 311     -27.058 -32.376  24.391  1.00 53.01           C  
ANISOU 2573  CA  ASP B 311     7109   6381   6649  -1698   1700   1871       C  
ATOM   2574  C   ASP B 311     -27.109 -32.525  25.905  1.00 55.41           C  
ANISOU 2574  C   ASP B 311     7762   6597   6691  -1160   2012   1776       C  
ATOM   2575  O   ASP B 311     -26.150 -32.192  26.607  1.00 58.98           O  
ANISOU 2575  O   ASP B 311     8167   7282   6959   -780   1618   1619       O  
ATOM   2576  CB  ASP B 311     -26.022 -33.337  23.789  1.00 58.19           C  
ANISOU 2576  CB  ASP B 311     8298   6652   7157   -915   1509   1825       C  
ATOM   2577  CG  ASP B 311     -26.391 -34.808  23.980  1.00 65.69           C  
ANISOU 2577  CG  ASP B 311     9783   6813   8362  -1171    945   2155       C  
ATOM   2578  OD1 ASP B 311     -26.388 -35.304  25.133  1.00 67.61           O  
ANISOU 2578  OD1 ASP B 311     9581   7940   8165    254   1592   2192       O  
ATOM   2579  OD2 ASP B 311     -26.665 -35.477  22.961  1.00 68.01           O  
ANISOU 2579  OD2 ASP B 311    11237   5921   8681   -278    300   2102       O  
ATOM   2580  N   THR B 312     -28.226 -33.061  26.387  1.00 56.40           N  
ANISOU 2580  N   THR B 312     8140   6555   6733   -892   2205   2672       N  
ATOM   2581  CA  THR B 312     -28.497 -33.194  27.820  1.00 60.89           C  
ANISOU 2581  CA  THR B 312     8343   7914   6877  -1158   2641   2345       C  
ATOM   2582  C   THR B 312     -27.447 -34.019  28.600  1.00 61.66           C  
ANISOU 2582  C   THR B 312     9242   7575   6611   -914   2752   2516       C  
ATOM   2583  O   THR B 312     -27.125 -33.686  29.738  1.00 63.81           O  
ANISOU 2583  O   THR B 312    10316   7808   6120   -699   3501   2442       O  
ATOM   2584  CB  THR B 312     -29.958 -33.646  28.084  1.00 63.90           C  
ANISOU 2584  CB  THR B 312     8535   7810   7932  -1612   2696   2299       C  
ATOM   2585  OG1 THR B 312     -30.186 -33.758  29.493  1.00 70.25           O  
ANISOU 2585  OG1 THR B 312     9676   9229   7786  -1628   2755    458       O  
ATOM   2586  CG2 THR B 312     -30.285 -34.979  27.400  1.00 63.59           C  
ANISOU 2586  CG2 THR B 312     9205   8766   6189  -1097   2813   1591       C  
ATOM   2587  N   ASP B 313     -26.893 -35.054  27.966  1.00 63.84           N  
ANISOU 2587  N   ASP B 313     9685   7189   7381   -982   2366   2354       N  
ATOM   2588  CA  ASP B 313     -25.869 -35.916  28.588  1.00 66.53           C  
ANISOU 2588  CA  ASP B 313     9581   7986   7708  -1252   1815   2393       C  
ATOM   2589  C   ASP B 313     -24.502 -35.240  28.733  1.00 57.54           C  
ANISOU 2589  C   ASP B 313     9661   6339   5860  -1139   2096   2937       C  
ATOM   2590  O   ASP B 313     -23.773 -35.504  29.696  1.00 62.46           O  
ANISOU 2590  O   ASP B 313    10621   7693   5415  -1016   1879   3032       O  
ATOM   2591  CB  ASP B 313     -25.711 -37.234  27.813  1.00 70.12           C  
ANISOU 2591  CB  ASP B 313    10444   7761   8438  -1577   1767   2331       C  
ATOM   2592  CG  ASP B 313     -27.035 -37.930  27.555  1.00 75.49           C  
ANISOU 2592  CG  ASP B 313    11230   8235   9218  -2583   1998   2096       C  
ATOM   2593  OD1 ASP B 313     -27.817 -38.126  28.512  1.00 77.56           O  
ANISOU 2593  OD1 ASP B 313    11857   8072   9538  -4295   1899   2874       O  
ATOM   2594  OD2 ASP B 313     -27.290 -38.284  26.386  1.00 84.41           O  
ANISOU 2594  OD2 ASP B 313    12322   9652  10099  -3272   1717    689       O  
ATOM   2595  N   TYR B 314     -24.155 -34.388  27.768  1.00 50.29           N  
ANISOU 2595  N   TYR B 314     8302   5300   5504   -635   1855   2473       N  
ATOM   2596  CA  TYR B 314     -22.898 -33.638  27.808  1.00 49.02           C  
ANISOU 2596  CA  TYR B 314     8209   5097   5317   -436   1726   2159       C  
ATOM   2597  C   TYR B 314     -22.978 -32.540  28.866  1.00 52.02           C  
ANISOU 2597  C   TYR B 314     8537   5577   5649   -253   2053   1899       C  
ATOM   2598  O   TYR B 314     -22.006 -32.299  29.593  1.00 52.91           O  
ANISOU 2598  O   TYR B 314     8497   5032   6572   -665   1914   2016       O  
ATOM   2599  CB  TYR B 314     -22.546 -33.079  26.422  1.00 47.64           C  
ANISOU 2599  CB  TYR B 314     7964   5067   5067   -753   1647   1781       C  
ATOM   2600  CG  TYR B 314     -22.087 -34.141  25.432  1.00 47.80           C  
ANISOU 2600  CG  TYR B 314     7782   5148   5229   -701   1629   1784       C  
ATOM   2601  CD1 TYR B 314     -22.982 -35.104  24.936  1.00 49.65           C  
ANISOU 2601  CD1 TYR B 314     8097   4894   5872   -712   1416   1865       C  
ATOM   2602  CD2 TYR B 314     -20.761 -34.183  24.984  1.00 46.46           C  
ANISOU 2602  CD2 TYR B 314     7822   4775   5055   -769   1697   2054       C  
ATOM   2603  CE1 TYR B 314     -22.573 -36.078  24.034  1.00 47.49           C  
ANISOU 2603  CE1 TYR B 314     8048   4528   5467   -991   1660   2184       C  
ATOM   2604  CE2 TYR B 314     -20.343 -35.151  24.073  1.00 46.64           C  
ANISOU 2604  CE2 TYR B 314     7874   4238   5609   -699   1399   1972       C  
ATOM   2605  CZ  TYR B 314     -21.253 -36.098  23.606  1.00 48.32           C  
ANISOU 2605  CZ  TYR B 314     7849   4919   5591   -967   1336   1954       C  
ATOM   2606  OH  TYR B 314     -20.859 -37.069  22.710  1.00 51.59           O  
ANISOU 2606  OH  TYR B 314     8730   5097   5774  -1143   1866   1800       O  
ATOM   2607  N   GLN B 315     -24.151 -31.906  28.957  1.00 51.75           N  
ANISOU 2607  N   GLN B 315     8090   6636   4935   -307   2352   1980       N  
ATOM   2608  CA  GLN B 315     -24.466 -30.927  30.001  1.00 53.09           C  
ANISOU 2608  CA  GLN B 315     7975   6807   5389    -35   2208   1727       C  
ATOM   2609  C   GLN B 315     -24.309 -31.527  31.403  1.00 56.65           C  
ANISOU 2609  C   GLN B 315     8900   6913   5709    -37   2053   2098       C  
ATOM   2610  O   GLN B 315     -23.652 -30.928  32.261  1.00 60.10           O  
ANISOU 2610  O   GLN B 315     9814   7522   5497    523   1526   1901       O  
ATOM   2611  CB  GLN B 315     -25.887 -30.387  29.831  1.00 49.29           C  
ANISOU 2611  CB  GLN B 315     8018   5817   4890    102   2218   1694       C  
ATOM   2612  CG  GLN B 315     -26.107 -29.515  28.608  1.00 50.06           C  
ANISOU 2612  CG  GLN B 315     8105   5311   5604    -80   1936   1890       C  
ATOM   2613  CD  GLN B 315     -27.573 -29.156  28.397  1.00 54.50           C  
ANISOU 2613  CD  GLN B 315     8054   6153   6498    174   2477   2019       C  
ATOM   2614  OE1 GLN B 315     -28.426 -29.421  29.248  1.00 58.17           O  
ANISOU 2614  OE1 GLN B 315     8577   6742   6780    -18   2668   2556       O  
ATOM   2615  NE2 GLN B 315     -27.872 -28.553  27.256  1.00 57.16           N  
ANISOU 2615  NE2 GLN B 315     9228   6143   6345    293   3062   2353       N  
ATOM   2616  N   GLU B 316     -24.900 -32.707  31.620  1.00 57.95           N  
ANISOU 2616  N   GLU B 316     9170   6764   6085    -53   1759   2254       N  
ATOM   2617  CA  GLU B 316     -24.799 -33.422  32.900  1.00 61.17           C  
ANISOU 2617  CA  GLU B 316     9752   7624   5866     -1   1860   2271       C  
ATOM   2618  C   GLU B 316     -23.356 -33.797  33.213  1.00 59.68           C  
ANISOU 2618  C   GLU B 316     9809   7037   5827    450   2479   2184       C  
ATOM   2619  O   GLU B 316     -22.949 -33.767  34.375  1.00 63.83           O  
ANISOU 2619  O   GLU B 316    10907   7589   5754    964   2562   2842       O  
ATOM   2620  CB  GLU B 316     -25.705 -34.660  32.927  1.00 68.19           C  
ANISOU 2620  CB  GLU B 316    10507   8366   7034   -728   1927   2814       C  
ATOM   2621  CG  GLU B 316     -27.166 -34.345  33.240  1.00 81.13           C  
ANISOU 2621  CG  GLU B 316    11306  10638   8881   -191   3167   3061       C  
ATOM   2622  CD  GLU B 316     -28.118 -35.504  32.961  1.00 94.78           C  
ANISOU 2622  CD  GLU B 316    13137  12051  10824  -1424   3018   2654       C  
ATOM   2623  OE1 GLU B 316     -28.069 -36.091  31.854  1.00 96.87           O  
ANISOU 2623  OE1 GLU B 316    13580  12524  10701  -2225   3635   2634       O  
ATOM   2624  OE2 GLU B 316     -28.939 -35.818  33.852  1.00 99.33           O  
ANISOU 2624  OE2 GLU B 316    12551  13896  11293   -153   4222    802       O  
ATOM   2625  N   GLY B 317     -22.592 -34.120  32.167  1.00 56.48           N  
ANISOU 2625  N   GLY B 317     9388   6368   5701    -22   1991   1375       N  
ATOM   2626  CA  GLY B 317     -21.150 -34.346  32.268  1.00 54.86           C  
ANISOU 2626  CA  GLY B 317     9436   6177   5229    250   2065   1584       C  
ATOM   2627  C   GLY B 317     -20.413 -33.152  32.851  1.00 52.60           C  
ANISOU 2627  C   GLY B 317     9154   5730   5100    692   1747   1819       C  
ATOM   2628  O   GLY B 317     -19.619 -33.305  33.787  1.00 52.49           O  
ANISOU 2628  O   GLY B 317     9836   5846   4262    982   1876   1722       O  
ATOM   2629  N   LEU B 318     -20.697 -31.965  32.310  1.00 49.44           N  
ANISOU 2629  N   LEU B 318     8540   5526   4717    689   2272   1635       N  
ATOM   2630  CA  LEU B 318     -20.112 -30.709  32.803  1.00 47.57           C  
ANISOU 2630  CA  LEU B 318     8519   5468   4087    972   2077   1510       C  
ATOM   2631  C   LEU B 318     -20.552 -30.356  34.226  1.00 49.35           C  
ANISOU 2631  C   LEU B 318     8955   5618   4175   1154   1990   1190       C  
ATOM   2632  O   LEU B 318     -19.729 -29.921  35.035  1.00 52.11           O  
ANISOU 2632  O   LEU B 318     9502   5275   5022   1344   1521    914       O  
ATOM   2633  CB  LEU B 318     -20.403 -29.546  31.847  1.00 46.39           C  
ANISOU 2633  CB  LEU B 318     8463   5093   4068    475   1786   1383       C  
ATOM   2634  CG  LEU B 318     -19.845 -29.584  30.417  1.00 45.37           C  
ANISOU 2634  CG  LEU B 318     8242   5001   3994    768   1611   1333       C  
ATOM   2635  CD1 LEU B 318     -20.189 -28.291  29.695  1.00 45.74           C  
ANISOU 2635  CD1 LEU B 318     8545   4607   4226    725   1375   1161       C  
ATOM   2636  CD2 LEU B 318     -18.339 -29.820  30.374  1.00 48.63           C  
ANISOU 2636  CD2 LEU B 318     8261   5648   4564    966   1342    569       C  
ATOM   2637  N   ARG B 319     -21.839 -30.559  34.517  1.00 50.88           N  
ANISOU 2637  N   ARG B 319     9001   6154   4177   1079   2266   1711       N  
ATOM   2638  CA  ARG B 319     -22.413 -30.325  35.847  1.00 55.54           C  
ANISOU 2638  CA  ARG B 319     9691   7035   4377   1051   2507   1360       C  
ATOM   2639  C   ARG B 319     -21.768 -31.225  36.896  1.00 60.94           C  
ANISOU 2639  C   ARG B 319    10257   7617   5278   1571   2292   1722       C  
ATOM   2640  O   ARG B 319     -21.444 -30.763  37.996  1.00 64.01           O  
ANISOU 2640  O   ARG B 319    10943   8470   4907   1753   3349   1139       O  
ATOM   2641  CB  ARG B 319     -23.928 -30.551  35.837  1.00 57.10           C  
ANISOU 2641  CB  ARG B 319     9631   7676   4385   1277   2627   1795       C  
ATOM   2642  CG  ARG B 319     -24.733 -29.458  35.150  1.00 57.81           C  
ANISOU 2642  CG  ARG B 319     9192   7466   5306   1690   2587   1171       C  
ATOM   2643  CD  ARG B 319     -26.218 -29.797  35.111  1.00 59.33           C  
ANISOU 2643  CD  ARG B 319     9002   8330   5208   1670   3212   1512       C  
ATOM   2644  NE  ARG B 319     -26.828 -29.825  36.444  1.00 62.24           N  
ANISOU 2644  NE  ARG B 319     9476   8724   5446   1084   3497   2356       N  
ATOM   2645  CZ  ARG B 319     -27.292 -28.761  37.100  1.00 66.36           C  
ANISOU 2645  CZ  ARG B 319     9990   9262   5959   1408   3636   2060       C  
ATOM   2646  NH1 ARG B 319     -27.224 -27.545  36.570  1.00 72.89           N  
ANISOU 2646  NH1 ARG B 319     9594   9529   8570    608   3707   2828       N  
ATOM   2647  NH2 ARG B 319     -27.827 -28.915  38.303  1.00 65.80           N  
ANISOU 2647  NH2 ARG B 319     9781   9216   6004    954   3518   2374       N  
ATOM   2648  N   SER B 320     -21.585 -32.498  36.535  1.00 61.74           N  
ANISOU 2648  N   SER B 320    10479   7564   5412   1460   2486   1574       N  
ATOM   2649  CA  SER B 320     -20.917 -33.497  37.371  1.00 63.53           C  
ANISOU 2649  CA  SER B 320    11114   7732   5290   1492   2652   1892       C  
ATOM   2650  C   SER B 320     -19.495 -33.069  37.758  1.00 61.92           C  
ANISOU 2650  C   SER B 320    11341   7247   4937   1675   2377   2051       C  
ATOM   2651  O   SER B 320     -19.110 -33.189  38.920  1.00 67.78           O  
ANISOU 2651  O   SER B 320    12148   8253   5352   2642   1855   2480       O  
ATOM   2652  CB  SER B 320     -20.905 -34.854  36.659  1.00 64.40           C  
ANISOU 2652  CB  SER B 320    11911   6920   5635    610   2689   2617       C  
ATOM   2653  OG  SER B 320     -20.036 -35.767  37.295  1.00 76.68           O  
ANISOU 2653  OG  SER B 320    12925   7509   8698   1511   1823   2434       O  
ATOM   2654  N   LEU B 321     -18.739 -32.565  36.781  1.00 56.91           N  
ANISOU 2654  N   LEU B 321    11128   5770   4723   1470   2111   1663       N  
ATOM   2655  CA  LEU B 321     -17.387 -32.039  36.997  1.00 58.46           C  
ANISOU 2655  CA  LEU B 321    10886   6974   4351   1691   1736   1378       C  
ATOM   2656  C   LEU B 321     -17.365 -30.897  38.006  1.00 61.88           C  
ANISOU 2656  C   LEU B 321    11395   7695   4419   1959   1827    974       C  
ATOM   2657  O   LEU B 321     -16.579 -30.923  38.955  1.00 65.40           O  
ANISOU 2657  O   LEU B 321    11678   8193   4975   2946   1442    599       O  
ATOM   2658  CB  LEU B 321     -16.764 -31.571  35.672  1.00 55.96           C  
ANISOU 2658  CB  LEU B 321    10054   6998   4209   1651   1788    854       C  
ATOM   2659  CG  LEU B 321     -16.272 -32.640  34.693  1.00 52.56           C  
ANISOU 2659  CG  LEU B 321     9900   6170   3897   1401   1794   1379       C  
ATOM   2660  CD1 LEU B 321     -15.921 -32.024  33.344  1.00 49.27           C  
ANISOU 2660  CD1 LEU B 321     9686   5621   3412   1022   1225    988       C  
ATOM   2661  CD2 LEU B 321     -15.082 -33.389  35.281  1.00 50.03           C  
ANISOU 2661  CD2 LEU B 321    10369   5019   3618   1298   1445   1130       C  
ATOM   2662  N   SER B 322     -18.248 -29.917  37.791  1.00 63.98           N  
ANISOU 2662  N   SER B 322    11429   7575   5305   1901   1778   1197       N  
ATOM   2663  CA  SER B 322     -18.375 -28.728  38.638  1.00 66.07           C  
ANISOU 2663  CA  SER B 322    11814   8045   5241   2243   1870   1051       C  
ATOM   2664  C   SER B 322     -18.771 -29.060  40.074  1.00 67.14           C  
ANISOU 2664  C   SER B 322    12019   8354   5136   2309   1852    962       C  
ATOM   2665  O   SER B 322     -18.303 -28.414  41.016  1.00 74.08           O  
ANISOU 2665  O   SER B 322    13891   9624   4630   2804   1670    315       O  
ATOM   2666  CB  SER B 322     -19.388 -27.756  38.028  1.00 69.72           C  
ANISOU 2666  CB  SER B 322    11582   8610   6296   2371   1141    789       C  
ATOM   2667  OG  SER B 322     -19.514 -26.581  38.809  1.00 71.36           O  
ANISOU 2667  OG  SER B 322    11291   8924   6898   2481   -670    277       O  
ATOM   2668  N   GLN B 323     -19.625 -30.070  40.223  1.00 65.88           N  
ANISOU 2668  N   GLN B 323    11947   8456   4624   2249   2355   1291       N  
ATOM   2669  CA  GLN B 323     -20.117 -30.505  41.526  1.00 69.25           C  
ANISOU 2669  CA  GLN B 323    12320   9289   4702   2291   2657   1322       C  
ATOM   2670  C   GLN B 323     -19.080 -31.299  42.327  1.00 66.04           C  
ANISOU 2670  C   GLN B 323    12857   7678   4557   1804   2371   1264       C  
ATOM   2671  O   GLN B 323     -19.208 -31.436  43.545  1.00 66.91           O  
ANISOU 2671  O   GLN B 323    13262   7596   4565   1305   1809   1982       O  
ATOM   2672  CB  GLN B 323     -21.429 -31.283  41.367  1.00 80.45           C  
ANISOU 2672  CB  GLN B 323    12964  11279   6322   1448   2682   1428       C  
ATOM   2673  CG  GLN B 323     -22.628 -30.380  41.080  1.00 88.19           C  
ANISOU 2673  CG  GLN B 323    13552  12838   7118   2405   2926   1173       C  
ATOM   2674  CD  GLN B 323     -23.896 -31.139  40.721  1.00 93.95           C  
ANISOU 2674  CD  GLN B 323    14660  13099   7936   1615   2545   1778       C  
ATOM   2675  OE1 GLN B 323     -24.318 -32.057  41.430  1.00101.98           O  
ANISOU 2675  OE1 GLN B 323    16742  12351   9651   1219   3076   1933       O  
ATOM   2676  NE2 GLN B 323     -24.524 -30.740  39.621  1.00 97.98           N  
ANISOU 2676  NE2 GLN B 323    14233  14907   8084   2982   2968   2104       N  
ATOM   2677  N   GLU B 324     -18.053 -31.801  41.641  1.00 70.24           N  
ANISOU 2677  N   GLU B 324    12367   8306   6012   2149   2298   1517       N  
ATOM   2678  CA  GLU B 324     -16.956 -32.532  42.291  1.00 72.89           C  
ANISOU 2678  CA  GLU B 324    13045   8398   6252   2158   1803   1625       C  
ATOM   2679  C   GLU B 324     -15.742 -31.640  42.595  1.00 72.82           C  
ANISOU 2679  C   GLU B 324    13116   8252   6299   2217   1304   2084       C  
ATOM   2680  O   GLU B 324     -14.666 -32.129  42.968  1.00 68.17           O  
ANISOU 2680  O   GLU B 324    13889   7303   4708   2852   1749   3120       O  
ATOM   2681  CB  GLU B 324     -16.553 -33.774  41.473  1.00 67.46           C  
ANISOU 2681  CB  GLU B 324    13480   9008   3144   1829   2655   1985       C  
ATOM   2682  CG  GLU B 324     -17.632 -34.852  41.367  1.00 75.64           C  
ANISOU 2682  CG  GLU B 324    14336   8982   5419   1569   2322   1512       C  
ATOM   2683  CD  GLU B 324     -17.863 -35.663  42.639  1.00 83.08           C  
ANISOU 2683  CD  GLU B 324    14543  10418   6605    999   2727   2608       C  
ATOM   2684  OE1 GLU B 324     -17.134 -35.492  43.643  1.00 90.14           O  
ANISOU 2684  OE1 GLU B 324    14937  12375   6935   1064   2523   2173       O  
ATOM   2685  OE2 GLU B 324     -18.793 -36.496  42.629  1.00 86.15           O  
ANISOU 2685  OE2 GLU B 324    13917  11169   7646    909   2411   2038       O  
ATOM   2686  N   GLY B 325     -15.930 -30.329  42.437  1.00 67.91           N  
ANISOU 2686  N   GLY B 325    12318   8199   5284   2556   2013   1499       N  
ATOM   2687  CA  GLY B 325     -14.910 -29.346  42.789  1.00 64.71           C  
ANISOU 2687  CA  GLY B 325    12047   7388   5148   2946   1764   2237       C  
ATOM   2688  C   GLY B 325     -14.060 -28.810  41.650  1.00 62.52           C  
ANISOU 2688  C   GLY B 325    11784   7003   4966   2550   1548   1841       C  
ATOM   2689  O   GLY B 325     -13.309 -27.848  41.852  1.00 65.75           O  
ANISOU 2689  O   GLY B 325    11541   8283   5157   2035    895   1234       O  
ATOM   2690  N   ALA B 326     -14.160 -29.426  40.467  1.00 57.74           N  
ANISOU 2690  N   ALA B 326    10850   6150   4937   2666   1849   1955       N  
ATOM   2691  CA  ALA B 326     -13.503 -28.897  39.270  1.00 54.99           C  
ANISOU 2691  CA  ALA B 326    10241   6171   4481   2548   1420   1679       C  
ATOM   2692  C   ALA B 326     -14.093 -27.541  38.929  1.00 58.36           C  
ANISOU 2692  C   ALA B 326    10673   6482   5016   2770   1655   2128       C  
ATOM   2693  O   ALA B 326     -15.315 -27.365  38.921  1.00 61.90           O  
ANISOU 2693  O   ALA B 326    10773   6632   6112   3077   1225   2082       O  
ATOM   2694  CB  ALA B 326     -13.636 -29.842  38.085  1.00 47.21           C  
ANISOU 2694  CB  ALA B 326     9714   3542   4682   3349   1917   2345       C  
ATOM   2695  N   SER B 327     -13.211 -26.579  38.689  1.00 62.31           N  
ANISOU 2695  N   SER B 327    10804   6819   6050   2274   1510   1380       N  
ATOM   2696  CA  SER B 327     -13.611 -25.271  38.202  1.00 62.25           C  
ANISOU 2696  CA  SER B 327    11703   6936   5011   2406   1539   1398       C  
ATOM   2697  C   SER B 327     -13.698 -25.363  36.680  1.00 57.12           C  
ANISOU 2697  C   SER B 327    10267   6529   4904   2235   1568   1849       C  
ATOM   2698  O   SER B 327     -12.689 -25.600  36.013  1.00 54.33           O  
ANISOU 2698  O   SER B 327    10150   6059   4432   3195    621    637       O  
ATOM   2699  CB  SER B 327     -12.595 -24.219  38.643  1.00 68.53           C  
ANISOU 2699  CB  SER B 327    12175   7438   6422   1825   2036   1516       C  
ATOM   2700  OG  SER B 327     -13.113 -22.913  38.479  1.00 83.60           O  
ANISOU 2700  OG  SER B 327    13841   8717   9203   3359   2125   1745       O  
ATOM   2701  N   VAL B 328     -14.908 -25.221  36.141  1.00 53.37           N  
ANISOU 2701  N   VAL B 328     9826   5672   4780   2313   1990   1395       N  
ATOM   2702  CA  VAL B 328     -15.118 -25.290  34.688  1.00 51.68           C  
ANISOU 2702  CA  VAL B 328     9234   5435   4968   2101   1523   1299       C  
ATOM   2703  C   VAL B 328     -15.384 -23.898  34.126  1.00 48.64           C  
ANISOU 2703  C   VAL B 328     9006   5101   4372   1787   1849    954       C  
ATOM   2704  O   VAL B 328     -16.348 -23.228  34.515  1.00 49.69           O  
ANISOU 2704  O   VAL B 328     9235   5938   3705   1832   1928    386       O  
ATOM   2705  CB  VAL B 328     -16.235 -26.286  34.275  1.00 52.11           C  
ANISOU 2705  CB  VAL B 328     9212   5747   4840   1882   1288   1630       C  
ATOM   2706  CG1 VAL B 328     -16.321 -26.405  32.757  1.00 50.98           C  
ANISOU 2706  CG1 VAL B 328     9200   5373   4797   2049   2000    942       C  
ATOM   2707  CG2 VAL B 328     -15.978 -27.662  34.868  1.00 56.34           C  
ANISOU 2707  CG2 VAL B 328     9507   5979   5918   2109   1188   2050       C  
ATOM   2708  N   GLU B 329     -14.512 -23.476  33.211  1.00 42.99           N  
ANISOU 2708  N   GLU B 329     9274   3955   3105   1737   1433    589       N  
ATOM   2709  CA  GLU B 329     -14.580 -22.147  32.619  1.00 44.78           C  
ANISOU 2709  CA  GLU B 329     9267   4066   3681   2266   1503    784       C  
ATOM   2710  C   GLU B 329     -14.273 -22.166  31.122  1.00 43.29           C  
ANISOU 2710  C   GLU B 329     8876   3895   3678   1906   1272    736       C  
ATOM   2711  O   GLU B 329     -13.682 -23.115  30.595  1.00 44.04           O  
ANISOU 2711  O   GLU B 329     9109   3711   3910   1497   1141    220       O  
ATOM   2712  CB  GLU B 329     -13.642 -21.181  33.362  1.00 48.82           C  
ANISOU 2712  CB  GLU B 329    10167   4564   3818   2074   1158    501       C  
ATOM   2713  CG  GLU B 329     -14.281 -20.528  34.592  1.00 61.74           C  
ANISOU 2713  CG  GLU B 329    11770   6808   4877   2025   2577    -12       C  
ATOM   2714  CD  GLU B 329     -13.337 -20.349  35.776  1.00 81.08           C  
ANISOU 2714  CD  GLU B 329    13761   9192   7852   1041    533   -947       C  
ATOM   2715  OE1 GLU B 329     -12.112 -20.186  35.579  1.00 86.45           O  
ANISOU 2715  OE1 GLU B 329    14566  10875   7406   1318   3374  -1443       O  
ATOM   2716  OE2 GLU B 329     -13.831 -20.360  36.927  1.00 89.42           O  
ANISOU 2716  OE2 GLU B 329    15083   9680   9212    603   2011  -1654       O  
ATOM   2717  N   ILE B 330     -14.694 -21.108  30.446  1.00 40.75           N  
ANISOU 2717  N   ILE B 330     8061   3676   3744   1787   1133    537       N  
ATOM   2718  CA  ILE B 330     -14.396 -20.930  29.046  1.00 43.46           C  
ANISOU 2718  CA  ILE B 330     8450   4270   3793   1241   1134    663       C  
ATOM   2719  C   ILE B 330     -13.149 -20.075  28.875  1.00 44.07           C  
ANISOU 2719  C   ILE B 330     8449   4005   4287   1324   1113    291       C  
ATOM   2720  O   ILE B 330     -12.991 -19.066  29.567  1.00 47.14           O  
ANISOU 2720  O   ILE B 330     9707   4033   4168    589   1043    496       O  
ATOM   2721  CB  ILE B 330     -15.648 -20.464  28.270  1.00 45.73           C  
ANISOU 2721  CB  ILE B 330     8697   4477   4200   1614   1228   1524       C  
ATOM   2722  CG1 ILE B 330     -16.432 -21.715  27.901  1.00 47.76           C  
ANISOU 2722  CG1 ILE B 330     7799   5835   4509   1073   1251   1630       C  
ATOM   2723  CG2 ILE B 330     -15.295 -19.770  26.958  1.00 39.75           C  
ANISOU 2723  CG2 ILE B 330     7722   3272   4109   1642    638   1380       C  
ATOM   2724  CD1 ILE B 330     -17.877 -21.661  28.263  1.00 51.18           C  
ANISOU 2724  CD1 ILE B 330     8415   7400   3629   2120   2061   1669       C  
ATOM   2725  N   MET B 331     -12.261 -20.516  27.977  1.00 41.22           N  
ANISOU 2725  N   MET B 331     7953   3803   3904    947    969    415       N  
ATOM   2726  CA  MET B 331     -11.025 -19.809  27.648  1.00 38.29           C  
ANISOU 2726  CA  MET B 331     7562   3261   3723   1245    943    116       C  
ATOM   2727  C   MET B 331     -11.317 -18.395  27.156  1.00 40.78           C  
ANISOU 2727  C   MET B 331     8232   3177   4084   1133    803    149       C  
ATOM   2728  O   MET B 331     -12.092 -18.207  26.218  1.00 42.30           O  
ANISOU 2728  O   MET B 331     8391   3541   4141   1036    508   -399       O  
ATOM   2729  CB  MET B 331     -10.222 -20.576  26.588  1.00 32.17           C  
ANISOU 2729  CB  MET B 331     6812   2056   3353   1100    253    222       C  
ATOM   2730  CG  MET B 331      -9.548 -21.843  27.094  1.00 25.87           C  
ANISOU 2730  CG  MET B 331     5671   1953   2203    863    444    -29       C  
ATOM   2731  SD  MET B 331      -8.603 -22.780  25.873  1.00 20.62           S  
ANISOU 2731  SD  MET B 331     5031   1000   1801    391    -21    -76       S  
ATOM   2732  CE  MET B 331      -7.130 -21.789  25.703  1.00 24.02           C  
ANISOU 2732  CE  MET B 331     5148   1863   2115    277     -2    703       C  
ATOM   2733  N   GLY B 332     -10.728 -17.411  27.833  1.00 40.18           N  
ANISOU 2733  N   GLY B 332     8413   2830   4023    954    952    429       N  
ATOM   2734  CA  GLY B 332     -10.759 -16.017  27.389  1.00 34.93           C  
ANISOU 2734  CA  GLY B 332     7740   2102   3429   1171    707   -689       C  
ATOM   2735  C   GLY B 332      -9.455 -15.682  26.693  1.00 36.25           C  
ANISOU 2735  C   GLY B 332     8235   2096   3441    744    765   -394       C  
ATOM   2736  O   GLY B 332      -8.576 -16.545  26.570  1.00 36.91           O  
ANISOU 2736  O   GLY B 332     8037   2796   3189    966    733    -59       O  
ATOM   2737  N   TYR B 333      -9.325 -14.428  26.251  1.00 37.06           N  
ANISOU 2737  N   TYR B 333     8366   2276   3438    736    699   -206       N  
ATOM   2738  CA  TYR B 333      -8.123 -13.930  25.567  1.00 39.61           C  
ANISOU 2738  CA  TYR B 333     8411   2419   4219    198    483   -246       C  
ATOM   2739  C   TYR B 333      -6.826 -14.333  26.275  1.00 39.57           C  
ANISOU 2739  C   TYR B 333     8694   2585   3754    194    274   -368       C  
ATOM   2740  O   TYR B 333      -5.902 -14.859  25.643  1.00 39.74           O  
ANISOU 2740  O   TYR B 333     8817   2949   3334    281    203   -261       O  
ATOM   2741  CB  TYR B 333      -8.195 -12.402  25.386  1.00 41.64           C  
ANISOU 2741  CB  TYR B 333     9164   2388   4268    456    165   -443       C  
ATOM   2742  CG  TYR B 333      -6.927 -11.782  24.824  1.00 46.01           C  
ANISOU 2742  CG  TYR B 333     9383   3186   4910     64    337   -346       C  
ATOM   2743  CD1 TYR B 333      -6.719 -11.688  23.444  1.00 50.32           C  
ANISOU 2743  CD1 TYR B 333     9638   4600   4882   -330    474   -957       C  
ATOM   2744  CD2 TYR B 333      -5.928 -11.294  25.675  1.00 44.70           C  
ANISOU 2744  CD2 TYR B 333     9835   2081   5066    175    293   -605       C  
ATOM   2745  CE1 TYR B 333      -5.556 -11.122  22.928  1.00 49.77           C  
ANISOU 2745  CE1 TYR B 333    10106   4051   4753   -482    687   -958       C  
ATOM   2746  CE2 TYR B 333      -4.760 -10.734  25.169  1.00 52.45           C  
ANISOU 2746  CE2 TYR B 333    10439   3340   6148   -417    593    -94       C  
ATOM   2747  CZ  TYR B 333      -4.579 -10.651  23.795  1.00 50.78           C  
ANISOU 2747  CZ  TYR B 333    10432   2971   5889   -573    238   -846       C  
ATOM   2748  OH  TYR B 333      -3.424 -10.092  23.294  1.00 53.56           O  
ANISOU 2748  OH  TYR B 333    11232   2910   6208   -142    644   1105       O  
ATOM   2749  N   LYS B 334      -6.774 -14.093  27.584  1.00 39.06           N  
ANISOU 2749  N   LYS B 334     8635   2478   3725    218    407   -228       N  
ATOM   2750  CA  LYS B 334      -5.567 -14.331  28.365  1.00 41.49           C  
ANISOU 2750  CA  LYS B 334     9188   2548   4027    260   -104   -575       C  
ATOM   2751  C   LYS B 334      -5.126 -15.799  28.387  1.00 39.11           C  
ANISOU 2751  C   LYS B 334     8431   2493   3935     61   -301   -575       C  
ATOM   2752  O   LYS B 334      -3.932 -16.074  28.418  1.00 44.05           O  
ANISOU 2752  O   LYS B 334     8398   4074   4264    114  -1012   -536       O  
ATOM   2753  CB  LYS B 334      -5.695 -13.725  29.763  1.00 47.45           C  
ANISOU 2753  CB  LYS B 334    10515   2962   4552    486     67  -1235       C  
ATOM   2754  CG  LYS B 334      -6.464 -14.515  30.811  1.00 59.42           C  
ANISOU 2754  CG  LYS B 334    11526   4963   6087     46    405     54       C  
ATOM   2755  CD  LYS B 334      -5.523 -15.252  31.761  1.00 69.79           C  
ANISOU 2755  CD  LYS B 334    12103   7094   7320    946  -1127  -1100       C  
ATOM   2756  CE  LYS B 334      -4.565 -14.314  32.492  1.00 73.11           C  
ANISOU 2756  CE  LYS B 334    12567   7970   7240    351   -907  -1604       C  
ATOM   2757  NZ  LYS B 334      -3.839 -15.033  33.576  1.00 77.15           N  
ANISOU 2757  NZ  LYS B 334    12167  11262   5884    -16   -979  -1370       N  
ATOM   2758  N   ASP B 335      -6.090 -16.719  28.344  1.00 37.02           N  
ANISOU 2758  N   ASP B 335     8088   2501   3475    125     70   -675       N  
ATOM   2759  CA  ASP B 335      -5.813 -18.159  28.291  1.00 37.98           C  
ANISOU 2759  CA  ASP B 335     8244   2553   3631    331     59   -425       C  
ATOM   2760  C   ASP B 335      -5.296 -18.613  26.918  1.00 35.52           C  
ANISOU 2760  C   ASP B 335     7539   2401   3554     58   -143   -416       C  
ATOM   2761  O   ASP B 335      -4.382 -19.440  26.844  1.00 38.41           O  
ANISOU 2761  O   ASP B 335     7780   2362   4449    262   -638   -106       O  
ATOM   2762  CB  ASP B 335      -7.052 -18.959  28.698  1.00 38.80           C  
ANISOU 2762  CB  ASP B 335     8275   2938   3529    435    174   -306       C  
ATOM   2763  CG  ASP B 335      -7.677 -18.449  29.982  1.00 45.75           C  
ANISOU 2763  CG  ASP B 335     9438   3755   4187   1133    668   -598       C  
ATOM   2764  OD1 ASP B 335      -6.982 -18.440  31.028  1.00 50.22           O  
ANISOU 2764  OD1 ASP B 335    10062   4388   4630   1087    274  -1429       O  
ATOM   2765  OD2 ASP B 335      -8.865 -18.052  29.939  1.00 50.13           O  
ANISOU 2765  OD2 ASP B 335     9778   4675   4591   1827    452   -733       O  
ATOM   2766  N   PHE B 336      -5.870 -18.073  25.840  1.00 34.39           N  
ANISOU 2766  N   PHE B 336     7123   2494   3449   -239   -228   -450       N  
ATOM   2767  CA  PHE B 336      -5.350 -18.324  24.485  1.00 33.25           C  
ANISOU 2767  CA  PHE B 336     6697   2320   3616   -102   -120   -374       C  
ATOM   2768  C   PHE B 336      -3.918 -17.817  24.341  1.00 32.81           C  
ANISOU 2768  C   PHE B 336     6775   2074   3615   -109   -133   -429       C  
ATOM   2769  O   PHE B 336      -3.073 -18.502  23.769  1.00 33.43           O  
ANISOU 2769  O   PHE B 336     7101   2268   3333   -166     97   -454       O  
ATOM   2770  CB  PHE B 336      -6.244 -17.695  23.410  1.00 32.99           C  
ANISOU 2770  CB  PHE B 336     6536   2554   3441   -227    107    -52       C  
ATOM   2771  CG  PHE B 336      -7.605 -18.324  23.302  1.00 31.87           C  
ANISOU 2771  CG  PHE B 336     6248   2211   3650    173    252   -226       C  
ATOM   2772  CD1 PHE B 336      -7.754 -19.641  22.854  1.00 30.33           C  
ANISOU 2772  CD1 PHE B 336     5844   1932   3744    308    414     87       C  
ATOM   2773  CD2 PHE B 336      -8.745 -17.593  23.631  1.00 31.19           C  
ANISOU 2773  CD2 PHE B 336     6377   2010   3462    305    302    -31       C  
ATOM   2774  CE1 PHE B 336      -9.014 -20.221  22.761  1.00 28.62           C  
ANISOU 2774  CE1 PHE B 336     5668   1911   3292    517    277     50       C  
ATOM   2775  CE2 PHE B 336     -10.007 -18.166  23.537  1.00 31.84           C  
ANISOU 2775  CE2 PHE B 336     6335   2161   3598    369    371     62       C  
ATOM   2776  CZ  PHE B 336     -10.142 -19.483  23.097  1.00 29.97           C  
ANISOU 2776  CZ  PHE B 336     5844   2071   3472    596    518    132       C  
ATOM   2777  N   LYS B 337      -3.667 -16.621  24.879  1.00 34.11           N  
ANISOU 2777  N   LYS B 337     7044   2408   3508   -438   -711   -547       N  
ATOM   2778  CA  LYS B 337      -2.354 -15.989  24.889  1.00 35.98           C  
ANISOU 2778  CA  LYS B 337     7118   2601   3952   -538   -378   -661       C  
ATOM   2779  C   LYS B 337      -1.372 -16.830  25.697  1.00 36.73           C  
ANISOU 2779  C   LYS B 337     7393   2651   3911   -614   -539   -530       C  
ATOM   2780  O   LYS B 337      -0.262 -17.099  25.241  1.00 38.41           O  
ANISOU 2780  O   LYS B 337     7224   3453   3915   -947   -500    -27       O  
ATOM   2781  CB  LYS B 337      -2.463 -14.579  25.480  1.00 38.95           C  
ANISOU 2781  CB  LYS B 337     8262   2590   3945   -891   -324   -715       C  
ATOM   2782  CG  LYS B 337      -1.188 -13.761  25.407  1.00 42.32           C  
ANISOU 2782  CG  LYS B 337     8496   3151   4430  -1202   -456   -583       C  
ATOM   2783  CD  LYS B 337      -1.452 -12.319  25.814  1.00 49.23           C  
ANISOU 2783  CD  LYS B 337     9682   3401   5619   -980   -203  -1044       C  
ATOM   2784  CE  LYS B 337      -0.279 -11.418  25.470  1.00 54.38           C  
ANISOU 2784  CE  LYS B 337     9834   3773   7054  -1668   -934  -1294       C  
ATOM   2785  NZ  LYS B 337       0.891 -11.686  26.348  1.00 57.38           N  
ANISOU 2785  NZ  LYS B 337    10524   4954   6321  -2107  -1072   -781       N  
ATOM   2786  N   TYR B 338      -1.798 -17.253  26.885  1.00 35.62           N  
ANISOU 2786  N   TYR B 338     7466   2514   3553   -410   -579  -1066       N  
ATOM   2787  CA  TYR B 338      -0.992 -18.116  27.754  1.00 39.92           C  
ANISOU 2787  CA  TYR B 338     7857   3322   3988   -324   -830   -639       C  
ATOM   2788  C   TYR B 338      -0.601 -19.432  27.049  1.00 37.76           C  
ANISOU 2788  C   TYR B 338     7094   3178   4072   -420   -987   -572       C  
ATOM   2789  O   TYR B 338       0.551 -19.868  27.143  1.00 39.69           O  
ANISOU 2789  O   TYR B 338     7507   2705   4867     13  -1042    -33       O  
ATOM   2790  CB  TYR B 338      -1.728 -18.376  29.073  1.00 39.22           C  
ANISOU 2790  CB  TYR B 338     8207   3339   3356   -346  -1061  -1108       C  
ATOM   2791  CG  TYR B 338      -0.939 -19.172  30.090  1.00 45.73           C  
ANISOU 2791  CG  TYR B 338     8627   4486   4261   -207  -1525   -645       C  
ATOM   2792  CD1 TYR B 338      -0.115 -18.529  31.031  1.00 46.42           C  
ANISOU 2792  CD1 TYR B 338     9229   4166   4242     53  -1476  -1190       C  
ATOM   2793  CD2 TYR B 338      -1.021 -20.574  30.124  1.00 44.43           C  
ANISOU 2793  CD2 TYR B 338     8211   4405   4263   -204  -1030   -755       C  
ATOM   2794  CE1 TYR B 338       0.604 -19.261  31.970  1.00 47.64           C  
ANISOU 2794  CE1 TYR B 338     9161   5010   3928    162  -1610  -1240       C  
ATOM   2795  CE2 TYR B 338      -0.304 -21.309  31.058  1.00 46.98           C  
ANISOU 2795  CE2 TYR B 338     8803   4035   5010   -191  -1476   -655       C  
ATOM   2796  CZ  TYR B 338       0.500 -20.653  31.975  1.00 49.92           C  
ANISOU 2796  CZ  TYR B 338     9442   5036   4488    -63  -1632   -939       C  
ATOM   2797  OH  TYR B 338       1.203 -21.392  32.893  1.00 58.20           O  
ANISOU 2797  OH  TYR B 338    10433   6487   5193    414  -1606    -10       O  
ATOM   2798  N   CYS B 339      -1.554 -20.031  26.333  1.00 35.88           N  
ANISOU 2798  N   CYS B 339     7051   2724   3858   -756   -654   -376       N  
ATOM   2799  CA  CYS B 339      -1.303 -21.245  25.551  1.00 37.38           C  
ANISOU 2799  CA  CYS B 339     6597   3292   4312   -426   -438   -726       C  
ATOM   2800  C   CYS B 339      -0.363 -21.028  24.378  1.00 34.90           C  
ANISOU 2800  C   CYS B 339     6085   3012   4161   -767   -759   -563       C  
ATOM   2801  O   CYS B 339       0.515 -21.849  24.134  1.00 36.25           O  
ANISOU 2801  O   CYS B 339     6269   3315   4189   -639   -774   -795       O  
ATOM   2802  CB  CYS B 339      -2.610 -21.867  25.070  1.00 39.74           C  
ANISOU 2802  CB  CYS B 339     6418   3715   4963   -337   -676   -488       C  
ATOM   2803  SG  CYS B 339      -3.540 -22.569  26.439  1.00 45.58           S  
ANISOU 2803  SG  CYS B 339     7675   3543   6098   -657   -370    317       S  
ATOM   2804  N   TRP B 340      -0.550 -19.921  23.665  1.00 33.84           N  
ANISOU 2804  N   TRP B 340     5863   3076   3917   -918   -849   -646       N  
ATOM   2805  CA  TRP B 340       0.347 -19.514  22.579  1.00 32.73           C  
ANISOU 2805  CA  TRP B 340     5709   2720   4004  -1055   -847   -574       C  
ATOM   2806  C   TRP B 340       1.796 -19.378  23.048  1.00 34.44           C  
ANISOU 2806  C   TRP B 340     5728   3139   4218  -1103   -871   -563       C  
ATOM   2807  O   TRP B 340       2.722 -19.734  22.321  1.00 36.74           O  
ANISOU 2807  O   TRP B 340     6164   3255   4539   -359   -909   -645       O  
ATOM   2808  CB  TRP B 340      -0.128 -18.197  21.982  1.00 30.55           C  
ANISOU 2808  CB  TRP B 340     5329   2589   3689  -1183   -558   -576       C  
ATOM   2809  CG  TRP B 340       0.754 -17.673  20.883  1.00 29.27           C  
ANISOU 2809  CG  TRP B 340     5027   2418   3675  -1356   -775   -662       C  
ATOM   2810  CD1 TRP B 340       1.747 -16.736  21.001  1.00 30.91           C  
ANISOU 2810  CD1 TRP B 340     5176   2466   4099  -1421  -1054   -898       C  
ATOM   2811  CD2 TRP B 340       0.718 -18.054  19.503  1.00 23.87           C  
ANISOU 2811  CD2 TRP B 340     3897   1517   3654  -1498   -758   -779       C  
ATOM   2812  NE1 TRP B 340       2.327 -16.506  19.776  1.00 33.16           N  
ANISOU 2812  NE1 TRP B 340     5437   2589   4572  -1716   -821   -602       N  
ATOM   2813  CE2 TRP B 340       1.713 -17.298  18.837  1.00 30.19           C  
ANISOU 2813  CE2 TRP B 340     4540   2488   4440  -1772   -329   -572       C  
ATOM   2814  CE3 TRP B 340      -0.073 -18.951  18.758  1.00 23.79           C  
ANISOU 2814  CE3 TRP B 340     3558   1749   3732  -1459   -623   -769       C  
ATOM   2815  CZ2 TRP B 340       1.956 -17.418  17.454  1.00 31.51           C  
ANISOU 2815  CZ2 TRP B 340     4948   2629   4394  -1526   -481   -769       C  
ATOM   2816  CZ3 TRP B 340       0.165 -19.074  17.375  1.00 27.56           C  
ANISOU 2816  CZ3 TRP B 340     4208   2402   3861  -1363   -153   -868       C  
ATOM   2817  CH2 TRP B 340       1.170 -18.303  16.741  1.00 28.75           C  
ANISOU 2817  CH2 TRP B 340     4337   2390   4196  -1444    -51   -742       C  
ATOM   2818  N   GLU B 341       1.976 -18.864  24.263  1.00 37.54           N  
ANISOU 2818  N   GLU B 341     6416   3344   4500  -1258  -1047   -872       N  
ATOM   2819  CA  GLU B 341       3.301 -18.596  24.813  1.00 41.65           C  
ANISOU 2819  CA  GLU B 341     6554   4300   4970  -1191  -1349   -869       C  
ATOM   2820  C   GLU B 341       3.975 -19.814  25.443  1.00 42.92           C  
ANISOU 2820  C   GLU B 341     6603   4502   5199   -921  -1195   -886       C  
ATOM   2821  O   GLU B 341       5.203 -19.849  25.540  1.00 45.14           O  
ANISOU 2821  O   GLU B 341     6619   5262   5270     10  -1600  -1293       O  
ATOM   2822  CB  GLU B 341       3.234 -17.442  25.818  1.00 44.64           C  
ANISOU 2822  CB  GLU B 341     6731   4294   5933  -1586  -1293  -1300       C  
ATOM   2823  CG  GLU B 341       3.128 -16.074  25.151  1.00 53.52           C  
ANISOU 2823  CG  GLU B 341     8687   4814   6832  -1417  -1151   -635       C  
ATOM   2824  CD  GLU B 341       2.619 -14.969  26.068  1.00 61.19           C  
ANISOU 2824  CD  GLU B 341     9939   5709   7602  -1278   -936  -1368       C  
ATOM   2825  OE1 GLU B 341       2.495 -15.184  27.300  1.00 63.23           O  
ANISOU 2825  OE1 GLU B 341     9775   6689   7561  -2010  -1299  -1260       O  
ATOM   2826  OE2 GLU B 341       2.344 -13.868  25.542  1.00 68.31           O  
ANISOU 2826  OE2 GLU B 341    10710   5723   9519  -1053   -847   -796       O  
ATOM   2827  N   ASN B 342       3.184 -20.805  25.861  1.00 42.10           N  
ANISOU 2827  N   ASN B 342     7159   3997   4837   -912  -1237  -1015       N  
ATOM   2828  CA  ASN B 342       3.720 -21.939  26.633  1.00 43.18           C  
ANISOU 2828  CA  ASN B 342     6976   4743   4688   -683  -1390   -821       C  
ATOM   2829  C   ASN B 342       3.574 -23.325  26.027  1.00 40.24           C  
ANISOU 2829  C   ASN B 342     6566   4297   4425   -298  -1166   -436       C  
ATOM   2830  O   ASN B 342       4.295 -24.231  26.417  1.00 46.84           O  
ANISOU 2830  O   ASN B 342     6703   5804   5289    576  -1353   -393       O  
ATOM   2831  CB  ASN B 342       3.163 -21.940  28.060  1.00 42.42           C  
ANISOU 2831  CB  ASN B 342     7316   4462   4336   -711  -1801   -762       C  
ATOM   2832  CG  ASN B 342       3.668 -20.772  28.880  1.00 46.77           C  
ANISOU 2832  CG  ASN B 342     7843   5083   4842   -731  -2027  -1312       C  
ATOM   2833  OD1 ASN B 342       2.910 -19.858  29.193  1.00 48.97           O  
ANISOU 2833  OD1 ASN B 342     8874   4714   5017   -679  -2157  -1644       O  
ATOM   2834  ND2 ASN B 342       4.954 -20.789  29.222  1.00 50.28           N  
ANISOU 2834  ND2 ASN B 342     7874   6484   4746   -583  -1934  -1707       N  
ATOM   2835  N   PHE B 343       2.652 -23.493  25.085  1.00 36.13           N  
ANISOU 2835  N   PHE B 343     6044   3362   4322   -123   -881   -404       N  
ATOM   2836  CA  PHE B 343       2.378 -24.819  24.502  1.00 36.49           C  
ANISOU 2836  CA  PHE B 343     6359   3251   4254   -137   -584   -288       C  
ATOM   2837  C   PHE B 343       2.560 -24.891  22.986  1.00 37.17           C  
ANISOU 2837  C   PHE B 343     6381   3444   4298   -219   -534   -325       C  
ATOM   2838  O   PHE B 343       2.319 -25.940  22.371  1.00 38.03           O  
ANISOU 2838  O   PHE B 343     6729   3344   4377   -360   -588   -195       O  
ATOM   2839  CB  PHE B 343       0.978 -25.299  24.909  1.00 32.97           C  
ANISOU 2839  CB  PHE B 343     6123   2866   3538    125   -806   -127       C  
ATOM   2840  CG  PHE B 343       0.749 -25.298  26.397  1.00 32.94           C  
ANISOU 2840  CG  PHE B 343     6198   2775   3542    362   -665   -183       C  
ATOM   2841  CD1 PHE B 343       1.458 -26.178  27.232  1.00 33.53           C  
ANISOU 2841  CD1 PHE B 343     6316   3084   3340    354   -910   -268       C  
ATOM   2842  CD2 PHE B 343      -0.164 -24.416  26.972  1.00 29.60           C  
ANISOU 2842  CD2 PHE B 343     5895   2486   2863    313  -1024    -13       C  
ATOM   2843  CE1 PHE B 343       1.249 -26.176  28.607  1.00 31.18           C  
ANISOU 2843  CE1 PHE B 343     5693   2859   3293    798   -954     25       C  
ATOM   2844  CE2 PHE B 343      -0.378 -24.414  28.350  1.00 30.47           C  
ANISOU 2844  CE2 PHE B 343     6079   2575   2922    438   -913    136       C  
ATOM   2845  CZ  PHE B 343       0.333 -25.293  29.168  1.00 29.71           C  
ANISOU 2845  CZ  PHE B 343     5941   2632   2714    676   -724     30       C  
ATOM   2846  N   VAL B 344       3.010 -23.776  22.407  1.00 35.24           N  
ANISOU 2846  N   VAL B 344     6046   3151   4193      6   -399   -488       N  
ATOM   2847  CA  VAL B 344       3.097 -23.584  20.963  1.00 34.18           C  
ANISOU 2847  CA  VAL B 344     5791   2934   4262   -239   -368    -92       C  
ATOM   2848  C   VAL B 344       4.513 -23.141  20.612  1.00 35.94           C  
ANISOU 2848  C   VAL B 344     5972   3327   4354   -475   -219   -328       C  
ATOM   2849  O   VAL B 344       5.080 -22.281  21.295  1.00 36.11           O  
ANISOU 2849  O   VAL B 344     6010   3188   4520   -271   -603   -240       O  
ATOM   2850  CB  VAL B 344       2.089 -22.490  20.502  1.00 33.06           C  
ANISOU 2850  CB  VAL B 344     5939   2606   4014   -181    -83   -249       C  
ATOM   2851  CG1 VAL B 344       2.218 -22.167  19.015  1.00 31.38           C  
ANISOU 2851  CG1 VAL B 344     6053   2035   3832   -357    -61   -552       C  
ATOM   2852  CG2 VAL B 344       0.656 -22.895  20.831  1.00 30.87           C  
ANISOU 2852  CG2 VAL B 344     5792   1773   4162     21    -54   -273       C  
ATOM   2853  N   TYR B 345       5.081 -23.729  19.555  1.00 34.62           N  
ANISOU 2853  N   TYR B 345     5763   2808   4579   -407   -256   -360       N  
ATOM   2854  CA  TYR B 345       6.300 -23.190  18.942  1.00 35.44           C  
ANISOU 2854  CA  TYR B 345     5709   3086   4669   -376   -238   -239       C  
ATOM   2855  C   TYR B 345       5.993 -21.865  18.248  1.00 37.50           C  
ANISOU 2855  C   TYR B 345     6193   3144   4911   -536   -155    -40       C  
ATOM   2856  O   TYR B 345       5.903 -21.788  17.022  1.00 38.70           O  
ANISOU 2856  O   TYR B 345     6755   3065   4882   -524   -232   -629       O  
ATOM   2857  CB  TYR B 345       6.919 -24.180  17.957  1.00 36.11           C  
ANISOU 2857  CB  TYR B 345     5837   3181   4701   -571    -87   -380       C  
ATOM   2858  CG  TYR B 345       7.514 -25.410  18.600  1.00 40.96           C  
ANISOU 2858  CG  TYR B 345     6176   4033   5352     46    -60    -35       C  
ATOM   2859  CD1 TYR B 345       8.678 -25.324  19.381  1.00 42.57           C  
ANISOU 2859  CD1 TYR B 345     6442   4645   5087     56   -167   -359       C  
ATOM   2860  CD2 TYR B 345       6.929 -26.675  18.411  1.00 40.68           C  
ANISOU 2860  CD2 TYR B 345     6093   3965   5395     -4    567     17       C  
ATOM   2861  CE1 TYR B 345       9.231 -26.456  19.965  1.00 44.34           C  
ANISOU 2861  CE1 TYR B 345     6822   4452   5571      6   -211   -247       C  
ATOM   2862  CE2 TYR B 345       7.481 -27.811  18.990  1.00 41.71           C  
ANISOU 2862  CE2 TYR B 345     6520   3896   5431    -97    520    119       C  
ATOM   2863  CZ  TYR B 345       8.627 -27.692  19.764  1.00 44.24           C  
ANISOU 2863  CZ  TYR B 345     6821   4406   5581   -165    202     73       C  
ATOM   2864  OH  TYR B 345       9.179 -28.805  20.337  1.00 51.61           O  
ANISOU 2864  OH  TYR B 345     8227   5270   6110    637    218    477       O  
ATOM   2865  N   ASN B 346       5.833 -20.819  19.049  1.00 38.99           N  
ANISOU 2865  N   ASN B 346     6416   3225   5171   -664   -319   -196       N  
ATOM   2866  CA  ASN B 346       5.430 -19.509  18.541  1.00 39.28           C  
ANISOU 2866  CA  ASN B 346     6345   3188   5389   -913   -353     43       C  
ATOM   2867  C   ASN B 346       6.514 -18.772  17.752  1.00 42.82           C  
ANISOU 2867  C   ASN B 346     6286   3886   6096   -956     24     66       C  
ATOM   2868  O   ASN B 346       6.212 -17.790  17.074  1.00 47.76           O  
ANISOU 2868  O   ASN B 346     6757   4156   7234  -1219    171    712       O  
ATOM   2869  CB  ASN B 346       4.895 -18.636  19.677  1.00 40.76           C  
ANISOU 2869  CB  ASN B 346     6308   3697   5481   -890   -175    -88       C  
ATOM   2870  CG  ASN B 346       5.868 -18.513  20.835  1.00 43.66           C  
ANISOU 2870  CG  ASN B 346     6775   3888   5926   -982   -636   -236       C  
ATOM   2871  OD1 ASN B 346       6.994 -18.038  20.675  1.00 47.46           O  
ANISOU 2871  OD1 ASN B 346     6834   4695   6503  -1123   -518   -359       O  
ATOM   2872  ND2 ASN B 346       5.431 -18.935  22.014  1.00 41.63           N  
ANISOU 2872  ND2 ASN B 346     6647   3653   5514  -1210   -847   -603       N  
ATOM   2873  N   ASP B 347       7.761 -19.246  17.843  1.00 43.01           N  
ANISOU 2873  N   ASP B 347     6273   3924   6142   -993   -174    281       N  
ATOM   2874  CA  ASP B 347       8.919 -18.650  17.143  1.00 51.06           C  
ANISOU 2874  CA  ASP B 347     7104   4479   7818  -1296    693    392       C  
ATOM   2875  C   ASP B 347       9.084 -17.142  17.443  1.00 51.09           C  
ANISOU 2875  C   ASP B 347     7084   4403   7923  -1308    106    652       C  
ATOM   2876  O   ASP B 347       9.386 -16.340  16.552  1.00 50.23           O  
ANISOU 2876  O   ASP B 347     7013   4691   7381  -1434    294    446       O  
ATOM   2877  CB  ASP B 347       8.847 -18.938  15.625  1.00 53.96           C  
ANISOU 2877  CB  ASP B 347     8156   4463   7881  -1464    580    515       C  
ATOM   2878  CG  ASP B 347      10.203 -18.829  14.932  1.00 65.96           C  
ANISOU 2878  CG  ASP B 347     8817   6597   9647  -1387   1560    857       C  
ATOM   2879  OD1 ASP B 347      11.160 -19.526  15.351  1.00 72.42           O  
ANISOU 2879  OD1 ASP B 347     8901   7658  10956  -1229   1286   1237       O  
ATOM   2880  OD2 ASP B 347      10.303 -18.052  13.953  1.00 66.72           O  
ANISOU 2880  OD2 ASP B 347    10272   5446   9630   -819   1428    518       O  
ATOM   2881  N   ASP B 348       8.864 -16.782  18.713  1.00 54.04           N  
ANISOU 2881  N   ASP B 348     7470   5005   8055  -1335   -480     96       N  
ATOM   2882  CA  ASP B 348       8.893 -15.392  19.222  1.00 58.20           C  
ANISOU 2882  CA  ASP B 348     8093   4763   9255  -1162   -438    149       C  
ATOM   2883  C   ASP B 348       7.849 -14.436  18.609  1.00 57.39           C  
ANISOU 2883  C   ASP B 348     7781   4949   9074  -1230   -299    159       C  
ATOM   2884  O   ASP B 348       7.893 -13.224  18.850  1.00 60.98           O  
ANISOU 2884  O   ASP B 348     8466   4592  10109   -678   -131   1027       O  
ATOM   2885  CB  ASP B 348      10.316 -14.788  19.159  1.00 65.30           C  
ANISOU 2885  CB  ASP B 348     8296   6204  10307  -1638    203    217       C  
ATOM   2886  CG  ASP B 348      11.354 -15.612  19.924  1.00 73.04           C  
ANISOU 2886  CG  ASP B 348     9358   7081  11314  -1536   -793    452       C  
ATOM   2887  OD1 ASP B 348      11.013 -16.255  20.941  1.00 72.85           O  
ANISOU 2887  OD1 ASP B 348     8783   7432  11464  -2785  -1156    420       O  
ATOM   2888  OD2 ASP B 348      12.531 -15.603  19.507  1.00 82.34           O  
ANISOU 2888  OD2 ASP B 348     9745   9065  12475   -589   -339     48       O  
ATOM   2889  N   GLU B 349       6.912 -14.982  17.834  1.00 52.90           N  
ANISOU 2889  N   GLU B 349     7940   3992   8164   -785   -142    176       N  
ATOM   2890  CA  GLU B 349       5.802 -14.204  17.287  1.00 52.78           C  
ANISOU 2890  CA  GLU B 349     8095   4123   7834   -787     80    611       C  
ATOM   2891  C   GLU B 349       4.779 -13.926  18.392  1.00 47.40           C  
ANISOU 2891  C   GLU B 349     7725   2888   7394  -1152   -351    378       C  
ATOM   2892  O   GLU B 349       4.526 -14.799  19.219  1.00 48.79           O  
ANISOU 2892  O   GLU B 349     8218   3332   6986  -1309   -779    470       O  
ATOM   2893  CB  GLU B 349       5.147 -14.919  16.089  1.00 49.57           C  
ANISOU 2893  CB  GLU B 349     7841   2901   8092  -1768    139   1383       C  
ATOM   2894  CG  GLU B 349       6.019 -15.025  14.832  1.00 59.74           C  
ANISOU 2894  CG  GLU B 349     9057   5138   8501   -929    680    883       C  
ATOM   2895  CD  GLU B 349       6.477 -13.674  14.270  1.00 68.67           C  
ANISOU 2895  CD  GLU B 349     9846   5958  10285  -1085    941   1999       C  
ATOM   2896  OE1 GLU B 349       5.653 -12.733  14.175  1.00 70.23           O  
ANISOU 2896  OE1 GLU B 349    11043   4685  10955  -1256    405   2348       O  
ATOM   2897  OE2 GLU B 349       7.670 -13.552  13.911  1.00 77.11           O  
ANISOU 2897  OE2 GLU B 349    10306   7298  11694   -812   2017   1682       O  
ATOM   2898  N   PRO B 350       4.212 -12.701  18.434  1.00 48.33           N  
ANISOU 2898  N   PRO B 350     7912   3105   7345   -836   -203    473       N  
ATOM   2899  CA  PRO B 350       3.195 -12.414  19.463  1.00 46.82           C  
ANISOU 2899  CA  PRO B 350     7689   2511   7587   -800   -100    676       C  
ATOM   2900  C   PRO B 350       1.871 -13.110  19.155  1.00 48.57           C  
ANISOU 2900  C   PRO B 350     7938   3334   7182  -1024   -133    147       C  
ATOM   2901  O   PRO B 350       1.615 -13.452  17.993  1.00 52.21           O  
ANISOU 2901  O   PRO B 350     8734   4020   7080   -325    445   -415       O  
ATOM   2902  CB  PRO B 350       3.033 -10.888  19.392  1.00 44.63           C  
ANISOU 2902  CB  PRO B 350     7713   2382   6861   -983   -269    167       C  
ATOM   2903  CG  PRO B 350       3.468 -10.520  18.012  1.00 46.98           C  
ANISOU 2903  CG  PRO B 350     7770   2566   7512   -743   -220   1140       C  
ATOM   2904  CD  PRO B 350       4.521 -11.513  17.609  1.00 48.68           C  
ANISOU 2904  CD  PRO B 350     7714   3116   7665   -864    116    588       C  
ATOM   2905  N   PHE B 351       1.048 -13.330  20.181  1.00 46.53           N  
ANISOU 2905  N   PHE B 351     7909   3212   6556   -837   -443    145       N  
ATOM   2906  CA  PHE B 351      -0.282 -13.892  19.968  1.00 43.78           C  
ANISOU 2906  CA  PHE B 351     7548   3426   5658   -626   -386    460       C  
ATOM   2907  C   PHE B 351      -1.140 -12.937  19.139  1.00 42.50           C  
ANISOU 2907  C   PHE B 351     7549   2826   5771   -457   -175    197       C  
ATOM   2908  O   PHE B 351      -1.203 -11.747  19.427  1.00 46.06           O  
ANISOU 2908  O   PHE B 351     8201   3032   6264   -797     12   -270       O  
ATOM   2909  CB  PHE B 351      -0.980 -14.249  21.286  1.00 41.17           C  
ANISOU 2909  CB  PHE B 351     7309   3371   4960   -345   -820     89       C  
ATOM   2910  CG  PHE B 351      -2.409 -14.705  21.110  1.00 38.64           C  
ANISOU 2910  CG  PHE B 351     7158   3058   4465    -51   -644    -32       C  
ATOM   2911  CD1 PHE B 351      -2.714 -15.827  20.332  1.00 38.28           C  
ANISOU 2911  CD1 PHE B 351     7071   2698   4775   -249   -527    135       C  
ATOM   2912  CD2 PHE B 351      -3.457 -14.002  21.704  1.00 38.43           C  
ANISOU 2912  CD2 PHE B 351     6944   3789   3868     16   -641    205       C  
ATOM   2913  CE1 PHE B 351      -4.032 -16.235  20.155  1.00 38.11           C  
ANISOU 2913  CE1 PHE B 351     6971   2833   4674    -61   -349    -41       C  
ATOM   2914  CE2 PHE B 351      -4.776 -14.413  21.538  1.00 36.00           C  
ANISOU 2914  CE2 PHE B 351     7096   3020   3562   -261   -484    124       C  
ATOM   2915  CZ  PHE B 351      -5.064 -15.528  20.760  1.00 35.75           C  
ANISOU 2915  CZ  PHE B 351     7195   2248   4137     18   -368    334       C  
ATOM   2916  N   LYS B 352      -1.773 -13.482  18.104  1.00 40.74           N  
ANISOU 2916  N   LYS B 352     7443   2792   5244     23    -38    223       N  
ATOM   2917  CA  LYS B 352      -2.631 -12.736  17.198  1.00 43.60           C  
ANISOU 2917  CA  LYS B 352     7986   2949   5627     39     17    962       C  
ATOM   2918  C   LYS B 352      -4.077 -13.231  17.352  1.00 44.87           C  
ANISOU 2918  C   LYS B 352     7948   3360   5740    217     30    767       C  
ATOM   2919  O   LYS B 352      -4.425 -14.291  16.822  1.00 49.52           O  
ANISOU 2919  O   LYS B 352     7934   4456   6425    -78   -662    -55       O  
ATOM   2920  CB  LYS B 352      -2.143 -12.904  15.755  1.00 48.24           C  
ANISOU 2920  CB  LYS B 352     9002   3519   5804    205    480    860       C  
ATOM   2921  CG  LYS B 352      -2.577 -11.793  14.810  1.00 59.19           C  
ANISOU 2921  CG  LYS B 352    10056   5386   7047    690    140   2125       C  
ATOM   2922  CD  LYS B 352      -2.359 -12.162  13.343  1.00 72.62           C  
ANISOU 2922  CD  LYS B 352    11519   7905   8168     85   1721    765       C  
ATOM   2923  CE  LYS B 352      -0.934 -11.891  12.873  1.00 81.01           C  
ANISOU 2923  CE  LYS B 352    11634   9278   9866   -612   1778   1262       C  
ATOM   2924  NZ  LYS B 352      -0.739 -12.254  11.440  1.00 84.42           N  
ANISOU 2924  NZ  LYS B 352    11884  10465   9724  -1228   1556   1053       N  
ATOM   2925  N   PRO B 353      -4.923 -12.469  18.087  1.00 43.93           N  
ANISOU 2925  N   PRO B 353     8050   3310   5329    134     12    703       N  
ATOM   2926  CA  PRO B 353      -6.309 -12.904  18.322  1.00 42.19           C  
ANISOU 2926  CA  PRO B 353     7926   3172   4931     30   -350    729       C  
ATOM   2927  C   PRO B 353      -7.150 -12.868  17.045  1.00 39.61           C  
ANISOU 2927  C   PRO B 353     7778   2818   4452    108    -23    649       C  
ATOM   2928  O   PRO B 353      -7.038 -11.936  16.256  1.00 43.63           O  
ANISOU 2928  O   PRO B 353     8060   3695   4819     68    255   1281       O  
ATOM   2929  CB  PRO B 353      -6.827 -11.885  19.350  1.00 44.69           C  
ANISOU 2929  CB  PRO B 353     7837   3480   5662   -267    128    337       C  
ATOM   2930  CG  PRO B 353      -6.017 -10.652  19.101  1.00 42.50           C  
ANISOU 2930  CG  PRO B 353     8267   2562   5318     62   -292    113       C  
ATOM   2931  CD  PRO B 353      -4.656 -11.135  18.670  1.00 43.11           C  
ANISOU 2931  CD  PRO B 353     7837   3479   5061    -80   -440    569       C  
ATOM   2932  N   TRP B 354      -7.964 -13.892  16.833  1.00 39.02           N  
ANISOU 2932  N   TRP B 354     6860   3726   4237    143   -237    254       N  
ATOM   2933  CA  TRP B 354      -8.865 -13.919  15.675  1.00 39.32           C  
ANISOU 2933  CA  TRP B 354     7598   3423   3917    325   -337    867       C  
ATOM   2934  C   TRP B 354     -10.071 -13.023  15.928  1.00 43.07           C  
ANISOU 2934  C   TRP B 354     7782   4268   4312    767   -401   1019       C  
ATOM   2935  O   TRP B 354     -10.398 -12.720  17.084  1.00 45.18           O  
ANISOU 2935  O   TRP B 354     8176   4322   4665    503   -550    212       O  
ATOM   2936  CB  TRP B 354      -9.321 -15.348  15.345  1.00 35.24           C  
ANISOU 2936  CB  TRP B 354     7083   3464   2842    392    -21    473       C  
ATOM   2937  CG  TRP B 354      -9.712 -16.152  16.557  1.00 34.59           C  
ANISOU 2937  CG  TRP B 354     6795   3314   3034    205   -231    596       C  
ATOM   2938  CD1 TRP B 354     -10.960 -16.272  17.098  1.00 33.65           C  
ANISOU 2938  CD1 TRP B 354     6719   3172   2893    187   -276    494       C  
ATOM   2939  CD2 TRP B 354      -8.839 -16.933  17.382  1.00 36.03           C  
ANISOU 2939  CD2 TRP B 354     6766   3508   3413    259   -414    524       C  
ATOM   2940  NE1 TRP B 354     -10.920 -17.083  18.210  1.00 32.48           N  
ANISOU 2940  NE1 TRP B 354     6620   2377   3344    166   -241    510       N  
ATOM   2941  CE2 TRP B 354      -9.632 -17.503  18.407  1.00 34.29           C  
ANISOU 2941  CE2 TRP B 354     6578   3082   3367     -3   -501    290       C  
ATOM   2942  CE3 TRP B 354      -7.461 -17.208  17.355  1.00 37.89           C  
ANISOU 2942  CE3 TRP B 354     6614   4024   3757     76   -736    180       C  
ATOM   2943  CZ2 TRP B 354      -9.096 -18.340  19.394  1.00 34.22           C  
ANISOU 2943  CZ2 TRP B 354     6574   3231   3195   -177   -859     79       C  
ATOM   2944  CZ3 TRP B 354      -6.928 -18.043  18.334  1.00 37.78           C  
ANISOU 2944  CZ3 TRP B 354     6879   4224   3248   -389   -745    251       C  
ATOM   2945  CH2 TRP B 354      -7.747 -18.598  19.344  1.00 37.96           C  
ANISOU 2945  CH2 TRP B 354     6558   3813   4051   -592   -259   -246       C  
ATOM   2946  N   LYS B 355     -10.706 -12.598  14.836  1.00 43.15           N  
ANISOU 2946  N   LYS B 355     7698   4524   4171    659   -144   1375       N  
ATOM   2947  CA  LYS B 355     -11.957 -11.853  14.855  1.00 41.90           C  
ANISOU 2947  CA  LYS B 355     7874   4494   3552    842   -400   1355       C  
ATOM   2948  C   LYS B 355     -13.026 -12.646  15.605  1.00 43.13           C  
ANISOU 2948  C   LYS B 355     7798   4491   4099    688   -478   1119       C  
ATOM   2949  O   LYS B 355     -13.197 -13.848  15.374  1.00 49.73           O  
ANISOU 2949  O   LYS B 355     8876   4725   5293     39   -858    706       O  
ATOM   2950  CB  LYS B 355     -12.407 -11.569  13.417  1.00 40.42           C  
ANISOU 2950  CB  LYS B 355     8091   3585   3682    917   -431   1667       C  
ATOM   2951  CG  LYS B 355     -13.655 -10.713  13.292  1.00 47.76           C  
ANISOU 2951  CG  LYS B 355     8145   5417   4584   1447   -681   1714       C  
ATOM   2952  CD  LYS B 355     -13.729 -10.053  11.922  1.00 51.51           C  
ANISOU 2952  CD  LYS B 355     9229   5679   4661   1541   -816   1843       C  
ATOM   2953  CE  LYS B 355     -15.126  -9.529  11.648  1.00 55.65           C  
ANISOU 2953  CE  LYS B 355     9452   6529   5161   1815  -1203   1750       C  
ATOM   2954  NZ  LYS B 355     -15.277  -9.096  10.231  1.00 65.39           N  
ANISOU 2954  NZ  LYS B 355    11737   7684   5423    841  -1463   2341       N  
ATOM   2955  N   GLY B 356     -13.714 -11.967  16.519  1.00 42.41           N  
ANISOU 2955  N   GLY B 356     7647   4914   3550    891   -679   1179       N  
ATOM   2956  CA  GLY B 356     -14.820 -12.555  17.258  1.00 39.68           C  
ANISOU 2956  CA  GLY B 356     7630   3758   3689    887   -730   1006       C  
ATOM   2957  C   GLY B 356     -14.458 -13.310  18.524  1.00 36.71           C  
ANISOU 2957  C   GLY B 356     7360   2664   3924   1010   -629    861       C  
ATOM   2958  O   GLY B 356     -15.353 -13.828  19.184  1.00 42.95           O  
ANISOU 2958  O   GLY B 356     8276   3560   4481    811   -223   1404       O  
ATOM   2959  N   LEU B 357     -13.171 -13.354  18.876  1.00 33.75           N  
ANISOU 2959  N   LEU B 357     7094   2076   3651    800   -265    354       N  
ATOM   2960  CA  LEU B 357     -12.685 -14.144  20.024  1.00 36.69           C  
ANISOU 2960  CA  LEU B 357     7345   3083   3510    677   -534    472       C  
ATOM   2961  C   LEU B 357     -13.452 -13.830  21.326  1.00 39.50           C  
ANISOU 2961  C   LEU B 357     7817   2934   4254    679    -54      5       C  
ATOM   2962  O   LEU B 357     -13.955 -14.747  21.994  1.00 41.07           O  
ANISOU 2962  O   LEU B 357     8020   3310   4273    838    166    436       O  
ATOM   2963  CB  LEU B 357     -11.163 -13.966  20.210  1.00 35.18           C  
ANISOU 2963  CB  LEU B 357     7152   2786   3429    757   -189    285       C  
ATOM   2964  CG  LEU B 357     -10.362 -14.782  21.248  1.00 35.72           C  
ANISOU 2964  CG  LEU B 357     7275   2605   3689    768   -556      6       C  
ATOM   2965  CD1 LEU B 357      -8.900 -14.934  20.837  1.00 33.23           C  
ANISOU 2965  CD1 LEU B 357     7158   1803   3664    250   -522   -397       C  
ATOM   2966  CD2 LEU B 357     -10.447 -14.206  22.660  1.00 36.54           C  
ANISOU 2966  CD2 LEU B 357     7264   2974   3646   1102   -822    -69       C  
ATOM   2967  N   LYS B 358     -13.539 -12.541  21.662  1.00 40.30           N  
ANISOU 2967  N   LYS B 358     8161   2676   4472    957   -154    424       N  
ATOM   2968  CA  LYS B 358     -14.202 -12.087  22.888  1.00 44.28           C  
ANISOU 2968  CA  LYS B 358     8732   3411   4682    951    -50    -45       C  
ATOM   2969  C   LYS B 358     -15.717 -12.242  22.818  1.00 42.54           C  
ANISOU 2969  C   LYS B 358     8737   2894   4532    956   -339   -412       C  
ATOM   2970  O   LYS B 358     -16.342 -12.610  23.813  1.00 47.70           O  
ANISOU 2970  O   LYS B 358     9124   4284   4715    375   -217   -412       O  
ATOM   2971  CB  LYS B 358     -13.814 -10.643  23.242  1.00 51.38           C  
ANISOU 2971  CB  LYS B 358    10186   3709   5625    579   -177   -498       C  
ATOM   2972  CG  LYS B 358     -12.384 -10.503  23.742  1.00 58.74           C  
ANISOU 2972  CG  LYS B 358    10700   4728   6888    416   -715   -442       C  
ATOM   2973  CD  LYS B 358     -12.263  -9.412  24.795  1.00 67.33           C  
ANISOU 2973  CD  LYS B 358    12555   5122   7903    440   -637  -1049       C  
ATOM   2974  CE  LYS B 358     -10.853  -9.333  25.362  1.00 71.45           C  
ANISOU 2974  CE  LYS B 358    12587   5809   8751    392  -1025  -1109       C  
ATOM   2975  NZ  LYS B 358      -9.914  -8.591  24.473  1.00 74.51           N  
ANISOU 2975  NZ  LYS B 358    12998   6505   8808    513  -1040   -274       N  
ATOM   2976  N   TYR B 359     -16.292 -11.975  21.644  1.00 41.21           N  
ANISOU 2976  N   TYR B 359     8449   2643   4565   1359     58    102       N  
ATOM   2977  CA  TYR B 359     -17.716 -12.214  21.382  1.00 45.42           C  
ANISOU 2977  CA  TYR B 359     8312   3751   5195   1573    160    146       C  
ATOM   2978  C   TYR B 359     -18.074 -13.691  21.599  1.00 42.74           C  
ANISOU 2978  C   TYR B 359     7580   3733   4927   1820     68    270       C  
ATOM   2979  O   TYR B 359     -19.043 -13.998  22.305  1.00 47.52           O  
ANISOU 2979  O   TYR B 359     7964   4679   5409   1396     -1   1294       O  
ATOM   2980  CB  TYR B 359     -18.098 -11.760  19.964  1.00 54.20           C  
ANISOU 2980  CB  TYR B 359     9677   5090   5823   2316   -523    681       C  
ATOM   2981  CG  TYR B 359     -19.589 -11.785  19.687  1.00 68.10           C  
ANISOU 2981  CG  TYR B 359     9935   8011   7929   2202   -829    677       C  
ATOM   2982  CD1 TYR B 359     -20.217 -12.950  19.209  1.00 71.30           C  
ANISOU 2982  CD1 TYR B 359    11371   6692   9027   2615   -735   1043       C  
ATOM   2983  CD2 TYR B 359     -20.380 -10.644  19.899  1.00 77.13           C  
ANISOU 2983  CD2 TYR B 359    12463   7949   8892   2813   -947     81       C  
ATOM   2984  CE1 TYR B 359     -21.586 -12.979  18.960  1.00 81.55           C  
ANISOU 2984  CE1 TYR B 359    11497   9103  10384   1519   -860   1320       C  
ATOM   2985  CE2 TYR B 359     -21.751 -10.663  19.649  1.00 88.53           C  
ANISOU 2985  CE2 TYR B 359    12364  10538  10735   2789   -841    910       C  
ATOM   2986  CZ  TYR B 359     -22.346 -11.832  19.180  1.00 87.71           C  
ANISOU 2986  CZ  TYR B 359    11620  10565  11139   2500   -469   1237       C  
ATOM   2987  OH  TYR B 359     -23.696 -11.858  18.929  1.00 96.04           O  
ANISOU 2987  OH  TYR B 359    11748  13525  11217    292   -552   2572       O  
ATOM   2988  N   ASN B 360     -17.286 -14.587  20.999  1.00 38.27           N  
ANISOU 2988  N   ASN B 360     7140   3226   4174   1390    -83    327       N  
ATOM   2989  CA  ASN B 360     -17.447 -16.031  21.184  1.00 37.72           C  
ANISOU 2989  CA  ASN B 360     7005   3302   4022   1161     17    222       C  
ATOM   2990  C   ASN B 360     -17.318 -16.453  22.647  1.00 37.80           C  
ANISOU 2990  C   ASN B 360     7240   3173   3949   1371     66     59       C  
ATOM   2991  O   ASN B 360     -18.137 -17.230  23.131  1.00 42.77           O  
ANISOU 2991  O   ASN B 360     7373   4324   4554    812    135     -5       O  
ATOM   2992  CB  ASN B 360     -16.475 -16.819  20.291  1.00 32.89           C  
ANISOU 2992  CB  ASN B 360     6647   2464   3386    778   -216    370       C  
ATOM   2993  CG  ASN B 360     -16.722 -16.591  18.807  1.00 35.09           C  
ANISOU 2993  CG  ASN B 360     6727   3201   3402    782   -486     28       C  
ATOM   2994  OD1 ASN B 360     -17.860 -16.392  18.374  1.00 39.30           O  
ANISOU 2994  OD1 ASN B 360     6778   3275   4877    927   -643    313       O  
ATOM   2995  ND2 ASN B 360     -15.648 -16.610  18.016  1.00 36.27           N  
ANISOU 2995  ND2 ASN B 360     6671   3323   3786    672   -313    356       N  
ATOM   2996  N   PHE B 361     -16.312 -15.914  23.343  1.00 38.22           N  
ANISOU 2996  N   PHE B 361     7382   3158   3980   1362    178   -177       N  
ATOM   2997  CA  PHE B 361     -16.118 -16.144  24.778  1.00 41.28           C  
ANISOU 2997  CA  PHE B 361     8088   3676   3921   1191    396     48       C  
ATOM   2998  C   PHE B 361     -17.383 -15.818  25.572  1.00 45.57           C  
ANISOU 2998  C   PHE B 361     8402   4182   4729   1977    465    -50       C  
ATOM   2999  O   PHE B 361     -17.799 -16.604  26.439  1.00 45.73           O  
ANISOU 2999  O   PHE B 361     8342   4395   4636   1825   1409   -451       O  
ATOM   3000  CB  PHE B 361     -14.926 -15.341  25.330  1.00 43.16           C  
ANISOU 3000  CB  PHE B 361     8461   3864   4074    816    333    -35       C  
ATOM   3001  CG  PHE B 361     -14.907 -15.232  26.840  1.00 45.56           C  
ANISOU 3001  CG  PHE B 361     9215   3900   4194   1237    -62   -463       C  
ATOM   3002  CD1 PHE B 361     -14.487 -16.302  27.629  1.00 44.27           C  
ANISOU 3002  CD1 PHE B 361     9714   3456   3648   1127    101   -754       C  
ATOM   3003  CD2 PHE B 361     -15.320 -14.058  27.476  1.00 50.55           C  
ANISOU 3003  CD2 PHE B 361    10100   4256   4851   2045     46   -446       C  
ATOM   3004  CE1 PHE B 361     -14.481 -16.210  29.014  1.00 46.56           C  
ANISOU 3004  CE1 PHE B 361    10183   3863   3644   1266   -410   -524       C  
ATOM   3005  CE2 PHE B 361     -15.316 -13.955  28.866  1.00 54.32           C  
ANISOU 3005  CE2 PHE B 361    10899   4834   4904   2220   -242   -612       C  
ATOM   3006  CZ  PHE B 361     -14.893 -15.034  29.638  1.00 51.92           C  
ANISOU 3006  CZ  PHE B 361    10709   4279   4738   1815    341   -595       C  
ATOM   3007  N   LEU B 362     -17.973 -14.661  25.267  1.00 45.33           N  
ANISOU 3007  N   LEU B 362     8972   3633   4616   1734    421   -262       N  
ATOM   3008  CA  LEU B 362     -19.183 -14.197  25.940  1.00 51.07           C  
ANISOU 3008  CA  LEU B 362     8939   4830   5634   2028    552   -296       C  
ATOM   3009  C   LEU B 362     -20.373 -15.110  25.669  1.00 49.98           C  
ANISOU 3009  C   LEU B 362     8856   4843   5289   1966    827    -31       C  
ATOM   3010  O   LEU B 362     -21.088 -15.470  26.604  1.00 52.47           O  
ANISOU 3010  O   LEU B 362     8970   6145   4818   2755   1454   -728       O  
ATOM   3011  CB  LEU B 362     -19.503 -12.733  25.587  1.00 54.98           C  
ANISOU 3011  CB  LEU B 362    10247   4735   5905   2134    508   -370       C  
ATOM   3012  CG  LEU B 362     -18.562 -11.644  26.132  1.00 56.04           C  
ANISOU 3012  CG  LEU B 362    10843   4588   5860   2241    253   -556       C  
ATOM   3013  CD1 LEU B 362     -18.868 -10.298  25.485  1.00 57.03           C  
ANISOU 3013  CD1 LEU B 362    11127   4669   5870   2190    128   -448       C  
ATOM   3014  CD2 LEU B 362     -18.598 -11.532  27.657  1.00 53.28           C  
ANISOU 3014  CD2 LEU B 362    10021   4362   5859   1909   1518   -810       C  
ATOM   3015  N   PHE B 363     -20.558 -15.507  24.406  1.00 47.63           N  
ANISOU 3015  N   PHE B 363     8600   4415   5080   1948    700    450       N  
ATOM   3016  CA  PHE B 363     -21.630 -16.433  24.032  1.00 46.66           C  
ANISOU 3016  CA  PHE B 363     8055   4899   4772   1926    595    524       C  
ATOM   3017  C   PHE B 363     -21.503 -17.760  24.781  1.00 43.64           C  
ANISOU 3017  C   PHE B 363     7250   4479   4851   1762    941    245       C  
ATOM   3018  O   PHE B 363     -22.488 -18.260  25.322  1.00 44.71           O  
ANISOU 3018  O   PHE B 363     7997   3407   5583   1034    532    952       O  
ATOM   3019  CB  PHE B 363     -21.662 -16.673  22.519  1.00 45.91           C  
ANISOU 3019  CB  PHE B 363     7732   4942   4768   1808    476    604       C  
ATOM   3020  CG  PHE B 363     -22.726 -17.648  22.082  1.00 50.43           C  
ANISOU 3020  CG  PHE B 363     7277   6261   5620   1344    643    670       C  
ATOM   3021  CD1 PHE B 363     -24.019 -17.204  21.782  1.00 53.33           C  
ANISOU 3021  CD1 PHE B 363     7542   6991   5727   1584    322    987       C  
ATOM   3022  CD2 PHE B 363     -22.443 -19.019  21.974  1.00 49.90           C  
ANISOU 3022  CD2 PHE B 363     7238   6272   5447   1480    696    461       C  
ATOM   3023  CE1 PHE B 363     -25.005 -18.107  21.382  1.00 58.84           C  
ANISOU 3023  CE1 PHE B 363     7771   7717   6867   1179    241    787       C  
ATOM   3024  CE2 PHE B 363     -23.426 -19.922  21.579  1.00 51.78           C  
ANISOU 3024  CE2 PHE B 363     7330   7079   5262   1231    973    -24       C  
ATOM   3025  CZ  PHE B 363     -24.707 -19.465  21.279  1.00 55.48           C  
ANISOU 3025  CZ  PHE B 363     7530   7663   5885   1320    498    464       C  
ATOM   3026  N   LEU B 364     -20.286 -18.302  24.811  1.00 42.20           N  
ANISOU 3026  N   LEU B 364     7301   4643   4087   1780    792    395       N  
ATOM   3027  CA  LEU B 364     -20.019 -19.610  25.409  1.00 40.82           C  
ANISOU 3027  CA  LEU B 364     6979   4542   3987   1524    826    340       C  
ATOM   3028  C   LEU B 364     -20.124 -19.575  26.929  1.00 43.78           C  
ANISOU 3028  C   LEU B 364     7698   4925   4010   1646    723    274       C  
ATOM   3029  O   LEU B 364     -20.735 -20.469  27.518  1.00 44.41           O  
ANISOU 3029  O   LEU B 364     8028   4639   4205   2106   1194    341       O  
ATOM   3030  CB  LEU B 364     -18.667 -20.173  24.946  1.00 36.70           C  
ANISOU 3030  CB  LEU B 364     6614   3945   3385   1092    641    115       C  
ATOM   3031  CG  LEU B 364     -18.575 -20.614  23.476  1.00 36.62           C  
ANISOU 3031  CG  LEU B 364     6278   4181   3453    789    431    -76       C  
ATOM   3032  CD1 LEU B 364     -17.123 -20.694  23.024  1.00 36.12           C  
ANISOU 3032  CD1 LEU B 364     6362   4095   3266   1574    527   -201       C  
ATOM   3033  CD2 LEU B 364     -19.296 -21.930  23.210  1.00 35.05           C  
ANISOU 3033  CD2 LEU B 364     6442   3434   3441   1315    285    -85       C  
ATOM   3034  N   ASP B 365     -19.553 -18.534  27.546  1.00 45.65           N  
ANISOU 3034  N   ASP B 365     7702   5159   4482   1752    804   -123       N  
ATOM   3035  CA  ASP B 365     -19.653 -18.310  28.993  1.00 50.08           C  
ANISOU 3035  CA  ASP B 365     8761   5970   4295   1983    919    324       C  
ATOM   3036  C   ASP B 365     -21.105 -18.247  29.454  1.00 52.23           C  
ANISOU 3036  C   ASP B 365     8867   5719   5256   2442   1116    100       C  
ATOM   3037  O   ASP B 365     -21.447 -18.784  30.513  1.00 53.01           O  
ANISOU 3037  O   ASP B 365     8910   5740   5492   2185   1778   -112       O  
ATOM   3038  CB  ASP B 365     -18.921 -17.031  29.420  1.00 53.59           C  
ANISOU 3038  CB  ASP B 365     9235   5729   5395   2039    810    438       C  
ATOM   3039  CG  ASP B 365     -18.864 -16.868  30.937  1.00 64.13           C  
ANISOU 3039  CG  ASP B 365    11116   7474   5776   1872    439   -724       C  
ATOM   3040  OD1 ASP B 365     -18.226 -17.710  31.616  1.00 65.65           O  
ANISOU 3040  OD1 ASP B 365    11482   8731   4729   1448      4   -167       O  
ATOM   3041  OD2 ASP B 365     -19.461 -15.898  31.453  1.00 70.05           O  
ANISOU 3041  OD2 ASP B 365    11489   7099   8026   2150    769   -459       O  
ATOM   3042  N   SER B 366     -21.944 -17.593  28.652  1.00 53.97           N  
ANISOU 3042  N   SER B 366     8908   6143   5452   2196   1201    681       N  
ATOM   3043  CA  SER B 366     -23.373 -17.497  28.924  1.00 56.08           C  
ANISOU 3043  CA  SER B 366     8938   6900   5467   2420   1364    708       C  
ATOM   3044  C   SER B 366     -24.033 -18.874  28.847  1.00 56.19           C  
ANISOU 3044  C   SER B 366     9028   6812   5509   2591   1459    348       C  
ATOM   3045  O   SER B 366     -24.876 -19.212  29.684  1.00 56.79           O  
ANISOU 3045  O   SER B 366     9218   6434   5925   3174   2116   -178       O  
ATOM   3046  CB  SER B 366     -24.037 -16.531  27.951  1.00 60.53           C  
ANISOU 3046  CB  SER B 366     9596   6905   6494   3214   1787   1223       C  
ATOM   3047  OG  SER B 366     -25.423 -16.441  28.217  1.00 70.24           O  
ANISOU 3047  OG  SER B 366     9606   9512   7568   2349   1347   2613       O  
ATOM   3048  N   LYS B 367     -23.627 -19.662  27.852  1.00 52.81           N  
ANISOU 3048  N   LYS B 367     8523   6375   5166   2733   1479    798       N  
ATOM   3049  CA  LYS B 367     -24.157 -21.002  27.650  1.00 54.75           C  
ANISOU 3049  CA  LYS B 367     8549   6906   5344   2014   1170    810       C  
ATOM   3050  C   LYS B 367     -23.753 -21.938  28.792  1.00 50.70           C  
ANISOU 3050  C   LYS B 367     7658   6178   5427   1880   1340    608       C  
ATOM   3051  O   LYS B 367     -24.579 -22.724  29.270  1.00 50.22           O  
ANISOU 3051  O   LYS B 367     8102   6347   4630   1768   1184    854       O  
ATOM   3052  CB  LYS B 367     -23.723 -21.542  26.279  1.00 58.08           C  
ANISOU 3052  CB  LYS B 367     8331   7574   6162   1984   1381   -170       C  
ATOM   3053  CG  LYS B 367     -24.810 -22.255  25.472  1.00 65.92           C  
ANISOU 3053  CG  LYS B 367     9419   8108   7518   1300   1593  -1493       C  
ATOM   3054  CD  LYS B 367     -26.206 -21.627  25.553  1.00 73.32           C  
ANISOU 3054  CD  LYS B 367     9623   9673   8561   1878   1200   -144       C  
ATOM   3055  CE  LYS B 367     -26.354 -20.326  24.769  1.00 77.30           C  
ANISOU 3055  CE  LYS B 367    10831  10479   8060    580   1283    584       C  
ATOM   3056  NZ  LYS B 367     -27.059 -20.509  23.472  1.00 79.45           N  
ANISOU 3056  NZ  LYS B 367    10306  10805   9073    772    836   -834       N  
ATOM   3057  N   LEU B 368     -22.505 -21.809  29.248  1.00 45.60           N  
ANISOU 3057  N   LEU B 368     7510   5214   4600   1581   1625    718       N  
ATOM   3058  CA  LEU B 368     -21.976 -22.621  30.343  1.00 48.44           C  
ANISOU 3058  CA  LEU B 368     7800   6322   4282   1565   1018    551       C  
ATOM   3059  C   LEU B 368     -22.683 -22.343  31.667  1.00 52.04           C  
ANISOU 3059  C   LEU B 368     8507   6644   4620   2146   1236    247       C  
ATOM   3060  O   LEU B 368     -23.009 -23.282  32.403  1.00 54.27           O  
ANISOU 3060  O   LEU B 368     8991   7194   4436   2306    893    781       O  
ATOM   3061  CB  LEU B 368     -20.460 -22.442  30.488  1.00 46.96           C  
ANISOU 3061  CB  LEU B 368     7858   5860   4125   1497    521     44       C  
ATOM   3062  CG  LEU B 368     -19.708 -23.264  31.554  1.00 45.20           C  
ANISOU 3062  CG  LEU B 368     7985   5132   4055   1583    738    -96       C  
ATOM   3063  CD1 LEU B 368     -19.650 -24.750  31.222  1.00 44.02           C  
ANISOU 3063  CD1 LEU B 368     7874   5098   3753   1501    742   -300       C  
ATOM   3064  CD2 LEU B 368     -18.303 -22.716  31.771  1.00 45.52           C  
ANISOU 3064  CD2 LEU B 368     7831   5433   4031   1791    464   -290       C  
ATOM   3065  N   GLN B 369     -22.929 -21.063  31.953  1.00 54.55           N  
ANISOU 3065  N   GLN B 369     9257   6581   4885   1937   1212    -62       N  
ATOM   3066  CA  GLN B 369     -23.631 -20.653  33.167  1.00 58.41           C  
ANISOU 3066  CA  GLN B 369     9595   7428   5169   2277   1819    327       C  
ATOM   3067  C   GLN B 369     -25.065 -21.175  33.222  1.00 59.22           C  
ANISOU 3067  C   GLN B 369     9464   7339   5696   2481   1877    181       C  
ATOM   3068  O   GLN B 369     -25.536 -21.557  34.298  1.00 60.80           O  
ANISOU 3068  O   GLN B 369     9754   6716   6630   2725   2574    529       O  
ATOM   3069  CB  GLN B 369     -23.591 -19.127  33.357  1.00 64.46           C  
ANISOU 3069  CB  GLN B 369    10641   7540   6308   2609   1678    301       C  
ATOM   3070  CG  GLN B 369     -22.205 -18.545  33.636  1.00 68.01           C  
ANISOU 3070  CG  GLN B 369    11459   7896   6484   1960   1569   -592       C  
ATOM   3071  CD  GLN B 369     -21.497 -19.173  34.830  1.00 75.75           C  
ANISOU 3071  CD  GLN B 369    12153   9508   7117   2312    831   -534       C  
ATOM   3072  OE1 GLN B 369     -21.852 -18.924  35.989  1.00 78.50           O  
ANISOU 3072  OE1 GLN B 369    13634   9268   6924   1299    909   -587       O  
ATOM   3073  NE2 GLN B 369     -20.477 -19.986  34.549  1.00 75.12           N  
ANISOU 3073  NE2 GLN B 369    11632   9136   7772   2252   -289   -967       N  
ATOM   3074  N   GLU B 370     -25.738 -21.198  32.069  1.00 59.86           N  
ANISOU 3074  N   GLU B 370     9486   8085   5173   2521   2348     66       N  
ATOM   3075  CA  GLU B 370     -27.056 -21.837  31.915  1.00 65.38           C  
ANISOU 3075  CA  GLU B 370     9321   8881   6636   2244   2688   1216       C  
ATOM   3076  C   GLU B 370     -27.010 -23.325  32.266  1.00 63.87           C  
ANISOU 3076  C   GLU B 370     8795   8848   6622   2236   2470   1293       C  
ATOM   3077  O   GLU B 370     -27.915 -23.834  32.935  1.00 64.95           O  
ANISOU 3077  O   GLU B 370     8295   9381   7001   2088   1990   1713       O  
ATOM   3078  CB  GLU B 370     -27.583 -21.686  30.485  1.00 70.44           C  
ANISOU 3078  CB  GLU B 370     9428  10059   7273   2123   1768   1058       C  
ATOM   3079  CG  GLU B 370     -28.102 -20.309  30.113  1.00 76.36           C  
ANISOU 3079  CG  GLU B 370     9572  10413   9029   2374   2141   1637       C  
ATOM   3080  CD  GLU B 370     -28.767 -20.306  28.749  1.00 82.13           C  
ANISOU 3080  CD  GLU B 370    10138  11622   9443   1674   1689   1145       C  
ATOM   3081  OE1 GLU B 370     -28.105 -19.925  27.760  1.00 83.11           O  
ANISOU 3081  OE1 GLU B 370    10118  12066   9393   1548   2268     -1       O  
ATOM   3082  OE2 GLU B 370     -29.946 -20.704  28.662  1.00 80.85           O  
ANISOU 3082  OE2 GLU B 370    10430  10960   9328   1265   2333    340       O  
ATOM   3083  N   ILE B 371     -25.956 -24.005  31.805  1.00 59.97           N  
ANISOU 3083  N   ILE B 371     8385   8079   6321   1706   2617   1704       N  
ATOM   3084  CA  ILE B 371     -25.735 -25.434  32.063  1.00 57.79           C  
ANISOU 3084  CA  ILE B 371     8084   8004   5869   1739   2148   1220       C  
ATOM   3085  C   ILE B 371     -25.453 -25.688  33.549  1.00 60.55           C  
ANISOU 3085  C   ILE B 371     8664   8464   5877   2174   2179   1262       C  
ATOM   3086  O   ILE B 371     -26.095 -26.544  34.164  1.00 66.08           O  
ANISOU 3086  O   ILE B 371     8821   9277   7008   1856   2312   1654       O  
ATOM   3087  CB  ILE B 371     -24.616 -26.019  31.153  1.00 54.85           C  
ANISOU 3087  CB  ILE B 371     8070   7403   5368   1486   2157   1518       C  
ATOM   3088  CG1 ILE B 371     -25.074 -26.050  29.688  1.00 57.52           C  
ANISOU 3088  CG1 ILE B 371     8144   7995   5715   1159   1677   1002       C  
ATOM   3089  CG2 ILE B 371     -24.203 -27.419  31.601  1.00 55.60           C  
ANISOU 3089  CG2 ILE B 371     8237   7189   5697   1443   2686   1500       C  
ATOM   3090  CD1 ILE B 371     -23.949 -26.070  28.668  1.00 55.56           C  
ANISOU 3090  CD1 ILE B 371     8074   7693   5344   1587   1502    852       C  
ATOM   3091  N   LEU B 372     -24.520 -24.922  34.117  1.00 59.86           N  
ANISOU 3091  N   LEU B 372     9165   7980   5597   2349   2278    995       N  
ATOM   3092  CA  LEU B 372     -24.083 -25.098  35.508  1.00 63.11           C  
ANISOU 3092  CA  LEU B 372     9619   8864   5496   2103   2256   1031       C  
ATOM   3093  C   LEU B 372     -25.098 -24.659  36.569  1.00 66.88           C  
ANISOU 3093  C   LEU B 372    10391   9301   5716   2056   2774    995       C  
ATOM   3094  O   LEU B 372     -25.014 -25.104  37.714  1.00 72.98           O  
ANISOU 3094  O   LEU B 372    11229  10975   5525   2760   1177    685       O  
ATOM   3095  CB  LEU B 372     -22.719 -24.429  35.749  1.00 59.48           C  
ANISOU 3095  CB  LEU B 372     9657   8451   4489   2163   1911   1021       C  
ATOM   3096  CG  LEU B 372     -21.495 -24.934  34.967  1.00 58.07           C  
ANISOU 3096  CG  LEU B 372     9512   7763   4788   1998   1737    750       C  
ATOM   3097  CD1 LEU B 372     -20.252 -24.155  35.372  1.00 62.52           C  
ANISOU 3097  CD1 LEU B 372     9740   8590   5424   1585   1536    885       C  
ATOM   3098  CD2 LEU B 372     -21.261 -26.432  35.126  1.00 58.90           C  
ANISOU 3098  CD2 LEU B 372    10239   7770   4371   2347   1484    563       C  
ATOM   3099  N   GLU B 373     -26.049 -23.802  36.191  1.00 70.03           N  
ANISOU 3099  N   GLU B 373    10700  10067   5841   2561   3055   1440       N  
ATOM   3100  CA  GLU B 373     -27.105 -23.356  37.105  1.00 79.11           C  
ANISOU 3100  CA  GLU B 373    11299  11414   7343   3284   3880   1635       C  
ATOM   3101  C   GLU B 373     -28.155 -24.451  37.315  1.00 87.14           C  
ANISOU 3101  C   GLU B 373    11870  12064   9173   2647   2976   1873       C  
ATOM   3102  O   GLU B 373     -28.559 -24.734  38.447  1.00 93.40           O  
ANISOU 3102  O   GLU B 373    12553  13588   9346   2581   2997   2554       O  
ATOM   3103  CB  GLU B 373     -27.760 -22.064  36.601  1.00 82.57           C  
ANISOU 3103  CB  GLU B 373    12095  11302   7972   3406   4030   1764       C  
ATOM   3104  CG  GLU B 373     -28.726 -21.421  37.593  1.00 94.31           C  
ANISOU 3104  CG  GLU B 373    13554  13049   9230   4446   4084    388       C  
ATOM   3105  CD  GLU B 373     -28.970 -19.936  37.356  1.00100.12           C  
ANISOU 3105  CD  GLU B 373    14614  13360  10066   4853   3642   1172       C  
ATOM   3106  OE1 GLU B 373     -29.495 -19.280  38.286  1.00101.50           O  
ANISOU 3106  OE1 GLU B 373    12000  14033  12532   6221   4132    921       O  
ATOM   3107  OE2 GLU B 373     -28.647 -19.419  36.260  1.00 97.97           O  
ANISOU 3107  OE2 GLU B 373    14566  13891   8766   5821   3154    758       O  
TER    3108      GLU B 373                                                      
ATOM   3109  O5'  DA C   1     -47.205 -25.839  12.328  1.00 71.86           O  
ANISOU 3109  O5'  DA C   1     5882  15055   6367   -525   -652   -714       O  
ATOM   3110  C5'  DA C   1     -47.112 -26.905  13.292  1.00 78.54           C  
ANISOU 3110  C5'  DA C   1     6915  14650   8275  -3064     85    441       C  
ATOM   3111  C4'  DA C   1     -45.692 -27.416  13.380  1.00 81.22           C  
ANISOU 3111  C4'  DA C   1     7484  14557   8817  -2373    290   1114       C  
ATOM   3112  O4'  DA C   1     -45.293 -27.991  12.116  1.00 75.24           O  
ANISOU 3112  O4'  DA C   1     7746  11317   9522  -2598   -290    709       O  
ATOM   3113  C3'  DA C   1     -44.631 -26.364  13.732  1.00 85.46           C  
ANISOU 3113  C3'  DA C   1     8391  14553   9528  -2645    815    219       C  
ATOM   3114  O3'  DA C   1     -43.820 -26.810  14.826  1.00 88.91           O  
ANISOU 3114  O3'  DA C   1     8754  15028   9998  -1895    973    582       O  
ATOM   3115  C2'  DA C   1     -43.787 -26.243  12.471  1.00 79.52           C  
ANISOU 3115  C2'  DA C   1     7841  13304   9067  -2460    366    306       C  
ATOM   3116  C1'  DA C   1     -43.961 -27.607  11.828  1.00 77.53           C  
ANISOU 3116  C1'  DA C   1     7836  11879   9743  -1859    820   1443       C  
ATOM   3117  N9   DA C   1     -43.778 -27.687  10.375  1.00 67.05           N  
ANISOU 3117  N9   DA C   1     6662   9203   9611  -1868      0   1127       N  
ATOM   3118  C8   DA C   1     -43.025 -28.622   9.710  1.00 64.79           C  
ANISOU 3118  C8   DA C   1     6994   9357   8266  -2212    308   1193       C  
ATOM   3119  N7   DA C   1     -43.051 -28.494   8.407  1.00 56.89           N  
ANISOU 3119  N7   DA C   1     5268   7975   8372  -2963    -58   2349       N  
ATOM   3120  C5   DA C   1     -43.888 -27.409   8.196  1.00 58.45           C  
ANISOU 3120  C5   DA C   1     5095   8652   8461  -2378    593   1574       C  
ATOM   3121  C6   DA C   1     -44.326 -26.768   7.024  1.00 59.55           C  
ANISOU 3121  C6   DA C   1     5063   9564   7997  -2404    830   1643       C  
ATOM   3122  N6   DA C   1     -43.970 -27.150   5.795  1.00 51.34           N  
ANISOU 3122  N6   DA C   1     3356   8479   7671  -2112    166   1747       N  
ATOM   3123  N1   DA C   1     -45.155 -25.709   7.159  1.00 62.85           N  
ANISOU 3123  N1   DA C   1     5954   9971   7955  -1656      1   1745       N  
ATOM   3124  C2   DA C   1     -45.516 -25.331   8.393  1.00 63.55           C  
ANISOU 3124  C2   DA C   1     6208   9248   8688  -1315    137    748       C  
ATOM   3125  N3   DA C   1     -45.176 -25.857   9.569  1.00 67.87           N  
ANISOU 3125  N3   DA C   1     6827  10407   8550  -1896   -331    896       N  
ATOM   3126  C4   DA C   1     -44.350 -26.905   9.399  1.00 64.97           C  
ANISOU 3126  C4   DA C   1     6465  10203   8017  -2387   -150    778       C  
ATOM   3127  P    DT C   2     -44.414 -26.891  16.324  1.00 90.39           P  
ANISOU 3127  P    DT C   2     8271  16539   9532  -2566    533   1015       P  
ATOM   3128  OP1  DT C   2     -44.473 -28.321  16.717  1.00 86.00           O  
ANISOU 3128  OP1  DT C   2     7761  16695   8220  -3243    402    568       O  
ATOM   3129  OP2  DT C   2     -45.648 -26.060  16.399  1.00 87.40           O  
ANISOU 3129  OP2  DT C   2     7807  16550   8850  -3067    382    892       O  
ATOM   3130  O5'  DT C   2     -43.273 -26.199  17.194  1.00 90.32           O  
ANISOU 3130  O5'  DT C   2     7849  17094   9373  -2263    529   1111       O  
ATOM   3131  C5'  DT C   2     -42.892 -24.823  16.984  1.00 88.40           C  
ANISOU 3131  C5'  DT C   2     7322  16903   9363  -2410    517    873       C  
ATOM   3132  C4'  DT C   2     -41.396 -24.660  17.131  1.00 82.44           C  
ANISOU 3132  C4'  DT C   2     7158  14951   9214  -2539   1624    961       C  
ATOM   3133  O4'  DT C   2     -40.883 -25.576  18.129  1.00 86.92           O  
ANISOU 3133  O4'  DT C   2     8065  15372   9587  -2733   1070   1269       O  
ATOM   3134  C3'  DT C   2     -40.591 -24.917  15.855  1.00 81.57           C  
ANISOU 3134  C3'  DT C   2     8062  14495   8436  -2036   1006    481       C  
ATOM   3135  O3'  DT C   2     -39.615 -23.885  15.663  1.00 76.16           O  
ANISOU 3135  O3'  DT C   2     7386  13562   7989  -1423   1138   -437       O  
ATOM   3136  C2'  DT C   2     -39.943 -26.270  16.092  1.00 85.59           C  
ANISOU 3136  C2'  DT C   2     8500  14516   9503  -2452    954   1361       C  
ATOM   3137  C1'  DT C   2     -39.791 -26.315  17.603  1.00 90.58           C  
ANISOU 3137  C1'  DT C   2     8373  16528   9511  -2505   1433   1502       C  
ATOM   3138  N1   DT C   2     -39.829 -27.671  18.199  1.00103.90           N  
ANISOU 3138  N1   DT C   2    10334  17392  11748  -2503    583   2665       N  
ATOM   3139  C2   DT C   2     -38.756 -28.081  18.960  1.00105.68           C  
ANISOU 3139  C2   DT C   2     9880  17590  12682  -2439    571   2798       C  
ATOM   3140  O2   DT C   2     -37.773 -27.385  19.160  1.00101.87           O  
ANISOU 3140  O2   DT C   2     9678  16816  12209  -2251    766   3385       O  
ATOM   3141  N3   DT C   2     -38.876 -29.346  19.483  1.00107.22           N  
ANISOU 3141  N3   DT C   2    10149  18163  12426  -2577    412   3494       N  
ATOM   3142  C4   DT C   2     -39.936 -30.220  19.324  1.00111.98           C  
ANISOU 3142  C4   DT C   2    11569  18495  12483  -3592    667   3919       C  
ATOM   3143  O4   DT C   2     -39.900 -31.328  19.854  1.00120.39           O  
ANISOU 3143  O4   DT C   2    13845  19319  12576  -2451    552   4780       O  
ATOM   3144  C5   DT C   2     -41.029 -29.723  18.515  1.00114.65           C  
ANISOU 3144  C5   DT C   2    11497  18704  13359  -3576    289   3588       C  
ATOM   3145  C7   DT C   2     -42.222 -30.598  18.288  1.00112.78           C  
ANISOU 3145  C7   DT C   2    10206  19177  13465  -3474    889   4814       C  
ATOM   3146  C6   DT C   2     -40.922 -28.490  18.003  1.00111.95           C  
ANISOU 3146  C6   DT C   2    11123  18187  13226  -3352    641   2970       C  
ATOM   3147  P    DT C   3     -39.817 -22.794  14.505  1.00 72.29           P  
ANISOU 3147  P    DT C   3     7009  12046   8412  -1030   1128   -877       P  
ATOM   3148  OP1  DT C   3     -38.512 -22.118  14.277  1.00 74.85           O  
ANISOU 3148  OP1  DT C   3     7502  11605   9331  -1213   1645  -1650       O  
ATOM   3149  OP2  DT C   3     -41.009 -21.977  14.843  1.00 63.22           O  
ANISOU 3149  OP2  DT C   3     5970  10870   7180  -2084    268  -1950       O  
ATOM   3150  O5'  DT C   3     -40.179 -23.688  13.236  1.00 73.20           O  
ANISOU 3150  O5'  DT C   3     7930  11799   8082  -1050    743   -338       O  
ATOM   3151  C5'  DT C   3     -39.173 -24.450  12.538  1.00 70.75           C  
ANISOU 3151  C5'  DT C   3     7608  11135   8137  -1007    725    213       C  
ATOM   3152  C4'  DT C   3     -39.106 -24.017  11.092  1.00 60.57           C  
ANISOU 3152  C4'  DT C   3     5691   9243   8078  -1100    172     84       C  
ATOM   3153  O4'  DT C   3     -40.417 -24.117  10.487  1.00 57.32           O  
ANISOU 3153  O4'  DT C   3     5488   9449   6839   -858    463    -22       O  
ATOM   3154  C3'  DT C   3     -38.639 -22.577  10.874  1.00 59.00           C  
ANISOU 3154  C3'  DT C   3     5505   8927   7984   -867    147    272       C  
ATOM   3155  O3'  DT C   3     -37.727 -22.519   9.775  1.00 62.93           O  
ANISOU 3155  O3'  DT C   3     6750   8961   8200   -731    834   -346       O  
ATOM   3156  C2'  DT C   3     -39.916 -21.818  10.562  1.00 54.67           C  
ANISOU 3156  C2'  DT C   3     4551   8361   7860  -1424    842    110       C  
ATOM   3157  C1'  DT C   3     -40.804 -22.872   9.923  1.00 56.15           C  
ANISOU 3157  C1'  DT C   3     5104   8767   7461  -1019    193   -386       C  
ATOM   3158  N1   DT C   3     -42.247 -22.682  10.187  1.00 56.83           N  
ANISOU 3158  N1   DT C   3     5174   8441   7976   -829    247   -313       N  
ATOM   3159  C2   DT C   3     -43.094 -22.466   9.120  1.00 55.29           C  
ANISOU 3159  C2   DT C   3     5143   7790   8074  -1197     75   -427       C  
ATOM   3160  O2   DT C   3     -42.716 -22.435   7.960  1.00 51.23           O  
ANISOU 3160  O2   DT C   3     5688   6188   7588   -922   -487    703       O  
ATOM   3161  N3   DT C   3     -44.412 -22.291   9.464  1.00 56.23           N  
ANISOU 3161  N3   DT C   3     4981   7772   8611  -1449    -25   -370       N  
ATOM   3162  C4   DT C   3     -44.954 -22.305  10.737  1.00 60.96           C  
ANISOU 3162  C4   DT C   3     5022   9395   8744  -1315    281   -303       C  
ATOM   3163  O4   DT C   3     -46.159 -22.133  10.888  1.00 57.56           O  
ANISOU 3163  O4   DT C   3     5358   9741   6768   -575    672   -780       O  
ATOM   3164  C5   DT C   3     -44.008 -22.534  11.808  1.00 66.93           C  
ANISOU 3164  C5   DT C   3     5614  11082   8731   -774    207    -30       C  
ATOM   3165  C7   DT C   3     -44.500 -22.564  13.221  1.00 68.35           C  
ANISOU 3165  C7   DT C   3     5487  12051   8430    261   -158    887       C  
ATOM   3166  C6   DT C   3     -42.720 -22.706  11.483  1.00 63.98           C  
ANISOU 3166  C6   DT C   3     5864  10323   8122   -529    511    205       C  
ATOM   3167  P    DT C   4     -36.724 -21.280   9.623  1.00 62.48           P  
ANISOU 3167  P    DT C   4     7226   8584   7928   -729    577     22       P  
ATOM   3168  OP1  DT C   4     -36.445 -20.723  10.972  1.00 64.83           O  
ANISOU 3168  OP1  DT C   4     7880   8897   7853    505    289    -17       O  
ATOM   3169  OP2  DT C   4     -37.252 -20.391   8.555  1.00 68.74           O  
ANISOU 3169  OP2  DT C   4     9248   7970   8897    518  -1072  -1028       O  
ATOM   3170  O5'  DT C   4     -35.384 -21.966   9.104  1.00 59.20           O  
ANISOU 3170  O5'  DT C   4     6955   7639   7896   -568   -203    279       O  
ATOM   3171  C5'  DT C   4     -34.902 -23.214   9.651  1.00 50.50           C  
ANISOU 3171  C5'  DT C   4     5703   7423   6061  -1003    287    226       C  
ATOM   3172  C4'  DT C   4     -33.890 -23.841   8.717  1.00 45.48           C  
ANISOU 3172  C4'  DT C   4     5540   5702   6037  -1049    -20    390       C  
ATOM   3173  O4'  DT C   4     -34.561 -24.577   7.668  1.00 45.69           O  
ANISOU 3173  O4'  DT C   4     5838   5296   6224  -1076   -224    460       O  
ATOM   3174  C3'  DT C   4     -32.953 -22.860   8.009  1.00 42.84           C  
ANISOU 3174  C3'  DT C   4     5331   5480   5463   -820    -20    407       C  
ATOM   3175  O3'  DT C   4     -31.658 -23.432   7.830  1.00 40.78           O  
ANISOU 3175  O3'  DT C   4     5123   5349   5021  -1066    -93    402       O  
ATOM   3176  C2'  DT C   4     -33.570 -22.712   6.631  1.00 42.25           C  
ANISOU 3176  C2'  DT C   4     5139   5537   5374  -1293    138    585       C  
ATOM   3177  C1'  DT C   4     -34.201 -24.069   6.389  1.00 45.09           C  
ANISOU 3177  C1'  DT C   4     5474   5660   5998  -1358    -71    309       C  
ATOM   3178  N1   DT C   4     -35.422 -24.022   5.564  1.00 44.16           N  
ANISOU 3178  N1   DT C   4     5569   5092   6118  -1398   -115    594       N  
ATOM   3179  C2   DT C   4     -35.342 -24.378   4.235  1.00 43.36           C  
ANISOU 3179  C2   DT C   4     5385   5152   5937  -1647   -229    781       C  
ATOM   3180  O2   DT C   4     -34.306 -24.736   3.699  1.00 44.21           O  
ANISOU 3180  O2   DT C   4     5502   5258   6035  -1615     58   1212       O  
ATOM   3181  N3   DT C   4     -36.533 -24.311   3.554  1.00 42.08           N  
ANISOU 3181  N3   DT C   4     5404   4925   5659  -1627   -168    865       N  
ATOM   3182  C4   DT C   4     -37.763 -23.931   4.056  1.00 39.92           C  
ANISOU 3182  C4   DT C   4     5106   4357   5702  -1824   -269   1091       C  
ATOM   3183  O4   DT C   4     -38.745 -23.920   3.321  1.00 42.62           O  
ANISOU 3183  O4   DT C   4     5597   5302   5294  -1468   -383    666       O  
ATOM   3184  C5   DT C   4     -37.772 -23.561   5.454  1.00 39.15           C  
ANISOU 3184  C5   DT C   4     4914   4192   5767  -1646   -111   1162       C  
ATOM   3185  C7   DT C   4     -39.059 -23.133   6.086  1.00 37.22           C  
ANISOU 3185  C7   DT C   4     4876   3885   5379  -1437   -206   1620       C  
ATOM   3186  C6   DT C   4     -36.617 -23.627   6.129  1.00 40.70           C  
ANISOU 3186  C6   DT C   4     5018   4574   5871  -1877   -253    875       C  
ATOM   3187  P    DT C   5     -30.592 -23.488   9.024  1.00 40.36           P  
ANISOU 3187  P    DT C   5     5134   5511   4686   -818     47    658       P  
ATOM   3188  OP1  DT C   5     -29.842 -24.760   8.881  1.00 41.04           O  
ANISOU 3188  OP1  DT C   5     5760   4832   5001  -1024   -535   1301       O  
ATOM   3189  OP2  DT C   5     -31.271 -23.180  10.307  1.00 37.24           O  
ANISOU 3189  OP2  DT C   5     4352   4758   5039   -279    128    829       O  
ATOM   3190  O5'  DT C   5     -29.619 -22.272   8.685  1.00 37.17           O  
ANISOU 3190  O5'  DT C   5     5022   5021   4078   -566   -278    895       O  
ATOM   3191  C5'  DT C   5     -28.829 -22.264   7.482  1.00 35.55           C  
ANISOU 3191  C5'  DT C   5     4746   4809   3949   -673   -432    994       C  
ATOM   3192  C4'  DT C   5     -27.551 -21.489   7.703  1.00 37.53           C  
ANISOU 3192  C4'  DT C   5     4677   5708   3873   -822   -363    769       C  
ATOM   3193  O4'  DT C   5     -27.853 -20.103   7.997  1.00 35.73           O  
ANISOU 3193  O4'  DT C   5     4581   5262   3730  -1053   -785   1495       O  
ATOM   3194  C3'  DT C   5     -26.679 -21.995   8.856  1.00 36.12           C  
ANISOU 3194  C3'  DT C   5     4826   5406   3493   -882   -225    660       C  
ATOM   3195  O3'  DT C   5     -25.316 -21.965   8.441  1.00 38.56           O  
ANISOU 3195  O3'  DT C   5     4918   5763   3970   -532    -35    444       O  
ATOM   3196  C2'  DT C   5     -26.861 -20.947   9.937  1.00 34.41           C  
ANISOU 3196  C2'  DT C   5     4285   5380   3405   -874   -334    765       C  
ATOM   3197  C1'  DT C   5     -27.112 -19.688   9.129  1.00 36.43           C  
ANISOU 3197  C1'  DT C   5     4493   5530   3816  -1096   -611   1042       C  
ATOM   3198  N1   DT C   5     -27.898 -18.671   9.855  1.00 39.52           N  
ANISOU 3198  N1   DT C   5     5071   5832   4110   -758   -652   1035       N  
ATOM   3199  C2   DT C   5     -27.226 -17.564  10.330  1.00 42.70           C  
ANISOU 3199  C2   DT C   5     5651   5626   4944   -846  -1049   1190       C  
ATOM   3200  O2   DT C   5     -26.037 -17.370  10.133  1.00 42.14           O  
ANISOU 3200  O2   DT C   5     6001   5082   4925  -1510   -902   1628       O  
ATOM   3201  N3   DT C   5     -28.005 -16.681  11.036  1.00 41.97           N  
ANISOU 3201  N3   DT C   5     5608   5077   5259   -802  -1295   1272       N  
ATOM   3202  C4   DT C   5     -29.354 -16.794  11.316  1.00 46.51           C  
ANISOU 3202  C4   DT C   5     5726   6144   5801   -406   -992    801       C  
ATOM   3203  O4   DT C   5     -29.920 -15.913  11.960  1.00 54.05           O  
ANISOU 3203  O4   DT C   5     7486   7069   5979    122   -909    298       O  
ATOM   3204  C5   DT C   5     -29.993 -17.989  10.803  1.00 42.32           C  
ANISOU 3204  C5   DT C   5     4983   5950   5146   -190   -754    792       C  
ATOM   3205  C7   DT C   5     -31.452 -18.200  11.057  1.00 38.99           C  
ANISOU 3205  C7   DT C   5     5069   5436   4306    108   -162    605       C  
ATOM   3206  C6   DT C   5     -29.242 -18.856  10.111  1.00 39.23           C  
ANISOU 3206  C6   DT C   5     4987   5330   4585   -608   -727    954       C  
ATOM   3207  P    DC C   6     -24.405 -23.250   8.582  1.00 38.92           P  
ANISOU 3207  P    DC C   6     5181   5834   3771   -327   -152    880       P  
ATOM   3208  OP1  DC C   6     -23.042 -22.882   8.132  1.00 38.12           O  
ANISOU 3208  OP1  DC C   6     5123   5401   3959    241    -11   1100       O  
ATOM   3209  OP2  DC C   6     -25.112 -24.376   7.925  1.00 37.48           O  
ANISOU 3209  OP2  DC C   6     4405   5534   4299    -50    213    859       O  
ATOM   3210  O5'  DC C   6     -24.387 -23.494  10.153  1.00 38.48           O  
ANISOU 3210  O5'  DC C   6     5165   5683   3770    -50    427    418       O  
ATOM   3211  C5'  DC C   6     -23.170 -23.458  10.917  1.00 40.07           C  
ANISOU 3211  C5'  DC C   6     5115   6237   3871   -121    419    749       C  
ATOM   3212  C4'  DC C   6     -23.436 -23.954  12.317  1.00 41.38           C  
ANISOU 3212  C4'  DC C   6     5358   6493   3872     -8    553    744       C  
ATOM   3213  O4'  DC C   6     -24.298 -23.014  12.985  1.00 41.83           O  
ANISOU 3213  O4'  DC C   6     5568   5981   4342     80    315    697       O  
ATOM   3214  C3'  DC C   6     -24.154 -25.297  12.400  1.00 42.45           C  
ANISOU 3214  C3'  DC C   6     5423   6390   4314     43    564    633       C  
ATOM   3215  O3'  DC C   6     -23.148 -26.307  12.472  1.00 41.26           O  
ANISOU 3215  O3'  DC C   6     5903   5970   3801     97    496   1029       O  
ATOM   3216  C2'  DC C   6     -24.944 -25.188  13.693  1.00 42.53           C  
ANISOU 3216  C2'  DC C   6     5535   6130   4491   -371    788    941       C  
ATOM   3217  C1'  DC C   6     -25.219 -23.689  13.831  1.00 43.90           C  
ANISOU 3217  C1'  DC C   6     5547   6272   4859   -136    550    665       C  
ATOM   3218  N1   DC C   6     -26.572 -23.217  13.478  1.00 45.04           N  
ANISOU 3218  N1   DC C   6     5472   6409   5231   -361    422   1031       N  
ATOM   3219  C2   DC C   6     -27.057 -22.049  14.084  1.00 49.19           C  
ANISOU 3219  C2   DC C   6     6091   7273   5323     61    251    567       C  
ATOM   3220  O2   DC C   6     -26.350 -21.467  14.921  1.00 54.72           O  
ANISOU 3220  O2   DC C   6     7005   8450   5333    -10   -487    805       O  
ATOM   3221  N3   DC C   6     -28.288 -21.593  13.750  1.00 47.20           N  
ANISOU 3221  N3   DC C   6     5631   6896   5405   -260    605    533       N  
ATOM   3222  C4   DC C   6     -29.017 -22.247  12.840  1.00 46.14           C  
ANISOU 3222  C4   DC C   6     5525   6953   5051   -191    481   1001       C  
ATOM   3223  N4   DC C   6     -30.225 -21.764  12.544  1.00 46.90           N  
ANISOU 3223  N4   DC C   6     5669   7146   5002    -30    736   1730       N  
ATOM   3224  C5   DC C   6     -28.541 -23.429  12.198  1.00 44.90           C  
ANISOU 3224  C5   DC C   6     5752   6508   4796   -451    665   1172       C  
ATOM   3225  C6   DC C   6     -27.320 -23.868  12.535  1.00 43.84           C  
ANISOU 3225  C6   DC C   6     5996   5769   4890    -21    749    608       C  
ATOM   3226  P    DA C   7     -23.405 -27.780  11.902  1.00 44.76           P  
ANISOU 3226  P    DA C   7     6242   5729   5034    161    333   1065       P  
ATOM   3227  OP1  DA C   7     -22.078 -28.409  11.661  1.00 42.80           O  
ANISOU 3227  OP1  DA C   7     6275   4862   5125   -264    776   1056       O  
ATOM   3228  OP2  DA C   7     -24.395 -27.714  10.806  1.00 42.44           O  
ANISOU 3228  OP2  DA C   7     6186   4814   5123   -360    214    659       O  
ATOM   3229  O5'  DA C   7     -24.117 -28.505  13.123  1.00 42.57           O  
ANISOU 3229  O5'  DA C   7     5909   5022   5243   -118    441    597       O  
ATOM   3230  C5'  DA C   7     -23.383 -28.822  14.313  1.00 46.98           C  
ANISOU 3230  C5'  DA C   7     6775   5413   5658    139    185   1364       C  
ATOM   3231  C4'  DA C   7     -24.322 -29.401  15.342  1.00 51.70           C  
ANISOU 3231  C4'  DA C   7     6653   6728   6259    107    505   1616       C  
ATOM   3232  O4'  DA C   7     -25.144 -28.343  15.877  1.00 48.44           O  
ANISOU 3232  O4'  DA C   7     6850   6434   5118    237   -109   1761       O  
ATOM   3233  C3'  DA C   7     -25.278 -30.469  14.804  1.00 55.64           C  
ANISOU 3233  C3'  DA C   7     7558   6636   6947    -93    -28   1779       C  
ATOM   3234  O3'  DA C   7     -25.147 -31.663  15.574  1.00 55.44           O  
ANISOU 3234  O3'  DA C   7     6845   6312   7904   -157   -144   1860       O  
ATOM   3235  C2'  DA C   7     -26.662 -29.858  14.946  1.00 56.78           C  
ANISOU 3235  C2'  DA C   7     7454   6838   7281   -295    472   1834       C  
ATOM   3236  C1'  DA C   7     -26.478 -28.793  16.011  1.00 57.28           C  
ANISOU 3236  C1'  DA C   7     7269   8039   6454   -413    454   1710       C  
ATOM   3237  N9   DA C   7     -27.353 -27.627  15.872  1.00 62.77           N  
ANISOU 3237  N9   DA C   7     8182   8594   7072     64    970   2247       N  
ATOM   3238  C8   DA C   7     -28.155 -27.288  14.809  1.00 61.96           C  
ANISOU 3238  C8   DA C   7     7886   8789   6867   -503    967   2227       C  
ATOM   3239  N7   DA C   7     -28.814 -26.167  14.980  1.00 61.48           N  
ANISOU 3239  N7   DA C   7     7408   8815   7134   -926   1768   2126       N  
ATOM   3240  C5   DA C   7     -28.413 -25.733  16.236  1.00 67.29           C  
ANISOU 3240  C5   DA C   7     8449   9890   7228   -411   1297   1994       C  
ATOM   3241  C6   DA C   7     -28.753 -24.601  17.000  1.00 76.38           C  
ANISOU 3241  C6   DA C   7     8876  10579   9564   -157   1110    855       C  
ATOM   3242  N6   DA C   7     -29.606 -23.660  16.590  1.00 85.24           N  
ANISOU 3242  N6   DA C   7     9012  11528  11846    154   1249   1694       N  
ATOM   3243  N1   DA C   7     -28.180 -24.469  18.218  1.00 78.04           N  
ANISOU 3243  N1   DA C   7     9012  10338  10298     36    483    567       N  
ATOM   3244  C2   DA C   7     -27.323 -25.413  18.630  1.00 78.63           C  
ANISOU 3244  C2   DA C   7     9450  10726   9700   -389   -192   1545       C  
ATOM   3245  N3   DA C   7     -26.921 -26.518  18.001  1.00 76.14           N  
ANISOU 3245  N3   DA C   7     9669  10429   8832   -388   -121   2089       N  
ATOM   3246  C4   DA C   7     -27.510 -26.620  16.796  1.00 68.80           C  
ANISOU 3246  C4   DA C   7     8913   9410   7817   -272   1086   1594       C  
ATOM   3247  P    DA C   8     -25.009 -33.062  14.841  1.00 57.82           P  
ANISOU 3247  P    DA C   8     7674   5582   8710   -179   -803   1806       P  
ATOM   3248  OP1  DA C   8     -25.928 -33.065  13.681  1.00 56.17           O  
ANISOU 3248  OP1  DA C   8     7667   4934   8738   -241   -735   1798       O  
ATOM   3249  OP2  DA C   8     -25.122 -34.125  15.869  1.00 57.63           O  
ANISOU 3249  OP2  DA C   8     6659   6027   9207   -101  -1005   2177       O  
ATOM   3250  O5'  DA C   8     -23.536 -33.017  14.235  1.00 52.01           O  
ANISOU 3250  O5'  DA C   8     8161   4348   7251     -6   -694   1227       O  
ATOM   3251  C5'  DA C   8     -22.361 -33.199  15.048  1.00 54.83           C  
ANISOU 3251  C5'  DA C   8     8123   5284   7425    564   -693    896       C  
ATOM   3252  C4'  DA C   8     -21.140 -32.744  14.283  1.00 52.56           C  
ANISOU 3252  C4'  DA C   8     7927   6022   6021   1177   -702    612       C  
ATOM   3253  O4'  DA C   8     -21.205 -31.313  14.111  1.00 44.50           O  
ANISOU 3253  O4'  DA C   8     6938   6034   3935   1241    -57    677       O  
ATOM   3254  C3'  DA C   8     -19.804 -33.003  14.972  1.00 55.04           C  
ANISOU 3254  C3'  DA C   8     7763   6566   6583   1381   -627    822       C  
ATOM   3255  O3'  DA C   8     -19.235 -34.235  14.542  1.00 62.67           O  
ANISOU 3255  O3'  DA C   8     8923   6389   8497   1545  -1103    700       O  
ATOM   3256  C2'  DA C   8     -18.928 -31.886  14.443  1.00 49.84           C  
ANISOU 3256  C2'  DA C   8     7259   6457   5218   1795    -74    488       C  
ATOM   3257  C1'  DA C   8     -19.910 -30.741  14.232  1.00 47.97           C  
ANISOU 3257  C1'  DA C   8     6622   6540   5063   1372    153   1305       C  
ATOM   3258  N9   DA C   8     -19.946 -29.744  15.304  1.00 46.35           N  
ANISOU 3258  N9   DA C   8     5593   6369   5648   1052    283   1283       N  
ATOM   3259  C8   DA C   8     -19.854 -28.385  15.138  1.00 44.99           C  
ANISOU 3259  C8   DA C   8     5672   6414   5008    989    248   1174       C  
ATOM   3260  N7   DA C   8     -19.893 -27.711  16.260  1.00 44.09           N  
ANISOU 3260  N7   DA C   8     5422   6605   4724    965    461   1429       N  
ATOM   3261  C5   DA C   8     -20.027 -28.690  17.233  1.00 45.14           C  
ANISOU 3261  C5   DA C   8     5510   6499   5141    959    -79   1750       C  
ATOM   3262  C6   DA C   8     -20.127 -28.624  18.634  1.00 46.59           C  
ANISOU 3262  C6   DA C   8     5881   6675   5145    843    514   2347       C  
ATOM   3263  N6   DA C   8     -20.112 -27.482  19.324  1.00 43.96           N  
ANISOU 3263  N6   DA C   8     6067   6563   4072   1352    171   2806       N  
ATOM   3264  N1   DA C   8     -20.246 -29.787  19.311  1.00 47.45           N  
ANISOU 3264  N1   DA C   8     6312   6965   4752    755    353   2540       N  
ATOM   3265  C2   DA C   8     -20.265 -30.931  18.618  1.00 49.40           C  
ANISOU 3265  C2   DA C   8     6199   6368   6201    772    258   2528       C  
ATOM   3266  N3   DA C   8     -20.181 -31.122  17.304  1.00 49.42           N  
ANISOU 3266  N3   DA C   8     6016   6315   6446   1004     96   1702       N  
ATOM   3267  C4   DA C   8     -20.057 -29.948  16.660  1.00 46.87           C  
ANISOU 3267  C4   DA C   8     5657   6438   5712   1141    -31   1618       C  
ATOM   3268  P    DC C   9     -18.444 -35.158  15.542  1.00 71.74           P  
ANISOU 3268  P    DC C   9    10821   5333  11104   2963  -1055   1182       P  
ATOM   3269  OP1  DC C   9     -18.307 -34.518  16.815  1.00 69.86           O  
ANISOU 3269  OP1  DC C   9    10727   4850  10967   1087  -1937   1699       O  
ATOM   3270  OP2  DC C   9     -17.285 -35.650  14.867  1.00 74.77           O  
ANISOU 3270  OP2  DC C   9    10346   6938  11124   3109  -1405   2635       O  
ATOM   3271  O5'  DC C   9     -19.463 -36.326  15.815  1.00 93.53           O  
ANISOU 3271  O5'  DC C   9    11823  10021  13692    472   -993   1613       O  
ATOM   3272  C5'  DC C   9     -19.114 -37.697  15.605  1.00118.01           C  
ANISOU 3272  C5'  DC C   9    14251  11488  19097   2959  -2143    467       C  
ATOM   3273  C4'  DC C   9     -19.154 -38.008  14.131  1.00129.67           C  
ANISOU 3273  C4'  DC C   9    17152  12212  19904   2838  -3813   -475       C  
ATOM   3274  O4'  DC C   9     -17.852 -37.768  13.568  1.00136.90           O  
ANISOU 3274  O4'  DC C   9    17214  14030  20768   3130  -3614   -420       O  
ATOM   3275  C3'  DC C   9     -19.438 -39.460  13.790  1.00137.91           C  
ANISOU 3275  C3'  DC C   9    17853  12047  22498   2178  -4825    211       C  
ATOM   3276  O3'  DC C   9     -19.798 -39.583  12.405  1.00129.31           O  
ANISOU 3276  O3'  DC C   9    17258   8619  23255   3143  -5146     27       O  
ATOM   3277  C2'  DC C   9     -18.074 -40.086  13.989  1.00143.81           C  
ANISOU 3277  C2'  DC C   9    18382  13407  22852   3167  -5531   -362       C  
ATOM   3278  C1'  DC C   9     -17.147 -38.999  13.452  1.00145.41           C  
ANISOU 3278  C1'  DC C   9    18480  13989  22779   3707  -4142   -124       C  
ATOM   3279  N1   DC C   9     -15.853 -38.819  14.125  1.00153.02           N  
ANISOU 3279  N1   DC C   9    18389  16726  23024   3879  -4130     12       N  
ATOM   3280  C2   DC C   9     -15.808 -38.813  15.517  1.00156.43           C  
ANISOU 3280  C2   DC C   9    19132  17249  23052   4052  -4760    221       C  
ATOM   3281  O2   DC C   9     -16.847 -39.041  16.150  1.00154.57           O  
ANISOU 3281  O2   DC C   9    20575  16638  21514   4306  -4414    988       O  
ATOM   3282  N3   DC C   9     -14.629 -38.582  16.139  1.00149.84           N  
ANISOU 3282  N3   DC C   9    18326  16755  21849   3187  -3471    573       N  
ATOM   3283  C4   DC C   9     -13.534 -38.339  15.419  1.00142.80           C  
ANISOU 3283  C4   DC C   9    17079  15122  22056   2308  -4460    713       C  
ATOM   3284  N4   DC C   9     -12.392 -38.125  16.071  1.00129.95           N  
ANISOU 3284  N4   DC C   9    16747  12355  20272   2116  -3940   2201       N  
ATOM   3285  C5   DC C   9     -13.558 -38.319  13.997  1.00142.42           C  
ANISOU 3285  C5   DC C   9    17472  14703  21937   2580  -3627    172       C  
ATOM   3286  C6   DC C   9     -14.731 -38.543  13.397  1.00150.46           C  
ANISOU 3286  C6   DC C   9    17744  16311  23109   3525  -4470    -53       C  
ATOM   3287  P    DT C  10     -20.607 -38.408  11.681  1.00 79.72           P  
ANISOU 3287  P    DT C  10    10654   7952  11681   1079   -323  -1162       P  
ATOM   3288  OP1  DT C  10     -21.112 -38.927  10.385  1.00 82.34           O  
ANISOU 3288  OP1  DT C  10    10997   8024  12264   1107   -480  -1442       O  
ATOM   3289  OP2  DT C  10     -19.763 -37.186  11.705  1.00 78.77           O  
ANISOU 3289  OP2  DT C  10    10472   8234  11222   1196   -131  -1343       O  
ATOM   3290  O5'  DT C  10     -21.852 -38.180  12.648  1.00 75.89           O  
ANISOU 3290  O5'  DT C  10    10263   7558  11011    827   -268   -727       O  
TER    3291       DT C  10                                                      
HETATM 3292 ZN    ZN A 401     -14.304  -6.045 -13.171  1.00 56.32          ZN  
HETATM 3293 AS   CAC A 402     -16.043  -8.829 -12.045  0.80 64.03          AS  
HETATM 3294  O1  CAC A 402     -14.959  -7.537 -11.620  0.80 65.15           O  
HETATM 3295  O2  CAC A 402     -17.469  -8.206 -12.827  0.80 65.12           O  
HETATM 3296  C1  CAC A 402     -16.594  -9.736 -10.407  0.80 64.37           C  
HETATM 3297  C2  CAC A 402     -15.158 -10.109 -13.242  0.80 64.38           C  
HETATM 3298 ZN    ZN B 401     -14.053 -38.328  26.105  1.00 52.58          ZN  
HETATM 3299 AS   CAC B 402     -13.347 -35.624  24.079  0.80 66.24          AS  
HETATM 3300  O1  CAC B 402     -14.014 -36.300  25.535  0.80 67.34           O  
HETATM 3301  O2  CAC B 402     -11.653 -35.992  23.939  0.80 65.50           O  
HETATM 3302  C1  CAC B 402     -14.292 -36.375  22.532  0.80 66.30           C  
HETATM 3303  C2  CAC B 402     -13.575 -33.685  24.092  0.80 65.81           C  
HETATM 3304  O   HOH A 501     -11.711  -9.985  -5.986  1.00 44.58           O  
HETATM 3305  O   HOH A 502     -27.422 -14.470 -14.717  1.00 52.34           O  
HETATM 3306  O   HOH A 503     -23.930 -16.800 -12.842  1.00 35.50           O  
HETATM 3307  O   HOH A 504     -21.665   3.378   2.487  1.00 58.85           O  
HETATM 3308  O   HOH A 505     -35.649   2.415  -3.829  1.00 45.63           O  
HETATM 3309  O   HOH A 506     -38.085  -5.409 -11.550  1.00 57.91           O  
HETATM 3310  O   HOH A 507     -27.541  -5.461   4.800  1.00 52.19           O  
HETATM 3311  O   HOH A 508     -24.472 -24.508  -0.903  1.00 57.69           O  
HETATM 3312  O   HOH A 509     -15.123 -16.973  -2.860  1.00 38.60           O  
HETATM 3313  O   HOH A 510     -22.812 -14.747  -9.499  1.00 28.39           O  
HETATM 3314  O   HOH A 511      -0.876 -14.483  -7.187  1.00 57.46           O  
HETATM 3315  O   HOH A 512     -17.116 -22.755 -13.303  1.00 53.61           O  
HETATM 3316  O   HOH A 513     -20.824 -15.006   2.163  1.00 33.93           O  
HETATM 3317  O   HOH A 514     -16.388   5.052   0.786  1.00 57.53           O  
HETATM 3318  O   HOH A 515     -26.847   2.711   1.174  1.00 51.52           O  
HETATM 3319  O   HOH A 516     -31.574 -11.906 -13.324  1.00 50.06           O  
HETATM 3320  O   HOH A 517     -27.662 -21.000  -2.267  1.00 45.96           O  
HETATM 3321  O   HOH A 518     -33.799  -7.417   6.830  1.00 46.56           O  
HETATM 3322  O   HOH A 519     -31.442 -24.810   4.297  1.00 57.57           O  
HETATM 3323  O   HOH A 520     -41.423 -14.968  -8.065  1.00 38.99           O  
HETATM 3324  O   HOH A 521      -9.399  -7.094  -7.311  1.00 51.48           O  
HETATM 3325  O   HOH A 522     -16.808  -9.047   6.596  1.00 43.01           O  
HETATM 3326  O   HOH A 523     -31.986 -21.367  -0.163  1.00 46.86           O  
HETATM 3327  O   HOH A 524     -37.180  -1.031 -13.076  1.00 59.78           O  
HETATM 3328  O   HOH A 525     -31.560 -22.031  -7.584  1.00 39.42           O  
HETATM 3329  O   HOH A 526     -25.379  -2.255 -17.867  1.00 59.79           O  
HETATM 3330  O   HOH A 527     -29.519 -25.908   2.014  1.00 48.53           O  
HETATM 3331  O   HOH A 528     -31.436  15.080   2.248  1.00 60.34           O  
HETATM 3332  O   HOH A 529     -24.119 -15.297   8.794  1.00 46.64           O  
HETATM 3333  O   HOH A 530     -21.641  -8.974   7.271  1.00 57.25           O  
HETATM 3334  O   HOH A 531     -32.193 -18.490  -0.893  1.00 49.44           O  
HETATM 3335  O   HOH A 532     -33.776 -13.657 -12.564  1.00 34.02           O  
HETATM 3336  O   HOH A 533     -45.665 -18.670   3.646  1.00 57.11           O  
HETATM 3337  O   HOH A 534     -24.663   1.740 -17.271  1.00 50.21           O  
HETATM 3338  O   HOH A 535     -30.997  -5.808 -13.724  1.00 49.50           O  
HETATM 3339  O   HOH A 536     -34.854 -17.907   0.159  1.00 40.52           O  
HETATM 3340  O   HOH A 537     -13.927 -15.949  10.638  1.00 56.64           O  
HETATM 3341  O   HOH A 538     -37.389 -12.707   5.040  1.00 54.02           O  
HETATM 3342  O   HOH A 539      -5.629 -19.198 -10.497  1.00 40.65           O  
HETATM 3343  O   HOH A 540     -42.553 -10.883  -5.683  1.00 43.72           O  
HETATM 3344  O   HOH A 541     -39.887 -11.618   2.456  1.00 56.38           O  
HETATM 3345  O   HOH A 542     -26.482 -25.847   0.796  1.00 53.37           O  
HETATM 3346  O   HOH A 543     -14.429   6.984  -0.284  1.00 55.16           O  
HETATM 3347  O   HOH A 544     -26.983  -4.303 -15.997  1.00 41.79           O  
HETATM 3348  O   HOH A 545     -27.133 -22.519  -5.026  1.00 47.39           O  
HETATM 3349  O   HOH A 546     -25.573 -11.719   9.775  1.00 52.59           O  
HETATM 3350  O   HOH A 547     -16.829 -24.703  -3.009  1.00 51.56           O  
HETATM 3351  O   HOH A 548     -34.164 -18.435   8.820  1.00 61.04           O  
HETATM 3352  O   HOH A 549     -28.993 -23.092  -7.126  1.00 47.20           O  
HETATM 3353  O   HOH A 550     -22.022 -27.617   6.351  1.00 49.26           O  
HETATM 3354  O   HOH A 551     -36.197 -20.123  -1.182  1.00 47.75           O  
HETATM 3355  O   HOH A 552     -34.634 -22.626  -0.756  1.00 51.91           O  
HETATM 3356  O   HOH A 553     -41.399 -17.796  -7.336  1.00 54.51           O  
HETATM 3357  O   HOH A 554     -24.339 -25.522 -12.733  1.00 52.72           O  
HETATM 3358  O   HOH A 555     -34.007 -22.687  -6.153  1.00 53.26           O  
HETATM 3359  O   HOH A 556     -29.434 -29.025   2.842  1.00 53.67           O  
HETATM 3360  O   HOH B 501       6.881 -26.518  15.159  1.00 45.23           O  
HETATM 3361  O   HOH B 502     -19.097 -31.064  26.879  1.00 46.99           O  
HETATM 3362  O   HOH B 503      -9.119 -31.502  10.145  1.00 48.30           O  
HETATM 3363  O   HOH B 504     -11.821 -35.405  19.825  1.00 69.00           O  
HETATM 3364  O   HOH B 505     -12.710 -33.006   8.171  1.00 44.86           O  
HETATM 3365  O   HOH B 506     -12.758  -9.500  17.199  1.00 61.21           O  
HETATM 3366  O   HOH B 507     -14.034 -21.043  12.699  1.00 45.82           O  
HETATM 3367  O   HOH B 508      -8.550 -31.451  14.846  1.00 39.87           O  
HETATM 3368  O   HOH B 509     -10.915 -29.597  41.748  1.00 56.43           O  
HETATM 3369  O   HOH B 510     -11.572 -31.979  27.289  1.00 55.68           O  
HETATM 3370  O   HOH B 511      -6.328 -25.794  39.760  1.00 54.57           O  
HETATM 3371  O   HOH B 512      -1.995 -22.187  34.411  1.00 54.82           O  
HETATM 3372  O   HOH B 513     -18.917 -24.733  21.414  1.00 42.74           O  
HETATM 3373  O   HOH B 514     -13.576 -19.294  24.119  1.00 38.22           O  
HETATM 3374  O   HOH B 515     -16.458 -31.990  11.240  1.00 47.43           O  
HETATM 3375  O   HOH B 516     -15.430 -24.654  10.868  1.00 40.27           O  
HETATM 3376  O   HOH B 517       7.237 -22.402  14.623  1.00 48.33           O  
HETATM 3377  O   HOH B 518       5.468 -29.337  16.814  1.00 51.68           O  
HETATM 3378  O   HOH B 519     -16.608 -22.356  12.243  1.00 42.06           O  
HETATM 3379  O   HOH B 520      -1.062 -19.418  13.377  1.00 56.40           O  
HETATM 3380  O   HOH B 521     -17.798 -26.264   6.429  1.00 60.85           O  
HETATM 3381  O   HOH B 522      -8.644 -19.194  15.071  1.00 51.10           O  
HETATM 3382  O   HOH B 523       1.521 -34.052  22.580  1.00 60.15           O  
HETATM 3383  O   HOH B 524      -4.565 -22.409  11.187  1.00 38.45           O  
HETATM 3384  O   HOH B 525      -9.722 -29.410  18.504  1.00 32.98           O  
HETATM 3385  O   HOH B 526     -19.723 -34.083  29.228  1.00 52.11           O  
HETATM 3386  O   HOH B 527      -3.756 -17.729  16.931  1.00 46.72           O  
HETATM 3387  O   HOH B 528     -11.606 -12.729  26.542  1.00 51.66           O  
HETATM 3388  O   HOH B 529      -1.313 -16.109  17.045  1.00 45.28           O  
HETATM 3389  O   HOH B 530     -26.513 -33.528  18.384  1.00 51.43           O  
HETATM 3390  O   HOH B 531       0.626 -32.158  20.450  1.00 57.66           O  
HETATM 3391  O   HOH B 532      -9.263 -38.389  17.587  1.00 50.82           O  
HETATM 3392  O   HOH B 533       1.151 -29.358  15.793  1.00 47.61           O  
HETATM 3393  O   HOH B 534     -13.106 -26.928   8.512  1.00 49.69           O  
HETATM 3394  O   HOH B 535      -0.717 -37.324  23.570  1.00 46.57           O  
HETATM 3395  O   HOH B 536       7.070 -29.920  45.495  1.00 64.82           O  
HETATM 3396  O   HOH B 537      -1.758 -25.305  37.498  1.00 49.43           O  
HETATM 3397  O   HOH B 538     -21.421 -13.953  29.127  1.00 55.13           O  
HETATM 3398  O   HOH B 539     -13.410 -17.519  13.774  1.00 57.11           O  
HETATM 3399  O   HOH B 540       4.712 -18.304  14.552  1.00 48.14           O  
HETATM 3400  O   HOH B 541       9.348 -21.516  18.954  1.00 46.42           O  
HETATM 3401  O   HOH B 542     -15.430 -30.202  14.439  1.00 37.13           O  
HETATM 3402  O   HOH B 543     -15.672 -32.786  15.998  1.00 52.72           O  
HETATM 3403  O   HOH B 544     -14.853 -10.093  19.601  1.00 48.99           O  
HETATM 3404  O   HOH B 545     -11.922 -10.235  19.971  1.00 66.49           O  
HETATM 3405  O   HOH B 546      -7.364 -22.056  10.853  1.00 49.15           O  
HETATM 3406  O   HOH B 547      -2.821 -19.853  11.012  1.00 55.52           O  
HETATM 3407  O   HOH B 548     -15.644 -24.873   7.923  1.00 47.59           O  
HETATM 3408  O   HOH C 201     -49.095 -25.483  10.602  1.00 40.87           O  
HETATM 3409  O   HOH C 202     -31.061 -24.186  14.417  1.00 59.88           O  
HETATM 3410  O   HOH C 203     -24.010 -27.001   8.225  1.00 40.73           O  
HETATM 3411  O   HOH C 204     -26.979 -27.131  11.531  1.00 53.09           O  
HETATM 3412  O   HOH C 205     -27.345 -25.945   8.905  1.00 46.20           O  
HETATM 3413  O   HOH C 206     -41.954 -19.692  13.199  1.00 55.95           O  
HETATM 3414  O   HOH C 207     -20.633 -30.911  10.876  1.00 52.44           O  
HETATM 3415  O   HOH C 208     -28.841 -33.042  14.433  1.00 53.65           O  
HETATM 3416  O   HOH C 209     -41.554 -20.144   6.343  1.00 55.27           O  
HETATM 3417  O   HOH C 210     -29.124 -29.063  11.576  1.00 70.92           O  
HETATM 3418  O   HOH C 211     -44.014 -18.569   6.074  1.00 46.98           O  
CONECT  504 3292                                                                
CONECT  769 3292                                                                
CONECT  791 3292                                                                
CONECT 2050 2091                                                                
CONECT 2057 3298                                                                
CONECT 2091 2050                                                                
CONECT 2322 3298                                                                
CONECT 2344 3298                                                                
CONECT 3292  504  769  791 3294                                                 
CONECT 3293 3294 3295 3296 3297                                                 
CONECT 3294 3292 3293                                                           
CONECT 3295 3293                                                                
CONECT 3296 3293                                                                
CONECT 3297 3293                                                                
CONECT 3298 2057 2322 2344 3300                                                 
CONECT 3299 3300 3301 3302 3303                                                 
CONECT 3300 3298 3299                                                           
CONECT 3301 3299                                                                
CONECT 3302 3299                                                                
CONECT 3303 3299                                                                
MASTER      397    0    4   12   12    0    8    6 3415    3   20   35          
END

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Related entries of code: 5zva

Entries with 90% protein sequence similarity cutoff in PDBbind
PDB Code	Check Database	Protein Sequence Similarity
5w2m	RCSB PDB PDBbind	184aa, >5W2M_1\|Chains... at 90%
5zvb	RCSB PDB PDBbind	209aa, >5ZVB_1\|Chains... at 100%
Complexes with the same small molecule ligand
PDB Code	Check Database	Ligand Name
3d2w	RCSB PDB PDBbind	10-mer
3glf	RCSB PDB PDBbind	10-mer
3i5x	RCSB PDB PDBbind	10-mer
3k49	RCSB PDB PDBbind	10-mer
3k4e	RCSB PDB PDBbind	10-mer
3kde	RCSB PDB PDBbind	10-mer
3kjo	RCSB PDB PDBbind	10-mer
5ho4	RCSB PDB PDBbind	10-mer
6kbs	RCSB PDB PDBbind	10-mer
6iir	RCSB PDB PDBbind	10-mer
5zc9	RCSB PDB PDBbind	10-mer

Entry Information

PDB ID	5zva
Complex Type	Protein-Nucleic Acid
PDBbind Subset	general set
Protein Name	APOBEC3F Chimeric Catalytic Domain (A3Fc-D2)
Ligand Name	10-mer
EC.Number	E.C.3.5.4.38
Resolution	2.3(Å)
Affinity (Kd/Ki/IC50)	Kd=54.86uM
Release Year	2018
Protein/NA Sequence	Check fasta file
Primary Reference	(2018) Chin.J.Chem. Vol. 36: pp. 1241-1248

Links to External Databases

RCSB PDB	The mother database
PDBsum	Enhanced annotations on PDB entries
Pubchem	Comprehensive collection of chemical and biological data
UniProtKB AC	UniProt accession number (AC): Q9HC16
Entrez Gene ID	NCBI Entrez Gene ID: 60489
ASD	Information of known allosteric effects of PDB entries

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