HEADER    STRUCTURAL PROTEIN                      02-JUL-21   7F8X              
TITLE     CRYSTAL STRUCTURE OF THE CHOLECYSTOKININ RECEPTOR CCKAR IN COMPLEX    
TITLE    2 WITH NN9056                                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CHOLECYSTOKININ RECEPTOR TYPE A,ENDOLYSIN;                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: CCK-A RECEPTOR,CCK-AR,CHOLECYSTOKININ-1 RECEPTOR,CCK1-R,    
COMPND   5 LYSIS PROTEIN,LYSOZYME,MURAMIDASE;                                   
COMPND   6 EC: 3.2.1.17;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES;                                                       
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: ASP-SMF-NLE-GLY-TRP-NLE-OEM-MEA-NH2 (NN9056);              
COMPND  11 CHAIN: C;                                                            
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ESCHERICHIA VIRUS T4;             
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606, 10665;                                         
SOURCE   5 GENE: CCKAR, CCKRA;                                                  
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 SYNTHETIC: YES;                                                      
SOURCE  10 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE  11 ORGANISM_TAXID: 32630                                                
KEYWDS    G PROTEIN-COULPED RECEPTOR, STRUCTURAL PROTEIN                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    X.ZHANG,C.HE,M.WANG,Q.ZHOU,D.YANG,Y.ZHU,B.WU,Q.ZHAO                   
REVDAT   1   29-DEC-21 7F8X    0                                                
JRNL        AUTH   X.ZHANG,C.HE,M.WANG,Q.ZHOU,D.YANG,Y.ZHU,W.FENG,H.ZHANG,      
JRNL        AUTH 2 A.DAI,X.CHU,J.WANG,Z.YANG,Y.JIANG,U.SENSFUSS,Q.TAN,S.HAN,    
JRNL        AUTH 3 S.REEDTZ-RUNGE,H.E.XU,S.ZHAO,M.W.WANG,B.WU,Q.ZHAO            
JRNL        TITL   STRUCTURES OF THE HUMAN CHOLECYSTOKININ RECEPTORS BOUND TO   
JRNL        TITL 2 AGONISTS AND ANTAGONISTS.                                    
JRNL        REF    NAT.CHEM.BIOL.                V.  17  1230 2021              
JRNL        REFN                   ESSN 1552-4469                               
JRNL        PMID   34556863                                                     
JRNL        DOI    10.1038/S41589-021-00866-8                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.19.2_4158                                   
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 : GEOSTD + MONOMER LIBRARY + CDL V1.2           
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.54                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 26392                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.240                           
REMARK   3   R VALUE            (WORKING SET) : 0.238                           
REMARK   3   FREE R VALUE                     : 0.261                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2636                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1  3.1070 -  3.0000    0.00        0  1374  0.3820 0.3140        
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)     : NULL             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL             
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 92.57                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 117.8                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.002           3674                                  
REMARK   3   ANGLE     :  0.606           4986                                  
REMARK   3   CHIRALITY :  0.042            583                                  
REMARK   3   PLANARITY :  0.005            610                                  
REMARK   3   DIHEDRAL  : 13.399           1321                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ALL                                                    
REMARK   3    ORIGIN FOR THE GROUP (A):   7.5318 -18.3596  15.4762              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1086 T22:   0.6206                                     
REMARK   3      T33:   0.5105 T12:  -0.1355                                     
REMARK   3      T13:  -0.0370 T23:  -0.0390                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9460 L22:   1.6508                                     
REMARK   3      L33:   6.0810 L12:  -0.1517                                     
REMARK   3      L13:  -0.7664 L23:  -1.0218                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0988 S12:  -0.1112 S13:  -0.0230                       
REMARK   3      S21:   0.0441 S22:  -0.0391 S23:  -0.0463                       
REMARK   3      S31:  -0.1332 S32:   0.1285 S33:   0.1602                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 7F8X COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-JUL-21.                  
REMARK 100 THE DEPOSITION ID IS D_1300022811.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-JUL-18                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL41XU                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS VERSION JAN 26, 2018           
REMARK 200  DATA SCALING SOFTWARE          : XSCALE VERSION JAN 26, 2018        
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 26470                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.1                               
REMARK 200  DATA REDUNDANCY                : 4.400                              
REMARK 200  R MERGE                    (I) : 0.20600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 4.4500                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.08                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.57300                            
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: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER 1.19.2                                         
REMARK 200 STARTING MODEL: 5ZBQ                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.70                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.98                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM HEPES,7.5, 10 (V/V) PPG400 AND    
REMARK 280  100 MM AMMONIUM ACETATE, LIPIDIC CUBIC PHASE, TEMPERATURE 293K      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       36.25000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2020 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23360 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 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 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     ASP A    -8                                                      
REMARK 465     TYR A    -7                                                      
REMARK 465     LYS A    -6                                                      
REMARK 465     ASP A    -5                                                      
REMARK 465     ASP A    -4                                                      
REMARK 465     ASP A    -3                                                      
REMARK 465     ASP A    -2                                                      
REMARK 465     GLY A    -1                                                      
REMARK 465     ALA A     0                                                      
REMARK 465     PRO A     1                                                      
REMARK 465     ASP A     2                                                      
REMARK 465     VAL A     3                                                      
REMARK 465     VAL A     4                                                      
REMARK 465     ASP A     5                                                      
REMARK 465     SER A     6                                                      
REMARK 465     LEU A     7                                                      
REMARK 465     LEU A     8                                                      
REMARK 465     VAL A     9                                                      
REMARK 465     ASN A    10                                                      
REMARK 465     GLY A    11                                                      
REMARK 465     SER A    12                                                      
REMARK 465     ASN A    13                                                      
REMARK 465     ILE A    14                                                      
REMARK 465     THR A    15                                                      
REMARK 465     PRO A    16                                                      
REMARK 465     PRO A    17                                                      
REMARK 465     CYS A    18                                                      
REMARK 465     GLU A    19                                                      
REMARK 465     LEU A    20                                                      
REMARK 465     GLY A    21                                                      
REMARK 465     LEU A    22                                                      
REMARK 465     GLU A    23                                                      
REMARK 465     ASN A    24                                                      
REMARK 465     GLU A    25                                                      
REMARK 465     THR A    26                                                      
REMARK 465     LEU A    27                                                      
REMARK 465     PHE A    28                                                      
REMARK 465     CYS A    29                                                      
REMARK 465     LEU A    30                                                      
REMARK 465     ASP A    31                                                      
REMARK 465     GLN A    32                                                      
REMARK 465     PRO A    33                                                      
REMARK 465     ARG A    34                                                      
REMARK 465     PRO A    35                                                      
REMARK 465     SER A    36                                                      
REMARK 465     PHE A   615                                                      
REMARK 465     MET A   616                                                      
REMARK 465     ALA A   617                                                      
REMARK 465     THR A   618                                                      
REMARK 465     PHE A   619                                                      
REMARK 465     PRO A   620                                                      
REMARK 465     CYS A   621                                                      
REMARK 465     CYS A   622                                                      
REMARK 465     PRO A   623                                                      
REMARK 465     ASN A   624                                                      
REMARK 465     PRO A   625                                                      
REMARK 465     GLY A   626                                                      
REMARK 465     PRO A   627                                                      
REMARK 465     PRO A   628                                                      
REMARK 465     GLY A   629                                                      
REMARK 465     ALA A   630                                                      
REMARK 465     ARG A   631                                                      
REMARK 465     GLY A   632                                                      
REMARK 465     GLU A   633                                                      
REMARK 465     VAL A   634                                                      
REMARK 465     GLY A   635                                                      
REMARK 465     GLU A   636                                                      
REMARK 465     GLU A   637                                                      
REMARK 465     GLU A   638                                                      
REMARK 465     GLU A   639                                                      
REMARK 465     GLY A   640                                                      
REMARK 465     GLU A   641                                                      
REMARK 465     PHE A   642                                                      
REMARK 465     LEU A   643                                                      
REMARK 465     GLU A   644                                                      
REMARK 465     VAL A   645                                                      
REMARK 465     LEU A   646                                                      
REMARK 465     PHE A   647                                                      
REMARK 465     GLN A   648                                                      
REMARK 465     GLY A   649                                                      
REMARK 465     PRO A   650                                                      
REMARK 465     HIS A   651                                                      
REMARK 465     HIS A   652                                                      
REMARK 465     HIS A   653                                                      
REMARK 465     HIS A   654                                                      
REMARK 465     HIS A   655                                                      
REMARK 465     HIS A   656                                                      
REMARK 465     HIS A   657                                                      
REMARK 465     HIS A   658                                                      
REMARK 465     HIS A   659                                                      
REMARK 465     HIS A   660                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A 250    CD   OE1  OE2                                       
REMARK 470     LYS A 255    CD   CE   NZ                                        
REMARK 470     LYS A 274    CD   CE   NZ                                        
REMARK 470     ASN A 279    CG   OD1  ND2                                       
REMARK 470     LYS A 355    CG   CD   CE   NZ                                   
REMARK 470     LYS A 439    CG   CD   CE   NZ                                   
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    CYS A  94      -37.99   -136.30                                   
REMARK 500    PHE A  97       11.24    -65.21                                   
REMARK 500    LYS A 187      -79.08    -98.96                                   
REMARK 500    PHE A 218      -48.81   -141.55                                   
REMARK 500    ILE A 268       70.21   -109.64                                   
REMARK 500    VAL A 431       74.77   -113.58                                   
REMARK 500    LYS A 498        5.40     57.96                                   
REMARK 500    SER A 582      -21.28   -155.41                                   
REMARK 500    NLE C   3      117.19     25.63                                   
REMARK 500    OEM C   7      109.65    -58.49                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  7F8X A    2   240  UNP    P32238   CCKAR_HUMAN      2    240             
DBREF  7F8X A  241   535  UNP    P00720   ENLYS_BPT4       2    161             
DBREF  7F8X A  536   640  UNP    P32238   CCKAR_HUMAN    302    406             
DBREF  7F8X C    1     9  PDB    7F8X     7F8X             1      9             
SEQADV 7F8X ASP A   -8  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8X TYR A   -7  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8X LYS A   -6  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8X ASP A   -5  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8X ASP A   -4  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8X ASP A   -3  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8X ASP A   -2  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8X GLY A   -1  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8X ALA A    0  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8X PRO A    1  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8X TRP A  130  UNP  P32238    PHE   130 ENGINEERED MUTATION            
SEQADV 7F8X GLY A  251  UNP  P00720    ARG    12 ENGINEERED MUTATION            
SEQADV 7F8X THR A  428  UNP  P00720    CYS    54 ENGINEERED MUTATION            
SEQADV 7F8X ALA A  471  UNP  P00720    CYS    97 ENGINEERED MUTATION            
SEQADV 7F8X ARG A  511  UNP  P00720    ILE   137 ENGINEERED MUTATION            
SEQADV 7F8X GLU A  641  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8X PHE A  642  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8X LEU A  643  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8X GLU A  644  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8X VAL A  645  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8X LEU A  646  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8X PHE A  647  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8X GLN A  648  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8X GLY A  649  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8X PRO A  650  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8X HIS A  651  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8X HIS A  652  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8X HIS A  653  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8X HIS A  654  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8X HIS A  655  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8X HIS A  656  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8X HIS A  657  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8X HIS A  658  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8X HIS A  659  UNP  P32238              EXPRESSION TAG                 
SEQADV 7F8X HIS A  660  UNP  P32238              EXPRESSION TAG                 
SEQRES   1 A  534  ASP TYR LYS ASP ASP ASP ASP GLY ALA PRO ASP VAL VAL          
SEQRES   2 A  534  ASP SER LEU LEU VAL ASN GLY SER ASN ILE THR PRO PRO          
SEQRES   3 A  534  CYS GLU LEU GLY LEU GLU ASN GLU THR LEU PHE CYS LEU          
SEQRES   4 A  534  ASP GLN PRO ARG PRO SER LYS GLU TRP GLN PRO ALA VAL          
SEQRES   5 A  534  GLN ILE LEU LEU TYR SER LEU ILE PHE LEU LEU SER VAL          
SEQRES   6 A  534  LEU GLY ASN THR LEU VAL ILE THR VAL LEU ILE ARG ASN          
SEQRES   7 A  534  LYS ARG MET ARG THR VAL THR ASN ILE PHE LEU LEU SER          
SEQRES   8 A  534  LEU ALA VAL SER ASP LEU MET LEU CYS LEU PHE CYS MET          
SEQRES   9 A  534  PRO PHE ASN LEU ILE PRO ASN LEU LEU LYS ASP PHE ILE          
SEQRES  10 A  534  PHE GLY SER ALA VAL CYS LYS THR THR THR TYR PHE MET          
SEQRES  11 A  534  GLY THR SER VAL SER VAL SER THR TRP ASN LEU VAL ALA          
SEQRES  12 A  534  ILE SER LEU GLU ARG TYR GLY ALA ILE CYS LYS PRO LEU          
SEQRES  13 A  534  GLN SER ARG VAL TRP GLN THR LYS SER HIS ALA LEU LYS          
SEQRES  14 A  534  VAL ILE ALA ALA THR TRP CYS LEU SER PHE THR ILE MET          
SEQRES  15 A  534  THR PRO TYR PRO ILE TYR SER ASN LEU VAL PRO PHE THR          
SEQRES  16 A  534  LYS ASN ASN ASN GLN THR ALA ASN MET CYS ARG PHE LEU          
SEQRES  17 A  534  LEU PRO ASN ASP VAL MET GLN GLN SER TRP HIS THR PHE          
SEQRES  18 A  534  LEU LEU LEU ILE LEU PHE LEU ILE PRO GLY ILE VAL MET          
SEQRES  19 A  534  MET VAL ALA TYR GLY LEU ILE SER LEU GLU LEU TYR GLN          
SEQRES  20 A  534  GLY ILE ASN ILE PHE GLU MET LEU ARG ILE ASP GLU GLY          
SEQRES  21 A  534  LEU ARG LEU LYS ILE TYR LYS ASP THR GLU GLY TYR TYR          
SEQRES  22 A  534  THR ILE GLY ILE GLY HIS LEU LEU THR LYS SER PRO SER          
SEQRES  23 A  534  LEU ASN ALA ALA LYS SER GLU LEU ASP LYS ALA ILE GLY          
SEQRES  24 A  534  ARG ASN THR ASN GLY VAL ILE THR LYS ASP GLU ALA GLU          
SEQRES  25 A  534  LYS LEU PHE ASN GLN ASP VAL ASP ALA ALA VAL ARG GLY          
SEQRES  26 A  534  ILE LEU ARG ASN ALA LYS LEU LYS PRO VAL TYR ASP SER          
SEQRES  27 A  534  LEU ASP ALA VAL ARG ARG ALA ALA LEU ILE ASN MET VAL          
SEQRES  28 A  534  PHE GLN MET GLY GLU THR GLY VAL ALA GLY PHE THR ASN          
SEQRES  29 A  534  SER LEU ARG MET LEU GLN GLN LYS ARG TRP ASP GLU ALA          
SEQRES  30 A  534  ALA VAL ASN LEU ALA LYS SER ARG TRP TYR ASN GLN THR          
SEQRES  31 A  534  PRO ASN ARG ALA LYS ARG VAL ILE THR THR PHE ARG THR          
SEQRES  32 A  534  GLY THR TRP ASP ALA TYR ALA ALA ASN LEU MET ALA LYS          
SEQRES  33 A  534  LYS ARG VAL ILE ARG MET LEU ILE VAL ILE VAL VAL LEU          
SEQRES  34 A  534  PHE PHE LEU CYS TRP MET PRO ILE PHE SER ALA ASN ALA          
SEQRES  35 A  534  TRP ARG ALA TYR ASP THR ALA SER ALA GLU ARG ARG LEU          
SEQRES  36 A  534  SER GLY THR PRO ILE SER PHE ILE LEU LEU LEU SER TYR          
SEQRES  37 A  534  THR SER SER CYS VAL ASN PRO ILE ILE TYR CYS PHE MET          
SEQRES  38 A  534  ASN LYS ARG PHE ARG LEU GLY PHE MET ALA THR PHE PRO          
SEQRES  39 A  534  CYS CYS PRO ASN PRO GLY PRO PRO GLY ALA ARG GLY GLU          
SEQRES  40 A  534  VAL GLY GLU GLU GLU GLU GLY GLU PHE LEU GLU VAL LEU          
SEQRES  41 A  534  PHE GLN GLY PRO HIS HIS HIS HIS HIS HIS HIS HIS HIS          
SEQRES  42 A  534  HIS                                                          
SEQRES   1 C    9  ASP SMF NLE GLY TRP NLE OEM MEA NH2                          
HET    SMF  C   2      16                                                       
HET    NLE  C   3       8                                                       
HET    NLE  C   6       8                                                       
HET    OEM  C   7       9                                                       
HET    MEA  C   8      12                                                       
HET    NH2  C   9       1                                                       
HETNAM     SMF 4-SULFOMETHYL-L-PHENYLALANINE                                    
HETNAM     NLE NORLEUCINE                                                       
HETNAM     OEM N-METHYL-D-ASPARTIC ACID                                         
HETNAM     MEA N-METHYLPHENYLALANINE                                            
HETNAM     NH2 AMINO GROUP                                                      
FORMUL   2  SMF    C10 H13 N O5 S                                               
FORMUL   2  NLE    2(C6 H13 N O2)                                               
FORMUL   2  OEM    C5 H9 N O4                                                   
FORMUL   2  MEA    C10 H13 N O2                                                 
FORMUL   2  NH2    H2 N                                                         
HELIX    1 AA1 GLU A   38  ASN A   69  1                                  32    
HELIX    2 AA2 THR A   74  PHE A   93  1                                  20    
HELIX    3 AA3 MET A   95  LYS A  105  1                                  11    
HELIX    4 AA4 GLY A  110  CYS A  144  1                                  35    
HELIX    5 AA5 THR A  154  MET A  173  1                                  20    
HELIX    6 AA6 THR A  174  TYR A  179  1                                   6    
HELIX    7 AA7 ASN A  202  PHE A  218  1                                  17    
HELIX    8 AA8 PHE A  218  GLN A  238  1                                  21    
HELIX    9 AA9 ASN A  241  GLY A  251  1                                  11    
HELIX   10 AB1 SER A  277  ILE A  424  1                                  13    
HELIX   11 AB2 THR A  433  ASN A  455  1                                  23    
HELIX   12 AB3 LYS A  457  ASP A  463  1                                   7    
HELIX   13 AB4 ASP A  466  GLY A  481  1                                  16    
HELIX   14 AB5 GLY A  481  GLY A  487  1                                   7    
HELIX   15 AB6 PHE A  488  GLN A  497  1                                  10    
HELIX   16 AB7 ARG A  499  ALA A  508  1                                  10    
HELIX   17 AB8 SER A  510  THR A  516  1                                   7    
HELIX   18 AB9 THR A  516  GLY A  530  1                                  15    
HELIX   19 AC1 ALA A  537  ASP A  573  1                                  37    
HELIX   20 AC2 ASP A  573  LEU A  581  1                                   9    
HELIX   21 AC3 THR A  584  PHE A  606  1                                  23    
HELIX   22 AC4 MET A  607  ASN A  608  5                                   2    
HELIX   23 AC5 LYS A  609  LEU A  613  5                                   5    
SHEET    1 AA1 2 SER A 180  THR A 186  0                                        
SHEET    2 AA1 2 THR A 192  PHE A 198 -1  O  MET A 195   N  VAL A 183           
SHEET    1 AA2 3 ARG A 253  LYS A 258  0                                        
SHEET    2 AA2 3 TYR A 264  GLY A 267 -1  O  THR A 265   N  TYR A 257           
SHEET    3 AA2 3 HIS A 270  THR A 273 -1  O  LEU A 272   N  TYR A 264           
SSBOND   1 CYS A  114    CYS A  196                          1555   1555  2.03  
LINK         C   ASP C   1                 N   SMF C   2     1555   1555  1.33  
LINK         C   SMF C   2                 N   NLE C   3     1555   1555  1.34  
LINK         C   NLE C   3                 N   GLY C   4     1555   1555  1.33  
LINK         C   TRP C   5                 N   NLE C   6     1555   1555  1.33  
LINK         C   NLE C   6                 N   OEM C   7     1555   1555  1.33  
LINK         C   OEM C   7                 N   MEA C   8     1555   1555  1.34  
LINK         C   MEA C   8                 N   NH2 C   9     1555   1555  1.33  
CRYST1   56.600   72.500   87.000  90.00 100.00  90.00 P 1 21 1      2          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.017668  0.000000  0.003115        0.00000                         
SCALE2      0.000000  0.013793  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011672        0.00000                         
ATOM      1  N   LYS A  37     -13.064  -5.273 -21.841  1.00164.84           N  
ANISOU    1  N   LYS A  37    24268  25306  13058   2826  -2851   1571       N  
ATOM      2  CA  LYS A  37     -13.924  -4.117 -21.621  1.00169.01           C  
ANISOU    2  CA  LYS A  37    24691  26139  13387   3491  -2827   1822       C  
ATOM      3  C   LYS A  37     -13.285  -3.249 -20.530  1.00174.63           C  
ANISOU    3  C   LYS A  37    25738  26279  14336   3778  -2549   1833       C  
ATOM      4  O   LYS A  37     -12.159  -3.518 -20.117  1.00170.40           O  
ANISOU    4  O   LYS A  37    25499  25155  14090   3450  -2400   1658       O  
ATOM      5  CB  LYS A  37     -15.340  -4.571 -21.243  1.00169.89           C  
ANISOU    5  CB  LYS A  37    24137  27077  13337   3518  -3031   1923       C  
ATOM      6  CG  LYS A  37     -16.421  -3.513 -21.415  1.00168.06           C  
ANISOU    6  CG  LYS A  37    23713  27363  12778   4229  -3070   2219       C  
ATOM      7  CD  LYS A  37     -16.588  -3.127 -22.876  1.00157.40           C  
ANISOU    7  CD  LYS A  37    22469  26107  11227   4351  -3156   2306       C  
ATOM      8  CE  LYS A  37     -17.733  -2.146 -23.060  1.00155.53           C  
ANISOU    8  CE  LYS A  37    21955  26297  10844   4954  -3139   2558       C  
ATOM      9  NZ  LYS A  37     -17.438  -0.830 -22.430  1.00162.57           N  
ANISOU    9  NZ  LYS A  37    23240  26706  11823   5561  -2846   2669       N  
ATOM     10  N   GLU A  38     -13.988  -2.213 -20.065  1.00226.08           N  
ANISOU   10  N   GLU A  38    32220  32972  20708   4393  -2475   2041       N  
ATOM     11  CA  GLU A  38     -13.379  -1.250 -19.154  1.00225.52           C  
ANISOU   11  CA  GLU A  38    32570  32318  20799   4698  -2207   2061       C  
ATOM     12  C   GLU A  38     -13.255  -1.767 -17.726  1.00220.15           C  
ANISOU   12  C   GLU A  38    31699  31527  20422   4447  -2127   1931       C  
ATOM     13  O   GLU A  38     -12.486  -1.196 -16.943  1.00214.89           O  
ANISOU   13  O   GLU A  38    31418  30286  19945   4517  -1912   1881       O  
ATOM     14  CB  GLU A  38     -14.177   0.059 -19.142  1.00230.33           C  
ANISOU   14  CB  GLU A  38    33284  33114  21118   5486  -2132   2333       C  
ATOM     15  CG  GLU A  38     -15.250   0.140 -18.058  1.00234.49           C  
ANISOU   15  CG  GLU A  38    33371  34113  21612   5804  -2131   2444       C  
ATOM     16  CD  GLU A  38     -16.594  -0.401 -18.503  1.00237.95           C  
ANISOU   16  CD  GLU A  38    33100  35437  21873   5820  -2363   2553       C  
ATOM     17  OE1 GLU A  38     -16.655  -1.042 -19.570  1.00237.16           O  
ANISOU   17  OE1 GLU A  38    32842  35597  21671   5490  -2562   2510       O  
ATOM     18  OE2 GLU A  38     -17.590  -0.187 -17.781  1.00236.74           O  
ANISOU   18  OE2 GLU A  38    32548  35725  21678   6146  -2340   2679       O  
ATOM     19  N   TRP A  39     -13.981  -2.827 -17.364  1.00216.13           N  
ANISOU   19  N   TRP A  39    30622  31548  19949   4135  -2294   1876       N  
ATOM     20  CA  TRP A  39     -14.010  -3.247 -15.967  1.00215.26           C  
ANISOU   20  CA  TRP A  39    30311  31389  20089   3968  -2214   1785       C  
ATOM     21  C   TRP A  39     -12.735  -3.970 -15.548  1.00213.09           C  
ANISOU   21  C   TRP A  39    30282  30520  20163   3403  -2122   1535       C  
ATOM     22  O   TRP A  39     -12.345  -3.891 -14.378  1.00212.50           O  
ANISOU   22  O   TRP A  39    30291  30135  20313   3373  -1974   1466       O  
ATOM     23  CB  TRP A  39     -15.228  -4.135 -15.704  1.00220.71           C  
ANISOU   23  CB  TRP A  39    30316  32858  20685   3804  -2414   1823       C  
ATOM     24  CG  TRP A  39     -15.167  -5.478 -16.363  1.00226.48           C  
ANISOU   24  CG  TRP A  39    30818  33797  21438   3145  -2617   1665       C  
ATOM     25  CD1 TRP A  39     -15.412  -5.760 -17.675  1.00227.22           C  
ANISOU   25  CD1 TRP A  39    30853  34185  21296   3021  -2808   1689       C  
ATOM     26  CD2 TRP A  39     -14.847  -6.726 -15.737  1.00226.17           C  
ANISOU   26  CD2 TRP A  39    30621  33666  21647   2526  -2645   1457       C  
ATOM     27  NE1 TRP A  39     -15.262  -7.106 -17.906  1.00226.60           N  
ANISOU   27  NE1 TRP A  39    30616  34186  21297   2350  -2948   1500       N  
ATOM     28  CE2 TRP A  39     -14.916  -7.722 -16.731  1.00230.55           C  
ANISOU   28  CE2 TRP A  39    31061  34445  22093   2045  -2846   1359       C  
ATOM     29  CE3 TRP A  39     -14.509  -7.098 -14.432  1.00219.76           C  
ANISOU   29  CE3 TRP A  39    29783  32595  21121   2339  -2514   1347       C  
ATOM     30  CZ2 TRP A  39     -14.656  -9.064 -16.463  1.00234.41           C  
ANISOU   30  CZ2 TRP A  39    31446  34877  22744   1399  -2908   1157       C  
ATOM     31  CZ3 TRP A  39     -14.252  -8.431 -14.167  1.00222.39           C  
ANISOU   31  CZ3 TRP A  39    29982  32894  21622   1710  -2581   1156       C  
ATOM     32  CH2 TRP A  39     -14.327  -9.398 -15.178  1.00232.13           C  
ANISOU   32  CH2 TRP A  39    31136  34326  22736   1252  -2770   1064       C  
ATOM     33  N   GLN A  40     -12.072  -4.673 -16.473  1.00159.05           N  
ANISOU   33  N   GLN A  40    23559  23520  13351   2975  -2201   1403       N  
ATOM     34  CA  GLN A  40     -10.855  -5.393 -16.098  1.00150.88           C  
ANISOU   34  CA  GLN A  40    22740  21961  12627   2479  -2105   1183       C  
ATOM     35  C   GLN A  40      -9.698  -4.452 -15.787  1.00136.94           C  
ANISOU   35  C   GLN A  40    21507  19515  11008   2637  -1870   1169       C  
ATOM     36  O   GLN A  40      -9.016  -4.665 -14.769  1.00131.07           O  
ANISOU   36  O   GLN A  40    20845  18428  10528   2437  -1746   1055       O  
ATOM     37  CB  GLN A  40     -10.489  -6.409 -17.186  1.00154.51           C  
ANISOU   37  CB  GLN A  40    23204  22454  13049   2018  -2237   1056       C  
ATOM     38  CG  GLN A  40     -11.654  -7.257 -17.664  1.00161.97           C  
ANISOU   38  CG  GLN A  40    23676  24080  13784   1830  -2490   1078       C  
ATOM     39  CD  GLN A  40     -11.283  -8.160 -18.824  1.00160.40           C  
ANISOU   39  CD  GLN A  40    23576  23870  13500   1403  -2613    952       C  
ATOM     40  OE1 GLN A  40     -10.350  -7.875 -19.575  1.00157.72           O  
ANISOU   40  OE1 GLN A  40    23643  23116  13166   1409  -2524    915       O  
ATOM     41  NE2 GLN A  40     -12.014  -9.258 -18.975  1.00163.66           N  
ANISOU   41  NE2 GLN A  40    23632  24736  13814   1017  -2811    888       N  
ATOM     42  N   PRO A  41      -9.402  -3.423 -16.594  1.00141.08           N  
ANISOU   42  N   PRO A  41    22415  19819  11369   2958  -1799   1280       N  
ATOM     43  CA  PRO A  41      -8.316  -2.510 -16.200  1.00134.51           C  
ANISOU   43  CA  PRO A  41    22098  18342  10666   3054  -1571   1268       C  
ATOM     44  C   PRO A  41      -8.630  -1.710 -14.950  1.00131.89           C  
ANISOU   44  C   PRO A  41    21831  17905  10377   3395  -1442   1339       C  
ATOM     45  O   PRO A  41      -7.724  -1.439 -14.152  1.00124.66           O  
ANISOU   45  O   PRO A  41    21197  16507   9663   3263  -1282   1254       O  
ATOM     46  CB  PRO A  41      -8.162  -1.604 -17.430  1.00133.06           C  
ANISOU   46  CB  PRO A  41    22286  18034  10236   3343  -1544   1398       C  
ATOM     47  CG  PRO A  41      -8.670  -2.425 -18.558  1.00145.67           C  
ANISOU   47  CG  PRO A  41    23599  20077  11673   3177  -1754   1391       C  
ATOM     48  CD  PRO A  41      -9.838  -3.162 -17.977  1.00150.43           C  
ANISOU   48  CD  PRO A  41    23633  21269  12255   3145  -1920   1396       C  
ATOM     49  N   ALA A  42      -9.894  -1.323 -14.755  1.00128.17           N  
ANISOU   49  N   ALA A  42    21103  17894   9701   3837  -1505   1498       N  
ATOM     50  CA  ALA A  42     -10.244  -0.486 -13.612  1.00117.87           C  
ANISOU   50  CA  ALA A  42    19907  16487   8392   4235  -1362   1581       C  
ATOM     51  C   ALA A  42     -10.017  -1.218 -12.295  1.00116.59           C  
ANISOU   51  C   ALA A  42    19526  16257   8514   3903  -1327   1431       C  
ATOM     52  O   ALA A  42      -9.480  -0.642 -11.341  1.00115.63           O  
ANISOU   52  O   ALA A  42    19713  15709   8512   3969  -1158   1395       O  
ATOM     53  CB  ALA A  42     -11.696  -0.023 -13.725  1.00122.10           C  
ANISOU   53  CB  ALA A  42    20150  17615   8627   4804  -1437   1800       C  
ATOM     54  N   VAL A  43     -10.415  -2.490 -12.223  1.00102.06           N  
ANISOU   54  N   VAL A  43    17184  14824   6770   3527  -1486   1340       N  
ATOM     55  CA  VAL A  43     -10.231  -3.240 -10.986  1.00 99.43           C  
ANISOU   55  CA  VAL A  43    16646  14439   6694   3213  -1453   1206       C  
ATOM     56  C   VAL A  43      -8.765  -3.597 -10.783  1.00 95.49           C  
ANISOU   56  C   VAL A  43    16459  13360   6464   2768  -1357   1022       C  
ATOM     57  O   VAL A  43      -8.315  -3.775  -9.645  1.00 93.31           O  
ANISOU   57  O   VAL A  43    16210  12849   6394   2614  -1264    929       O  
ATOM     58  CB  VAL A  43     -11.126  -4.493 -10.974  1.00 99.98           C  
ANISOU   58  CB  VAL A  43    16120  15111   6758   2929  -1644   1174       C  
ATOM     59  CG1 VAL A  43     -12.589  -4.099 -11.116  1.00104.30           C  
ANISOU   59  CG1 VAL A  43    16302  16307   7022   3378  -1737   1380       C  
ATOM     60  CG2 VAL A  43     -10.715  -5.462 -12.073  1.00101.98           C  
ANISOU   60  CG2 VAL A  43    16326  15399   7022   2468  -1783   1062       C  
ATOM     61  N   GLN A  44      -7.991  -3.701 -11.866  1.00107.08           N  
ANISOU   61  N   GLN A  44    18154  14612   7921   2567  -1374    976       N  
ATOM     62  CA  GLN A  44      -6.570  -3.993 -11.718  1.00105.85           C  
ANISOU   62  CA  GLN A  44    18271  13950   7996   2181  -1271    826       C  
ATOM     63  C   GLN A  44      -5.812  -2.804 -11.144  1.00104.37           C  
ANISOU   63  C   GLN A  44    18550  13256   7848   2363  -1079    856       C  
ATOM     64  O   GLN A  44      -4.799  -2.989 -10.461  1.00 98.32           O  
ANISOU   64  O   GLN A  44    17922  12138   7296   2074   -983    743       O  
ATOM     65  CB  GLN A  44      -5.969  -4.407 -13.061  1.00111.15           C  
ANISOU   65  CB  GLN A  44    19058  14555   8619   1945  -1324    784       C  
ATOM     66  CG  GLN A  44      -6.110  -5.887 -13.376  1.00115.67           C  
ANISOU   66  CG  GLN A  44    19293  15402   9255   1534  -1467    662       C  
ATOM     67  CD  GLN A  44      -5.502  -6.258 -14.714  1.00124.35           C  
ANISOU   67  CD  GLN A  44    20557  16412  10280   1333  -1503    619       C  
ATOM     68  OE1 GLN A  44      -4.354  -6.698 -14.785  1.00122.68           O  
ANISOU   68  OE1 GLN A  44    20521  15865  10225   1040  -1413    509       O  
ATOM     69  NE2 GLN A  44      -6.269  -6.082 -15.784  1.00124.41           N  
ANISOU   69  NE2 GLN A  44    20501  16742  10028   1509  -1631    714       N  
ATOM     70  N   ILE A  45      -6.283  -1.585 -11.402  1.00102.28           N  
ANISOU   70  N   ILE A  45    18548  12952   7361   2834  -1020   1012       N  
ATOM     71  CA  ILE A  45      -5.600  -0.401 -10.894  1.00102.43           C  
ANISOU   71  CA  ILE A  45    19086  12457   7375   2991   -833   1041       C  
ATOM     72  C   ILE A  45      -5.881  -0.210  -9.409  1.00 99.00           C  
ANISOU   72  C   ILE A  45    18611  11974   7031   3102   -758   1019       C  
ATOM     73  O   ILE A  45      -4.966   0.044  -8.618  1.00 99.03           O  
ANISOU   73  O   ILE A  45    18882  11561   7183   2899   -642    931       O  
ATOM     74  CB  ILE A  45      -6.000   0.841 -11.711  1.00101.37           C  
ANISOU   74  CB  ILE A  45    19323  12250   6942   3474   -779   1220       C  
ATOM     75  CG1 ILE A  45      -5.535   0.696 -13.162  1.00 97.86           C  
ANISOU   75  CG1 ILE A  45    18984  11782   6416   3324   -832   1233       C  
ATOM     76  CG2 ILE A  45      -5.422   2.103 -11.087  1.00 98.51           C  
ANISOU   76  CG2 ILE A  45    19549  11342   6537   3645   -578   1254       C  
ATOM     77  CD1 ILE A  45      -6.231   1.633 -14.122  1.00101.68           C  
ANISOU   77  CD1 ILE A  45    19685  12375   6572   3824   -836   1426       C  
ATOM     78  N   LEU A  46      -7.148  -0.335  -9.003  1.00 96.87           N  
ANISOU   78  N   LEU A  46    17993  12155   6659   3417   -825   1102       N  
ATOM     79  CA  LEU A  46      -7.483  -0.093  -7.603  1.00 96.91           C  
ANISOU   79  CA  LEU A  46    17976  12127   6718   3576   -738   1095       C  
ATOM     80  C   LEU A  46      -7.017  -1.234  -6.708  1.00 93.47           C  
ANISOU   80  C   LEU A  46    17244  11699   6573   3093   -773    925       C  
ATOM     81  O   LEU A  46      -6.728  -1.009  -5.529  1.00 99.12           O  
ANISOU   81  O   LEU A  46    18089  12182   7390   3074   -672    870       O  
ATOM     82  CB  LEU A  46      -8.988   0.147  -7.450  1.00100.28           C  
ANISOU   82  CB  LEU A  46    18100  13074   6927   4093   -779   1259       C  
ATOM     83  CG  LEU A  46      -9.993  -1.001  -7.555  1.00100.60           C  
ANISOU   83  CG  LEU A  46    17459  13789   6975   3981   -961   1270       C  
ATOM     84  CD1 LEU A  46     -10.342  -1.535  -6.172  1.00 99.52           C  
ANISOU   84  CD1 LEU A  46    17028  13800   6986   3891   -933   1211       C  
ATOM     85  CD2 LEU A  46     -11.246  -0.550  -8.293  1.00105.53           C  
ANISOU   85  CD2 LEU A  46    17878  14934   7286   4489  -1037   1480       C  
ATOM     86  N   LEU A  47      -6.929  -2.456  -7.238  1.00 90.50           N  
ANISOU   86  N   LEU A  47    16506  11570   6311   2707   -911    840       N  
ATOM     87  CA  LEU A  47      -6.381  -3.558  -6.450  1.00 87.36           C  
ANISOU   87  CA  LEU A  47    15892  11126   6176   2253   -929    682       C  
ATOM     88  C   LEU A  47      -4.878  -3.400  -6.252  1.00 85.66           C  
ANISOU   88  C   LEU A  47    16040  10376   6130   1949   -822    573       C  
ATOM     89  O   LEU A  47      -4.371  -3.548  -5.134  1.00 88.40           O  
ANISOU   89  O   LEU A  47    16420  10529   6638   1786   -755    490       O  
ATOM     90  CB  LEU A  47      -6.695  -4.901  -7.111  1.00 86.70           C  
ANISOU   90  CB  LEU A  47    15395  11415   6133   1931  -1091    623       C  
ATOM     91  CG  LEU A  47      -7.937  -5.668  -6.645  1.00 88.68           C  
ANISOU   91  CG  LEU A  47    15142  12204   6350   1943  -1200    650       C  
ATOM     92  CD1 LEU A  47      -7.781  -6.090  -5.192  1.00 87.73           C  
ANISOU   92  CD1 LEU A  47    14920  11993   6422   1795  -1130    568       C  
ATOM     93  CD2 LEU A  47      -9.209  -4.865  -6.832  1.00 93.53           C  
ANISOU   93  CD2 LEU A  47    15623  13210   6703   2454  -1229    835       C  
ATOM     94  N   TYR A  48      -4.148  -3.098  -7.327  1.00 93.64           N  
ANISOU   94  N   TYR A  48    17314  11173   7093   1862   -806    581       N  
ATOM     95  CA  TYR A  48      -2.700  -2.958  -7.215  1.00 92.87           C  
ANISOU   95  CA  TYR A  48    17518  10631   7138   1551   -706    497       C  
ATOM     96  C   TYR A  48      -2.307  -1.712  -6.434  1.00 91.33           C  
ANISOU   96  C   TYR A  48    17753  10050   6900   1709   -564    530       C  
ATOM     97  O   TYR A  48      -1.296  -1.725  -5.722  1.00 91.73           O  
ANISOU   97  O   TYR A  48    17939   9816   7099   1425   -493    444       O  
ATOM     98  CB  TYR A  48      -2.063  -2.939  -8.604  1.00 96.51           C  
ANISOU   98  CB  TYR A  48    18139  10994   7536   1428   -713    512       C  
ATOM     99  CG  TYR A  48      -1.694  -4.310  -9.127  1.00 93.88           C  
ANISOU   99  CG  TYR A  48    17517  10826   7329   1069   -798    412       C  
ATOM    100  CD1 TYR A  48      -0.480  -4.896  -8.792  1.00 94.50           C  
ANISOU  100  CD1 TYR A  48    17613  10688   7603    705   -736    307       C  
ATOM    101  CD2 TYR A  48      -2.560  -5.021  -9.947  1.00 90.43           C  
ANISOU  101  CD2 TYR A  48    16803  10767   6789   1101   -937    427       C  
ATOM    102  CE1 TYR A  48      -0.137  -6.148  -9.265  1.00 96.67           C  
ANISOU  102  CE1 TYR A  48    17678  11086   7967    424   -790    221       C  
ATOM    103  CE2 TYR A  48      -2.225  -6.273 -10.424  1.00100.45           C  
ANISOU  103  CE2 TYR A  48    17881  12141   8143    770  -1003    327       C  
ATOM    104  CZ  TYR A  48      -1.013  -6.832 -10.080  1.00 99.60           C  
ANISOU  104  CZ  TYR A  48    17836  11780   8229    454   -919    224       C  
ATOM    105  OH  TYR A  48      -0.674  -8.079 -10.552  1.00103.62           O  
ANISOU  105  OH  TYR A  48    18205  12368   8798    170   -962    131       O  
ATOM    106  N   SER A  49      -3.082  -0.631  -6.549  1.00 88.26           N  
ANISOU  106  N   SER A  49    17599   9649   6287   2158   -518    656       N  
ATOM    107  CA  SER A  49      -2.766   0.576  -5.793  1.00 90.80           C  
ANISOU  107  CA  SER A  49    18405   9566   6530   2318   -372    683       C  
ATOM    108  C   SER A  49      -3.017   0.386  -4.302  1.00 89.93           C  
ANISOU  108  C   SER A  49    18170   9477   6523   2324   -345    620       C  
ATOM    109  O   SER A  49      -2.310   0.975  -3.477  1.00 88.34           O  
ANISOU  109  O   SER A  49    18314   8900   6350   2208   -244    570       O  
ATOM    110  CB  SER A  49      -3.575   1.760  -6.324  1.00 93.03           C  
ANISOU  110  CB  SER A  49    19014   9818   6515   2854   -314    846       C  
ATOM    111  OG  SER A  49      -4.963   1.564  -6.121  1.00 98.97           O  
ANISOU  111  OG  SER A  49    19419  11023   7162   3255   -379    932       O  
ATOM    112  N   LEU A  50      -4.008  -0.432  -3.938  1.00 87.30           N  
ANISOU  112  N   LEU A  50    17354   9585   6231   2431   -436    624       N  
ATOM    113  CA  LEU A  50      -4.280  -0.681  -2.525  1.00 86.62           C  
ANISOU  113  CA  LEU A  50    17126   9547   6240   2434   -407    570       C  
ATOM    114  C   LEU A  50      -3.203  -1.564  -1.905  1.00 83.22           C  
ANISOU  114  C   LEU A  50    16575   8975   6071   1917   -424    417       C  
ATOM    115  O   LEU A  50      -2.678  -1.254  -0.829  1.00 85.92           O  
ANISOU  115  O   LEU A  50    17117   9055   6474   1820   -348    356       O  
ATOM    116  CB  LEU A  50      -5.661  -1.315  -2.357  1.00 87.15           C  
ANISOU  116  CB  LEU A  50    16692  10161   6259   2673   -493    633       C  
ATOM    117  CG  LEU A  50      -6.862  -0.376  -2.483  1.00 90.98           C  
ANISOU  117  CG  LEU A  50    17254  10844   6469   3283   -447    804       C  
ATOM    118  CD1 LEU A  50      -8.164  -1.153  -2.360  1.00 91.95           C  
ANISOU  118  CD1 LEU A  50    16785  11597   6556   3433   -550    871       C  
ATOM    119  CD2 LEU A  50      -6.793   0.733  -1.445  1.00 92.64           C  
ANISOU  119  CD2 LEU A  50    17924  10695   6580   3572   -279    825       C  
ATOM    120  N   ILE A  51      -2.860  -2.671  -2.568  1.00 81.89           N  
ANISOU  120  N   ILE A  51    16096   8979   6038   1594   -522    357       N  
ATOM    121  CA  ILE A  51      -1.835  -3.558  -2.031  1.00 87.32           C  
ANISOU  121  CA  ILE A  51    16666   9556   6955   1153   -530    230       C  
ATOM    122  C   ILE A  51      -0.458  -2.911  -2.067  1.00 88.69           C  
ANISOU  122  C   ILE A  51    17230   9306   7162    927   -443    195       C  
ATOM    123  O   ILE A  51       0.431  -3.313  -1.308  1.00 91.07           O  
ANISOU  123  O   ILE A  51    17506   9480   7618    626   -423    110       O  
ATOM    124  CB  ILE A  51      -1.827  -4.904  -2.781  1.00 83.19           C  
ANISOU  124  CB  ILE A  51    15774   9301   6534    899   -637    181       C  
ATOM    125  CG1 ILE A  51      -1.324  -4.722  -4.215  1.00 97.63           C  
ANISOU  125  CG1 ILE A  51    17758  11047   8290    840   -649    211       C  
ATOM    126  CG2 ILE A  51      -3.213  -5.532  -2.766  1.00 83.07           C  
ANISOU  126  CG2 ILE A  51    15370   9733   6459   1060   -734    220       C  
ATOM    127  CD1 ILE A  51      -1.171  -6.021  -4.977  1.00 95.25           C  
ANISOU  127  CD1 ILE A  51    17179  10943   8067    575   -736    151       C  
ATOM    128  N   PHE A  52      -0.253  -1.914  -2.931  1.00105.58           N  
ANISOU  128  N   PHE A  52    19728  11242   9145   1054   -392    270       N  
ATOM    129  CA  PHE A  52       1.000  -1.167  -2.903  1.00106.69           C  
ANISOU  129  CA  PHE A  52    20269  10984   9284    820   -300    250       C  
ATOM    130  C   PHE A  52       1.070  -0.271  -1.675  1.00107.32           C  
ANISOU  130  C   PHE A  52    20677  10795   9306    891   -215    236       C  
ATOM    131  O   PHE A  52       2.111  -0.196  -1.012  1.00107.67           O  
ANISOU  131  O   PHE A  52    20847  10625   9436    562   -180    166       O  
ATOM    132  CB  PHE A  52       1.151  -0.342  -4.181  1.00106.24           C  
ANISOU  132  CB  PHE A  52    20537  10775   9056    929   -258    342       C  
ATOM    133  CG  PHE A  52       2.511   0.278  -4.348  1.00108.71           C  
ANISOU  133  CG  PHE A  52    21209  10727   9367    605   -169    329       C  
ATOM    134  CD1 PHE A  52       2.783   1.535  -3.832  1.00109.52           C  
ANISOU  134  CD1 PHE A  52    21824  10459   9331    642    -65    355       C  
ATOM    135  CD2 PHE A  52       3.516  -0.396  -5.021  1.00111.72           C  
ANISOU  135  CD2 PHE A  52    21430  11151   9867    256   -182    296       C  
ATOM    136  CE1 PHE A  52       4.032   2.107  -3.984  1.00106.29           C  
ANISOU  136  CE1 PHE A  52    21737   9745   8902    284     11    348       C  
ATOM    137  CE2 PHE A  52       4.767   0.170  -5.176  1.00107.85           C  
ANISOU  137  CE2 PHE A  52    21224  10390   9364    -60    -97    301       C  
ATOM    138  CZ  PHE A  52       5.025   1.424  -4.657  1.00109.32           C  
ANISOU  138  CZ  PHE A  52    21898  10226   9413    -71     -7    327       C  
ATOM    139  N   LEU A  53      -0.031   0.414  -1.356  1.00105.09           N  
ANISOU  139  N   LEU A  53    20537  10535   8856   1327   -181    305       N  
ATOM    140  CA  LEU A  53      -0.058   1.277  -0.180  1.00100.98           C  
ANISOU  140  CA  LEU A  53    20377   9744   8246   1440    -88    289       C  
ATOM    141  C   LEU A  53       0.015   0.463   1.106  1.00100.46           C  
ANISOU  141  C   LEU A  53    20007   9807   8357   1260   -124    190       C  
ATOM    142  O   LEU A  53       0.657   0.881   2.076  1.00104.38           O  
ANISOU  142  O   LEU A  53    20766  10037   8858   1082    -72    126       O  
ATOM    143  CB  LEU A  53      -1.320   2.140  -0.198  1.00101.27           C  
ANISOU  143  CB  LEU A  53    20623   9814   8041   2021    -25    405       C  
ATOM    144  CG  LEU A  53      -1.495   3.154   0.934  1.00106.98           C  
ANISOU  144  CG  LEU A  53    21811  10228   8610   2238     98    403       C  
ATOM    145  CD1 LEU A  53      -0.450   4.256   0.839  1.00105.68           C  
ANISOU  145  CD1 LEU A  53    22304   9525   8324   2023    197    385       C  
ATOM    146  CD2 LEU A  53      -2.900   3.737   0.914  1.00102.99           C  
ANISOU  146  CD2 LEU A  53    21372   9885   7876   2886    157    534       C  
ATOM    147  N   LEU A  54      -0.635  -0.702   1.130  1.00 91.50           N  
ANISOU  147  N   LEU A  54    18338   9077   7351   1282   -216    177       N  
ATOM    148  CA  LEU A  54      -0.653  -1.515   2.342  1.00 86.59           C  
ANISOU  148  CA  LEU A  54    17431   8588   6883   1136   -244     95       C  
ATOM    149  C   LEU A  54       0.719  -2.109   2.633  1.00 89.07           C  
ANISOU  149  C   LEU A  54    17691   8771   7382    647   -268     -4       C  
ATOM    150  O   LEU A  54       1.172  -2.103   3.783  1.00 90.31           O  
ANISOU  150  O   LEU A  54    17912   8808   7592    497   -246    -69       O  
ATOM    151  CB  LEU A  54      -1.700  -2.622   2.214  1.00 89.56           C  
ANISOU  151  CB  LEU A  54    17277   9425   7328   1247   -331    115       C  
ATOM    152  CG  LEU A  54      -3.056  -2.375   2.879  1.00 93.70           C  
ANISOU  152  CG  LEU A  54    17692  10179   7729   1665   -301    184       C  
ATOM    153  CD1 LEU A  54      -3.714  -1.119   2.326  1.00 96.71           C  
ANISOU  153  CD1 LEU A  54    18407  10481   7856   2123   -231    306       C  
ATOM    154  CD2 LEU A  54      -3.966  -3.581   2.705  1.00 89.92           C  
ANISOU  154  CD2 LEU A  54    16655  10187   7325   1654   -401    200       C  
ATOM    155  N   SER A  55       1.396  -2.627   1.608  1.00101.55           N  
ANISOU  155  N   SER A  55    19148  10392   9043    412   -310     -9       N  
ATOM    156  CA  SER A  55       2.701  -3.242   1.808  1.00 98.10           C  
ANISOU  156  CA  SER A  55    18617   9890   8767     -8   -323    -80       C  
ATOM    157  C   SER A  55       3.810  -2.221   2.023  1.00 99.79           C  
ANISOU  157  C   SER A  55    19244   9761   8912   -223   -256    -87       C  
ATOM    158  O   SER A  55       4.850  -2.571   2.591  1.00100.75           O  
ANISOU  158  O   SER A  55    19295   9847   9138   -553   -264   -140       O  
ATOM    159  CB  SER A  55       3.051  -4.137   0.617  1.00 95.15           C  
ANISOU  159  CB  SER A  55    17993   9681   8477   -156   -370    -75       C  
ATOM    160  OG  SER A  55       3.215  -3.374  -0.566  1.00115.48           O  
ANISOU  160  OG  SER A  55    20822  12129  10925    -95   -338     -9       O  
ATOM    161  N   VAL A  56       3.620  -0.976   1.585  1.00103.51           N  
ANISOU  161  N   VAL A  56    20149   9989   9192    -55   -190    -27       N  
ATOM    162  CA  VAL A  56       4.638   0.049   1.788  1.00107.99           C  
ANISOU  162  CA  VAL A  56    21163  10206   9661   -305   -123    -34       C  
ATOM    163  C   VAL A  56       4.450   0.792   3.105  1.00108.96           C  
ANISOU  163  C   VAL A  56    21605  10113   9682   -243    -80    -75       C  
ATOM    164  O   VAL A  56       5.408   1.398   3.607  1.00108.13           O  
ANISOU  164  O   VAL A  56    21803   9759   9523   -561    -51   -111       O  
ATOM    165  CB  VAL A  56       4.659   1.050   0.617  1.00113.71           C  
ANISOU  165  CB  VAL A  56    22281  10717  10207   -203    -58     52       C  
ATOM    166  CG1 VAL A  56       3.540   2.072   0.759  1.00116.87           C  
ANISOU  166  CG1 VAL A  56    23063  10954  10389    256      8    110       C  
ATOM    167  CG2 VAL A  56       6.015   1.734   0.520  1.00113.25           C  
ANISOU  167  CG2 VAL A  56    22552  10380  10096   -627     -5     46       C  
ATOM    168  N   LEU A  57       3.251   0.757   3.686  1.00118.87           N  
ANISOU  168  N   LEU A  57    22800  11473  10893    142    -73    -67       N  
ATOM    169  CA  LEU A  57       3.009   1.355   4.993  1.00120.42           C  
ANISOU  169  CA  LEU A  57    23280  11487  10988    236    -23   -109       C  
ATOM    170  C   LEU A  57       3.363   0.410   6.134  1.00118.95           C  
ANISOU  170  C   LEU A  57    22747  11472  10977      1    -87   -197       C  
ATOM    171  O   LEU A  57       3.932   0.847   7.142  1.00120.82           O  
ANISOU  171  O   LEU A  57    23240  11505  11161   -196    -69   -259       O  
ATOM    172  CB  LEU A  57       1.546   1.786   5.119  1.00118.62           C  
ANISOU  172  CB  LEU A  57    23143  11320  10607    802     35    -42       C  
ATOM    173  CG  LEU A  57       1.167   3.135   4.507  1.00121.81           C  
ANISOU  173  CG  LEU A  57    24117  11423  10743   1119    142     44       C  
ATOM    174  CD1 LEU A  57      -0.334   3.375   4.613  1.00119.41           C  
ANISOU  174  CD1 LEU A  57    23780  11294  10295   1734    195    134       C  
ATOM    175  CD2 LEU A  57       1.945   4.273   5.161  1.00124.23           C  
ANISOU  175  CD2 LEU A  57    25081  11240  10880    917    229     -5       C  
ATOM    176  N   GLY A  58       3.046  -0.880   5.993  1.00102.47           N  
ANISOU  176  N   GLY A  58    20110   9745   9079      7   -161   -203       N  
ATOM    177  CA  GLY A  58       3.328  -1.818   7.067  1.00 96.81           C  
ANISOU  177  CA  GLY A  58    19082   9186   8516   -180   -211   -273       C  
ATOM    178  C   GLY A  58       4.797  -2.196   7.141  1.00 95.36           C  
ANISOU  178  C   GLY A  58    18822   8968   8443   -646   -254   -318       C  
ATOM    179  O   GLY A  58       5.403  -2.163   8.214  1.00102.48           O  
ANISOU  179  O   GLY A  58    19784   9801   9352   -855   -268   -373       O  
ATOM    180  N   ASN A  59       5.394  -2.551   5.999  1.00 96.24           N  
ANISOU  180  N   ASN A  59    18792   9150   8625   -804   -274   -286       N  
ATOM    181  CA  ASN A  59       6.797  -2.961   5.998  1.00 93.99           C  
ANISOU  181  CA  ASN A  59    18381   8897   8435  -1212   -303   -305       C  
ATOM    182  C   ASN A  59       7.719  -1.819   6.400  1.00100.69           C  
ANISOU  182  C   ASN A  59    19641   9471   9146  -1488   -275   -316       C  
ATOM    183  O   ASN A  59       8.747  -2.055   7.040  1.00100.28           O  
ANISOU  183  O   ASN A  59    19492   9470   9138  -1818   -311   -344       O  
ATOM    184  CB  ASN A  59       7.181  -3.509   4.625  1.00 91.79           C  
ANISOU  184  CB  ASN A  59    17900   8746   8229  -1278   -307   -258       C  
ATOM    185  CG  ASN A  59       6.541  -4.847   4.340  1.00 92.56           C  
ANISOU  185  CG  ASN A  59    17578   9123   8466  -1129   -349   -265       C  
ATOM    186  OD1 ASN A  59       6.955  -5.869   4.884  1.00 96.21           O  
ANISOU  186  OD1 ASN A  59    17751   9745   9058  -1257   -379   -297       O  
ATOM    187  ND2 ASN A  59       5.536  -4.852   3.472  1.00 96.58           N  
ANISOU  187  ND2 ASN A  59    18069   9697   8930   -867   -351   -231       N  
ATOM    188  N   THR A  60       7.374  -0.581   6.039  1.00111.66           N  
ANISOU  188  N   THR A  60    21504  10576  10347  -1368   -210   -289       N  
ATOM    189  CA  THR A  60       8.144   0.559   6.526  1.00112.03           C  
ANISOU  189  CA  THR A  60    22024  10316  10225  -1652   -179   -310       C  
ATOM    190  C   THR A  60       7.928   0.767   8.019  1.00114.08           C  
ANISOU  190  C   THR A  60    22433  10488  10424  -1644   -192   -384       C  
ATOM    191  O   THR A  60       8.830   1.243   8.719  1.00116.33           O  
ANISOU  191  O   THR A  60    22933  10641  10625  -2009   -212   -426       O  
ATOM    192  CB  THR A  60       7.767   1.819   5.747  1.00103.42           C  
ANISOU  192  CB  THR A  60    21469   8901   8924  -1493    -89   -258       C  
ATOM    193  OG1 THR A  60       7.943   1.582   4.345  1.00109.45           O  
ANISOU  193  OG1 THR A  60    22082   9764   9739  -1490    -79   -186       O  
ATOM    194  CG2 THR A  60       8.641   2.995   6.159  1.00104.98           C  
ANISOU  194  CG2 THR A  60    22212   8750   8925  -1859    -51   -281       C  
ATOM    195  N   LEU A  61       6.750   0.400   8.525  1.00113.38           N  
ANISOU  195  N   LEU A  61    22220  10496  10365  -1249   -183   -397       N  
ATOM    196  CA  LEU A  61       6.478   0.542   9.951  1.00109.99           C  
ANISOU  196  CA  LEU A  61    21920   9999   9872  -1203   -183   -464       C  
ATOM    197  C   LEU A  61       7.253  -0.487  10.765  1.00109.26           C  
ANISOU  197  C   LEU A  61    21418  10153   9944  -1503   -275   -511       C  
ATOM    198  O   LEU A  61       7.826  -0.155  11.809  1.00113.62           O  
ANISOU  198  O   LEU A  61    22156  10602  10413  -1742   -302   -569       O  
ATOM    199  CB  LEU A  61       4.974   0.422  10.204  1.00112.27           C  
ANISOU  199  CB  LEU A  61    22153  10369  10136   -680   -133   -444       C  
ATOM    200  CG  LEU A  61       4.421   0.701  11.603  1.00120.98           C  
ANISOU  200  CG  LEU A  61    23448  11385  11133   -510    -96   -496       C  
ATOM    201  CD1 LEU A  61       3.037   1.320  11.496  1.00119.59           C  
ANISOU  201  CD1 LEU A  61    23495  11143  10800     39      9   -440       C  
ATOM    202  CD2 LEU A  61       4.360  -0.572  12.438  1.00124.81           C  
ANISOU  202  CD2 LEU A  61    23424  12191  11808   -566   -165   -532       C  
ATOM    203  N   VAL A  62       7.290  -1.739  10.300  1.00 84.26           N  
ANISOU  203  N   VAL A  62    17722   7306   6988  -1493   -322   -484       N  
ATOM    204  CA  VAL A  62       7.917  -2.795  11.089  1.00 82.37           C  
ANISOU  204  CA  VAL A  62    17101   7304   6891  -1696   -394   -514       C  
ATOM    205  C   VAL A  62       9.436  -2.660  11.089  1.00 88.37           C  
ANISOU  205  C   VAL A  62    17857   8080   7641  -2155   -442   -510       C  
ATOM    206  O   VAL A  62      10.094  -3.030  12.068  1.00 91.71           O  
ANISOU  206  O   VAL A  62    18146   8617   8084  -2367   -501   -539       O  
ATOM    207  CB  VAL A  62       7.466  -4.181  10.587  1.00 73.11           C  
ANISOU  207  CB  VAL A  62    15430   6432   5917  -1533   -413   -486       C  
ATOM    208  CG1 VAL A  62       5.950  -4.283  10.613  1.00 80.27           C  
ANISOU  208  CG1 VAL A  62    16310   7379   6811  -1126   -375   -479       C  
ATOM    209  CG2 VAL A  62       7.986  -4.441   9.190  1.00 84.05           C  
ANISOU  209  CG2 VAL A  62    16680   7888   7367  -1629   -410   -432       C  
ATOM    210  N   ILE A  63      10.024  -2.129  10.013  1.00129.98           N  
ANISOU  210  N   ILE A  63    23256  13265  12865  -2320   -417   -464       N  
ATOM    211  CA  ILE A  63      11.464  -1.903  10.019  1.00130.91           C  
ANISOU  211  CA  ILE A  63    23363  13432  12944  -2781   -456   -444       C  
ATOM    212  C   ILE A  63      11.827  -0.708  10.886  1.00132.62           C  
ANISOU  212  C   ILE A  63    24061  13383  12945  -3043   -467   -496       C  
ATOM    213  O   ILE A  63      12.979  -0.583  11.315  1.00132.72           O  
ANISOU  213  O   ILE A  63    24034  13488  12905  -3466   -528   -494       O  
ATOM    214  CB  ILE A  63      12.012  -1.716   8.590  1.00128.68           C  
ANISOU  214  CB  ILE A  63    23065  13159  12667  -2900   -414   -370       C  
ATOM    215  CG1 ILE A  63      11.405  -0.474   7.937  1.00136.86           C  
ANISOU  215  CG1 ILE A  63    24622  13842  13535  -2776   -338   -361       C  
ATOM    216  CG2 ILE A  63      11.754  -2.958   7.749  1.00126.99           C  
ANISOU  216  CG2 ILE A  63    22398  13207  12645  -2677   -406   -328       C  
ATOM    217  CD1 ILE A  63      12.090  -0.064   6.652  1.00146.46           C  
ANISOU  217  CD1 ILE A  63    25918  15020  14709  -2970   -291   -286       C  
ATOM    218  N   THR A  64      10.867   0.177  11.159  1.00107.31           N  
ANISOU  218  N   THR A  64    21321   9860   9593  -2798   -407   -537       N  
ATOM    219  CA  THR A  64      11.122   1.308  12.043  1.00100.95           C  
ANISOU  219  CA  THR A  64    21053   8751   8551  -3022   -406   -600       C  
ATOM    220  C   THR A  64      11.032   0.893  13.507  1.00103.60           C  
ANISOU  220  C   THR A  64    21291   9184   8890  -3025   -469   -671       C  
ATOM    221  O   THR A  64      11.949   1.160  14.291  1.00110.24           O  
ANISOU  221  O   THR A  64    22228  10032   9628  -3434   -543   -709       O  
ATOM    222  CB  THR A  64      10.141   2.444  11.745  1.00107.83           C  
ANISOU  222  CB  THR A  64    22519   9220   9232  -2709   -293   -606       C  
ATOM    223  OG1 THR A  64      10.340   2.913  10.406  1.00 98.89           O  
ANISOU  223  OG1 THR A  64    21526   7979   8068  -2749   -238   -534       O  
ATOM    224  CG2 THR A  64      10.347   3.597  12.717  1.00113.17           C  
ANISOU  224  CG2 THR A  64    23831   9534   9636  -2918   -276   -682       C  
ATOM    225  N   VAL A  65       9.941   0.223  13.888  1.00 95.71           N  
ANISOU  225  N   VAL A  65    20086   8284   7995  -2592   -444   -683       N  
ATOM    226  CA  VAL A  65       9.746  -0.169  15.281  1.00 92.21           C  
ANISOU  226  CA  VAL A  65    19570   7921   7545  -2553   -486   -744       C  
ATOM    227  C   VAL A  65      10.808  -1.153  15.750  1.00100.36           C  
ANISOU  227  C   VAL A  65    20132   9295   8707  -2872   -599   -734       C  
ATOM    228  O   VAL A  65      11.053  -1.268  16.955  1.00105.80           O  
ANISOU  228  O   VAL A  65    20833  10032   9335  -2994   -658   -785       O  
ATOM    229  CB  VAL A  65       8.330  -0.751  15.483  1.00 82.42           C  
ANISOU  229  CB  VAL A  65    18158   6763   6395  -2029   -424   -739       C  
ATOM    230  CG1 VAL A  65       7.277   0.236  15.007  1.00 85.47           C  
ANISOU  230  CG1 VAL A  65    18981   6865   6630  -1663   -307   -725       C  
ATOM    231  CG2 VAL A  65       8.188  -2.083  14.762  1.00 93.40           C  
ANISOU  231  CG2 VAL A  65    18950   8496   8041  -1912   -449   -679       C  
ATOM    232  N   LEU A  66      11.450  -1.869  14.827  1.00118.27           N  
ANISOU  232  N   LEU A  66    21993  11809  11135  -2986   -625   -663       N  
ATOM    233  CA  LEU A  66      12.542  -2.763  15.190  1.00117.60           C  
ANISOU  233  CA  LEU A  66    21471  12065  11146  -3257   -717   -630       C  
ATOM    234  C   LEU A  66      13.878  -2.034  15.259  1.00124.48           C  
ANISOU  234  C   LEU A  66    22482  12947  11868  -3778   -783   -618       C  
ATOM    235  O   LEU A  66      14.701  -2.332  16.131  1.00126.30           O  
ANISOU  235  O   LEU A  66    22533  13394  12063  -4042   -879   -618       O  
ATOM    236  CB  LEU A  66      12.630  -3.924  14.196  1.00109.94           C  
ANISOU  236  CB  LEU A  66    20014  11365  10395  -3110   -697   -553       C  
ATOM    237  CG  LEU A  66      11.494  -4.945  14.264  1.00106.32           C  
ANISOU  237  CG  LEU A  66    19313  10992  10091  -2692   -659   -559       C  
ATOM    238  CD1 LEU A  66      11.622  -5.969  13.146  1.00108.92           C  
ANISOU  238  CD1 LEU A  66    19265  11528  10592  -2592   -633   -493       C  
ATOM    239  CD2 LEU A  66      11.470  -5.629  15.620  1.00107.23           C  
ANISOU  239  CD2 LEU A  66    19264  11249  10228  -2665   -709   -590       C  
ATOM    240  N   ILE A  67      14.109  -1.077  14.356  1.00140.69           N  
ANISOU  240  N   ILE A  67    24851  14788  13816  -3944   -736   -599       N  
ATOM    241  CA  ILE A  67      15.344  -0.296  14.387  1.00144.82           C  
ANISOU  241  CA  ILE A  67    25542  15314  14170  -4494   -793   -583       C  
ATOM    242  C   ILE A  67      15.325   0.787  15.452  1.00148.99           C  
ANISOU  242  C   ILE A  67    26627  15542  14441  -4728   -828   -679       C  
ATOM    243  O   ILE A  67      16.383   1.343  15.775  1.00151.47           O  
ANISOU  243  O   ILE A  67    27057  15905  14590  -5251   -907   -679       O  
ATOM    244  CB  ILE A  67      15.622   0.326  13.004  1.00141.97           C  
ANISOU  244  CB  ILE A  67    25342  14825  13776  -4615   -718   -520       C  
ATOM    245  CG1 ILE A  67      17.129   0.442  12.760  1.00145.54           C  
ANISOU  245  CG1 ILE A  67    25591  15543  14164  -5167   -780   -445       C  
ATOM    246  CG2 ILE A  67      14.942   1.682  12.870  1.00148.35           C  
ANISOU  246  CG2 ILE A  67    26867  15124  14375  -4570   -637   -577       C  
ATOM    247  CD1 ILE A  67      17.816  -0.887  12.535  1.00143.80           C  
ANISOU  247  CD1 ILE A  67    24665  15829  14142  -5127   -818   -352       C  
ATOM    248  N   ARG A  68      14.157   1.099  16.016  1.00158.96           N  
ANISOU  248  N   ARG A  68    28238  16513  15645  -4364   -769   -758       N  
ATOM    249  CA  ARG A  68      14.050   2.098  17.073  1.00160.81           C  
ANISOU  249  CA  ARG A  68    28912  16513  15677  -4443   -751   -781       C  
ATOM    250  C   ARG A  68      14.177   1.475  18.459  1.00160.19           C  
ANISOU  250  C   ARG A  68    28621  16638  15606  -4478   -849   -832       C  
ATOM    251  O   ARG A  68      14.898   1.997  19.315  1.00162.61           O  
ANISOU  251  O   ARG A  68    29041  16976  15768  -4819   -908   -819       O  
ATOM    252  CB  ARG A  68      12.719   2.850  16.961  1.00157.35           C  
ANISOU  252  CB  ARG A  68    28942  15685  15159  -3966   -605   -793       C  
ATOM    253  CG  ARG A  68      12.633   3.831  15.803  1.00159.15           C  
ANISOU  253  CG  ARG A  68    29537  15646  15288  -3953   -498   -728       C  
ATOM    254  CD  ARG A  68      13.774   4.833  15.821  1.00167.26           C  
ANISOU  254  CD  ARG A  68    30815  16617  16121  -4481   -512   -668       C  
ATOM    255  NE  ARG A  68      14.044   5.361  14.489  1.00174.99           N  
ANISOU  255  NE  ARG A  68    31941  17488  17058  -4583   -444   -602       N  
ATOM    256  CZ  ARG A  68      15.130   6.047  14.160  1.00177.50           C  
ANISOU  256  CZ  ARG A  68    32378  17833  17230  -5076   -456   -543       C  
ATOM    257  NH1 ARG A  68      16.073   6.315  15.047  1.00173.20           N  
ANISOU  257  NH1 ARG A  68    31820  17430  16559  -5533   -540   -538       N  
ATOM    258  NH2 ARG A  68      15.272   6.475  12.908  1.00176.68           N  
ANISOU  258  NH2 ARG A  68    32409  17629  17091  -5119   -382   -485       N  
ATOM    259  N   ASN A  69      13.484   0.362  18.693  1.00147.73           N  
ANISOU  259  N   ASN A  69    26750  15206  14175  -4137   -867   -886       N  
ATOM    260  CA  ASN A  69      13.442  -0.284  20.000  1.00149.79           C  
ANISOU  260  CA  ASN A  69    26828  15646  14440  -4095   -941   -929       C  
ATOM    261  C   ASN A  69      14.367  -1.496  19.985  1.00148.31           C  
ANISOU  261  C   ASN A  69    25973  15946  14431  -4245  -1041   -846       C  
ATOM    262  O   ASN A  69      14.074  -2.501  19.329  1.00146.23           O  
ANISOU  262  O   ASN A  69    25277  15883  14400  -3959   -998   -777       O  
ATOM    263  CB  ASN A  69      12.015  -0.693  20.355  1.00148.11           C  
ANISOU  263  CB  ASN A  69    26622  15341  14311  -3530   -842   -956       C  
ATOM    264  CG  ASN A  69      11.006   0.403  20.074  1.00150.87           C  
ANISOU  264  CG  ASN A  69    27529  15272  14521  -3248   -706   -986       C  
ATOM    265  OD1 ASN A  69      11.352   1.583  20.019  1.00155.50           O  
ANISOU  265  OD1 ASN A  69    28504  15622  14956  -3436   -666   -948       O  
ATOM    266  ND2 ASN A  69       9.748   0.017  19.894  1.00144.96           N  
ANISOU  266  ND2 ASN A  69    26705  14508  13866  -2738   -607   -979       N  
ATOM    267  N   LYS A  70      15.484  -1.400  20.711  1.00144.28           N  
ANISOU  267  N   LYS A  70    25396  15633  13791  -4688  -1173   -846       N  
ATOM    268  CA  LYS A  70      16.364  -2.551  20.870  1.00143.50           C  
ANISOU  268  CA  LYS A  70    24673  16026  13826  -4779  -1265   -754       C  
ATOM    269  C   LYS A  70      15.743  -3.626  21.752  1.00142.69           C  
ANISOU  269  C   LYS A  70    24307  16067  13841  -4410  -1264   -760       C  
ATOM    270  O   LYS A  70      16.193  -4.777  21.716  1.00143.11           O  
ANISOU  270  O   LYS A  70    23846  16483  14046  -4323  -1295   -672       O  
ATOM    271  CB  LYS A  70      17.709  -2.112  21.451  1.00142.15           C  
ANISOU  271  CB  LYS A  70    24483  16076  13450  -5356  -1417   -739       C  
ATOM    272  CG  LYS A  70      18.331  -0.919  20.744  1.00150.57           C  
ANISOU  272  CG  LYS A  70    25894  16971  14346  -5810  -1421   -742       C  
ATOM    273  CD  LYS A  70      19.744  -0.656  21.242  1.00153.63           C  
ANISOU  273  CD  LYS A  70    26091  17707  14574  -6376  -1562   -673       C  
ATOM    274  CE  LYS A  70      20.331   0.597  20.611  1.00153.92           C  
ANISOU  274  CE  LYS A  70    26420  17584  14477  -6767  -1506   -612       C  
ATOM    275  NZ  LYS A  70      20.410   0.490  19.127  1.00154.39           N  
ANISOU  275  NZ  LYS A  70    26380  17638  14642  -6756  -1436   -570       N  
ATOM    276  N   ARG A  71      14.723  -3.275  22.539  1.00154.07           N  
ANISOU  276  N   ARG A  71    26111  17228  15202  -4180  -1217   -856       N  
ATOM    277  CA  ARG A  71      14.045  -4.261  23.373  1.00153.48           C  
ANISOU  277  CA  ARG A  71    25813  17272  15230  -3833  -1198   -858       C  
ATOM    278  C   ARG A  71      13.266  -5.266  22.534  1.00155.96           C  
ANISOU  278  C   ARG A  71    25788  17663  15805  -3418  -1092   -797       C  
ATOM    279  O   ARG A  71      13.063  -6.407  22.966  1.00155.55           O  
ANISOU  279  O   ARG A  71    25399  17823  15881  -3211  -1089   -758       O  
ATOM    280  CB  ARG A  71      13.108  -3.554  24.354  1.00155.94           C  
ANISOU  280  CB  ARG A  71    26615  17265  15370  -3678  -1151   -967       C  
ATOM    281  CG  ARG A  71      12.682  -4.397  25.544  1.00156.68           C  
ANISOU  281  CG  ARG A  71    26537  17505  15489  -3458  -1162   -976       C  
ATOM    282  CD  ARG A  71      13.876  -4.828  26.378  1.00160.53           C  
ANISOU  282  CD  ARG A  71    26780  18315  15898  -3787  -1322   -946       C  
ATOM    283  NE  ARG A  71      13.463  -5.547  27.577  1.00170.86           N  
ANISOU  283  NE  ARG A  71    27990  19730  17198  -3580  -1329   -955       N  
ATOM    284  CZ  ARG A  71      13.661  -5.114  28.815  1.00170.37           C  
ANISOU  284  CZ  ARG A  71    28193  19631  16909  -3744  -1408  -1024       C  
ATOM    285  NH1 ARG A  71      14.267  -3.963  29.057  1.00171.05           N  
ANISOU  285  NH1 ARG A  71    28674  19567  16750  -4142  -1493  -1095       N  
ATOM    286  NH2 ARG A  71      13.239  -5.854  29.837  1.00166.61           N  
ANISOU  286  NH2 ARG A  71    27602  19262  16439  -3520  -1399  -1020       N  
ATOM    287  N   MET A  72      12.826  -4.866  21.339  1.00135.14           N  
ANISOU  287  N   MET A  72    23260  14854  13233  -3309  -1006   -787       N  
ATOM    288  CA  MET A  72      12.035  -5.742  20.484  1.00130.92           C  
ANISOU  288  CA  MET A  72    22445  14383  12916  -2949   -914   -738       C  
ATOM    289  C   MET A  72      12.889  -6.669  19.630  1.00124.38           C  
ANISOU  289  C   MET A  72    21166  13846  12246  -3034   -938   -642       C  
ATOM    290  O   MET A  72      12.374  -7.672  19.126  1.00116.27           O  
ANISOU  290  O   MET A  72    19865  12920  11393  -2768   -880   -602       O  
ATOM    291  CB  MET A  72      11.130  -4.908  19.574  1.00122.56           C  
ANISOU  291  CB  MET A  72    21702  13032  11835  -2761   -815   -762       C  
ATOM    292  CG  MET A  72       9.958  -4.252  20.283  1.00124.14           C  
ANISOU  292  CG  MET A  72    22284  12975  11909  -2496   -742   -832       C  
ATOM    293  SD  MET A  72       8.497  -5.306  20.327  1.00132.88           S  
ANISOU  293  SD  MET A  72    23098  14206  13185  -2005   -650   -806       S  
ATOM    294  CE  MET A  72       7.253  -4.133  20.861  1.00140.25           C  
ANISOU  294  CE  MET A  72    24548  14827  13913  -1699   -542   -864       C  
ATOM    295  N   ARG A  73      14.177  -6.363  19.460  1.00123.86           N  
ANISOU  295  N   ARG A  73    21028  13927  12107  -3401  -1016   -601       N  
ATOM    296  CA  ARG A  73      15.045  -7.116  18.553  1.00118.73           C  
ANISOU  296  CA  ARG A  73    19976  13559  11578  -3463  -1017   -496       C  
ATOM    297  C   ARG A  73      15.444  -8.447  19.192  1.00120.96           C  
ANISOU  297  C   ARG A  73    19846  14165  11947  -3347  -1050   -431       C  
ATOM    298  O   ARG A  73      16.573  -8.657  19.641  1.00123.74           O  
ANISOU  298  O   ARG A  73    19978  14808  12231  -3568  -1136   -367       O  
ATOM    299  CB  ARG A  73      16.269  -6.290  18.180  1.00121.06           C  
ANISOU  299  CB  ARG A  73    20318  13939  11741  -3900  -1080   -457       C  
ATOM    300  CG  ARG A  73      15.951  -5.036  17.387  1.00127.50           C  
ANISOU  300  CG  ARG A  73    21561  14418  12467  -4015  -1028   -503       C  
ATOM    301  CD  ARG A  73      17.067  -4.702  16.411  1.00127.46           C  
ANISOU  301  CD  ARG A  73    21438  14563  12429  -4343  -1036   -419       C  
ATOM    302  NE  ARG A  73      18.303  -4.352  17.099  1.00132.06           N  
ANISOU  302  NE  ARG A  73    21944  15383  12848  -4804  -1155   -388       N  
ATOM    303  CZ  ARG A  73      18.616  -3.128  17.501  1.00137.11           C  
ANISOU  303  CZ  ARG A  73    22996  15835  13265  -5201  -1212   -447       C  
ATOM    304  NH1 ARG A  73      17.800  -2.105  17.302  1.00134.54           N  
ANISOU  304  NH1 ARG A  73    23225  15048  12846  -5157  -1146   -537       N  
ATOM    305  NH2 ARG A  73      19.775  -2.924  18.120  1.00138.44           N  
ANISOU  305  NH2 ARG A  73    23032  16291  13279  -5652  -1337   -408       N  
ATOM    306  N   THR A  74      14.480  -9.363  19.224  1.00104.55           N  
ANISOU  306  N   THR A  74    17670  12048  10007  -2991   -978   -440       N  
ATOM    307  CA  THR A  74      14.760 -10.730  19.630  1.00100.88           C  
ANISOU  307  CA  THR A  74    16858  11840   9633  -2832   -976   -370       C  
ATOM    308  C   THR A  74      15.303 -11.512  18.436  1.00104.20           C  
ANISOU  308  C   THR A  74    16995  12428  10170  -2759   -918   -277       C  
ATOM    309  O   THR A  74      15.385 -11.006  17.313  1.00105.63           O  
ANISOU  309  O   THR A  74    17237  12528  10371  -2828   -882   -272       O  
ATOM    310  CB  THR A  74      13.507 -11.387  20.206  1.00 99.48           C  
ANISOU  310  CB  THR A  74    16726  11541   9529  -2528   -916   -416       C  
ATOM    311  OG1 THR A  74      13.837 -12.682  20.723  1.00104.56           O  
ANISOU  311  OG1 THR A  74    17094  12405  10230  -2397   -912   -346       O  
ATOM    312  CG2 THR A  74      12.439 -11.534  19.134  1.00 89.62           C  
ANISOU  312  CG2 THR A  74    15529  10121   8400  -2313   -817   -440       C  
ATOM    313  N   VAL A  75      15.687 -12.766  18.680  1.00129.05           N  
ANISOU  313  N   VAL A  75    19857  15799  13378  -2600   -899   -197       N  
ATOM    314  CA  VAL A  75      16.241 -13.589  17.608  1.00127.92           C  
ANISOU  314  CA  VAL A  75    19475  15811  13319  -2492   -826   -104       C  
ATOM    315  C   VAL A  75      15.187 -13.851  16.538  1.00122.89           C  
ANISOU  315  C   VAL A  75    18948  14942  12802  -2298   -727   -153       C  
ATOM    316  O   VAL A  75      15.492 -13.883  15.340  1.00123.71           O  
ANISOU  316  O   VAL A  75    18996  15064  12944  -2297   -674   -116       O  
ATOM    317  CB  VAL A  75      16.810 -14.898  18.183  1.00136.90           C  
ANISOU  317  CB  VAL A  75    20347  17202  14466  -2312   -809     -6       C  
ATOM    318  CG1 VAL A  75      17.343 -15.788  17.070  1.00138.79           C  
ANISOU  318  CG1 VAL A  75    20391  17572  14770  -2149   -709     91       C  
ATOM    319  CG2 VAL A  75      17.900 -14.596  19.200  1.00146.81           C  
ANISOU  319  CG2 VAL A  75    21456  18746  15578  -2511   -925     57       C  
ATOM    320  N   THR A  76      13.930 -14.029  16.949  1.00104.23           N  
ANISOU  320  N   THR A  76    16733  12385  10485  -2142   -703   -231       N  
ATOM    321  CA  THR A  76      12.861 -14.261  15.982  1.00100.41           C  
ANISOU  321  CA  THR A  76    16332  11727  10092  -1983   -628   -273       C  
ATOM    322  C   THR A  76      12.567 -13.005  15.170  1.00 96.15           C  
ANISOU  322  C   THR A  76    15991  11023   9518  -2086   -636   -319       C  
ATOM    323  O   THR A  76      12.310 -13.086  13.963  1.00 97.04           O  
ANISOU  323  O   THR A  76    16108  11081   9682  -2025   -586   -313       O  
ATOM    324  CB  THR A  76      11.600 -14.742  16.700  1.00101.09           C  
ANISOU  324  CB  THR A  76    16488  11708  10214  -1816   -603   -328       C  
ATOM    325  OG1 THR A  76      11.919 -15.863  17.534  1.00103.24           O  
ANISOU  325  OG1 THR A  76    16618  12110  10497  -1733   -591   -280       O  
ATOM    326  CG2 THR A  76      10.534 -15.154  15.693  1.00 94.14           C  
ANISOU  326  CG2 THR A  76    15634  10721   9413  -1677   -537   -356       C  
ATOM    327  N   ASN A  77      12.607 -11.835  15.811  1.00108.44           N  
ANISOU  327  N   ASN A  77    17749  12484  10970  -2240   -695   -363       N  
ATOM    328  CA  ASN A  77      12.295 -10.592  15.115  1.00103.83           C  
ANISOU  328  CA  ASN A  77    17424  11701  10324  -2317   -689   -402       C  
ATOM    329  C   ASN A  77      13.393 -10.170  14.149  1.00105.73           C  
ANISOU  329  C   ASN A  77    17622  12015  10537  -2528   -692   -344       C  
ATOM    330  O   ASN A  77      13.126  -9.382  13.236  1.00108.89           O  
ANISOU  330  O   ASN A  77    18211  12255  10909  -2552   -662   -357       O  
ATOM    331  CB  ASN A  77      12.034  -9.474  16.126  1.00107.03           C  
ANISOU  331  CB  ASN A  77    18130  11944  10593  -2416   -735   -469       C  
ATOM    332  CG  ASN A  77      10.669  -9.583  16.776  1.00108.14           C  
ANISOU  332  CG  ASN A  77    18380  11964  10743  -2160   -699   -527       C  
ATOM    333  OD1 ASN A  77       9.808 -10.335  16.318  1.00108.79           O  
ANISOU  333  OD1 ASN A  77    18334  12072  10930  -1939   -645   -519       O  
ATOM    334  ND2 ASN A  77      10.465  -8.833  17.853  1.00114.81           N  
ANISOU  334  ND2 ASN A  77    19469  12692  11460  -2202   -726   -582       N  
ATOM    335  N   ILE A  78      14.619 -10.667  14.330  1.00 91.34           N  
ANISOU  335  N   ILE A  78    15549  10451   8706  -2668   -720   -267       N  
ATOM    336  CA  ILE A  78      15.687 -10.353  13.385  1.00 95.34           C  
ANISOU  336  CA  ILE A  78    15960  11084   9181  -2861   -707   -192       C  
ATOM    337  C   ILE A  78      15.384 -10.960  12.021  1.00 94.40           C  
ANISOU  337  C   ILE A  78    15760  10943   9163  -2666   -613   -163       C  
ATOM    338  O   ILE A  78      15.571 -10.314  10.982  1.00 91.63           O  
ANISOU  338  O   ILE A  78    15509  10521   8784  -2761   -580   -145       O  
ATOM    339  CB  ILE A  78      17.045 -10.827  13.935  1.00 95.84           C  
ANISOU  339  CB  ILE A  78    15717  11501   9197  -3015   -754    -94       C  
ATOM    340  CG1 ILE A  78      17.474  -9.953  15.114  1.00 96.90           C  
ANISOU  340  CG1 ILE A  78    15970  11661   9185  -3309   -867   -125       C  
ATOM    341  CG2 ILE A  78      18.106 -10.804  12.845  1.00102.29           C  
ANISOU  341  CG2 ILE A  78    16347  12522   9998  -3141   -709     11       C  
ATOM    342  CD1 ILE A  78      18.718 -10.446  15.818  1.00109.72           C  
ANISOU  342  CD1 ILE A  78    17264  13685  10741  -3447   -936    -24       C  
ATOM    343  N   PHE A  79      14.905 -12.206  11.999  1.00105.55           N  
ANISOU  343  N   PHE A  79    17025  12402  10677  -2406   -567   -159       N  
ATOM    344  CA  PHE A  79      14.491 -12.815  10.740  1.00104.49           C  
ANISOU  344  CA  PHE A  79    16865  12218  10617  -2231   -485   -150       C  
ATOM    345  C   PHE A  79      13.284 -12.096  10.154  1.00100.36           C  
ANISOU  345  C   PHE A  79    16592  11444  10096  -2166   -481   -227       C  
ATOM    346  O   PHE A  79      13.209 -11.886   8.938  1.00105.22           O  
ANISOU  346  O   PHE A  79    17263  12003  10711  -2147   -439   -213       O  
ATOM    347  CB  PHE A  79      14.171 -14.293  10.949  1.00107.22           C  
ANISOU  347  CB  PHE A  79    17067  12631  11042  -2002   -439   -141       C  
ATOM    348  CG  PHE A  79      15.355 -15.124  11.347  1.00111.52           C  
ANISOU  348  CG  PHE A  79    17372  13432  11570  -1982   -417    -43       C  
ATOM    349  CD1 PHE A  79      16.436 -15.267  10.497  1.00108.58           C  
ANISOU  349  CD1 PHE A  79    16850  13237  11167  -2008   -360     52       C  
ATOM    350  CD2 PHE A  79      15.382 -15.769  12.573  1.00110.63           C  
ANISOU  350  CD2 PHE A  79    17177  13401  11455  -1910   -444    -33       C  
ATOM    351  CE1 PHE A  79      17.525 -16.033  10.862  1.00111.55           C  
ANISOU  351  CE1 PHE A  79    16984  13892  11507  -1940   -329    163       C  
ATOM    352  CE2 PHE A  79      16.468 -16.537  12.944  1.00116.16           C  
ANISOU  352  CE2 PHE A  79    17656  14360  12121  -1848   -421     74       C  
ATOM    353  CZ  PHE A  79      17.542 -16.669  12.087  1.00117.74           C  
ANISOU  353  CZ  PHE A  79    17692  14759  12286  -1850   -363    177       C  
ATOM    354  N   LEU A  80      12.326 -11.717  11.004  1.00 82.15           N  
ANISOU  354  N   LEU A  80    14433   9005   7776  -2107   -520   -296       N  
ATOM    355  CA  LEU A  80      11.145 -11.004  10.531  1.00 78.40           C  
ANISOU  355  CA  LEU A  80    14177   8332   7278  -1996   -512   -350       C  
ATOM    356  C   LEU A  80      11.495  -9.641   9.951  1.00 77.58           C  
ANISOU  356  C   LEU A  80    14312   8090   7073  -2146   -514   -342       C  
ATOM    357  O   LEU A  80      10.725  -9.106   9.146  1.00 77.75           O  
ANISOU  357  O   LEU A  80    14500   7973   7067  -2032   -489   -356       O  
ATOM    358  CB  LEU A  80      10.134 -10.851  11.668  1.00 82.84           C  
ANISOU  358  CB  LEU A  80    14837   8817   7822  -1881   -536   -409       C  
ATOM    359  CG  LEU A  80       9.006 -11.885  11.727  1.00 79.26           C  
ANISOU  359  CG  LEU A  80    14255   8412   7448  -1670   -512   -429       C  
ATOM    360  CD1 LEU A  80       9.557 -13.303  11.775  1.00 78.50           C  
ANISOU  360  CD1 LEU A  80    13924   8468   7435  -1671   -491   -395       C  
ATOM    361  CD2 LEU A  80       8.099 -11.619  12.919  1.00 75.04           C  
ANISOU  361  CD2 LEU A  80    13806   7830   6876  -1569   -523   -472       C  
ATOM    362  N   LEU A  81      12.633  -9.066  10.347  1.00 79.10           N  
ANISOU  362  N   LEU A  81    14532   8329   7194  -2409   -544   -314       N  
ATOM    363  CA  LEU A  81      13.108  -7.849   9.698  1.00 79.11           C  
ANISOU  363  CA  LEU A  81    14770   8202   7088  -2609   -535   -296       C  
ATOM    364  C   LEU A  81      13.613  -8.144   8.292  1.00 89.16           C  
ANISOU  364  C   LEU A  81    15918   9561   8397  -2620   -477   -228       C  
ATOM    365  O   LEU A  81      13.346  -7.380   7.356  1.00 92.73           O  
ANISOU  365  O   LEU A  81    16586   9853   8793  -2618   -442   -222       O  
ATOM    366  CB  LEU A  81      14.205  -7.199  10.539  1.00 79.50           C  
ANISOU  366  CB  LEU A  81    14869   8309   7029  -2949   -593   -282       C  
ATOM    367  CG  LEU A  81      14.820  -5.916   9.976  1.00 82.15           C  
ANISOU  367  CG  LEU A  81    15479   8508   7225  -3242   -583   -260       C  
ATOM    368  CD1 LEU A  81      13.916  -4.726  10.248  1.00 85.84           C  
ANISOU  368  CD1 LEU A  81    16426   8618   7570  -3193   -576   -334       C  
ATOM    369  CD2 LEU A  81      16.208  -5.682  10.553  1.00 83.82           C  
ANISOU  369  CD2 LEU A  81    15570   8929   7347  -3640   -644   -211       C  
ATOM    370  N   SER A  82      14.347  -9.247   8.125  1.00 94.78           N  
ANISOU  370  N   SER A  82    16303  10523   9186  -2607   -456   -170       N  
ATOM    371  CA  SER A  82      14.780  -9.654   6.792  1.00 92.97           C  
ANISOU  371  CA  SER A  82    15959  10381   8983  -2571   -383   -107       C  
ATOM    372  C   SER A  82      13.589 -10.017   5.916  1.00 87.75           C  
ANISOU  372  C   SER A  82    15384   9584   8373  -2310   -351   -151       C  
ATOM    373  O   SER A  82      13.549  -9.667   4.731  1.00 94.14           O  
ANISOU  373  O   SER A  82    16291  10329   9149  -2298   -307   -127       O  
ATOM    374  CB  SER A  82      15.753 -10.829   6.895  1.00 93.98           C  
ANISOU  374  CB  SER A  82    15746  10800   9162  -2547   -351    -32       C  
ATOM    375  OG  SER A  82      16.141 -11.287   5.612  1.00 94.99           O  
ANISOU  375  OG  SER A  82    15784  11006   9300  -2472   -262     28       O  
ATOM    376  N   LEU A  83      12.606 -10.721   6.485  1.00 75.63           N  
ANISOU  376  N   LEU A  83    13806   8026   6903  -2116   -375   -209       N  
ATOM    377  CA  LEU A  83      11.394 -11.044   5.741  1.00 73.19           C  
ANISOU  377  CA  LEU A  83    13557   7632   6620  -1907   -365   -249       C  
ATOM    378  C   LEU A  83      10.650  -9.786   5.313  1.00 76.75           C  
ANISOU  378  C   LEU A  83    14281   7896   6986  -1871   -378   -268       C  
ATOM    379  O   LEU A  83      10.027  -9.766   4.245  1.00 77.76           O  
ANISOU  379  O   LEU A  83    14467   7983   7094  -1749   -362   -265       O  
ATOM    380  CB  LEU A  83      10.488 -11.940   6.589  1.00 73.78           C  
ANISOU  380  CB  LEU A  83    13532   7740   6761  -1760   -391   -300       C  
ATOM    381  CG  LEU A  83       9.106 -12.288   6.031  1.00 76.67           C  
ANISOU  381  CG  LEU A  83    13925   8071   7137  -1582   -399   -340       C  
ATOM    382  CD1 LEU A  83       9.207 -13.404   5.004  1.00 79.32           C  
ANISOU  382  CD1 LEU A  83    14156   8479   7503  -1542   -360   -330       C  
ATOM    383  CD2 LEU A  83       8.152 -12.669   7.152  1.00 69.73           C  
ANISOU  383  CD2 LEU A  83    12994   7212   6287  -1490   -430   -383       C  
ATOM    384  N   ALA A  84      10.713  -8.727   6.121  1.00 84.86           N  
ANISOU  384  N   ALA A  84    15502   8801   7940  -1967   -404   -283       N  
ATOM    385  CA  ALA A  84      10.030  -7.485   5.778  1.00 85.23           C  
ANISOU  385  CA  ALA A  84    15870   8637   7877  -1896   -398   -292       C  
ATOM    386  C   ALA A  84      10.807  -6.663   4.760  1.00 86.71           C  
ANISOU  386  C   ALA A  84    16229   8736   7981  -2060   -357   -238       C  
ATOM    387  O   ALA A  84      10.208  -5.876   4.019  1.00 86.39           O  
ANISOU  387  O   ALA A  84    16435   8538   7853  -1945   -334   -225       O  
ATOM    388  CB  ALA A  84       9.782  -6.657   7.038  1.00 89.72           C  
ANISOU  388  CB  ALA A  84    16656   9066   8368  -1923   -424   -334       C  
ATOM    389  N   VAL A  85      12.131  -6.821   4.712  1.00 87.11           N  
ANISOU  389  N   VAL A  85    16149   8906   8042  -2318   -343   -193       N  
ATOM    390  CA  VAL A  85      12.925  -6.105   3.718  1.00 89.39           C  
ANISOU  390  CA  VAL A  85    16569   9147   8249  -2504   -293   -128       C  
ATOM    391  C   VAL A  85      12.701  -6.698   2.332  1.00 86.73           C  
ANISOU  391  C   VAL A  85    16130   8874   7948  -2341   -243    -94       C  
ATOM    392  O   VAL A  85      12.624  -5.970   1.334  1.00 89.61           O  
ANISOU  392  O   VAL A  85    16709   9113   8226  -2342   -202    -59       O  
ATOM    393  CB  VAL A  85      14.413  -6.119   4.119  1.00 90.06           C  
ANISOU  393  CB  VAL A  85    16491   9410   8318  -2841   -292    -74       C  
ATOM    394  CG1 VAL A  85      15.295  -5.716   2.947  1.00 83.12           C  
ANISOU  394  CG1 VAL A  85    15635   8572   7373  -3023   -221     14       C  
ATOM    395  CG2 VAL A  85      14.647  -5.193   5.303  1.00 78.64           C  
ANISOU  395  CG2 VAL A  85    15258   7848   6775  -3071   -348   -109       C  
ATOM    396  N   SER A  86      12.572  -8.024   2.246  1.00 87.55           N  
ANISOU  396  N   SER A  86    15945   9157   8162  -2199   -243   -106       N  
ATOM    397  CA  SER A  86      12.329  -8.658   0.954  1.00 90.95           C  
ANISOU  397  CA  SER A  86    16311   9638   8606  -2054   -200    -88       C  
ATOM    398  C   SER A  86      10.933  -8.338   0.434  1.00 89.87           C  
ANISOU  398  C   SER A  86    16348   9370   8427  -1831   -234   -126       C  
ATOM    399  O   SER A  86      10.743  -8.153  -0.774  1.00 97.55           O  
ANISOU  399  O   SER A  86    17417  10310   9339  -1763   -205    -97       O  
ATOM    400  CB  SER A  86      12.526 -10.170   1.063  1.00 89.12           C  
ANISOU  400  CB  SER A  86    15794   9592   8474  -1967   -185    -97       C  
ATOM    401  OG  SER A  86      11.511 -10.766   1.850  1.00 90.23           O  
ANISOU  401  OG  SER A  86    15881   9725   8676  -1823   -243   -168       O  
ATOM    402  N   ASP A  87       9.941  -8.272   1.327  1.00 85.95           N  
ANISOU  402  N   ASP A  87    15879   8830   7947  -1703   -292   -180       N  
ATOM    403  CA  ASP A  87       8.587  -7.935   0.899  1.00 89.22           C  
ANISOU  403  CA  ASP A  87    16416   9183   8301  -1468   -324   -196       C  
ATOM    404  C   ASP A  87       8.510  -6.514   0.359  1.00 92.25           C  
ANISOU  404  C   ASP A  87    17136   9369   8544  -1446   -296   -152       C  
ATOM    405  O   ASP A  87       7.723  -6.238  -0.554  1.00 94.35           O  
ANISOU  405  O   ASP A  87    17502   9615   8732  -1259   -302   -128       O  
ATOM    406  CB  ASP A  87       7.607  -8.117   2.058  1.00 94.13           C  
ANISOU  406  CB  ASP A  87    16978   9832   8957  -1333   -374   -246       C  
ATOM    407  CG  ASP A  87       7.454  -9.569   2.469  1.00100.99           C  
ANISOU  407  CG  ASP A  87    17552  10878   9943  -1331   -397   -285       C  
ATOM    408  OD1 ASP A  87       8.067 -10.441   1.818  1.00101.52           O  
ANISOU  408  OD1 ASP A  87    17489  11028  10055  -1404   -371   -276       O  
ATOM    409  OD2 ASP A  87       6.721  -9.837   3.445  1.00100.05           O  
ANISOU  409  OD2 ASP A  87    17357  10803   9855  -1249   -429   -320       O  
ATOM    410  N   LEU A  88       9.311  -5.600   0.907  1.00 87.48           N  
ANISOU  410  N   LEU A  88    16731   8620   7888  -1642   -268   -137       N  
ATOM    411  CA  LEU A  88       9.367  -4.245   0.374  1.00 87.58           C  
ANISOU  411  CA  LEU A  88    17129   8401   7745  -1662   -223    -91       C  
ATOM    412  C   LEU A  88      10.216  -4.178  -0.887  1.00 94.79           C  
ANISOU  412  C   LEU A  88    18059   9330   8625  -1809   -165    -26       C  
ATOM    413  O   LEU A  88       9.928  -3.378  -1.785  1.00100.83           O  
ANISOU  413  O   LEU A  88    19096   9949   9266  -1721   -128     22       O  
ATOM    414  CB  LEU A  88       9.910  -3.287   1.435  1.00 94.90           C  
ANISOU  414  CB  LEU A  88    18313   9145   8599  -1870   -213   -107       C  
ATOM    415  CG  LEU A  88       9.834  -1.788   1.139  1.00 96.33           C  
ANISOU  415  CG  LEU A  88    19001   9014   8587  -1884   -158    -71       C  
ATOM    416  CD1 LEU A  88       8.384  -1.342   1.016  1.00 96.67           C  
ANISOU  416  CD1 LEU A  88    19244   8947   8540  -1466   -156    -69       C  
ATOM    417  CD2 LEU A  88      10.554  -0.995   2.218  1.00 88.56           C  
ANISOU  417  CD2 LEU A  88    18269   7859   7521  -2182   -155    -99       C  
ATOM    418  N   MET A  89      11.262  -5.005  -0.968  1.00 95.01           N  
ANISOU  418  N   MET A  89    17809   9545   8747  -2007   -146    -12       N  
ATOM    419  CA  MET A  89      12.037  -5.111  -2.199  1.00 93.46           C  
ANISOU  419  CA  MET A  89    17580   9412   8520  -2108    -77     56       C  
ATOM    420  C   MET A  89      11.171  -5.608  -3.349  1.00 92.31           C  
ANISOU  420  C   MET A  89    17408   9305   8359  -1844    -82     55       C  
ATOM    421  O   MET A  89      11.313  -5.153  -4.489  1.00 99.98           O  
ANISOU  421  O   MET A  89    18539  10215   9234  -1837    -30    113       O  
ATOM    422  CB  MET A  89      13.225  -6.048  -1.982  1.00 93.55           C  
ANISOU  422  CB  MET A  89    17256   9663   8627  -2292    -47     79       C  
ATOM    423  CG  MET A  89      14.255  -6.044  -3.093  1.00 97.03           C  
ANISOU  423  CG  MET A  89    17654  10196   9017  -2433     49    168       C  
ATOM    424  SD  MET A  89      15.574  -7.229  -2.762  1.00103.19           S  
ANISOU  424  SD  MET A  89    18006  11311   9891  -2555     97    214       S  
ATOM    425  CE  MET A  89      16.762  -6.786  -4.025  1.00113.45           C  
ANISOU  425  CE  MET A  89    19320  12704  11082  -2748    228    341       C  
ATOM    426  N   LEU A  90      10.261  -6.539  -3.063  1.00 96.29           N  
ANISOU  426  N   LEU A  90    17721   9920   8943  -1646   -148     -7       N  
ATOM    427  CA  LEU A  90       9.395  -7.093  -4.096  1.00 97.85           C  
ANISOU  427  CA  LEU A  90    17877  10192   9111  -1438   -175    -16       C  
ATOM    428  C   LEU A  90       8.231  -6.166  -4.428  1.00 97.58           C  
ANISOU  428  C   LEU A  90    18078  10046   8953  -1217   -216      2       C  
ATOM    429  O   LEU A  90       7.718  -6.202  -5.552  1.00104.64           O  
ANISOU  429  O   LEU A  90    19019  10977   9761  -1079   -228     28       O  
ATOM    430  CB  LEU A  90       8.889  -8.469  -3.656  1.00 90.62           C  
ANISOU  430  CB  LEU A  90    16680   9446   8305  -1365   -230    -86       C  
ATOM    431  CG  LEU A  90       7.956  -9.265  -4.567  1.00 92.89           C  
ANISOU  431  CG  LEU A  90    16893   9844   8558  -1211   -279   -113       C  
ATOM    432  CD1 LEU A  90       8.296 -10.738  -4.488  1.00 99.51           C  
ANISOU  432  CD1 LEU A  90    17518  10806   9485  -1273   -265   -161       C  
ATOM    433  CD2 LEU A  90       6.515  -9.046  -4.148  1.00 93.19           C  
ANISOU  433  CD2 LEU A  90    16924   9922   8562  -1027   -372   -139       C  
ATOM    434  N   CYS A  91       7.804  -5.333  -3.479  1.00103.71           N  
ANISOU  434  N   CYS A  91    19012  10695   9697  -1158   -232     -5       N  
ATOM    435  CA  CYS A  91       6.699  -4.421  -3.745  1.00105.74           C  
ANISOU  435  CA  CYS A  91    19508  10856   9813   -887   -251     30       C  
ATOM    436  C   CYS A  91       7.172  -3.158  -4.455  1.00116.26           C  
ANISOU  436  C   CYS A  91    21231  11950  10992   -925   -174    106       C  
ATOM    437  O   CYS A  91       6.535  -2.705  -5.412  1.00118.17           O  
ANISOU  437  O   CYS A  91    21632  12166  11102   -711   -173    163       O  
ATOM    438  CB  CYS A  91       5.987  -4.063  -2.440  1.00111.19           C  
ANISOU  438  CB  CYS A  91    20241  11500  10506   -757   -279     -3       C  
ATOM    439  SG  CYS A  91       4.843  -2.669  -2.574  1.00120.64           S  
ANISOU  439  SG  CYS A  91    21818  12530  11488   -390   -259     64       S  
ATOM    440  N   LEU A  92       8.286  -2.579  -4.005  1.00118.99           N  
ANISOU  440  N   LEU A  92    21741  12134  11337  -1211   -110    115       N  
ATOM    441  CA  LEU A  92       8.768  -1.335  -4.595  1.00118.69           C  
ANISOU  441  CA  LEU A  92    22121  11841  11136  -1303    -27    188       C  
ATOM    442  C   LEU A  92       9.433  -1.574  -5.945  1.00116.64           C  
ANISOU  442  C   LEU A  92    21816  11651  10852  -1412     24    248       C  
ATOM    443  O   LEU A  92       9.111  -0.903  -6.931  1.00124.05           O  
ANISOU  443  O   LEU A  92    23022  12470  11642  -1272     62    317       O  
ATOM    444  CB  LEU A  92       9.743  -0.645  -3.638  1.00115.77           C  
ANISOU  444  CB  LEU A  92    21943  11295  10750  -1637     15    176       C  
ATOM    445  CG  LEU A  92       9.143   0.122  -2.460  1.00112.84           C  
ANISOU  445  CG  LEU A  92    21848  10721  10306  -1533      2    136       C  
ATOM    446  CD1 LEU A  92      10.246   0.754  -1.627  1.00115.30           C  
ANISOU  446  CD1 LEU A  92    22359  10871  10578  -1943     34    119       C  
ATOM    447  CD2 LEU A  92       8.168   1.179  -2.949  1.00112.91           C  
ANISOU  447  CD2 LEU A  92    22291  10494  10115  -1196     45    191       C  
ATOM    448  N   PHE A  93      10.355  -2.530  -6.009  1.00108.66           N  
ANISOU  448  N   PHE A  93    20479  10836   9970  -1631     36    232       N  
ATOM    449  CA  PHE A  93      11.210  -2.711  -7.174  1.00112.13           C  
ANISOU  449  CA  PHE A  93    20885  11343  10377  -1770    113    296       C  
ATOM    450  C   PHE A  93      10.642  -3.677  -8.206  1.00114.32           C  
ANISOU  450  C   PHE A  93    20971  11796  10668  -1549     83    285       C  
ATOM    451  O   PHE A  93      11.260  -3.859  -9.260  1.00116.62           O  
ANISOU  451  O   PHE A  93    21256  12141  10912  -1619    154    337       O  
ATOM    452  CB  PHE A  93      12.596  -3.203  -6.737  1.00109.55           C  
ANISOU  452  CB  PHE A  93    20310  11164  10149  -2101    163    305       C  
ATOM    453  CG  PHE A  93      13.380  -2.200  -5.936  1.00113.10           C  
ANISOU  453  CG  PHE A  93    20958  11469  10544  -2417    195    331       C  
ATOM    454  CD1 PHE A  93      12.997  -0.869  -5.888  1.00117.58           C  
ANISOU  454  CD1 PHE A  93    21989  11729  10957  -2421    214    354       C  
ATOM    455  CD2 PHE A  93      14.504  -2.594  -5.228  1.00113.94           C  
ANISOU  455  CD2 PHE A  93    20806  11754  10731  -2713    207    338       C  
ATOM    456  CE1 PHE A  93      13.721   0.049  -5.150  1.00123.33           C  
ANISOU  456  CE1 PHE A  93    22953  12299  11608  -2757    242    367       C  
ATOM    457  CE2 PHE A  93      15.231  -1.681  -4.488  1.00118.16           C  
ANISOU  457  CE2 PHE A  93    21518  12185  11194  -3055    220    359       C  
ATOM    458  CZ  PHE A  93      14.840  -0.358  -4.449  1.00127.00           C  
ANISOU  458  CZ  PHE A  93    23134  12966  12155  -3099    236    366       C  
ATOM    459  N   CYS A  94       9.495  -4.303  -7.943  1.00107.65           N  
ANISOU  459  N   CYS A  94    19979  11054   9870  -1306    -18    221       N  
ATOM    460  CA  CYS A  94       9.030  -5.363  -8.831  1.00100.83           C  
ANISOU  460  CA  CYS A  94    18921  10376   9013  -1171    -59    195       C  
ATOM    461  C   CYS A  94       7.541  -5.274  -9.145  1.00104.83           C  
ANISOU  461  C   CYS A  94    19467  10934   9431   -874   -162    185       C  
ATOM    462  O   CYS A  94       7.128  -5.558 -10.274  1.00111.41           O  
ANISOU  462  O   CYS A  94    20307  11855  10169   -761   -189    203       O  
ATOM    463  CB  CYS A  94       9.353  -6.729  -8.224  1.00104.22           C  
ANISOU  463  CB  CYS A  94    19012  10982   9603  -1260    -79    120       C  
ATOM    464  SG  CYS A  94      11.112  -7.008  -7.909  1.00112.84           S  
ANISOU  464  SG  CYS A  94    19974  12118  10782  -1556     40    155       S  
ATOM    465  N   MET A  95       6.726  -4.897  -8.161  1.00115.96           N  
ANISOU  465  N   MET A  95    20888  12318  10854   -742   -221    164       N  
ATOM    466  CA  MET A  95       5.284  -4.846  -8.388  1.00116.72           C  
ANISOU  466  CA  MET A  95    20957  12535  10855   -442   -318    173       C  
ATOM    467  C   MET A  95       4.872  -3.858  -9.476  1.00120.12           C  
ANISOU  467  C   MET A  95    21678  12882  11080   -238   -303    270       C  
ATOM    468  O   MET A  95       3.966  -4.196 -10.258  1.00121.23           O  
ANISOU  468  O   MET A  95    21721  13215  11124    -51   -387    287       O  
ATOM    469  CB  MET A  95       4.556  -4.538  -7.073  1.00120.81           C  
ANISOU  469  CB  MET A  95    21444  13048  11411   -315   -355    150       C  
ATOM    470  CG  MET A  95       3.082  -4.919  -7.084  1.00122.80           C  
ANISOU  470  CG  MET A  95    21499  13550  11608    -49   -466    149       C  
ATOM    471  SD  MET A  95       2.213  -4.427  -5.584  1.00127.53           S  
ANISOU  471  SD  MET A  95    22085  14152  12217    151   -478    145       S  
ATOM    472  CE  MET A  95       3.001  -5.484  -4.371  1.00123.69           C  
ANISOU  472  CE  MET A  95    21351  13679  11966   -166   -472     35       C  
ATOM    473  N   PRO A  96       5.450  -2.654  -9.586  1.00110.42           N  
ANISOU  473  N   PRO A  96    20816  11383   9757   -267   -203    340       N  
ATOM    474  CA  PRO A  96       5.087  -1.798 -10.732  1.00105.52           C  
ANISOU  474  CA  PRO A  96    20493  10676   8924    -61   -179    442       C  
ATOM    475  C   PRO A  96       5.430  -2.423 -12.073  1.00105.42           C  
ANISOU  475  C   PRO A  96    20396  10787   8872   -134   -181    455       C  
ATOM    476  O   PRO A  96       4.569  -2.498 -12.957  1.00105.61           O  
ANISOU  476  O   PRO A  96    20408  10960   8760     97   -254    494       O  
ATOM    477  CB  PRO A  96       5.882  -0.508 -10.469  1.00104.18           C  
ANISOU  477  CB  PRO A  96    20757  10151   8676   -182    -51    500       C  
ATOM    478  CG  PRO A  96       6.953  -0.901  -9.502  1.00106.45           C  
ANISOU  478  CG  PRO A  96    20900  10401   9145   -545    -13    427       C  
ATOM    479  CD  PRO A  96       6.309  -1.929  -8.635  1.00109.68           C  
ANISOU  479  CD  PRO A  96    20923  11042   9707   -472   -117    336       C  
ATOM    480  N   PHE A  97       6.663  -2.908 -12.241  1.00101.82           N  
ANISOU  480  N   PHE A  97    19868  10302   8517   -441   -102    428       N  
ATOM    481  CA  PHE A  97       7.112  -3.514 -13.497  1.00 97.09           C  
ANISOU  481  CA  PHE A  97    19217   9803   7871   -510    -75    441       C  
ATOM    482  C   PHE A  97       6.376  -4.810 -13.847  1.00 98.11           C  
ANISOU  482  C   PHE A  97    19044  10205   8027   -428   -193    363       C  
ATOM    483  O   PHE A  97       6.816  -5.520 -14.759  1.00 96.35           O  
ANISOU  483  O   PHE A  97    18769  10063   7778   -509   -167    349       O  
ATOM    484  CB  PHE A  97       8.617  -3.770 -13.435  1.00 97.59           C  
ANISOU  484  CB  PHE A  97    19234   9811   8034   -833     53    441       C  
ATOM    485  CG  PHE A  97       9.440  -2.517 -13.392  1.00 94.87           C  
ANISOU  485  CG  PHE A  97    19209   9221   7617   -991    174    529       C  
ATOM    486  CD1 PHE A  97       9.581  -1.729 -14.522  1.00104.25           C  
ANISOU  486  CD1 PHE A  97    20706  10283   8620   -947    249    629       C  
ATOM    487  CD2 PHE A  97      10.069  -2.125 -12.223  1.00 99.13           C  
ANISOU  487  CD2 PHE A  97    19761   9652   8251  -1206    212    514       C  
ATOM    488  CE1 PHE A  97      10.334  -0.574 -14.486  1.00108.22           C  
ANISOU  488  CE1 PHE A  97    21540  10541   9037  -1134    368    713       C  
ATOM    489  CE2 PHE A  97      10.824  -0.971 -12.182  1.00104.41           C  
ANISOU  489  CE2 PHE A  97    20753  10090   8828  -1410    318    591       C  
ATOM    490  CZ  PHE A  97      10.956  -0.195 -13.314  1.00108.76           C  
ANISOU  490  CZ  PHE A  97    21626  10502   9196  -1383    400    691       C  
ATOM    491  N   ASN A  98       5.292  -5.130 -13.147  1.00110.01           N  
ANISOU  491  N   ASN A  98    20372  11855   9572   -286   -315    315       N  
ATOM    492  CA  ASN A  98       4.439  -6.266 -13.459  1.00115.32           C  
ANISOU  492  CA  ASN A  98    20787  12795  10236   -237   -443    247       C  
ATOM    493  C   ASN A  98       3.029  -5.863 -13.860  1.00112.61           C  
ANISOU  493  C   ASN A  98    20441  12626   9720     49   -570    300       C  
ATOM    494  O   ASN A  98       2.386  -6.593 -14.619  1.00111.70           O  
ANISOU  494  O   ASN A  98    20191  12738   9511     72   -677    274       O  
ATOM    495  CB  ASN A  98       4.368  -7.224 -12.256  1.00115.13           C  
ANISOU  495  CB  ASN A  98    20481  12862  10403   -364   -481    147       C  
ATOM    496  CG  ASN A  98       3.574  -8.483 -12.551  1.00120.19           C  
ANISOU  496  CG  ASN A  98    20888  13753  11026   -388   -602     70       C  
ATOM    497  OD1 ASN A  98       2.352  -8.510 -12.403  1.00125.48           O  
ANISOU  497  OD1 ASN A  98    21428  14620  11627   -250   -726     74       O  
ATOM    498  ND2 ASN A  98       4.269  -9.536 -12.968  1.00121.98           N  
ANISOU  498  ND2 ASN A  98    21069  13981  11296   -569   -559      4       N  
ATOM    499  N   LEU A  99       2.538  -4.718 -13.384  1.00102.49           N  
ANISOU  499  N   LEU A  99    19318  11254   8371    272   -558    379       N  
ATOM    500  CA  LEU A  99       1.184  -4.268 -13.692  1.00104.90           C  
ANISOU  500  CA  LEU A  99    19601  11763   8493    606   -667    456       C  
ATOM    501  C   LEU A  99       1.145  -3.384 -14.937  1.00107.01           C  
ANISOU  501  C   LEU A  99    20172  11955   8533    799   -639    572       C  
ATOM    502  O   LEU A  99       0.413  -3.674 -15.888  1.00109.79           O  
ANISOU  502  O   LEU A  99    20433  12558   8725    926   -750    605       O  
ATOM    503  CB  LEU A  99       0.592  -3.520 -12.492  1.00105.82           C  
ANISOU  503  CB  LEU A  99    19745  11833   8627    816   -653    491       C  
ATOM    504  CG  LEU A  99      -0.602  -2.621 -12.829  1.00108.14           C  
ANISOU  504  CG  LEU A  99    20138  12264   8688   1251   -704    621       C  
ATOM    505  CD1 LEU A  99      -1.860  -3.451 -13.040  1.00114.29           C  
ANISOU  505  CD1 LEU A  99    20510  13516   9399   1360   -879    618       C  
ATOM    506  CD2 LEU A  99      -0.816  -1.567 -11.755  1.00104.42           C  
ANISOU  506  CD2 LEU A  99    19883  11594   8199   1478   -617    673       C  
ATOM    507  N   ILE A 100       1.922  -2.304 -14.942  1.00 98.84           N  
ANISOU  507  N   ILE A 100    19511  10579   7463    804   -495    639       N  
ATOM    508  CA  ILE A 100       1.873  -1.338 -16.038  1.00 94.94           C  
ANISOU  508  CA  ILE A 100    19366   9969   6736   1007   -448    766       C  
ATOM    509  C   ILE A 100       2.416  -1.938 -17.337  1.00 99.64           C  
ANISOU  509  C   ILE A 100    19954  10629   7277    843   -448    754       C  
ATOM    510  O   ILE A 100       1.945  -1.543 -18.414  1.00105.87           O  
ANISOU  510  O   ILE A 100    20891  11490   7844   1057   -484    846       O  
ATOM    511  CB  ILE A 100       2.574  -0.017 -15.651  1.00100.59           C  
ANISOU  511  CB  ILE A 100    20537  10270   7414   1010   -282    838       C  
ATOM    512  CG1 ILE A 100       2.660   0.947 -16.840  1.00114.19           C  
ANISOU  512  CG1 ILE A 100    22669  11828   8889   1180   -209    973       C  
ATOM    513  CG2 ILE A 100       3.939  -0.237 -15.016  1.00102.15           C  
ANISOU  513  CG2 ILE A 100    20742  10255   7816    590   -171    758       C  
ATOM    514  CD1 ILE A 100       3.129   2.337 -16.461  1.00116.80           C  
ANISOU  514  CD1 ILE A 100    23517  11736   9127   1216    -51   1056       C  
ATOM    515  N   PRO A 101       3.357  -2.898 -17.329  1.00 85.33           N  
ANISOU  515  N   PRO A 101    17982   8809   5630    505   -407    652       N  
ATOM    516  CA  PRO A 101       3.629  -3.602 -18.594  1.00 85.59           C  
ANISOU  516  CA  PRO A 101    17989   8956   5574    414   -423    635       C  
ATOM    517  C   PRO A 101       2.448  -4.425 -19.074  1.00 86.10           C  
ANISOU  517  C   PRO A 101    17804   9375   5535    532   -614    595       C  
ATOM    518  O   PRO A 101       2.207  -4.513 -20.285  1.00 87.62           O  
ANISOU  518  O   PRO A 101    18079   9678   5535    606   -664    632       O  
ATOM    519  CB  PRO A 101       4.838  -4.480 -18.247  1.00 83.44           C  
ANISOU  519  CB  PRO A 101    17585   8612   5507     73   -325    538       C  
ATOM    520  CG  PRO A 101       5.522  -3.722 -17.185  1.00 82.87           C  
ANISOU  520  CG  PRO A 101    17620   8303   5565    -27   -213    561       C  
ATOM    521  CD  PRO A 101       4.376  -3.267 -16.329  1.00 83.19           C  
ANISOU  521  CD  PRO A 101    17615   8398   5595    207   -315    571       C  
ATOM    522  N   ASN A 102       1.699  -5.033 -18.152  1.00100.90           N  
ANISOU  522  N   ASN A 102    19375  11445   7516    530   -727    524       N  
ATOM    523  CA  ASN A 102       0.528  -5.808 -18.547  1.00103.77           C  
ANISOU  523  CA  ASN A 102    19481  12183   7765    591   -919    491       C  
ATOM    524  C   ASN A 102      -0.595  -4.902 -19.032  1.00103.51           C  
ANISOU  524  C   ASN A 102    19503  12337   7489    961  -1017    628       C  
ATOM    525  O   ASN A 102      -1.280  -5.222 -20.011  1.00101.93           O  
ANISOU  525  O   ASN A 102    19228  12411   7088   1027  -1152    651       O  
ATOM    526  CB  ASN A 102       0.050  -6.674 -17.382  1.00106.63           C  
ANISOU  526  CB  ASN A 102    19508  12707   8300    465   -998    391       C  
ATOM    527  CG  ASN A 102       0.786  -7.994 -17.297  1.00113.00           C  
ANISOU  527  CG  ASN A 102    20209  13470   9256    125   -968    250       C  
ATOM    528  OD1 ASN A 102       0.262  -9.036 -17.691  1.00114.46           O  
ANISOU  528  OD1 ASN A 102    20235  13877   9376     -5  -1087    173       O  
ATOM    529  ND2 ASN A 102       2.007  -7.959 -16.775  1.00111.51           N  
ANISOU  529  ND2 ASN A 102    20120  13002   9246    -22   -806    221       N  
ATOM    530  N   LEU A 103      -0.801  -3.767 -18.359  1.00 97.02           N  
ANISOU  530  N   LEU A 103    18828  11377   6660   1216   -949    726       N  
ATOM    531  CA  LEU A 103      -1.851  -2.842 -18.771  1.00 94.88           C  
ANISOU  531  CA  LEU A 103    18637  11274   6138   1638  -1017    878       C  
ATOM    532  C   LEU A 103      -1.556  -2.227 -20.132  1.00 94.58           C  
ANISOU  532  C   LEU A 103    18928  11130   5878   1759   -977    978       C  
ATOM    533  O   LEU A 103      -2.486  -1.914 -20.883  1.00 97.23           O  
ANISOU  533  O   LEU A 103    19246  11734   5963   2056  -1090   1087       O  
ATOM    534  CB  LEU A 103      -2.027  -1.743 -17.724  1.00 98.68           C  
ANISOU  534  CB  LEU A 103    19290  11559   6646   1901   -917    957       C  
ATOM    535  CG  LEU A 103      -2.877  -2.086 -16.500  1.00 93.92           C  
ANISOU  535  CG  LEU A 103    18346  11194   6146   1978   -992    922       C  
ATOM    536  CD1 LEU A 103      -2.902  -0.916 -15.533  1.00102.69           C  
ANISOU  536  CD1 LEU A 103    19726  12035   7255   2245   -860    997       C  
ATOM    537  CD2 LEU A 103      -4.287  -2.474 -16.916  1.00103.37           C  
ANISOU  537  CD2 LEU A 103    19187  12931   7156   2199  -1187    985       C  
ATOM    538  N   LEU A 104      -0.278  -2.047 -20.463  1.00 99.05           N  
ANISOU  538  N   LEU A 104    19779  11337   6518   1539   -816    954       N  
ATOM    539  CA  LEU A 104       0.125  -1.510 -21.755  1.00 97.46           C  
ANISOU  539  CA  LEU A 104    19905  11011   6114   1610   -754   1047       C  
ATOM    540  C   LEU A 104       0.260  -2.579 -22.830  1.00 95.30           C  
ANISOU  540  C   LEU A 104    19495  10938   5775   1409   -839    971       C  
ATOM    541  O   LEU A 104       0.345  -2.233 -24.013  1.00105.87           O  
ANISOU  541  O   LEU A 104    21061  12265   6900   1510   -827   1051       O  
ATOM    542  CB  LEU A 104       1.458  -0.763 -21.625  1.00 94.66           C  
ANISOU  542  CB  LEU A 104    19926  10195   5845   1444   -526   1073       C  
ATOM    543  CG  LEU A 104       1.442   0.568 -20.872  1.00 95.85           C  
ANISOU  543  CG  LEU A 104    20403  10049   5967   1647   -411   1173       C  
ATOM    544  CD1 LEU A 104       2.811   1.227 -20.930  1.00 97.60           C  
ANISOU  544  CD1 LEU A 104    21001   9848   6236   1392   -200   1198       C  
ATOM    545  CD2 LEU A 104       0.377   1.488 -21.444  1.00 99.17           C  
ANISOU  545  CD2 LEU A 104    21029  10561   6091   2131   -465   1335       C  
ATOM    546  N   LYS A 105       0.282  -3.858 -22.447  1.00114.41           N  
ANISOU  546  N   LYS A 105    21592  13522   8357   1134   -917    819       N  
ATOM    547  CA  LYS A 105       0.526  -4.965 -23.374  1.00113.88           C  
ANISOU  547  CA  LYS A 105    21455  13583   8232    906   -973    723       C  
ATOM    548  C   LYS A 105       1.849  -4.791 -24.114  1.00113.12           C  
ANISOU  548  C   LYS A 105    21662  13186   8132    767   -780    736       C  
ATOM    549  O   LYS A 105       1.997  -5.225 -25.259  1.00118.55           O  
ANISOU  549  O   LYS A 105    22443  13943   8659    716   -798    723       O  
ATOM    550  CB  LYS A 105      -0.630  -5.133 -24.365  1.00116.50           C  
ANISOU  550  CB  LYS A 105    21699  14289   8276   1075  -1179    768       C  
ATOM    551  CG  LYS A 105      -1.972  -5.404 -23.705  1.00118.38           C  
ANISOU  551  CG  LYS A 105    21574  14914   8492   1184  -1378    766       C  
ATOM    552  CD  LYS A 105      -2.331  -6.879 -23.764  1.00120.62           C  
ANISOU  552  CD  LYS A 105    21572  15463   8795    865  -1529    611       C  
ATOM    553  CE  LYS A 105      -3.120  -7.304 -22.535  1.00125.57           C  
ANISOU  553  CE  LYS A 105    21834  16314   9564    819  -1628    565       C  
ATOM    554  NZ  LYS A 105      -4.550  -6.899 -22.619  1.00132.75           N  
ANISOU  554  NZ  LYS A 105    22502  17677  10259   1095  -1818    684       N  
ATOM    555  N   ASP A 106       2.818  -4.155 -23.458  1.00105.55           N  
ANISOU  555  N   ASP A 106    20856  11912   7338    691   -594    766       N  
ATOM    556  CA  ASP A 106       4.115  -3.872 -24.054  1.00107.20           C  
ANISOU  556  CA  ASP A 106    21325  11861   7545    544   -393    804       C  
ATOM    557  C   ASP A 106       5.084  -3.510 -22.938  1.00104.21           C  
ANISOU  557  C   ASP A 106    20962  11231   7402    363   -236    795       C  
ATOM    558  O   ASP A 106       4.718  -2.797 -22.001  1.00104.27           O  
ANISOU  558  O   ASP A 106    20992  11153   7474    465   -247    829       O  
ATOM    559  CB  ASP A 106       4.019  -2.732 -25.078  1.00110.75           C  
ANISOU  559  CB  ASP A 106    22136  12207   7737    767   -343    962       C  
ATOM    560  CG  ASP A 106       5.370  -2.342 -25.654  1.00114.14           C  
ANISOU  560  CG  ASP A 106    22839  12372   8156    593   -119   1020       C  
ATOM    561  OD1 ASP A 106       6.291  -3.185 -25.661  1.00114.83           O  
ANISOU  561  OD1 ASP A 106    22804  12453   8374    335    -27    936       O  
ATOM    562  OD2 ASP A 106       5.509  -1.185 -26.104  1.00118.49           O  
ANISOU  562  OD2 ASP A 106    23737  12732   8553    722    -24   1160       O  
ATOM    563  N   PHE A 107       6.315  -4.012 -23.044  1.00 92.48           N  
ANISOU  563  N   PHE A 107    19465   9649   6026    104    -88    755       N  
ATOM    564  CA  PHE A 107       7.358  -3.722 -22.060  1.00 89.90           C  
ANISOU  564  CA  PHE A 107    19123   9133   5901   -109     59    756       C  
ATOM    565  C   PHE A 107       8.169  -2.531 -22.564  1.00 98.64           C  
ANISOU  565  C   PHE A 107    20582   9999   6898   -158    232    893       C  
ATOM    566  O   PHE A 107       9.225  -2.667 -23.187  1.00 97.70           O  
ANISOU  566  O   PHE A 107    20524   9839   6758   -330    383    928       O  
ATOM    567  CB  PHE A 107       8.228  -4.950 -21.823  1.00 88.62           C  
ANISOU  567  CB  PHE A 107    18714   9052   5904   -342    124    654       C  
ATOM    568  CG  PHE A 107       8.905  -4.965 -20.482  1.00 96.50           C  
ANISOU  568  CG  PHE A 107    19555   9975   7136   -527    189    621       C  
ATOM    569  CD1 PHE A 107       8.180  -5.220 -19.330  1.00 95.07           C  
ANISOU  569  CD1 PHE A 107    19179   9852   7092   -487     65    545       C  
ATOM    570  CD2 PHE A 107      10.266  -4.728 -20.373  1.00 99.63           C  
ANISOU  570  CD2 PHE A 107    19981  10273   7599   -748    372    675       C  
ATOM    571  CE1 PHE A 107       8.797  -5.234 -18.094  1.00 95.04           C  
ANISOU  571  CE1 PHE A 107    19041   9785   7286   -654    117    515       C  
ATOM    572  CE2 PHE A 107      10.889  -4.743 -19.139  1.00 94.84           C  
ANISOU  572  CE2 PHE A 107    19214   9634   7185   -930    414    650       C  
ATOM    573  CZ  PHE A 107      10.154  -4.996 -17.999  1.00 95.85           C  
ANISOU  573  CZ  PHE A 107    19175   9796   7447   -878    284    566       C  
ATOM    574  N   ILE A 108       7.651  -1.332 -22.280  1.00103.27           N  
ANISOU  574  N   ILE A 108    21421  10421   7396      4    221    981       N  
ATOM    575  CA  ILE A 108       8.282  -0.108 -22.766  1.00102.69           C  
ANISOU  575  CA  ILE A 108    21758  10079   7179    -39    381   1119       C  
ATOM    576  C   ILE A 108       9.635   0.112 -22.100  1.00103.08           C  
ANISOU  576  C   ILE A 108    21813   9971   7380   -410    548   1125       C  
ATOM    577  O   ILE A 108      10.517   0.767 -22.670  1.00109.36           O  
ANISOU  577  O   ILE A 108    22864  10610   8076   -578    711   1227       O  
ATOM    578  CB  ILE A 108       7.339   1.094 -22.552  1.00100.94           C  
ANISOU  578  CB  ILE A 108    21854   9695   6805    259    335   1211       C  
ATOM    579  CG1 ILE A 108       7.926   2.366 -23.172  1.00115.02           C  
ANISOU  579  CG1 ILE A 108    24142  11165   8397    225    507   1361       C  
ATOM    580  CG2 ILE A 108       7.054   1.299 -21.070  1.00104.63           C  
ANISOU  580  CG2 ILE A 108    22229  10090   7435    249    292   1151       C  
ATOM    581  CD1 ILE A 108       8.113   2.292 -24.673  1.00115.41           C  
ANISOU  581  CD1 ILE A 108    24330  11274   8248    281    556   1439       C  
ATOM    582  N   PHE A 109       9.831  -0.434 -20.904  1.00 99.05           N  
ANISOU  582  N   PHE A 109    21014   9525   7096   -558    510   1025       N  
ATOM    583  CA  PHE A 109      11.099  -0.278 -20.213  1.00100.30           C  
ANISOU  583  CA  PHE A 109    21125   9596   7387   -918    645   1033       C  
ATOM    584  C   PHE A 109      12.194  -1.078 -20.920  1.00105.32           C  
ANISOU  584  C   PHE A 109    21572  10395   8051  -1114    765   1043       C  
ATOM    585  O   PHE A 109      11.931  -1.945 -21.759  1.00109.22           O  
ANISOU  585  O   PHE A 109    21945  11058   8496   -973    729   1006       O  
ATOM    586  CB  PHE A 109      10.961  -0.704 -18.753  1.00101.79           C  
ANISOU  586  CB  PHE A 109    21044   9838   7793   -991    560    926       C  
ATOM    587  CG  PHE A 109       9.770  -0.106 -18.059  1.00100.18           C  
ANISOU  587  CG  PHE A 109    20976   9529   7559   -740    441    909       C  
ATOM    588  CD1 PHE A 109       9.838   1.162 -17.508  1.00100.77           C  
ANISOU  588  CD1 PHE A 109    21414   9314   7559   -781    502    972       C  
ATOM    589  CD2 PHE A 109       8.582  -0.811 -17.961  1.00101.88           C  
ANISOU  589  CD2 PHE A 109    20969   9942   7799   -466    276    835       C  
ATOM    590  CE1 PHE A 109       8.745   1.717 -16.871  1.00105.57           C  
ANISOU  590  CE1 PHE A 109    22169   9826   8117   -500    415    965       C  
ATOM    591  CE2 PHE A 109       7.484  -0.261 -17.326  1.00100.40           C  
ANISOU  591  CE2 PHE A 109    20873   9706   7570   -207    182    837       C  
ATOM    592  CZ  PHE A 109       7.566   1.004 -16.780  1.00103.19           C  
ANISOU  592  CZ  PHE A 109    21595   9765   7848   -196    258    904       C  
ATOM    593  N   GLY A 110      13.439  -0.772 -20.569  1.00119.38           N  
ANISOU  593  N   GLY A 110    23333  12135   9890  -1443    912   1097       N  
ATOM    594  CA  GLY A 110      14.582  -1.317 -21.269  1.00123.23           C  
ANISOU  594  CA  GLY A 110    23670  12784  10367  -1617   1065   1148       C  
ATOM    595  C   GLY A 110      14.764  -2.810 -21.055  1.00116.91           C  
ANISOU  595  C   GLY A 110    22455  12248   9716  -1570   1033   1044       C  
ATOM    596  O   GLY A 110      14.020  -3.479 -20.337  1.00121.41           O  
ANISOU  596  O   GLY A 110    22841  12879  10411  -1441    886    926       O  
ATOM    597  N   SER A 111      15.792  -3.342 -21.719  1.00109.09           N  
ANISOU  597  N   SER A 111    21338  11418   8695  -1669   1190   1098       N  
ATOM    598  CA  SER A 111      16.139  -4.749 -21.569  1.00109.24           C  
ANISOU  598  CA  SER A 111    21017  11667   8824  -1612   1205   1020       C  
ATOM    599  C   SER A 111      16.944  -5.018 -20.306  1.00108.90           C  
ANISOU  599  C   SER A 111    20665  11743   8970  -1817   1234   1012       C  
ATOM    600  O   SER A 111      16.951  -6.155 -19.823  1.00114.09           O  
ANISOU  600  O   SER A 111    21058  12545   9746  -1728   1199    925       O  
ATOM    601  CB  SER A 111      16.923  -5.233 -22.790  1.00115.13           C  
ANISOU  601  CB  SER A 111    21764  12546   9434  -1582   1382   1092       C  
ATOM    602  OG  SER A 111      17.321  -6.584 -22.637  1.00118.14           O  
ANISOU  602  OG  SER A 111    21866  13125   9898  -1498   1425   1025       O  
ATOM    603  N   ALA A 112      17.618  -4.001 -19.764  1.00112.38           N  
ANISOU  603  N   ALA A 112    21154  12123   9422  -2099   1296   1102       N  
ATOM    604  CA  ALA A 112      18.389  -4.181 -18.541  1.00109.51           C  
ANISOU  604  CA  ALA A 112    20495  11899   9214  -2321   1306   1101       C  
ATOM    605  C   ALA A 112      17.504  -4.278 -17.306  1.00107.54           C  
ANISOU  605  C   ALA A 112    20197  11551   9113  -2253   1119    976       C  
ATOM    606  O   ALA A 112      17.930  -4.854 -16.300  1.00111.92           O  
ANISOU  606  O   ALA A 112    20457  12257   9812  -2335   1097    939       O  
ATOM    607  CB  ALA A 112      19.391  -3.038 -18.377  1.00110.44           C  
ANISOU  607  CB  ALA A 112    20700  11997   9266  -2702   1420   1237       C  
ATOM    608  N   VAL A 113      16.292  -3.729 -17.354  1.00 94.28           N  
ANISOU  608  N   VAL A 113    18791   9645   7386  -2088    992    921       N  
ATOM    609  CA  VAL A 113      15.385  -3.834 -16.217  1.00 94.64           C  
ANISOU  609  CA  VAL A 113    18783   9619   7555  -1993    827    810       C  
ATOM    610  C   VAL A 113      14.550  -5.111 -16.277  1.00 98.86           C  
ANISOU  610  C   VAL A 113    19125  10275   8161  -1726    721    693       C  
ATOM    611  O   VAL A 113      14.096  -5.598 -15.237  1.00103.02           O  
ANISOU  611  O   VAL A 113    19480  10837   8826  -1687    615    603       O  
ATOM    612  CB  VAL A 113      14.487  -2.590 -16.123  1.00 94.63           C  
ANISOU  612  CB  VAL A 113    19160   9341   7455  -1922    755    824       C  
ATOM    613  CG1 VAL A 113      15.335  -1.332 -16.008  1.00 94.90           C  
ANISOU  613  CG1 VAL A 113    19449   9210   7398  -2233    867    932       C  
ATOM    614  CG2 VAL A 113      13.575  -2.508 -17.324  1.00103.59           C  
ANISOU  614  CG2 VAL A 113    20508  10417   8434  -1639    719    837       C  
ATOM    615  N   CYS A 114      14.326  -5.661 -17.475  1.00 99.63           N  
ANISOU  615  N   CYS A 114    19272  10431   8150  -1564    746    692       N  
ATOM    616  CA  CYS A 114      13.752  -6.998 -17.577  1.00 93.12           C  
ANISOU  616  CA  CYS A 114    18277   9732   7371  -1386    668    581       C  
ATOM    617  C   CYS A 114      14.653  -8.032 -16.919  1.00 89.45           C  
ANISOU  617  C   CYS A 114    17513   9430   7044  -1468    745    556       C  
ATOM    618  O   CYS A 114      14.164  -9.030 -16.376  1.00 95.28           O  
ANISOU  618  O   CYS A 114    18101  10227   7874  -1376    661    452       O  
ATOM    619  CB  CYS A 114      13.504  -7.352 -19.045  1.00 99.15           C  
ANISOU  619  CB  CYS A 114    19193  10522   7958  -1238    699    590       C  
ATOM    620  SG  CYS A 114      13.084  -9.088 -19.384  1.00 97.36           S  
ANISOU  620  SG  CYS A 114    18832  10431   7731  -1090    649    458       S  
ATOM    621  N   LYS A 115      15.967  -7.806 -16.946  1.00 80.56           N  
ANISOU  621  N   LYS A 115    16296   8396   5918  -1639    907    661       N  
ATOM    622  CA  LYS A 115      16.900  -8.691 -16.262  1.00 87.89           C  
ANISOU  622  CA  LYS A 115    16918   9518   6958  -1690    988    667       C  
ATOM    623  C   LYS A 115      17.002  -8.369 -14.777  1.00 89.97           C  
ANISOU  623  C   LYS A 115    17023   9787   7373  -1846    908    648       C  
ATOM    624  O   LYS A 115      17.307  -9.258 -13.975  1.00 92.65           O  
ANISOU  624  O   LYS A 115    17117  10260   7825  -1818    905    612       O  
ATOM    625  CB  LYS A 115      18.283  -8.596 -16.909  1.00 89.96           C  
ANISOU  625  CB  LYS A 115    17095   9951   7136  -1799   1198    809       C  
ATOM    626  CG  LYS A 115      18.294  -8.851 -18.407  1.00 90.43           C  
ANISOU  626  CG  LYS A 115    17330  10006   7022  -1649   1303    840       C  
ATOM    627  CD  LYS A 115      19.683  -8.641 -18.988  1.00 85.82           C  
ANISOU  627  CD  LYS A 115    16644   9615   6347  -1768   1527   1001       C  
ATOM    628  CE  LYS A 115      19.743  -9.050 -20.450  1.00 92.18           C  
ANISOU  628  CE  LYS A 115    17619  10432   6972  -1585   1651   1027       C  
ATOM    629  NZ  LYS A 115      19.585 -10.519 -20.626  1.00 93.52           N  
ANISOU  629  NZ  LYS A 115    17730  10666   7137  -1320   1673    933       N  
ATOM    630  N   THR A 116      16.747  -7.116 -14.395  1.00123.80           N  
ANISOU  630  N   THR A 116    21480  13913  11645  -1998    848    674       N  
ATOM    631  CA  THR A 116      16.908  -6.707 -13.003  1.00123.66           C  
ANISOU  631  CA  THR A 116    21361  13884  11741  -2174    780    657       C  
ATOM    632  C   THR A 116      15.689  -7.076 -12.165  1.00123.03           C  
ANISOU  632  C   THR A 116    21273  13710  11762  -2008    613    527       C  
ATOM    633  O   THR A 116      15.829  -7.599 -11.053  1.00126.22           O  
ANISOU  633  O   THR A 116    21463  14202  12293  -2042    567    481       O  
ATOM    634  CB  THR A 116      17.170  -5.201 -12.926  1.00128.77           C  
ANISOU  634  CB  THR A 116    22260  14365  12301  -2422    800    735       C  
ATOM    635  OG1 THR A 116      18.327  -4.876 -13.706  1.00132.03           O  
ANISOU  635  OG1 THR A 116    22660  14895  12611  -2616    963    867       O  
ATOM    636  CG2 THR A 116      17.400  -4.774 -11.484  1.00129.02           C  
ANISOU  636  CG2 THR A 116    22218  14380  12423  -2634    731    711       C  
ATOM    637  N   THR A 117      14.486  -6.805 -12.677  1.00 97.61           N  
ANISOU  637  N   THR A 117    18272  10339   8475  -1822    523    478       N  
ATOM    638  CA  THR A 117      13.275  -7.108 -11.921  1.00 93.14           C  
ANISOU  638  CA  THR A 117    17675   9727   7986  -1667    370    372       C  
ATOM    639  C   THR A 117      13.126  -8.608 -11.700  1.00 97.92           C  
ANISOU  639  C   THR A 117    18033  10486   8685  -1564    343    288       C  
ATOM    640  O   THR A 117      12.865  -9.058 -10.579  1.00102.34           O  
ANISOU  640  O   THR A 117    18437  11081   9367  -1566    273    225       O  
ATOM    641  CB  THR A 117      12.047  -6.546 -12.638  1.00 87.72           C  
ANISOU  641  CB  THR A 117    17233   8919   7176  -1470    286    362       C  
ATOM    642  OG1 THR A 117      11.963  -7.107 -13.953  1.00 99.81           O  
ANISOU  642  OG1 THR A 117    18801  10519   8602  -1361    318    369       O  
ATOM    643  CG2 THR A 117      12.132  -5.031 -12.735  1.00 97.64           C  
ANISOU  643  CG2 THR A 117    18800   9973   8324  -1541    322    446       C  
ATOM    644  N   THR A 118      13.294  -9.401 -12.762  1.00 88.51           N  
ANISOU  644  N   THR A 118    16838   9370   7421  -1475    405    287       N  
ATOM    645  CA  THR A 118      13.206 -10.850 -12.618  1.00 93.02           C  
ANISOU  645  CA  THR A 118    17250  10044   8048  -1384    401    209       C  
ATOM    646  C   THR A 118      14.277 -11.384 -11.675  1.00 93.11           C  
ANISOU  646  C   THR A 118    17028  10173   8177  -1470    485    236       C  
ATOM    647  O   THR A 118      14.064 -12.400 -11.004  1.00 90.25           O  
ANISOU  647  O   THR A 118    16538   9856   7897  -1406    452    166       O  
ATOM    648  CB  THR A 118      13.319 -11.528 -13.984  1.00 86.99           C  
ANISOU  648  CB  THR A 118    16591   9313   7149  -1280    477    208       C  
ATOM    649  OG1 THR A 118      14.484 -11.047 -14.664  1.00 95.04           O  
ANISOU  649  OG1 THR A 118    17640  10374   8095  -1350    640    325       O  
ATOM    650  CG2 THR A 118      12.087 -11.232 -14.827  1.00 87.62           C  
ANISOU  650  CG2 THR A 118    16866   9322   7104  -1179    357    165       C  
ATOM    651  N   TYR A 119      15.430 -10.714 -11.608  1.00 82.84           N  
ANISOU  651  N   TYR A 119    15666   8939   6869  -1622    592    345       N  
ATOM    652  CA  TYR A 119      16.455 -11.098 -10.645  1.00 78.78           C  
ANISOU  652  CA  TYR A 119    14893   8590   6448  -1714    653    390       C  
ATOM    653  C   TYR A 119      15.990 -10.841  -9.217  1.00 88.56           C  
ANISOU  653  C   TYR A 119    16059   9781   7810  -1790    524    332       C  
ATOM    654  O   TYR A 119      16.193 -11.679  -8.331  1.00 90.78           O  
ANISOU  654  O   TYR A 119    16148  10162   8183  -1751    514    304       O  
ATOM    655  CB  TYR A 119      17.749 -10.339 -10.934  1.00 80.56           C  
ANISOU  655  CB  TYR A 119    15054   8944   6613  -1909    783    532       C  
ATOM    656  CG  TYR A 119      18.968 -10.874 -10.218  1.00 79.44           C  
ANISOU  656  CG  TYR A 119    14593   9069   6523  -1973    871    612       C  
ATOM    657  CD1 TYR A 119      19.035 -12.198  -9.804  1.00 76.54           C  
ANISOU  657  CD1 TYR A 119    14061   8807   6213  -1773    893    574       C  
ATOM    658  CD2 TYR A 119      20.056 -10.052  -9.960  1.00 84.23           C  
ANISOU  658  CD2 TYR A 119    15070   9836   7098  -2241    933    735       C  
ATOM    659  CE1 TYR A 119      20.153 -12.686  -9.152  1.00 81.58           C  
ANISOU  659  CE1 TYR A 119    14401   9718   6878  -1785    977    666       C  
ATOM    660  CE2 TYR A 119      21.176 -10.529  -9.309  1.00 80.78           C  
ANISOU  660  CE2 TYR A 119    14297   9708   6687  -2295   1002    825       C  
ATOM    661  CZ  TYR A 119      21.220 -11.845  -8.907  1.00 80.60           C  
ANISOU  661  CZ  TYR A 119    14102   9801   6723  -2040   1026    795       C  
ATOM    662  OH  TYR A 119      22.338 -12.318  -8.259  1.00 82.57           O  
ANISOU  662  OH  TYR A 119    14009  10384   6978  -2050   1098    904       O  
ATOM    663  N   PHE A 120      15.358  -9.690  -8.977  1.00120.17           N  
ANISOU  663  N   PHE A 120    20240  13620  11798  -1876    434    317       N  
ATOM    664  CA  PHE A 120      14.893  -9.361  -7.636  1.00121.08           C  
ANISOU  664  CA  PHE A 120    20326  13673  12005  -1934    323    262       C  
ATOM    665  C   PHE A 120      13.601 -10.087  -7.285  1.00117.55           C  
ANISOU  665  C   PHE A 120    19872  13176  11617  -1740    210    149       C  
ATOM    666  O   PHE A 120      13.356 -10.368  -6.106  1.00120.41           O  
ANISOU  666  O   PHE A 120    20120  13556  12076  -1747    145    100       O  
ATOM    667  CB  PHE A 120      14.701  -7.848  -7.499  1.00122.09           C  
ANISOU  667  CB  PHE A 120    20701  13622  12066  -2072    289    291       C  
ATOM    668  CG  PHE A 120      15.990  -7.070  -7.477  1.00124.96           C  
ANISOU  668  CG  PHE A 120    21064  14041  12376  -2360    380    396       C  
ATOM    669  CD1 PHE A 120      17.213  -7.720  -7.422  1.00126.50           C  
ANISOU  669  CD1 PHE A 120    20973  14492  12598  -2464    472    466       C  
ATOM    670  CD2 PHE A 120      15.976  -5.685  -7.512  1.00128.52           C  
ANISOU  670  CD2 PHE A 120    21807  14297  12727  -2529    380    434       C  
ATOM    671  CE1 PHE A 120      18.397  -7.004  -7.403  1.00128.09           C  
ANISOU  671  CE1 PHE A 120    21130  14805  12734  -2764    549    576       C  
ATOM    672  CE2 PHE A 120      17.156  -4.964  -7.492  1.00135.05           C  
ANISOU  672  CE2 PHE A 120    22647  15181  13486  -2856    459    531       C  
ATOM    673  CZ  PHE A 120      18.367  -5.625  -7.438  1.00134.73           C  
ANISOU  673  CZ  PHE A 120    22268  15446  13478  -2990    538    604       C  
ATOM    674  N   MET A 121      12.765 -10.395  -8.281  1.00 99.78           N  
ANISOU  674  N   MET A 121    17735  10882   9295  -1585    183    112       N  
ATOM    675  CA  MET A 121      11.559 -11.174  -8.017  1.00 97.13           C  
ANISOU  675  CA  MET A 121    17363  10548   8994  -1447     76     13       C  
ATOM    676  C   MET A 121      11.897 -12.579  -7.541  1.00 91.50           C  
ANISOU  676  C   MET A 121    16470   9934   8360  -1425    110    -30       C  
ATOM    677  O   MET A 121      11.179 -13.142  -6.707  1.00 89.11           O  
ANISOU  677  O   MET A 121    16089   9639   8129  -1391     30   -100       O  
ATOM    678  CB  MET A 121      10.683 -11.241  -9.269  1.00 99.97           C  
ANISOU  678  CB  MET A 121    17870  10884   9229  -1324     33     -8       C  
ATOM    679  CG  MET A 121      10.004  -9.933  -9.640  1.00 96.56           C  
ANISOU  679  CG  MET A 121    17631  10354   8703  -1270    -23     31       C  
ATOM    680  SD  MET A 121       9.068 -10.053 -11.176  1.00102.50           S  
ANISOU  680  SD  MET A 121    18529  11135   9281  -1118    -80     23       S  
ATOM    681  CE  MET A 121       8.469  -8.375 -11.353  1.00 99.21           C  
ANISOU  681  CE  MET A 121    18349  10593   8754  -1017   -119    102       C  
ATOM    682  N   GLY A 122      12.978 -13.160  -8.055  1.00 90.35           N  
ANISOU  682  N   GLY A 122    16273   9867   8189  -1427    239     21       N  
ATOM    683  CA  GLY A 122      13.375 -14.496  -7.664  1.00 89.74           C  
ANISOU  683  CA  GLY A 122    16075   9867   8157  -1360    298     -4       C  
ATOM    684  C   GLY A 122      14.124 -14.527  -6.349  1.00 95.20           C  
ANISOU  684  C   GLY A 122    16566  10651   8956  -1426    315     35       C  
ATOM    685  O   GLY A 122      13.960 -15.458  -5.555  1.00 97.03           O  
ANISOU  685  O   GLY A 122    16713  10903   9251  -1366    300     -9       O  
ATOM    686  N   THR A 123      14.954 -13.509  -6.109  1.00 87.57           N  
ANISOU  686  N   THR A 123    15534   9745   7993  -1570    344    121       N  
ATOM    687  CA  THR A 123      15.691 -13.440  -4.852  1.00 86.65           C  
ANISOU  687  CA  THR A 123    15221   9748   7955  -1670    340    163       C  
ATOM    688  C   THR A 123      14.754 -13.197  -3.675  1.00 85.49           C  
ANISOU  688  C   THR A 123    15091   9501   7892  -1698    203     80       C  
ATOM    689  O   THR A 123      14.970 -13.733  -2.582  1.00 86.00           O  
ANISOU  689  O   THR A 123    15006   9644   8027  -1693    184     72       O  
ATOM    690  CB  THR A 123      16.755 -12.343  -4.926  1.00 84.35           C  
ANISOU  690  CB  THR A 123    14879   9553   7617  -1880    390    272       C  
ATOM    691  OG1 THR A 123      17.565 -12.538  -6.092  1.00 85.35           O  
ANISOU  691  OG1 THR A 123    14986   9790   7655  -1844    530    359       O  
ATOM    692  CG2 THR A 123      17.645 -12.374  -3.691  1.00 89.92           C  
ANISOU  692  CG2 THR A 123    15347  10445   8375  -2004    383    326       C  
ATOM    693  N   SER A 124      13.700 -12.404  -3.885  1.00 83.22           N  
ANISOU  693  N   SER A 124    14984   9054   7580  -1700    115     27       N  
ATOM    694  CA  SER A 124      12.790 -12.066  -2.794  1.00 78.42           C  
ANISOU  694  CA  SER A 124    14400   8365   7030  -1700      3    -39       C  
ATOM    695  C   SER A 124      12.061 -13.297  -2.268  1.00 76.61           C  
ANISOU  695  C   SER A 124    14078   8164   6867  -1578    -37   -114       C  
ATOM    696  O   SER A 124      11.887 -13.450  -1.053  1.00 84.59           O  
ANISOU  696  O   SER A 124    15003   9190   7949  -1595    -84   -141       O  
ATOM    697  CB  SER A 124      11.786 -11.012  -3.258  1.00 74.45           C  
ANISOU  697  CB  SER A 124    14116   7713   6459  -1661    -62    -60       C  
ATOM    698  OG  SER A 124      10.820 -10.758  -2.254  1.00 84.88           O  
ANISOU  698  OG  SER A 124    15456   8977   7819  -1608   -154   -117       O  
ATOM    699  N   VAL A 125      11.621 -14.181  -3.165  1.00 78.35           N  
ANISOU  699  N   VAL A 125    14339   8381   7048  -1475    -17   -148       N  
ATOM    700  CA  VAL A 125      10.892 -15.368  -2.728  1.00 78.49           C  
ANISOU  700  CA  VAL A 125    14314   8405   7104  -1405    -50   -221       C  
ATOM    701  C   VAL A 125      11.827 -16.361  -2.052  1.00 75.91           C  
ANISOU  701  C   VAL A 125    13866   8150   6827  -1383     33   -194       C  
ATOM    702  O   VAL A 125      11.424 -17.069  -1.120  1.00 75.32           O  
ANISOU  702  O   VAL A 125    13738   8074   6808  -1362      4   -235       O  
ATOM    703  CB  VAL A 125      10.155 -16.009  -3.920  1.00 75.50           C  
ANISOU  703  CB  VAL A 125    14057   7995   6635  -1346    -60   -271       C  
ATOM    704  CG1 VAL A 125       9.263 -17.147  -3.447  1.00 73.68           C  
ANISOU  704  CG1 VAL A 125    13813   7761   6422  -1337   -108   -351       C  
ATOM    705  CG2 VAL A 125       9.342 -14.962  -4.662  1.00 70.58           C  
ANISOU  705  CG2 VAL A 125    13537   7341   5939  -1336   -139   -271       C  
ATOM    706  N   SER A 126      13.084 -16.429  -2.495  1.00 95.60           N  
ANISOU  706  N   SER A 126    16309  10727   9288  -1372    146   -111       N  
ATOM    707  CA  SER A 126      14.018 -17.395  -1.926  1.00 95.47           C  
ANISOU  707  CA  SER A 126    16167  10815   9291  -1294    239    -62       C  
ATOM    708  C   SER A 126      14.387 -17.038  -0.491  1.00 98.33           C  
ANISOU  708  C   SER A 126    16362  11265   9733  -1370    187    -32       C  
ATOM    709  O   SER A 126      14.419 -17.914   0.381  1.00104.17           O  
ANISOU  709  O   SER A 126    17037  12034  10510  -1295    197    -39       O  
ATOM    710  CB  SER A 126      15.268 -17.486  -2.798  1.00 97.81           C  
ANISOU  710  CB  SER A 126    16418  11233   9511  -1238    381     40       C  
ATOM    711  OG  SER A 126      15.782 -16.196  -3.071  1.00105.20           O  
ANISOU  711  OG  SER A 126    17306  12232  10432  -1390    370    105       O  
ATOM    712  N   VAL A 127      14.672 -15.760  -0.222  1.00 95.38           N  
ANISOU  712  N   VAL A 127    15950  10923   9367  -1529    135      1       N  
ATOM    713  CA  VAL A 127      15.000 -15.368   1.145  1.00 95.04           C  
ANISOU  713  CA  VAL A 127    15781  10955   9373  -1631     74     19       C  
ATOM    714  C   VAL A 127      13.770 -15.452   2.038  1.00 92.16           C  
ANISOU  714  C   VAL A 127    15485  10464   9069  -1606    -27    -78       C  
ATOM    715  O   VAL A 127      13.880 -15.788   3.223  1.00 97.99           O  
ANISOU  715  O   VAL A 127    16124  11257   9850  -1605    -56    -79       O  
ATOM    716  CB  VAL A 127      15.621 -13.958   1.184  1.00 97.82           C  
ANISOU  716  CB  VAL A 127    16134  11344   9688  -1849     46     72       C  
ATOM    717  CG1 VAL A 127      17.016 -13.969   0.583  1.00 99.81           C  
ANISOU  717  CG1 VAL A 127    16235  11809   9879  -1906    152    194       C  
ATOM    718  CG2 VAL A 127      14.733 -12.955   0.468  1.00 99.90           C  
ANISOU  718  CG2 VAL A 127    16632  11409   9917  -1891      0     21       C  
ATOM    719  N   SER A 128      12.585 -15.163   1.496  1.00 75.60           N  
ANISOU  719  N   SER A 128    13540   8223   6960  -1575    -79   -149       N  
ATOM    720  CA  SER A 128      11.377 -15.186   2.313  1.00 73.38           C  
ANISOU  720  CA  SER A 128    13292   7869   6720  -1544   -165   -225       C  
ATOM    721  C   SER A 128      11.026 -16.605   2.744  1.00 75.34           C  
ANISOU  721  C   SER A 128    13486   8135   7005  -1456   -145   -259       C  
ATOM    722  O   SER A 128      10.619 -16.826   3.890  1.00 84.54           O  
ANISOU  722  O   SER A 128    14600   9305   8215  -1455   -185   -285       O  
ATOM    723  CB  SER A 128      10.216 -14.550   1.550  1.00 70.01           C  
ANISOU  723  CB  SER A 128    13005   7347   6248  -1508   -221   -269       C  
ATOM    724  OG  SER A 128      10.472 -13.181   1.289  1.00 74.85           O  
ANISOU  724  OG  SER A 128    13727   7900   6814  -1575   -233   -235       O  
ATOM    725  N   THR A 129      11.176 -17.579   1.843  1.00 83.61           N  
ANISOU  725  N   THR A 129    14577   9176   8014  -1387    -73   -259       N  
ATOM    726  CA  THR A 129      10.912 -18.965   2.216  1.00 87.44           C  
ANISOU  726  CA  THR A 129    15080   9638   8507  -1318    -35   -289       C  
ATOM    727  C   THR A 129      11.945 -19.474   3.212  1.00 85.71           C  
ANISOU  727  C   THR A 129    14744   9504   8317  -1263     25   -224       C  
ATOM    728  O   THR A 129      11.596 -20.159   4.181  1.00 86.40           O  
ANISOU  728  O   THR A 129    14820   9573   8435  -1237     16   -244       O  
ATOM    729  CB  THR A 129      10.893 -19.859   0.976  1.00 85.11           C  
ANISOU  729  CB  THR A 129    14927   9282   8130  -1259     39   -309       C  
ATOM    730  OG1 THR A 129      12.079 -19.634   0.203  1.00 88.53           O  
ANISOU  730  OG1 THR A 129    15342   9775   8519  -1205    133   -233       O  
ATOM    731  CG2 THR A 129       9.672 -19.571   0.122  1.00 80.68           C  
ANISOU  731  CG2 THR A 129    14468   8664   7521  -1322    -44   -380       C  
ATOM    732  N   TRP A 130      13.218 -19.149   2.994  1.00101.98           N  
ANISOU  732  N   TRP A 130    16705  11685  10356  -1246     87   -134       N  
ATOM    733  CA  TRP A 130      14.281 -19.682   3.835  1.00105.37           C  
ANISOU  733  CA  TRP A 130    16990  12260  10786  -1167    146    -48       C  
ATOM    734  C   TRP A 130      14.501 -18.871   5.105  1.00105.90           C  
ANISOU  734  C   TRP A 130    16916  12423  10898  -1285     54    -29       C  
ATOM    735  O   TRP A 130      15.217 -19.336   5.999  1.00107.35           O  
ANISOU  735  O   TRP A 130    16969  12743  11077  -1225     75     36       O  
ATOM    736  CB  TRP A 130      15.580 -19.784   3.033  1.00106.27           C  
ANISOU  736  CB  TRP A 130    17019  12527  10832  -1086    263     60       C  
ATOM    737  CG  TRP A 130      15.569 -20.953   2.095  1.00110.41           C  
ANISOU  737  CG  TRP A 130    17705  12962  11285   -901    388     54       C  
ATOM    738  CD1 TRP A 130      15.218 -20.943   0.777  1.00108.65           C  
ANISOU  738  CD1 TRP A 130    17645  12629  11007   -898    424     11       C  
ATOM    739  CD2 TRP A 130      15.885 -22.314   2.415  1.00111.61           C  
ANISOU  739  CD2 TRP A 130    17920  13098  11387   -687    498     88       C  
ATOM    740  NE1 TRP A 130      15.315 -22.209   0.251  1.00112.02           N  
ANISOU  740  NE1 TRP A 130    18245  12969  11349   -714    549      8       N  
ATOM    741  CE2 TRP A 130      15.722 -23.069   1.238  1.00113.85           C  
ANISOU  741  CE2 TRP A 130    18435  13243  11581   -574    603     56       C  
ATOM    742  CE3 TRP A 130      16.299 -22.964   3.582  1.00107.93           C  
ANISOU  742  CE3 TRP A 130    17367  12715  10927   -570    523    146       C  
ATOM    743  CZ2 TRP A 130      15.958 -24.441   1.193  1.00118.96           C  
ANISOU  743  CZ2 TRP A 130    19264  13800  12135   -348    742     77       C  
ATOM    744  CZ3 TRP A 130      16.532 -24.326   3.536  1.00107.22           C  
ANISOU  744  CZ3 TRP A 130    17437  12549  10752   -326    661    178       C  
ATOM    745  CH2 TRP A 130      16.362 -25.050   2.349  1.00120.66           C  
ANISOU  745  CH2 TRP A 130    19405  14082  12358   -217    775    141       C  
ATOM    746  N   ASN A 131      13.916 -17.677   5.209  1.00 97.57           N  
ANISOU  746  N   ASN A 131    15907  11299   9866  -1437    -44    -80       N  
ATOM    747  CA  ASN A 131      13.836 -17.023   6.509  1.00 88.02           C  
ANISOU  747  CA  ASN A 131    14645  10117   8681  -1540   -134    -93       C  
ATOM    748  C   ASN A 131      12.667 -17.557   7.322  1.00 86.10           C  
ANISOU  748  C   ASN A 131    14466   9767   8482  -1477   -175   -169       C  
ATOM    749  O   ASN A 131      12.713 -17.537   8.557  1.00 98.85           O  
ANISOU  749  O   ASN A 131    16023  11425  10110  -1498   -217   -167       O  
ATOM    750  CB  ASN A 131      13.714 -15.508   6.345  1.00 90.02           C  
ANISOU  750  CB  ASN A 131    14983  10311   8911  -1709   -202   -112       C  
ATOM    751  CG  ASN A 131      15.024 -14.857   5.949  1.00 95.67           C  
ANISOU  751  CG  ASN A 131    15608  11171   9570  -1851   -174    -23       C  
ATOM    752  OD1 ASN A 131      15.044 -13.873   5.209  1.00 93.20           O  
ANISOU  752  OD1 ASN A 131    15407  10788   9218  -1965   -179    -21       O  
ATOM    753  ND2 ASN A 131      16.129 -15.409   6.438  1.00 96.78           N  
ANISOU  753  ND2 ASN A 131    15543  11536   9693  -1843   -141     65       N  
ATOM    754  N   LEU A 132      11.619 -18.040   6.650  1.00 62.67           N  
ANISOU  754  N   LEU A 132    11609   6681   5522  -1419   -165   -232       N  
ATOM    755  CA  LEU A 132      10.487 -18.632   7.350  1.00 66.43           C  
ANISOU  755  CA  LEU A 132    12123   7092   6027  -1387   -194   -293       C  
ATOM    756  C   LEU A 132      10.817 -20.002   7.925  1.00 75.17           C  
ANISOU  756  C   LEU A 132    13213   8215   7135  -1299   -125   -265       C  
ATOM    757  O   LEU A 132      10.140 -20.447   8.857  1.00 74.84           O  
ANISOU  757  O   LEU A 132    13180   8144   7112  -1295   -143   -294       O  
ATOM    758  CB  LEU A 132       9.284 -18.734   6.413  1.00 65.44           C  
ANISOU  758  CB  LEU A 132    12097   6884   5883  -1390   -214   -357       C  
ATOM    759  CG  LEU A 132       8.453 -17.460   6.254  1.00 59.98           C  
ANISOU  759  CG  LEU A 132    11438   6172   5181  -1423   -294   -388       C  
ATOM    760  CD1 LEU A 132       7.224 -17.722   5.397  1.00 67.32           C  
ANISOU  760  CD1 LEU A 132    12416   7088   6074  -1411   -324   -435       C  
ATOM    761  CD2 LEU A 132       8.058 -16.903   7.610  1.00 66.84           C  
ANISOU  761  CD2 LEU A 132    12274   7051   6072  -1428   -342   -400       C  
ATOM    762  N   VAL A 133      11.829 -20.686   7.388  1.00 83.36           N  
ANISOU  762  N   VAL A 133    14242   9296   8135  -1207    -32   -202       N  
ATOM    763  CA  VAL A 133      12.306 -21.914   8.012  1.00 85.02           C  
ANISOU  763  CA  VAL A 133    14460   9522   8321  -1075     49   -153       C  
ATOM    764  C   VAL A 133      13.351 -21.631   9.082  1.00 89.79           C  
ANISOU  764  C   VAL A 133    14885  10306   8925  -1045     33    -66       C  
ATOM    765  O   VAL A 133      13.576 -22.481   9.956  1.00 96.73           O  
ANISOU  765  O   VAL A 133    15758  11211   9785   -934     72    -24       O  
ATOM    766  CB  VAL A 133      12.883 -22.895   6.974  1.00 84.35           C  
ANISOU  766  CB  VAL A 133    14484   9399   8165   -932    179   -115       C  
ATOM    767  CG1 VAL A 133      11.857 -23.198   5.894  1.00 84.35           C  
ANISOU  767  CG1 VAL A 133    14680   9229   8139   -996    180   -209       C  
ATOM    768  CG2 VAL A 133      14.166 -22.348   6.371  1.00 96.25           C  
ANISOU  768  CG2 VAL A 133    15853  11077   9642   -883    223    -22       C  
ATOM    769  N   ALA A 134      13.995 -20.462   9.042  1.00 74.89           N  
ANISOU  769  N   ALA A 134    12867   8549   7040  -1157    -26    -34       N  
ATOM    770  CA  ALA A 134      14.942 -20.106  10.091  1.00 83.19           C  
ANISOU  770  CA  ALA A 134    13739   9800   8068  -1189    -68     43       C  
ATOM    771  C   ALA A 134      14.226 -19.837  11.408  1.00 85.66           C  
ANISOU  771  C   ALA A 134    14077  10061   8410  -1258   -158    -13       C  
ATOM    772  O   ALA A 134      14.733 -20.190  12.479  1.00 92.59           O  
ANISOU  772  O   ALA A 134    14860  11062   9258  -1210   -171     42       O  
ATOM    773  CB  ALA A 134      15.765 -18.891   9.666  1.00 87.94           C  
ANISOU  773  CB  ALA A 134    14229  10543   8643  -1357   -111     85       C  
ATOM    774  N   ILE A 135      13.046 -19.216  11.351  1.00 92.87           N  
ANISOU  774  N   ILE A 135    15115  10810   9363  -1349   -215   -114       N  
ATOM    775  CA  ILE A 135      12.275 -18.999  12.571  1.00 94.64           C  
ANISOU  775  CA  ILE A 135    15375  10985   9600  -1383   -278   -165       C  
ATOM    776  C   ILE A 135      11.699 -20.312  13.082  1.00 93.81           C  
ANISOU  776  C   ILE A 135    15316  10821   9508  -1260   -220   -169       C  
ATOM    777  O   ILE A 135      11.563 -20.505  14.296  1.00 98.34           O  
ANISOU  777  O   ILE A 135    15873  11421  10072  -1243   -243   -163       O  
ATOM    778  CB  ILE A 135      11.173 -17.948  12.339  1.00 87.80           C  
ANISOU  778  CB  ILE A 135    14622   9989   8750  -1466   -336   -252       C  
ATOM    779  CG1 ILE A 135      10.190 -18.416  11.265  1.00 90.44           C  
ANISOU  779  CG1 ILE A 135    15035  10218   9110  -1414   -298   -297       C  
ATOM    780  CG2 ILE A 135      11.779 -16.618  11.955  1.00 85.41           C  
ANISOU  780  CG2 ILE A 135    14337   9705   8411  -1600   -384   -244       C  
ATOM    781  CD1 ILE A 135       8.969 -17.540  11.135  1.00 92.52           C  
ANISOU  781  CD1 ILE A 135    15379  10402   9372  -1438   -349   -363       C  
ATOM    782  N   SER A 136      11.355 -21.235  12.180  1.00 75.44           N  
ANISOU  782  N   SER A 136    13076   8401   7185  -1188   -142   -180       N  
ATOM    783  CA  SER A 136      10.875 -22.542  12.614  1.00 75.74           C  
ANISOU  783  CA  SER A 136    13212   8356   7211  -1104    -73   -180       C  
ATOM    784  C   SER A 136      11.978 -23.324  13.313  1.00 81.49           C  
ANISOU  784  C   SER A 136    13892   9180   7890   -954    -12    -79       C  
ATOM    785  O   SER A 136      11.736 -23.970  14.339  1.00 76.34           O  
ANISOU  785  O   SER A 136    13281   8504   7220   -902      6    -62       O  
ATOM    786  CB  SER A 136      10.336 -23.326  11.419  1.00 72.21           C  
ANISOU  786  CB  SER A 136    12916   7773   6747  -1097     -5   -219       C  
ATOM    787  OG  SER A 136      11.394 -23.907  10.677  1.00 73.30           O  
ANISOU  787  OG  SER A 136    13085   7929   6836   -968     87   -154       O  
ATOM    788  N   LEU A 137      13.198 -23.276  12.772  1.00 91.03           N  
ANISOU  788  N   LEU A 137    15004  10521   9063   -869     25      3       N  
ATOM    789  CA  LEU A 137      14.327 -23.909  13.443  1.00 95.20           C  
ANISOU  789  CA  LEU A 137    15436  11213   9523   -693     77    125       C  
ATOM    790  C   LEU A 137      14.681 -23.189  14.737  1.00 95.65           C  
ANISOU  790  C   LEU A 137    15328  11443   9573   -773    -33    153       C  
ATOM    791  O   LEU A 137      15.140 -23.824  15.693  1.00 94.51           O  
ANISOU  791  O   LEU A 137    15141  11397   9371   -639    -14    232       O  
ATOM    792  CB  LEU A 137      15.538 -23.949  12.511  1.00 91.61           C  
ANISOU  792  CB  LEU A 137    14872  10918   9016   -579    147    221       C  
ATOM    793  CG  LEU A 137      15.531 -25.018  11.418  1.00 80.16           C  
ANISOU  793  CG  LEU A 137    13617   9320   7519   -402    296    230       C  
ATOM    794  CD1 LEU A 137      16.862 -25.030  10.685  1.00 90.58           C  
ANISOU  794  CD1 LEU A 137    14790  10858   8767   -244    380    353       C  
ATOM    795  CD2 LEU A 137      15.222 -26.389  12.001  1.00 90.53           C  
ANISOU  795  CD2 LEU A 137    15143  10478   8776   -223    394    249       C  
ATOM    796  N   GLU A 138      14.476 -21.871  14.786  1.00 98.20           N  
ANISOU  796  N   GLU A 138    15588  11793   9931   -984   -145     92       N  
ATOM    797  CA  GLU A 138      14.745 -21.121  16.008  1.00101.95           C  
ANISOU  797  CA  GLU A 138    15964  12398  10374  -1095   -255     99       C  
ATOM    798  C   GLU A 138      13.757 -21.494  17.105  1.00100.08           C  
ANISOU  798  C   GLU A 138    15842  12035  10150  -1070   -267     46       C  
ATOM    799  O   GLU A 138      14.151 -21.756  18.248  1.00 99.94           O  
ANISOU  799  O   GLU A 138    15766  12132  10074  -1019   -294     99       O  
ATOM    800  CB  GLU A 138      14.698 -19.619  15.721  1.00 98.19           C  
ANISOU  800  CB  GLU A 138    15481  11919   9908  -1329   -352     37       C  
ATOM    801  CG  GLU A 138      15.109 -18.735  16.892  1.00111.74           C  
ANISOU  801  CG  GLU A 138    17139  13760  11556  -1487   -469     39       C  
ATOM    802  CD  GLU A 138      13.946 -18.384  17.803  1.00110.44           C  
ANISOU  802  CD  GLU A 138    17137  13421  11405  -1520   -512    -61       C  
ATOM    803  OE1 GLU A 138      12.799 -18.323  17.310  1.00103.77           O  
ANISOU  803  OE1 GLU A 138    16427  12377  10624  -1492   -476   -140       O  
ATOM    804  OE2 GLU A 138      14.177 -18.169  19.012  1.00106.09           O  
ANISOU  804  OE2 GLU A 138    16567  12956  10785  -1569   -580    -53       O  
ATOM    805  N   ARG A 139      12.463 -21.524  16.776  1.00 90.57           N  
ANISOU  805  N   ARG A 139    14786  10622   9005  -1106   -246    -50       N  
ATOM    806  CA  ARG A 139      11.453 -21.877  17.765  1.00 87.94           C  
ANISOU  806  CA  ARG A 139    14543  10193   8677  -1095   -243    -93       C  
ATOM    807  C   ARG A 139      11.534 -23.341  18.178  1.00 91.52           C  
ANISOU  807  C   ARG A 139    15063  10614   9098   -938   -145    -29       C  
ATOM    808  O   ARG A 139      11.089 -23.685  19.278  1.00 95.76           O  
ANISOU  808  O   ARG A 139    15646  11130   9610   -916   -142    -26       O  
ATOM    809  CB  ARG A 139      10.056 -21.561  17.227  1.00 81.23           C  
ANISOU  809  CB  ARG A 139    13791   9192   7882  -1173   -242   -190       C  
ATOM    810  CG  ARG A 139       9.815 -20.086  16.935  1.00 76.20           C  
ANISOU  810  CG  ARG A 139    13146   8551   7255  -1285   -325   -249       C  
ATOM    811  CD  ARG A 139       9.413 -19.326  18.188  1.00 89.87           C  
ANISOU  811  CD  ARG A 139    14906  10292   8948  -1322   -383   -282       C  
ATOM    812  NE  ARG A 139      10.567 -18.971  19.007  1.00 95.31           N  
ANISOU  812  NE  ARG A 139    15537  11105   9573  -1363   -443   -236       N  
ATOM    813  CZ  ARG A 139      10.532 -18.816  20.323  1.00 90.46           C  
ANISOU  813  CZ  ARG A 139    14944  10528   8898  -1368   -481   -239       C  
ATOM    814  NH1 ARG A 139       9.413 -18.979  21.009  1.00 85.65           N  
ANISOU  814  NH1 ARG A 139    14414   9840   8290  -1316   -450   -279       N  
ATOM    815  NH2 ARG A 139      11.649 -18.490  20.967  1.00 90.46           N  
ANISOU  815  NH2 ARG A 139    14875  10674   8821  -1436   -553   -193       N  
ATOM    816  N   TYR A 140      12.087 -24.207  17.328  1.00 83.77           N  
ANISOU  816  N   TYR A 140    14120   9611   8098   -817    -53     25       N  
ATOM    817  CA  TYR A 140      12.258 -25.605  17.709  1.00 86.64           C  
ANISOU  817  CA  TYR A 140    14608   9911   8400   -638     58     96       C  
ATOM    818  C   TYR A 140      13.377 -25.758  18.730  1.00 95.57           C  
ANISOU  818  C   TYR A 140    15612  11250   9452   -488     42    215       C  
ATOM    819  O   TYR A 140      13.226 -26.467  19.732  1.00 99.10           O  
ANISOU  819  O   TYR A 140    16142  11667   9846   -393     78    257       O  
ATOM    820  CB  TYR A 140      12.537 -26.460  16.472  1.00 85.48           C  
ANISOU  820  CB  TYR A 140    14593   9658   8227   -525    176    119       C  
ATOM    821  CG  TYR A 140      13.091 -27.831  16.791  1.00 79.11           C  
ANISOU  821  CG  TYR A 140    13940   8800   7318   -276    310    222       C  
ATOM    822  CD1 TYR A 140      12.258 -28.854  17.227  1.00 83.69           C  
ANISOU  822  CD1 TYR A 140    14778   9160   7862   -274    391    201       C  
ATOM    823  CD2 TYR A 140      14.447 -28.102  16.661  1.00 81.16           C  
ANISOU  823  CD2 TYR A 140    14096   9242   7498    -35    365    353       C  
ATOM    824  CE1 TYR A 140      12.760 -30.108  17.522  1.00 86.75           C  
ANISOU  824  CE1 TYR A 140    15369   9459   8132    -29    529    300       C  
ATOM    825  CE2 TYR A 140      14.958 -29.352  16.955  1.00 87.35           C  
ANISOU  825  CE2 TYR A 140    15047   9978   8165    251    503    462       C  
ATOM    826  CZ  TYR A 140      14.110 -30.351  17.385  1.00 93.48           C  
ANISOU  826  CZ  TYR A 140    16133  10482   8903    258    588    432       C  
ATOM    827  OH  TYR A 140      14.614 -31.599  17.678  1.00 96.39           O  
ANISOU  827  OH  TYR A 140    16730  10761   9132    559    740    546       O  
ATOM    828  N   GLY A 141      14.513 -25.098  18.492  1.00111.66           N  
ANISOU  828  N   GLY A 141    17439  13523  11464   -478    -14    279       N  
ATOM    829  CA  GLY A 141      15.627 -25.201  19.417  1.00116.75           C  
ANISOU  829  CA  GLY A 141    17912  14437  12011   -352    -48    405       C  
ATOM    830  C   GLY A 141      15.377 -24.506  20.740  1.00119.36           C  
ANISOU  830  C   GLY A 141    18187  14843  12323   -492   -174    371       C  
ATOM    831  O   GLY A 141      15.944 -24.895  21.764  1.00129.08           O  
ANISOU  831  O   GLY A 141    19350  16237  13459   -371   -192    464       O  
ATOM    832  N   ALA A 142      14.528 -23.478  20.743  1.00110.77           N  
ANISOU  832  N   ALA A 142    17143  13641  11305   -724   -256    243       N  
ATOM    833  CA  ALA A 142      14.245 -22.747  21.971  1.00109.88           C  
ANISOU  833  CA  ALA A 142    17025  13571  11155   -849   -363    199       C  
ATOM    834  C   ALA A 142      13.185 -23.424  22.830  1.00110.13           C  
ANISOU  834  C   ALA A 142    17223  13431  11189   -784   -307    167       C  
ATOM    835  O   ALA A 142      13.124 -23.157  24.035  1.00116.00           O  
ANISOU  835  O   ALA A 142    17969  14238  11868   -811   -369    166       O  
ATOM    836  CB  ALA A 142      13.804 -21.318  21.646  1.00107.55           C  
ANISOU  836  CB  ALA A 142    16749  13212  10902  -1087   -454     86       C  
ATOM    837  N   ILE A 143      12.360 -24.290  22.248  1.00 97.06           N  
ANISOU  837  N   ILE A 143    15716  11572   9592   -720   -192    141       N  
ATOM    838  CA  ILE A 143      11.269 -24.950  22.963  1.00 94.07           C  
ANISOU  838  CA  ILE A 143    15494  11036   9211   -706   -127    113       C  
ATOM    839  C   ILE A 143      11.545 -26.439  23.150  1.00101.26           C  
ANISOU  839  C   ILE A 143    16534  11882  10060   -511     -2    212       C  
ATOM    840  O   ILE A 143      11.535 -26.945  24.274  1.00103.17           O  
ANISOU  840  O   ILE A 143    16834  12139  10227   -425     19    267       O  
ATOM    841  CB  ILE A 143       9.917 -24.718  22.252  1.00 85.86           C  
ANISOU  841  CB  ILE A 143    14540   9823   8260   -845   -101      4       C  
ATOM    842  CG1 ILE A 143       9.563 -23.230  22.239  1.00 84.83           C  
ANISOU  842  CG1 ILE A 143    14332   9737   8161   -984   -207    -81       C  
ATOM    843  CG2 ILE A 143       8.823 -25.534  22.918  1.00 79.24           C  
ANISOU  843  CG2 ILE A 143    13839   8862   7405   -855    -19     -5       C  
ATOM    844  CD1 ILE A 143       8.368 -22.899  21.373  1.00 80.46           C  
ANISOU  844  CD1 ILE A 143    13820   9074   7679  -1078   -189   -167       C  
ATOM    845  N   CYS A 144      11.795 -27.160  22.056  1.00118.75           N  
ANISOU  845  N   CYS A 144    18830  14006  12285   -426     90    237       N  
ATOM    846  CA  CYS A 144      11.885 -28.614  22.130  1.00117.83           C  
ANISOU  846  CA  CYS A 144    18932  13748  12089   -241    236    316       C  
ATOM    847  C   CYS A 144      13.200 -29.077  22.748  1.00121.27           C  
ANISOU  847  C   CYS A 144    19297  14372  12408     32    256    469       C  
ATOM    848  O   CYS A 144      13.216 -30.044  23.517  1.00129.15           O  
ANISOU  848  O   CYS A 144    20461  15298  13311    196    343    550       O  
ATOM    849  CB  CYS A 144      11.706 -29.220  20.739  1.00118.34           C  
ANISOU  849  CB  CYS A 144    19158  13631  12173   -236    336    285       C  
ATOM    850  SG  CYS A 144      10.027 -29.077  20.084  1.00125.62           S  
ANISOU  850  SG  CYS A 144    20201  14343  13185   -540    332    132       S  
ATOM    851  N   LYS A 145      14.308 -28.412  22.428  1.00105.15           N  
ANISOU  851  N   LYS A 145    17007  12591  10356     86    180    524       N  
ATOM    852  CA  LYS A 145      15.624 -28.764  22.963  1.00114.01           C  
ANISOU  852  CA  LYS A 145    17986  13984  11350    347    183    688       C  
ATOM    853  C   LYS A 145      16.348 -27.505  23.434  1.00124.16           C  
ANISOU  853  C   LYS A 145    18944  15607  12625    202      2    699       C  
ATOM    854  O   LYS A 145      17.341 -27.074  22.834  1.00131.48           O  
ANISOU  854  O   LYS A 145    19647  16780  13530    222    -35    762       O  
ATOM    855  CB  LYS A 145      16.439 -29.542  21.927  1.00114.01           C  
ANISOU  855  CB  LYS A 145    18027  13999  11291    609    317    789       C  
ATOM    856  CG  LYS A 145      16.602 -28.861  20.571  1.00118.18           C  
ANISOU  856  CG  LYS A 145    18443  14553  11907    480    299    725       C  
ATOM    857  CD  LYS A 145      17.354 -29.752  19.594  1.00123.82           C  
ANISOU  857  CD  LYS A 145    19246  15260  12540    779    461    829       C  
ATOM    858  CE  LYS A 145      18.802 -29.933  20.015  1.00134.42           C  
ANISOU  858  CE  LYS A 145    20334  16998  13743   1079    470   1028       C  
ATOM    859  NZ  LYS A 145      19.571 -30.749  19.036  1.00133.53           N  
ANISOU  859  NZ  LYS A 145    20297  16907  13533   1418    647   1143       N  
ATOM    860  N   PRO A 146      15.887 -26.901  24.535  1.00128.39           N  
ANISOU  860  N   PRO A 146    19461  16166  13154     41   -107    642       N  
ATOM    861  CA  PRO A 146      16.517 -25.664  25.022  1.00128.94           C  
ANISOU  861  CA  PRO A 146    19285  16518  13188   -147   -285    633       C  
ATOM    862  C   PRO A 146      17.919 -25.856  25.579  1.00137.02           C  
ANISOU  862  C   PRO A 146    20066  17938  14056     16   -341    804       C  
ATOM    863  O   PRO A 146      18.556 -24.863  25.952  1.00139.05           O  
ANISOU  863  O   PRO A 146    20109  18468  14255   -178   -499    807       O  
ATOM    864  CB  PRO A 146      15.555 -25.194  26.129  1.00121.36           C  
ANISOU  864  CB  PRO A 146    18448  15432  12231   -306   -352    532       C  
ATOM    865  CG  PRO A 146      14.287 -25.977  25.916  1.00116.62           C  
ANISOU  865  CG  PRO A 146    18108  14491  11713   -263   -214    467       C  
ATOM    866  CD  PRO A 146      14.740 -27.290  25.370  1.00121.55           C  
ANISOU  866  CD  PRO A 146    18818  15067  12300      2    -68    579       C  
ATOM    867  N   LEU A 147      18.425 -27.087  25.647  1.00137.82           N  
ANISOU  867  N   LEU A 147    20205  18093  14069    364   -218    952       N  
ATOM    868  CA  LEU A 147      19.719 -27.351  26.264  1.00143.55           C  
ANISOU  868  CA  LEU A 147    20681  19241  14621    576   -266   1141       C  
ATOM    869  C   LEU A 147      20.875 -27.265  25.272  1.00151.26           C  
ANISOU  869  C   LEU A 147    21386  20525  15561    679   -246   1257       C  
ATOM    870  O   LEU A 147      21.944 -26.751  25.615  1.00151.16           O  
ANISOU  870  O   LEU A 147    21035  20965  15433    635   -371   1365       O  
ATOM    871  CB  LEU A 147      19.716 -28.731  26.930  1.00140.21           C  
ANISOU  871  CB  LEU A 147    20452  18737  14085    958   -131   1268       C  
ATOM    872  CG  LEU A 147      19.195 -28.848  28.367  1.00133.57           C  
ANISOU  872  CG  LEU A 147    19737  17840  13175    934   -187   1254       C  
ATOM    873  CD1 LEU A 147      20.044 -28.015  29.317  1.00127.63           C  
ANISOU  873  CD1 LEU A 147    18671  17529  12292    814   -395   1314       C  
ATOM    874  CD2 LEU A 147      17.723 -28.468  28.476  1.00128.83           C  
ANISOU  874  CD2 LEU A 147    19386  16844  12718    651   -183   1054       C  
ATOM    875  N   GLN A 148      20.684 -27.758  24.048  1.00193.18           N  
ANISOU  875  N   GLN A 148    26831  25618  20949    800    -91   1240       N  
ATOM    876  CA  GLN A 148      21.760 -27.855  23.069  1.00195.72           C  
ANISOU  876  CA  GLN A 148    26929  26216  21221    967    -28   1367       C  
ATOM    877  C   GLN A 148      21.600 -26.866  21.919  1.00198.38           C  
ANISOU  877  C   GLN A 148    27193  26492  21690    657    -68   1247       C  
ATOM    878  O   GLN A 148      22.222 -27.040  20.866  1.00197.15           O  
ANISOU  878  O   GLN A 148    26939  26448  21520    792     28   1321       O  
ATOM    879  CB  GLN A 148      21.851 -29.282  22.524  1.00195.69           C  
ANISOU  879  CB  GLN A 148    27166  26034  21154   1416    207   1471       C  
ATOM    880  CG  GLN A 148      21.712 -30.369  23.579  1.00197.12           C  
ANISOU  880  CG  GLN A 148    27562  26121  21214   1723    285   1564       C  
ATOM    881  CD  GLN A 148      20.272 -30.794  23.794  1.00196.56           C  
ANISOU  881  CD  GLN A 148    27921  25519  21243   1592    347   1402       C  
ATOM    882  OE1 GLN A 148      19.343 -30.150  23.306  1.00192.40           O  
ANISOU  882  OE1 GLN A 148    27480  24746  20877   1252    298   1217       O  
ATOM    883  NE2 GLN A 148      20.079 -31.885  24.527  1.00204.26           N  
ANISOU  883  NE2 GLN A 148    29166  26334  22109   1864    459   1483       N  
ATOM    884  N   SER A 149      20.783 -25.829  22.097  1.00199.97           N  
ANISOU  884  N   SER A 149    27458  26517  22003    269   -197   1070       N  
ATOM    885  CA  SER A 149      20.543 -24.842  21.052  1.00201.24           C  
ANISOU  885  CA  SER A 149    27596  26587  22278    -19   -235    954       C  
ATOM    886  C   SER A 149      21.190 -23.496  21.356  1.00202.85           C  
ANISOU  886  C   SER A 149    27534  27100  22439   -360   -421    949       C  
ATOM    887  O   SER A 149      20.946 -22.528  20.628  1.00198.96           O  
ANISOU  887  O   SER A 149    27061  26509  22027   -637   -466    846       O  
ATOM    888  CB  SER A 149      19.040 -24.661  20.831  1.00193.62           C  
ANISOU  888  CB  SER A 149    26949  25159  21459   -182   -218    759       C  
ATOM    889  OG  SER A 149      18.378 -24.362  22.048  1.00192.87           O  
ANISOU  889  OG  SER A 149    26942  24979  21359   -308   -312    686       O  
ATOM    890  N   ARG A 150      22.019 -23.416  22.402  1.00179.32           N  
ANISOU  890  N   ARG A 150    24327  24492  19314   -358   -530   1062       N  
ATOM    891  CA  ARG A 150      22.609 -22.139  22.793  1.00176.08           C  
ANISOU  891  CA  ARG A 150    23705  24367  18831   -743   -721   1047       C  
ATOM    892  C   ARG A 150      23.429 -21.519  21.669  1.00173.08           C  
ANISOU  892  C   ARG A 150    23097  24218  18448   -902   -719   1102       C  
ATOM    893  O   ARG A 150      23.565 -20.291  21.606  1.00170.78           O  
ANISOU  893  O   ARG A 150    22763  23982  18143  -1308   -847   1028       O  
ATOM    894  CB  ARG A 150      23.477 -22.321  24.039  1.00171.16           C  
ANISOU  894  CB  ARG A 150    22841  24172  18019   -690   -836   1187       C  
ATOM    895  CG  ARG A 150      22.728 -22.857  25.246  1.00166.67           C  
ANISOU  895  CG  ARG A 150    22496  23401  17431   -555   -847   1142       C  
ATOM    896  CD  ARG A 150      23.548 -22.696  26.514  1.00166.77           C  
ANISOU  896  CD  ARG A 150    22279  23844  17241   -611  -1011   1250       C  
ATOM    897  NE  ARG A 150      22.854 -23.214  27.687  1.00160.39           N  
ANISOU  897  NE  ARG A 150    21694  22848  16400   -473  -1013   1215       N  
ATOM    898  CZ  ARG A 150      23.342 -23.186  28.919  1.00159.92           C  
ANISOU  898  CZ  ARG A 150    21513  23089  16161   -487  -1148   1291       C  
ATOM    899  NH1 ARG A 150      24.532 -22.670  29.179  1.00159.90           N  
ANISOU  899  NH1 ARG A 150    21150  23616  15987   -654  -1307   1407       N  
ATOM    900  NH2 ARG A 150      22.618 -23.689  29.915  1.00163.63           N  
ANISOU  900  NH2 ARG A 150    22221  23343  16609   -349  -1126   1254       N  
ATOM    901  N   VAL A 151      23.977 -22.342  20.772  1.00165.28           N  
ANISOU  901  N   VAL A 151    21992  23353  17455   -589   -563   1231       N  
ATOM    902  CA  VAL A 151      24.727 -21.824  19.634  1.00163.15           C  
ANISOU  902  CA  VAL A 151    21510  23301  17179   -711   -533   1293       C  
ATOM    903  C   VAL A 151      23.831 -21.233  18.559  1.00158.60           C  
ANISOU  903  C   VAL A 151    21201  22296  16764   -901   -486   1120       C  
ATOM    904  O   VAL A 151      24.339 -20.654  17.593  1.00157.82           O  
ANISOU  904  O   VAL A 151    20973  22326  16667  -1055   -466   1149       O  
ATOM    905  CB  VAL A 151      25.609 -22.928  19.017  1.00159.51           C  
ANISOU  905  CB  VAL A 151    20852  23118  16636   -262   -358   1498       C  
ATOM    906  CG1 VAL A 151      26.652 -23.397  20.019  1.00157.13           C  
ANISOU  906  CG1 VAL A 151    20218  23342  16142    -63   -413   1705       C  
ATOM    907  CG2 VAL A 151      24.750 -24.091  18.545  1.00161.56           C  
ANISOU  907  CG2 VAL A 151    21475  22926  16986    114   -165   1445       C  
ATOM    908  N   TRP A 152      22.511 -21.359  18.700  1.00195.28           N  
ANISOU  908  N   TRP A 152    26202  26463  21532   -893   -465    952       N  
ATOM    909  CA  TRP A 152      21.568 -20.854  17.709  1.00192.54           C  
ANISOU  909  CA  TRP A 152    26105  25728  21324  -1036   -425    797       C  
ATOM    910  C   TRP A 152      20.913 -19.542  18.118  1.00192.27           C  
ANISOU  910  C   TRP A 152    26216  25514  21324  -1419   -570    644       C  
ATOM    911  O   TRP A 152      20.787 -18.637  17.287  1.00196.67           O  
ANISOU  911  O   TRP A 152    26836  25968  21923  -1642   -584    578       O  
ATOM    912  CB  TRP A 152      20.480 -21.898  17.431  1.00190.44           C  
ANISOU  912  CB  TRP A 152    26134  25072  21154   -769   -292    723       C  
ATOM    913  CG  TRP A 152      19.583 -21.534  16.286  1.00188.51           C  
ANISOU  913  CG  TRP A 152    26104  24495  21028   -871   -244    591       C  
ATOM    914  CD1 TRP A 152      18.462 -20.757  16.336  1.00184.20           C  
ANISOU  914  CD1 TRP A 152    25758  23662  20568  -1085   -314    432       C  
ATOM    915  CD2 TRP A 152      19.735 -21.930  14.917  1.00189.93           C  
ANISOU  915  CD2 TRP A 152    26317  24616  21232   -741   -113    616       C  
ATOM    916  NE1 TRP A 152      17.906 -20.646  15.085  1.00182.64           N  
ANISOU  916  NE1 TRP A 152    25697  23252  20446  -1099   -247    363       N  
ATOM    917  CE2 TRP A 152      18.669 -21.357  14.196  1.00185.48           C  
ANISOU  917  CE2 TRP A 152    25968  23735  20771   -906   -127    466       C  
ATOM    918  CE3 TRP A 152      20.669 -22.713  14.231  1.00192.20           C  
ANISOU  918  CE3 TRP A 152    26482  25097  21447   -478     20    758       C  
ATOM    919  CZ2 TRP A 152      18.510 -21.543  12.824  1.00184.35           C  
ANISOU  919  CZ2 TRP A 152    25922  23462  20661   -845    -27    446       C  
ATOM    920  CZ3 TRP A 152      20.510 -22.896  12.869  1.00193.57           C  
ANISOU  920  CZ3 TRP A 152    26774  25119  21654   -411    134    731       C  
ATOM    921  CH2 TRP A 152      19.439 -22.314  12.180  1.00187.77           C  
ANISOU  921  CH2 TRP A 152    26256  24066  21023   -609    102    573       C  
ATOM    922  N   GLN A 153      20.490 -19.410  19.375  1.00183.37           N  
ANISOU  922  N   GLN A 153    25175  24335  20164  -1481   -665    589       N  
ATOM    923  CA  GLN A 153      19.821 -18.196  19.828  1.00183.47           C  
ANISOU  923  CA  GLN A 153    25380  24148  20183  -1796   -782    442       C  
ATOM    924  C   GLN A 153      20.784 -17.054  20.135  1.00180.32           C  
ANISOU  924  C   GLN A 153    24836  24025  19653  -2161   -927    473       C  
ATOM    925  O   GLN A 153      20.369 -16.067  20.751  1.00179.95           O  
ANISOU  925  O   GLN A 153    24981  23831  19560  -2421  -1032    361       O  
ATOM    926  CB  GLN A 153      18.956 -18.485  21.059  1.00187.95           C  
ANISOU  926  CB  GLN A 153    26120  24543  20748  -1716   -814    370       C  
ATOM    927  CG  GLN A 153      17.652 -19.205  20.747  1.00184.86           C  
ANISOU  927  CG  GLN A 153    25956  23795  20488  -1501   -694    287       C  
ATOM    928  CD  GLN A 153      17.791 -20.711  20.765  1.00183.64           C  
ANISOU  928  CD  GLN A 153    25751  23683  20340  -1166   -574    388       C  
ATOM    929  OE1 GLN A 153      18.699 -21.252  21.392  1.00190.65           O  
ANISOU  929  OE1 GLN A 153    26462  24852  21125  -1039   -589    517       O  
ATOM    930  NE2 GLN A 153      16.892 -21.398  20.069  1.00173.39           N  
ANISOU  930  NE2 GLN A 153    24626  22110  19143  -1021   -454    336       N  
ATOM    931  N   THR A 154      22.047 -17.160  19.734  1.00131.51           N  
ANISOU  931  N   THR A 154    18335  18245  13388  -2194   -930    624       N  
ATOM    932  CA  THR A 154      22.957 -16.028  19.826  1.00128.63           C  
ANISOU  932  CA  THR A 154    17830  18153  12891  -2611  -1062    655       C  
ATOM    933  C   THR A 154      22.746 -15.100  18.636  1.00126.73           C  
ANISOU  933  C   THR A 154    17742  17698  12711  -2837  -1024    582       C  
ATOM    934  O   THR A 154      22.504 -15.551  17.513  1.00126.74           O  
ANISOU  934  O   THR A 154    17760  17573  12823  -2630   -886    595       O  
ATOM    935  CB  THR A 154      24.412 -16.501  19.890  1.00128.44           C  
ANISOU  935  CB  THR A 154    17352  18715  12733  -2567  -1081    868       C  
ATOM    936  OG1 THR A 154      25.291 -15.373  19.794  1.00124.11           O  
ANISOU  936  OG1 THR A 154    16655  18449  12053  -3033  -1201    903       O  
ATOM    937  CG2 THR A 154      24.716 -17.487  18.774  1.00126.09           C  
ANISOU  937  CG2 THR A 154    16896  18503  12509  -2196   -897    986       C  
ATOM    938  N   LYS A 155      22.824 -13.792  18.894  1.00161.69           N  
ANISOU  938  N   LYS A 155    22323  22065  17047  -3265  -1143    503       N  
ATOM    939  CA  LYS A 155      22.490 -12.815  17.863  1.00156.32           C  
ANISOU  939  CA  LYS A 155    21875  21112  16407  -3478  -1106    422       C  
ATOM    940  C   LYS A 155      23.486 -12.837  16.710  1.00153.15           C  
ANISOU  940  C   LYS A 155    21198  21003  15990  -3546  -1036    558       C  
ATOM    941  O   LYS A 155      23.122 -12.507  15.576  1.00155.44           O  
ANISOU  941  O   LYS A 155    21640  21061  16358  -3544   -945    519       O  
ATOM    942  CB  LYS A 155      22.412 -11.416  18.472  1.00161.14           C  
ANISOU  942  CB  LYS A 155    22769  21571  16884  -3923  -1239    314       C  
ATOM    943  CG  LYS A 155      21.484 -11.319  19.674  1.00163.24           C  
ANISOU  943  CG  LYS A 155    23316  21573  17134  -3857  -1301    185       C  
ATOM    944  CD  LYS A 155      20.025 -11.407  19.254  1.00155.91           C  
ANISOU  944  CD  LYS A 155    22704  20173  16362  -3573  -1191     61       C  
ATOM    945  CE  LYS A 155      19.096 -11.032  20.397  1.00156.05           C  
ANISOU  945  CE  LYS A 155    23036  19922  16332  -3557  -1243    -67       C  
ATOM    946  NZ  LYS A 155      19.167  -9.579  20.717  1.00150.12           N  
ANISOU  946  NZ  LYS A 155    22624  18999  15416  -3945  -1331   -158       N  
ATOM    947  N   SER A 156      24.737 -13.221  16.972  1.00123.87           N  
ANISOU  947  N   SER A 156    17074  17824  12166  -3589  -1074    728       N  
ATOM    948  CA  SER A 156      25.728 -13.274  15.902  1.00122.84           C  
ANISOU  948  CA  SER A 156    16642  18029  12003  -3631   -991    879       C  
ATOM    949  C   SER A 156      25.451 -14.416  14.933  1.00126.09           C  
ANISOU  949  C   SER A 156    17000  18356  12551  -3139   -800    930       C  
ATOM    950  O   SER A 156      25.853 -14.347  13.765  1.00126.11           O  
ANISOU  950  O   SER A 156    16912  18437  12567  -3136   -694    998       O  
ATOM    951  CB  SER A 156      27.133 -13.403  16.490  1.00124.43           C  
ANISOU  951  CB  SER A 156    16371  18885  12022  -3784  -1081   1068       C  
ATOM    952  OG  SER A 156      27.225 -14.525  17.350  1.00129.89           O  
ANISOU  952  OG  SER A 156    16874  19776  12702  -3408  -1085   1144       O  
ATOM    953  N   HIS A 157      24.772 -15.470  15.392  1.00129.72           N  
ANISOU  953  N   HIS A 157    17543  18646  13097  -2739   -750    896       N  
ATOM    954  CA  HIS A 157      24.436 -16.577  14.501  1.00125.63           C  
ANISOU  954  CA  HIS A 157    17054  17993  12686  -2301   -569    925       C  
ATOM    955  C   HIS A 157      23.336 -16.182  13.524  1.00123.84           C  
ANISOU  955  C   HIS A 157    17184  17280  12591  -2321   -505    771       C  
ATOM    956  O   HIS A 157      23.395 -16.533  12.340  1.00128.44           O  
ANISOU  956  O   HIS A 157    17766  17821  13216  -2162   -372    807       O  
ATOM    957  CB  HIS A 157      24.012 -17.798  15.317  1.00126.86           C  
ANISOU  957  CB  HIS A 157    17244  18087  12871  -1916   -534    932       C  
ATOM    958  CG  HIS A 157      23.959 -19.067  14.525  1.00133.31           C  
ANISOU  958  CG  HIS A 157    18069  18847  13736  -1468   -344    999       C  
ATOM    959  ND1 HIS A 157      25.091 -19.723  14.093  1.00134.91           N  
ANISOU  959  ND1 HIS A 157    17965  19452  13842  -1232   -238   1194       N  
ATOM    960  CD2 HIS A 157      22.909 -19.803  14.089  1.00137.36           C  
ANISOU  960  CD2 HIS A 157    18880  18950  14361  -1221   -238    899       C  
ATOM    961  CE1 HIS A 157      24.742 -20.807  13.424  1.00137.70           C  
ANISOU  961  CE1 HIS A 157    18475  19603  14242   -841    -65   1203       C  
ATOM    962  NE2 HIS A 157      23.423 -20.879  13.407  1.00140.82           N  
ANISOU  962  NE2 HIS A 157    19238  19505  14763   -856    -70   1021       N  
ATOM    963  N   ALA A 158      22.324 -15.453  14.002  1.00104.85           N  
ANISOU  963  N   ALA A 158    15087  14518  10233  -2497   -595    607       N  
ATOM    964  CA  ALA A 158      21.231 -15.044  13.127  1.00 99.77           C  
ANISOU  964  CA  ALA A 158    14764  13449   9695  -2493   -544    474       C  
ATOM    965  C   ALA A 158      21.696 -14.058  12.064  1.00101.38           C  
ANISOU  965  C   ALA A 158    14985  13675   9860  -2755   -526    497       C  
ATOM    966  O   ALA A 158      21.133 -14.025  10.964  1.00 99.72           O  
ANISOU  966  O   ALA A 158    14937  13231   9720  -2661   -440    451       O  
ATOM    967  CB  ALA A 158      20.095 -14.440  13.952  1.00 95.62           C  
ANISOU  967  CB  ALA A 158    14542  12590   9199  -2589   -635    318       C  
ATOM    968  N   LEU A 159      22.715 -13.252  12.365  1.00112.30           N  
ANISOU  968  N   LEU A 159    16208  15344  11115  -3103   -609    571       N  
ATOM    969  CA  LEU A 159      23.196 -12.283  11.386  1.00113.60           C  
ANISOU  969  CA  LEU A 159    16406  15532  11226  -3396   -585    602       C  
ATOM    970  C   LEU A 159      23.943 -12.967  10.248  1.00117.27           C  
ANISOU  970  C   LEU A 159    16606  16256  11697  -3206   -440    744       C  
ATOM    971  O   LEU A 159      23.867 -12.525   9.096  1.00120.79           O  
ANISOU  971  O   LEU A 159    17168  16570  12156  -3267   -361    739       O  
ATOM    972  CB  LEU A 159      24.089 -11.245  12.065  1.00117.72           C  
ANISOU  972  CB  LEU A 159    16845  16300  11585  -3879   -717    644       C  
ATOM    973  CG  LEU A 159      23.423 -10.365  13.123  1.00115.41           C  
ANISOU  973  CG  LEU A 159    16888  15720  11242  -4119   -853    497       C  
ATOM    974  CD1 LEU A 159      24.427  -9.385  13.710  1.00113.02           C  
ANISOU  974  CD1 LEU A 159    16516  15683  10745  -4645   -983    544       C  
ATOM    975  CD2 LEU A 159      22.228  -9.632  12.536  1.00110.87           C  
ANISOU  975  CD2 LEU A 159    16778  14612  10734  -4101   -812    349       C  
ATOM    976  N   LYS A 160      24.668 -14.045  10.547  1.00137.87           N  
ANISOU  976  N   LYS A 160    18876  19230  14277  -2947   -393    877       N  
ATOM    977  CA  LYS A 160      25.442 -14.728   9.519  1.00139.95           C  
ANISOU  977  CA  LYS A 160    18891  19765  14517  -2721   -235   1027       C  
ATOM    978  C   LYS A 160      24.611 -15.701   8.694  1.00137.56           C  
ANISOU  978  C   LYS A 160    18795  19144  14329  -2300    -91    966       C  
ATOM    979  O   LYS A 160      25.078 -16.143   7.639  1.00138.59           O  
ANISOU  979  O   LYS A 160    18827  19394  14436  -2118     56   1058       O  
ATOM    980  CB  LYS A 160      26.628 -15.464  10.149  1.00149.16           C  
ANISOU  980  CB  LYS A 160    19612  21490  15571  -2578   -228   1219       C  
ATOM    981  CG  LYS A 160      26.295 -16.823  10.737  1.00154.34           C  
ANISOU  981  CG  LYS A 160    20267  22106  16271  -2105   -174   1231       C  
ATOM    982  CD  LYS A 160      27.484 -17.387  11.501  1.00162.69           C  
ANISOU  982  CD  LYS A 160    20888  23741  17187  -1979   -189   1433       C  
ATOM    983  CE  LYS A 160      27.314 -18.870  11.782  1.00165.87           C  
ANISOU  983  CE  LYS A 160    21306  24113  17604  -1426    -73   1486       C  
ATOM    984  NZ  LYS A 160      28.481 -19.431  12.517  1.00165.04           N  
ANISOU  984  NZ  LYS A 160    20773  24594  17339  -1243    -81   1704       N  
ATOM    985  N   VAL A 161      23.403 -16.044   9.137  1.00104.24           N  
ANISOU  985  N   VAL A 161    14858  14536  10211  -2157   -126    817       N  
ATOM    986  CA  VAL A 161      22.535 -16.886   8.322  1.00104.96           C  
ANISOU  986  CA  VAL A 161    15173  14315  10392  -1839     -8    745       C  
ATOM    987  C   VAL A 161      21.600 -16.052   7.448  1.00106.62           C  
ANISOU  987  C   VAL A 161    15686  14159  10664  -1994    -21    613       C  
ATOM    988  O   VAL A 161      21.209 -16.500   6.366  1.00107.67           O  
ANISOU  988  O   VAL A 161    15951  14131  10828  -1815     85    589       O  
ATOM    989  CB  VAL A 161      21.746 -17.874   9.198  1.00 94.89           C  
ANISOU  989  CB  VAL A 161    14017  12861   9176  -1587    -20    677       C  
ATOM    990  CG1 VAL A 161      22.698 -18.718  10.031  1.00104.41           C  
ANISOU  990  CG1 VAL A 161    14942  14429  10299  -1390      3    824       C  
ATOM    991  CG2 VAL A 161      20.766 -17.139  10.092  1.00104.82           C  
ANISOU  991  CG2 VAL A 161    15472  13866  10489  -1795   -164    532       C  
ATOM    992  N   ILE A 162      21.232 -14.845   7.886  1.00119.80           N  
ANISOU  992  N   ILE A 162    17494  15693  12332  -2311   -145    531       N  
ATOM    993  CA  ILE A 162      20.521 -13.940   6.988  1.00119.61           C  
ANISOU  993  CA  ILE A 162    17745  15371  12331  -2444   -146    441       C  
ATOM    994  C   ILE A 162      21.483 -13.349   5.970  1.00117.47           C  
ANISOU  994  C   ILE A 162    17369  15283  11980  -2620    -78    546       C  
ATOM    995  O   ILE A 162      21.073 -12.963   4.868  1.00116.14           O  
ANISOU  995  O   ILE A 162    17389  14919  11821  -2622    -22    512       O  
ATOM    996  CB  ILE A 162      19.781 -12.842   7.777  1.00119.15           C  
ANISOU  996  CB  ILE A 162    17928  15074  12270  -2676   -276    325       C  
ATOM    997  CG1 ILE A 162      20.771 -11.860   8.407  1.00126.97           C  
ANISOU  997  CG1 ILE A 162    18822  16275  13145  -3055   -361    384       C  
ATOM    998  CG2 ILE A 162      18.872 -13.454   8.825  1.00118.45           C  
ANISOU  998  CG2 ILE A 162    17909  14847  12249  -2497   -329    237       C  
ATOM    999  CD1 ILE A 162      20.111 -10.658   9.042  1.00127.49           C  
ANISOU  999  CD1 ILE A 162    19211  16061  13170  -3295   -466    269       C  
ATOM   1000  N   ALA A 163      22.771 -13.267   6.310  1.00 79.23           N  
ANISOU 1000  N   ALA A 163    12214  10846   7045  -2774    -81    685       N  
ATOM   1001  CA  ALA A 163      23.768 -12.893   5.316  1.00 78.76           C  
ANISOU 1001  CA  ALA A 163    11993  11033   6900  -2914     10    814       C  
ATOM   1002  C   ALA A 163      23.959 -14.008   4.298  1.00 82.37           C  
ANISOU 1002  C   ALA A 163    12352  11570   7373  -2532    181    886       C  
ATOM   1003  O   ALA A 163      24.096 -13.746   3.098  1.00 84.77           O  
ANISOU 1003  O   ALA A 163    12721  11837   7650  -2546    281    917       O  
ATOM   1004  CB  ALA A 163      25.091 -12.550   5.997  1.00 81.28           C  
ANISOU 1004  CB  ALA A 163    11955  11831   7096  -3194    -45    959       C  
ATOM   1005  N   ALA A 164      23.959 -15.262   4.758  1.00 97.33           N  
ANISOU 1005  N   ALA A 164    14132  13553   9296  -2182    227    912       N  
ATOM   1006  CA  ALA A 164      24.064 -16.388   3.838  1.00 97.36           C  
ANISOU 1006  CA  ALA A 164    14128  13571   9292  -1794    401    965       C  
ATOM   1007  C   ALA A 164      22.781 -16.584   3.043  1.00 92.20           C  
ANISOU 1007  C   ALA A 164    13855  12455   8721  -1667    426    808       C  
ATOM   1008  O   ALA A 164      22.833 -16.993   1.878  1.00 96.30           O  
ANISOU 1008  O   ALA A 164    14453  12927   9208  -1494    560    831       O  
ATOM   1009  CB  ALA A 164      24.416 -17.663   4.603  1.00 94.86           C  
ANISOU 1009  CB  ALA A 164    13645  13443   8956  -1450    450   1041       C  
ATOM   1010  N   THR A 165      21.625 -16.304   3.649  1.00 93.19           N  
ANISOU 1010  N   THR A 165    14210  12264   8935  -1748    301    655       N  
ATOM   1011  CA  THR A 165      20.367 -16.424   2.920  1.00 86.08           C  
ANISOU 1011  CA  THR A 165    13629  10983   8095  -1657    306    518       C  
ATOM   1012  C   THR A 165      20.286 -15.403   1.792  1.00 94.11           C  
ANISOU 1012  C   THR A 165    14778  11899   9079  -1835    319    507       C  
ATOM   1013  O   THR A 165      19.848 -15.730   0.684  1.00 95.56           O  
ANISOU 1013  O   THR A 165    15124  11932   9254  -1695    395    473       O  
ATOM   1014  CB  THR A 165      19.182 -16.260   3.871  1.00 90.53           C  
ANISOU 1014  CB  THR A 165    14360  11297   8742  -1707    172    380       C  
ATOM   1015  OG1 THR A 165      19.344 -17.135   4.994  1.00 97.15           O  
ANISOU 1015  OG1 THR A 165    15073  12244   9597  -1568    160    403       O  
ATOM   1016  CG2 THR A 165      17.879 -16.592   3.161  1.00 87.04           C  
ANISOU 1016  CG2 THR A 165    14186  10540   8345  -1585    178    258       C  
ATOM   1017  N   TRP A 166      20.712 -14.165   2.051  1.00103.29           N  
ANISOU 1017  N   TRP A 166    15904  13135  10208  -2154    248    537       N  
ATOM   1018  CA  TRP A 166      20.664 -13.141   1.014  1.00100.62           C  
ANISOU 1018  CA  TRP A 166    15729  12681   9821  -2333    270    538       C  
ATOM   1019  C   TRP A 166      21.763 -13.348  -0.022  1.00106.94           C  
ANISOU 1019  C   TRP A 166    16354  13741  10536  -2302    420    679       C  
ATOM   1020  O   TRP A 166      21.547 -13.121  -1.217  1.00108.19           O  
ANISOU 1020  O   TRP A 166    16675  13773  10661  -2271    493    674       O  
ATOM   1021  CB  TRP A 166      20.770 -11.751   1.642  1.00 99.64           C  
ANISOU 1021  CB  TRP A 166    15687  12511   9659  -2704    160    524       C  
ATOM   1022  CG  TRP A 166      19.466 -11.224   2.164  1.00100.60           C  
ANISOU 1022  CG  TRP A 166    16106  12283   9833  -2710     47    378       C  
ATOM   1023  CD1 TRP A 166      18.951 -11.404   3.414  1.00 98.90           C  
ANISOU 1023  CD1 TRP A 166    15898  12010   9671  -2682    -51    305       C  
ATOM   1024  CD2 TRP A 166      18.512 -10.429   1.448  1.00102.60           C  
ANISOU 1024  CD2 TRP A 166    16687  12222  10074  -2717     33    302       C  
ATOM   1025  NE1 TRP A 166      17.736 -10.771   3.522  1.00 94.79           N  
ANISOU 1025  NE1 TRP A 166    15675  11171   9170  -2664   -117    191       N  
ATOM   1026  CE2 TRP A 166      17.444 -10.165   2.329  1.00100.71           C  
ANISOU 1026  CE2 TRP A 166    16623  11766   9878  -2674    -70    191       C  
ATOM   1027  CE3 TRP A 166      18.458  -9.916   0.148  1.00102.20           C  
ANISOU 1027  CE3 TRP A 166    16799  12067   9965  -2735    102    328       C  
ATOM   1028  CZ2 TRP A 166      16.335  -9.411   1.952  1.00100.36           C  
ANISOU 1028  CZ2 TRP A 166    16890  11429   9815  -2623   -102    115       C  
ATOM   1029  CZ3 TRP A 166      17.355  -9.167  -0.224  1.00 99.60           C  
ANISOU 1029  CZ3 TRP A 166    16794  11432   9619  -2695     60    248       C  
ATOM   1030  CH2 TRP A 166      16.309  -8.922   0.675  1.00 99.07           C  
ANISOU 1030  CH2 TRP A 166    16877  11175   9590  -2628    -40    147       C  
ATOM   1031  N   CYS A 167      22.947 -13.785   0.415  1.00117.65           N  
ANISOU 1031  N   CYS A 167    17371  15489  11843  -2291    472    817       N  
ATOM   1032  CA  CYS A 167      24.056 -13.974  -0.515  1.00121.35           C  
ANISOU 1032  CA  CYS A 167    17628  16267  12212  -2242    631    976       C  
ATOM   1033  C   CYS A 167      23.795 -15.143  -1.458  1.00120.08           C  
ANISOU 1033  C   CYS A 167    17565  16014  12047  -1834    780    967       C  
ATOM   1034  O   CYS A 167      23.944 -15.014  -2.679  1.00120.84           O  
ANISOU 1034  O   CYS A 167    17748  16085  12080  -1796    894   1002       O  
ATOM   1035  CB  CYS A 167      25.359 -14.186   0.255  1.00124.67           C  
ANISOU 1035  CB  CYS A 167    17622  17187  12561  -2300    646   1142       C  
ATOM   1036  SG  CYS A 167      26.819 -14.400  -0.789  1.00145.83           S  
ANISOU 1036  SG  CYS A 167    19962  20351  15094  -2227    855   1374       S  
ATOM   1037  N   LEU A 168      23.405 -16.296  -0.908  1.00108.06           N  
ANISOU 1037  N   LEU A 168    16063  14424  10570  -1535    786    920       N  
ATOM   1038  CA  LEU A 168      23.181 -17.470  -1.746  1.00109.65           C  
ANISOU 1038  CA  LEU A 168    16412  14512  10737  -1164    933    905       C  
ATOM   1039  C   LEU A 168      21.933 -17.325  -2.608  1.00109.54           C  
ANISOU 1039  C   LEU A 168    16773  14088  10759  -1172    897    747       C  
ATOM   1040  O   LEU A 168      21.852 -17.934  -3.680  1.00112.48           O  
ANISOU 1040  O   LEU A 168    17301  14372  11063   -967   1021    741       O  
ATOM   1041  CB  LEU A 168      23.089 -18.729  -0.882  1.00110.91           C  
ANISOU 1041  CB  LEU A 168    16546  14678  10915   -871    953    899       C  
ATOM   1042  CG  LEU A 168      24.405 -19.433  -0.533  1.00118.94           C  
ANISOU 1042  CG  LEU A 168    17236  16122  11834   -635   1083   1091       C  
ATOM   1043  CD1 LEU A 168      25.232 -18.628   0.460  1.00121.69           C  
ANISOU 1043  CD1 LEU A 168    17215  16842  12178   -907    976   1199       C  
ATOM   1044  CD2 LEU A 168      24.137 -20.832   0.002  1.00113.19           C  
ANISOU 1044  CD2 LEU A 168    16625  15285  11097   -265   1146   1071       C  
ATOM   1045  N   SER A 169      20.956 -16.530  -2.167  1.00100.26           N  
ANISOU 1045  N   SER A 169    15748  12676   9669  -1391    731    624       N  
ATOM   1046  CA  SER A 169      19.763 -16.321  -2.981  1.00 96.81           C  
ANISOU 1046  CA  SER A 169    15625  11910   9247  -1391    685    494       C  
ATOM   1047  C   SER A 169      20.093 -15.549  -4.252  1.00 97.02           C  
ANISOU 1047  C   SER A 169    15726  11946   9190  -1489    757    547       C  
ATOM   1048  O   SER A 169      19.535 -15.831  -5.319  1.00100.61           O  
ANISOU 1048  O   SER A 169    16396  12234   9597  -1370    801    492       O  
ATOM   1049  CB  SER A 169      18.694 -15.591  -2.173  1.00 97.72           C  
ANISOU 1049  CB  SER A 169    15858  11819   9452  -1562    507    377       C  
ATOM   1050  OG  SER A 169      18.140 -16.442  -1.184  1.00 96.18           O  
ANISOU 1050  OG  SER A 169    15653  11564   9326  -1442    452    310       O  
ATOM   1051  N   PHE A 170      20.993 -14.568  -4.157  1.00103.98           N  
ANISOU 1051  N   PHE A 170    16445  13025  10036  -1728    766    655       N  
ATOM   1052  CA  PHE A 170      21.429 -13.855  -5.352  1.00103.52           C  
ANISOU 1052  CA  PHE A 170    16449  12999   9883  -1835    856    727       C  
ATOM   1053  C   PHE A 170      22.271 -14.747  -6.256  1.00102.72           C  
ANISOU 1053  C   PHE A 170    16239  13105   9685  -1593   1054    834       C  
ATOM   1054  O   PHE A 170      22.272 -14.563  -7.478  1.00108.88           O  
ANISOU 1054  O   PHE A 170    17166  13822  10382  -1558   1146    852       O  
ATOM   1055  CB  PHE A 170      22.215 -12.603  -4.962  1.00104.24           C  
ANISOU 1055  CB  PHE A 170    16409  13256   9942  -2202    822    821       C  
ATOM   1056  CG  PHE A 170      21.348 -11.430  -4.599  1.00104.72           C  
ANISOU 1056  CG  PHE A 170    16726  13026  10037  -2440    673    721       C  
ATOM   1057  CD1 PHE A 170      20.509 -10.854  -5.538  1.00106.70           C  
ANISOU 1057  CD1 PHE A 170    17294  12992  10255  -2427    662    658       C  
ATOM   1058  CD2 PHE A 170      21.379 -10.898  -3.320  1.00103.57           C  
ANISOU 1058  CD2 PHE A 170    16522  12895   9933  -2653    549    697       C  
ATOM   1059  CE1 PHE A 170      19.712  -9.773  -5.207  1.00106.65           C  
ANISOU 1059  CE1 PHE A 170    17545  12722  10256  -2587    544    582       C  
ATOM   1060  CE2 PHE A 170      20.584  -9.819  -2.983  1.00106.84           C  
ANISOU 1060  CE2 PHE A 170    17217  13023  10353  -2832    433    609       C  
ATOM   1061  CZ  PHE A 170      19.750  -9.256  -3.927  1.00107.60           C  
ANISOU 1061  CZ  PHE A 170    17632  12837  10414  -2781    438    556       C  
ATOM   1062  N   THR A 171      22.984 -15.715  -5.677  1.00 93.33           N  
ANISOU 1062  N   THR A 171    14811  12161   8489  -1396   1131    911       N  
ATOM   1063  CA  THR A 171      23.818 -16.610  -6.471  1.00 88.07           C  
ANISOU 1063  CA  THR A 171    14054  11702   7708  -1105   1343   1026       C  
ATOM   1064  C   THR A 171      22.997 -17.725  -7.108  1.00 87.62           C  
ANISOU 1064  C   THR A 171    14313  11355   7625   -790   1400    909       C  
ATOM   1065  O   THR A 171      23.257 -18.114  -8.252  1.00 95.19           O  
ANISOU 1065  O   THR A 171    15389  12312   8466   -610   1557    945       O  
ATOM   1066  CB  THR A 171      24.930 -17.199  -5.602  1.00 89.86           C  
ANISOU 1066  CB  THR A 171    13907  12328   7907   -975   1414   1175       C  
ATOM   1067  OG1 THR A 171      25.568 -16.150  -4.864  1.00102.23           O  
ANISOU 1067  OG1 THR A 171    15192  14157   9492  -1336   1317   1261       O  
ATOM   1068  CG2 THR A 171      25.966 -17.904  -6.464  1.00 97.27           C  
ANISOU 1068  CG2 THR A 171    14710  13554   8696   -673   1659   1336       C  
ATOM   1069  N   ILE A 172      22.006 -18.249  -6.386  1.00 89.42           N  
ANISOU 1069  N   ILE A 172    14694  11338   7944   -740   1278    768       N  
ATOM   1070  CA  ILE A 172      21.174 -19.317  -6.933  1.00 89.63           C  
ANISOU 1070  CA  ILE A 172    15041  11084   7929   -509   1315    649       C  
ATOM   1071  C   ILE A 172      20.323 -18.795  -8.085  1.00 89.57           C  
ANISOU 1071  C   ILE A 172    15311  10838   7883   -614   1268    551       C  
ATOM   1072  O   ILE A 172      20.176 -19.462  -9.117  1.00 86.64           O  
ANISOU 1072  O   ILE A 172    15171  10354   7396   -438   1374    519       O  
ATOM   1073  CB  ILE A 172      20.309 -19.940  -5.821  1.00 86.28           C  
ANISOU 1073  CB  ILE A 172    14693  10485   7606   -486   1190    534       C  
ATOM   1074  CG1 ILE A 172      21.168 -20.814  -4.906  1.00 96.42           C  
ANISOU 1074  CG1 ILE A 172    15779  11980   8876   -269   1284    638       C  
ATOM   1075  CG2 ILE A 172      19.167 -20.752  -6.414  1.00 79.49           C  
ANISOU 1075  CG2 ILE A 172    14199   9298   6704   -392   1172    381       C  
ATOM   1076  CD1 ILE A 172      20.494 -21.177  -3.599  1.00 95.50           C  
ANISOU 1076  CD1 ILE A 172    15668  11750   8867   -303   1151    556       C  
ATOM   1077  N   MET A 173      19.764 -17.594  -7.939  1.00 92.41           N  
ANISOU 1077  N   MET A 173    15675  11118   8318   -887   1114    507       N  
ATOM   1078  CA  MET A 173      18.898 -17.008  -8.954  1.00 90.39           C  
ANISOU 1078  CA  MET A 173    15672  10654   8017   -971   1052    426       C  
ATOM   1079  C   MET A 173      19.670 -16.289 -10.057  1.00 92.60           C  
ANISOU 1079  C   MET A 173    15946  11049   8190  -1026   1172    538       C  
ATOM   1080  O   MET A 173      19.109 -15.405 -10.717  1.00 94.18           O  
ANISOU 1080  O   MET A 173    16311  11114   8361  -1155   1105    505       O  
ATOM   1081  CB  MET A 173      17.900 -16.051  -8.302  1.00 89.64           C  
ANISOU 1081  CB  MET A 173    15622  10412   8027  -1182    850    341       C  
ATOM   1082  CG  MET A 173      16.972 -16.729  -7.309  1.00 84.38           C  
ANISOU 1082  CG  MET A 173    14979   9627   7454  -1137    731    226       C  
ATOM   1083  SD  MET A 173      15.463 -17.332  -8.088  1.00 99.05           S  
ANISOU 1083  SD  MET A 173    17136  11244   9256  -1064    645     73       S  
ATOM   1084  CE  MET A 173      14.832 -18.410  -6.806  1.00 87.93           C  
ANISOU 1084  CE  MET A 173    15693   9776   7940  -1016    574    -15       C  
ATOM   1085  N   THR A 174      20.936 -16.648 -10.265  1.00 86.38           N  
ANISOU 1085  N   THR A 174    14969  10523   7330   -915   1355    679       N  
ATOM   1086  CA  THR A 174      21.713 -16.040 -11.340  1.00 85.00           C  
ANISOU 1086  CA  THR A 174    14773  10486   7036   -964   1493    799       C  
ATOM   1087  C   THR A 174      21.180 -16.341 -12.743  1.00 92.85           C  
ANISOU 1087  C   THR A 174    16089  11289   7902   -822   1556    737       C  
ATOM   1088  O   THR A 174      21.303 -15.455 -13.607  1.00 94.96           O  
ANISOU 1088  O   THR A 174    16433  11551   8095   -949   1587    787       O  
ATOM   1089  CB  THR A 174      23.183 -16.475 -11.215  1.00 86.34           C  
ANISOU 1089  CB  THR A 174    14625  11039   7140   -839   1687    981       C  
ATOM   1090  OG1 THR A 174      23.640 -16.236  -9.878  1.00 98.32           O  
ANISOU 1090  OG1 THR A 174    15838  12759   8761   -981   1606   1036       O  
ATOM   1091  CG2 THR A 174      24.062 -15.693 -12.175  1.00 93.68           C  
ANISOU 1091  CG2 THR A 174    15469  12172   7954   -955   1828   1129       C  
ATOM   1092  N   PRO A 175      20.617 -17.519 -13.050  1.00 89.69           N  
ANISOU 1092  N   PRO A 175    15906  10724   7448   -585   1580    632       N  
ATOM   1093  CA  PRO A 175      20.077 -17.731 -14.407  1.00 89.93           C  
ANISOU 1093  CA  PRO A 175    16264  10575   7331   -495   1619    564       C  
ATOM   1094  C   PRO A 175      19.017 -16.727 -14.835  1.00 92.41           C  
ANISOU 1094  C   PRO A 175    16749  10703   7659   -698   1440    481       C  
ATOM   1095  O   PRO A 175      18.793 -16.577 -16.042  1.00 93.76           O  
ANISOU 1095  O   PRO A 175    17140  10795   7691   -662   1480    470       O  
ATOM   1096  CB  PRO A 175      19.492 -19.148 -14.348  1.00 83.24           C  
ANISOU 1096  CB  PRO A 175    15640   9552   6437   -285   1625    439       C  
ATOM   1097  CG  PRO A 175      20.110 -19.803 -13.190  1.00 83.83           C  
ANISOU 1097  CG  PRO A 175    15495   9762   6594   -172   1680    493       C  
ATOM   1098  CD  PRO A 175      20.740 -18.786 -12.302  1.00 90.13           C  
ANISOU 1098  CD  PRO A 175    15927  10794   7526   -366   1628    606       C  
ATOM   1099  N   TYR A 176      18.352 -16.036 -13.901  1.00 95.55           N  
ANISOU 1099  N   TYR A 176    17068  11034   8201   -883   1252    430       N  
ATOM   1100  CA  TYR A 176      17.271 -15.140 -14.311  1.00 91.97           C  
ANISOU 1100  CA  TYR A 176    16798  10411   7737  -1008   1092    361       C  
ATOM   1101  C   TYR A 176      17.787 -13.896 -15.028  1.00 96.44           C  
ANISOU 1101  C   TYR A 176    17392  11018   8231  -1137   1153    475       C  
ATOM   1102  O   TYR A 176      17.262 -13.577 -16.109  1.00 98.97           O  
ANISOU 1102  O   TYR A 176    17943  11231   8430  -1109   1136    454       O  
ATOM   1103  CB  TYR A 176      16.386 -14.796 -13.108  1.00 88.65           C  
ANISOU 1103  CB  TYR A 176    16309   9907   7468  -1120    897    280       C  
ATOM   1104  CG  TYR A 176      15.150 -15.660 -13.003  1.00 84.36           C  
ANISOU 1104  CG  TYR A 176    15896   9230   6927  -1041    769    133       C  
ATOM   1105  CD1 TYR A 176      13.983 -15.316 -13.671  1.00 85.83           C  
ANISOU 1105  CD1 TYR A 176    16269   9304   7038  -1055    637     59       C  
ATOM   1106  CD2 TYR A 176      15.152 -16.821 -12.242  1.00 91.17           C  
ANISOU 1106  CD2 TYR A 176    16695  10098   7848   -960    782     78       C  
ATOM   1107  CE1 TYR A 176      12.851 -16.102 -13.584  1.00 84.38           C  
ANISOU 1107  CE1 TYR A 176    16173   9049   6838  -1030    513    -66       C  
ATOM   1108  CE2 TYR A 176      14.023 -17.615 -12.147  1.00 90.24           C  
ANISOU 1108  CE2 TYR A 176    16709   9862   7717   -941    670    -53       C  
ATOM   1109  CZ  TYR A 176      12.876 -17.250 -12.821  1.00 88.38           C  
ANISOU 1109  CZ  TYR A 176    16626   9548   7406   -995    531   -125       C  
ATOM   1110  OH  TYR A 176      11.750 -18.035 -12.731  1.00 97.89           O  
ANISOU 1110  OH  TYR A 176    17930  10685   8579  -1020    410   -246       O  
ATOM   1111  N   PRO A 177      18.779 -13.154 -14.516  1.00111.05           N  
ANISOU 1111  N   PRO A 177    19038  13025  10132  -1300   1220    599       N  
ATOM   1112  CA  PRO A 177      19.320 -12.036 -15.310  1.00111.76           C  
ANISOU 1112  CA  PRO A 177    19196  13146  10123  -1450   1303    715       C  
ATOM   1113  C   PRO A 177      20.026 -12.479 -16.580  1.00117.71           C  
ANISOU 1113  C   PRO A 177    20003  14008  10715  -1310   1503    796       C  
ATOM   1114  O   PRO A 177      20.152 -11.672 -17.510  1.00121.61           O  
ANISOU 1114  O   PRO A 177    20647  14465  11095  -1392   1560    864       O  
ATOM   1115  CB  PRO A 177      20.299 -11.344 -14.350  1.00114.77           C  
ANISOU 1115  CB  PRO A 177    19318  13708  10582  -1694   1330    825       C  
ATOM   1116  CG  PRO A 177      20.504 -12.280 -13.224  1.00117.34           C  
ANISOU 1116  CG  PRO A 177    19400  14159  11024  -1606   1304    792       C  
ATOM   1117  CD  PRO A 177      19.295 -13.142 -13.136  1.00112.60           C  
ANISOU 1117  CD  PRO A 177    18961  13356  10466  -1406   1189    630       C  
ATOM   1118  N   ILE A 178      20.489 -13.727 -16.653  1.00106.23           N  
ANISOU 1118  N   ILE A 178    18460  12673   9231  -1086   1624    795       N  
ATOM   1119  CA  ILE A 178      21.224 -14.185 -17.827  1.00102.61           C  
ANISOU 1119  CA  ILE A 178    18062  12327   8599   -916   1841    879       C  
ATOM   1120  C   ILE A 178      20.272 -14.512 -18.970  1.00 99.90           C  
ANISOU 1120  C   ILE A 178    18086  11753   8120   -780   1801    766       C  
ATOM   1121  O   ILE A 178      20.445 -14.035 -20.098  1.00101.95           O  
ANISOU 1121  O   ILE A 178    18501  12004   8232   -783   1890    826       O  
ATOM   1122  CB  ILE A 178      22.105 -15.397 -17.468  1.00100.83           C  
ANISOU 1122  CB  ILE A 178    17639  12311   8360   -679   2007    934       C  
ATOM   1123  CG1 ILE A 178      23.031 -15.062 -16.299  1.00106.71           C  
ANISOU 1123  CG1 ILE A 178    17984  13336   9224   -823   2022   1055       C  
ATOM   1124  CG2 ILE A 178      22.908 -15.851 -18.677  1.00 96.51           C  
ANISOU 1124  CG2 ILE A 178    17162  11895   7613   -465   2259   1034       C  
ATOM   1125  CD1 ILE A 178      23.827 -16.247 -15.797  1.00107.13           C  
ANISOU 1125  CD1 ILE A 178    17826  13614   9265   -552   2166   1119       C  
ATOM   1126  N   TYR A 179      19.253 -15.327 -18.699  1.00 97.42           N  
ANISOU 1126  N   TYR A 179    17916  11262   7837   -681   1664    604       N  
ATOM   1127  CA  TYR A 179      18.359 -15.838 -19.731  1.00 94.03           C  
ANISOU 1127  CA  TYR A 179    17821  10650   7255   -569   1614    487       C  
ATOM   1128  C   TYR A 179      17.037 -15.078 -19.793  1.00 95.10           C  
ANISOU 1128  C   TYR A 179    18097  10624   7414   -706   1373    395       C  
ATOM   1129  O   TYR A 179      15.993 -15.672 -20.084  1.00 94.90           O  
ANISOU 1129  O   TYR A 179    18263  10472   7324   -659   1244    260       O  
ATOM   1130  CB  TYR A 179      18.110 -17.330 -19.514  1.00 95.80           C  
ANISOU 1130  CB  TYR A 179    18152  10800   7449   -388   1635    374       C  
ATOM   1131  CG  TYR A 179      19.354 -18.179 -19.660  1.00101.03           C  
ANISOU 1131  CG  TYR A 179    18751  11608   8029   -161   1900    471       C  
ATOM   1132  CD1 TYR A 179      19.751 -18.656 -20.903  1.00 98.82           C  
ANISOU 1132  CD1 TYR A 179    18707  11317   7524     26   2084    494       C  
ATOM   1133  CD2 TYR A 179      20.131 -18.503 -18.555  1.00101.08           C  
ANISOU 1133  CD2 TYR A 179    18464  11780   8161   -107   1973    548       C  
ATOM   1134  CE1 TYR A 179      20.887 -19.430 -21.042  1.00 97.24           C  
ANISOU 1134  CE1 TYR A 179    18454  11267   7227    286   2348    598       C  
ATOM   1135  CE2 TYR A 179      21.269 -19.278 -18.685  1.00104.16           C  
ANISOU 1135  CE2 TYR A 179    18777  12345   8455    151   2225    658       C  
ATOM   1136  CZ  TYR A 179      21.642 -19.739 -19.930  1.00101.64           C  
ANISOU 1136  CZ  TYR A 179    18697  12010   7911    360   2419    686       C  
ATOM   1137  OH  TYR A 179      22.774 -20.510 -20.065  1.00105.19           O  
ANISOU 1137  OH  TYR A 179    19075  12648   8244    667   2690    810       O  
ATOM   1138  N   SER A 180      17.060 -13.774 -19.529  1.00 95.32           N  
ANISOU 1138  N   SER A 180    18045  10662   7512   -874   1314    472       N  
ATOM   1139  CA  SER A 180      15.888 -12.918 -19.671  1.00 99.32           C  
ANISOU 1139  CA  SER A 180    18699  11030   8007   -948   1118    419       C  
ATOM   1140  C   SER A 180      16.181 -11.877 -20.740  1.00100.46           C  
ANISOU 1140  C   SER A 180    19007  11156   8007   -988   1195    529       C  
ATOM   1141  O   SER A 180      17.130 -11.097 -20.608  1.00 98.36           O  
ANISOU 1141  O   SER A 180    18646  10962   7766  -1116   1316    660       O  
ATOM   1142  CB  SER A 180      15.524 -12.243 -18.347  1.00 94.11           C  
ANISOU 1142  CB  SER A 180    17880  10343   7533  -1083    979    408       C  
ATOM   1143  OG  SER A 180      14.819 -13.132 -17.499  1.00 92.90           O  
ANISOU 1143  OG  SER A 180    17644  10170   7484  -1038    858    285       O  
ATOM   1144  N   ASN A 181      15.370 -11.867 -21.795  1.00110.29           N  
ANISOU 1144  N   ASN A 181    20503  12317   9086   -897   1123    481       N  
ATOM   1145  CA  ASN A 181      15.562 -10.951 -22.907  1.00114.48           C  
ANISOU 1145  CA  ASN A 181    21232  12814   9450   -905   1196    584       C  
ATOM   1146  C   ASN A 181      14.207 -10.428 -23.364  1.00112.07           C  
ANISOU 1146  C   ASN A 181    21133  12403   9047   -850    993    529       C  
ATOM   1147  O   ASN A 181      13.154 -10.869 -22.895  1.00106.57           O  
ANISOU 1147  O   ASN A 181    20400  11692   8398   -810    805    412       O  
ATOM   1148  CB  ASN A 181      16.304 -11.627 -24.067  1.00118.71           C  
ANISOU 1148  CB  ASN A 181    21878  13419   9808   -792   1393    620       C  
ATOM   1149  CG  ASN A 181      17.781 -11.816 -23.781  1.00120.64           C  
ANISOU 1149  CG  ASN A 181    21905  13826  10108   -827   1631    738       C  
ATOM   1150  OD1 ASN A 181      18.510 -10.850 -23.551  1.00119.36           O  
ANISOU 1150  OD1 ASN A 181    21635  13726   9989   -990   1715    872       O  
ATOM   1151  ND2 ASN A 181      18.231 -13.066 -23.790  1.00112.93           N  
ANISOU 1151  ND2 ASN A 181    20870  12928   9109   -675   1744    697       N  
ATOM   1152  N   LEU A 182      14.247  -9.472 -24.288  1.00 92.51           N  
ANISOU 1152  N   LEU A 182    18863   9871   6414   -843   1037    628       N  
ATOM   1153  CA  LEU A 182      13.040  -8.881 -24.848  1.00 92.07           C  
ANISOU 1153  CA  LEU A 182    19013   9744   6224   -747    862    611       C  
ATOM   1154  C   LEU A 182      12.635  -9.643 -26.103  1.00 88.62           C  
ANISOU 1154  C   LEU A 182    18753   9351   5566   -620    840    551       C  
ATOM   1155  O   LEU A 182      13.456  -9.849 -27.002  1.00 95.64           O  
ANISOU 1155  O   LEU A 182    19754  10259   6326   -599   1021    607       O  
ATOM   1156  CB  LEU A 182      13.262  -7.403 -25.169  1.00 93.72           C  
ANISOU 1156  CB  LEU A 182    19406   9845   6357   -792    923    757       C  
ATOM   1157  CG  LEU A 182      13.052  -6.421 -24.015  1.00 92.28           C  
ANISOU 1157  CG  LEU A 182    19180   9561   6323   -883    855    790       C  
ATOM   1158  CD1 LEU A 182      13.284  -4.989 -24.472  1.00 89.72           C  
ANISOU 1158  CD1 LEU A 182    19134   9083   5874   -929    936    936       C  
ATOM   1159  CD2 LEU A 182      11.660  -6.579 -23.424  1.00 95.01           C  
ANISOU 1159  CD2 LEU A 182    19470   9915   6715   -752    618    687       C  
ATOM   1160  N   VAL A 183      11.374 -10.058 -26.160  1.00 87.80           N  
ANISOU 1160  N   VAL A 183    18673   9284   5403   -549    620    442       N  
ATOM   1161  CA  VAL A 183      10.844 -10.832 -27.275  1.00 89.11           C  
ANISOU 1161  CA  VAL A 183    19014   9504   5340   -471    554    363       C  
ATOM   1162  C   VAL A 183       9.976  -9.899 -28.120  1.00 90.64           C  
ANISOU 1162  C   VAL A 183    19395   9713   5332   -367    423    428       C  
ATOM   1163  O   VAL A 183       8.901  -9.478 -27.668  1.00 90.25           O  
ANISOU 1163  O   VAL A 183    19270   9715   5304   -322    221    415       O  
ATOM   1164  CB  VAL A 183      10.045 -12.049 -26.792  1.00 88.15           C  
ANISOU 1164  CB  VAL A 183    18789   9447   5256   -510    392    196       C  
ATOM   1165  CG1 VAL A 183       9.381 -12.747 -27.967  1.00 89.93           C  
ANISOU 1165  CG1 VAL A 183    19234   9729   5207   -477    293    110       C  
ATOM   1166  CG2 VAL A 183      10.951 -13.011 -26.039  1.00 86.99           C  
ANISOU 1166  CG2 VAL A 183    18509   9268   5275   -569    544    144       C  
ATOM   1167  N   PRO A 184      10.394  -9.547 -29.334  1.00 93.79           N  
ANISOU 1167  N   PRO A 184    20033  10084   5519   -304    536    511       N  
ATOM   1168  CA  PRO A 184       9.578  -8.655 -30.163  1.00 94.32           C  
ANISOU 1168  CA  PRO A 184    20295  10170   5371   -176    414    587       C  
ATOM   1169  C   PRO A 184       8.319  -9.345 -30.663  1.00 95.10           C  
ANISOU 1169  C   PRO A 184    20416  10427   5289   -119    167    475       C  
ATOM   1170  O   PRO A 184       8.284 -10.561 -30.867  1.00 95.08           O  
ANISOU 1170  O   PRO A 184    20411  10477   5238   -194    143    341       O  
ATOM   1171  CB  PRO A 184      10.513  -8.298 -31.325  1.00 96.26           C  
ANISOU 1171  CB  PRO A 184    20791  10348   5437   -147    632    698       C  
ATOM   1172  CG  PRO A 184      11.896  -8.593 -30.802  1.00 95.39           C  
ANISOU 1172  CG  PRO A 184    20550  10186   5507   -273    881    725       C  
ATOM   1173  CD  PRO A 184      11.704  -9.808 -29.952  1.00 93.56           C  
ANISOU 1173  CD  PRO A 184    20098  10014   5435   -327    804    568       C  
ATOM   1174  N   PHE A 185       7.274  -8.544 -30.863  1.00100.49           N  
ANISOU 1174  N   PHE A 185    21135  11195   5853     13    -16    537       N  
ATOM   1175  CA  PHE A 185       6.008  -9.045 -31.378  1.00104.66           C  
ANISOU 1175  CA  PHE A 185    21648  11942   6175     58   -275    459       C  
ATOM   1176  C   PHE A 185       5.219  -7.879 -31.954  1.00108.24           C  
ANISOU 1176  C   PHE A 185    22185  12479   6463    277   -390    596       C  
ATOM   1177  O   PHE A 185       5.461  -6.716 -31.620  1.00106.68           O  
ANISOU 1177  O   PHE A 185    22067  12145   6320    390   -299    733       O  
ATOM   1178  CB  PHE A 185       5.208  -9.778 -30.291  1.00 97.40           C  
ANISOU 1178  CB  PHE A 185    20431  11157   5419    -46   -456    334       C  
ATOM   1179  CG  PHE A 185       4.339  -8.879 -29.454  1.00 97.36           C  
ANISOU 1179  CG  PHE A 185    20245  11240   5506     81   -595    410       C  
ATOM   1180  CD1 PHE A 185       4.853  -8.251 -28.332  1.00100.50           C  
ANISOU 1180  CD1 PHE A 185    20546  11475   6164     82   -476    462       C  
ATOM   1181  CD2 PHE A 185       3.001  -8.689 -29.767  1.00 99.96           C  
ANISOU 1181  CD2 PHE A 185    20497  11839   5643    204   -843    433       C  
ATOM   1182  CE1 PHE A 185       4.059  -7.431 -27.552  1.00107.05           C  
ANISOU 1182  CE1 PHE A 185    21254  12364   7058    224   -584    530       C  
ATOM   1183  CE2 PHE A 185       2.202  -7.869 -28.992  1.00103.66           C  
ANISOU 1183  CE2 PHE A 185    20802  12407   6178    372   -948    517       C  
ATOM   1184  CZ  PHE A 185       2.732  -7.241 -27.883  1.00109.46           C  
ANISOU 1184  CZ  PHE A 185    21486  12932   7170    391   -811    561       C  
ATOM   1185  N   THR A 186       4.271  -8.208 -32.828  1.00101.42           N  
ANISOU 1185  N   THR A 186    21291  11841   5403    332   -587    559       N  
ATOM   1186  CA  THR A 186       3.427  -7.222 -33.489  1.00103.80           C  
ANISOU 1186  CA  THR A 186    21628  12282   5529    572   -713    690       C  
ATOM   1187  C   THR A 186       2.028  -7.250 -32.889  1.00104.13           C  
ANISOU 1187  C   THR A 186    21424  12627   5515    650   -990    679       C  
ATOM   1188  O   THR A 186       1.461  -8.324 -32.662  1.00105.38           O  
ANISOU 1188  O   THR A 186    21404  12984   5651    471  -1154    540       O  
ATOM   1189  CB  THR A 186       3.350  -7.481 -34.995  1.00106.44           C  
ANISOU 1189  CB  THR A 186    22090  12711   5643    598   -741    682       C  
ATOM   1190  OG1 THR A 186       3.004  -8.852 -35.229  1.00107.99           O  
ANISOU 1190  OG1 THR A 186    22192  13066   5774    392   -870    507       O  
ATOM   1191  CG2 THR A 186       4.687  -7.181 -35.655  1.00106.64           C  
ANISOU 1191  CG2 THR A 186    22361  12459   5697    585   -453    740       C  
ATOM   1192  N   LYS A 187       1.474  -6.064 -32.641  1.00152.93           N  
ANISOU 1192  N   LYS A 187    27602  18843  11661    918  -1032    833       N  
ATOM   1193  CA  LYS A 187       0.164  -5.950 -32.012  1.00150.68           C  
ANISOU 1193  CA  LYS A 187    27065  18872  11314   1054  -1270    859       C  
ATOM   1194  C   LYS A 187      -0.933  -5.706 -33.042  1.00161.55           C  
ANISOU 1194  C   LYS A 187    28363  20608  12412   1251  -1476    939       C  
ATOM   1195  O   LYS A 187      -1.659  -6.633 -33.415  1.00167.63           O  
ANISOU 1195  O   LYS A 187    28946  21707  13040   1099  -1686    842       O  
ATOM   1196  CB  LYS A 187       0.168  -4.830 -30.970  1.00148.25           C  
ANISOU 1196  CB  LYS A 187    26792  18399  11137   1268  -1182    981       C  
ATOM   1197  CG  LYS A 187      -0.966  -4.918 -29.962  1.00153.49           C  
ANISOU 1197  CG  LYS A 187    27135  19348  11835   1362  -1375    977       C  
ATOM   1198  CD  LYS A 187      -0.834  -3.859 -28.877  1.00148.51           C  
ANISOU 1198  CD  LYS A 187    26547  18494  11386   1555  -1246   1075       C  
ATOM   1199  CE  LYS A 187       0.539  -3.898 -28.225  1.00135.74           C  
ANISOU 1199  CE  LYS A 187    25056  16460  10059   1308  -1002   1006       C  
ATOM   1200  NZ  LYS A 187       0.629  -2.971 -27.063  1.00133.15           N  
ANISOU 1200  NZ  LYS A 187    24767  15922   9903   1436   -899   1074       N  
ATOM   1201  N   ASN A 188      -1.063  -4.464 -33.506  1.00175.89           N  
ANISOU 1201  N   ASN A 188    30324  22367  14138   1572  -1416   1117       N  
ATOM   1202  CA  ASN A 188      -2.138  -4.073 -34.411  1.00172.85           C  
ANISOU 1202  CA  ASN A 188    29849  22343  13483   1819  -1604   1228       C  
ATOM   1203  C   ASN A 188      -1.551  -3.311 -35.589  1.00170.84           C  
ANISOU 1203  C   ASN A 188    29906  21877  13129   1960  -1449   1332       C  
ATOM   1204  O   ASN A 188      -0.963  -2.240 -35.404  1.00177.20           O  
ANISOU 1204  O   ASN A 188    30952  22345  14032   2128  -1244   1445       O  
ATOM   1205  CB  ASN A 188      -3.180  -3.215 -33.687  1.00178.41           C  
ANISOU 1205  CB  ASN A 188    30376  23261  14151   2168  -1709   1373       C  
ATOM   1206  CG  ASN A 188      -3.973  -4.002 -32.663  1.00187.83           C  
ANISOU 1206  CG  ASN A 188    31211  24773  15384   2045  -1904   1285       C  
ATOM   1207  OD1 ASN A 188      -4.142  -5.215 -32.790  1.00189.07           O  
ANISOU 1207  OD1 ASN A 188    31205  25134  15500   1719  -2046   1130       O  
ATOM   1208  ND2 ASN A 188      -4.462  -3.314 -31.637  1.00188.08           N  
ANISOU 1208  ND2 ASN A 188    31136  24835  15492   2302  -1900   1381       N  
ATOM   1209  N   ASN A 189      -1.715  -3.863 -36.793  1.00132.12           N  
ANISOU 1209  N   ASN A 189    25012  17166   8023   1872  -1546   1291       N  
ATOM   1210  CA  ASN A 189      -1.292  -3.219 -38.037  1.00126.51           C  
ANISOU 1210  CA  ASN A 189    24575  16318   7175   2009  -1430   1390       C  
ATOM   1211  C   ASN A 189       0.210  -2.928 -38.028  1.00122.01           C  
ANISOU 1211  C   ASN A 189    24320  15243   6797   1891  -1109   1381       C  
ATOM   1212  O   ASN A 189       0.654  -1.790 -38.194  1.00122.88           O  
ANISOU 1212  O   ASN A 189    24672  15088   6930   2077   -934   1519       O  
ATOM   1213  CB  ASN A 189      -2.102  -1.944 -38.295  1.00127.00           C  
ANISOU 1213  CB  ASN A 189    24659  16506   7090   2433  -1483   1601       C  
ATOM   1214  CG  ASN A 189      -2.457  -1.764 -39.756  1.00130.68           C  
ANISOU 1214  CG  ASN A 189    25209  17167   7276   2557  -1564   1677       C  
ATOM   1215  OD1 ASN A 189      -2.407  -2.712 -40.540  1.00135.35           O  
ANISOU 1215  OD1 ASN A 189    25767  17916   7742   2323  -1655   1562       O  
ATOM   1216  ND2 ASN A 189      -2.817  -0.542 -40.131  1.00135.25           N  
ANISOU 1216  ND2 ASN A 189    25920  17721   7746   2932  -1526   1867       N  
ATOM   1217  N   ASN A 190       0.989  -3.995 -37.836  1.00116.70           N  
ANISOU 1217  N   ASN A 190    23637  14454   6250   1567  -1031   1217       N  
ATOM   1218  CA  ASN A 190       2.451  -3.922 -37.806  1.00114.98           C  
ANISOU 1218  CA  ASN A 190    23648  13837   6202   1416   -733   1202       C  
ATOM   1219  C   ASN A 190       2.929  -2.944 -36.732  1.00113.36           C  
ANISOU 1219  C   ASN A 190    23520  13350   6201   1482   -570   1295       C  
ATOM   1220  O   ASN A 190       3.778  -2.082 -36.971  1.00113.86           O  
ANISOU 1220  O   ASN A 190    23830  13122   6309   1513   -348   1397       O  
ATOM   1221  CB  ASN A 190       3.012  -3.554 -39.184  1.00117.35           C  
ANISOU 1221  CB  ASN A 190    24207  14030   6351   1476   -599   1274       C  
ATOM   1222  CG  ASN A 190       4.503  -3.825 -39.303  1.00115.94           C  
ANISOU 1222  CG  ASN A 190    24199  13547   6307   1271   -312   1235       C  
ATOM   1223  OD1 ASN A 190       5.136  -4.303 -38.362  1.00113.23           O  
ANISOU 1223  OD1 ASN A 190    23776  13080   6168   1086   -212   1157       O  
ATOM   1224  ND2 ASN A 190       5.069  -3.519 -40.466  1.00118.01           N  
ANISOU 1224  ND2 ASN A 190    24682  13712   6443   1313   -173   1301       N  
ATOM   1225  N   GLN A 191       2.364  -3.081 -35.535  1.00135.89           N  
ANISOU 1225  N   GLN A 191    26168  16295   9170   1483   -684   1258       N  
ATOM   1226  CA  GLN A 191       2.771  -2.282 -34.381  1.00132.03           C  
ANISOU 1226  CA  GLN A 191    25744  15545   8877   1513   -548   1321       C  
ATOM   1227  C   GLN A 191       3.806  -3.081 -33.601  1.00120.07           C  
ANISOU 1227  C   GLN A 191    24179  13864   7577   1191   -411   1198       C  
ATOM   1228  O   GLN A 191       3.462  -3.992 -32.845  1.00122.76           O  
ANISOU 1228  O   GLN A 191    24295  14352   7996   1063   -532   1075       O  
ATOM   1229  CB  GLN A 191       1.571  -1.927 -33.512  1.00135.53           C  
ANISOU 1229  CB  GLN A 191    25999  16187   9310   1733   -734   1362       C  
ATOM   1230  CG  GLN A 191       1.681  -0.577 -32.821  1.00139.74           C  
ANISOU 1230  CG  GLN A 191    26719  16447   9927   1935   -601   1497       C  
ATOM   1231  CD  GLN A 191       0.351  -0.087 -32.281  1.00143.69           C  
ANISOU 1231  CD  GLN A 191    27060  17187  10348   2269   -778   1575       C  
ATOM   1232  OE1 GLN A 191      -0.693  -0.693 -32.522  1.00149.14           O  
ANISOU 1232  OE1 GLN A 191    27473  18296  10898   2352  -1013   1550       O  
ATOM   1233  NE2 GLN A 191       0.384   1.017 -31.544  1.00143.60           N  
ANISOU 1233  NE2 GLN A 191    27222  16923  10416   2455   -660   1671       N  
ATOM   1234  N   THR A 192       5.079  -2.743 -33.786  1.00120.49           N  
ANISOU 1234  N   THR A 192    24432  13630   7717   1058   -154   1239       N  
ATOM   1235  CA  THR A 192       6.142  -3.458 -33.095  1.00126.83           C  
ANISOU 1235  CA  THR A 192    25172  14310   8706    775     -4   1148       C  
ATOM   1236  C   THR A 192       6.096  -3.174 -31.597  1.00127.46           C  
ANISOU 1236  C   THR A 192    25158  14301   8971    726     -9   1144       C  
ATOM   1237  O   THR A 192       5.897  -2.035 -31.165  1.00129.94           O  
ANISOU 1237  O   THR A 192    25592  14472   9307    860     19   1254       O  
ATOM   1238  CB  THR A 192       7.508  -3.083 -33.678  1.00127.48           C  
ANISOU 1238  CB  THR A 192    25456  14169   8812    648    276   1222       C  
ATOM   1239  OG1 THR A 192       8.541  -3.802 -32.991  1.00133.91           O  
ANISOU 1239  OG1 THR A 192    26167  14921   9790    397    425   1152       O  
ATOM   1240  CG2 THR A 192       7.765  -1.581 -33.575  1.00128.97           C  
ANISOU 1240  CG2 THR A 192    25870  14118   9014    728    401   1381       C  
ATOM   1241  N   ALA A 193       6.260  -4.230 -30.803  1.00131.54           N  
ANISOU 1241  N   ALA A 193    25478  14891   9612    542    -42   1012       N  
ATOM   1242  CA  ALA A 193       6.224  -4.119 -29.353  1.00129.95           C  
ANISOU 1242  CA  ALA A 193    25072  14630   9672    471    -54    974       C  
ATOM   1243  C   ALA A 193       7.031  -5.260 -28.752  1.00124.55           C  
ANISOU 1243  C   ALA A 193    24158  13947   9217    212     27    838       C  
ATOM   1244  O   ALA A 193       7.113  -6.350 -29.324  1.00127.28           O  
ANISOU 1244  O   ALA A 193    24454  14408   9499    138      6    738       O  
ATOM   1245  CB  ALA A 193       4.788  -4.140 -28.816  1.00123.53           C  
ANISOU 1245  CB  ALA A 193    24063  14032   8839    650   -305    944       C  
ATOM   1246  N   ASN A 194       7.625  -4.998 -27.594  1.00 93.37           N  
ANISOU 1246  N   ASN A 194    20096   9865   5515     85    124    838       N  
ATOM   1247  CA  ASN A 194       8.470  -5.965 -26.914  1.00 91.35           C  
ANISOU 1247  CA  ASN A 194    19620   9611   5478   -131    218    736       C  
ATOM   1248  C   ASN A 194       7.770  -6.502 -25.672  1.00 89.38           C  
ANISOU 1248  C   ASN A 194    19085   9454   5422   -155     65    626       C  
ATOM   1249  O   ASN A 194       6.886  -5.861 -25.099  1.00 89.41           O  
ANISOU 1249  O   ASN A 194    19058   9476   5439    -30    -61    654       O  
ATOM   1250  CB  ASN A 194       9.815  -5.338 -26.529  1.00 91.18           C  
ANISOU 1250  CB  ASN A 194    19653   9411   5580   -297    452    826       C  
ATOM   1251  CG  ASN A 194      10.788  -5.290 -27.690  1.00 92.84           C  
ANISOU 1251  CG  ASN A 194    20051   9586   5638   -346    648    908       C  
ATOM   1252  OD1 ASN A 194      11.951  -4.921 -27.527  1.00 93.10           O  
ANISOU 1252  OD1 ASN A 194    20095   9538   5742   -511    848    988       O  
ATOM   1253  ND2 ASN A 194      10.317  -5.665 -28.872  1.00 94.20           N  
ANISOU 1253  ND2 ASN A 194    20363   9844   5584   -213    590    892       N  
ATOM   1254  N   MET A 195       8.172  -7.704 -25.268  1.00 88.03           N  
ANISOU 1254  N   MET A 195    18721   9342   5385   -297     90    508       N  
ATOM   1255  CA  MET A 195       7.710  -8.289 -24.021  1.00 86.10           C  
ANISOU 1255  CA  MET A 195    18212   9163   5340   -358    -18    406       C  
ATOM   1256  C   MET A 195       8.883  -8.969 -23.333  1.00 84.76           C  
ANISOU 1256  C   MET A 195    17905   8931   5368   -526    144    364       C  
ATOM   1257  O   MET A 195       9.810  -9.454 -23.986  1.00 85.15           O  
ANISOU 1257  O   MET A 195    18026   8962   5366   -574    300    372       O  
ATOM   1258  CB  MET A 195       6.560  -9.285 -24.236  1.00 86.27           C  
ANISOU 1258  CB  MET A 195    18128   9382   5270   -336   -224    288       C  
ATOM   1259  CG  MET A 195       6.816 -10.353 -25.283  1.00 89.37           C  
ANISOU 1259  CG  MET A 195    18634   9819   5505   -397   -194    210       C  
ATOM   1260  SD  MET A 195       5.336 -11.339 -25.595  1.00 98.59           S  
ANISOU 1260  SD  MET A 195    19723  11228   6508   -431   -469     81       S  
ATOM   1261  CE  MET A 195       5.921 -12.451 -26.871  1.00 89.57           C  
ANISOU 1261  CE  MET A 195    18834  10043   5156   -514   -376     -5       C  
ATOM   1262  N   CYS A 196       8.837  -8.986 -22.004  1.00 97.61           N  
ANISOU 1262  N   CYS A 196    19334  10545   7209   -591    111    329       N  
ATOM   1263  CA  CYS A 196       9.912  -9.525 -21.180  1.00 94.70           C  
ANISOU 1263  CA  CYS A 196    18804  10145   7031   -731    248    307       C  
ATOM   1264  C   CYS A 196       9.551 -10.956 -20.797  1.00 93.04           C  
ANISOU 1264  C   CYS A 196    18443  10025   6882   -759    175    168       C  
ATOM   1265  O   CYS A 196       8.638 -11.179 -19.996  1.00 98.92           O  
ANISOU 1265  O   CYS A 196    19051  10825   7709   -760     22     99       O  
ATOM   1266  CB  CYS A 196      10.130  -8.649 -19.946  1.00 99.00           C  
ANISOU 1266  CB  CYS A 196    19258  10609   7749   -800    258    355       C  
ATOM   1267  SG  CYS A 196      11.200  -9.347 -18.668  1.00105.24           S  
ANISOU 1267  SG  CYS A 196    19785  11424   8779   -963    364    320       S  
ATOM   1268  N   ARG A 197      10.263 -11.922 -21.377  1.00 81.74           N  
ANISOU 1268  N   ARG A 197    17061   8603   5394   -777    298    134       N  
ATOM   1269  CA  ARG A 197      10.003 -13.336 -21.150  1.00 82.28           C  
ANISOU 1269  CA  ARG A 197    17080   8708   5476   -805    260      4       C  
ATOM   1270  C   ARG A 197      11.282 -14.041 -20.725  1.00 84.46           C  
ANISOU 1270  C   ARG A 197    17277   8958   5856   -823    463     16       C  
ATOM   1271  O   ARG A 197      12.373 -13.705 -21.196  1.00 82.79           O  
ANISOU 1271  O   ARG A 197    17102   8743   5610   -799    649    116       O  
ATOM   1272  CB  ARG A 197       9.439 -14.009 -22.409  1.00 81.89           C  
ANISOU 1272  CB  ARG A 197    17246   8687   5181   -772    199    -68       C  
ATOM   1273  CG  ARG A 197       8.113 -13.444 -22.880  1.00 82.72           C  
ANISOU 1273  CG  ARG A 197    17395   8884   5149   -742    -21    -74       C  
ATOM   1274  CD  ARG A 197       6.953 -14.158 -22.210  1.00 82.99           C  
ANISOU 1274  CD  ARG A 197    17290   9024   5218   -825   -222   -188       C  
ATOM   1275  NE  ARG A 197       5.664 -13.646 -22.656  1.00 84.67           N  
ANISOU 1275  NE  ARG A 197    17491   9398   5280   -781   -438   -176       N  
ATOM   1276  CZ  ARG A 197       5.057 -12.589 -22.135  1.00 86.84           C  
ANISOU 1276  CZ  ARG A 197    17638   9743   5616   -683   -531    -95       C  
ATOM   1277  NH1 ARG A 197       5.601 -11.897 -21.146  1.00 83.15           N  
ANISOU 1277  NH1 ARG A 197    17072   9168   5355   -653   -436    -32       N  
ATOM   1278  NH2 ARG A 197       3.876 -12.215 -22.619  1.00 90.61           N  
ANISOU 1278  NH2 ARG A 197    18094  10412   5921   -605   -722    -71       N  
ATOM   1279  N   PHE A 198      11.139 -15.021 -19.835  1.00 78.75           N  
ANISOU 1279  N   PHE A 198    16440   8236   5245   -856    433    -74       N  
ATOM   1280  CA  PHE A 198      12.258 -15.847 -19.392  1.00 78.60           C  
ANISOU 1280  CA  PHE A 198    16351   8212   5303   -825    618    -63       C  
ATOM   1281  C   PHE A 198      12.363 -17.051 -20.321  1.00 80.09           C  
ANISOU 1281  C   PHE A 198    16779   8350   5301   -747    703   -137       C  
ATOM   1282  O   PHE A 198      11.462 -17.896 -20.358  1.00 80.21           O  
ANISOU 1282  O   PHE A 198    16913   8320   5245   -793    581   -265       O  
ATOM   1283  CB  PHE A 198      12.069 -16.288 -17.943  1.00 76.91           C  
ANISOU 1283  CB  PHE A 198    15932   8004   5286   -879    555   -113       C  
ATOM   1284  CG  PHE A 198      13.224 -17.079 -17.393  1.00 76.92           C  
ANISOU 1284  CG  PHE A 198    15840   8025   5361   -813    740    -80       C  
ATOM   1285  CD1 PHE A 198      14.503 -16.548 -17.379  1.00 77.47           C  
ANISOU 1285  CD1 PHE A 198    15782   8184   5469   -783    914     57       C  
ATOM   1286  CD2 PHE A 198      13.030 -18.359 -16.898  1.00 76.71           C  
ANISOU 1286  CD2 PHE A 198    15857   7945   5346   -782    744   -174       C  
ATOM   1287  CE1 PHE A 198      15.566 -17.275 -16.875  1.00 77.84           C  
ANISOU 1287  CE1 PHE A 198    15704   8308   5562   -690   1083    109       C  
ATOM   1288  CE2 PHE A 198      14.090 -19.091 -16.394  1.00 77.02           C  
ANISOU 1288  CE2 PHE A 198    15823   8010   5430   -669    923   -127       C  
ATOM   1289  CZ  PHE A 198      15.359 -18.548 -16.383  1.00 77.60           C  
ANISOU 1289  CZ  PHE A 198    15728   8216   5540   -606   1091     19       C  
ATOM   1290  N   LEU A 199      13.460 -17.130 -21.069  1.00 96.53           N  
ANISOU 1290  N   LEU A 199    18949  10446   7283   -639    920    -56       N  
ATOM   1291  CA  LEU A 199      13.660 -18.188 -22.050  1.00 98.74           C  
ANISOU 1291  CA  LEU A 199    19512  10659   7347   -530   1035   -116       C  
ATOM   1292  C   LEU A 199      15.021 -18.835 -21.841  1.00100.56           C  
ANISOU 1292  C   LEU A 199    19690  10924   7593   -369   1302    -39       C  
ATOM   1293  O   LEU A 199      16.045 -18.146 -21.800  1.00102.55           O  
ANISOU 1293  O   LEU A 199    19757  11303   7904   -331   1451    110       O  
ATOM   1294  CB  LEU A 199      13.516 -17.641 -23.481  1.00 93.66           C  
ANISOU 1294  CB  LEU A 199    19089  10013   6485   -503   1042    -86       C  
ATOM   1295  CG  LEU A 199      14.205 -16.326 -23.865  1.00 94.23           C  
ANISOU 1295  CG  LEU A 199    19065  10166   6574   -498   1137     77       C  
ATOM   1296  CD1 LEU A 199      15.617 -16.536 -24.389  1.00104.70           C  
ANISOU 1296  CD1 LEU A 199    20405  11554   7821   -365   1431    192       C  
ATOM   1297  CD2 LEU A 199      13.362 -15.568 -24.881  1.00 94.99           C  
ANISOU 1297  CD2 LEU A 199    19345  10243   6503   -527    998     75       C  
ATOM   1298  N   LEU A 200      15.021 -20.149 -21.694  1.00 88.82           N  
ANISOU 1298  N   LEU A 200    18371   9339   6039   -278   1365   -130       N  
ATOM   1299  CA  LEU A 200      16.215 -20.961 -21.539  1.00 85.95           C  
ANISOU 1299  CA  LEU A 200    18009   9003   5644    -57   1627    -62       C  
ATOM   1300  C   LEU A 200      16.555 -21.635 -22.862  1.00 93.75           C  
ANISOU 1300  C   LEU A 200    19370   9906   6346    120   1804    -81       C  
ATOM   1301  O   LEU A 200      15.753 -21.623 -23.801  1.00 93.53           O  
ANISOU 1301  O   LEU A 200    19617   9775   6145     34   1692   -178       O  
ATOM   1302  CB  LEU A 200      15.993 -21.996 -20.431  1.00 95.21           C  
ANISOU 1302  CB  LEU A 200    19177  10087   6913    -37   1599   -144       C  
ATOM   1303  CG  LEU A 200      16.264 -21.506 -19.003  1.00 86.42           C  
ANISOU 1303  CG  LEU A 200    17659   9105   6071   -104   1544    -70       C  
ATOM   1304  CD1 LEU A 200      15.447 -22.292 -17.992  1.00 88.96           C  
ANISOU 1304  CD1 LEU A 200    18015   9302   6484   -188   1406   -193       C  
ATOM   1305  CD2 LEU A 200      17.746 -21.583 -18.664  1.00 87.66           C  
ANISOU 1305  CD2 LEU A 200    17594   9447   6265    101   1790     96       C  
ATOM   1306  N   PRO A 201      17.768 -22.219 -22.990  1.00108.05           N  
ANISOU 1306  N   PRO A 201    21197  11780   8077    388   2090     19       N  
ATOM   1307  CA  PRO A 201      18.153 -22.851 -24.262  1.00109.01           C  
ANISOU 1307  CA  PRO A 201    21698  11817   7902    596   2290      9       C  
ATOM   1308  C   PRO A 201      17.136 -23.840 -24.814  1.00110.15           C  
ANISOU 1308  C   PRO A 201    22334  11682   7836    539   2186   -196       C  
ATOM   1309  O   PRO A 201      16.610 -23.633 -25.912  1.00119.36           O  
ANISOU 1309  O   PRO A 201    23758  12782   8811    460   2115   -261       O  
ATOM   1310  CB  PRO A 201      19.472 -23.544 -23.905  1.00107.88           C  
ANISOU 1310  CB  PRO A 201    21466  11787   7737    924   2596    138       C  
ATOM   1311  CG  PRO A 201      20.073 -22.627 -22.903  1.00106.60           C  
ANISOU 1311  CG  PRO A 201    20766  11895   7842    837   2573    291       C  
ATOM   1312  CD  PRO A 201      18.908 -22.181 -22.052  1.00106.67           C  
ANISOU 1312  CD  PRO A 201    20662  11809   8059    526   2253    173       C  
ATOM   1313  N   ASN A 202      16.848 -24.907 -24.079  1.00110.33           N  
ANISOU 1313  N   ASN A 202    22506  11543   7871    559   2171   -298       N  
ATOM   1314  CA  ASN A 202      15.909 -25.924 -24.529  1.00114.83           C  
ANISOU 1314  CA  ASN A 202    23571  11837   8222    453   2077   -496       C  
ATOM   1315  C   ASN A 202      14.808 -26.120 -23.495  1.00104.27           C  
ANISOU 1315  C   ASN A 202    22138  10430   7050    169   1812   -615       C  
ATOM   1316  O   ASN A 202      14.856 -25.583 -22.386  1.00105.27           O  
ANISOU 1316  O   ASN A 202    21847  10697   7455    110   1732   -545       O  
ATOM   1317  CB  ASN A 202      16.622 -27.253 -24.813  1.00112.94           C  
ANISOU 1317  CB  ASN A 202    23675  11404   7833    758   2339   -503       C  
ATOM   1318  CG  ASN A 202      17.501 -27.706 -23.662  1.00114.55           C  
ANISOU 1318  CG  ASN A 202    23745  11668   8111   1009   2541   -404       C  
ATOM   1319  OD1 ASN A 202      17.043 -27.839 -22.525  1.00115.46           O  
ANISOU 1319  OD1 ASN A 202    23685  11763   8422    862   2397   -444       O  
ATOM   1320  ND2 ASN A 202      18.770 -27.962 -23.955  1.00112.41           N  
ANISOU 1320  ND2 ASN A 202    23454  11497   7760   1398   2852   -253       N  
ATOM   1321  N   ASP A 203      13.800 -26.906 -23.880  1.00119.97           N  
ANISOU 1321  N   ASP A 203    24462  12212   8908    -29   1661   -783       N  
ATOM   1322  CA  ASP A 203      12.685 -27.167 -22.978  1.00119.55           C  
ANISOU 1322  CA  ASP A 203    24342  12113   8968   -327   1416   -896       C  
ATOM   1323  C   ASP A 203      13.094 -28.078 -21.829  1.00118.99           C  
ANISOU 1323  C   ASP A 203    24322  11916   8974   -211   1548   -897       C  
ATOM   1324  O   ASP A 203      12.472 -28.046 -20.763  1.00121.54           O  
ANISOU 1324  O   ASP A 203    24452  12269   9460   -399   1391   -936       O  
ATOM   1325  CB  ASP A 203      11.515 -27.778 -23.752  1.00125.51           C  
ANISOU 1325  CB  ASP A 203    25331  12731   9627   -606   1209  -1031       C  
ATOM   1326  CG  ASP A 203      10.859 -26.792 -24.695  1.00134.02           C  
ANISOU 1326  CG  ASP A 203    26298  13983  10641   -757   1016  -1033       C  
ATOM   1327  OD1 ASP A 203      11.363 -25.656 -24.814  1.00137.27           O  
ANISOU 1327  OD1 ASP A 203    26501  14576  11079   -632   1062   -927       O  
ATOM   1328  OD2 ASP A 203       9.838 -27.153 -25.316  1.00136.15           O  
ANISOU 1328  OD2 ASP A 203    26694  14217  10819  -1006    821  -1129       O  
ATOM   1329  N   VAL A 204      14.127 -28.897 -22.026  1.00 95.08           N  
ANISOU 1329  N   VAL A 204    21514   8755   5858    119   1833   -837       N  
ATOM   1330  CA  VAL A 204      14.610 -29.752 -20.947  1.00 95.20           C  
ANISOU 1330  CA  VAL A 204    21584   8661   5927    294   1982   -812       C  
ATOM   1331  C   VAL A 204      15.197 -28.904 -19.825  1.00 92.50           C  
ANISOU 1331  C   VAL A 204    20695   8595   5855    382   1991   -667       C  
ATOM   1332  O   VAL A 204      14.917 -29.129 -18.642  1.00 93.41           O  
ANISOU 1332  O   VAL A 204    20647   8699   6144    297   1909   -677       O  
ATOM   1333  CB  VAL A 204      15.632 -30.771 -21.484  1.00 98.49           C  
ANISOU 1333  CB  VAL A 204    22321   8901   6200    689   2289   -744       C  
ATOM   1334  CG1 VAL A 204      16.423 -31.387 -20.340  1.00 98.56           C  
ANISOU 1334  CG1 VAL A 204    22293   8896   6259    984   2489   -656       C  
ATOM   1335  CG2 VAL A 204      14.926 -31.851 -22.288  1.00101.39           C  
ANISOU 1335  CG2 VAL A 204    23156   8928   6438    539   2226   -865       C  
ATOM   1336  N   MET A 205      16.009 -27.907 -20.182  1.00 97.24           N  
ANISOU 1336  N   MET A 205    20960   9452   6534    524   2074   -515       N  
ATOM   1337  CA  MET A 205      16.551 -26.992 -19.185  1.00101.11           C  
ANISOU 1337  CA  MET A 205    20880  10220   7318    540   2047   -366       C  
ATOM   1338  C   MET A 205      15.471 -26.124 -18.551  1.00 99.06           C  
ANISOU 1338  C   MET A 205    20331  10030   7276    181   1733   -427       C  
ATOM   1339  O   MET A 205      15.674 -25.613 -17.444  1.00102.28           O  
ANISOU 1339  O   MET A 205    20349  10590   7922    147   1677   -350       O  
ATOM   1340  CB  MET A 205      17.626 -26.107 -19.819  1.00104.37           C  
ANISOU 1340  CB  MET A 205    21043  10885   7726    712   2206   -193       C  
ATOM   1341  CG  MET A 205      18.981 -26.783 -19.964  1.00102.76           C  
ANISOU 1341  CG  MET A 205    20896  10756   7392   1131   2544    -55       C  
ATOM   1342  SD  MET A 205      20.127 -25.824 -20.976  1.00107.84           S  
ANISOU 1342  SD  MET A 205    21308  11703   7963   1289   2741    139       S  
ATOM   1343  CE  MET A 205      20.872 -24.769 -19.734  1.00116.33           C  
ANISOU 1343  CE  MET A 205    21690  13158   9351   1204   2696    325       C  
ATOM   1344  N   GLN A 206      14.332 -25.949 -19.225  1.00 91.85           N  
ANISOU 1344  N   GLN A 206    19601   9030   6268    -72   1531   -558       N  
ATOM   1345  CA  GLN A 206      13.238 -25.165 -18.663  1.00 88.76           C  
ANISOU 1345  CA  GLN A 206    18946   8727   6051   -369   1244   -606       C  
ATOM   1346  C   GLN A 206      12.472 -25.959 -17.611  1.00 96.26           C  
ANISOU 1346  C   GLN A 206    19938   9562   7076   -521   1130   -708       C  
ATOM   1347  O   GLN A 206      12.211 -25.457 -16.512  1.00 96.08           O  
ANISOU 1347  O   GLN A 206    19575   9649   7282   -614   1014   -676       O  
ATOM   1348  CB  GLN A 206      12.296 -24.704 -19.777  1.00 85.94           C  
ANISOU 1348  CB  GLN A 206    18740   8374   5540   -556   1069   -687       C  
ATOM   1349  CG  GLN A 206      11.240 -23.705 -19.331  1.00 86.80           C  
ANISOU 1349  CG  GLN A 206    18545   8629   5806   -789    795   -699       C  
ATOM   1350  CD  GLN A 206      11.749 -22.277 -19.331  1.00 91.03           C  
ANISOU 1350  CD  GLN A 206    18757   9343   6487   -723    803   -555       C  
ATOM   1351  OE1 GLN A 206      12.813 -21.988 -19.876  1.00 92.86           O  
ANISOU 1351  OE1 GLN A 206    18995   9612   6676   -550    995   -450       O  
ATOM   1352  NE2 GLN A 206      10.989 -21.376 -18.719  1.00 91.66           N  
ANISOU 1352  NE2 GLN A 206    18570   9533   6722   -863    604   -543       N  
ATOM   1353  N   GLN A 207      12.105 -27.202 -17.929  1.00124.89           N  
ANISOU 1353  N   GLN A 207    24008  12953  10492   -560   1170   -833       N  
ATOM   1354  CA  GLN A 207      11.329 -28.006 -16.994  1.00127.18           C  
ANISOU 1354  CA  GLN A 207    24384  13117  10822   -747   1068   -931       C  
ATOM   1355  C   GLN A 207      12.172 -28.530 -15.838  1.00127.76           C  
ANISOU 1355  C   GLN A 207    24365  13149  11029   -525   1239   -849       C  
ATOM   1356  O   GLN A 207      11.614 -28.883 -14.794  1.00131.99           O  
ANISOU 1356  O   GLN A 207    24829  13644  11676   -669   1144   -890       O  
ATOM   1357  CB  GLN A 207      10.657 -29.167 -17.730  1.00123.77           C  
ANISOU 1357  CB  GLN A 207    24509  12426  10091   -911   1054  -1094       C  
ATOM   1358  CG  GLN A 207      11.622 -30.103 -18.433  1.00132.86           C  
ANISOU 1358  CG  GLN A 207    26098  13352  11031   -615   1337  -1080       C  
ATOM   1359  CD  GLN A 207      11.050 -30.664 -19.720  1.00140.14           C  
ANISOU 1359  CD  GLN A 207    27330  14119  11799   -768   1272  -1151       C  
ATOM   1360  OE1 GLN A 207      10.139 -30.086 -20.312  1.00140.24           O  
ANISOU 1360  OE1 GLN A 207    27229  14262  11795  -1037   1045  -1204       O  
ATOM   1361  NE2 GLN A 207      11.583 -31.798 -20.159  1.00145.58           N  
ANISOU 1361  NE2 GLN A 207    28421  14535  12356   -583   1475  -1144       N  
ATOM   1362  N   SER A 208      13.496 -28.591 -15.996  1.00 85.92           N  
ANISOU 1362  N   SER A 208    19050   7888   5708   -171   1490   -722       N  
ATOM   1363  CA  SER A 208      14.360 -28.965 -14.884  1.00 85.60           C  
ANISOU 1363  CA  SER A 208    18847   7885   5792     69   1642   -613       C  
ATOM   1364  C   SER A 208      14.659 -27.788 -13.964  1.00 87.29           C  
ANISOU 1364  C   SER A 208    18478   8393   6297     34   1546   -493       C  
ATOM   1365  O   SER A 208      15.129 -27.999 -12.841  1.00 90.16           O  
ANISOU 1365  O   SER A 208    18648   8817   6790    149   1599   -419       O  
ATOM   1366  CB  SER A 208      15.670 -29.561 -15.404  1.00 88.09           C  
ANISOU 1366  CB  SER A 208    19362   8173   5937    489   1960   -507       C  
ATOM   1367  OG  SER A 208      16.565 -28.546 -15.822  1.00 87.72           O  
ANISOU 1367  OG  SER A 208    18963   8410   5957    630   2037   -358       O  
ATOM   1368  N   TRP A 209      14.396 -26.561 -14.414  1.00 84.47           N  
ANISOU 1368  N   TRP A 209    17869   8203   6021   -120   1408   -473       N  
ATOM   1369  CA  TRP A 209      14.575 -25.386 -13.569  1.00 79.35           C  
ANISOU 1369  CA  TRP A 209    16739   7789   5621   -197   1304   -376       C  
ATOM   1370  C   TRP A 209      13.364 -25.165 -12.671  1.00 78.65           C  
ANISOU 1370  C   TRP A 209    16527   7678   5678   -466   1062   -469       C  
ATOM   1371  O   TRP A 209      13.507 -24.984 -11.457  1.00 84.29           O  
ANISOU 1371  O   TRP A 209    16980   8475   6570   -473   1027   -421       O  
ATOM   1372  CB  TRP A 209      14.832 -24.155 -14.440  1.00 80.95           C  
ANISOU 1372  CB  TRP A 209    16786   8147   5824   -234   1283   -306       C  
ATOM   1373  CG  TRP A 209      14.857 -22.856 -13.691  1.00 77.98           C  
ANISOU 1373  CG  TRP A 209    16004   7959   5666   -366   1158   -229       C  
ATOM   1374  CD1 TRP A 209      13.918 -21.867 -13.738  1.00 77.79           C  
ANISOU 1374  CD1 TRP A 209    15886   7958   5712   -578    951   -272       C  
ATOM   1375  CD2 TRP A 209      15.882 -22.393 -12.801  1.00 76.61           C  
ANISOU 1375  CD2 TRP A 209    15495   7976   5639   -291   1238    -91       C  
ATOM   1376  NE1 TRP A 209      14.289 -20.822 -12.927  1.00 76.16           N  
ANISOU 1376  NE1 TRP A 209    15355   7898   5683   -638    908   -180       N  
ATOM   1377  CE2 TRP A 209      15.492 -21.118 -12.342  1.00 74.92           C  
ANISOU 1377  CE2 TRP A 209    15039   7853   5576   -493   1071    -73       C  
ATOM   1378  CE3 TRP A 209      17.089 -22.933 -12.346  1.00 77.71           C  
ANISOU 1378  CE3 TRP A 209    15516   8236   5775    -66   1433     25       C  
ATOM   1379  CZ2 TRP A 209      16.264 -20.377 -11.449  1.00 74.31           C  
ANISOU 1379  CZ2 TRP A 209    14636   7956   5641   -527   1085     41       C  
ATOM   1380  CZ3 TRP A 209      17.855 -22.195 -11.460  1.00 77.09           C  
ANISOU 1380  CZ3 TRP A 209    15057   8390   5844    -96   1434    150       C  
ATOM   1381  CH2 TRP A 209      17.438 -20.932 -11.020  1.00 75.40           C  
ANISOU 1381  CH2 TRP A 209    14635   8237   5775   -349   1257    149       C  
ATOM   1382  N   HIS A 210      12.162 -25.183 -13.253  1.00103.77           N  
ANISOU 1382  N   HIS A 210    19882  10776   8770   -686    893   -593       N  
ATOM   1383  CA  HIS A 210      10.952 -25.005 -12.457  1.00106.08           C  
ANISOU 1383  CA  HIS A 210    20040  11091   9175   -931    672   -669       C  
ATOM   1384  C   HIS A 210      10.729 -26.172 -11.504  1.00102.00           C  
ANISOU 1384  C   HIS A 210    19656  10432   8669   -959    703   -726       C  
ATOM   1385  O   HIS A 210      10.112 -25.998 -10.447  1.00102.80           O  
ANISOU 1385  O   HIS A 210    19551  10590   8918  -1092    577   -739       O  
ATOM   1386  CB  HIS A 210       9.743 -24.821 -13.374  1.00104.80           C  
ANISOU 1386  CB  HIS A 210    20013  10929   8877  -1149    489   -771       C  
ATOM   1387  CG  HIS A 210       9.830 -23.610 -14.249  1.00106.59           C  
ANISOU 1387  CG  HIS A 210    20119  11290   9089  -1120    442   -710       C  
ATOM   1388  ND1 HIS A 210       9.696 -22.328 -13.761  1.00109.70           N  
ANISOU 1388  ND1 HIS A 210    20184  11843   9653  -1141    341   -634       N  
ATOM   1389  CD2 HIS A 210      10.039 -23.485 -15.581  1.00104.84           C  
ANISOU 1389  CD2 HIS A 210    20100  11048   8685  -1067    492   -711       C  
ATOM   1390  CE1 HIS A 210       9.819 -21.466 -14.754  1.00104.87           C  
ANISOU 1390  CE1 HIS A 210    19586  11294   8966  -1103    334   -586       C  
ATOM   1391  NE2 HIS A 210      10.027 -22.142 -15.869  1.00100.35           N  
ANISOU 1391  NE2 HIS A 210    19317  10628   8185  -1059    421   -630       N  
ATOM   1392  N   THR A 211      11.216 -27.364 -11.858  1.00 92.83           N  
ANISOU 1392  N   THR A 211    18865   9072   7336   -825    879   -754       N  
ATOM   1393  CA  THR A 211      11.183 -28.477 -10.916  1.00 92.55           C  
ANISOU 1393  CA  THR A 211    18994   8873   7297   -805    948   -784       C  
ATOM   1394  C   THR A 211      12.171 -28.253  -9.779  1.00 94.33           C  
ANISOU 1394  C   THR A 211    18912   9223   7707   -578   1052   -648       C  
ATOM   1395  O   THR A 211      11.874 -28.561  -8.619  1.00102.44           O  
ANISOU 1395  O   THR A 211    19849  10230   8842   -637   1006   -653       O  
ATOM   1396  CB  THR A 211      11.484 -29.790 -11.639  1.00 98.12           C  
ANISOU 1396  CB  THR A 211    20245   9300   7735   -686   1132   -845       C  
ATOM   1397  OG1 THR A 211      10.505 -30.010 -12.663  1.00 93.90           O  
ANISOU 1397  OG1 THR A 211    20007   8662   7010   -953   1009   -983       O  
ATOM   1398  CG2 THR A 211      11.458 -30.958 -10.662  1.00101.71           C  
ANISOU 1398  CG2 THR A 211    20930   9550   8166   -653   1219   -867       C  
ATOM   1399  N   PHE A 212      13.347 -27.705 -10.094  1.00 82.34           N  
ANISOU 1399  N   PHE A 212    17217   7857   6212   -333   1188   -520       N  
ATOM   1400  CA  PHE A 212      14.332 -27.400  -9.062  1.00 83.67           C  
ANISOU 1400  CA  PHE A 212    17047   8208   6535   -147   1268   -378       C  
ATOM   1401  C   PHE A 212      13.803 -26.361  -8.081  1.00 80.80           C  
ANISOU 1401  C   PHE A 212    16295   8005   6401   -361   1064   -371       C  
ATOM   1402  O   PHE A 212      14.022 -26.472  -6.869  1.00 78.14           O  
ANISOU 1402  O   PHE A 212    15778   7727   6183   -322   1058   -323       O  
ATOM   1403  CB  PHE A 212      15.628 -26.920  -9.716  1.00 79.97           C  
ANISOU 1403  CB  PHE A 212    16434   7925   6025     95   1437   -236       C  
ATOM   1404  CG  PHE A 212      16.620 -26.337  -8.751  1.00 80.09           C  
ANISOU 1404  CG  PHE A 212    16022   8213   6194    209   1477    -81       C  
ATOM   1405  CD1 PHE A 212      17.313 -27.149  -7.869  1.00 85.04           C  
ANISOU 1405  CD1 PHE A 212    16624   8873   6816    448   1607      2       C  
ATOM   1406  CD2 PHE A 212      16.865 -24.974  -8.734  1.00 78.00           C  
ANISOU 1406  CD2 PHE A 212    15403   8175   6059     68   1383    -12       C  
ATOM   1407  CE1 PHE A 212      18.229 -26.610  -6.985  1.00 88.05           C  
ANISOU 1407  CE1 PHE A 212    16590   9548   7316    531   1626    149       C  
ATOM   1408  CE2 PHE A 212      17.779 -24.430  -7.853  1.00 81.17           C  
ANISOU 1408  CE2 PHE A 212    15426   8838   6577    117   1406    125       C  
ATOM   1409  CZ  PHE A 212      18.462 -25.249  -6.978  1.00 88.37           C  
ANISOU 1409  CZ  PHE A 212    16274   9822   7482    342   1519    206       C  
ATOM   1410  N   LEU A 213      13.094 -25.348  -8.584  1.00 76.52           N  
ANISOU 1410  N   LEU A 213    15644   7529   5903   -567    900   -415       N  
ATOM   1411  CA  LEU A 213      12.570 -24.299  -7.712  1.00 76.57           C  
ANISOU 1411  CA  LEU A 213    15329   7668   6098   -735    723   -406       C  
ATOM   1412  C   LEU A 213      11.422 -24.812  -6.853  1.00 81.13           C  
ANISOU 1412  C   LEU A 213    15947   8155   6723   -904    592   -504       C  
ATOM   1413  O   LEU A 213      11.373 -24.545  -5.647  1.00 83.48           O  
ANISOU 1413  O   LEU A 213    16026   8527   7167   -932    537   -474       O  
ATOM   1414  CB  LEU A 213      12.132 -23.094  -8.543  1.00 71.53           C  
ANISOU 1414  CB  LEU A 213    14610   7109   5459   -857    607   -413       C  
ATOM   1415  CG  LEU A 213      13.187 -21.998  -8.704  1.00 74.10           C  
ANISOU 1415  CG  LEU A 213    14714   7597   5843   -785    674   -285       C  
ATOM   1416  CD1 LEU A 213      14.401 -22.523  -9.443  1.00 76.15           C  
ANISOU 1416  CD1 LEU A 213    15069   7882   5982   -574    892   -204       C  
ATOM   1417  CD2 LEU A 213      12.601 -20.796  -9.425  1.00 77.62           C  
ANISOU 1417  CD2 LEU A 213    15133   8078   6280   -911    552   -294       C  
ATOM   1418  N   LEU A 214      10.485 -25.549  -7.454  1.00 86.29           N  
ANISOU 1418  N   LEU A 214    16882   8665   7240  -1039    540   -619       N  
ATOM   1419  CA  LEU A 214       9.409 -26.144  -6.667  1.00 89.44           C  
ANISOU 1419  CA  LEU A 214    17326   8997   7659  -1230    432   -703       C  
ATOM   1420  C   LEU A 214       9.954 -27.082  -5.598  1.00 91.50           C  
ANISOU 1420  C   LEU A 214    17653   9158   7954  -1109    557   -669       C  
ATOM   1421  O   LEU A 214       9.331 -27.253  -4.544  1.00 89.01           O  
ANISOU 1421  O   LEU A 214    17245   8849   7727  -1228    478   -691       O  
ATOM   1422  CB  LEU A 214       8.439 -26.892  -7.582  1.00 89.21           C  
ANISOU 1422  CB  LEU A 214    17620   8840   7434  -1430    370   -826       C  
ATOM   1423  CG  LEU A 214       7.300 -26.078  -8.198  1.00 95.16           C  
ANISOU 1423  CG  LEU A 214    18249   9745   8164  -1641    163   -876       C  
ATOM   1424  CD1 LEU A 214       6.645 -26.858  -9.329  1.00 90.76           C  
ANISOU 1424  CD1 LEU A 214    18040   9081   7365  -1818    125   -985       C  
ATOM   1425  CD2 LEU A 214       6.277 -25.697  -7.141  1.00 85.41           C  
ANISOU 1425  CD2 LEU A 214    16742   8651   7058  -1807      3   -885       C  
ATOM   1426  N   LEU A 215      11.117 -27.686  -5.847  1.00 98.99           N  
ANISOU 1426  N   LEU A 215    18759  10031   8823   -848    759   -604       N  
ATOM   1427  CA  LEU A 215      11.713 -28.605  -4.885  1.00 95.50           C  
ANISOU 1427  CA  LEU A 215    18400   9501   8383   -672    895   -551       C  
ATOM   1428  C   LEU A 215      12.491 -27.863  -3.803  1.00 96.90           C  
ANISOU 1428  C   LEU A 215    18172   9903   8744   -543    894   -427       C  
ATOM   1429  O   LEU A 215      12.408 -28.220  -2.623  1.00100.70           O  
ANISOU 1429  O   LEU A 215    18588  10375   9298   -536    884   -408       O  
ATOM   1430  CB  LEU A 215      12.612 -29.604  -5.617  1.00 98.67           C  
ANISOU 1430  CB  LEU A 215    19162   9742   8586   -397   1128   -520       C  
ATOM   1431  CG  LEU A 215      13.315 -30.718  -4.839  1.00102.41           C  
ANISOU 1431  CG  LEU A 215    19822  10094   8997   -130   1314   -451       C  
ATOM   1432  CD1 LEU A 215      13.366 -31.980  -5.678  1.00113.06           C  
ANISOU 1432  CD1 LEU A 215    21747  11130  10080    -15   1486   -512       C  
ATOM   1433  CD2 LEU A 215      14.725 -30.298  -4.457  1.00102.92           C  
ANISOU 1433  CD2 LEU A 215    19565  10411   9130    203   1440   -274       C  
ATOM   1434  N   ILE A 216      13.247 -26.827  -4.179  1.00 82.64           N  
ANISOU 1434  N   ILE A 216    16102   8300   6998   -467    900   -341       N  
ATOM   1435  CA  ILE A 216      14.110 -26.137  -3.222  1.00 78.11           C  
ANISOU 1435  CA  ILE A 216    15164   7954   6562   -376    903   -219       C  
ATOM   1436  C   ILE A 216      13.426 -24.963  -2.536  1.00 79.99           C  
ANISOU 1436  C   ILE A 216    15128   8301   6965   -608    704   -247       C  
ATOM   1437  O   ILE A 216      13.936 -24.473  -1.516  1.00 86.97           O  
ANISOU 1437  O   ILE A 216    15751   9338   7956   -589    678   -172       O  
ATOM   1438  CB  ILE A 216      15.403 -25.646  -3.906  1.00 83.12           C  
ANISOU 1438  CB  ILE A 216    15652   8777   7154   -195   1031    -93       C  
ATOM   1439  CG1 ILE A 216      16.531 -25.497  -2.882  1.00 87.35           C  
ANISOU 1439  CG1 ILE A 216    15880   9552   7757    -42   1093     53       C  
ATOM   1440  CG2 ILE A 216      15.165 -24.331  -4.634  1.00 75.55           C  
ANISOU 1440  CG2 ILE A 216    14554   7909   6243   -379    922   -107       C  
ATOM   1441  CD1 ILE A 216      17.882 -25.213  -3.496  1.00 90.13           C  
ANISOU 1441  CD1 ILE A 216    16067  10141   8038    148   1244    201       C  
ATOM   1442  N   LEU A 217      12.284 -24.498  -3.045  1.00 77.15           N  
ANISOU 1442  N   LEU A 217    14828   7878   6608   -813    565   -347       N  
ATOM   1443  CA  LEU A 217      11.615 -23.337  -2.479  1.00 75.65           C  
ANISOU 1443  CA  LEU A 217    14412   7785   6545   -980    397   -364       C  
ATOM   1444  C   LEU A 217      10.257 -23.637  -1.865  1.00 72.04           C  
ANISOU 1444  C   LEU A 217    13993   7261   6118  -1142    272   -458       C  
ATOM   1445  O   LEU A 217       9.668 -22.738  -1.255  1.00 76.44           O  
ANISOU 1445  O   LEU A 217    14370   7904   6771  -1238    149   -465       O  
ATOM   1446  CB  LEU A 217      11.436 -22.244  -3.546  1.00 79.71           C  
ANISOU 1446  CB  LEU A 217    14900   8350   7035  -1050    336   -366       C  
ATOM   1447  CG  LEU A 217      12.686 -21.515  -4.043  1.00 72.24           C  
ANISOU 1447  CG  LEU A 217    13844   7521   6082   -961    429   -259       C  
ATOM   1448  CD1 LEU A 217      12.286 -20.312  -4.878  1.00 72.33           C  
ANISOU 1448  CD1 LEU A 217    13848   7555   6079  -1062    344   -265       C  
ATOM   1449  CD2 LEU A 217      13.575 -21.097  -2.884  1.00 80.09           C  
ANISOU 1449  CD2 LEU A 217    14589   8661   7182   -935    448   -165       C  
ATOM   1450  N   PHE A 218       9.738 -24.857  -2.003  1.00 88.23           N  
ANISOU 1450  N   PHE A 218    16287   9164   8073  -1181    307   -527       N  
ATOM   1451  CA  PHE A 218       8.393 -25.139  -1.516  1.00 86.10           C  
ANISOU 1451  CA  PHE A 218    16035   8869   7810  -1382    186   -610       C  
ATOM   1452  C   PHE A 218       8.287 -26.525  -0.890  1.00 88.26           C  
ANISOU 1452  C   PHE A 218    16522   8984   8027  -1395    269   -637       C  
ATOM   1453  O   PHE A 218       7.754 -26.668   0.215  1.00 91.31           O  
ANISOU 1453  O   PHE A 218    16815   9392   8485  -1476    220   -643       O  
ATOM   1454  CB  PHE A 218       7.380 -24.991  -2.653  1.00 88.41           C  
ANISOU 1454  CB  PHE A 218    16426   9168   7996  -1548     81   -689       C  
ATOM   1455  CG  PHE A 218       7.111 -23.564  -3.038  1.00 92.88           C  
ANISOU 1455  CG  PHE A 218    16781   9893   8618  -1553    -30   -662       C  
ATOM   1456  CD1 PHE A 218       6.133 -22.830  -2.388  1.00 94.64           C  
ANISOU 1456  CD1 PHE A 218    16798  10246   8915  -1641   -166   -669       C  
ATOM   1457  CD2 PHE A 218       7.839 -22.954  -4.046  1.00 99.08           C  
ANISOU 1457  CD2 PHE A 218    17593  10690   9363  -1451     17   -622       C  
ATOM   1458  CE1 PHE A 218       5.885 -21.515  -2.736  1.00 98.75           C  
ANISOU 1458  CE1 PHE A 218    17178  10881   9460  -1606   -250   -636       C  
ATOM   1459  CE2 PHE A 218       7.597 -21.639  -4.400  1.00 97.53           C  
ANISOU 1459  CE2 PHE A 218    17254  10605   9199  -1452    -73   -591       C  
ATOM   1460  CZ  PHE A 218       6.619 -20.919  -3.744  1.00101.15           C  
ANISOU 1460  CZ  PHE A 218    17543  11168   9723  -1519   -205   -599       C  
ATOM   1461  N   LEU A 219       8.783 -27.552  -1.582  1.00 94.26           N  
ANISOU 1461  N   LEU A 219    17602   9570   8642  -1308    406   -652       N  
ATOM   1462  CA  LEU A 219       8.664 -28.913  -1.066  1.00 90.32           C  
ANISOU 1462  CA  LEU A 219    17395   8869   8054  -1318    501   -679       C  
ATOM   1463  C   LEU A 219       9.588 -29.132   0.126  1.00 93.04           C  
ANISOU 1463  C   LEU A 219    17634   9234   8482  -1090    605   -576       C  
ATOM   1464  O   LEU A 219       9.143 -29.539   1.206  1.00 95.02           O  
ANISOU 1464  O   LEU A 219    17877   9450   8776  -1164    584   -580       O  
ATOM   1465  CB  LEU A 219       8.960 -29.927  -2.172  1.00 93.23           C  
ANISOU 1465  CB  LEU A 219    18201   9012   8211  -1261    635   -724       C  
ATOM   1466  CG  LEU A 219       8.807 -31.390  -1.753  1.00 98.56           C  
ANISOU 1466  CG  LEU A 219    19286   9414   8749  -1283    752   -760       C  
ATOM   1467  CD1 LEU A 219       7.344 -31.806  -1.774  1.00 98.62           C  
ANISOU 1467  CD1 LEU A 219    19435   9352   8684  -1690    617   -880       C  
ATOM   1468  CD2 LEU A 219       9.640 -32.301  -2.642  1.00106.20           C  
ANISOU 1468  CD2 LEU A 219    20687  10152   9511  -1055    956   -755       C  
ATOM   1469  N   ILE A 220      10.886 -28.874  -0.054  1.00 80.30           N  
ANISOU 1469  N   ILE A 220    15927   7706   6878   -813    718   -474       N  
ATOM   1470  CA  ILE A 220      11.831 -29.036   1.053  1.00 79.74           C  
ANISOU 1470  CA  ILE A 220    15711   7719   6867   -586    804   -359       C  
ATOM   1471  C   ILE A 220      11.545 -28.063   2.193  1.00 82.20           C  
ANISOU 1471  C   ILE A 220    15656   8220   7356   -701    656   -337       C  
ATOM   1472  O   ILE A 220      11.509 -28.503   3.353  1.00 82.98           O  
ANISOU 1472  O   ILE A 220    15736   8304   7488   -668    667   -308       O  
ATOM   1473  CB  ILE A 220      13.277 -28.946   0.534  1.00 78.60           C  
ANISOU 1473  CB  ILE A 220    15501   7692   6670   -279    953   -239       C  
ATOM   1474  CG1 ILE A 220      13.626 -30.191  -0.286  1.00 83.27           C  
ANISOU 1474  CG1 ILE A 220    16528   8055   7054    -81   1147   -245       C  
ATOM   1475  CG2 ILE A 220      14.253 -28.777   1.687  1.00 73.37           C  
ANISOU 1475  CG2 ILE A 220    14560   7234   6082    -83    991   -103       C  
ATOM   1476  CD1 ILE A 220      15.031 -30.179  -0.845  1.00 77.85           C  
ANISOU 1476  CD1 ILE A 220    15777   7512   6289    261   1320   -112       C  
ATOM   1477  N   PRO A 221      11.329 -26.763   1.955  1.00 93.76           N  
ANISOU 1477  N   PRO A 221    16860   9845   8919   -826    527   -348       N  
ATOM   1478  CA  PRO A 221      10.927 -25.888   3.070  1.00 86.09           C  
ANISOU 1478  CA  PRO A 221    15618   9005   8086   -937    395   -343       C  
ATOM   1479  C   PRO A 221       9.600 -26.278   3.696  1.00 84.35           C  
ANISOU 1479  C   PRO A 221    15469   8700   7882  -1123    313   -426       C  
ATOM   1480  O   PRO A 221       9.324 -25.868   4.829  1.00 88.40           O  
ANISOU 1480  O   PRO A 221    15809   9295   8485  -1165    245   -412       O  
ATOM   1481  CB  PRO A 221      10.850 -24.499   2.420  1.00 90.41           C  
ANISOU 1481  CB  PRO A 221    15988   9675   8687  -1027    295   -350       C  
ATOM   1482  CG  PRO A 221      11.745 -24.587   1.240  1.00 89.31           C  
ANISOU 1482  CG  PRO A 221    15931   9539   8464   -902    402   -308       C  
ATOM   1483  CD  PRO A 221      11.563 -25.982   0.725  1.00 91.64           C  
ANISOU 1483  CD  PRO A 221    16550   9640   8628   -839    511   -351       C  
ATOM   1484  N   GLY A 222       8.775 -27.058   3.003  1.00 85.22           N  
ANISOU 1484  N   GLY A 222    15827   8661   7890  -1252    318   -509       N  
ATOM   1485  CA  GLY A 222       7.483 -27.450   3.529  1.00 78.56           C  
ANISOU 1485  CA  GLY A 222    15029   7780   7041  -1472    241   -578       C  
ATOM   1486  C   GLY A 222       7.551 -28.586   4.527  1.00 77.29           C  
ANISOU 1486  C   GLY A 222    15036   7483   6846  -1442    335   -557       C  
ATOM   1487  O   GLY A 222       6.888 -28.541   5.567  1.00 82.66           O  
ANISOU 1487  O   GLY A 222    15605   8216   7587  -1547    278   -560       O  
ATOM   1488  N   ILE A 223       8.345 -29.615   4.227  1.00 94.94           N  
ANISOU 1488  N   ILE A 223    17561   9541   8969  -1278    491   -529       N  
ATOM   1489  CA  ILE A 223       8.419 -30.757   5.131  1.00 98.33           C  
ANISOU 1489  CA  ILE A 223    18216   9807   9338  -1223    599   -501       C  
ATOM   1490  C   ILE A 223       9.269 -30.438   6.356  1.00 99.54           C  
ANISOU 1490  C   ILE A 223    18135  10096   9591  -1000    624   -391       C  
ATOM   1491  O   ILE A 223       8.993 -30.942   7.451  1.00101.63           O  
ANISOU 1491  O   ILE A 223    18443  10311   9860  -1019    642   -369       O  
ATOM   1492  CB  ILE A 223       8.940 -32.005   4.395  1.00 98.62           C  
ANISOU 1492  CB  ILE A 223    18708   9576   9186  -1089    775   -504       C  
ATOM   1493  CG1 ILE A 223      10.324 -31.747   3.795  1.00107.71           C  
ANISOU 1493  CG1 ILE A 223    19803  10804  10319   -749    882   -415       C  
ATOM   1494  CG2 ILE A 223       7.951 -32.444   3.324  1.00 95.20           C  
ANISOU 1494  CG2 ILE A 223    18558   8990   8624  -1382    734   -629       C  
ATOM   1495  CD1 ILE A 223      11.028 -33.004   3.323  1.00102.97           C  
ANISOU 1495  CD1 ILE A 223    19649   9954   9520   -501   1097   -382       C  
ATOM   1496  N   VAL A 224      10.301 -29.602   6.209  1.00 88.24           N  
ANISOU 1496  N   VAL A 224    16453   8851   8225   -811    620   -316       N  
ATOM   1497  CA  VAL A 224      11.120 -29.245   7.361  1.00 90.19           C  
ANISOU 1497  CA  VAL A 224    16455   9269   8545   -641    621   -211       C  
ATOM   1498  C   VAL A 224      10.390 -28.291   8.294  1.00 85.98           C  
ANISOU 1498  C   VAL A 224    15656   8872   8142   -827    465   -242       C  
ATOM   1499  O   VAL A 224      10.779 -28.156   9.460  1.00 90.79           O  
ANISOU 1499  O   VAL A 224    16120   9583   8792   -744    452   -178       O  
ATOM   1500  CB  VAL A 224      12.466 -28.639   6.919  1.00 86.72           C  
ANISOU 1500  CB  VAL A 224    15814   9025   8112   -429    662   -112       C  
ATOM   1501  CG1 VAL A 224      13.138 -29.531   5.884  1.00 81.58           C  
ANISOU 1501  CG1 VAL A 224    15430   8251   7315   -215    833    -79       C  
ATOM   1502  CG2 VAL A 224      12.269 -27.232   6.380  1.00 93.15           C  
ANISOU 1502  CG2 VAL A 224    16380   9989   9024   -599    527   -153       C  
ATOM   1503  N   MET A 225       9.338 -27.623   7.819  1.00 88.53           N  
ANISOU 1503  N   MET A 225    15918   9209   8511  -1055    350   -334       N  
ATOM   1504  CA  MET A 225       8.546 -26.759   8.683  1.00 82.68           C  
ANISOU 1504  CA  MET A 225    14962   8585   7867  -1194    223   -361       C  
ATOM   1505  C   MET A 225       7.386 -27.491   9.344  1.00 86.03           C  
ANISOU 1505  C   MET A 225    15498   8924   8267  -1352    218   -407       C  
ATOM   1506  O   MET A 225       6.963 -27.100  10.438  1.00 93.93           O  
ANISOU 1506  O   MET A 225    16352  10011   9326  -1391    164   -397       O  
ATOM   1507  CB  MET A 225       8.011 -25.558   7.900  1.00 74.77           C  
ANISOU 1507  CB  MET A 225    13817   7681   6913  -1309    109   -413       C  
ATOM   1508  CG  MET A 225       9.011 -24.423   7.765  1.00 82.02           C  
ANISOU 1508  CG  MET A 225    14552   8728   7882  -1214     81   -360       C  
ATOM   1509  SD  MET A 225       8.239 -22.844   7.359  1.00 89.19           S  
ANISOU 1509  SD  MET A 225    15316   9729   8844  -1333    -56   -407       S  
ATOM   1510  CE  MET A 225       8.220 -22.911   5.570  1.00 89.27           C  
ANISOU 1510  CE  MET A 225    15451   9683   8783  -1353    -36   -439       C  
ATOM   1511  N   MET A 226       6.857 -28.541   8.711  1.00 88.52           N  
ANISOU 1511  N   MET A 226    16083   9071   8480  -1463    276   -456       N  
ATOM   1512  CA  MET A 226       5.821 -29.334   9.362  1.00 94.66           C  
ANISOU 1512  CA  MET A 226    16985   9770   9212  -1653    285   -488       C  
ATOM   1513  C   MET A 226       6.393 -30.218  10.461  1.00 97.44           C  
ANISOU 1513  C   MET A 226    17484  10009   9531  -1510    399   -417       C  
ATOM   1514  O   MET A 226       5.729 -30.436  11.481  1.00 98.30           O  
ANISOU 1514  O   MET A 226    17566  10132   9651  -1615    389   -411       O  
ATOM   1515  CB  MET A 226       5.070 -30.186   8.341  1.00 89.93           C  
ANISOU 1515  CB  MET A 226    16661   9023   8484  -1874    303   -566       C  
ATOM   1516  CG  MET A 226       4.188 -29.378   7.405  1.00 96.34           C  
ANISOU 1516  CG  MET A 226    17307   9992   9307  -2058    168   -632       C  
ATOM   1517  SD  MET A 226       3.173 -30.413   6.334  1.00124.95           S  
ANISOU 1517  SD  MET A 226    21237  13490  12750  -2395    159   -727       S  
ATOM   1518  CE  MET A 226       2.001 -31.063   7.523  1.00103.04           C  
ANISOU 1518  CE  MET A 226    18454  10749   9946  -2669    151   -727       C  
ATOM   1519  N   VAL A 227       7.612 -30.733  10.280  1.00 87.22           N  
ANISOU 1519  N   VAL A 227    16338   8619   8181  -1252    515   -351       N  
ATOM   1520  CA  VAL A 227       8.239 -31.497  11.354  1.00 87.12           C  
ANISOU 1520  CA  VAL A 227    16443   8534   8125  -1057    622   -262       C  
ATOM   1521  C   VAL A 227       8.739 -30.567  12.449  1.00 89.23           C  
ANISOU 1521  C   VAL A 227    16365   9036   8503   -939    544   -194       C  
ATOM   1522  O   VAL A 227       8.843 -30.968  13.613  1.00 93.85           O  
ANISOU 1522  O   VAL A 227    16971   9615   9071   -862    579   -135       O  
ATOM   1523  CB  VAL A 227       9.372 -32.386  10.806  1.00 82.88           C  
ANISOU 1523  CB  VAL A 227    16179   7848   7463   -770    785   -194       C  
ATOM   1524  CG1 VAL A 227       8.841 -33.313   9.728  1.00 86.78           C  
ANISOU 1524  CG1 VAL A 227    17083   8072   7819   -910    865   -276       C  
ATOM   1525  CG2 VAL A 227      10.512 -31.535  10.269  1.00 92.08           C  
ANISOU 1525  CG2 VAL A 227    17085   9221   8680   -555    767   -135       C  
ATOM   1526  N   ALA A 228       9.052 -29.317  12.107  1.00 78.84           N  
ANISOU 1526  N   ALA A 228    14757   7917   7282   -936    439   -202       N  
ATOM   1527  CA  ALA A 228       9.459 -28.352  13.122  1.00 72.45           C  
ANISOU 1527  CA  ALA A 228    13659   7315   6555   -882    352   -155       C  
ATOM   1528  C   ALA A 228       8.253 -27.851  13.908  1.00 74.63           C  
ANISOU 1528  C   ALA A 228    13836   7631   6890  -1079    259   -215       C  
ATOM   1529  O   ALA A 228       8.209 -27.961  15.137  1.00 82.29           O  
ANISOU 1529  O   ALA A 228    14768   8637   7860  -1045    259   -177       O  
ATOM   1530  CB  ALA A 228      10.207 -27.185  12.473  1.00 69.99           C  
ANISOU 1530  CB  ALA A 228    13123   7172   6298   -846    281   -144       C  
ATOM   1531  N   TYR A 229       7.256 -27.306  13.207  1.00 88.74           N  
ANISOU 1531  N   TYR A 229    15575   9430   8711  -1264    186   -299       N  
ATOM   1532  CA  TYR A 229       6.058 -26.814  13.876  1.00 89.89           C  
ANISOU 1532  CA  TYR A 229    15607   9654   8895  -1417    113   -341       C  
ATOM   1533  C   TYR A 229       5.209 -27.944  14.442  1.00 91.78           C  
ANISOU 1533  C   TYR A 229    16008   9791   9072  -1540    180   -345       C  
ATOM   1534  O   TYR A 229       4.418 -27.706  15.362  1.00 98.19           O  
ANISOU 1534  O   TYR A 229    16719  10688   9902  -1617    152   -347       O  
ATOM   1535  CB  TYR A 229       5.231 -25.963  12.911  1.00 85.48           C  
ANISOU 1535  CB  TYR A 229    14943   9173   8363  -1543     24   -407       C  
ATOM   1536  CG  TYR A 229       5.783 -24.570  12.721  1.00 85.49           C  
ANISOU 1536  CG  TYR A 229    14775   9284   8425  -1457    -54   -402       C  
ATOM   1537  CD1 TYR A 229       5.782 -23.653  13.764  1.00 85.53           C  
ANISOU 1537  CD1 TYR A 229    14646   9383   8467  -1414   -107   -388       C  
ATOM   1538  CD2 TYR A 229       6.323 -24.176  11.504  1.00 87.00           C  
ANISOU 1538  CD2 TYR A 229    14976   9465   8616  -1430    -66   -411       C  
ATOM   1539  CE1 TYR A 229       6.292 -22.379  13.597  1.00 85.73           C  
ANISOU 1539  CE1 TYR A 229    14580   9473   8522  -1371   -173   -388       C  
ATOM   1540  CE2 TYR A 229       6.836 -22.905  11.327  1.00 86.75           C  
ANISOU 1540  CE2 TYR A 229    14825   9514   8623  -1384   -128   -402       C  
ATOM   1541  CZ  TYR A 229       6.819 -22.012  12.377  1.00 87.24           C  
ANISOU 1541  CZ  TYR A 229    14783   9651   8715  -1366   -182   -392       C  
ATOM   1542  OH  TYR A 229       7.329 -20.747  12.205  1.00 89.88           O  
ANISOU 1542  OH  TYR A 229    15057  10030   9063  -1355   -239   -387       O  
ATOM   1543  N   GLY A 230       5.351 -29.162  13.918  1.00 72.56           N  
ANISOU 1543  N   GLY A 230    13849   7170   6550  -1563    280   -345       N  
ATOM   1544  CA  GLY A 230       4.649 -30.290  14.505  1.00 74.91           C  
ANISOU 1544  CA  GLY A 230    14358   7337   6766  -1703    358   -341       C  
ATOM   1545  C   GLY A 230       5.262 -30.728  15.821  1.00 79.92           C  
ANISOU 1545  C   GLY A 230    15048   7934   7385  -1529    431   -256       C  
ATOM   1546  O   GLY A 230       4.547 -30.988  16.793  1.00 78.40           O  
ANISOU 1546  O   GLY A 230    14857   7755   7177  -1635    446   -243       O  
ATOM   1547  N   LEU A 231       6.594 -30.815  15.872  1.00 84.53           N  
ANISOU 1547  N   LEU A 231    15661   8499   7957  -1254    478   -186       N  
ATOM   1548  CA  LEU A 231       7.266 -31.155  17.121  1.00 83.90           C  
ANISOU 1548  CA  LEU A 231    15599   8433   7847  -1056    531    -90       C  
ATOM   1549  C   LEU A 231       7.110 -30.052  18.159  1.00 82.30           C  
ANISOU 1549  C   LEU A 231    15094   8447   7728  -1067    418    -86       C  
ATOM   1550  O   LEU A 231       7.066 -30.337  19.361  1.00 87.97           O  
ANISOU 1550  O   LEU A 231    15833   9176   8414  -1017    445    -34       O  
ATOM   1551  CB  LEU A 231       8.747 -31.438  16.863  1.00 83.35           C  
ANISOU 1551  CB  LEU A 231    15576   8367   7727   -743    598      0       C  
ATOM   1552  CG  LEU A 231       9.071 -32.761  16.163  1.00 85.23           C  
ANISOU 1552  CG  LEU A 231    16205   8347   7830   -630    760     27       C  
ATOM   1553  CD1 LEU A 231      10.573 -32.923  15.979  1.00 80.96           C  
ANISOU 1553  CD1 LEU A 231    15645   7886   7232   -261    832    141       C  
ATOM   1554  CD2 LEU A 231       8.493 -33.936  16.934  1.00 92.66           C  
ANISOU 1554  CD2 LEU A 231    17477   9065   8665   -686    870     50       C  
ATOM   1555  N   ILE A 232       7.024 -28.795  17.720  1.00 82.56           N  
ANISOU 1555  N   ILE A 232    14883   8636   7851  -1124    301   -138       N  
ATOM   1556  CA  ILE A 232       6.793 -27.695  18.652  1.00 75.01           C  
ANISOU 1556  CA  ILE A 232    13703   7847   6950  -1142    203   -147       C  
ATOM   1557  C   ILE A 232       5.406 -27.809  19.269  1.00 77.87           C  
ANISOU 1557  C   ILE A 232    14071   8209   7308  -1311    209   -183       C  
ATOM   1558  O   ILE A 232       5.237 -27.671  20.486  1.00 88.60           O  
ANISOU 1558  O   ILE A 232    15385   9627   8652  -1280    207   -154       O  
ATOM   1559  CB  ILE A 232       6.987 -26.343  17.943  1.00 74.50           C  
ANISOU 1559  CB  ILE A 232    13449   7902   6957  -1165     95   -194       C  
ATOM   1560  CG1 ILE A 232       8.476 -26.049  17.754  1.00 74.91           C  
ANISOU 1560  CG1 ILE A 232    13428   8031   7003  -1010     80   -134       C  
ATOM   1561  CG2 ILE A 232       6.316 -25.223  18.723  1.00 77.48           C  
ANISOU 1561  CG2 ILE A 232    13679   8393   7367  -1225     10   -231       C  
ATOM   1562  CD1 ILE A 232       8.754 -24.946  16.762  1.00 77.59           C  
ANISOU 1562  CD1 ILE A 232    13648   8440   7392  -1058      4   -173       C  
ATOM   1563  N   SER A 233       4.392 -28.074  18.440  1.00 82.82           N  
ANISOU 1563  N   SER A 233    14742   8794   7931  -1498    217   -240       N  
ATOM   1564  CA  SER A 233       3.034 -28.226  18.949  1.00 88.83           C  
ANISOU 1564  CA  SER A 233    15468   9613   8672  -1681    227   -259       C  
ATOM   1565  C   SER A 233       2.896 -29.427  19.877  1.00 91.67           C  
ANISOU 1565  C   SER A 233    16027   9853   8952  -1718    338   -204       C  
ATOM   1566  O   SER A 233       1.992 -29.446  20.719  1.00 89.39           O  
ANISOU 1566  O   SER A 233    15676   9646   8642  -1822    357   -192       O  
ATOM   1567  CB  SER A 233       2.049 -28.342  17.785  1.00 87.67           C  
ANISOU 1567  CB  SER A 233    15312   9489   8511  -1898    202   -319       C  
ATOM   1568  OG  SER A 233       1.957 -27.116  17.079  1.00 88.56           O  
ANISOU 1568  OG  SER A 233    15227   9737   8685  -1855    100   -359       O  
ATOM   1569  N   LEU A 234       3.767 -30.429  19.740  1.00 82.47           N  
ANISOU 1569  N   LEU A 234    15113   8496   7727  -1616    426   -162       N  
ATOM   1570  CA  LEU A 234       3.743 -31.553  20.671  1.00 80.45           C  
ANISOU 1570  CA  LEU A 234    15093   8097   7377  -1609    543    -96       C  
ATOM   1571  C   LEU A 234       4.222 -31.131  22.054  1.00 80.77           C  
ANISOU 1571  C   LEU A 234    15017   8247   7426  -1422    527    -31       C  
ATOM   1572  O   LEU A 234       3.621 -31.507  23.067  1.00 87.14           O  
ANISOU 1572  O   LEU A 234    15876   9051   8184  -1491    580      3       O  
ATOM   1573  CB  LEU A 234       4.599 -32.700  20.134  1.00 79.70           C  
ANISOU 1573  CB  LEU A 234    15336   7757   7191  -1488    656    -57       C  
ATOM   1574  CG  LEU A 234       3.994 -33.557  19.020  1.00 77.61           C  
ANISOU 1574  CG  LEU A 234    15342   7297   6850  -1721    716   -116       C  
ATOM   1575  CD1 LEU A 234       4.894 -34.744  18.724  1.00 76.66           C  
ANISOU 1575  CD1 LEU A 234    15629   6894   6603  -1538    860    -63       C  
ATOM   1576  CD2 LEU A 234       2.594 -34.020  19.388  1.00 74.41           C  
ANISOU 1576  CD2 LEU A 234    14997   6883   6392  -2071    740   -142       C  
ATOM   1577  N   GLU A 235       5.303 -30.349  22.117  1.00 92.60           N  
ANISOU 1577  N   GLU A 235    16360   9854   8969  -1208    452    -10       N  
ATOM   1578  CA  GLU A 235       5.801 -29.874  23.404  1.00 92.40           C  
ANISOU 1578  CA  GLU A 235    16222   9955   8931  -1058    413     44       C  
ATOM   1579  C   GLU A 235       4.817 -28.914  24.059  1.00 95.31           C  
ANISOU 1579  C   GLU A 235    16407  10468   9340  -1179    347     -7       C  
ATOM   1580  O   GLU A 235       4.571 -28.999  25.268  1.00102.63           O  
ANISOU 1580  O   GLU A 235    17347  11432  10217  -1152    373     31       O  
ATOM   1581  CB  GLU A 235       7.162 -29.202  23.225  1.00 96.34           C  
ANISOU 1581  CB  GLU A 235    16579  10574   9450   -864    333     74       C  
ATOM   1582  CG  GLU A 235       7.785 -28.713  24.523  1.00108.57           C  
ANISOU 1582  CG  GLU A 235    18017  12276  10958   -737    273    130       C  
ATOM   1583  CD  GLU A 235       9.007 -29.514  24.924  1.00115.27           C  
ANISOU 1583  CD  GLU A 235    18948  13139  11710   -492    323    252       C  
ATOM   1584  OE1 GLU A 235       9.469 -30.343  24.111  1.00119.52           O  
ANISOU 1584  OE1 GLU A 235    19628  13566  12219   -388    411    293       O  
ATOM   1585  OE2 GLU A 235       9.509 -29.313  26.051  1.00109.51           O  
ANISOU 1585  OE2 GLU A 235    18148  12543  10916   -387    277    313       O  
ATOM   1586  N   LEU A 236       4.246 -27.992  23.281  1.00 85.93           N  
ANISOU 1586  N   LEU A 236    15061   9363   8226  -1284    272    -85       N  
ATOM   1587  CA  LEU A 236       3.292 -27.039  23.833  1.00 91.71           C  
ANISOU 1587  CA  LEU A 236    15634  10237   8975  -1345    226   -124       C  
ATOM   1588  C   LEU A 236       2.004 -27.708  24.297  1.00 93.45           C  
ANISOU 1588  C   LEU A 236    15889  10469   9150  -1502    314   -110       C  
ATOM   1589  O   LEU A 236       1.315 -27.160  25.164  1.00 92.90           O  
ANISOU 1589  O   LEU A 236    15717  10524   9058  -1496    316   -107       O  
ATOM   1590  CB  LEU A 236       2.980 -25.948  22.805  1.00 87.91           C  
ANISOU 1590  CB  LEU A 236    15004   9837   8562  -1384    139   -195       C  
ATOM   1591  CG  LEU A 236       3.901 -24.723  22.793  1.00 89.04           C  
ANISOU 1591  CG  LEU A 236    15064  10034   8734  -1264     39   -216       C  
ATOM   1592  CD1 LEU A 236       5.313 -25.079  22.367  1.00 80.25           C  
ANISOU 1592  CD1 LEU A 236    14000   8865   7626  -1180     26   -180       C  
ATOM   1593  CD2 LEU A 236       3.338 -23.648  21.883  1.00 93.87           C  
ANISOU 1593  CD2 LEU A 236    15572  10706   9389  -1302    -24   -279       C  
ATOM   1594  N   TYR A 237       1.666 -28.876  23.748  1.00 85.88           N  
ANISOU 1594  N   TYR A 237    15088   9385   8156  -1654    393    -98       N  
ATOM   1595  CA  TYR A 237       0.504 -29.612  24.227  1.00 86.54           C  
ANISOU 1595  CA  TYR A 237    15221   9485   8174  -1857    482    -73       C  
ATOM   1596  C   TYR A 237       0.781 -30.354  25.527  1.00 96.58           C  
ANISOU 1596  C   TYR A 237    16661  10668   9366  -1785    577      6       C  
ATOM   1597  O   TYR A 237      -0.166 -30.685  26.249  1.00100.31           O  
ANISOU 1597  O   TYR A 237    17129  11203   9782  -1924    649     38       O  
ATOM   1598  CB  TYR A 237       0.021 -30.600  23.163  1.00 85.32           C  
ANISOU 1598  CB  TYR A 237    15222   9214   7983  -2102    528    -95       C  
ATOM   1599  CG  TYR A 237      -1.331 -31.202  23.473  1.00 84.08           C  
ANISOU 1599  CG  TYR A 237    15059   9138   7750  -2396    598    -75       C  
ATOM   1600  CD1 TYR A 237      -2.501 -30.506  23.200  1.00 77.79           C  
ANISOU 1600  CD1 TYR A 237    13973   8615   6968  -2539    544    -99       C  
ATOM   1601  CD2 TYR A 237      -1.436 -32.463  24.046  1.00 81.59           C  
ANISOU 1601  CD2 TYR A 237    15027   8643   7331  -2529    725    -20       C  
ATOM   1602  CE1 TYR A 237      -3.738 -31.050  23.484  1.00 82.18           C  
ANISOU 1602  CE1 TYR A 237    14474   9310   7441  -2827    608    -64       C  
ATOM   1603  CE2 TYR A 237      -2.669 -33.015  24.335  1.00 86.11           C  
ANISOU 1603  CE2 TYR A 237    15588   9307   7821  -2846    793      5       C  
ATOM   1604  CZ  TYR A 237      -3.816 -32.305  24.052  1.00 89.30           C  
ANISOU 1604  CZ  TYR A 237    15655  10031   8245  -3005    730    -15       C  
ATOM   1605  OH  TYR A 237      -5.046 -32.850  24.339  1.00 96.83           O  
ANISOU 1605  OH  TYR A 237    16549  11138   9103  -3339    796     26       O  
ATOM   1606  N   GLN A 238       2.052 -30.617  25.844  1.00110.21           N  
ANISOU 1606  N   GLN A 238    18522  12278  11075  -1566    580     49       N  
ATOM   1607  CA  GLN A 238       2.388 -31.238  27.119  1.00111.74           C  
ANISOU 1607  CA  GLN A 238    18868  12410  11179  -1454    659    135       C  
ATOM   1608  C   GLN A 238       1.988 -30.368  28.303  1.00110.73           C  
ANISOU 1608  C   GLN A 238    18564  12466  11043  -1400    623    140       C  
ATOM   1609  O   GLN A 238       1.879 -30.875  29.424  1.00112.17           O  
ANISOU 1609  O   GLN A 238    18858  12625  11138  -1366    700    208       O  
ATOM   1610  CB  GLN A 238       3.885 -31.546  27.179  1.00110.79           C  
ANISOU 1610  CB  GLN A 238    18865  12203  11028  -1187    650    193       C  
ATOM   1611  CG  GLN A 238       4.345 -32.587  26.173  1.00109.09           C  
ANISOU 1611  CG  GLN A 238    18900  11771  10778  -1176    729    210       C  
ATOM   1612  CD  GLN A 238       3.580 -33.890  26.294  1.00118.01           C  
ANISOU 1612  CD  GLN A 238    20350  12685  11805  -1360    879    242       C  
ATOM   1613  OE1 GLN A 238       2.700 -34.184  25.485  1.00123.28           O  
ANISOU 1613  OE1 GLN A 238    21075  13288  12478  -1634    903    181       O  
ATOM   1614  NE2 GLN A 238       3.914 -34.681  27.308  1.00120.56           N  
ANISOU 1614  NE2 GLN A 238    20894  12899  12015  -1227    979    341       N  
ATOM   1615  N   GLY A 239       1.769 -29.075  28.079  1.00 94.83           N  
ANISOU 1615  N   GLY A 239    16313  10618   9100  -1379    518     72       N  
ATOM   1616  CA  GLY A 239       1.293 -28.197  29.123  1.00102.46           C  
ANISOU 1616  CA  GLY A 239    17154  11739  10037  -1320    499     67       C  
ATOM   1617  C   GLY A 239       2.362 -27.865  30.151  1.00106.72           C  
ANISOU 1617  C   GLY A 239    17740  12288  10520  -1118    447     99       C  
ATOM   1618  O   GLY A 239       3.544 -28.181  30.010  1.00102.28           O  
ANISOU 1618  O   GLY A 239    17250  11661   9950  -1005    409    132       O  
ATOM   1619  N   ILE A 240       1.908 -27.202  31.208  1.00120.36           N  
ANISOU 1619  N   ILE A 240    19418  14125  12190  -1069    448     95       N  
ATOM   1620  CA  ILE A 240       2.779 -26.825  32.313  1.00118.86           C  
ANISOU 1620  CA  ILE A 240    19277  13969  11914   -912    390    119       C  
ATOM   1621  C   ILE A 240       3.002 -28.035  33.208  1.00114.88           C  
ANISOU 1621  C   ILE A 240    18945  13392  11312   -864    486    222       C  
ATOM   1622  O   ILE A 240       2.090 -28.840  33.433  1.00111.29           O  
ANISOU 1622  O   ILE A 240    18568  12890  10828   -971    617    263       O  
ATOM   1623  CB  ILE A 240       2.173 -25.647  33.098  1.00115.28           C  
ANISOU 1623  CB  ILE A 240    18761  13633  11407   -870    366     68       C  
ATOM   1624  CG1 ILE A 240       1.820 -24.499  32.150  1.00117.03           C  
ANISOU 1624  CG1 ILE A 240    18858  13900  11709   -897    298    -22       C  
ATOM   1625  CG2 ILE A 240       3.133 -25.165  34.174  1.00118.09           C  
ANISOU 1625  CG2 ILE A 240    19189  14025  11655   -746    281     76       C  
ATOM   1626  CD1 ILE A 240       0.338 -24.352  31.893  1.00119.52           C  
ANISOU 1626  CD1 ILE A 240    19067  14304  12040   -959    389    -32       C  
ATOM   1627  N   ASN A 241       4.221 -28.172  33.712  1.00116.28           N  
ANISOU 1627  N   ASN A 241    19182  13575  11423   -711    423    273       N  
ATOM   1628  CA  ASN A 241       4.602 -29.255  34.605  1.00116.83           C  
ANISOU 1628  CA  ASN A 241    19431  13585  11375   -605    504    386       C  
ATOM   1629  C   ASN A 241       5.029 -28.678  35.952  1.00113.33           C  
ANISOU 1629  C   ASN A 241    18983  13271  10806   -484    433    406       C  
ATOM   1630  O   ASN A 241       5.031 -27.462  36.162  1.00114.20           O  
ANISOU 1630  O   ASN A 241    18983  13492  10916   -501    327    325       O  
ATOM   1631  CB  ASN A 241       5.716 -30.102  33.984  1.00114.18           C  
ANISOU 1631  CB  ASN A 241    19181  13168  11036   -482    504    458       C  
ATOM   1632  CG  ASN A 241       6.974 -29.303  33.724  1.00123.80           C  
ANISOU 1632  CG  ASN A 241    20237  14537  12265   -368    343    445       C  
ATOM   1633  OD1 ASN A 241       7.826 -29.167  34.600  1.00119.27           O  
ANISOU 1633  OD1 ASN A 241    19644  14094  11580   -228    269    506       O  
ATOM   1634  ND2 ASN A 241       7.096 -28.765  32.515  1.00124.18           N  
ANISOU 1634  ND2 ASN A 241    20161  14588  12433   -447    283    371       N  
ATOM   1635  N   ILE A 242       5.398 -29.572  36.871  1.00114.68           N  
ANISOU 1635  N   ILE A 242    19312  13413  10849   -361    496    518       N  
ATOM   1636  CA  ILE A 242       5.775 -29.135  38.211  1.00116.03           C  
ANISOU 1636  CA  ILE A 242    19501  13712  10872   -252    431    546       C  
ATOM   1637  C   ILE A 242       7.124 -28.429  38.202  1.00119.65           C  
ANISOU 1637  C   ILE A 242    19834  14334  11292   -158    241    538       C  
ATOM   1638  O   ILE A 242       7.335 -27.471  38.957  1.00125.81           O  
ANISOU 1638  O   ILE A 242    20571  15246  11985   -166    128    489       O  
ATOM   1639  CB  ILE A 242       5.766 -30.329  39.184  1.00110.67           C  
ANISOU 1639  CB  ILE A 242    19038  12960  10050   -138    556    680       C  
ATOM   1640  CG1 ILE A 242       6.125 -29.864  40.595  1.00112.10           C  
ANISOU 1640  CG1 ILE A 242    19243  13288  10061    -27    483    708       C  
ATOM   1641  CG2 ILE A 242       6.706 -31.432  38.708  1.00111.42           C  
ANISOU 1641  CG2 ILE A 242    19244  12969  10122     17    590    792       C  
ATOM   1642  CD1 ILE A 242       5.878 -30.898  41.646  1.00125.83           C  
ANISOU 1642  CD1 ILE A 242    21204  14955  11650     70    621    833       C  
ATOM   1643  N   PHE A 243       8.055 -28.872  37.353  1.00108.45           N  
ANISOU 1643  N   PHE A 243    18363  12924   9920    -80    207    589       N  
ATOM   1644  CA  PHE A 243       9.372 -28.247  37.323  1.00107.92           C  
ANISOU 1644  CA  PHE A 243    18135  13069   9802    -12     30    603       C  
ATOM   1645  C   PHE A 243       9.295 -26.829  36.775  1.00105.93           C  
ANISOU 1645  C   PHE A 243    17733  12879   9636   -194    -98    461       C  
ATOM   1646  O   PHE A 243      10.050 -25.952  37.212  1.00103.74           O  
ANISOU 1646  O   PHE A 243    17367  12781   9270   -230   -257    437       O  
ATOM   1647  CB  PHE A 243      10.338 -29.091  36.494  1.00105.95           C  
ANISOU 1647  CB  PHE A 243    17852  12833   9571    144     52    706       C  
ATOM   1648  CG  PHE A 243      10.907 -30.263  37.240  1.00112.33           C  
ANISOU 1648  CG  PHE A 243    18799  13659  10221    399    126    874       C  
ATOM   1649  CD1 PHE A 243      10.140 -31.398  37.454  1.00109.23           C  
ANISOU 1649  CD1 PHE A 243    18674  13024   9806    449    318    931       C  
ATOM   1650  CD2 PHE A 243      12.196 -30.228  37.741  1.00120.42           C  
ANISOU 1650  CD2 PHE A 243    19695  14958  11101    582      5    984       C  
ATOM   1651  CE1 PHE A 243      10.655 -32.480  38.142  1.00114.08           C  
ANISOU 1651  CE1 PHE A 243    19467  13622  10256    706    400   1094       C  
ATOM   1652  CE2 PHE A 243      12.714 -31.306  38.433  1.00125.52           C  
ANISOU 1652  CE2 PHE A 243    20475  15634  11581    864     78   1155       C  
ATOM   1653  CZ  PHE A 243      11.944 -32.432  38.633  1.00120.81           C  
ANISOU 1653  CZ  PHE A 243    20188  14750  10964    940    282   1209       C  
ATOM   1654  N   GLU A 244       8.389 -26.585  35.825  1.00138.83           N  
ANISOU 1654  N   GLU A 244    21890  16903  13957   -320    -32    370       N  
ATOM   1655  CA  GLU A 244       8.163 -25.226  35.348  1.00139.71           C  
ANISOU 1655  CA  GLU A 244    21911  17039  14133   -467   -129    241       C  
ATOM   1656  C   GLU A 244       7.417 -24.392  36.381  1.00136.49           C  
ANISOU 1656  C   GLU A 244    21589  16637  13633   -509   -136    170       C  
ATOM   1657  O   GLU A 244       7.666 -23.187  36.500  1.00135.89           O  
ANISOU 1657  O   GLU A 244    21506  16614  13511   -587   -253     85       O  
ATOM   1658  CB  GLU A 244       7.392 -25.257  34.028  1.00141.81           C  
ANISOU 1658  CB  GLU A 244    22138  17173  14569   -556    -54    181       C  
ATOM   1659  CG  GLU A 244       7.187 -23.895  33.385  1.00145.87           C  
ANISOU 1659  CG  GLU A 244    22580  17696  15147   -673   -141     63       C  
ATOM   1660  CD  GLU A 244       6.424 -23.979  32.077  1.00153.44           C  
ANISOU 1660  CD  GLU A 244    23490  18553  16256   -744    -74     18       C  
ATOM   1661  OE1 GLU A 244       6.197 -25.108  31.592  1.00151.48           O  
ANISOU 1661  OE1 GLU A 244    23268  18228  16061   -731     25     72       O  
ATOM   1662  OE2 GLU A 244       6.046 -22.917  31.535  1.00153.63           O  
ANISOU 1662  OE2 GLU A 244    23478  18567  16326   -812   -119    -70       O  
ATOM   1663  N   MET A 245       6.508 -25.014  37.136  1.00 97.13           N  
ANISOU 1663  N   MET A 245    16713  11590   8602   -461     -2    207       N  
ATOM   1664  CA  MET A 245       5.770 -24.289  38.165  1.00 96.59           C  
ANISOU 1664  CA  MET A 245    16737  11538   8426   -462     18    153       C  
ATOM   1665  C   MET A 245       6.695 -23.838  39.289  1.00 95.41           C  
ANISOU 1665  C   MET A 245    16654  11508   8090   -421   -114    162       C  
ATOM   1666  O   MET A 245       6.656 -22.677  39.712  1.00 95.76           O  
ANISOU 1666  O   MET A 245    16764  11574   8045   -474   -194     68       O  
ATOM   1667  CB  MET A 245       4.643 -25.163  38.715  1.00 94.79           C  
ANISOU 1667  CB  MET A 245    16589  11249   8179   -430    203    212       C  
ATOM   1668  CG  MET A 245       4.067 -24.669  40.032  1.00 99.50           C  
ANISOU 1668  CG  MET A 245    17299  11890   8618   -377    243    196       C  
ATOM   1669  SD  MET A 245       2.749 -25.721  40.669  1.00 91.18           S  
ANISOU 1669  SD  MET A 245    16313  10801   7532   -368    475    285       S  
ATOM   1670  CE  MET A 245       3.675 -27.197  41.076  1.00 96.66           C  
ANISOU 1670  CE  MET A 245    17118  11446   8161   -294    495    429       C  
ATOM   1671  N   LEU A 246       7.536 -24.748  39.788  1.00 85.37           N  
ANISOU 1671  N   LEU A 246    15385  10315   6735   -323   -136    279       N  
ATOM   1672  CA  LEU A 246       8.468 -24.390  40.851  1.00 86.53           C  
ANISOU 1672  CA  LEU A 246    15566  10627   6684   -292   -280    303       C  
ATOM   1673  C   LEU A 246       9.523 -23.404  40.368  1.00 91.20           C  
ANISOU 1673  C   LEU A 246    16039  11351   7260   -418   -479    244       C  
ATOM   1674  O   LEU A 246      10.005 -22.580  41.155  1.00 91.86           O  
ANISOU 1674  O   LEU A 246    16180  11548   7175   -497   -618    197       O  
ATOM   1675  CB  LEU A 246       9.132 -25.647  41.412  1.00 85.82           C  
ANISOU 1675  CB  LEU A 246    15490  10618   6498   -120   -252    465       C  
ATOM   1676  CG  LEU A 246       8.327 -26.409  42.465  1.00 91.69           C  
ANISOU 1676  CG  LEU A 246    16415  11278   7144    -17    -98    532       C  
ATOM   1677  CD1 LEU A 246       8.931 -27.782  42.717  1.00 89.79           C  
ANISOU 1677  CD1 LEU A 246    16223  11057   6835    175    -37    704       C  
ATOM   1678  CD2 LEU A 246       8.246 -25.608  43.756  1.00 86.33           C  
ANISOU 1678  CD2 LEU A 246    15846  10688   6267    -34   -173    481       C  
ATOM   1679  N   ARG A 247       9.895 -23.470  39.088  1.00107.79           N  
ANISOU 1679  N   ARG A 247    17991  13443   9520   -460   -495    244       N  
ATOM   1680  CA  ARG A 247      10.842 -22.503  38.543  1.00105.55           C  
ANISOU 1680  CA  ARG A 247    17591  13287   9228   -614   -668    191       C  
ATOM   1681  C   ARG A 247      10.213 -21.121  38.420  1.00100.21           C  
ANISOU 1681  C   ARG A 247    17036  12486   8553   -780   -702     32       C  
ATOM   1682  O   ARG A 247      10.924 -20.110  38.445  1.00 97.89           O  
ANISOU 1682  O   ARG A 247    16749  12279   8167   -951   -857    -30       O  
ATOM   1683  CB  ARG A 247      11.358 -22.988  37.188  1.00104.88           C  
ANISOU 1683  CB  ARG A 247    17327  13219   9303   -592   -650    243       C  
ATOM   1684  CG  ARG A 247      12.545 -22.212  36.644  1.00108.43           C  
ANISOU 1684  CG  ARG A 247    17610  13862   9725   -740   -822    234       C  
ATOM   1685  CD  ARG A 247      13.022 -22.805  35.326  1.00116.82           C  
ANISOU 1685  CD  ARG A 247    18504  14947  10936   -675   -774    300       C  
ATOM   1686  NE  ARG A 247      13.478 -24.183  35.483  1.00116.62           N  
ANISOU 1686  NE  ARG A 247    18428  15003  10881   -427   -695    458       N  
ATOM   1687  CZ  ARG A 247      12.865 -25.239  34.966  1.00114.65           C  
ANISOU 1687  CZ  ARG A 247    18266  14557  10740   -277   -521    499       C  
ATOM   1688  NH1 ARG A 247      11.761 -25.116  34.248  1.00114.05           N  
ANISOU 1688  NH1 ARG A 247    18282  14236  10816   -365   -421    398       N  
ATOM   1689  NH2 ARG A 247      13.373 -26.451  35.176  1.00103.42           N  
ANISOU 1689  NH2 ARG A 247    16854  13190   9251    -36   -445    649       N  
ATOM   1690  N   ILE A 248       8.887 -21.058  38.289  1.00 84.92           N  
ANISOU 1690  N   ILE A 248    15206  10357   6701   -733   -552    -27       N  
ATOM   1691  CA  ILE A 248       8.189 -19.778  38.303  1.00 81.07           C  
ANISOU 1691  CA  ILE A 248    14874   9749   6181   -814   -554   -161       C  
ATOM   1692  C   ILE A 248       8.046 -19.260  39.729  1.00 88.97           C  
ANISOU 1692  C   ILE A 248    16086  10761   6956   -802   -582   -201       C  
ATOM   1693  O   ILE A 248       8.260 -18.073  39.996  1.00 90.15           O  
ANISOU 1693  O   ILE A 248    16403  10875   6976   -921   -679   -302       O  
ATOM   1694  CB  ILE A 248       6.820 -19.918  37.612  1.00 82.65           C  
ANISOU 1694  CB  ILE A 248    15068   9801   6536   -738   -382   -188       C  
ATOM   1695  CG1 ILE A 248       6.993 -20.079  36.101  1.00 85.17           C  
ANISOU 1695  CG1 ILE A 248    15224  10090   7048   -793   -386   -185       C  
ATOM   1696  CG2 ILE A 248       5.929 -18.726  37.929  1.00 78.45           C  
ANISOU 1696  CG2 ILE A 248    14725   9163   5920   -723   -341   -296       C  
ATOM   1697  CD1 ILE A 248       5.727 -20.503  35.390  1.00 81.21           C  
ANISOU 1697  CD1 ILE A 248    14669   9497   6689   -735   -230   -184       C  
ATOM   1698  N   ASP A 249       7.694 -20.144  40.667  1.00 97.25           N  
ANISOU 1698  N   ASP A 249    17167  11846   7937   -666   -493   -121       N  
ATOM   1699  CA  ASP A 249       7.435 -19.730  42.041  1.00 94.99           C  
ANISOU 1699  CA  ASP A 249    17097  11565   7430   -629   -494   -154       C  
ATOM   1700  C   ASP A 249       8.705 -19.351  42.793  1.00 99.11           C  
ANISOU 1700  C   ASP A 249    17665  12248   7744   -746   -702   -155       C  
ATOM   1701  O   ASP A 249       8.620 -18.646  43.805  1.00100.88           O  
ANISOU 1701  O   ASP A 249    18118  12457   7754   -780   -746   -224       O  
ATOM   1702  CB  ASP A 249       6.706 -20.845  42.793  1.00 92.61           C  
ANISOU 1702  CB  ASP A 249    16812  11265   7112   -460   -329    -55       C  
ATOM   1703  CG  ASP A 249       5.202 -20.794  42.601  1.00 91.23           C  
ANISOU 1703  CG  ASP A 249    16675  10967   7023   -378   -127    -83       C  
ATOM   1704  OD1 ASP A 249       4.689 -19.740  42.169  1.00 88.71           O  
ANISOU 1704  OD1 ASP A 249    16422  10564   6721   -401   -116   -187       O  
ATOM   1705  OD2 ASP A 249       4.534 -21.812  42.879  1.00 89.28           O  
ANISOU 1705  OD2 ASP A 249    16392  10720   6811   -291     26      8       O  
ATOM   1706  N   GLU A 250       9.872 -19.798  42.332  1.00 96.11           N  
ANISOU 1706  N   GLU A 250    17073  12044   7401   -808   -829    -75       N  
ATOM   1707  CA  GLU A 250      11.128 -19.563  43.033  1.00104.99           C  
ANISOU 1707  CA  GLU A 250    18171  13406   8316   -925  -1037    -45       C  
ATOM   1708  C   GLU A 250      12.090 -18.676  42.258  1.00113.48           C  
ANISOU 1708  C   GLU A 250    19147  14580   9392  -1177  -1214   -100       C  
ATOM   1709  O   GLU A 250      12.678 -17.754  42.831  1.00122.09           O  
ANISOU 1709  O   GLU A 250    20360  15755  10272  -1392  -1380   -171       O  
ATOM   1710  CB  GLU A 250      11.805 -20.903  43.358  1.00110.73           C  
ANISOU 1710  CB  GLU A 250    18710  14341   9021   -752  -1041    134       C  
ATOM   1711  CG  GLU A 250      11.073 -21.734  44.399  1.00107.55           C  
ANISOU 1711  CG  GLU A 250    18450  13875   8540   -544   -898    201       C  
ATOM   1712  N   GLY A 251      12.272 -18.932  40.965  1.00166.95           N  
ANISOU 1712  N   GLY A 251    25714  21341  16378  -1179  -1181    -68       N  
ATOM   1713  CA  GLY A 251      13.224 -18.176  40.177  1.00172.90           C  
ANISOU 1713  CA  GLY A 251    26347  22211  17135  -1420  -1334    -99       C  
ATOM   1714  C   GLY A 251      14.645 -18.664  40.381  1.00181.14           C  
ANISOU 1714  C   GLY A 251    27121  23637  18068  -1461  -1494     38       C  
ATOM   1715  O   GLY A 251      14.929 -19.568  41.169  1.00182.97           O  
ANISOU 1715  O   GLY A 251    27278  24039  18205  -1281  -1495    157       O  
ATOM   1716  N   LEU A 252      15.563 -18.039  39.647  1.00169.09           N  
ANISOU 1716  N   LEU A 252    25439  22268  16538  -1697  -1628     31       N  
ATOM   1717  CA  LEU A 252      16.973 -18.411  39.670  1.00171.91           C  
ANISOU 1717  CA  LEU A 252    25474  23056  16788  -1750  -1783    176       C  
ATOM   1718  C   LEU A 252      17.807 -17.208  40.086  1.00175.08           C  
ANISOU 1718  C   LEU A 252    25913  23653  16956  -2156  -2014    106       C  
ATOM   1719  O   LEU A 252      17.777 -16.166  39.423  1.00174.88           O  
ANISOU 1719  O   LEU A 252    26002  23483  16961  -2431  -2050    -11       O  
ATOM   1720  CB  LEU A 252      17.428 -18.930  38.304  1.00169.09           C  
ANISOU 1720  CB  LEU A 252    24831  22782  16633  -1662  -1719    269       C  
ATOM   1721  CG  LEU A 252      18.935 -19.149  38.149  1.00171.65           C  
ANISOU 1721  CG  LEU A 252    24783  23595  16843  -1725  -1871    426       C  
ATOM   1722  CD1 LEU A 252      19.425 -20.229  39.103  1.00173.24           C  
ANISOU 1722  CD1 LEU A 252    24844  24083  16898  -1446  -1891    598       C  
ATOM   1723  CD2 LEU A 252      19.283 -19.502  36.711  1.00170.19           C  
ANISOU 1723  CD2 LEU A 252    24364  23445  16854  -1645  -1784    496       C  
ATOM   1724  N   ARG A 253      18.549 -17.358  41.182  1.00198.58           N  
ANISOU 1724  N   ARG A 253    28813  26957  19682  -2207  -2172    181       N  
ATOM   1725  CA  ARG A 253      19.507 -16.358  41.643  1.00200.01           C  
ANISOU 1725  CA  ARG A 253    28985  27412  19598  -2631  -2422    140       C  
ATOM   1726  C   ARG A 253      20.831 -17.069  41.882  1.00204.34           C  
ANISOU 1726  C   ARG A 253    29090  28542  20008  -2587  -2571    351       C  
ATOM   1727  O   ARG A 253      20.929 -17.922  42.770  1.00205.22           O  
ANISOU 1727  O   ARG A 253    29135  28830  20011  -2323  -2574    466       O  
ATOM   1728  CB  ARG A 253      19.018 -15.660  42.913  1.00200.52           C  
ANISOU 1728  CB  ARG A 253    29455  27311  19422  -2777  -2490      1       C  
ATOM   1729  CG  ARG A 253      17.857 -14.701  42.695  1.00200.42           C  
ANISOU 1729  CG  ARG A 253    29896  26776  19480  -2859  -2367   -206       C  
ATOM   1730  CD  ARG A 253      18.251 -13.554  41.778  1.00200.91           C  
ANISOU 1730  CD  ARG A 253    30024  26763  19548  -3246  -2446   -304       C  
ATOM   1731  NE  ARG A 253      17.106 -12.727  41.413  1.00198.97           N  
ANISOU 1731  NE  ARG A 253    30199  26011  19389  -3236  -2296   -476       N  
ATOM   1732  CZ  ARG A 253      16.759 -11.609  42.036  1.00199.72           C  
ANISOU 1732  CZ  ARG A 253    30765  25855  19266  -3454  -2338   -640       C  
ATOM   1733  NH1 ARG A 253      17.449 -11.150  43.068  1.00202.00           N  
ANISOU 1733  NH1 ARG A 253    31189  26330  19232  -3749  -2537   -674       N  
ATOM   1734  NH2 ARG A 253      15.694 -10.935  41.614  1.00193.92           N  
ANISOU 1734  NH2 ARG A 253    30388  24676  18617  -3363  -2173   -769       N  
ATOM   1735  N   LEU A 254      21.847 -16.721  41.088  1.00196.79           N  
ANISOU 1735  N   LEU A 254    27827  27902  19044  -2829  -2685    415       N  
ATOM   1736  CA  LEU A 254      23.115 -17.442  41.148  1.00196.41           C  
ANISOU 1736  CA  LEU A 254    27291  28458  18878  -2731  -2801    646       C  
ATOM   1737  C   LEU A 254      23.825 -17.217  42.478  1.00199.11           C  
ANISOU 1737  C   LEU A 254    27585  29206  18863  -2928  -3043    690       C  
ATOM   1738  O   LEU A 254      24.346 -18.166  43.076  1.00202.93           O  
ANISOU 1738  O   LEU A 254    27814  30061  19230  -2628  -3077    878       O  
ATOM   1739  CB  LEU A 254      24.009 -17.026  39.981  1.00194.60           C  
ANISOU 1739  CB  LEU A 254    26737  28497  18707  -2976  -2860    704       C  
ATOM   1740  CG  LEU A 254      23.491 -17.385  38.586  1.00193.74           C  
ANISOU 1740  CG  LEU A 254    26607  28075  18930  -2749  -2631    698       C  
ATOM   1741  CD1 LEU A 254      24.530 -17.064  37.521  1.00193.54           C  
ANISOU 1741  CD1 LEU A 254    26213  28402  18922  -2966  -2695    791       C  
ATOM   1742  CD2 LEU A 254      23.081 -18.850  38.520  1.00193.76           C  
ANISOU 1742  CD2 LEU A 254    26538  27996  19085  -2168  -2428    829       C  
ATOM   1743  N   LYS A 255      23.861 -15.977  42.953  1.00185.90           N  
ANISOU 1743  N   LYS A 255    26178  27464  16992  -3423  -3211    521       N  
ATOM   1744  CA  LYS A 255      24.498 -15.685  44.226  1.00185.28           C  
ANISOU 1744  CA  LYS A 255    26098  27753  16546  -3667  -3457    540       C  
ATOM   1745  C   LYS A 255      23.599 -16.111  45.383  1.00183.22           C  
ANISOU 1745  C   LYS A 255    26184  27215  16217  -3376  -3377    486       C  
ATOM   1746  O   LYS A 255      22.379 -16.233  45.246  1.00183.76           O  
ANISOU 1746  O   LYS A 255    26590  26741  16491  -3137  -3153    372       O  
ATOM   1747  CB  LYS A 255      24.826 -14.196  44.338  1.00183.33           C  
ANISOU 1747  CB  LYS A 255    26092  27484  16082  -4333  -3658    365       C  
ATOM   1748  CG  LYS A 255      23.605 -13.290  44.351  1.00179.32           C  
ANISOU 1748  CG  LYS A 255    26215  26272  15645  -4451  -3531    101       C  
ATOM   1749  N   ILE A 256      24.225 -16.347  46.537  1.00174.59           N  
ANISOU 1749  N   ILE A 256    24985  26536  14815  -3401  -3564    580       N  
ATOM   1750  CA  ILE A 256      23.469 -16.681  47.738  1.00176.30           C  
ANISOU 1750  CA  ILE A 256    25539  26534  14914  -3169  -3510    533       C  
ATOM   1751  C   ILE A 256      22.629 -15.480  48.151  1.00179.49           C  
ANISOU 1751  C   ILE A 256    26523  26447  15229  -3498  -3510    260       C  
ATOM   1752  O   ILE A 256      23.142 -14.364  48.313  1.00177.94           O  
ANISOU 1752  O   ILE A 256    26386  26275  14947  -3941  -3647    138       O  
ATOM   1753  CB  ILE A 256      24.412 -17.139  48.862  1.00174.22           C  
ANISOU 1753  CB  ILE A 256    25025  26864  14307  -3143  -3734    702       C  
ATOM   1754  CG1 ILE A 256      25.499 -16.095  49.133  1.00174.20           C  
ANISOU 1754  CG1 ILE A 256    24844  27203  14140  -3671  -3985    647       C  
ATOM   1755  CG2 ILE A 256      25.038 -18.483  48.517  1.00170.30           C  
ANISOU 1755  CG2 ILE A 256    24029  26774  13904  -2662  -3667    989       C  
ATOM   1756  CD1 ILE A 256      26.356 -16.406  50.339  1.00177.81           C  
ANISOU 1756  CD1 ILE A 256    25063  28153  14342  -3631  -4169    771       C  
ATOM   1757  N   TYR A 257      21.325 -15.696  48.299  1.00221.16           N  
ANISOU 1757  N   TYR A 257    32162  31196  20671  -3190  -3267    161       N  
ATOM   1758  CA  TYR A 257      20.390 -14.619  48.580  1.00219.94           C  
ANISOU 1758  CA  TYR A 257    32571  30537  20460  -3392  -3206    -84       C  
ATOM   1759  C   TYR A 257      19.456 -15.018  49.712  1.00220.77           C  
ANISOU 1759  C   TYR A 257    33000  30407  20474  -3085  -3081   -118       C  
ATOM   1760  O   TYR A 257      19.180 -16.201  49.930  1.00221.89           O  
ANISOU 1760  O   TYR A 257    32970  30609  20730  -2656  -2947     30       O  
ATOM   1761  CB  TYR A 257      19.575 -14.244  47.330  1.00216.11           C  
ANISOU 1761  CB  TYR A 257    32212  29597  20303  -3345  -2995   -190       C  
ATOM   1762  CG  TYR A 257      18.485 -15.230  46.975  1.00215.18           C  
ANISOU 1762  CG  TYR A 257    32076  29188  20496  -2832  -2703   -136       C  
ATOM   1763  CD1 TYR A 257      18.781 -16.410  46.305  1.00215.37           C  
ANISOU 1763  CD1 TYR A 257    31677  29412  20741  -2526  -2618     52       C  
ATOM   1764  CD2 TYR A 257      17.157 -14.975  47.295  1.00214.59           C  
ANISOU 1764  CD2 TYR A 257    32416  28647  20472  -2664  -2506   -271       C  
ATOM   1765  CE1 TYR A 257      17.789 -17.313  45.973  1.00215.04           C  
ANISOU 1765  CE1 TYR A 257    31654  29094  20959  -2117  -2358     94       C  
ATOM   1766  CE2 TYR A 257      16.158 -15.873  46.967  1.00215.03           C  
ANISOU 1766  CE2 TYR A 257    32431  28476  20793  -2251  -2248   -216       C  
ATOM   1767  CZ  TYR A 257      16.479 -17.039  46.305  1.00216.28           C  
ANISOU 1767  CZ  TYR A 257    32192  28820  21163  -2005  -2181    -39       C  
ATOM   1768  OH  TYR A 257      15.488 -17.936  45.976  1.00214.97           O  
ANISOU 1768  OH  TYR A 257    32022  28419  21237  -1650  -1932      9       O  
ATOM   1769  N   LYS A 258      18.975 -14.008  50.431  1.00182.82           N  
ANISOU 1769  N   LYS A 258    28581  25283  15598  -3238  -3050   -309       N  
ATOM   1770  CA  LYS A 258      18.064 -14.220  51.546  1.00180.29           C  
ANISOU 1770  CA  LYS A 258    28589  24731  15182  -2974  -2919   -358       C  
ATOM   1771  C   LYS A 258      16.665 -14.527  51.027  1.00181.40           C  
ANISOU 1771  C   LYS A 258    28972  24431  15522  -2650  -2633   -402       C  
ATOM   1772  O   LYS A 258      16.157 -13.836  50.138  1.00181.96           O  
ANISOU 1772  O   LYS A 258    29186  24185  15765  -2733  -2529   -518       O  
ATOM   1773  CB  LYS A 258      18.039 -12.982  52.441  1.00174.89           C  
ANISOU 1773  CB  LYS A 258    28243  23855  14351  -3241  -2970   -539       C  
ATOM   1774  CG  LYS A 258      18.206 -11.682  51.669  1.00169.88           C  
ANISOU 1774  CG  LYS A 258    27752  22983  13812  -3614  -2991   -686       C  
ATOM   1775  CD  LYS A 258      18.501 -10.508  52.585  1.00160.96           C  
ANISOU 1775  CD  LYS A 258    26930  21742  12487  -3940  -3088   -825       C  
ATOM   1776  CE  LYS A 258      18.828  -9.261  51.778  1.00152.55           C  
ANISOU 1776  CE  LYS A 258    26001  20465  11496  -4344  -3117   -932       C  
ATOM   1777  NZ  LYS A 258      19.217  -8.115  52.644  1.00154.29           N  
ANISOU 1777  NZ  LYS A 258    26545  20576  11503  -4708  -3218  -1049       N  
ATOM   1778  N   ASP A 259      16.044 -15.563  51.581  1.00219.27           N  
ANISOU 1778  N   ASP A 259    33786  29210  20315  -2271  -2491   -300       N  
ATOM   1779  CA  ASP A 259      14.693 -15.944  51.196  1.00217.47           C  
ANISOU 1779  CA  ASP A 259    33673  28599  20355  -1933  -2180   -320       C  
ATOM   1780  C   ASP A 259      13.691 -15.137  52.026  1.00215.45           C  
ANISOU 1780  C   ASP A 259    33933  28004  19926  -1914  -2068   -487       C  
ATOM   1781  O   ASP A 259      14.038 -14.108  52.612  1.00211.76           O  
ANISOU 1781  O   ASP A 259    33630  27500  19328  -2158  -2177   -609       O  
ATOM   1782  CB  ASP A 259      14.518 -17.460  51.342  1.00217.70           C  
ANISOU 1782  CB  ASP A 259    33429  28758  20529  -1542  -2044   -120       C  
ATOM   1783  CG  ASP A 259      14.746 -17.947  52.762  1.00216.69           C  
ANISOU 1783  CG  ASP A 259    33394  28830  20109  -1430  -2113    -40       C  
ATOM   1784  OD1 ASP A 259      15.157 -17.138  53.621  1.00218.31           O  
ANISOU 1784  OD1 ASP A 259    33831  29125  19991  -1677  -2297   -135       O  
ATOM   1785  OD2 ASP A 259      14.514 -19.147  53.021  1.00214.98           O  
ANISOU 1785  OD2 ASP A 259    33046  28669  19969  -1103  -1981    120       O  
ATOM   1786  N   THR A 260      12.438 -15.593  52.087  1.00207.42           N  
ANISOU 1786  N   THR A 260    33026  26731  19054  -1578  -1793   -477       N  
ATOM   1787  CA  THR A 260      11.435 -14.878  52.868  1.00204.78           C  
ANISOU 1787  CA  THR A 260    33101  26100  18606  -1485  -1640   -609       C  
ATOM   1788  C   THR A 260      11.666 -15.042  54.365  1.00205.62           C  
ANISOU 1788  C   THR A 260    33311  26347  18469  -1445  -1700   -583       C  
ATOM   1789  O   THR A 260      11.345 -14.136  55.142  1.00206.26           O  
ANISOU 1789  O   THR A 260    33689  26251  18429  -1496  -1671   -710       O  
ATOM   1790  CB  THR A 260      10.033 -15.358  52.492  1.00199.77           C  
ANISOU 1790  CB  THR A 260    32518  25227  18160  -1149  -1332   -584       C  
ATOM   1791  OG1 THR A 260       9.992 -16.790  52.520  1.00201.90           O  
ANISOU 1791  OG1 THR A 260    32455  25665  18591   -919  -1245   -396       O  
ATOM   1792  CG2 THR A 260       9.664 -14.873  51.098  1.00194.88           C  
ANISOU 1792  CG2 THR A 260    31813  24418  17814  -1190  -1253   -646       C  
ATOM   1793  N   GLU A 261      12.218 -16.181  54.786  1.00196.73           N  
ANISOU 1793  N   GLU A 261    31964  25528  17255  -1335  -1779   -413       N  
ATOM   1794  CA  GLU A 261      12.515 -16.398  56.196  1.00196.33           C  
ANISOU 1794  CA  GLU A 261    31988  25650  16960  -1289  -1853   -373       C  
ATOM   1795  C   GLU A 261      13.803 -15.714  56.635  1.00197.50           C  
ANISOU 1795  C   GLU A 261    32056  26070  16916  -1638  -2158   -420       C  
ATOM   1796  O   GLU A 261      14.002 -15.509  57.837  1.00196.60           O  
ANISOU 1796  O   GLU A 261    32077  26045  16578  -1669  -2230   -445       O  
ATOM   1797  CB  GLU A 261      12.601 -17.899  56.490  1.00195.35           C  
ANISOU 1797  CB  GLU A 261    31679  25742  16804  -1003  -1805   -153       C  
ATOM   1798  CG  GLU A 261      12.379 -18.266  57.950  1.00192.63           C  
ANISOU 1798  CG  GLU A 261    31484  25459  16247   -833  -1758   -106       C  
ATOM   1799  CD  GLU A 261      11.112 -17.658  58.520  1.00189.73           C  
ANISOU 1799  CD  GLU A 261    31460  24743  15886   -721  -1522   -239       C  
ATOM   1800  OE1 GLU A 261      10.035 -17.849  57.916  1.00184.98           O  
ANISOU 1800  OE1 GLU A 261    30916  23895  15474   -543  -1273   -243       O  
ATOM   1801  OE2 GLU A 261      11.194 -16.989  59.571  1.00185.76           O  
ANISOU 1801  OE2 GLU A 261    31163  24233  15185   -804  -1583   -332       O  
ATOM   1802  N   GLY A 262      14.674 -15.353  55.694  1.00194.51           N  
ANISOU 1802  N   GLY A 262    31453  25839  16613  -1914  -2334   -428       N  
ATOM   1803  CA  GLY A 262      15.931 -14.699  55.989  1.00192.22           C  
ANISOU 1803  CA  GLY A 262    31036  25843  16156  -2286  -2620   -460       C  
ATOM   1804  C   GLY A 262      17.149 -15.575  55.795  1.00191.17           C  
ANISOU 1804  C   GLY A 262    30446  26239  15951  -2313  -2835   -261       C  
ATOM   1805  O   GLY A 262      18.268 -15.048  55.719  1.00191.59           O  
ANISOU 1805  O   GLY A 262    30294  26590  15912  -2649  -3075   -269       O  
ATOM   1806  N   TYR A 263      16.970 -16.890  55.713  1.00183.72           N  
ANISOU 1806  N   TYR A 263    29344  25423  15040  -1960  -2746    -70       N  
ATOM   1807  CA  TYR A 263      18.096 -17.791  55.531  1.00184.74           C  
ANISOU 1807  CA  TYR A 263    29050  26058  15085  -1907  -2926    154       C  
ATOM   1808  C   TYR A 263      18.649 -17.680  54.112  1.00190.53           C  
ANISOU 1808  C   TYR A 263    29487  26898  16006  -2075  -2991    188       C  
ATOM   1809  O   TYR A 263      17.960 -17.268  53.174  1.00192.52           O  
ANISOU 1809  O   TYR A 263    29841  26782  16525  -2103  -2829     73       O  
ATOM   1810  CB  TYR A 263      17.683 -19.234  55.819  1.00183.38           C  
ANISOU 1810  CB  TYR A 263    28813  25907  14957  -1427  -2752    356       C  
ATOM   1811  CG  TYR A 263      16.971 -19.427  57.140  1.00184.20           C  
ANISOU 1811  CG  TYR A 263    29267  25865  14854  -1244  -2653    335       C  
ATOM   1812  CD1 TYR A 263      17.375 -18.740  58.277  1.00184.30           C  
ANISOU 1812  CD1 TYR A 263    29369  26025  14630  -1429  -2809    245       C  
ATOM   1813  CD2 TYR A 263      15.894 -20.297  57.248  1.00180.96           C  
ANISOU 1813  CD2 TYR A 263    28985  25163  14609   -863  -2352    400       C  
ATOM   1814  CE1 TYR A 263      16.726 -18.914  59.485  1.00185.06           C  
ANISOU 1814  CE1 TYR A 263    29736  25991  14586  -1242  -2692    227       C  
ATOM   1815  CE2 TYR A 263      15.239 -20.477  58.452  1.00175.48           C  
ANISOU 1815  CE2 TYR A 263    28598  24352  13724   -699  -2246    393       C  
ATOM   1816  CZ  TYR A 263      15.659 -19.784  59.566  1.00184.64           C  
ANISOU 1816  CZ  TYR A 263    29844  25667  14642   -876  -2408    305       C  
ATOM   1817  OH  TYR A 263      15.010 -19.961  60.766  1.00191.52           O  
ANISOU 1817  OH  TYR A 263    30964  26424  15380   -698  -2278    298       O  
ATOM   1818  N   TYR A 264      19.915 -18.058  53.963  1.00218.21           N  
ANISOU 1818  N   TYR A 264    32557  30932  19420  -2144  -3202    356       N  
ATOM   1819  CA  TYR A 264      20.559 -18.014  52.658  1.00220.98           C  
ANISOU 1819  CA  TYR A 264    32528  31443  19990  -2261  -3241    411       C  
ATOM   1820  C   TYR A 264      20.068 -19.157  51.778  1.00215.99           C  
ANISOU 1820  C   TYR A 264    31697  30642  19727  -1806  -2970    544       C  
ATOM   1821  O   TYR A 264      20.143 -20.328  52.160  1.00214.76           O  
ANISOU 1821  O   TYR A 264    31401  30633  19566  -1412  -2889    732       O  
ATOM   1822  CB  TYR A 264      22.078 -18.080  52.809  1.00227.92           C  
ANISOU 1822  CB  TYR A 264    32970  33002  20628  -2457  -3544    571       C  
ATOM   1823  CG  TYR A 264      22.733 -16.742  53.067  1.00233.86           C  
ANISOU 1823  CG  TYR A 264    33726  33832  21297  -2964  -3737    400       C  
ATOM   1824  CD1 TYR A 264      22.050 -15.555  52.833  1.00232.53           C  
ANISOU 1824  CD1 TYR A 264    33950  33162  21239  -3252  -3655    144       C  
ATOM   1825  CD2 TYR A 264      24.039 -16.665  53.533  1.00241.93           C  
ANISOU 1825  CD2 TYR A 264    34369  35421  22133  -3146  -3987    506       C  
ATOM   1826  CE1 TYR A 264      22.647 -14.329  53.063  1.00241.42           C  
ANISOU 1826  CE1 TYR A 264    35133  34312  22283  -3727  -3809      1       C  
ATOM   1827  CE2 TYR A 264      24.644 -15.445  53.766  1.00243.79           C  
ANISOU 1827  CE2 TYR A 264    34633  35705  22290  -3653  -4153    357       C  
ATOM   1828  CZ  TYR A 264      23.944 -14.280  53.530  1.00245.78           C  
ANISOU 1828  CZ  TYR A 264    35322  35419  22646  -3950  -4060    106       C  
ATOM   1829  OH  TYR A 264      24.543 -13.063  53.760  1.00249.91           O  
ANISOU 1829  OH  TYR A 264    35927  35952  23075  -4466  -4207    -28       O  
ATOM   1830  N   THR A 265      19.562 -18.809  50.599  1.00203.63           N  
ANISOU 1830  N   THR A 265    30152  28756  18464  -1867  -2828    444       N  
ATOM   1831  CA  THR A 265      19.165 -19.776  49.589  1.00199.66           C  
ANISOU 1831  CA  THR A 265    29462  28095  18304  -1518  -2594    549       C  
ATOM   1832  C   THR A 265      19.937 -19.502  48.305  1.00198.32           C  
ANISOU 1832  C   THR A 265    28958  28105  18289  -1696  -2667    579       C  
ATOM   1833  O   THR A 265      20.415 -18.389  48.070  1.00198.94           O  
ANISOU 1833  O   THR A 265    29047  28270  18272  -2122  -2842    465       O  
ATOM   1834  CB  THR A 265      17.655 -19.724  49.319  1.00198.57           C  
ANISOU 1834  CB  THR A 265    29662  27385  18400  -1381  -2319    411       C  
ATOM   1835  OG1 THR A 265      17.263 -18.375  49.036  1.00202.60           O  
ANISOU 1835  OG1 THR A 265    30431  27640  18908  -1724  -2357    191       O  
ATOM   1836  CG2 THR A 265      16.880 -20.228  50.528  1.00193.49           C  
ANISOU 1836  CG2 THR A 265    29295  26597  17625  -1141  -2203    425       C  
ATOM   1837  N   ILE A 266      20.065 -20.536  47.473  1.00167.76           N  
ANISOU 1837  N   ILE A 266    24818  24281  14641  -1372  -2524    735       N  
ATOM   1838  CA  ILE A 266      20.798 -20.440  46.219  1.00166.73           C  
ANISOU 1838  CA  ILE A 266    24351  24337  14663  -1469  -2560    791       C  
ATOM   1839  C   ILE A 266      20.053 -21.221  45.146  1.00166.95           C  
ANISOU 1839  C   ILE A 266    24382  24018  15032  -1161  -2286    816       C  
ATOM   1840  O   ILE A 266      19.269 -22.129  45.432  1.00163.77           O  
ANISOU 1840  O   ILE A 266    24140  23371  14713   -828  -2092    861       O  
ATOM   1841  CB  ILE A 266      22.253 -20.951  46.351  1.00164.58           C  
ANISOU 1841  CB  ILE A 266    23622  24711  14199  -1399  -2740   1023       C  
ATOM   1842  CG1 ILE A 266      23.158 -20.273  45.320  1.00168.53           C  
ANISOU 1842  CG1 ILE A 266    23803  25489  14740  -1718  -2870   1028       C  
ATOM   1843  CG2 ILE A 266      22.313 -22.466  46.211  1.00162.94           C  
ANISOU 1843  CG2 ILE A 266    23259  24568  14083   -845  -2561   1245       C  
ATOM   1844  CD1 ILE A 266      24.626 -20.584  45.497  1.00170.77           C  
ANISOU 1844  CD1 ILE A 266    23599  26492  14795  -1711  -3072   1255       C  
ATOM   1845  N   GLY A 267      20.300 -20.844  43.895  1.00214.55           N  
ANISOU 1845  N   GLY A 267    30248  30028  21244  -1304  -2275    784       N  
ATOM   1846  CA  GLY A 267      19.680 -21.546  42.783  1.00212.90           C  
ANISOU 1846  CA  GLY A 267    30031  29520  21340  -1050  -2037    804       C  
ATOM   1847  C   GLY A 267      18.185 -21.305  42.747  1.00206.83           C  
ANISOU 1847  C   GLY A 267    29638  28213  20736  -1045  -1857    629       C  
ATOM   1848  O   GLY A 267      17.715 -20.162  42.738  1.00205.67           O  
ANISOU 1848  O   GLY A 267    29698  27865  20583  -1334  -1903    447       O  
ATOM   1849  N   ILE A 268      17.421 -22.396  42.730  1.00150.83           N  
ANISOU 1849  N   ILE A 268    22644  20892  13773   -710  -1642    693       N  
ATOM   1850  CA  ILE A 268      15.967 -22.323  42.656  1.00141.03           C  
ANISOU 1850  CA  ILE A 268    21698  19200  12688   -681  -1454    560       C  
ATOM   1851  C   ILE A 268      15.367 -22.753  43.988  1.00139.42           C  
ANISOU 1851  C   ILE A 268    21719  18921  12332   -532  -1393    581       C  
ATOM   1852  O   ILE A 268      14.760 -23.824  44.093  1.00134.59           O  
ANISOU 1852  O   ILE A 268    21188  18153  11796   -271  -1207    664       O  
ATOM   1853  CB  ILE A 268      15.429 -23.185  41.499  1.00129.20           C  
ANISOU 1853  CB  ILE A 268    20157  17477  11457   -487  -1244    602       C  
ATOM   1854  CG1 ILE A 268      16.372 -23.107  40.298  1.00134.45           C  
ANISOU 1854  CG1 ILE A 268    20541  18326  12217   -542  -1309    654       C  
ATOM   1855  CG2 ILE A 268      14.028 -22.742  41.107  1.00123.54           C  
ANISOU 1855  CG2 ILE A 268    19660  16368  10910   -566  -1098    443       C  
ATOM   1856  CD1 ILE A 268      15.935 -23.948  39.121  1.00135.24           C  
ANISOU 1856  CD1 ILE A 268    20621  18212  12551   -361  -1114    691       C  
ATOM   1857  N   GLY A 269      15.538 -21.922  45.013  1.00140.16           N  
ANISOU 1857  N   GLY A 269    21942  19118  12196   -713  -1546    505       N  
ATOM   1858  CA  GLY A 269      14.954 -22.207  46.310  1.00136.80           C  
ANISOU 1858  CA  GLY A 269    21753  18620  11604   -587  -1490    512       C  
ATOM   1859  C   GLY A 269      15.649 -23.294  47.098  1.00142.11           C  
ANISOU 1859  C   GLY A 269    22319  19567  12108   -335  -1522    713       C  
ATOM   1860  O   GLY A 269      15.011 -23.955  47.923  1.00133.81           O  
ANISOU 1860  O   GLY A 269    21457  18393  10992   -136  -1392    762       O  
ATOM   1861  N   HIS A 270      16.944 -23.501  46.868  1.00181.51           N  
ANISOU 1861  N   HIS A 270    27008  24945  17013   -323  -1683    843       N  
ATOM   1862  CA  HIS A 270      17.715 -24.497  47.604  1.00183.64           C  
ANISOU 1862  CA  HIS A 270    27154  25532  17089    -43  -1726   1058       C  
ATOM   1863  C   HIS A 270      18.283 -23.846  48.859  1.00187.83           C  
ANISOU 1863  C   HIS A 270    27716  26363  17286   -217  -1963   1042       C  
ATOM   1864  O   HIS A 270      19.229 -23.055  48.784  1.00193.44           O  
ANISOU 1864  O   HIS A 270    28226  27407  17865   -493  -2200   1021       O  
ATOM   1865  CB  HIS A 270      18.828 -25.077  46.735  1.00184.03           C  
ANISOU 1865  CB  HIS A 270    26840  25898  17186    107  -1770   1231       C  
ATOM   1866  CG  HIS A 270      19.763 -25.981  47.478  1.00185.80           C  
ANISOU 1866  CG  HIS A 270    26905  26521  17171    416  -1838   1469       C  
ATOM   1867  ND1 HIS A 270      20.976 -25.553  47.972  1.00191.23           N  
ANISOU 1867  ND1 HIS A 270    27312  27749  17596    297  -2106   1555       N  
ATOM   1868  CD2 HIS A 270      19.661 -27.289  47.813  1.00185.61           C  
ANISOU 1868  CD2 HIS A 270    26973  26442  17109    842  -1672   1649       C  
ATOM   1869  CE1 HIS A 270      21.582 -26.558  48.579  1.00189.32           C  
ANISOU 1869  CE1 HIS A 270    26970  27797  17167    673  -2105   1786       C  
ATOM   1870  NE2 HIS A 270      20.805 -27.623  48.496  1.00189.64           N  
ANISOU 1870  NE2 HIS A 270    27256  27460  17338   1019  -1836   1846       N  
ATOM   1871  N   LEU A 271      17.705 -24.176  50.010  1.00152.66           N  
ANISOU 1871  N   LEU A 271    23522  21799  12681    -79  -1898   1052       N  
ATOM   1872  CA  LEU A 271      18.186 -23.635  51.272  1.00153.43           C  
ANISOU 1872  CA  LEU A 271    23693  22168  12437   -225  -2114   1037       C  
ATOM   1873  C   LEU A 271      19.576 -24.174  51.588  1.00159.67           C  
ANISOU 1873  C   LEU A 271    24143  23519  13004    -93  -2308   1258       C  
ATOM   1874  O   LEU A 271      19.846 -25.369  51.441  1.00157.05           O  
ANISOU 1874  O   LEU A 271    23682  23283  12708    297  -2193   1466       O  
ATOM   1875  CB  LEU A 271      17.216 -23.982  52.402  1.00148.20           C  
ANISOU 1875  CB  LEU A 271    23389  21257  11665    -59  -1970   1018       C  
ATOM   1876  CG  LEU A 271      17.771 -23.934  53.827  1.00145.82           C  
ANISOU 1876  CG  LEU A 271    23158  21268  10979    -55  -2154   1082       C  
ATOM   1877  CD1 LEU A 271      17.997 -22.498  54.270  1.00153.38           C  
ANISOU 1877  CD1 LEU A 271    24239  22306  11731   -493  -2386    886       C  
ATOM   1878  CD2 LEU A 271      16.842 -24.657  54.790  1.00134.90           C  
ANISOU 1878  CD2 LEU A 271    22087  19642   9525    218  -1951   1128       C  
ATOM   1879  N   LEU A 272      20.465 -23.278  52.018  1.00188.07           N  
ANISOU 1879  N   LEU A 272    27607  27502  16349   -421  -2601   1220       N  
ATOM   1880  CA  LEU A 272      21.810 -23.691  52.401  1.00194.54           C  
ANISOU 1880  CA  LEU A 272    28060  28944  16912   -324  -2815   1438       C  
ATOM   1881  C   LEU A 272      21.824 -24.245  53.822  1.00194.56           C  
ANISOU 1881  C   LEU A 272    28214  29097  16613    -98  -2856   1548       C  
ATOM   1882  O   LEU A 272      22.173 -25.409  54.044  1.00195.46           O  
ANISOU 1882  O   LEU A 272    28203  29397  16667    341  -2780   1784       O  
ATOM   1883  CB  LEU A 272      22.787 -22.518  52.270  1.00200.58           C  
ANISOU 1883  CB  LEU A 272    28594  30112  17506   -823  -3127   1363       C  
ATOM   1884  CG  LEU A 272      23.345 -22.209  50.876  1.00194.00           C  
ANISOU 1884  CG  LEU A 272    27430  29397  16886   -986  -3147   1369       C  
ATOM   1885  CD1 LEU A 272      24.055 -23.427  50.303  1.00198.45           C  
ANISOU 1885  CD1 LEU A 272    27602  30278  17521   -531  -3061   1646       C  
ATOM   1886  CD2 LEU A 272      22.271 -21.702  49.925  1.00187.96           C  
ANISOU 1886  CD2 LEU A 272    26928  28029  16459  -1115  -2945   1156       C  
ATOM   1887  N   THR A 273      21.444 -23.419  54.794  1.00203.46           N  
ANISOU 1887  N   THR A 273    29645  30130  17532   -376  -2966   1382       N  
ATOM   1888  CA  THR A 273      21.361 -23.847  56.182  1.00212.10           C  
ANISOU 1888  CA  THR A 273    30933  31329  18327   -189  -3000   1463       C  
ATOM   1889  C   THR A 273      20.500 -22.856  56.951  1.00214.14           C  
ANISOU 1889  C   THR A 273    31646  31249  18468   -488  -3009   1212       C  
ATOM   1890  O   THR A 273      20.536 -21.653  56.681  1.00212.99           O  
ANISOU 1890  O   THR A 273    31583  31039  18306   -928  -3141   1010       O  
ATOM   1891  CB  THR A 273      22.750 -23.960  56.826  1.00220.44           C  
ANISOU 1891  CB  THR A 273    31645  33096  19018   -202  -3309   1651       C  
ATOM   1892  OG1 THR A 273      22.612 -24.239  58.225  1.00221.04           O  
ANISOU 1892  OG1 THR A 273    31956  33251  18777    -62  -3358   1702       O  
ATOM   1893  CG2 THR A 273      23.541 -22.670  56.639  1.00227.26           C  
ANISOU 1893  CG2 THR A 273    32334  34284  19732   -778  -3622   1519       C  
ATOM   1894  N   LYS A 274      19.718 -23.373  57.901  1.00207.29           N  
ANISOU 1894  N   LYS A 274    31100  30153  17507   -234  -2853   1232       N  
ATOM   1895  CA  LYS A 274      18.907 -22.513  58.752  1.00203.45           C  
ANISOU 1895  CA  LYS A 274    31063  29375  16865   -448  -2841   1019       C  
ATOM   1896  C   LYS A 274      19.707 -21.911  59.898  1.00207.19           C  
ANISOU 1896  C   LYS A 274    31547  30240  16936   -680  -3138    992       C  
ATOM   1897  O   LYS A 274      19.288 -20.894  60.461  1.00209.42           O  
ANISOU 1897  O   LYS A 274    32076  30309  17184   -931  -3143    764       O  
ATOM   1898  CB  LYS A 274      17.713 -23.292  59.309  1.00199.05           C  
ANISOU 1898  CB  LYS A 274    30822  28430  16378    -91  -2530   1052       C  
ATOM   1899  CG  LYS A 274      18.094 -24.514  60.128  1.00199.89           C  
ANISOU 1899  CG  LYS A 274    30865  28788  16296    301  -2512   1307       C  
ATOM   1900  N   SER A 275      20.839 -22.511  60.252  1.00203.40           N  
ANISOU 1900  N   SER A 275    30731  30313  16239   -554  -3339   1211       N  
ATOM   1901  CA  SER A 275      21.674 -21.957  61.305  1.00209.34           C  
ANISOU 1901  CA  SER A 275    31378  31446  16715   -733  -3596   1170       C  
ATOM   1902  C   SER A 275      22.367 -20.690  60.807  1.00215.78           C  
ANISOU 1902  C   SER A 275    32020  32377  17588  -1245  -3811    984       C  
ATOM   1903  O   SER A 275      22.818 -20.638  59.659  1.00214.84           O  
ANISOU 1903  O   SER A 275    31612  32369  17648  -1360  -3850   1028       O  
ATOM   1904  CB  SER A 275      22.715 -22.981  61.758  1.00208.79           C  
ANISOU 1904  CB  SER A 275    30980  31922  16428   -404  -3743   1466       C  
ATOM   1905  OG  SER A 275      23.643 -22.403  62.659  1.00208.85           O  
ANISOU 1905  OG  SER A 275    30862  32294  16198   -615  -4027   1420       O  
ATOM   1906  N   PRO A 276      22.465 -19.655  61.643  1.00237.95           N  
ANISOU 1906  N   PRO A 276    35014  35149  20248  -1569  -3940    782       N  
ATOM   1907  CA  PRO A 276      23.105 -18.408  61.199  1.00242.18           C  
ANISOU 1907  CA  PRO A 276    35447  35741  20831  -2095  -4125    606       C  
ATOM   1908  C   PRO A 276      24.609 -18.553  61.038  1.00255.02           C  
ANISOU 1908  C   PRO A 276    36543  37999  22354  -2225  -4407    772       C  
ATOM   1909  O   PRO A 276      25.381 -18.049  61.860  1.00265.24           O  
ANISOU 1909  O   PRO A 276    37767  39586  23425  -2473  -4635    736       O  
ATOM   1910  CB  PRO A 276      22.753 -17.410  62.315  1.00242.08           C  
ANISOU 1910  CB  PRO A 276    35839  35499  20642  -2347  -4159    377       C  
ATOM   1911  CG  PRO A 276      21.709 -18.098  63.166  1.00238.24           C  
ANISOU 1911  CG  PRO A 276    35676  34762  20082  -1939  -3938    409       C  
ATOM   1912  CD  PRO A 276      21.972 -19.558  63.024  1.00235.83           C  
ANISOU 1912  CD  PRO A 276    35085  34763  19757  -1482  -3902    707       C  
ATOM   1913  N   SER A 277      25.036 -19.239  59.980  1.00230.54           N  
ANISOU 1913  N   SER A 277    33058  35120  19417  -2060  -4384    961       N  
ATOM   1914  CA  SER A 277      26.452 -19.472  59.704  1.00231.63           C  
ANISOU 1914  CA  SER A 277    32624  35885  19498  -2128  -4608   1153       C  
ATOM   1915  C   SER A 277      26.712 -19.138  58.238  1.00229.82           C  
ANISOU 1915  C   SER A 277    32128  35662  19530  -2345  -4579   1144       C  
ATOM   1916  O   SER A 277      26.380 -19.925  57.347  1.00229.83           O  
ANISOU 1916  O   SER A 277    32025  35587  19713  -2025  -4405   1275       O  
ATOM   1917  CB  SER A 277      26.847 -20.910  60.024  1.00231.92           C  
ANISOU 1917  CB  SER A 277    32402  36280  19437  -1565  -4585   1471       C  
ATOM   1918  OG  SER A 277      26.703 -21.184  61.406  1.00237.49           O  
ANISOU 1918  OG  SER A 277    33349  37007  19880  -1387  -4633   1487       O  
ATOM   1919  N   LEU A 278      27.306 -17.967  57.992  1.00217.59           N  
ANISOU 1919  N   LEU A 278    30490  34196  17990  -2900  -4739    994       N  
ATOM   1920  CA  LEU A 278      27.634 -17.571  56.628  1.00213.46           C  
ANISOU 1920  CA  LEU A 278    29709  33702  17694  -3147  -4722    987       C  
ATOM   1921  C   LEU A 278      28.736 -18.432  56.027  1.00220.41           C  
ANISOU 1921  C   LEU A 278    29944  35207  18596  -2925  -4793   1285       C  
ATOM   1922  O   LEU A 278      28.817 -18.544  54.799  1.00217.82           O  
ANISOU 1922  O   LEU A 278    29395  34889  18476  -2914  -4704   1342       O  
ATOM   1923  CB  LEU A 278      28.033 -16.092  56.594  1.00204.96           C  
ANISOU 1923  CB  LEU A 278    28730  32553  16594  -3814  -4864    770       C  
ATOM   1924  CG  LEU A 278      29.150 -15.617  57.531  1.00204.41           C  
ANISOU 1924  CG  LEU A 278    28451  32960  16257  -4157  -5135    794       C  
ATOM   1925  CD1 LEU A 278      30.524 -15.728  56.878  1.00206.41           C  
ANISOU 1925  CD1 LEU A 278    28037  33873  16517  -4336  -5290    998       C  
ATOM   1926  CD2 LEU A 278      28.887 -14.192  57.995  1.00191.38           C  
ANISOU 1926  CD2 LEU A 278    27262  30925  14529  -4706  -5186    510       C  
ATOM   1927  N   ASN A 279      29.583 -19.041  56.859  1.00264.94           N  
ANISOU 1927  N   ASN A 279    35276  41366  24022  -2725  -4938   1482       N  
ATOM   1928  CA  ASN A 279      30.629 -19.918  56.347  1.00267.92           C  
ANISOU 1928  CA  ASN A 279    35032  42349  24416  -2433  -4971   1788       C  
ATOM   1929  C   ASN A 279      30.078 -21.293  55.990  1.00265.27           C  
ANISOU 1929  C   ASN A 279    34714  41891  24187  -1747  -4735   1987       C  
ATOM   1930  O   ASN A 279      30.511 -21.900  55.004  1.00264.25           O  
ANISOU 1930  O   ASN A 279    34205  41999  24198  -1496  -4644   2175       O  
ATOM   1931  CB  ASN A 279      31.758 -20.044  57.370  1.00267.34           C  
ANISOU 1931  CB  ASN A 279    34616  42887  24074  -2462  -5202   1934       C  
ATOM   1932  N   ALA A 280      29.125 -21.798  56.778  1.00198.72           N  
ANISOU 1932  N   ALA A 280    26736  33084  15683  -1436  -4614   1955       N  
ATOM   1933  CA  ALA A 280      28.517 -23.088  56.477  1.00192.54           C  
ANISOU 1933  CA  ALA A 280    26041  32120  14996   -817  -4359   2139       C  
ATOM   1934  C   ALA A 280      27.683 -23.050  55.205  1.00192.12           C  
ANISOU 1934  C   ALA A 280    26137  31650  15211   -819  -4145   2056       C  
ATOM   1935  O   ALA A 280      27.464 -24.100  54.592  1.00189.72           O  
ANISOU 1935  O   ALA A 280    25761  31300  15024   -338  -3936   2240       O  
ATOM   1936  CB  ALA A 280      27.655 -23.554  57.651  1.00185.05           C  
ANISOU 1936  CB  ALA A 280    25566  30850  13893   -550  -4269   2117       C  
ATOM   1937  N   ALA A 281      27.210 -21.869  54.799  1.00237.83           N  
ANISOU 1937  N   ALA A 281    32154  37109  21101  -1335  -4179   1783       N  
ATOM   1938  CA  ALA A 281      26.483 -21.762  53.538  1.00238.57           C  
ANISOU 1938  CA  ALA A 281    32366  36829  21450  -1377  -3995   1704       C  
ATOM   1939  C   ALA A 281      27.404 -22.017  52.352  1.00239.92           C  
ANISOU 1939  C   ALA A 281    32007  37401  21751  -1323  -4010   1874       C  
ATOM   1940  O   ALA A 281      26.985 -22.604  51.347  1.00239.27           O  
ANISOU 1940  O   ALA A 281    31909  37060  21944  -1031  -3774   1924       O  
ATOM   1941  CB  ALA A 281      25.824 -20.388  53.425  1.00238.61           C  
ANISOU 1941  CB  ALA A 281    32758  36368  21535  -1923  -4022   1372       C  
ATOM   1942  N   LYS A 355      28.663 -21.587  52.449  1.00202.14           N  
ANISOU 1942  N   LYS A 355    26781  33149  16874  -1572  -4230   1938       N  
ATOM   1943  CA  LYS A 355      29.624 -21.858  51.387  1.00196.41           C  
ANISOU 1943  CA  LYS A 355    25508  32870  16249  -1497  -4236   2125       C  
ATOM   1944  C   LYS A 355      30.133 -23.292  51.433  1.00202.50           C  
ANISOU 1944  C   LYS A 355    25965  33999  16977   -809  -4125   2453       C  
ATOM   1945  O   LYS A 355      30.394 -23.885  50.380  1.00197.81           O  
ANISOU 1945  O   LYS A 355    25106  33532  16522   -511  -3985   2612       O  
ATOM   1946  CB  LYS A 355      30.799 -20.882  51.478  1.00189.66           C  
ANISOU 1946  CB  LYS A 355    24274  32485  15302  -2033  -4488   2092       C  
ATOM   1947  N   SER A 387      30.273 -23.866  52.630  1.00254.38           N  
ANISOU 1947  N   SER A 387    32592  40705  23356   -527  -4169   2556       N  
ATOM   1948  CA  SER A 387      30.771 -25.233  52.742  1.00255.15           C  
ANISOU 1948  CA  SER A 387    32442  41092  23410    154  -4044   2867       C  
ATOM   1949  C   SER A 387      29.716 -26.241  52.303  1.00253.68           C  
ANISOU 1949  C   SER A 387    32624  40394  23369    676  -3726   2922       C  
ATOM   1950  O   SER A 387      30.017 -27.187  51.566  1.00252.69           O  
ANISOU 1950  O   SER A 387    32304  40364  23344   1166  -3542   3132       O  
ATOM   1951  CB  SER A 387      31.220 -25.511  54.177  1.00257.20           C  
ANISOU 1951  CB  SER A 387    32684  41623  23416    277  -4184   2955       C  
ATOM   1952  OG  SER A 387      30.107 -25.619  55.047  1.00258.82           O  
ANISOU 1952  OG  SER A 387    33464  41320  23556    340  -4111   2825       O  
ATOM   1953  N   GLU A 407      28.471 -26.057  52.751  1.00217.26           N  
ANISOU 1953  N   GLU A 407    28560  35226  18762    583  -3640   2735       N  
ATOM   1954  CA  GLU A 407      27.403 -26.971  52.358  1.00209.28           C  
ANISOU 1954  CA  GLU A 407    27925  33621  17971   1019  -3298   2744       C  
ATOM   1955  C   GLU A 407      27.118 -26.893  50.864  1.00206.93           C  
ANISOU 1955  C   GLU A 407    27580  32990  18054    972  -3110   2656       C  
ATOM   1956  O   GLU A 407      26.715 -27.892  50.258  1.00203.19           O  
ANISOU 1956  O   GLU A 407    27231  32186  17785   1418  -2826   2746       O  
ATOM   1957  CB  GLU A 407      26.134 -26.675  53.156  1.00203.72           C  
ANISOU 1957  CB  GLU A 407    27786  32314  17306    863  -3211   2514       C  
ATOM   1958  CG  GLU A 407      26.079 -27.359  54.513  1.00203.43           C  
ANISOU 1958  CG  GLU A 407    27933  32386  16974   1184  -3227   2652       C  
ATOM   1959  CD  GLU A 407      26.100 -28.871  54.404  1.00197.97           C  
ANISOU 1959  CD  GLU A 407    27270  31633  16315   1875  -2974   2917       C  
ATOM   1960  OE1 GLU A 407      25.284 -29.425  53.638  1.00192.63           O  
ANISOU 1960  OE1 GLU A 407    26838  30398  15953   2066  -2673   2869       O  
ATOM   1961  OE2 GLU A 407      26.932 -29.505  55.087  1.00197.79           O  
ANISOU 1961  OE2 GLU A 407    27045  31993  16114   2178  -3045   3132       O  
ATOM   1962  N   LEU A 420      27.318 -25.722  50.256  1.00206.79           N  
ANISOU 1962  N   LEU A 420    27415  33038  18117    425  -3262   2482       N  
ATOM   1963  CA  LEU A 420      27.143 -25.599  48.813  1.00203.15           C  
ANISOU 1963  CA  LEU A 420    26878  32318  17992    371  -3103   2412       C  
ATOM   1964  C   LEU A 420      28.249 -26.335  48.067  1.00203.61           C  
ANISOU 1964  C   LEU A 420    26446  32894  18021    738  -3076   2694       C  
ATOM   1965  O   LEU A 420      27.979 -27.122  47.152  1.00200.90           O  
ANISOU 1965  O   LEU A 420    26156  32264  17914   1110  -2814   2759       O  
ATOM   1966  CB  LEU A 420      27.109 -24.125  48.411  1.00199.58           C  
ANISOU 1966  CB  LEU A 420    26424  31810  17597   -310  -3275   2164       C  
ATOM   1967  CG  LEU A 420      27.257 -23.828  46.918  1.00199.62           C  
ANISOU 1967  CG  LEU A 420    26238  31731  17878   -438  -3184   2123       C  
ATOM   1968  CD1 LEU A 420      25.970 -24.157  46.175  1.00191.40           C  
ANISOU 1968  CD1 LEU A 420    25590  29929  17205   -265  -2874   1974       C  
ATOM   1969  CD2 LEU A 420      27.655 -22.377  46.695  1.00199.33           C  
ANISOU 1969  CD2 LEU A 420    26100  31866  17772  -1123  -3423   1955       C  
ATOM   1970  N   ASP A 421      29.506 -26.093  48.450  1.00220.91           N  
ANISOU 1970  N   ASP A 421    28160  35872  19904    641  -3344   2871       N  
ATOM   1971  CA  ASP A 421      30.627 -26.774  47.812  1.00220.12           C  
ANISOU 1971  CA  ASP A 421    27547  36356  19731   1027  -3321   3169       C  
ATOM   1972  C   ASP A 421      30.656 -28.262  48.130  1.00220.73           C  
ANISOU 1972  C   ASP A 421    27708  36426  19735   1808  -3108   3428       C  
ATOM   1973  O   ASP A 421      31.284 -29.028  47.391  1.00220.26           O  
ANISOU 1973  O   ASP A 421    27381  36578  19729   2253  -2957   3639       O  
ATOM   1974  CB  ASP A 421      31.945 -26.124  48.234  1.00224.61           C  
ANISOU 1974  CB  ASP A 421    27579  37651  20112    692  -3611   3244       C  
ATOM   1975  CG  ASP A 421      31.994 -24.644  47.909  1.00222.21           C  
ANISOU 1975  CG  ASP A 421    27227  37355  19846   -101  -3817   3001       C  
ATOM   1976  OD1 ASP A 421      31.363 -24.231  46.914  1.00219.32           O  
ANISOU 1976  OD1 ASP A 421    27041  36635  19656   -302  -3727   2863       O  
ATOM   1977  OD2 ASP A 421      32.668 -23.893  48.646  1.00225.36           O  
ANISOU 1977  OD2 ASP A 421    27434  38096  20097   -528  -4058   2946       O  
ATOM   1978  N   LYS A 422      29.999 -28.688  49.211  1.00219.82           N  
ANISOU 1978  N   LYS A 422    27986  36007  19527   1980  -3064   3400       N  
ATOM   1979  CA  LYS A 422      29.917 -30.113  49.512  1.00215.00           C  
ANISOU 1979  CA  LYS A 422    27556  35232  18902   2688  -2816   3610       C  
ATOM   1980  C   LYS A 422      29.040 -30.835  48.496  1.00213.28           C  
ANISOU 1980  C   LYS A 422    27702  34367  18966   2994  -2470   3574       C  
ATOM   1981  O   LYS A 422      29.337 -31.971  48.106  1.00213.18           O  
ANISOU 1981  O   LYS A 422    27695  34368  18936   3595  -2256   3802       O  
ATOM   1982  CB  LYS A 422      29.388 -30.315  50.934  1.00210.95           C  
ANISOU 1982  CB  LYS A 422    27398  34514  18238   2726  -2850   3567       C  
ATOM   1983  CG  LYS A 422      28.519 -31.548  51.128  1.00205.88           C  
ANISOU 1983  CG  LYS A 422    27257  33308  17660   3263  -2529   3642       C  
ATOM   1984  CD  LYS A 422      29.363 -32.794  51.342  1.00204.44           C  
ANISOU 1984  CD  LYS A 422    26906  33365  17407   3899  -2394   3930       C  
ATOM   1985  CE  LYS A 422      28.495 -33.999  51.667  1.00202.68           C  
ANISOU 1985  CE  LYS A 422    27237  32535  17236   4363  -2078   3986       C  
ATOM   1986  NZ  LYS A 422      29.293 -35.253  51.752  1.00205.07           N  
ANISOU 1986  NZ  LYS A 422    27428  33012  17478   5011  -1906   4256       N  
ATOM   1987  N   ALA A 423      27.964 -30.187  48.047  1.00186.76           N  
ANISOU 1987  N   ALA A 423    24666  30386  15910   2569  -2392   3267       N  
ATOM   1988  CA  ALA A 423      27.077 -30.800  47.064  1.00177.43           C  
ANISOU 1988  CA  ALA A 423    23824  28536  15055   2759  -2067   3185       C  
ATOM   1989  C   ALA A 423      27.687 -30.769  45.668  1.00178.32           C  
ANISOU 1989  C   ALA A 423    23615  28814  15324   2804  -2006   3241       C  
ATOM   1990  O   ALA A 423      27.760 -31.801  44.992  1.00176.45           O  
ANISOU 1990  O   ALA A 423    23462  28426  15156   3290  -1760   3390       O  
ATOM   1991  CB  ALA A 423      25.718 -30.097  47.073  1.00167.10           C  
ANISOU 1991  CB  ALA A 423    22927  26572  13992   2307  -2013   2857       C  
ATOM   1992  N   ILE A 424      28.133 -29.595  45.219  1.00214.85           N  
ANISOU 1992  N   ILE A 424    27907  33736  19991   2297  -2217   3125       N  
ATOM   1993  CA  ILE A 424      28.725 -29.454  43.893  1.00218.91           C  
ANISOU 1993  CA  ILE A 424    28099  34432  20646   2287  -2168   3171       C  
ATOM   1994  C   ILE A 424      30.158 -29.969  43.924  1.00225.57           C  
ANISOU 1994  C   ILE A 424    28422  36074  21212   2683  -2247   3509       C  
ATOM   1995  O   ILE A 424      30.640 -30.438  44.961  1.00222.61           O  
ANISOU 1995  O   ILE A 424    27955  36085  20543   2968  -2340   3701       O  
ATOM   1996  CB  ILE A 424      28.668 -27.996  43.403  1.00214.63           C  
ANISOU 1996  CB  ILE A 424    27417  33900  20233   1585  -2354   2930       C  
ATOM   1997  CG1 ILE A 424      29.495 -27.090  44.316  1.00220.73           C  
ANISOU 1997  CG1 ILE A 424    27857  35307  20704   1183  -2706   2955       C  
ATOM   1998  CG2 ILE A 424      27.225 -27.517  43.326  1.00208.59           C  
ANISOU 1998  CG2 ILE A 424    27163  32359  19731   1270  -2252   2617       C  
ATOM   1999  CD1 ILE A 424      29.275 -25.611  44.074  1.00219.88           C  
ANISOU 1999  CD1 ILE A 424    27768  35094  20682    447  -2887   2687       C  
ATOM   2000  N   GLY A 425      30.848 -29.883  42.791  1.00250.75           N  
ANISOU 2000  N   GLY A 425    31257  39541  24477   2720  -2205   3595       N  
ATOM   2001  CA  GLY A 425      32.171 -30.449  42.638  1.00254.20           C  
ANISOU 2001  CA  GLY A 425    31185  40732  24668   3168  -2225   3937       C  
ATOM   2002  C   GLY A 425      33.333 -29.485  42.745  1.00254.08           C  
ANISOU 2002  C   GLY A 425    30523  41573  24442   2758  -2545   4023       C  
ATOM   2003  O   GLY A 425      34.464 -29.874  42.431  1.00256.23           O  
ANISOU 2003  O   GLY A 425    30304  42456  24594   3079  -2526   4279       O  
ATOM   2004  N   ARG A 426      33.103 -28.247  43.175  1.00199.45           N  
ANISOU 2004  N   ARG A 426    23607  34650  17524   2033  -2803   3790       N  
ATOM   2005  CA  ARG A 426      34.187 -27.282  43.313  1.00196.23           C  
ANISOU 2005  CA  ARG A 426    22635  34985  16938   1540  -3101   3835       C  
ATOM   2006  C   ARG A 426      33.752 -26.186  44.274  1.00198.79           C  
ANISOU 2006  C   ARG A 426    23174  35164  17195    864  -3363   3577       C  
ATOM   2007  O   ARG A 426      32.578 -26.077  44.638  1.00199.73           O  
ANISOU 2007  O   ARG A 426    23845  34634  17410    765  -3308   3365       O  
ATOM   2008  CB  ARG A 426      34.590 -26.693  41.957  1.00189.04           C  
ANISOU 2008  CB  ARG A 426    21419  34250  16156   1264  -3085   3824       C  
ATOM   2009  CG  ARG A 426      33.430 -26.151  41.139  1.00182.06           C  
ANISOU 2009  CG  ARG A 426    21020  32499  15657    925  -2935   3492       C  
ATOM   2010  CD  ARG A 426      33.926 -25.278  39.998  1.00171.37           C  
ANISOU 2010  CD  ARG A 426    19347  31353  14411    484  -2982   3442       C  
ATOM   2011  NE  ARG A 426      32.830 -24.665  39.257  1.00166.54           N  
ANISOU 2011  NE  ARG A 426    19194  29946  14138    139  -2863   3127       N  
ATOM   2012  CZ  ARG A 426      32.987 -23.781  38.282  1.00160.79           C  
ANISOU 2012  CZ  ARG A 426    18341  29211  13541   -310  -2891   3020       C  
ATOM   2013  NH1 ARG A 426      34.188 -23.380  37.900  1.00148.19           N  
ANISOU 2013  NH1 ARG A 426    16172  28355  11779   -515  -3028   3193       N  
ATOM   2014  NH2 ARG A 426      31.912 -23.285  37.676  1.00158.78           N  
ANISOU 2014  NH2 ARG A 426    18539  28212  13579   -558  -2775   2743       N  
ATOM   2015  N   ASN A 427      34.724 -25.369  44.682  1.00235.58           N  
ANISOU 2015  N   ASN A 427    27406  40371  21731    391  -3608   3577       N  
ATOM   2016  CA  ASN A 427      34.472 -24.246  45.585  1.00234.07           C  
ANISOU 2016  CA  ASN A 427    27416  40063  21457   -285  -3858   3330       C  
ATOM   2017  C   ASN A 427      34.179 -23.004  44.748  1.00235.72           C  
ANISOU 2017  C   ASN A 427    27721  40043  21797   -967  -3935   3093       C  
ATOM   2018  O   ASN A 427      35.039 -22.156  44.501  1.00237.05           O  
ANISOU 2018  O   ASN A 427    27521  40619  21929  -1466  -4086   3082       O  
ATOM   2019  CB  ASN A 427      35.654 -24.033  46.523  1.00235.06           C  
ANISOU 2019  CB  ASN A 427    27091  40857  21364   -448  -4068   3449       C  
ATOM   2020  CG  ASN A 427      35.836 -25.177  47.500  1.00238.33           C  
ANISOU 2020  CG  ASN A 427    27493  41427  21633    188  -4005   3651       C  
ATOM   2021  OD1 ASN A 427      35.363 -25.121  48.635  1.00242.82           O  
ANISOU 2021  OD1 ASN A 427    28397  41772  22093    125  -4099   3548       O  
ATOM   2022  ND2 ASN A 427      36.527 -26.224  47.063  1.00238.06           N  
ANISOU 2022  ND2 ASN A 427    27098  41763  21590    822  -3831   3942       N  
ATOM   2023  N   THR A 428      32.925 -22.905  44.304  1.00232.69           N  
ANISOU 2023  N   THR A 428    27861  38983  21566   -991  -3811   2904       N  
ATOM   2024  CA  THR A 428      32.495 -21.768  43.499  1.00228.27           C  
ANISOU 2024  CA  THR A 428    27493  38051  21189  -1583  -3830   2650       C  
ATOM   2025  C   THR A 428      32.371 -20.484  44.307  1.00229.86           C  
ANISOU 2025  C   THR A 428    27931  38137  21270  -2290  -4067   2402       C  
ATOM   2026  O   THR A 428      32.247 -19.410  43.707  1.00226.63           O  
ANISOU 2026  O   THR A 428    27639  37518  20953  -2841  -4117   2212       O  
ATOM   2027  CB  THR A 428      31.156 -22.074  42.825  1.00221.31           C  
ANISOU 2027  CB  THR A 428    27135  36255  20698  -1339  -3516   2457       C  
ATOM   2028  OG1 THR A 428      30.166 -22.345  43.826  1.00222.67           O  
ANISOU 2028  OG1 THR A 428    27793  35948  20865  -1188  -3466   2334       O  
ATOM   2029  CG2 THR A 428      31.283 -23.278  41.906  1.00215.08           C  
ANISOU 2029  CG2 THR A 428    26178  35454  20089   -686  -3240   2658       C  
ATOM   2030  N   ASN A 429      32.400 -20.570  45.640  1.00229.70           N  
ANISOU 2030  N   ASN A 429    28023  38173  21080  -2261  -4178   2387       N  
ATOM   2031  CA  ASN A 429      32.260 -19.406  46.517  1.00224.90           C  
ANISOU 2031  CA  ASN A 429    27705  37371  20376  -2865  -4362   2140       C  
ATOM   2032  C   ASN A 429      30.948 -18.669  46.253  1.00219.66           C  
ANISOU 2032  C   ASN A 429    27679  35925  19855  -3142  -4279   1835       C  
ATOM   2033  O   ASN A 429      30.875 -17.441  46.334  1.00218.99           O  
ANISOU 2033  O   ASN A 429    27823  35608  19775  -3727  -4376   1610       O  
ATOM   2034  CB  ASN A 429      33.455 -18.459  46.382  1.00224.90           C  
ANISOU 2034  CB  ASN A 429    27292  37861  20298  -3442  -4546   2152       C  
ATOM   2035  CG  ASN A 429      34.711 -19.011  47.029  1.00226.37           C  
ANISOU 2035  CG  ASN A 429    26904  38821  20287  -3254  -4662   2419       C  
ATOM   2036  OD1 ASN A 429      34.935 -18.833  48.226  1.00224.68           O  
ANISOU 2036  OD1 ASN A 429    26748  38735  19884  -3381  -4812   2389       O  
ATOM   2037  ND2 ASN A 429      35.537 -19.685  46.238  1.00229.62           N  
ANISOU 2037  ND2 ASN A 429    26759  39757  20730  -2929  -4583   2685       N  
ATOM   2038  N   GLY A 430      29.902 -19.427  45.934  1.00165.23           N  
ANISOU 2038  N   GLY A 430    21090  28616  13075  -2708  -4078   1835       N  
ATOM   2039  CA  GLY A 430      28.600 -18.859  45.662  1.00155.66           C  
ANISOU 2039  CA  GLY A 430    20457  26577  12109  -2848  -3913   1547       C  
ATOM   2040  C   GLY A 430      28.318 -18.544  44.211  1.00156.16           C  
ANISOU 2040  C   GLY A 430    20525  26311  12497  -2929  -3744   1464       C  
ATOM   2041  O   GLY A 430      27.306 -17.893  43.924  1.00151.52           O  
ANISOU 2041  O   GLY A 430    20392  25090  12087  -3108  -3635   1223       O  
ATOM   2042  N   VAL A 431      29.172 -18.982  43.287  1.00218.42           N  
ANISOU 2042  N   VAL A 431    27922  34618  20451  -2781  -3711   1663       N  
ATOM   2043  CA  VAL A 431      28.979 -18.705  41.868  1.00220.62           C  
ANISOU 2043  CA  VAL A 431    28183  34622  21020  -2853  -3553   1598       C  
ATOM   2044  C   VAL A 431      28.693 -20.007  41.132  1.00216.99           C  
ANISOU 2044  C   VAL A 431    27628  34005  20814  -2184  -3268   1744       C  
ATOM   2045  O   VAL A 431      29.558 -20.539  40.426  1.00215.02           O  
ANISOU 2045  O   VAL A 431    26933  34194  20572  -1965  -3229   1957       O  
ATOM   2046  CB  VAL A 431      30.201 -17.987  41.266  1.00222.25           C  
ANISOU 2046  CB  VAL A 431    27937  35419  21090  -3313  -3739   1688       C  
ATOM   2047  CG1 VAL A 431      29.856 -17.399  39.904  1.00222.29           C  
ANISOU 2047  CG1 VAL A 431    28053  35037  21370  -3515  -3597   1560       C  
ATOM   2048  CG2 VAL A 431      30.698 -16.903  42.210  1.00222.32           C  
ANISOU 2048  CG2 VAL A 431    27991  35726  20754  -3962  -4057   1598       C  
ATOM   2049  N   ILE A 432      27.483 -20.529  41.293  1.00208.87           N  
ANISOU 2049  N   ILE A 432    27028  32358  19976  -1864  -3061   1635       N  
ATOM   2050  CA  ILE A 432      27.084 -21.752  40.608  1.00206.08           C  
ANISOU 2050  CA  ILE A 432    26684  31765  19853  -1282  -2782   1744       C  
ATOM   2051  C   ILE A 432      26.632 -21.409  39.196  1.00202.21           C  
ANISOU 2051  C   ILE A 432    26276  30894  19661  -1386  -2625   1625       C  
ATOM   2052  O   ILE A 432      25.923 -20.420  38.975  1.00201.81           O  
ANISOU 2052  O   ILE A 432    26525  30437  19716  -1767  -2640   1393       O  
ATOM   2053  CB  ILE A 432      25.972 -22.475  41.389  1.00205.61           C  
ANISOU 2053  CB  ILE A 432    27044  31229  19850   -944  -2629   1685       C  
ATOM   2054  CG1 ILE A 432      24.896 -21.481  41.832  1.00202.07           C  
ANISOU 2054  CG1 ILE A 432    27052  30277  19449  -1322  -2660   1403       C  
ATOM   2055  CG2 ILE A 432      26.554 -23.209  42.587  1.00205.70           C  
ANISOU 2055  CG2 ILE A 432    26915  31665  19577   -656  -2726   1882       C  
ATOM   2056  CD1 ILE A 432      23.563 -22.124  42.144  1.00199.34           C  
ANISOU 2056  CD1 ILE A 432    27125  29356  19261  -1016  -2436   1317       C  
ATOM   2057  N   THR A 433      27.048 -22.224  38.231  1.00206.26           N  
ANISOU 2057  N   THR A 433    26540  31537  20291  -1026  -2468   1789       N  
ATOM   2058  CA  THR A 433      26.611 -22.026  36.860  1.00206.71           C  
ANISOU 2058  CA  THR A 433    26682  31235  20625  -1074  -2305   1690       C  
ATOM   2059  C   THR A 433      25.142 -22.421  36.714  1.00202.83           C  
ANISOU 2059  C   THR A 433    26671  30021  20373   -882  -2089   1526       C  
ATOM   2060  O   THR A 433      24.542 -23.041  37.597  1.00201.79           O  
ANISOU 2060  O   THR A 433    26772  29696  20203   -643  -2032   1526       O  
ATOM   2061  CB  THR A 433      27.482 -22.829  35.894  1.00205.44           C  
ANISOU 2061  CB  THR A 433    26143  31422  20492   -717  -2186   1916       C  
ATOM   2062  OG1 THR A 433      27.709 -24.139  36.428  1.00215.39           O  
ANISOU 2062  OG1 THR A 433    27348  32842  21650   -147  -2085   2122       O  
ATOM   2063  CG2 THR A 433      28.819 -22.134  35.680  1.00201.22           C  
ANISOU 2063  CG2 THR A 433    25111  31572  19773  -1039  -2386   2041       C  
ATOM   2064  N   LYS A 434      24.558 -22.049  35.572  1.00190.62           N  
ANISOU 2064  N   LYS A 434    25262  28098  19066  -1001  -1970   1392       N  
ATOM   2065  CA  LYS A 434      23.135 -22.296  35.363  1.00188.55           C  
ANISOU 2065  CA  LYS A 434    25420  27199  19023   -885  -1785   1231       C  
ATOM   2066  C   LYS A 434      22.831 -23.781  35.210  1.00192.02           C  
ANISOU 2066  C   LYS A 434    25933  27485  19539   -357  -1566   1358       C  
ATOM   2067  O   LYS A 434      21.747 -24.231  35.597  1.00192.19           O  
ANISOU 2067  O   LYS A 434    26286  27095  19644   -226  -1443   1276       O  
ATOM   2068  CB  LYS A 434      22.640 -21.516  34.145  1.00186.79           C  
ANISOU 2068  CB  LYS A 434    25300  26662  19010  -1137  -1727   1074       C  
ATOM   2069  CG  LYS A 434      22.642 -20.009  34.348  1.00189.02           C  
ANISOU 2069  CG  LYS A 434    25671  26928  19219  -1662  -1907    911       C  
ATOM   2070  CD  LYS A 434      22.115 -19.276  33.126  1.00185.31           C  
ANISOU 2070  CD  LYS A 434    25337  26125  18948  -1862  -1831    770       C  
ATOM   2071  CE  LYS A 434      22.194 -17.770  33.317  1.00177.77           C  
ANISOU 2071  CE  LYS A 434    24520  25137  17887  -2375  -1998    620       C  
ATOM   2072  NZ  LYS A 434      21.282 -17.298  34.396  1.00176.55           N  
ANISOU 2072  NZ  LYS A 434    24744  24678  17658  -2463  -2033    466       N  
ATOM   2073  N   ASP A 435      23.763 -24.556  34.652  1.00207.67           N  
ANISOU 2073  N   ASP A 435    27634  29792  21480    -52  -1502   1562       N  
ATOM   2074  CA  ASP A 435      23.571 -25.999  34.571  1.00206.06           C  
ANISOU 2074  CA  ASP A 435    27556  29438  21299    467  -1288   1696       C  
ATOM   2075  C   ASP A 435      23.829 -26.693  35.901  1.00202.18           C  
ANISOU 2075  C   ASP A 435    27081  29150  20589    735  -1327   1837       C  
ATOM   2076  O   ASP A 435      23.333 -27.806  36.111  1.00198.90           O  
ANISOU 2076  O   ASP A 435    26921  28466  20187   1106  -1145   1901       O  
ATOM   2077  CB  ASP A 435      24.474 -26.597  33.489  1.00210.08           C  
ANISOU 2077  CB  ASP A 435    27805  30202  21815    755  -1179   1871       C  
ATOM   2078  CG  ASP A 435      25.948 -26.373  33.764  1.00217.13           C  
ANISOU 2078  CG  ASP A 435    28209  31816  22476    769  -1345   2074       C  
ATOM   2079  OD1 ASP A 435      26.275 -25.509  34.603  1.00216.29           O  
ANISOU 2079  OD1 ASP A 435    27955  31997  22227    423  -1577   2039       O  
ATOM   2080  OD2 ASP A 435      26.781 -27.064  33.141  1.00221.17           O  
ANISOU 2080  OD2 ASP A 435    28484  32621  22928   1125  -1242   2275       O  
ATOM   2081  N   GLU A 436      24.592 -26.065  36.799  1.00179.37           N  
ANISOU 2081  N   GLU A 436    23945  26725  17482    539  -1561   1890       N  
ATOM   2082  CA  GLU A 436      24.805 -26.640  38.123  1.00174.61           C  
ANISOU 2082  CA  GLU A 436    23365  26326  16651    771  -1619   2017       C  
ATOM   2083  C   GLU A 436      23.557 -26.508  38.986  1.00166.29           C  
ANISOU 2083  C   GLU A 436    22739  24800  15645    649  -1592   1839       C  
ATOM   2084  O   GLU A 436      23.250 -27.401  39.784  1.00162.19           O  
ANISOU 2084  O   GLU A 436    22414  24175  15035    965  -1501   1926       O  
ATOM   2085  CB  GLU A 436      25.997 -25.967  38.802  1.00176.44           C  
ANISOU 2085  CB  GLU A 436    23192  27233  16614    556  -1898   2123       C  
ATOM   2086  CG  GLU A 436      27.329 -26.657  38.561  1.00179.06           C  
ANISOU 2086  CG  GLU A 436    23081  28183  16772    925  -1904   2419       C  
ATOM   2087  CD  GLU A 436      28.507 -25.821  39.024  1.00182.70           C  
ANISOU 2087  CD  GLU A 436    23075  29363  16980    598  -2199   2510       C  
ATOM   2088  OE1 GLU A 436      28.285 -24.679  39.479  1.00182.20           O  
ANISOU 2088  OE1 GLU A 436    23084  29263  16881     53  -2396   2323       O  
ATOM   2089  OE2 GLU A 436      29.655 -26.306  38.934  1.00182.70           O  
ANISOU 2089  OE2 GLU A 436    22645  29975  16798    884  -2231   2773       O  
ATOM   2090  N   ALA A 437      22.826 -25.400  38.841  1.00165.20           N  
ANISOU 2090  N   ALA A 437    22761  24377  15631    209  -1656   1601       N  
ATOM   2091  CA  ALA A 437      21.613 -25.206  39.627  1.00159.73           C  
ANISOU 2091  CA  ALA A 437    22455  23261  14975    105  -1615   1436       C  
ATOM   2092  C   ALA A 437      20.503 -26.152  39.192  1.00155.81           C  
ANISOU 2092  C   ALA A 437    22266  22257  14679    371  -1345   1407       C  
ATOM   2093  O   ALA A 437      19.670 -26.546  40.016  1.00153.63           O  
ANISOU 2093  O   ALA A 437    22270  21727  14377    463  -1263   1374       O  
ATOM   2094  CB  ALA A 437      21.146 -23.755  39.525  1.00156.58           C  
ANISOU 2094  CB  ALA A 437    22163  22697  14634   -389  -1736   1202       C  
ATOM   2095  N   GLU A 438      20.471 -26.527  37.911  1.00149.98           N  
ANISOU 2095  N   GLU A 438    21486  21374  14125    475  -1204   1420       N  
ATOM   2096  CA  GLU A 438      19.447 -27.454  37.441  1.00145.40           C  
ANISOU 2096  CA  GLU A 438    21206  20326  13713    682   -957   1392       C  
ATOM   2097  C   GLU A 438      19.672 -28.861  37.980  1.00151.44           C  
ANISOU 2097  C   GLU A 438    22082  21110  14347   1129   -822   1590       C  
ATOM   2098  O   GLU A 438      18.705 -29.588  38.231  1.00152.40           O  
ANISOU 2098  O   GLU A 438    22532  20852  14520   1242   -652   1564       O  
ATOM   2099  CB  GLU A 438      19.408 -27.470  35.913  1.00150.19           C  
ANISOU 2099  CB  GLU A 438    21758  20785  14521    662   -855   1351       C  
ATOM   2100  CG  GLU A 438      18.503 -26.410  35.308  1.00145.67           C  
ANISOU 2100  CG  GLU A 438    21282  19928  14138    290   -877   1125       C  
ATOM   2101  CD  GLU A 438      17.032 -26.701  35.537  1.00138.66           C  
ANISOU 2101  CD  GLU A 438    20733  18588  13362    271   -733   1006       C  
ATOM   2102  OE1 GLU A 438      16.642 -27.886  35.469  1.00140.56           O  
ANISOU 2102  OE1 GLU A 438    21153  18628  13624    525   -554   1082       O  
ATOM   2103  OE2 GLU A 438      16.266 -25.746  35.784  1.00134.00           O  
ANISOU 2103  OE2 GLU A 438    20241  17852  12822      3   -791    843       O  
ATOM   2104  N   LYS A 439      20.932 -29.263  38.160  1.00168.02           N  
ANISOU 2104  N   LYS A 439    23920  23658  16261   1390   -888   1799       N  
ATOM   2105  CA  LYS A 439      21.209 -30.568  38.753  1.00166.01           C  
ANISOU 2105  CA  LYS A 439    23796  23439  15843   1859   -761   2006       C  
ATOM   2106  C   LYS A 439      20.822 -30.592  40.226  1.00166.64           C  
ANISOU 2106  C   LYS A 439    24041  23512  15763   1845   -826   2007       C  
ATOM   2107  O   LYS A 439      20.323 -31.606  40.727  1.00170.60           O  
ANISOU 2107  O   LYS A 439    24854  23757  16210   2116   -658   2083       O  
ATOM   2108  CB  LYS A 439      22.685 -30.924  38.577  1.00164.30           C  
ANISOU 2108  CB  LYS A 439    23217  23767  15443   2176   -820   2248       C  
ATOM   2109  N   LEU A 440      21.044 -29.483  40.936  1.00148.24           N  
ANISOU 2109  N   LEU A 440    21539  21447  13338   1519  -1063   1921       N  
ATOM   2110  CA  LEU A 440      20.637 -29.407  42.334  1.00148.22           C  
ANISOU 2110  CA  LEU A 440    21714  21428  13175   1480  -1129   1902       C  
ATOM   2111  C   LEU A 440      19.130 -29.234  42.468  1.00149.71           C  
ANISOU 2111  C   LEU A 440    22273  21078  13531   1284   -998   1702       C  
ATOM   2112  O   LEU A 440      18.537 -29.705  43.445  1.00151.22           O  
ANISOU 2112  O   LEU A 440    22720  21109  13626   1392   -924   1723       O  
ATOM   2113  CB  LEU A 440      21.370 -28.260  43.030  1.00147.77           C  
ANISOU 2113  CB  LEU A 440    21392  21819  12934   1171  -1427   1866       C  
ATOM   2114  CG  LEU A 440      21.185 -28.128  44.543  1.00155.33           C  
ANISOU 2114  CG  LEU A 440    22497  22858  13663   1138  -1533   1864       C  
ATOM   2115  CD1 LEU A 440      21.401 -29.466  45.235  1.00157.83           C  
ANISOU 2115  CD1 LEU A 440    22921  23238  13811   1631  -1414   2093       C  
ATOM   2116  CD2 LEU A 440      22.127 -27.073  45.102  1.00156.60           C  
ANISOU 2116  CD2 LEU A 440    22370  23526  13604    827  -1844   1853       C  
ATOM   2117  N   PHE A 441      18.494 -28.568  41.500  1.00134.43           N  
ANISOU 2117  N   PHE A 441    20360  18885  11832   1008   -964   1520       N  
ATOM   2118  CA  PHE A 441      17.045 -28.404  41.547  1.00129.74           C  
ANISOU 2118  CA  PHE A 441    20072  17833  11392    844   -833   1348       C  
ATOM   2119  C   PHE A 441      16.336 -29.725  41.276  1.00131.52           C  
ANISOU 2119  C   PHE A 441    20562  17710  11701   1102   -571   1421       C  
ATOM   2120  O   PHE A 441      15.280 -30.000  41.858  1.00134.84           O  
ANISOU 2120  O   PHE A 441    21249  17850  12133   1073   -451   1369       O  
ATOM   2121  CB  PHE A 441      16.608 -27.338  40.542  1.00121.17           C  
ANISOU 2121  CB  PHE A 441    18923  16603  10512    513   -870   1155       C  
ATOM   2122  CG  PHE A 441      15.118 -27.194  40.416  1.00115.66           C  
ANISOU 2122  CG  PHE A 441    18486  15482   9976    381   -724    999       C  
ATOM   2123  CD1 PHE A 441      14.333 -26.963  41.533  1.00116.45           C  
ANISOU 2123  CD1 PHE A 441    18786  15474   9985    320   -710    936       C  
ATOM   2124  CD2 PHE A 441      14.503 -27.281  39.178  1.00115.57           C  
ANISOU 2124  CD2 PHE A 441    18505  15216  10192    321   -601    923       C  
ATOM   2125  CE1 PHE A 441      12.962 -26.827  41.419  1.00111.02           C  
ANISOU 2125  CE1 PHE A 441    18294  14458   9431    216   -568    813       C  
ATOM   2126  CE2 PHE A 441      13.133 -27.146  39.057  1.00112.41           C  
ANISOU 2126  CE2 PHE A 441    18297  14494   9921    198   -476    796       C  
ATOM   2127  CZ  PHE A 441      12.362 -26.919  40.179  1.00112.54           C  
ANISOU 2127  CZ  PHE A 441    18481  14433   9846    152   -456    747       C  
ATOM   2128  N   ASN A 442      16.903 -30.558  40.399  1.00157.33           N  
ANISOU 2128  N   ASN A 442    23780  20991  15009   1347   -471   1544       N  
ATOM   2129  CA  ASN A 442      16.325 -31.874  40.153  1.00159.20           C  
ANISOU 2129  CA  ASN A 442    24327  20879  15281   1586   -220   1621       C  
ATOM   2130  C   ASN A 442      16.477 -32.785  41.364  1.00164.67           C  
ANISOU 2130  C   ASN A 442    25213  21607  15748   1881   -157   1789       C  
ATOM   2131  O   ASN A 442      15.594 -33.607  41.635  1.00163.34           O  
ANISOU 2131  O   ASN A 442    25388  21089  15585   1940     35   1801       O  
ATOM   2132  CB  ASN A 442      16.974 -32.517  38.927  1.00162.13           C  
ANISOU 2132  CB  ASN A 442    24639  21250  15713   1803   -124   1714       C  
ATOM   2133  CG  ASN A 442      16.648 -31.785  37.639  1.00162.49           C  
ANISOU 2133  CG  ASN A 442    24567  21181  15992   1525   -142   1549       C  
ATOM   2134  OD1 ASN A 442      15.661 -31.055  37.558  1.00157.88           O  
ANISOU 2134  OD1 ASN A 442    24036  20404  15548   1203   -163   1367       O  
ATOM   2135  ND2 ASN A 442      17.480 -31.979  36.623  1.00164.31           N  
ANISOU 2135  ND2 ASN A 442    24637  21545  16250   1673   -125   1623       N  
ATOM   2136  N   GLN A 443      17.583 -32.653  42.100  1.00201.75           N  
ANISOU 2136  N   GLN A 443    29692  26735  20227   2053   -318   1927       N  
ATOM   2137  CA  GLN A 443      17.794 -33.482  43.281  1.00202.20           C  
ANISOU 2137  CA  GLN A 443    29922  26862  20042   2360   -273   2102       C  
ATOM   2138  C   GLN A 443      16.879 -33.067  44.427  1.00201.38           C  
ANISOU 2138  C   GLN A 443    29999  26628  19890   2144   -300   1995       C  
ATOM   2139  O   GLN A 443      16.424 -33.922  45.196  1.00203.22           O  
ANISOU 2139  O   GLN A 443    30535  26670  20008   2325   -155   2085       O  
ATOM   2140  CB  GLN A 443      19.261 -33.410  43.709  1.00204.76           C  
ANISOU 2140  CB  GLN A 443    29914  27754  20131   2603   -458   2289       C  
ATOM   2141  CG  GLN A 443      19.566 -34.055  45.052  1.00216.21           C  
ANISOU 2141  CG  GLN A 443    31490  29366  21295   2904   -466   2470       C  
ATOM   2142  CD  GLN A 443      19.414 -35.563  45.023  1.00220.63           C  
ANISOU 2142  CD  GLN A 443    32420  29628  21780   3346   -193   2649       C  
ATOM   2143  OE1 GLN A 443      18.525 -36.122  45.664  1.00215.77           O  
ANISOU 2143  OE1 GLN A 443    32187  28659  21135   3359    -42   2639       O  
ATOM   2144  NE2 GLN A 443      20.285 -36.231  44.275  1.00220.94           N  
ANISOU 2144  NE2 GLN A 443    32371  29804  21772   3713   -117   2818       N  
ATOM   2145  N   ASP A 444      16.592 -31.769  44.552  1.00169.80           N  
ANISOU 2145  N   ASP A 444    25847  22711  15960   1769   -468   1807       N  
ATOM   2146  CA  ASP A 444      15.731 -31.302  45.634  1.00167.18           C  
ANISOU 2146  CA  ASP A 444    25694  22265  15563   1586   -484   1703       C  
ATOM   2147  C   ASP A 444      14.295 -31.777  45.447  1.00163.78           C  
ANISOU 2147  C   ASP A 444    25577  21361  15292   1504   -241   1619       C  
ATOM   2148  O   ASP A 444      13.606 -32.085  46.426  1.00164.76           O  
ANISOU 2148  O   ASP A 444    25936  21352  15314   1527   -150   1635       O  
ATOM   2149  CB  ASP A 444      15.783 -29.777  45.724  1.00164.22           C  
ANISOU 2149  CB  ASP A 444    25131  22059  15206   1221   -705   1519       C  
ATOM   2150  CG  ASP A 444      17.116 -29.269  46.235  1.00172.17           C  
ANISOU 2150  CG  ASP A 444    25859  23568  15989   1227   -966   1602       C  
ATOM   2151  OD1 ASP A 444      17.759 -29.980  47.035  1.00173.12           O  
ANISOU 2151  OD1 ASP A 444    25974  23921  15884   1510   -992   1788       O  
ATOM   2152  OD2 ASP A 444      17.521 -28.159  45.831  1.00175.93           O  
ANISOU 2152  OD2 ASP A 444    26126  24220  16501    938  -1146   1486       O  
ATOM   2153  N   VAL A 445      13.826 -31.838  44.199  1.00110.01           N  
ANISOU 2153  N   VAL A 445    18764  14318   8718   1394   -136   1534       N  
ATOM   2154  CA  VAL A 445      12.470 -32.313  43.942  1.00103.94           C  
ANISOU 2154  CA  VAL A 445    18255  13148   8088   1280     84   1464       C  
ATOM   2155  C   VAL A 445      12.357 -33.798  44.266  1.00106.30           C  
ANISOU 2155  C   VAL A 445    18865  13246   8280   1547    293   1637       C  
ATOM   2156  O   VAL A 445      11.336 -34.258  44.793  1.00103.49           O  
ANISOU 2156  O   VAL A 445    18768  12648   7907   1477    453   1631       O  
ATOM   2157  CB  VAL A 445      12.066 -32.012  42.487  1.00 97.48           C  
ANISOU 2157  CB  VAL A 445    17346  12167   7525   1090    123   1338       C  
ATOM   2158  CG1 VAL A 445      10.701 -32.606  42.175  1.00 86.26           C  
ANISOU 2158  CG1 VAL A 445    16170  10380   6224    959    343   1285       C  
ATOM   2159  CG2 VAL A 445      12.065 -30.512  42.238  1.00 96.01           C  
ANISOU 2159  CG2 VAL A 445    16919  12133   7427    824    -63   1167       C  
ATOM   2160  N   ASP A 446      13.403 -34.571  43.963  1.00153.24           N  
ANISOU 2160  N   ASP A 446    24802  19291  14130   1864    306   1803       N  
ATOM   2161  CA  ASP A 446      13.398 -35.987  44.313  1.00153.50           C  
ANISOU 2161  CA  ASP A 446    25187  19117  14018   2164    511   1984       C  
ATOM   2162  C   ASP A 446      13.382 -36.174  45.825  1.00153.69           C  
ANISOU 2162  C   ASP A 446    25345  19240  13809   2290    498   2084       C  
ATOM   2163  O   ASP A 446      12.751 -37.106  46.338  1.00153.07           O  
ANISOU 2163  O   ASP A 446    25632  18885  13644   2367    697   2164       O  
ATOM   2164  CB  ASP A 446      14.610 -36.685  43.694  1.00161.97           C  
ANISOU 2164  CB  ASP A 446    26216  20316  15008   2541    526   2154       C  
ATOM   2165  CG  ASP A 446      14.467 -38.196  43.669  1.00165.44           C  
ANISOU 2165  CG  ASP A 446    27111  20416  15334   2834    790   2314       C  
ATOM   2166  OD1 ASP A 446      13.389 -38.702  44.046  1.00165.77           O  
ANISOU 2166  OD1 ASP A 446    27495  20110  15381   2683    958   2282       O  
ATOM   2167  OD2 ASP A 446      15.434 -38.878  43.271  1.00166.60           O  
ANISOU 2167  OD2 ASP A 446    27288  20643  15370   3219    838   2478       O  
ATOM   2168  N   ALA A 447      14.065 -35.291  46.557  1.00135.92           N  
ANISOU 2168  N   ALA A 447    22823  17383  11439   2288    263   2079       N  
ATOM   2169  CA  ALA A 447      14.042 -35.352  48.014  1.00135.52           C  
ANISOU 2169  CA  ALA A 447    22890  17449  11152   2383    227   2157       C  
ATOM   2170  C   ALA A 447      12.699 -34.919  48.588  1.00129.22           C  
ANISOU 2170  C   ALA A 447    22255  16426  10416   2080    306   2007       C  
ATOM   2171  O   ALA A 447      12.360 -35.320  49.706  1.00128.01           O  
ANISOU 2171  O   ALA A 447    22326  16227  10085   2169    380   2086       O  
ATOM   2172  CB  ALA A 447      15.165 -34.492  48.593  1.00136.84           C  
ANISOU 2172  CB  ALA A 447    22721  18120  11153   2422    -64   2183       C  
ATOM   2173  N   ALA A 448      11.931 -34.119  47.848  1.00129.09           N  
ANISOU 2173  N   ALA A 448    22128  16286  10634   1749    300   1808       N  
ATOM   2174  CA  ALA A 448      10.608 -33.688  48.283  1.00128.25           C  
ANISOU 2174  CA  ALA A 448    22143  15997  10590   1489    394   1676       C  
ATOM   2175  C   ALA A 448       9.518 -34.700  47.961  1.00126.79           C  
ANISOU 2175  C   ALA A 448    22241  15439  10495   1430    672   1706       C  
ATOM   2176  O   ALA A 448       8.552 -34.820  48.723  1.00122.88           O  
ANISOU 2176  O   ALA A 448    21921  14824   9942   1330    800   1698       O  
ATOM   2177  CB  ALA A 448      10.251 -32.344  47.643  1.00125.98           C  
ANISOU 2177  CB  ALA A 448    21616  15764  10486   1191    269   1462       C  
ATOM   2178  N   VAL A 449       9.648 -35.430  46.852  1.00118.14           N  
ANISOU 2178  N   VAL A 449    21204  14164   9520   1473    771   1743       N  
ATOM   2179  CA  VAL A 449       8.639 -36.426  46.511  1.00113.65           C  
ANISOU 2179  CA  VAL A 449    20937  13234   9010   1365   1027   1769       C  
ATOM   2180  C   VAL A 449       8.856 -37.715  47.296  1.00114.20           C  
ANISOU 2180  C   VAL A 449    21381  13156   8854   1629   1189   1975       C  
ATOM   2181  O   VAL A 449       7.893 -38.429  47.597  1.00109.03           O  
ANISOU 2181  O   VAL A 449    21023  12239   8166   1501   1399   2009       O  
ATOM   2182  CB  VAL A 449       8.619 -36.679  44.992  1.00111.71           C  
ANISOU 2182  CB  VAL A 449    20659  12823   8964   1272   1074   1711       C  
ATOM   2183  CG1 VAL A 449       9.863 -37.435  44.548  1.00120.92           C  
ANISOU 2183  CG1 VAL A 449    21897  14004  10043   1619   1068   1856       C  
ATOM   2184  CG2 VAL A 449       7.357 -37.435  44.591  1.00104.39           C  
ANISOU 2184  CG2 VAL A 449    19998  11554   8112   1022   1305   1686       C  
ATOM   2185  N   ARG A 450      10.103 -38.031  47.653  1.00144.46           N  
ANISOU 2185  N   ARG A 450    25207  17169  12512   1997   1100   2125       N  
ATOM   2186  CA  ARG A 450      10.359 -39.198  48.487  1.00142.02           C  
ANISOU 2186  CA  ARG A 450    25267  16740  11956   2300   1248   2335       C  
ATOM   2187  C   ARG A 450      10.119 -38.915  49.963  1.00139.00           C  
ANISOU 2187  C   ARG A 450    24927  16500  11385   2317   1211   2373       C  
ATOM   2188  O   ARG A 450       9.969 -39.860  50.745  1.00143.60           O  
ANISOU 2188  O   ARG A 450    25868  16922  11771   2486   1375   2530       O  
ATOM   2189  CB  ARG A 450      11.786 -39.709  48.269  1.00149.60           C  
ANISOU 2189  CB  ARG A 450    26201  17866  12776   2746   1183   2509       C  
ATOM   2190  CG  ARG A 450      12.865 -38.959  49.033  1.00153.64           C  
ANISOU 2190  CG  ARG A 450    26376  18868  13133   2944    920   2563       C  
ATOM   2191  CD  ARG A 450      14.173 -39.739  49.014  1.00156.11           C  
ANISOU 2191  CD  ARG A 450    26718  19355  13243   3450    911   2796       C  
ATOM   2192  NE  ARG A 450      15.335 -38.887  49.237  1.00160.00           N  
ANISOU 2192  NE  ARG A 450    26754  20390  13649   3567    623   2823       N  
ATOM   2193  CZ  ARG A 450      16.097 -38.396  48.269  1.00159.22           C  
ANISOU 2193  CZ  ARG A 450    26306  20526  13665   3572    489   2787       C  
ATOM   2194  NH1 ARG A 450      15.846 -38.650  46.995  1.00156.35           N  
ANISOU 2194  NH1 ARG A 450    25997  19898  13509   3496    613   2718       N  
ATOM   2195  NH2 ARG A 450      17.137 -37.630  48.587  1.00162.84           N  
ANISOU 2195  NH2 ARG A 450    26352  21509  14011   3633    223   2824       N  
ATOM   2196  N   GLY A 451      10.079 -37.641  50.359  1.00115.60           N  
ANISOU 2196  N   GLY A 451    21645  13817   8460   2147   1009   2235       N  
ATOM   2197  CA  GLY A 451       9.638 -37.308  51.701  1.00114.01           C  
ANISOU 2197  CA  GLY A 451    21519  13707   8091   2109    999   2238       C  
ATOM   2198  C   GLY A 451       8.140 -37.445  51.869  1.00109.18           C  
ANISOU 2198  C   GLY A 451    21096  12827   7562   1817   1215   2164       C  
ATOM   2199  O   GLY A 451       7.655 -37.687  52.978  1.00117.44           O  
ANISOU 2199  O   GLY A 451    22344  13842   8436   1838   1315   2231       O  
ATOM   2200  N   ILE A 452       7.387 -37.294  50.778  1.00103.16           N  
ANISOU 2200  N   ILE A 452    20253  11895   7048   1542   1291   2036       N  
ATOM   2201  CA  ILE A 452       5.947 -37.523  50.827  1.00 99.86           C  
ANISOU 2201  CA  ILE A 452    19977  11263   6701   1250   1505   1989       C  
ATOM   2202  C   ILE A 452       5.652 -39.013  50.935  1.00107.34           C  
ANISOU 2202  C   ILE A 452    21353  11893   7540   1300   1759   2156       C  
ATOM   2203  O   ILE A 452       4.731 -39.430  51.649  1.00107.07           O  
ANISOU 2203  O   ILE A 452    21532  11738   7412   1165   1944   2207       O  
ATOM   2204  CB  ILE A 452       5.269 -36.898  49.592  1.00 99.92           C  
ANISOU 2204  CB  ILE A 452    19746  11233   6987    946   1489   1813       C  
ATOM   2205  CG1 ILE A 452       5.409 -35.375  49.614  1.00100.27           C  
ANISOU 2205  CG1 ILE A 452    19439  11551   7109    882   1269   1648       C  
ATOM   2206  CG2 ILE A 452       3.802 -37.295  49.518  1.00 95.91           C  
ANISOU 2206  CG2 ILE A 452    19361  10540   6540    638   1719   1793       C  
ATOM   2207  CD1 ILE A 452       5.014 -34.709  48.312  1.00 93.47           C  
ANISOU 2207  CD1 ILE A 452    18332  10676   6505    658   1219   1490       C  
ATOM   2208  N   LEU A 453       6.437 -39.841  50.240  1.00111.54           N  
ANISOU 2208  N   LEU A 453    22042  12278   8061   1499   1785   2251       N  
ATOM   2209  CA  LEU A 453       6.189 -41.279  50.237  1.00106.03           C  
ANISOU 2209  CA  LEU A 453    21827  11218   7243   1546   2039   2404       C  
ATOM   2210  C   LEU A 453       6.464 -41.906  51.598  1.00115.13           C  
ANISOU 2210  C   LEU A 453    23206  12371   8168   1804   2104   2560       C  
ATOM   2211  O   LEU A 453       5.770 -42.851  51.992  1.00124.58           O  
ANISOU 2211  O   LEU A 453    24688  13299   9347   1693   2313   2608       O  
ATOM   2212  CB  LEU A 453       7.039 -41.952  49.158  1.00115.16           C  
ANISOU 2212  CB  LEU A 453    23105  12217   8432   1752   2050   2459       C  
ATOM   2213  CG  LEU A 453       6.778 -41.502  47.717  1.00114.18           C  
ANISOU 2213  CG  LEU A 453    22748  12056   8580   1492   1994   2287       C  
ATOM   2214  CD1 LEU A 453       7.694 -42.232  46.746  1.00103.61           C  
ANISOU 2214  CD1 LEU A 453    21575  10561   7230   1753   2024   2361       C  
ATOM   2215  CD2 LEU A 453       5.318 -41.703  47.335  1.00102.68           C  
ANISOU 2215  CD2 LEU A 453    21400  10372   7241   1019   2163   2192       C  
ATOM   2216  N   ARG A 454       7.461 -41.403  52.329  1.00124.14           N  
ANISOU 2216  N   ARG A 454    24166  13827   9173   2119   1908   2614       N  
ATOM   2217  CA  ARG A 454       7.760 -41.941  53.650  1.00116.94           C  
ANISOU 2217  CA  ARG A 454    23383  12960   8088   2364   1934   2737       C  
ATOM   2218  C   ARG A 454       6.824 -41.409  54.727  1.00118.69           C  
ANISOU 2218  C   ARG A 454    23587  13264   8245   2151   1970   2687       C  
ATOM   2219  O   ARG A 454       6.734 -42.010  55.803  1.00129.02           O  
ANISOU 2219  O   ARG A 454    25072  14523   9426   2269   2059   2783       O  
ATOM   2220  CB  ARG A 454       9.209 -41.632  54.037  1.00117.24           C  
ANISOU 2220  CB  ARG A 454    23208  13351   7985   2769   1699   2824       C  
ATOM   2221  CG  ARG A 454       9.507 -40.152  54.218  1.00119.66           C  
ANISOU 2221  CG  ARG A 454    23159  14057   8251   2686   1433   2719       C  
ATOM   2222  CD  ARG A 454      10.944 -39.928  54.665  1.00121.31           C  
ANISOU 2222  CD  ARG A 454    23144  14655   8294   3043   1193   2819       C  
ATOM   2223  NE  ARG A 454      11.885 -40.759  53.924  1.00130.92           N  
ANISOU 2223  NE  ARG A 454    24376  15838   9528   3358   1218   2944       N  
ATOM   2224  CZ  ARG A 454      12.571 -40.353  52.865  1.00139.57           C  
ANISOU 2224  CZ  ARG A 454    25248  17088  10694   3408   1093   2923       C  
ATOM   2225  NH1 ARG A 454      12.451 -39.122  52.394  1.00138.61           N  
ANISOU 2225  NH1 ARG A 454    24824  17153  10689   3126    916   2751       N  
ATOM   2226  NH2 ARG A 454      13.399 -41.202  52.262  1.00134.22           N  
ANISOU 2226  NH2 ARG A 454    24606  16372  10018   3736   1150   3049       N  
ATOM   2227  N   ASN A 455       6.128 -40.306  54.466  1.00119.91           N  
ANISOU 2227  N   ASN A 455    23543  13544   8474   1861   1913   2543       N  
ATOM   2228  CA  ASN A 455       5.221 -39.727  55.447  1.00119.89           C  
ANISOU 2228  CA  ASN A 455    23511  13639   8403   1686   1960   2489       C  
ATOM   2229  C   ASN A 455       3.889 -40.468  55.431  1.00117.81           C  
ANISOU 2229  C   ASN A 455    23452  13099   8210   1386   2245   2504       C  
ATOM   2230  O   ASN A 455       3.282 -40.648  54.371  1.00121.17           O  
ANISOU 2230  O   ASN A 455    23893  13358   8788   1124   2346   2450       O  
ATOM   2231  CB  ASN A 455       5.010 -38.241  55.162  1.00119.50           C  
ANISOU 2231  CB  ASN A 455    23115  13836   8454   1515   1784   2299       C  
ATOM   2232  CG  ASN A 455       4.372 -37.510  56.324  1.00124.76           C  
ANISOU 2232  CG  ASN A 455    23756  14659   8988   1451   1793   2251       C  
ATOM   2233  OD1 ASN A 455       3.190 -37.691  56.613  1.00125.52           O  
ANISOU 2233  OD1 ASN A 455    23952  14651   9090   1247   2006   2253       O  
ATOM   2234  ND2 ASN A 455       5.154 -36.677  57.001  1.00129.32           N  
ANISOU 2234  ND2 ASN A 455    24204  15504   9429   1616   1565   2212       N  
ATOM   2235  N   ALA A 456       3.436 -40.894  56.609  1.00109.72           N  
ANISOU 2235  N   ALA A 456    22577  12046   7065   1403   2368   2579       N  
ATOM   2236  CA  ALA A 456       2.191 -41.643  56.732  1.00111.22           C  
ANISOU 2236  CA  ALA A 456    22955  12012   7291   1104   2637   2611       C  
ATOM   2237  C   ALA A 456       0.952 -40.762  56.656  1.00109.67           C  
ANISOU 2237  C   ALA A 456    22561  11958   7152    767   2711   2507       C  
ATOM   2238  O   ALA A 456      -0.166 -41.290  56.682  1.00110.97           O  
ANISOU 2238  O   ALA A 456    22814  12003   7345    469   2931   2535       O  
ATOM   2239  CB  ALA A 456       2.181 -42.434  58.042  1.00114.60           C  
ANISOU 2239  CB  ALA A 456    23618  12368   7555   1256   2748   2740       C  
ATOM   2240  N   LYS A 457       1.116 -39.443  56.570  1.00108.27           N  
ANISOU 2240  N   LYS A 457    22119  12044   6975    807   2537   2389       N  
ATOM   2241  CA  LYS A 457      -0.002 -38.520  56.431  1.00107.20           C  
ANISOU 2241  CA  LYS A 457    21764  12064   6904    548   2599   2277       C  
ATOM   2242  C   LYS A 457      -0.089 -37.884  55.054  1.00107.68           C  
ANISOU 2242  C   LYS A 457    21498  12165   7249    382   2476   2111       C  
ATOM   2243  O   LYS A 457      -1.189 -37.558  54.605  1.00108.40           O  
ANISOU 2243  O   LYS A 457    21400  12316   7471    107   2576   2038       O  
ATOM   2244  CB  LYS A 457       0.091 -37.412  57.490  1.00112.23           C  
ANISOU 2244  CB  LYS A 457    22274  12966   7403    714   2482   2211       C  
ATOM   2245  CG  LYS A 457      -1.122 -36.494  57.567  1.00114.86           C  
ANISOU 2245  CG  LYS A 457    22365  13470   7806    518   2569   2098       C  
ATOM   2246  CD  LYS A 457      -2.413 -37.275  57.755  1.00115.56           C  
ANISOU 2246  CD  LYS A 457    22559  13485   7862    258   2880   2207       C  
ATOM   2247  CE  LYS A 457      -2.447 -37.973  59.105  1.00119.90           C  
ANISOU 2247  CE  LYS A 457    23356  13991   8208    375   3003   2347       C  
ATOM   2248  NZ  LYS A 457      -3.689 -38.774  59.288  1.00118.76           N  
ANISOU 2248  NZ  LYS A 457    23267  13788   8067     82   3290   2447       N  
ATOM   2249  N   LEU A 458       1.043 -37.712  54.371  1.00101.57           N  
ANISOU 2249  N   LEU A 458    20644  11386   6562    551   2265   2064       N  
ATOM   2250  CA  LEU A 458       1.067 -37.105  53.047  1.00 98.92           C  
ANISOU 2250  CA  LEU A 458    20015  11083   6486    414   2140   1913       C  
ATOM   2251  C   LEU A 458       0.871 -38.116  51.927  1.00 99.02           C  
ANISOU 2251  C   LEU A 458    20157  10840   6625    236   2258   1952       C  
ATOM   2252  O   LEU A 458       0.319 -37.767  50.878  1.00 97.36           O  
ANISOU 2252  O   LEU A 458    19731  10640   6620      1   2246   1839       O  
ATOM   2253  CB  LEU A 458       2.391 -36.369  52.830  1.00 97.43           C  
ANISOU 2253  CB  LEU A 458    19660  11040   6319    655   1857   1844       C  
ATOM   2254  CG  LEU A 458       2.656 -35.143  53.702  1.00 97.08           C  
ANISOU 2254  CG  LEU A 458    19466  11253   6168    770   1688   1756       C  
ATOM   2255  CD1 LEU A 458       4.076 -34.647  53.491  1.00 96.31           C  
ANISOU 2255  CD1 LEU A 458    19240  11299   6056    966   1413   1722       C  
ATOM   2256  CD2 LEU A 458       1.648 -34.045  53.403  1.00 95.51           C  
ANISOU 2256  CD2 LEU A 458    19028  11159   6104    567   1701   1594       C  
ATOM   2257  N   LYS A 459       1.314 -39.356  52.120  1.00103.85           N  
ANISOU 2257  N   LYS A 459    21144  11213   7100    349   2373   2110       N  
ATOM   2258  CA  LYS A 459       1.209 -40.381  51.088  1.00105.78           C  
ANISOU 2258  CA  LYS A 459    21604  11164   7422    195   2494   2148       C  
ATOM   2259  C   LYS A 459      -0.241 -40.774  50.801  1.00107.85           C  
ANISOU 2259  C   LYS A 459    21908  11330   7740   -252   2707   2136       C  
ATOM   2260  O   LYS A 459      -0.593 -40.957  49.628  1.00111.19           O  
ANISOU 2260  O   LYS A 459    22275  11650   8322   -500   2722   2063       O  
ATOM   2261  CB  LYS A 459       2.027 -41.617  51.474  1.00105.57           C  
ANISOU 2261  CB  LYS A 459    22039  10884   7188    468   2590   2335       C  
ATOM   2262  CG  LYS A 459       2.372 -42.517  50.298  1.00105.80           C  
ANISOU 2262  CG  LYS A 459    22281  10616   7304    443   2645   2347       C  
ATOM   2263  CD  LYS A 459       2.817 -43.896  50.759  1.00120.01           C  
ANISOU 2263  CD  LYS A 459    24455  12133   9012    654   2769   2468       C  
ATOM   2264  CE  LYS A 459       1.634 -44.738  51.208  1.00122.10           C  
ANISOU 2264  CE  LYS A 459    24957  12184   9251    313   3000   2494       C  
ATOM   2265  NZ  LYS A 459       0.728 -45.066  50.072  1.00114.04           N  
ANISOU 2265  NZ  LYS A 459    23993  10979   8359   -144   3107   2409       N  
ATOM   2266  N   PRO A 460      -1.110 -40.935  51.812  1.00104.46           N  
ANISOU 2266  N   PRO A 460    21569  10951   7171   -381   2876   2213       N  
ATOM   2267  CA  PRO A 460      -2.513 -41.261  51.495  1.00105.56           C  
ANISOU 2267  CA  PRO A 460    21679  11072   7358   -843   3071   2210       C  
ATOM   2268  C   PRO A 460      -3.204 -40.227  50.622  1.00103.17           C  
ANISOU 2268  C   PRO A 460    20895  11022   7281  -1059   2970   2043       C  
ATOM   2269  O   PRO A 460      -3.987 -40.599  49.739  1.00103.55           O  
ANISOU 2269  O   PRO A 460    20901  11018   7426  -1428   3054   2016       O  
ATOM   2270  CB  PRO A 460      -3.159 -41.360  52.882  1.00107.84           C  
ANISOU 2270  CB  PRO A 460    22071  11461   7443   -857   3238   2322       C  
ATOM   2271  CG  PRO A 460      -2.061 -41.838  53.743  1.00109.05           C  
ANISOU 2271  CG  PRO A 460    22472  11487   7474   -456   3175   2406       C  
ATOM   2272  CD  PRO A 460      -0.855 -41.080  53.259  1.00106.36           C  
ANISOU 2272  CD  PRO A 460    22008  11234   7169   -137   2930   2337       C  
ATOM   2273  N   VAL A 461      -2.944 -38.936  50.839  1.00101.66           N  
ANISOU 2273  N   VAL A 461    20363  11104   7160   -845   2791   1934       N  
ATOM   2274  CA  VAL A 461      -3.593 -37.915  50.022  1.00104.90           C  
ANISOU 2274  CA  VAL A 461    20346  11744   7766  -1003   2704   1786       C  
ATOM   2275  C   VAL A 461      -2.883 -37.708  48.691  1.00101.38           C  
ANISOU 2275  C   VAL A 461    19791  11214   7515   -979   2524   1676       C  
ATOM   2276  O   VAL A 461      -3.499 -37.210  47.741  1.00 99.56           O  
ANISOU 2276  O   VAL A 461    19280  11099   7449  -1183   2486   1575       O  
ATOM   2277  CB  VAL A 461      -3.691 -36.577  50.775  1.00 97.87           C  
ANISOU 2277  CB  VAL A 461    19192  11147   6848   -795   2611   1709       C  
ATOM   2278  CG1 VAL A 461      -4.513 -36.742  52.042  1.00108.02           C  
ANISOU 2278  CG1 VAL A 461    20565  12541   7938   -826   2811   1816       C  
ATOM   2279  CG2 VAL A 461      -2.309 -36.034  51.095  1.00 96.48           C  
ANISOU 2279  CG2 VAL A 461    19060  10961   6636   -434   2389   1663       C  
ATOM   2280  N   TYR A 462      -1.605 -38.079  48.593  1.00116.11           N  
ANISOU 2280  N   TYR A 462    21861  12905   9351   -720   2417   1704       N  
ATOM   2281  CA  TYR A 462      -0.885 -37.919  47.333  1.00111.07           C  
ANISOU 2281  CA  TYR A 462    21124  12196   8883   -681   2262   1613       C  
ATOM   2282  C   TYR A 462      -1.359 -38.927  46.294  1.00118.78           C  
ANISOU 2282  C   TYR A 462    22278  12934   9920   -982   2388   1630       C  
ATOM   2283  O   TYR A 462      -1.448 -38.604  45.103  1.00122.48           O  
ANISOU 2283  O   TYR A 462    22557  13419  10561  -1118   2302   1522       O  
ATOM   2284  CB  TYR A 462       0.620 -38.054  47.571  1.00108.17           C  
ANISOU 2284  CB  TYR A 462    20897  11763   8438   -298   2127   1662       C  
ATOM   2285  CG  TYR A 462       1.456 -37.974  46.313  1.00113.67           C  
ANISOU 2285  CG  TYR A 462    21508  12397   9285   -226   1986   1593       C  
ATOM   2286  CD1 TYR A 462       1.846 -36.747  45.792  1.00113.96           C  
ANISOU 2286  CD1 TYR A 462    21186  12645   9469   -169   1776   1455       C  
ATOM   2287  CD2 TYR A 462       1.863 -39.126  45.651  1.00121.33           C  
ANISOU 2287  CD2 TYR A 462    22787  13081  10230   -208   2077   1669       C  
ATOM   2288  CE1 TYR A 462       2.612 -36.670  44.643  1.00119.45           C  
ANISOU 2288  CE1 TYR A 462    21796  13296  10292   -109   1659   1400       C  
ATOM   2289  CE2 TYR A 462       2.627 -39.058  44.502  1.00122.83           C  
ANISOU 2289  CE2 TYR A 462    22904  13223  10542   -120   1966   1611       C  
ATOM   2290  CZ  TYR A 462       2.999 -37.829  44.003  1.00118.59           C  
ANISOU 2290  CZ  TYR A 462    21971  12927  10160    -76   1755   1480       C  
ATOM   2291  OH  TYR A 462       3.762 -37.760  42.860  1.00117.46           O  
ANISOU 2291  OH  TYR A 462    21749  12751  10131      6   1654   1432       O  
ATOM   2292  N   ASP A 463      -1.673 -40.151  46.723  1.00122.18           N  
ANISOU 2292  N   ASP A 463    23102  13128  10192  -1107   2593   1764       N  
ATOM   2293  CA  ASP A 463      -2.069 -41.192  45.783  1.00119.76           C  
ANISOU 2293  CA  ASP A 463    23057  12546   9900  -1419   2720   1781       C  
ATOM   2294  C   ASP A 463      -3.470 -40.979  45.226  1.00125.56           C  
ANISOU 2294  C   ASP A 463    23539  13440  10729  -1893   2785   1714       C  
ATOM   2295  O   ASP A 463      -3.822 -41.603  44.219  1.00134.73           O  
ANISOU 2295  O   ASP A 463    24826  14433  11932  -2202   2835   1686       O  
ATOM   2296  CB  ASP A 463      -1.984 -42.564  46.453  1.00115.62           C  
ANISOU 2296  CB  ASP A 463    23092  11693   9146  -1424   2932   1951       C  
ATOM   2297  CG  ASP A 463      -0.558 -42.977  46.754  1.00121.46           C  
ANISOU 2297  CG  ASP A 463    24120  12253   9776   -941   2879   2038       C  
ATOM   2298  OD1 ASP A 463       0.367 -42.429  46.119  1.00118.21           O  
ANISOU 2298  OD1 ASP A 463    23512  11919   9482   -685   2692   1962       O  
ATOM   2299  OD2 ASP A 463      -0.362 -43.851  47.625  1.00129.11           O  
ANISOU 2299  OD2 ASP A 463    25464  13033  10560   -807   3015   2175       O  
ATOM   2300  N   SER A 464      -4.274 -40.116  45.848  1.00103.25           N  
ANISOU 2300  N   SER A 464    20363  10950   7919  -1949   2788   1693       N  
ATOM   2301  CA  SER A 464      -5.654 -39.897  45.434  1.00102.24           C  
ANISOU 2301  CA  SER A 464    19945  11051   7849  -2364   2862   1661       C  
ATOM   2302  C   SER A 464      -5.875 -38.507  44.848  1.00108.80           C  
ANISOU 2302  C   SER A 464    20264  12212   8863  -2284   2688   1520       C  
ATOM   2303  O   SER A 464      -7.006 -38.011  44.851  1.00113.23           O  
ANISOU 2303  O   SER A 464    20500  13079   9444  -2487   2742   1511       O  
ATOM   2304  CB  SER A 464      -6.600 -40.129  46.612  1.00112.72           C  
ANISOU 2304  CB  SER A 464    21293  12525   9011  -2513   3061   1780       C  
ATOM   2305  OG  SER A 464      -6.586 -39.025  47.499  1.00116.96           O  
ANISOU 2305  OG  SER A 464    21558  13345   9537  -2208   3001   1758       O  
ATOM   2306  N   LEU A 465      -4.823 -37.872  44.342  1.00123.97           N  
ANISOU 2306  N   LEU A 465    22112  14089  10902  -1985   2490   1423       N  
ATOM   2307  CA  LEU A 465      -4.913 -36.538  43.771  1.00123.60           C  
ANISOU 2307  CA  LEU A 465    21645  14302  11014  -1887   2323   1290       C  
ATOM   2308  C   LEU A 465      -4.640 -36.579  42.274  1.00127.88           C  
ANISOU 2308  C   LEU A 465    22127  14746  11716  -2006   2210   1196       C  
ATOM   2309  O   LEU A 465      -3.998 -37.498  41.758  1.00127.22           O  
ANISOU 2309  O   LEU A 465    22348  14368  11620  -2035   2221   1218       O  
ATOM   2310  CB  LEU A 465      -3.929 -35.579  44.451  1.00123.34           C  
ANISOU 2310  CB  LEU A 465    21556  14335  10972  -1470   2173   1245       C  
ATOM   2311  CG  LEU A 465      -4.415 -34.862  45.711  1.00128.02           C  
ANISOU 2311  CG  LEU A 465    22039  15155  11448  -1333   2228   1271       C  
ATOM   2312  CD1 LEU A 465      -3.372 -33.865  46.196  1.00124.13           C  
ANISOU 2312  CD1 LEU A 465    21513  14709  10942   -975   2045   1200       C  
ATOM   2313  CD2 LEU A 465      -5.744 -34.172  45.456  1.00130.38           C  
ANISOU 2313  CD2 LEU A 465    21991  15750  11797  -1508   2294   1235       C  
ATOM   2314  N   ASP A 466      -5.142 -35.561  41.579  1.00131.69           N  
ANISOU 2314  N   ASP A 466    22231  15476  12331  -2049   2110   1094       N  
ATOM   2315  CA  ASP A 466      -4.876 -35.416  40.158  1.00125.64           C  
ANISOU 2315  CA  ASP A 466    21370  14651  11715  -2130   1985    996       C  
ATOM   2316  C   ASP A 466      -3.425 -35.003  39.930  1.00119.37           C  
ANISOU 2316  C   ASP A 466    20650  13717  10989  -1790   1818    937       C  
ATOM   2317  O   ASP A 466      -2.737 -34.528  40.837  1.00121.50           O  
ANISOU 2317  O   ASP A 466    20944  14017  11202  -1500   1764    951       O  
ATOM   2318  CB  ASP A 466      -5.815 -34.380  39.538  1.00131.38           C  
ANISOU 2318  CB  ASP A 466    21671  15704  12545  -2229   1927    919       C  
ATOM   2319  CG  ASP A 466      -7.267 -34.809  39.583  1.00144.49           C  
ANISOU 2319  CG  ASP A 466    23190  17576  14135  -2596   2079    989       C  
ATOM   2320  OD1 ASP A 466      -7.530 -36.029  39.556  1.00150.84           O  
ANISOU 2320  OD1 ASP A 466    24249  18209  14853  -2898   2202   1062       O  
ATOM   2321  OD2 ASP A 466      -8.146 -33.923  39.647  1.00146.25           O  
ANISOU 2321  OD2 ASP A 466    23053  18145  14372  -2582   2083    979       O  
ATOM   2322  N   ALA A 467      -2.963 -35.190  38.690  1.00109.47           N  
ANISOU 2322  N   ALA A 467    19422  12329   9841  -1844   1735    874       N  
ATOM   2323  CA  ALA A 467      -1.601 -34.795  38.342  1.00104.35           C  
ANISOU 2323  CA  ALA A 467    18799  11593   9258  -1548   1581    827       C  
ATOM   2324  C   ALA A 467      -1.370 -33.309  38.579  1.00106.03           C  
ANISOU 2324  C   ALA A 467    18711  12040   9537  -1345   1430    744       C  
ATOM   2325  O   ALA A 467      -0.267 -32.905  38.966  1.00100.05           O  
ANISOU 2325  O   ALA A 467    17981  11273   8759  -1082   1321    739       O  
ATOM   2326  CB  ALA A 467      -1.306 -35.152  36.886  1.00117.01           C  
ANISOU 2326  CB  ALA A 467    20447  13048  10962  -1659   1532    769       C  
ATOM   2327  N   VAL A 468      -2.394 -32.483  38.355  1.00100.46           N  
ANISOU 2327  N   VAL A 468    17729  11554   8889  -1463   1425    684       N  
ATOM   2328  CA  VAL A 468      -2.269 -31.055  38.625  1.00 95.95           C  
ANISOU 2328  CA  VAL A 468    16940  11167   8348  -1267   1308    606       C  
ATOM   2329  C   VAL A 468      -2.239 -30.799  40.126  1.00 96.27           C  
ANISOU 2329  C   VAL A 468    17058  11278   8243  -1098   1355    656       C  
ATOM   2330  O   VAL A 468      -1.455 -29.977  40.615  1.00 94.11           O  
ANISOU 2330  O   VAL A 468    16785  11034   7937   -881   1237    612       O  
ATOM   2331  CB  VAL A 468      -3.411 -30.283  37.942  1.00 99.69           C  
ANISOU 2331  CB  VAL A 468    17124  11855   8899  -1393   1311    547       C  
ATOM   2332  CG1 VAL A 468      -3.151 -28.785  38.001  1.00103.52           C  
ANISOU 2332  CG1 VAL A 468    17458  12462   9414  -1170   1186    455       C  
ATOM   2333  CG2 VAL A 468      -3.583 -30.751  36.505  1.00102.93           C  
ANISOU 2333  CG2 VAL A 468    17486  12202   9422  -1611   1283    513       C  
ATOM   2334  N   ARG A 469      -3.089 -31.498  40.880  1.00 96.55           N  
ANISOU 2334  N   ARG A 469    17169  11344   8170  -1217   1529    750       N  
ATOM   2335  CA  ARG A 469      -3.138 -31.314  42.325  1.00 94.84           C  
ANISOU 2335  CA  ARG A 469    17042  11195   7797  -1061   1593    805       C  
ATOM   2336  C   ARG A 469      -1.978 -32.003  43.031  1.00 93.93           C  
ANISOU 2336  C   ARG A 469    17211  10899   7581   -900   1566    874       C  
ATOM   2337  O   ARG A 469      -1.568 -31.561  44.111  1.00 94.55           O  
ANISOU 2337  O   ARG A 469    17354  11033   7537   -702   1532    887       O  
ATOM   2338  CB  ARG A 469      -4.473 -31.823  42.871  1.00 93.80           C  
ANISOU 2338  CB  ARG A 469    16877  11188   7575  -1251   1801    896       C  
ATOM   2339  CG  ARG A 469      -5.653 -30.947  42.487  1.00 95.78           C  
ANISOU 2339  CG  ARG A 469    16800  11720   7873  -1320   1834    853       C  
ATOM   2340  CD  ARG A 469      -6.965 -31.708  42.532  1.00 99.33           C  
ANISOU 2340  CD  ARG A 469    17155  12318   8267  -1619   2027    954       C  
ATOM   2341  NE  ARG A 469      -8.104 -30.815  42.362  1.00103.90           N  
ANISOU 2341  NE  ARG A 469    17386  13240   8851  -1616   2072    942       N  
ATOM   2342  CZ  ARG A 469      -9.279 -31.182  41.870  1.00109.30           C  
ANISOU 2342  CZ  ARG A 469    17842  14152   9534  -1902   2176   1002       C  
ATOM   2343  NH1 ARG A 469      -9.508 -32.426  41.481  1.00113.00           N  
ANISOU 2343  NH1 ARG A 469    18424  14513   9998  -2267   2245   1064       N  
ATOM   2344  NH2 ARG A 469     -10.248 -30.277  41.761  1.00109.05           N  
ANISOU 2344  NH2 ARG A 469    17471  14474   9488  -1821   2213   1005       N  
ATOM   2345  N   ARG A 470      -1.442 -33.079  42.449  1.00 83.05           N  
ANISOU 2345  N   ARG A 470    16017   9309   6229   -966   1584    925       N  
ATOM   2346  CA  ARG A 470      -0.264 -33.717  43.029  1.00 83.65           C  
ANISOU 2346  CA  ARG A 470    16348   9237   6198   -753   1555   1006       C  
ATOM   2347  C   ARG A 470       0.938 -32.785  42.985  1.00 82.03           C  
ANISOU 2347  C   ARG A 470    16028   9118   6020   -513   1339    937       C  
ATOM   2348  O   ARG A 470       1.723 -32.726  43.938  1.00 82.68           O  
ANISOU 2348  O   ARG A 470    16207   9238   5968   -304   1280    988       O  
ATOM   2349  CB  ARG A 470       0.047 -35.022  42.298  1.00 84.49           C  
ANISOU 2349  CB  ARG A 470    16702   9085   6315   -838   1635   1073       C  
ATOM   2350  CG  ARG A 470      -0.795 -36.204  42.738  1.00 87.00           C  
ANISOU 2350  CG  ARG A 470    17283   9257   6517  -1044   1858   1184       C  
ATOM   2351  CD  ARG A 470      -0.181 -37.516  42.282  1.00 88.32           C  
ANISOU 2351  CD  ARG A 470    17822   9108   6627  -1030   1938   1266       C  
ATOM   2352  NE  ARG A 470      -1.147 -38.607  42.317  1.00 90.76           N  
ANISOU 2352  NE  ARG A 470    18391   9243   6850  -1348   2149   1340       N  
ATOM   2353  CZ  ARG A 470      -0.839 -39.885  42.142  1.00 92.77           C  
ANISOU 2353  CZ  ARG A 470    19080   9171   6996  -1375   2276   1430       C  
ATOM   2354  NH1 ARG A 470       0.405 -40.271  41.916  1.00 92.68           N  
ANISOU 2354  NH1 ARG A 470    19276   8988   6949  -1053   2226   1471       N  
ATOM   2355  NH2 ARG A 470      -1.805 -40.798  42.197  1.00 95.24           N  
ANISOU 2355  NH2 ARG A 470    19638   9332   7217  -1731   2467   1489       N  
ATOM   2356  N   ALA A 471       1.098 -32.047  41.885  1.00 94.96           N  
ANISOU 2356  N   ALA A 471    17460  10803   7817   -560   1216    826       N  
ATOM   2357  CA  ALA A 471       2.215 -31.117  41.777  1.00100.53           C  
ANISOU 2357  CA  ALA A 471    18051  11602   8544   -390   1012    760       C  
ATOM   2358  C   ALA A 471       2.114 -30.000  42.806  1.00 96.60           C  
ANISOU 2358  C   ALA A 471    17490  11268   7946   -303    943    707       C  
ATOM   2359  O   ALA A 471       3.140 -29.514  43.298  1.00 95.89           O  
ANISOU 2359  O   ALA A 471    17408  11254   7772   -158    795    699       O  
ATOM   2360  CB  ALA A 471       2.281 -30.539  40.364  1.00 90.87           C  
ANISOU 2360  CB  ALA A 471    16639  10383   7503   -485    917    654       C  
ATOM   2361  N   ALA A 472       0.893 -29.584  43.148  1.00 81.59           N  
ANISOU 2361  N   ALA A 472    15531   9439   6032   -391   1050    677       N  
ATOM   2362  CA  ALA A 472       0.723 -28.526  44.138  1.00 80.17           C  
ANISOU 2362  CA  ALA A 472    15344   9387   5730   -286   1012    624       C  
ATOM   2363  C   ALA A 472       1.145 -28.994  45.525  1.00 83.69           C  
ANISOU 2363  C   ALA A 472    15990   9838   5971   -153   1041    717       C  
ATOM   2364  O   ALA A 472       1.686 -28.209  46.312  1.00 82.20           O  
ANISOU 2364  O   ALA A 472    15849   9731   5653    -34    926    674       O  
ATOM   2365  CB  ALA A 472      -0.728 -28.047  44.146  1.00 80.55           C  
ANISOU 2365  CB  ALA A 472    15278   9534   5795   -364   1151    593       C  
ATOM   2366  N   LEU A 473       0.907 -30.270  45.841  1.00 82.71           N  
ANISOU 2366  N   LEU A 473    16012   9619   5796   -183   1192    845       N  
ATOM   2367  CA  LEU A 473       1.329 -30.801  47.134  1.00 84.50           C  
ANISOU 2367  CA  LEU A 473    16450   9841   5815    -38   1226    952       C  
ATOM   2368  C   LEU A 473       2.848 -30.852  47.239  1.00 84.43           C  
ANISOU 2368  C   LEU A 473    16488   9848   5744    136   1039    979       C  
ATOM   2369  O   LEU A 473       3.410 -30.596  48.310  1.00 85.54           O  
ANISOU 2369  O   LEU A 473    16716  10086   5700    280    960   1007       O  
ATOM   2370  CB  LEU A 473       0.724 -32.188  47.354  1.00 86.14           C  
ANISOU 2370  CB  LEU A 473    16842   9912   5977   -125   1444   1091       C  
ATOM   2371  CG  LEU A 473       0.990 -32.844  48.711  1.00 88.31           C  
ANISOU 2371  CG  LEU A 473    17368  10164   6023     23   1520   1222       C  
ATOM   2372  CD1 LEU A 473       0.381 -32.017  49.831  1.00 89.10           C  
ANISOU 2372  CD1 LEU A 473    17449  10421   5984     71   1555   1188       C  
ATOM   2373  CD2 LEU A 473       0.451 -34.268  48.745  1.00 90.06           C  
ANISOU 2373  CD2 LEU A 473    17817  10198   6204    -94   1742   1360       C  
ATOM   2374  N   ILE A 474       3.531 -31.177  46.138  1.00 95.20           N  
ANISOU 2374  N   ILE A 474    17783  11147   7241    128    965    977       N  
ATOM   2375  CA  ILE A 474       4.990 -31.202  46.156  1.00 96.07           C  
ANISOU 2375  CA  ILE A 474    17880  11335   7288    304    789   1019       C  
ATOM   2376  C   ILE A 474       5.553 -29.788  46.171  1.00 94.83           C  
ANISOU 2376  C   ILE A 474    17546  11359   7127    291    571    892       C  
ATOM   2377  O   ILE A 474       6.637 -29.550  46.719  1.00 99.05           O  
ANISOU 2377  O   ILE A 474    18067  12045   7523    411    410    924       O  
ATOM   2378  CB  ILE A 474       5.528 -32.008  44.960  1.00 91.26           C  
ANISOU 2378  CB  ILE A 474    17264  10606   6806    323    803   1067       C  
ATOM   2379  CG1 ILE A 474       4.709 -33.284  44.761  1.00 99.70           C  
ANISOU 2379  CG1 ILE A 474    18551  11441   7891    244   1038   1154       C  
ATOM   2380  CG2 ILE A 474       6.999 -32.343  45.156  1.00101.50           C  
ANISOU 2380  CG2 ILE A 474    18567  12011   7987    567    676   1170       C  
ATOM   2381  CD1 ILE A 474       5.023 -34.016  43.475  1.00100.41           C  
ANISOU 2381  CD1 ILE A 474    18681  11367   8103    222   1075   1172       C  
ATOM   2382  N   ASN A 475       4.842 -28.832  45.568  1.00 90.77           N  
ANISOU 2382  N   ASN A 475    16905  10839   6744    140    561    753       N  
ATOM   2383  CA  ASN A 475       5.264 -27.437  45.646  1.00 87.95           C  
ANISOU 2383  CA  ASN A 475    16457  10605   6354    107    377    626       C  
ATOM   2384  C   ASN A 475       5.293 -26.964  47.094  1.00 93.71           C  
ANISOU 2384  C   ASN A 475    17330  11429   6847    180    341    622       C  
ATOM   2385  O   ASN A 475       6.173 -26.189  47.487  1.00 91.81           O  
ANISOU 2385  O   ASN A 475    17085  11315   6484    182    149    571       O  
ATOM   2386  CB  ASN A 475       4.331 -26.566  44.801  1.00 85.96           C  
ANISOU 2386  CB  ASN A 475    16099  10301   6259    -27    415    495       C  
ATOM   2387  CG  ASN A 475       4.847 -25.145  44.620  1.00 90.60           C  
ANISOU 2387  CG  ASN A 475    16637  10958   6827    -77    231    361       C  
ATOM   2388  OD1 ASN A 475       5.139 -24.443  45.587  1.00 97.30           O  
ANISOU 2388  OD1 ASN A 475    17599  11878   7492    -48    144    320       O  
ATOM   2389  ND2 ASN A 475       4.957 -24.717  43.368  1.00 89.72           N  
ANISOU 2389  ND2 ASN A 475    16386  10813   6889   -169    173    292       N  
ATOM   2390  N   MET A 476       4.345 -27.436  47.906  1.00 87.28           N  
ANISOU 2390  N   MET A 476    16650  10564   5947    219    525    678       N  
ATOM   2391  CA  MET A 476       4.316 -27.061  49.315  1.00 85.03           C  
ANISOU 2391  CA  MET A 476    16530  10359   5419    304    513    681       C  
ATOM   2392  C   MET A 476       5.448 -27.725  50.087  1.00 86.60           C  
ANISOU 2392  C   MET A 476    16814  10652   5439    437    409    801       C  
ATOM   2393  O   MET A 476       6.067 -27.097  50.955  1.00 89.84           O  
ANISOU 2393  O   MET A 476    17293  11196   5648    474    258    770       O  
ATOM   2394  CB  MET A 476       2.961 -27.426  49.919  1.00 85.88           C  
ANISOU 2394  CB  MET A 476    16739  10409   5484    313    760    724       C  
ATOM   2395  CG  MET A 476       1.795 -26.662  49.317  1.00 84.90           C  
ANISOU 2395  CG  MET A 476    16507  10266   5487    224    862    620       C  
ATOM   2396  SD  MET A 476       0.332 -26.655  50.368  1.00 86.68           S  
ANISOU 2396  SD  MET A 476    16832  10533   5569    275   1118    660       S  
ATOM   2397  CE  MET A 476      -0.224 -28.347  50.185  1.00 87.27           C  
ANISOU 2397  CE  MET A 476    16903  10535   5721    179   1327    833       C  
ATOM   2398  N   VAL A 477       5.733 -28.996  49.788  1.00 91.94           N  
ANISOU 2398  N   VAL A 477    17505  11264   6163    516    489    944       N  
ATOM   2399  CA  VAL A 477       6.833 -29.688  50.455  1.00 95.36           C  
ANISOU 2399  CA  VAL A 477    18012  11805   6415    699    401   1084       C  
ATOM   2400  C   VAL A 477       8.169 -29.064  50.075  1.00 98.38           C  
ANISOU 2400  C   VAL A 477    18210  12391   6780    706    136   1050       C  
ATOM   2401  O   VAL A 477       9.105 -29.037  50.884  1.00101.24           O  
ANISOU 2401  O   VAL A 477    18583  12956   6928    816    -14   1118       O  
ATOM   2402  CB  VAL A 477       6.794 -31.191  50.120  1.00 99.40           C  
ANISOU 2402  CB  VAL A 477    18633  12160   6974    807    574   1247       C  
ATOM   2403  CG1 VAL A 477       7.922 -31.931  50.824  1.00101.49           C  
ANISOU 2403  CG1 VAL A 477    18988  12545   7028   1061    500   1416       C  
ATOM   2404  CG2 VAL A 477       5.448 -31.783  50.498  1.00 94.09           C  
ANISOU 2404  CG2 VAL A 477    18139  11306   6305    732    835   1283       C  
ATOM   2405  N   PHE A 478       8.282 -28.546  48.849  1.00106.66           N  
ANISOU 2405  N   PHE A 478    19075  13415   8036    575     72    952       N  
ATOM   2406  CA  PHE A 478       9.518 -27.895  48.428  1.00109.06           C  
ANISOU 2406  CA  PHE A 478    19184  13928   8324    538   -171    920       C  
ATOM   2407  C   PHE A 478       9.786 -26.637  49.243  1.00111.43           C  
ANISOU 2407  C   PHE A 478    19512  14383   8442    418   -354    805       C  
ATOM   2408  O   PHE A 478      10.939 -26.339  49.580  1.00115.05           O  
ANISOU 2408  O   PHE A 478    19875  15094   8743    414   -568    837       O  
ATOM   2409  CB  PHE A 478       9.448 -27.563  46.937  1.00105.13           C  
ANISOU 2409  CB  PHE A 478    18515  13345   8086    407   -176    833       C  
ATOM   2410  CG  PHE A 478      10.781 -27.248  46.320  1.00109.54           C  
ANISOU 2410  CG  PHE A 478    18853  14120   8648    392   -380    850       C  
ATOM   2411  CD1 PHE A 478      11.277 -25.954  46.332  1.00112.32           C  
ANISOU 2411  CD1 PHE A 478    19111  14621   8943    203   -584    728       C  
ATOM   2412  CD2 PHE A 478      11.537 -28.244  45.726  1.00112.61           C  
ANISOU 2412  CD2 PHE A 478    19145  14564   9078    565   -357    995       C  
ATOM   2413  CE1 PHE A 478      12.503 -25.661  45.765  1.00114.80           C  
ANISOU 2413  CE1 PHE A 478    19198  15171   9250    152   -769    756       C  
ATOM   2414  CE2 PHE A 478      12.763 -27.957  45.157  1.00115.67           C  
ANISOU 2414  CE2 PHE A 478    19294  15199   9458    566   -532   1028       C  
ATOM   2415  CZ  PHE A 478      13.247 -26.664  45.176  1.00114.43           C  
ANISOU 2415  CZ  PHE A 478    19003  15223   9251    342   -742    911       C  
ATOM   2416  N   GLN A 479       8.735 -25.889  49.575  1.00103.26           N  
ANISOU 2416  N   GLN A 479    18617  13211   7405    318   -271    676       N  
ATOM   2417  CA  GLN A 479       8.878 -24.625  50.285  1.00 95.69           C  
ANISOU 2417  CA  GLN A 479    17763  12332   6261    196   -420    545       C  
ATOM   2418  C   GLN A 479       8.895 -24.798  51.798  1.00100.66           C  
ANISOU 2418  C   GLN A 479    18595  13048   6602    300   -425    600       C  
ATOM   2419  O   GLN A 479       9.685 -24.142  52.486  1.00109.21           O  
ANISOU 2419  O   GLN A 479    19726  14309   7459    225   -632    560       O  
ATOM   2420  CB  GLN A 479       7.744 -23.674  49.892  1.00 92.78           C  
ANISOU 2420  CB  GLN A 479    17480  11771   6002     90   -313    384       C  
ATOM   2421  CG  GLN A 479       7.923 -22.249  50.387  1.00 94.77           C  
ANISOU 2421  CG  GLN A 479    17892  12044   6072    -48   -461    226       C  
ATOM   2422  CD  GLN A 479       6.713 -21.379  50.106  1.00 92.59           C  
ANISOU 2422  CD  GLN A 479    17745  11568   5866    -67   -315     93       C  
ATOM   2423  OE1 GLN A 479       5.735 -21.830  49.511  1.00 88.20           O  
ANISOU 2423  OE1 GLN A 479    17105  10903   5504      5   -117    122       O  
ATOM   2424  NE2 GLN A 479       6.775 -20.123  50.533  1.00 92.99           N  
ANISOU 2424  NE2 GLN A 479    18015  11580   5738   -163   -410    -50       N  
ATOM   2425  N   MET A 480       8.042 -25.671  52.332  1.00113.60           N  
ANISOU 2425  N   MET A 480    20362  14572   8229    448   -204    692       N  
ATOM   2426  CA  MET A 480       7.864 -25.791  53.773  1.00117.15           C  
ANISOU 2426  CA  MET A 480    21033  15073   8404    551   -171    738       C  
ATOM   2427  C   MET A 480       8.530 -27.019  54.374  1.00118.00           C  
ANISOU 2427  C   MET A 480    21159  15297   8380    746   -172    941       C  
ATOM   2428  O   MET A 480       8.928 -26.981  55.543  1.00125.54           O  
ANISOU 2428  O   MET A 480    22248  16395   9057    820   -259    985       O  
ATOM   2429  CB  MET A 480       6.370 -25.815  54.116  1.00116.18           C  
ANISOU 2429  CB  MET A 480    21069  14763   8312    583     96    708       C  
ATOM   2430  CG  MET A 480       5.676 -24.476  53.932  1.00118.79           C  
ANISOU 2430  CG  MET A 480    21461  15010   8662    470    105    520       C  
ATOM   2431  SD  MET A 480       3.914 -24.551  54.297  1.00128.77           S  
ANISOU 2431  SD  MET A 480    22843  16136   9948    552    437    520       S  
ATOM   2432  CE  MET A 480       3.260 -25.016  52.696  1.00114.74           C  
ANISOU 2432  CE  MET A 480    20800  14254   8541    468    566    534       C  
ATOM   2433  N   GLY A 481       8.661 -28.100  53.617  1.00115.56           N  
ANISOU 2433  N   GLY A 481    20747  14921   8238    843    -74   1067       N  
ATOM   2434  CA  GLY A 481       9.223 -29.333  54.127  1.00117.91           C  
ANISOU 2434  CA  GLY A 481    21112  15285   8404   1075    -36   1274       C  
ATOM   2435  C   GLY A 481       8.154 -30.376  54.406  1.00119.55           C  
ANISOU 2435  C   GLY A 481    21529  15253   8642   1161    261   1374       C  
ATOM   2436  O   GLY A 481       6.952 -30.099  54.442  1.00118.80           O  
ANISOU 2436  O   GLY A 481    21512  15001   8626   1041    430   1290       O  
ATOM   2437  N   GLU A 482       8.622 -31.609  54.611  1.00117.73           N  
ANISOU 2437  N   GLU A 482    21397  15008   8326   1377    332   1569       N  
ATOM   2438  CA  GLU A 482       7.705 -32.726  54.816  1.00116.64           C  
ANISOU 2438  CA  GLU A 482    21496  14619   8201   1432    620   1683       C  
ATOM   2439  C   GLU A 482       6.931 -32.576  56.120  1.00116.70           C  
ANISOU 2439  C   GLU A 482    21713  14619   8010   1431    728   1688       C  
ATOM   2440  O   GLU A 482       5.709 -32.763  56.153  1.00116.88           O  
ANISOU 2440  O   GLU A 482    21836  14465   8108   1311    956   1668       O  
ATOM   2441  CB  GLU A 482       8.478 -34.046  54.796  1.00116.84           C  
ANISOU 2441  CB  GLU A 482    21646  14612   8137   1697    671   1899       C  
ATOM   2442  CG  GLU A 482       7.703 -35.224  55.364  1.00121.17           C  
ANISOU 2442  CG  GLU A 482    22532  14914   8594   1772    952   2045       C  
ATOM   2443  CD  GLU A 482       8.583 -36.430  55.635  1.00119.06           C  
ANISOU 2443  CD  GLU A 482    22458  14630   8149   2104    988   2273       C  
ATOM   2444  OE1 GLU A 482       9.707 -36.484  55.094  1.00123.25           O  
ANISOU 2444  OE1 GLU A 482    22825  15319   8684   2277    829   2324       O  
ATOM   2445  OE2 GLU A 482       8.146 -37.326  56.387  1.00112.87           O  
ANISOU 2445  OE2 GLU A 482    21996  13682   7207   2204   1186   2414       O  
ATOM   2446  N   THR A 483       7.625 -32.233  57.208  1.00115.47           N  
ANISOU 2446  N   THR A 483    21613  14679   7583   1556    566   1719       N  
ATOM   2447  CA  THR A 483       6.963 -32.132  58.504  1.00118.14           C  
ANISOU 2447  CA  THR A 483    22177  15013   7697   1585    671   1734       C  
ATOM   2448  C   THR A 483       6.024 -30.935  58.573  1.00109.06           C  
ANISOU 2448  C   THR A 483    20996  13839   6603   1385    700   1535       C  
ATOM   2449  O   THR A 483       5.004 -30.991  59.269  1.00107.76           O  
ANISOU 2449  O   THR A 483    20998  13590   6356   1373    902   1543       O  
ATOM   2450  CB  THR A 483       8.001 -32.047  59.624  1.00123.46           C  
ANISOU 2450  CB  THR A 483    22924  15944   8042   1766    467   1814       C  
ATOM   2451  OG1 THR A 483       8.869 -30.931  59.389  1.00131.44           O  
ANISOU 2451  OG1 THR A 483    23720  17191   9032   1661    165   1680       O  
ATOM   2452  CG2 THR A 483       8.828 -33.323  59.684  1.00123.16           C  
ANISOU 2452  CG2 THR A 483    22953  15936   7907   2039    481   2048       C  
ATOM   2453  N   GLY A 484       6.345 -29.851  57.865  1.00100.13           N  
ANISOU 2453  N   GLY A 484    19669  12783   5594   1243    515   1366       N  
ATOM   2454  CA  GLY A 484       5.510 -28.662  57.938  1.00 99.36           C  
ANISOU 2454  CA  GLY A 484    19585  12650   5516   1101    545   1182       C  
ATOM   2455  C   GLY A 484       4.150 -28.861  57.295  1.00 98.50           C  
ANISOU 2455  C   GLY A 484    19434  12359   5633   1010    813   1160       C  
ATOM   2456  O   GLY A 484       3.118 -28.518  57.877  1.00 98.58           O  
ANISOU 2456  O   GLY A 484    19552  12338   5567   1005    982   1124       O  
ATOM   2457  N   VAL A 485       4.129 -29.421  56.083  1.00103.18           N  
ANISOU 2457  N   VAL A 485    19861  12854   6487    938    855   1189       N  
ATOM   2458  CA  VAL A 485       2.864 -29.597  55.377  1.00104.33           C  
ANISOU 2458  CA  VAL A 485    19931  12868   6841    811   1083   1167       C  
ATOM   2459  C   VAL A 485       2.067 -30.754  55.970  1.00102.87           C  
ANISOU 2459  C   VAL A 485    19912  12591   6584    835   1349   1327       C  
ATOM   2460  O   VAL A 485       0.830 -30.755  55.921  1.00102.13           O  
ANISOU 2460  O   VAL A 485    19791  12464   6549    731   1561   1321       O  
ATOM   2461  CB  VAL A 485       3.123 -29.787  53.870  1.00 97.32           C  
ANISOU 2461  CB  VAL A 485    18835  11906   6236    702   1027   1135       C  
ATOM   2462  CG1 VAL A 485       3.933 -31.044  53.627  1.00108.93           C  
ANISOU 2462  CG1 VAL A 485    20364  13313   7713    794   1021   1289       C  
ATOM   2463  CG2 VAL A 485       1.812 -29.824  53.094  1.00 95.56           C  
ANISOU 2463  CG2 VAL A 485    18503  11594   6213    542   1227   1097       C  
ATOM   2464  N   ALA A 486       2.748 -31.744  56.554  1.00116.33           N  
ANISOU 2464  N   ALA A 486    21791  14269   8140    973   1349   1483       N  
ATOM   2465  CA  ALA A 486       2.047 -32.849  57.198  1.00111.35           C  
ANISOU 2465  CA  ALA A 486    21376  13528   7405    987   1606   1645       C  
ATOM   2466  C   ALA A 486       1.229 -32.389  58.398  1.00123.68           C  
ANISOU 2466  C   ALA A 486    23056  15172   8765   1014   1734   1637       C  
ATOM   2467  O   ALA A 486       0.311 -33.101  58.820  1.00124.36           O  
ANISOU 2467  O   ALA A 486    23266  15187   8797    957   1989   1746       O  
ATOM   2468  CB  ALA A 486       3.042 -33.929  57.623  1.00112.38           C  
ANISOU 2468  CB  ALA A 486    21709  13610   7382   1184   1570   1820       C  
ATOM   2469  N   GLY A 487       1.542 -31.221  58.957  1.00108.56           N  
ANISOU 2469  N   GLY A 487    21126  13401   6719   1088   1570   1512       N  
ATOM   2470  CA  GLY A 487       0.738 -30.647  60.017  1.00103.15           C  
ANISOU 2470  CA  GLY A 487    20566  12790   5838   1132   1697   1483       C  
ATOM   2471  C   GLY A 487      -0.545 -29.991  59.567  1.00102.35           C  
ANISOU 2471  C   GLY A 487    20313  12703   5872   1016   1867   1389       C  
ATOM   2472  O   GLY A 487      -1.362 -29.618  60.414  1.00103.92           O  
ANISOU 2472  O   GLY A 487    20607  12970   5907   1075   2028   1389       O  
ATOM   2473  N   PHE A 488      -0.750 -29.850  58.258  1.00117.80           N  
ANISOU 2473  N   PHE A 488    22031  14618   8108    874   1843   1320       N  
ATOM   2474  CA  PHE A 488      -2.000 -29.321  57.729  1.00117.61           C  
ANISOU 2474  CA  PHE A 488    21825  14645   8217    777   2009   1257       C  
ATOM   2475  C   PHE A 488      -3.075 -30.398  57.745  1.00117.49           C  
ANISOU 2475  C   PHE A 488    21785  14617   8238    645   2298   1411       C  
ATOM   2476  O   PHE A 488      -3.691 -30.676  56.713  1.00120.62           O  
ANISOU 2476  O   PHE A 488    21976  15005   8849    463   2377   1414       O  
ATOM   2477  CB  PHE A 488      -1.799 -28.796  56.309  1.00114.53           C  
ANISOU 2477  CB  PHE A 488    21194  14227   8095    668   1867   1135       C  
ATOM   2478  CG  PHE A 488      -1.080 -27.473  56.241  1.00112.35           C  
ANISOU 2478  CG  PHE A 488    20927  13982   7779    748   1630    964       C  
ATOM   2479  CD1 PHE A 488       0.267 -27.385  56.559  1.00111.89           C  
ANISOU 2479  CD1 PHE A 488    20980  13917   7615    804   1385    943       C  
ATOM   2480  CD2 PHE A 488      -1.749 -26.322  55.852  1.00114.33           C  
ANISOU 2480  CD2 PHE A 488    21084  14277   8079    761   1655    835       C  
ATOM   2481  CE1 PHE A 488       0.931 -26.179  56.487  1.00115.02           C  
ANISOU 2481  CE1 PHE A 488    21400  14345   7957    813   1164    786       C  
ATOM   2482  CE2 PHE A 488      -1.087 -25.113  55.782  1.00113.66           C  
ANISOU 2482  CE2 PHE A 488    21070  14179   7937    805   1447    676       C  
ATOM   2483  CZ  PHE A 488       0.254 -25.044  56.100  1.00113.38           C  
ANISOU 2483  CZ  PHE A 488    21153  14130   7798    802   1199    648       C  
ATOM   2484  N   THR A 489      -3.325 -30.985  58.921  1.00111.49           N  
ANISOU 2484  N   THR A 489    21240  13869   7252    714   2455   1539       N  
ATOM   2485  CA  THR A 489      -4.208 -32.144  59.003  1.00116.49           C  
ANISOU 2485  CA  THR A 489    21901  14471   7890    549   2724   1705       C  
ATOM   2486  C   THR A 489      -5.633 -31.810  58.580  1.00119.63           C  
ANISOU 2486  C   THR A 489    22037  15032   8385    399   2931   1696       C  
ATOM   2487  O   THR A 489      -6.321 -32.660  58.001  1.00124.95           O  
ANISOU 2487  O   THR A 489    22611  15691   9173    150   3087   1789       O  
ATOM   2488  CB  THR A 489      -4.202 -32.711  60.421  1.00120.75           C  
ANISOU 2488  CB  THR A 489    22737  15003   8141    669   2856   1844       C  
ATOM   2489  OG1 THR A 489      -4.537 -31.675  61.352  1.00132.43           O  
ANISOU 2489  OG1 THR A 489    24253  16639   9424    847   2882   1774       O  
ATOM   2490  CG2 THR A 489      -2.830 -33.266  60.766  1.00118.49           C  
ANISOU 2490  CG2 THR A 489    22690  14580   7752    815   2669   1896       C  
ATOM   2491  N   ASN A 490      -6.100 -30.593  58.867  1.00116.94           N  
ANISOU 2491  N   ASN A 490    21595  14860   7977    549   2939   1592       N  
ATOM   2492  CA  ASN A 490      -7.448 -30.212  58.457  1.00121.05           C  
ANISOU 2492  CA  ASN A 490    21832  15592   8570    464   3136   1599       C  
ATOM   2493  C   ASN A 490      -7.545 -30.070  56.943  1.00123.53           C  
ANISOU 2493  C   ASN A 490    21861  15903   9173    293   3033   1521       C  
ATOM   2494  O   ASN A 490      -8.512 -30.538  56.331  1.00129.92           O  
ANISOU 2494  O   ASN A 490    22438  16836  10091     70   3190   1596       O  
ATOM   2495  CB  ASN A 490      -7.864 -28.915  59.149  1.00131.92           C  
ANISOU 2495  CB  ASN A 490    23222  17128   9773    734   3180   1512       C  
ATOM   2496  CG  ASN A 490      -7.827 -29.022  60.662  1.00135.08           C  
ANISOU 2496  CG  ASN A 490    23917  17542   9865    906   3291   1584       C  
ATOM   2497  OD1 ASN A 490      -8.273 -30.015  61.235  1.00137.84           O  
ANISOU 2497  OD1 ASN A 490    24334  17918  10120    801   3490   1750       O  
ATOM   2498  ND2 ASN A 490      -7.297 -27.995  61.316  1.00131.97           N  
ANISOU 2498  ND2 ASN A 490    23726  17121   9294   1154   3166   1460       N  
ATOM   2499  N   SER A 491      -6.551 -29.431  56.320  1.00111.97           N  
ANISOU 2499  N   SER A 491    20405  14316   7821    374   2768   1376       N  
ATOM   2500  CA  SER A 491      -6.572 -29.273  54.870  1.00102.10           C  
ANISOU 2500  CA  SER A 491    18905  13052   6837    226   2662   1299       C  
ATOM   2501  C   SER A 491      -6.245 -30.578  54.154  1.00 99.73           C  
ANISOU 2501  C   SER A 491    18620  12590   6681    -23   2650   1382       C  
ATOM   2502  O   SER A 491      -6.786 -30.840  53.074  1.00108.02           O  
ANISOU 2502  O   SER A 491    19453  13677   7914   -237   2683   1382       O  
ATOM   2503  CB  SER A 491      -5.595 -28.178  54.444  1.00 96.89           C  
ANISOU 2503  CB  SER A 491    18269  12310   6235    375   2394   1125       C  
ATOM   2504  OG  SER A 491      -5.835 -26.975  55.153  1.00107.28           O  
ANISOU 2504  OG  SER A 491    19662  13720   7380    605   2408   1041       O  
ATOM   2505  N   LEU A 492      -5.367 -31.401  54.733  1.00105.23           N  
ANISOU 2505  N   LEU A 492    19594  13108   7281     13   2607   1456       N  
ATOM   2506  CA  LEU A 492      -5.008 -32.663  54.093  1.00103.93           C  
ANISOU 2506  CA  LEU A 492    19521  12748   7219   -177   2615   1541       C  
ATOM   2507  C   LEU A 492      -6.205 -33.600  54.010  1.00106.72           C  
ANISOU 2507  C   LEU A 492    19837  13142   7570   -466   2877   1671       C  
ATOM   2508  O   LEU A 492      -6.397 -34.286  52.999  1.00110.87           O  
ANISOU 2508  O   LEU A 492    20307  13575   8245   -720   2898   1689       O  
ATOM   2509  CB  LEU A 492      -3.856 -33.328  54.846  1.00 99.40           C  
ANISOU 2509  CB  LEU A 492    19272  11999   6496    -15   2537   1617       C  
ATOM   2510  CG  LEU A 492      -2.464 -32.737  54.608  1.00103.30           C  
ANISOU 2510  CG  LEU A 492    19779  12447   7022    183   2247   1514       C  
ATOM   2511  CD1 LEU A 492      -1.434 -33.423  55.492  1.00100.70           C  
ANISOU 2511  CD1 LEU A 492    19741  12022   6500    370   2190   1623       C  
ATOM   2512  CD2 LEU A 492      -2.073 -32.835  53.140  1.00 98.07           C  
ANISOU 2512  CD2 LEU A 492    18960  11692   6609     64   2125   1446       C  
ATOM   2513  N   ARG A 493      -7.026 -33.642  55.061  1.00125.82           N  
ANISOU 2513  N   ARG A 493    22292  15708   9804   -453   3083   1765       N  
ATOM   2514  CA  ARG A 493      -8.231 -34.462  55.011  1.00129.41           C  
ANISOU 2514  CA  ARG A 493    22673  16258  10238   -770   3340   1897       C  
ATOM   2515  C   ARG A 493      -9.261 -33.866  54.061  1.00131.31           C  
ANISOU 2515  C   ARG A 493    22497  16762  10632   -937   3373   1840       C  
ATOM   2516  O   ARG A 493      -9.983 -34.602  53.380  1.00136.41           O  
ANISOU 2516  O   ARG A 493    23027  17449  11352  -1291   3482   1907       O  
ATOM   2517  CB  ARG A 493      -8.821 -34.624  56.411  1.00130.70           C  
ANISOU 2517  CB  ARG A 493    22967  16544  10149   -699   3560   2024       C  
ATOM   2518  CG  ARG A 493      -9.852 -35.736  56.515  1.00138.53           C  
ANISOU 2518  CG  ARG A 493    23976  17583  11076  -1066   3831   2195       C  
ATOM   2519  CD  ARG A 493     -10.849 -35.466  57.628  1.00142.20           C  
ANISOU 2519  CD  ARG A 493    24362  18335  11334  -1014   4071   2296       C  
ATOM   2520  NE  ARG A 493     -11.796 -34.419  57.264  1.00152.88           N  
ANISOU 2520  NE  ARG A 493    25281  20060  12748   -973   4112   2237       N  
ATOM   2521  CZ  ARG A 493     -11.800 -33.199  57.785  1.00155.35           C  
ANISOU 2521  CZ  ARG A 493    25510  20534  12981   -608   4074   2151       C  
ATOM   2522  NH1 ARG A 493     -10.921 -32.838  58.706  1.00151.87           N  
ANISOU 2522  NH1 ARG A 493    25373  19935  12396   -293   3979   2102       N  
ATOM   2523  NH2 ARG A 493     -12.708 -32.320  57.371  1.00154.78           N  
ANISOU 2523  NH2 ARG A 493    25059  20794  12955   -554   4133   2116       N  
ATOM   2524  N   MET A 494      -9.342 -32.533  54.000  1.00124.42           N  
ANISOU 2524  N   MET A 494    21415  16071   9788   -690   3279   1720       N  
ATOM   2525  CA  MET A 494     -10.260 -31.891  53.065  1.00123.30           C  
ANISOU 2525  CA  MET A 494    20878  16192   9780   -784   3298   1671       C  
ATOM   2526  C   MET A 494      -9.883 -32.204  51.623  1.00125.79           C  
ANISOU 2526  C   MET A 494    21098  16366  10329   -998   3137   1599       C  
ATOM   2527  O   MET A 494     -10.759 -32.379  50.768  1.00127.37           O  
ANISOU 2527  O   MET A 494    21020  16748  10627  -1258   3200   1625       O  
ATOM   2528  CB  MET A 494     -10.279 -30.380  53.298  1.00124.11           C  
ANISOU 2528  CB  MET A 494    20868  16448   9842   -425   3226   1553       C  
ATOM   2529  CG  MET A 494     -11.103 -29.940  54.497  1.00134.22           C  
ANISOU 2529  CG  MET A 494    22137  17972  10890   -232   3443   1630       C  
ATOM   2530  SD  MET A 494     -10.946 -28.174  54.837  1.00138.32           S  
ANISOU 2530  SD  MET A 494    22673  18566  11315    226   3355   1476       S  
ATOM   2531  CE  MET A 494     -12.103 -27.983  56.190  1.00137.44           C  
ANISOU 2531  CE  MET A 494    22546  18761  10914    410   3678   1610       C  
ATOM   2532  N   LEU A 495      -8.582 -32.274  51.332  1.00104.21           N  
ANISOU 2532  N   LEU A 495    18583  13339   7673   -891   2929   1515       N  
ATOM   2533  CA  LEU A 495      -8.148 -32.674  49.997  1.00105.66           C  
ANISOU 2533  CA  LEU A 495    18723  13364   8060  -1079   2793   1457       C  
ATOM   2534  C   LEU A 495      -8.497 -34.131  49.722  1.00109.26           C  
ANISOU 2534  C   LEU A 495    19317  13687   8509  -1444   2932   1578       C  
ATOM   2535  O   LEU A 495      -8.918 -34.476  48.612  1.00111.66           O  
ANISOU 2535  O   LEU A 495    19476  14007   8944  -1727   2923   1561       O  
ATOM   2536  CB  LEU A 495      -6.646 -32.438  49.837  1.00102.15           C  
ANISOU 2536  CB  LEU A 495    18472  12671   7670   -858   2557   1361       C  
ATOM   2537  CG  LEU A 495      -6.214 -30.997  49.553  1.00 96.04           C  
ANISOU 2537  CG  LEU A 495    17548  11980   6963   -615   2369   1207       C  
ATOM   2538  CD1 LEU A 495      -4.698 -30.877  49.551  1.00 91.11           C  
ANISOU 2538  CD1 LEU A 495    17114  11151   6353   -442   2147   1141       C  
ATOM   2539  CD2 LEU A 495      -6.794 -30.518  48.232  1.00 91.61           C  
ANISOU 2539  CD2 LEU A 495    16679  11538   6590   -749   2324   1131       C  
ATOM   2540  N   GLN A 496      -8.332 -35.001  50.722  1.00132.46           N  
ANISOU 2540  N   GLN A 496    22568  16482  11277  -1453   3062   1700       N  
ATOM   2541  CA  GLN A 496      -8.729 -36.395  50.556  1.00134.01           C  
ANISOU 2541  CA  GLN A 496    22966  16523  11428  -1819   3224   1823       C  
ATOM   2542  C   GLN A 496     -10.244 -36.539  50.495  1.00143.69           C  
ANISOU 2542  C   GLN A 496    23917  18061  12616  -2165   3425   1905       C  
ATOM   2543  O   GLN A 496     -10.751 -37.502  49.910  1.00151.47           O  
ANISOU 2543  O   GLN A 496    24961  18980  13611  -2579   3519   1968       O  
ATOM   2544  CB  GLN A 496      -8.157 -37.247  51.689  1.00130.59           C  
ANISOU 2544  CB  GLN A 496    22968  15852  10800  -1708   3321   1945       C  
ATOM   2545  CG  GLN A 496      -7.819 -38.672  51.279  1.00137.10           C  
ANISOU 2545  CG  GLN A 496    24172  16318  11600  -1945   3390   2028       C  
ATOM   2546  CD  GLN A 496      -6.887 -39.363  52.258  1.00140.08           C  
ANISOU 2546  CD  GLN A 496    25002  16423  11799  -1696   3422   2131       C  
ATOM   2547  OE1 GLN A 496      -6.777 -38.963  53.418  1.00140.07           O  
ANISOU 2547  OE1 GLN A 496    25037  16532  11653  -1446   3449   2172       O  
ATOM   2548  NE2 GLN A 496      -6.212 -40.408  51.793  1.00137.88           N  
ANISOU 2548  NE2 GLN A 496    25091  15787  11509  -1744   3424   2177       N  
ATOM   2549  N   GLN A 497     -10.978 -35.597  51.087  1.00153.03           N  
ANISOU 2549  N   GLN A 497    24810  19599  13736  -2007   3495   1910       N  
ATOM   2550  CA  GLN A 497     -12.433 -35.577  51.004  1.00156.29           C  
ANISOU 2550  CA  GLN A 497    24871  20407  14105  -2283   3679   1998       C  
ATOM   2551  C   GLN A 497     -12.938 -35.021  49.679  1.00153.31           C  
ANISOU 2551  C   GLN A 497    24091  20255  13906  -2417   3570   1911       C  
ATOM   2552  O   GLN A 497     -14.152 -34.862  49.520  1.00154.86           O  
ANISOU 2552  O   GLN A 497    23917  20858  14066  -2610   3697   1985       O  
ATOM   2553  CB  GLN A 497     -13.014 -34.756  52.160  1.00155.70           C  
ANISOU 2553  CB  GLN A 497    24647  20643  13870  -1996   3816   2049       C  
ATOM   2554  CG  GLN A 497     -13.042 -35.481  53.498  1.00160.78           C  
ANISOU 2554  CG  GLN A 497    25604  21195  14290  -2000   4010   2191       C  
ATOM   2555  CD  GLN A 497     -13.947 -36.695  53.491  1.00169.48           C  
ANISOU 2555  CD  GLN A 497    26722  22365  15306  -2508   4232   2357       C  
ATOM   2556  OE1 GLN A 497     -15.089 -36.629  53.035  1.00174.50           O  
ANISOU 2556  OE1 GLN A 497    26971  23378  15954  -2786   4337   2414       O  
ATOM   2557  NE2 GLN A 497     -13.443 -37.812  54.002  1.00170.13           N  
ANISOU 2557  NE2 GLN A 497    27263  22096  15283  -2638   4307   2444       N  
ATOM   2558  N   LYS A 498     -12.033 -34.701  48.751  1.00140.55           N  
ANISOU 2558  N   LYS A 498    22522  18416  12464  -2302   3340   1769       N  
ATOM   2559  CA  LYS A 498     -12.333 -34.185  47.416  1.00142.60           C  
ANISOU 2559  CA  LYS A 498    22453  18831  12896  -2403   3209   1675       C  
ATOM   2560  C   LYS A 498     -13.147 -32.892  47.463  1.00143.11           C  
ANISOU 2560  C   LYS A 498    22094  19329  12951  -2165   3229   1656       C  
ATOM   2561  O   LYS A 498     -13.539 -32.363  46.419  1.00140.49           O  
ANISOU 2561  O   LYS A 498    21451  19192  12737  -2212   3139   1598       O  
ATOM   2562  CB  LYS A 498     -13.035 -35.256  46.567  1.00143.76           C  
ANISOU 2562  CB  LYS A 498    22544  19013  13066  -2948   3278   1742       C  
ATOM   2563  CG  LYS A 498     -14.564 -35.221  46.542  1.00150.85           C  
ANISOU 2563  CG  LYS A 498    23016  20419  13880  -3236   3443   1855       C  
ATOM   2564  CD  LYS A 498     -15.135 -36.593  46.224  1.00157.84           C  
ANISOU 2564  CD  LYS A 498    24021  21257  14695  -3840   3562   1958       C  
ATOM   2565  CE  LYS A 498     -16.637 -36.649  46.449  1.00159.30           C  
ANISOU 2565  CE  LYS A 498    23785  21993  14749  -4153   3752   2107       C  
ATOM   2566  NZ  LYS A 498     -17.176 -38.022  46.222  1.00148.66           N  
ANISOU 2566  NZ  LYS A 498    22601  20582  13301  -4806   3873   2210       N  
ATOM   2567  N   ARG A 499     -13.375 -32.355  48.661  1.00132.00           N  
ANISOU 2567  N   ARG A 499    20698  18065  11390  -1877   3351   1705       N  
ATOM   2568  CA  ARG A 499     -14.041 -31.064  48.827  1.00128.49           C  
ANISOU 2568  CA  ARG A 499    19937  17983  10900  -1556   3388   1686       C  
ATOM   2569  C   ARG A 499     -12.993 -29.977  48.620  1.00127.40           C  
ANISOU 2569  C   ARG A 499    19938  17620  10849  -1166   3171   1512       C  
ATOM   2570  O   ARG A 499     -12.278 -29.582  49.542  1.00123.56           O  
ANISOU 2570  O   ARG A 499    19727  16953  10267   -877   3143   1468       O  
ATOM   2571  CB  ARG A 499     -14.705 -30.970  50.194  1.00139.71           C  
ANISOU 2571  CB  ARG A 499    21360  19630  12095  -1406   3624   1809       C  
ATOM   2572  CG  ARG A 499     -15.850 -31.954  50.386  1.00140.99           C  
ANISOU 2572  CG  ARG A 499    21331  20083  12154  -1820   3855   1995       C  
ATOM   2573  CD  ARG A 499     -16.215 -32.130  51.852  1.00144.44           C  
ANISOU 2573  CD  ARG A 499    21897  20622  12360  -1703   4087   2123       C  
ATOM   2574  NE  ARG A 499     -16.506 -30.864  52.515  1.00152.42           N  
ANISOU 2574  NE  ARG A 499    22790  21869  13255  -1212   4153   2101       N  
ATOM   2575  CZ  ARG A 499     -15.847 -30.404  53.570  1.00151.36           C  
ANISOU 2575  CZ  ARG A 499    22985  21530  12996   -847   4152   2051       C  
ATOM   2576  NH1 ARG A 499     -14.845 -31.080  54.108  1.00147.39           N  
ANISOU 2576  NH1 ARG A 499    22910  20620  12471   -893   4081   2030       N  
ATOM   2577  NH2 ARG A 499     -16.203 -29.237  54.098  1.00146.79           N  
ANISOU 2577  NH2 ARG A 499    22321  21164  12290   -416   4226   2027       N  
ATOM   2578  N   TRP A 500     -12.904 -29.488  47.381  1.00131.07           N  
ANISOU 2578  N   TRP A 500    20213  18104  11482  -1183   3013   1416       N  
ATOM   2579  CA  TRP A 500     -11.802 -28.614  46.992  1.00121.95           C  
ANISOU 2579  CA  TRP A 500    19214  16693  10430   -910   2789   1251       C  
ATOM   2580  C   TRP A 500     -12.030 -27.176  47.443  1.00124.24           C  
ANISOU 2580  C   TRP A 500    19446  17138  10622   -488   2806   1194       C  
ATOM   2581  O   TRP A 500     -11.114 -26.533  47.967  1.00121.49           O  
ANISOU 2581  O   TRP A 500    19374  16560  10226   -230   2699   1094       O  
ATOM   2582  CB  TRP A 500     -11.602 -28.672  45.478  1.00114.20           C  
ANISOU 2582  CB  TRP A 500    18084  15653   9654  -1097   2624   1175       C  
ATOM   2583  CG  TRP A 500     -11.646 -30.060  44.925  1.00112.65           C  
ANISOU 2583  CG  TRP A 500    17930  15347   9523  -1534   2643   1237       C  
ATOM   2584  CD1 TRP A 500     -12.606 -30.589  44.114  1.00114.19           C  
ANISOU 2584  CD1 TRP A 500    17853  15778   9756  -1885   2703   1303       C  
ATOM   2585  CD2 TRP A 500     -10.692 -31.104  45.153  1.00113.45           C  
ANISOU 2585  CD2 TRP A 500    18400  15073   9633  -1666   2607   1244       C  
ATOM   2586  NE1 TRP A 500     -12.306 -31.897  43.816  1.00118.42           N  
ANISOU 2586  NE1 TRP A 500    18608  16067  10319  -2253   2709   1336       N  
ATOM   2587  CE2 TRP A 500     -11.136 -32.237  44.443  1.00117.46           C  
ANISOU 2587  CE2 TRP A 500    18889  15560  10180  -2098   2661   1307       C  
ATOM   2588  CE3 TRP A 500      -9.505 -31.190  45.886  1.00111.76           C  
ANISOU 2588  CE3 TRP A 500    18536  14553   9376  -1453   2535   1211       C  
ATOM   2589  CZ2 TRP A 500     -10.435 -33.441  44.445  1.00120.02           C  
ANISOU 2589  CZ2 TRP A 500    19578  15527  10499  -2289   2664   1335       C  
ATOM   2590  CZ3 TRP A 500      -8.811 -32.385  45.887  1.00113.82           C  
ANISOU 2590  CZ3 TRP A 500    19102  14507   9637  -1620   2531   1254       C  
ATOM   2591  CH2 TRP A 500      -9.278 -33.494  45.171  1.00117.73           C  
ANISOU 2591  CH2 TRP A 500    19616  14947  10168  -2018   2605   1314       C  
ATOM   2592  N   ASP A 501     -13.241 -26.652  47.237  1.00158.32           N  
ANISOU 2592  N   ASP A 501    23419  21851  14886   -412   2939   1261       N  
ATOM   2593  CA  ASP A 501     -13.506 -25.257  47.578  1.00158.86           C  
ANISOU 2593  CA  ASP A 501    23469  22048  14841     30   2975   1211       C  
ATOM   2594  C   ASP A 501     -13.373 -25.010  49.075  1.00160.81           C  
ANISOU 2594  C   ASP A 501    23994  22237  14869    284   3100   1232       C  
ATOM   2595  O   ASP A 501     -12.997 -23.908  49.491  1.00160.67           O  
ANISOU 2595  O   ASP A 501    24187  22109  14753    639   3058   1132       O  
ATOM   2596  CB  ASP A 501     -14.897 -24.850  47.090  1.00162.27           C  
ANISOU 2596  CB  ASP A 501    23453  22969  15234     92   3121   1314       C  
ATOM   2597  CG  ASP A 501     -15.273 -23.440  47.508  1.00165.42           C  
ANISOU 2597  CG  ASP A 501    23869  23508  15476    604   3204   1287       C  
ATOM   2598  OD1 ASP A 501     -14.556 -22.492  47.121  1.00163.56           O  
ANISOU 2598  OD1 ASP A 501    23837  23021  15286    833   3046   1140       O  
ATOM   2599  OD2 ASP A 501     -16.284 -23.279  48.222  1.00167.96           O  
ANISOU 2599  OD2 ASP A 501    24020  24186  15611    778   3440   1417       O  
ATOM   2600  N   GLU A 502     -13.667 -26.019  49.897  1.00147.94           N  
ANISOU 2600  N   GLU A 502    22403  20663  13143     94   3254   1358       N  
ATOM   2601  CA  GLU A 502     -13.521 -25.867  51.340  1.00144.94           C  
ANISOU 2601  CA  GLU A 502    22304  20225  12542    321   3373   1384       C  
ATOM   2602  C   GLU A 502     -12.059 -25.941  51.764  1.00135.60           C  
ANISOU 2602  C   GLU A 502    21550  18605  11366    360   3174   1266       C  
ATOM   2603  O   GLU A 502     -11.646 -25.245  52.699  1.00134.91           O  
ANISOU 2603  O   GLU A 502    21738  18413  11108    647   3169   1205       O  
ATOM   2604  CB  GLU A 502     -14.344 -26.933  52.064  1.00152.18           C  
ANISOU 2604  CB  GLU A 502    23120  21359  13341     95   3614   1572       C  
ATOM   2605  CG  GLU A 502     -15.848 -26.765  51.909  1.00158.50           C  
ANISOU 2605  CG  GLU A 502    23472  22684  14067     95   3841   1715       C  
ATOM   2606  CD  GLU A 502     -16.389 -27.432  50.658  1.00163.51           C  
ANISOU 2606  CD  GLU A 502    23739  23508  14878   -313   3800   1771       C  
ATOM   2607  OE1 GLU A 502     -15.582 -27.807  49.781  1.00159.19           O  
ANISOU 2607  OE1 GLU A 502    23301  22659  14525   -525   3586   1670       O  
ATOM   2608  OE2 GLU A 502     -17.624 -27.582  50.551  1.00169.95           O  
ANISOU 2608  OE2 GLU A 502    24154  24796  15623   -426   3984   1920       O  
ATOM   2609  N   ALA A 503     -11.264 -26.777  51.091  1.00108.40           N  
ANISOU 2609  N   ALA A 503    18169  14921   8097     80   3012   1239       N  
ATOM   2610  CA  ALA A 503      -9.840 -26.850  51.400  1.00103.67           C  
ANISOU 2610  CA  ALA A 503    17920  13967   7504    132   2812   1144       C  
ATOM   2611  C   ALA A 503      -9.121 -25.561  51.029  1.00102.29           C  
ANISOU 2611  C   ALA A 503    17835  13669   7362    367   2611    972       C  
ATOM   2612  O   ALA A 503      -8.088 -25.234  51.625  1.00 97.02           O  
ANISOU 2612  O   ALA A 503    17460  12796   6608    491   2472    891       O  
ATOM   2613  CB  ALA A 503      -9.204 -28.038  50.680  1.00 96.93           C  
ANISOU 2613  CB  ALA A 503    17102  12909   6819   -181   2708   1169       C  
ATOM   2614  N   ALA A 504      -9.646 -24.819  50.051  1.00118.93           N  
ANISOU 2614  N   ALA A 504    19703  15907   9578    416   2591    920       N  
ATOM   2615  CA  ALA A 504      -9.036 -23.548  49.678  1.00113.73           C  
ANISOU 2615  CA  ALA A 504    19163  15116   8932    629   2422    763       C  
ATOM   2616  C   ALA A 504      -9.215 -22.508  50.776  1.00105.55           C  
ANISOU 2616  C   ALA A 504    18360  14102   7642    965   2509    720       C  
ATOM   2617  O   ALA A 504      -8.289 -21.744  51.073  1.00102.58           O  
ANISOU 2617  O   ALA A 504    18280  13507   7187   1087   2351    591       O  
ATOM   2618  CB  ALA A 504      -9.628 -23.049  48.360  1.00108.60           C  
ANISOU 2618  CB  ALA A 504    18216  14607   8441    617   2399    736       C  
ATOM   2619  N   VAL A 505     -10.399 -22.464  51.392  1.00 98.36           N  
ANISOU 2619  N   VAL A 505    17329  13462   6581   1109   2764    831       N  
ATOM   2620  CA  VAL A 505     -10.642 -21.505  52.465  1.00100.48           C  
ANISOU 2620  CA  VAL A 505    17848  13749   6579   1460   2880    798       C  
ATOM   2621  C   VAL A 505      -9.820 -21.862  53.697  1.00100.83           C  
ANISOU 2621  C   VAL A 505    18251  13602   6458   1451   2835    782       C  
ATOM   2622  O   VAL A 505      -9.335 -20.978  54.413  1.00101.48           O  
ANISOU 2622  O   VAL A 505    18680  13533   6344   1666   2781    675       O  
ATOM   2623  CB  VAL A 505     -12.146 -21.434  52.786  1.00103.56           C  
ANISOU 2623  CB  VAL A 505    17978  14528   6842   1635   3185    945       C  
ATOM   2624  CG1 VAL A 505     -12.441 -20.246  53.690  1.00105.86           C  
ANISOU 2624  CG1 VAL A 505    18547  14828   6848   2070   3315    897       C  
ATOM   2625  CG2 VAL A 505     -12.958 -21.349  51.504  1.00103.35           C  
ANISOU 2625  CG2 VAL A 505    17523  14756   6991   1577   3212    994       C  
ATOM   2626  N   ASN A 506      -9.649 -23.158  53.965  1.00105.47           N  
ANISOU 2626  N   ASN A 506    18788  14186   7100   1199   2857    890       N  
ATOM   2627  CA  ASN A 506      -8.850 -23.574  55.112  1.00104.63           C  
ANISOU 2627  CA  ASN A 506    19010  13916   6828   1202   2809    895       C  
ATOM   2628  C   ASN A 506      -7.371 -23.270  54.909  1.00102.28           C  
ANISOU 2628  C   ASN A 506    18945  13340   6577   1156   2502    753       C  
ATOM   2629  O   ASN A 506      -6.664 -22.971  55.877  1.00104.55           O  
ANISOU 2629  O   ASN A 506    19550  13511   6662   1261   2419    699       O  
ATOM   2630  CB  ASN A 506      -9.053 -25.064  55.384  1.00109.25           C  
ANISOU 2630  CB  ASN A 506    19509  14551   7451    957   2923   1061       C  
ATOM   2631  CG  ASN A 506      -8.529 -25.485  56.743  1.00113.35           C  
ANISOU 2631  CG  ASN A 506    20354  14970   7743   1024   2945   1107       C  
ATOM   2632  OD1 ASN A 506      -7.326 -25.673  56.927  1.00110.58           O  
ANISOU 2632  OD1 ASN A 506    20222  14409   7383    991   2735   1050       O  
ATOM   2633  ND2 ASN A 506      -9.432 -25.633  57.706  1.00121.76           N  
ANISOU 2633  ND2 ASN A 506    21440  16216   8609   1127   3203   1220       N  
ATOM   2634  N   LEU A 507      -6.887 -23.340  53.668  1.00 99.02           N  
ANISOU 2634  N   LEU A 507    18369  12842   6412    991   2329    696       N  
ATOM   2635  CA  LEU A 507      -5.487 -23.044  53.392  1.00 94.64           C  
ANISOU 2635  CA  LEU A 507    17982  12072   5904    933   2043    576       C  
ATOM   2636  C   LEU A 507      -5.206 -21.550  53.319  1.00 94.62           C  
ANISOU 2636  C   LEU A 507    18158  11986   5807   1098   1931    411       C  
ATOM   2637  O   LEU A 507      -4.055 -21.140  53.505  1.00 94.03           O  
ANISOU 2637  O   LEU A 507    18299  11760   5667   1062   1709    309       O  
ATOM   2638  CB  LEU A 507      -5.052 -23.716  52.089  1.00 92.24           C  
ANISOU 2638  CB  LEU A 507    17452  11708   5886    701   1917    585       C  
ATOM   2639  CG  LEU A 507      -4.707 -25.204  52.190  1.00 92.08           C  
ANISOU 2639  CG  LEU A 507    17414  11643   5928    521   1934    714       C  
ATOM   2640  CD1 LEU A 507      -4.985 -25.922  50.876  1.00 91.05           C  
ANISOU 2640  CD1 LEU A 507    17025  11515   6055    304   1943    755       C  
ATOM   2641  CD2 LEU A 507      -3.258 -25.390  52.611  1.00 91.50           C  
ANISOU 2641  CD2 LEU A 507    17555  11424   5785    529   1718    684       C  
ATOM   2642  N   ALA A 508      -6.223 -20.731  53.059  1.00 95.58           N  
ANISOU 2642  N   ALA A 508    18206  12210   5899   1275   2082    390       N  
ATOM   2643  CA  ALA A 508      -6.067 -19.284  52.995  1.00 96.03           C  
ANISOU 2643  CA  ALA A 508    18499  12152   5836   1459   2014    240       C  
ATOM   2644  C   ALA A 508      -6.021 -18.629  54.371  1.00 98.54           C  
ANISOU 2644  C   ALA A 508    19215  12409   5815   1667   2075    189       C  
ATOM   2645  O   ALA A 508      -6.010 -17.397  54.454  1.00 99.58           O  
ANISOU 2645  O   ALA A 508    19621  12423   5791   1843   2059     66       O  
ATOM   2646  CB  ALA A 508      -7.198 -18.669  52.167  1.00 96.45           C  
ANISOU 2646  CB  ALA A 508    18337  12345   5965   1622   2168    255       C  
ATOM   2647  N   LYS A 509      -5.995 -19.420  55.444  1.00 99.73           N  
ANISOU 2647  N   LYS A 509    19441  12620   5831   1653   2151    281       N  
ATOM   2648  CA  LYS A 509      -5.957 -18.895  56.803  1.00102.28           C  
ANISOU 2648  CA  LYS A 509    20153  12895   5814   1843   2213    240       C  
ATOM   2649  C   LYS A 509      -4.721 -19.349  57.569  1.00102.14           C  
ANISOU 2649  C   LYS A 509    20356  12769   5684   1687   2002    216       C  
ATOM   2650  O   LYS A 509      -4.678 -19.205  58.796  1.00104.36           O  
ANISOU 2650  O   LYS A 509    20935  13040   5676   1806   2055    212       O  
ATOM   2651  CB  LYS A 509      -7.220 -19.307  57.566  1.00104.66           C  
ANISOU 2651  CB  LYS A 509    20366  13416   5984   2033   2542    388       C  
ATOM   2652  CG  LYS A 509      -8.520 -18.961  56.858  1.00105.31           C  
ANISOU 2652  CG  LYS A 509    20158  13699   6156   2200   2766    449       C  
ATOM   2653  CD  LYS A 509      -9.726 -19.376  57.687  1.00108.10           C  
ANISOU 2653  CD  LYS A 509    20400  14321   6351   2374   3094    612       C  
ATOM   2654  CE  LYS A 509      -9.857 -20.891  57.755  1.00110.82           C  
ANISOU 2654  CE  LYS A 509    20472  14799   6835   2095   3151    778       C  
ATOM   2655  NZ  LYS A 509     -11.258 -21.318  58.029  1.00110.02           N  
ANISOU 2655  NZ  LYS A 509    20087  15040   6677   2180   3479    959       N  
ATOM   2656  N   SER A 510      -3.716 -19.886  56.884  1.00 99.85           N  
ANISOU 2656  N   SER A 510    19924  12419   5594   1443   1768    209       N  
ATOM   2657  CA  SER A 510      -2.535 -20.420  57.540  1.00 99.91           C  
ANISOU 2657  CA  SER A 510    20074  12387   5500   1317   1567    220       C  
ATOM   2658  C   SER A 510      -1.422 -19.376  57.583  1.00100.04           C  
ANISOU 2658  C   SER A 510    20355  12273   5383   1238   1290     47       C  
ATOM   2659  O   SER A 510      -1.545 -18.269  57.053  1.00 99.95           O  
ANISOU 2659  O   SER A 510    20446  12159   5371   1266   1258    -84       O  
ATOM   2660  CB  SER A 510      -2.062 -21.688  56.829  1.00 97.85           C  
ANISOU 2660  CB  SER A 510    19515  12162   5501   1128   1492    336       C  
ATOM   2661  OG  SER A 510      -1.541 -21.388  55.546  1.00 95.56           O  
ANISOU 2661  OG  SER A 510    19050  11809   5448    989   1321    259       O  
ATOM   2662  N   ARG A 511      -0.314 -19.736  58.237  1.00102.22           N  
ANISOU 2662  N   ARG A 511    20752  12566   5522   1130   1087     56       N  
ATOM   2663  CA  ARG A 511       0.854 -18.863  58.253  1.00102.59           C  
ANISOU 2663  CA  ARG A 511    20962  12541   5477    975    789    -90       C  
ATOM   2664  C   ARG A 511       1.536 -18.822  56.893  1.00102.24           C  
ANISOU 2664  C   ARG A 511    20693  12476   5676    785    610   -125       C  
ATOM   2665  O   ARG A 511       2.090 -17.786  56.507  1.00105.59           O  
ANISOU 2665  O   ARG A 511    21258  12808   6055    661    439   -270       O  
ATOM   2666  CB  ARG A 511       1.842 -19.326  59.325  1.00104.18           C  
ANISOU 2666  CB  ARG A 511    21229  12836   5518    905    609    -45       C  
ATOM   2667  CG  ARG A 511       3.058 -18.429  59.480  1.00105.23           C  
ANISOU 2667  CG  ARG A 511    21478  12952   5552    700    294   -184       C  
ATOM   2668  CD  ARG A 511       3.834 -18.754  60.744  1.00107.59           C  
ANISOU 2668  CD  ARG A 511    21859  13381   5638    669    149   -142       C  
ATOM   2669  NE  ARG A 511       5.132 -18.092  60.770  1.00108.63           N  
ANISOU 2669  NE  ARG A 511    22022  13576   5676    418   -178   -242       N  
ATOM   2670  CZ  ARG A 511       5.325 -16.838  61.157  1.00112.94           C  
ANISOU 2670  CZ  ARG A 511    22802  14010   6101    298   -277   -409       C  
ATOM   2671  NH1 ARG A 511       4.323 -16.080  61.570  1.00114.42           N  
ANISOU 2671  NH1 ARG A 511    23237  13999   6239    450    -77   -495       N  
ATOM   2672  NH2 ARG A 511       6.555 -16.333  61.130  1.00117.92           N  
ANISOU 2672  NH2 ARG A 511    23422  14736   6646     19   -579   -481       N  
ATOM   2673  N   TRP A 512       1.503 -19.934  56.155  1.00 96.43           N  
ANISOU 2673  N   TRP A 512    19607  11812   5219    745    651      6       N  
ATOM   2674  CA  TRP A 512       2.133 -19.975  54.841  1.00 94.11           C  
ANISOU 2674  CA  TRP A 512    19061  11505   5193    581    497    -16       C  
ATOM   2675  C   TRP A 512       1.454 -19.026  53.863  1.00 93.10           C  
ANISOU 2675  C   TRP A 512    18904  11265   5203    592    567   -124       C  
ATOM   2676  O   TRP A 512       2.116 -18.465  52.982  1.00 91.96           O  
ANISOU 2676  O   TRP A 512    18707  11068   5166    444    394   -210       O  
ATOM   2677  CB  TRP A 512       2.115 -21.409  54.307  1.00 95.94           C  
ANISOU 2677  CB  TRP A 512    18987  11805   5659    565    566    148       C  
ATOM   2678  CG  TRP A 512       2.308 -21.528  52.828  1.00 90.12           C  
ANISOU 2678  CG  TRP A 512    17978  11037   5227    448    507    137       C  
ATOM   2679  CD1 TRP A 512       3.413 -21.169  52.113  1.00 92.90           C  
ANISOU 2679  CD1 TRP A 512    18248  11395   5653    301    270     76       C  
ATOM   2680  CD2 TRP A 512       1.371 -22.055  51.882  1.00 88.59           C  
ANISOU 2680  CD2 TRP A 512    17555  10819   5286    453    687    193       C  
ATOM   2681  NE1 TRP A 512       3.220 -21.435  50.778  1.00 90.98           N  
ANISOU 2681  NE1 TRP A 512    17757  11113   5698    239    301     88       N  
ATOM   2682  CE2 TRP A 512       1.974 -21.980  50.611  1.00 88.67           C  
ANISOU 2682  CE2 TRP A 512    17376  10798   5515    323    547    155       C  
ATOM   2683  CE3 TRP A 512       0.079 -22.580  51.987  1.00 88.94           C  
ANISOU 2683  CE3 TRP A 512    17525  10889   5378    533    949    277       C  
ATOM   2684  CZ2 TRP A 512       1.329 -22.411  49.454  1.00 87.26           C  
ANISOU 2684  CZ2 TRP A 512    16966  10596   5594    279    654    188       C  
ATOM   2685  CZ3 TRP A 512      -0.558 -23.007  50.838  1.00 87.41           C  
ANISOU 2685  CZ3 TRP A 512    17079  10696   5438    461   1046    313       C  
ATOM   2686  CH2 TRP A 512       0.067 -22.920  49.588  1.00 85.57           C  
ANISOU 2686  CH2 TRP A 512    16687  10412   5413    339    895    264       C  
ATOM   2687  N   TYR A 513       0.142 -18.824  54.004  1.00 98.44           N  
ANISOU 2687  N   TYR A 513    19611  11927   5864    778    824   -110       N  
ATOM   2688  CA  TYR A 513      -0.554 -17.897  53.119  1.00 98.05           C  
ANISOU 2688  CA  TYR A 513    19543  11796   5915    845    903   -195       C  
ATOM   2689  C   TYR A 513      -0.207 -16.449  53.438  1.00104.53           C  
ANISOU 2689  C   TYR A 513    20760  12459   6498    862    802   -367       C  
ATOM   2690  O   TYR A 513      -0.154 -15.614  52.529  1.00107.32           O  
ANISOU 2690  O   TYR A 513    21140  12700   6937    822    744   -461       O  
ATOM   2691  CB  TYR A 513      -2.067 -18.116  53.206  1.00100.71           C  
ANISOU 2691  CB  TYR A 513    19762  12226   6277   1062   1213   -107       C  
ATOM   2692  CG  TYR A 513      -2.868 -17.326  52.191  1.00 98.80           C  
ANISOU 2692  CG  TYR A 513    19424  11961   6156   1167   1309   -156       C  
ATOM   2693  CD1 TYR A 513      -3.267 -16.020  52.450  1.00101.70           C  
ANISOU 2693  CD1 TYR A 513    20105  12219   6317   1369   1377   -264       C  
ATOM   2694  CD2 TYR A 513      -3.225 -17.887  50.973  1.00 99.00           C  
ANISOU 2694  CD2 TYR A 513    19072  12066   6478   1079   1335    -89       C  
ATOM   2695  CE1 TYR A 513      -3.997 -15.297  51.526  1.00 99.91           C  
ANISOU 2695  CE1 TYR A 513    19802  11978   6180   1510   1471   -291       C  
ATOM   2696  CE2 TYR A 513      -3.955 -17.171  50.041  1.00108.21           C  
ANISOU 2696  CE2 TYR A 513    20136  13239   7738   1190   1413   -122       C  
ATOM   2697  CZ  TYR A 513      -4.338 -15.877  50.324  1.00105.12           C  
ANISOU 2697  CZ  TYR A 513    20045  12753   7141   1420   1483   -216       C  
ATOM   2698  OH  TYR A 513      -5.065 -15.162  49.399  1.00107.71           O  
ANISOU 2698  OH  TYR A 513    20285  13096   7543   1574   1568   -233       O  
ATOM   2699  N   ASN A 514       0.029 -16.127  54.710  1.00110.22           N  
ANISOU 2699  N   ASN A 514    21826  13151   6902    911    782   -410       N  
ATOM   2700  CA  ASN A 514       0.352 -14.754  55.077  1.00112.11           C  
ANISOU 2700  CA  ASN A 514    22434  13207   6955    891    683   -575       C  
ATOM   2701  C   ASN A 514       1.833 -14.438  54.920  1.00112.66           C  
ANISOU 2701  C   ASN A 514    22543  13242   7019    563    351   -660       C  
ATOM   2702  O   ASN A 514       2.185 -13.267  54.741  1.00117.95           O  
ANISOU 2702  O   ASN A 514    23419  13738   7657    455    244   -793       O  
ATOM   2703  CB  ASN A 514      -0.091 -14.476  56.515  1.00121.85           C  
ANISOU 2703  CB  ASN A 514    23897  14417   7982   1064    799   -580       C  
ATOM   2704  CG  ASN A 514      -1.596 -14.357  56.645  1.00118.64           C  
ANISOU 2704  CG  ASN A 514    23489  14033   7555   1407   1133   -521       C  
ATOM   2705  OD1 ASN A 514      -2.268 -15.287  57.090  1.00119.99           O  
ANISOU 2705  OD1 ASN A 514    23507  14375   7710   1537   1320   -385       O  
ATOM   2706  ND2 ASN A 514      -2.135 -13.206  56.256  1.00114.88           N  
ANISOU 2706  ND2 ASN A 514    23180  13398   7070   1558   1218   -610       N  
ATOM   2707  N   GLN A 515       2.705 -15.447  54.980  1.00120.99           N  
ANISOU 2707  N   GLN A 515    23407  14471   8093    407    195   -571       N  
ATOM   2708  CA  GLN A 515       4.128 -15.206  54.770  1.00123.79           C  
ANISOU 2708  CA  GLN A 515    23729  14872   8433    101   -119   -626       C  
ATOM   2709  C   GLN A 515       4.439 -14.969  53.296  1.00125.07           C  
ANISOU 2709  C   GLN A 515    23730  14990   8800    -46   -204   -661       C  
ATOM   2710  O   GLN A 515       5.260 -14.107  52.962  1.00127.03           O  
ANISOU 2710  O   GLN A 515    24063  15175   9028   -284   -401   -767       O  
ATOM   2711  CB  GLN A 515       4.945 -16.382  55.308  1.00123.77           C  
ANISOU 2711  CB  GLN A 515    23555  15104   8369     40   -246   -493       C  
ATOM   2712  CG  GLN A 515       5.042 -16.432  56.826  1.00122.80           C  
ANISOU 2712  CG  GLN A 515    23597  15040   8021    101   -255   -480       C  
ATOM   2713  CD  GLN A 515       5.832 -15.274  57.403  1.00129.36           C  
ANISOU 2713  CD  GLN A 515    24642  15820   8688   -115   -467   -625       C  
ATOM   2714  OE1 GLN A 515       5.284 -14.422  58.103  1.00134.81           O  
ANISOU 2714  OE1 GLN A 515    25620  16343   9260    -36   -371   -721       O  
ATOM   2715  NE2 GLN A 515       7.128 -15.239  57.114  1.00132.14           N  
ANISOU 2715  NE2 GLN A 515    24859  16327   9020   -394   -751   -632       N  
ATOM   2716  N   THR A 516       3.795 -15.721  52.405  1.00100.13           N  
ANISOU 2716  N   THR A 516    20221  11867   5955     72    -53   -559       N  
ATOM   2717  CA  THR A 516       3.963 -15.560  50.960  1.00102.45           C  
ANISOU 2717  CA  THR A 516    20281  12120   6526    -37   -105   -577       C  
ATOM   2718  C   THR A 516       2.589 -15.601  50.311  1.00101.07           C  
ANISOU 2718  C   THR A 516    19989  11880   6533    185    154   -546       C  
ATOM   2719  O   THR A 516       2.132 -16.652  49.844  1.00 96.37           O  
ANISOU 2719  O   THR A 516    19066  11388   6163    247    265   -424       O  
ATOM   2720  CB  THR A 516       4.878 -16.643  50.382  1.00107.99           C  
ANISOU 2720  CB  THR A 516    20602  12996   7433   -173   -244   -463       C  
ATOM   2721  OG1 THR A 516       4.492 -17.923  50.896  1.00110.94           O  
ANISOU 2721  OG1 THR A 516    20815  13484   7853    -22   -112   -314       O  
ATOM   2722  CG2 THR A 516       6.329 -16.371  50.751  1.00109.86           C  
ANISOU 2722  CG2 THR A 516    20899  13347   7497   -417   -531   -497       C  
ATOM   2723  N   PRO A 517       1.892 -14.461  50.264  1.00 98.62           N  
ANISOU 2723  N   PRO A 517    19956  11407   6108    311    259   -651       N  
ATOM   2724  CA  PRO A 517       0.522 -14.473  49.722  1.00 94.21           C  
ANISOU 2724  CA  PRO A 517    19260  10851   5686    560    512   -601       C  
ATOM   2725  C   PRO A 517       0.456 -14.790  48.240  1.00 97.87           C  
ANISOU 2725  C   PRO A 517    19366  11347   6475    483    492   -562       C  
ATOM   2726  O   PRO A 517      -0.439 -15.530  47.812  1.00 95.11           O  
ANISOU 2726  O   PRO A 517    18717  11118   6302    593    656   -456       O  
ATOM   2727  CB  PRO A 517       0.015 -13.054  50.024  1.00 96.04           C  
ANISOU 2727  CB  PRO A 517    19932  10887   5673    731    600   -726       C  
ATOM   2728  CG  PRO A 517       0.919 -12.541  51.107  1.00 98.20           C  
ANISOU 2728  CG  PRO A 517    20610  11065   5637    588    440   -827       C  
ATOM   2729  CD  PRO A 517       2.254 -13.147  50.818  1.00 98.64           C  
ANISOU 2729  CD  PRO A 517    20443  11226   5811    256    171   -807       C  
ATOM   2730  N   ASN A 518       1.376 -14.248  47.439  1.00 97.96           N  
ANISOU 2730  N   ASN A 518    19403  11264   6554    275    296   -643       N  
ATOM   2731  CA  ASN A 518       1.304 -14.448  45.995  1.00 96.09           C  
ANISOU 2731  CA  ASN A 518    18863  11042   6605    214    282   -615       C  
ATOM   2732  C   ASN A 518       1.582 -15.898  45.620  1.00 92.88           C  
ANISOU 2732  C   ASN A 518    18063  10802   6427    118    258   -488       C  
ATOM   2733  O   ASN A 518       0.877 -16.473  44.782  1.00 90.37           O  
ANISOU 2733  O   ASN A 518    17470  10547   6320    170    369   -417       O  
ATOM   2734  CB  ASN A 518       2.280 -13.508  45.289  1.00 98.25           C  
ANISOU 2734  CB  ASN A 518    19283  11176   6871      1     84   -726       C  
ATOM   2735  CG  ASN A 518       1.924 -12.048  45.486  1.00 99.41           C  
ANISOU 2735  CG  ASN A 518    19876  11101   6793     99    132   -853       C  
ATOM   2736  OD1 ASN A 518       0.823 -11.614  45.145  1.00 98.72           O  
ANISOU 2736  OD1 ASN A 518    19832  10958   6718    356    318   -849       O  
ATOM   2737  ND2 ASN A 518       2.855 -11.281  46.040  1.00 95.52           N  
ANISOU 2737  ND2 ASN A 518    19733  10488   6072   -102    -35   -962       N  
ATOM   2738  N   ARG A 519       2.602 -16.506  46.229  1.00 92.93           N  
ANISOU 2738  N   ARG A 519    18056  10884   6371    -17    115   -453       N  
ATOM   2739  CA  ARG A 519       2.893 -17.909  45.952  1.00 89.29           C  
ANISOU 2739  CA  ARG A 519    17289  10550   6087    -64    112   -323       C  
ATOM   2740  C   ARG A 519       1.769 -18.814  46.441  1.00 92.93           C  
ANISOU 2740  C   ARG A 519    17662  11078   6568     94    339   -215       C  
ATOM   2741  O   ARG A 519       1.441 -19.812  45.790  1.00 93.96           O  
ANISOU 2741  O   ARG A 519    17547  11260   6895     73    418   -122       O  
ATOM   2742  CB  ARG A 519       4.221 -18.307  46.598  1.00 89.95           C  
ANISOU 2742  CB  ARG A 519    17396  10727   6054   -188    -81   -291       C  
ATOM   2743  CG  ARG A 519       4.585 -19.773  46.418  1.00 89.00           C  
ANISOU 2743  CG  ARG A 519    17025  10719   6072   -182    -69   -144       C  
ATOM   2744  CD  ARG A 519       6.057 -20.020  46.704  1.00 94.73           C  
ANISOU 2744  CD  ARG A 519    17711  11578   6705   -289   -288   -107       C  
ATOM   2745  NE  ARG A 519       6.409 -21.428  46.564  1.00 95.93           N  
ANISOU 2745  NE  ARG A 519    17672  11818   6958   -222   -255     46       N  
ATOM   2746  CZ  ARG A 519       7.649 -21.895  46.579  1.00 99.14           C  
ANISOU 2746  CZ  ARG A 519    17965  12378   7325   -255   -414    123       C  
ATOM   2747  NH1 ARG A 519       8.689 -21.091  46.726  1.00101.36           N  
ANISOU 2747  NH1 ARG A 519    18259  12781   7473   -399   -634     65       N  
ATOM   2748  NH2 ARG A 519       7.852 -23.203  46.446  1.00 99.28           N  
ANISOU 2748  NH2 ARG A 519    17864  12438   7419   -140   -344    269       N  
ATOM   2749  N   ALA A 520       1.159 -18.475  47.580  1.00 92.96           N  
ANISOU 2749  N   ALA A 520    17883  11082   6356    238    452   -226       N  
ATOM   2750  CA  ALA A 520       0.130 -19.337  48.151  1.00 88.49           C  
ANISOU 2750  CA  ALA A 520    17233  10608   5781    366    674   -112       C  
ATOM   2751  C   ALA A 520      -1.169 -19.281  47.358  1.00 90.09           C  
ANISOU 2751  C   ALA A 520    17245  10857   6129    453    863    -84       C  
ATOM   2752  O   ALA A 520      -1.885 -20.285  47.279  1.00 90.67           O  
ANISOU 2752  O   ALA A 520    17116  11035   6299    445   1011     32       O  
ATOM   2753  CB  ALA A 520      -0.125 -18.959  49.608  1.00 95.57           C  
ANISOU 2753  CB  ALA A 520    18419  11509   6384    506    748   -127       C  
ATOM   2754  N   LYS A 521      -1.496 -18.126  46.772  1.00 99.18           N  
ANISOU 2754  N   LYS A 521    18463  11943   7278    529    861   -180       N  
ATOM   2755  CA  LYS A 521      -2.735 -18.019  46.007  1.00 99.53           C  
ANISOU 2755  CA  LYS A 521    18299  12079   7437    640   1030   -141       C  
ATOM   2756  C   LYS A 521      -2.687 -18.889  44.756  1.00104.66           C  
ANISOU 2756  C   LYS A 521    18621  12782   8364    462    989    -83       C  
ATOM   2757  O   LYS A 521      -3.699 -19.488  44.371  1.00104.90           O  
ANISOU 2757  O   LYS A 521    18406  12960   8491    469   1140      7       O  
ATOM   2758  CB  LYS A 521      -3.005 -16.561  45.637  1.00104.85           C  
ANISOU 2758  CB  LYS A 521    19160  12653   8025    797   1032   -250       C  
ATOM   2759  CG  LYS A 521      -4.246 -16.364  44.777  1.00115.34           C  
ANISOU 2759  CG  LYS A 521    20253  14116   9454    948   1192   -198       C  
ATOM   2760  CD  LYS A 521      -4.374 -14.929  44.292  1.00124.22           C  
ANISOU 2760  CD  LYS A 521    21598  15107  10494   1122   1181   -299       C  
ATOM   2761  CE  LYS A 521      -5.478 -14.796  43.255  1.00128.78           C  
ANISOU 2761  CE  LYS A 521    21889  15851  11189   1266   1304   -233       C  
ATOM   2762  NZ  LYS A 521      -6.813 -15.160  43.807  1.00131.27           N  
ANISOU 2762  NZ  LYS A 521    22013  16443  11422   1476   1548   -108       N  
ATOM   2763  N   ARG A 522      -1.521 -18.979  44.114  1.00 80.62           N  
ANISOU 2763  N   ARG A 522    15568   9632   5431    291    789   -130       N  
ATOM   2764  CA  ARG A 522      -1.398 -19.792  42.909  1.00 78.39           C  
ANISOU 2764  CA  ARG A 522    15019   9373   5391    135    751    -84       C  
ATOM   2765  C   ARG A 522      -1.544 -21.275  43.229  1.00 78.42           C  
ANISOU 2765  C   ARG A 522    14904   9446   5445     49    837     41       C  
ATOM   2766  O   ARG A 522      -2.260 -22.002  42.531  1.00 80.94           O  
ANISOU 2766  O   ARG A 522    15017   9837   5900    -32    935    108       O  
ATOM   2767  CB  ARG A 522      -0.057 -19.518  42.227  1.00 77.29           C  
ANISOU 2767  CB  ARG A 522    14912   9123   5331     -2    531   -153       C  
ATOM   2768  CG  ARG A 522       0.067 -18.124  41.635  1.00 76.90           C  
ANISOU 2768  CG  ARG A 522    14980   8979   5261     28    451   -271       C  
ATOM   2769  CD  ARG A 522       1.261 -18.027  40.701  1.00 75.45           C  
ANISOU 2769  CD  ARG A 522    14743   8728   5197   -149    259   -313       C  
ATOM   2770  NE  ARG A 522       2.520 -17.957  41.433  1.00 76.05           N  
ANISOU 2770  NE  ARG A 522    14960   8789   5146   -248     98   -336       N  
ATOM   2771  CZ  ARG A 522       3.115 -16.828  41.795  1.00 77.13           C  
ANISOU 2771  CZ  ARG A 522    15339   8845   5120   -300    -20   -437       C  
ATOM   2772  NH1 ARG A 522       2.588 -15.648  41.513  1.00 77.73           N  
ANISOU 2772  NH1 ARG A 522    15597   8801   5135   -233     19   -528       N  
ATOM   2773  NH2 ARG A 522       4.266 -16.885  42.459  1.00 77.92           N  
ANISOU 2773  NH2 ARG A 522    15519   8991   5096   -424   -179   -441       N  
ATOM   2774  N   VAL A 523      -0.875 -21.739  44.287  1.00 79.17           N  
ANISOU 2774  N   VAL A 523    15151   9518   5411     54    802     77       N  
ATOM   2775  CA  VAL A 523      -0.938 -23.153  44.647  1.00 79.49           C  
ANISOU 2775  CA  VAL A 523    15146   9586   5471    -11    891    204       C  
ATOM   2776  C   VAL A 523      -2.343 -23.538  45.098  1.00 80.90           C  
ANISOU 2776  C   VAL A 523    15255   9882   5602     26   1125    285       C  
ATOM   2777  O   VAL A 523      -2.764 -24.689  44.930  1.00 81.12           O  
ANISOU 2777  O   VAL A 523    15189   9935   5698    -94   1234    388       O  
ATOM   2778  CB  VAL A 523       0.116 -23.468  45.726  1.00 80.29           C  
ANISOU 2778  CB  VAL A 523    15437   9656   5413     27    796    233       C  
ATOM   2779  CG1 VAL A 523       0.130 -24.954  46.053  1.00 80.80           C  
ANISOU 2779  CG1 VAL A 523    15501   9714   5484    -14    893    374       C  
ATOM   2780  CG2 VAL A 523       1.493 -23.009  45.272  1.00 79.30           C  
ANISOU 2780  CG2 VAL A 523    15330   9486   5316    -27    559    163       C  
ATOM   2781  N   ILE A 524      -3.096 -22.590  45.657  1.00 82.17           N  
ANISOU 2781  N   ILE A 524    15471  10121   5628    185   1216    247       N  
ATOM   2782  CA  ILE A 524      -4.449 -22.890  46.116  1.00 83.88           C  
ANISOU 2782  CA  ILE A 524    15584  10508   5779    239   1450    340       C  
ATOM   2783  C   ILE A 524      -5.414 -22.993  44.939  1.00 83.49           C  
ANISOU 2783  C   ILE A 524    15237  10594   5893    152   1527    369       C  
ATOM   2784  O   ILE A 524      -6.278 -23.878  44.909  1.00 84.47           O  
ANISOU 2784  O   ILE A 524    15191  10861   6043     29   1679    480       O  
ATOM   2785  CB  ILE A 524      -4.901 -21.834  47.142  1.00 85.72           C  
ANISOU 2785  CB  ILE A 524    15993  10793   5784    487   1537    299       C  
ATOM   2786  CG1 ILE A 524      -4.293 -22.134  48.514  1.00 86.84           C  
ANISOU 2786  CG1 ILE A 524    16395  10870   5729    533   1526    321       C  
ATOM   2787  CG2 ILE A 524      -6.417 -21.777  47.235  1.00 87.50           C  
ANISOU 2787  CG2 ILE A 524    16028  11256   5963    592   1778    384       C  
ATOM   2788  CD1 ILE A 524      -4.388 -20.984  49.489  1.00 88.53           C  
ANISOU 2788  CD1 ILE A 524    16876  11065   5697    760   1554    243       C  
ATOM   2789  N   THR A 525      -5.279 -22.105  43.949  1.00104.77           N  
ANISOU 2789  N   THR A 525    17868  13256   8684    193   1420    275       N  
ATOM   2790  CA  THR A 525      -6.169 -22.148  42.791  1.00102.54           C  
ANISOU 2790  CA  THR A 525    17296  13124   8540    122   1473    304       C  
ATOM   2791  C   THR A 525      -5.978 -23.419  41.972  1.00 98.19           C  
ANISOU 2791  C   THR A 525    16607  12540   8160   -166   1438    357       C  
ATOM   2792  O   THR A 525      -6.919 -23.871  41.310  1.00104.53           O  
ANISOU 2792  O   THR A 525    17166  13516   9033   -299   1526    421       O  
ATOM   2793  CB  THR A 525      -5.956 -20.916  41.911  1.00 96.17           C  
ANISOU 2793  CB  THR A 525    16499  12258   7784    243   1358    194       C  
ATOM   2794  OG1 THR A 525      -4.572 -20.811  41.557  1.00 98.17           O  
ANISOU 2794  OG1 THR A 525    16909  12278   8113    149   1152    105       O  
ATOM   2795  CG2 THR A 525      -6.397 -19.655  42.641  1.00112.04           C  
ANISOU 2795  CG2 THR A 525    18675  14299   9596    547   1438    151       C  
ATOM   2796  N   THR A 526      -4.779 -24.005  41.996  1.00 80.30           N  
ANISOU 2796  N   THR A 526    14500  10066   5943   -263   1312    337       N  
ATOM   2797  CA  THR A 526      -4.590 -25.300  41.351  1.00 83.14           C  
ANISOU 2797  CA  THR A 526    14807  10358   6424   -502   1311    397       C  
ATOM   2798  C   THR A 526      -5.266 -26.418  42.135  1.00 87.55           C  
ANISOU 2798  C   THR A 526    15387  10982   6895   -618   1491    523       C  
ATOM   2799  O   THR A 526      -5.753 -27.383  41.538  1.00 87.95           O  
ANISOU 2799  O   THR A 526    15348  11052   7016   -853   1561    586       O  
ATOM   2800  CB  THR A 526      -3.100 -25.600  41.178  1.00 82.83           C  
ANISOU 2800  CB  THR A 526    14933  10102   6435   -514   1146    359       C  
ATOM   2801  OG1 THR A 526      -2.504 -25.826  42.462  1.00 94.57           O  
ANISOU 2801  OG1 THR A 526    16626  11535   7771   -412   1149    397       O  
ATOM   2802  CG2 THR A 526      -2.397 -24.441  40.488  1.00 83.10           C  
ANISOU 2802  CG2 THR A 526    14956  10085   6535   -429    973    240       C  
ATOM   2803  N   PHE A 527      -5.302 -26.308  43.467  1.00 88.76           N  
ANISOU 2803  N   PHE A 527    15685  11162   6879   -477   1570    561       N  
ATOM   2804  CA  PHE A 527      -6.035 -27.283  44.269  1.00 85.88           C  
ANISOU 2804  CA  PHE A 527    15344  10876   6410   -584   1762    690       C  
ATOM   2805  C   PHE A 527      -7.537 -27.163  44.044  1.00 90.07           C  
ANISOU 2805  C   PHE A 527    15599  11696   6929   -663   1928    750       C  
ATOM   2806  O   PHE A 527      -8.246 -28.175  43.992  1.00 93.27           O  
ANISOU 2806  O   PHE A 527    15926  12186   7328   -911   2061    855       O  
ATOM   2807  CB  PHE A 527      -5.711 -27.099  45.752  1.00 85.53           C  
ANISOU 2807  CB  PHE A 527    15523  10806   6170   -391   1805    715       C  
ATOM   2808  CG  PHE A 527      -4.497 -27.856  46.212  1.00 86.18           C  
ANISOU 2808  CG  PHE A 527    15857  10672   6215   -390   1715    741       C  
ATOM   2809  CD1 PHE A 527      -4.364 -29.208  45.947  1.00 90.25           C  
ANISOU 2809  CD1 PHE A 527    16448  11067   6777   -580   1772    834       C  
ATOM   2810  CD2 PHE A 527      -3.498 -27.216  46.927  1.00 84.73           C  
ANISOU 2810  CD2 PHE A 527    15851  10417   5926   -195   1578    681       C  
ATOM   2811  CE1 PHE A 527      -3.250 -29.907  46.376  1.00 90.06           C  
ANISOU 2811  CE1 PHE A 527    16663  10860   6696   -519   1704    878       C  
ATOM   2812  CE2 PHE A 527      -2.383 -27.908  47.359  1.00 84.69           C  
ANISOU 2812  CE2 PHE A 527    16038  10273   5866   -168   1491    725       C  
ATOM   2813  CZ  PHE A 527      -2.259 -29.256  47.084  1.00 85.03           C  
ANISOU 2813  CZ  PHE A 527    16145  10204   5957   -301   1560    830       C  
ATOM   2814  N   ARG A 528      -8.038 -25.933  43.909  1.00 92.33           N  
ANISOU 2814  N   ARG A 528    15742  12148   7191   -458   1925    694       N  
ATOM   2815  CA  ARG A 528      -9.477 -25.723  43.787  1.00 97.02           C  
ANISOU 2815  CA  ARG A 528    16039  13086   7739   -464   2091    772       C  
ATOM   2816  C   ARG A 528      -9.994 -26.159  42.422  1.00103.52           C  
ANISOU 2816  C   ARG A 528    16591  14027   8714   -728   2057    788       C  
ATOM   2817  O   ARG A 528     -11.038 -26.816  42.329  1.00 97.32           O  
ANISOU 2817  O   ARG A 528    15584  13494   7899   -948   2196    899       O  
ATOM   2818  CB  ARG A 528      -9.808 -24.253  44.041  1.00 98.02           C  
ANISOU 2818  CB  ARG A 528    16139  13335   7768   -104   2107    714       C  
ATOM   2819  CG  ARG A 528     -11.295 -23.948  44.099  1.00108.00           C  
ANISOU 2819  CG  ARG A 528    17091  15006   8937    -14   2303    819       C  
ATOM   2820  CD  ARG A 528     -11.582 -22.537  43.609  1.00115.12           C  
ANISOU 2820  CD  ARG A 528    17921  16004   9816    310   2273    751       C  
ATOM   2821  NE  ARG A 528     -10.587 -21.581  44.082  1.00118.12           N  
ANISOU 2821  NE  ARG A 528    18668  16082  10131    561   2163    618       N  
ATOM   2822  CZ  ARG A 528     -10.425 -20.362  43.586  1.00118.50           C  
ANISOU 2822  CZ  ARG A 528    18796  16059  10170    801   2085    522       C  
ATOM   2823  NH1 ARG A 528     -11.177 -19.913  42.593  1.00124.44           N  
ANISOU 2823  NH1 ARG A 528    19280  17023  10978    876   2104    548       N  
ATOM   2824  NH2 ARG A 528      -9.486 -19.572  44.099  1.00103.30           N  
ANISOU 2824  NH2 ARG A 528    17242  13847   8161    959   1984    400       N  
ATOM   2825  N   THR A 529      -9.280 -25.807  41.352  1.00108.82           N  
ANISOU 2825  N   THR A 529    17277  14535   9535   -734   1874    682       N  
ATOM   2826  CA  THR A 529      -9.751 -26.058  39.996  1.00102.93           C  
ANISOU 2826  CA  THR A 529    16286  13905   8918   -953   1825    682       C  
ATOM   2827  C   THR A 529      -9.149 -27.303  39.360  1.00101.81           C  
ANISOU 2827  C   THR A 529    16267  13533   8884  -1279   1759    681       C  
ATOM   2828  O   THR A 529      -9.749 -27.851  38.429  1.00105.30           O  
ANISOU 2828  O   THR A 529    16531  14092   9387  -1553   1764    710       O  
ATOM   2829  CB  THR A 529      -9.448 -24.855  39.095  1.00 97.38           C  
ANISOU 2829  CB  THR A 529    15522  13180   8299   -748   1681    573       C  
ATOM   2830  OG1 THR A 529      -8.031 -24.653  39.026  1.00 91.98           O  
ANISOU 2830  OG1 THR A 529    15112  12152   7683   -678   1518    467       O  
ATOM   2831  CG2 THR A 529     -10.105 -23.599  39.647  1.00106.05           C  
ANISOU 2831  CG2 THR A 529    16546  14483   9265   -395   1765    578       C  
ATOM   2832  N   GLY A 530      -7.991 -27.759  39.828  1.00107.28           N  
ANISOU 2832  N   GLY A 530    17268  13913   9581  -1248   1699    654       N  
ATOM   2833  CA  GLY A 530      -7.332 -28.872  39.176  1.00112.76           C  
ANISOU 2833  CA  GLY A 530    18119  14363  10360  -1484   1645    653       C  
ATOM   2834  C   GLY A 530      -6.761 -28.544  37.818  1.00110.39           C  
ANISOU 2834  C   GLY A 530    17768  13961  10213  -1503   1480    555       C  
ATOM   2835  O   GLY A 530      -6.522 -29.452  37.018  1.00107.24           O  
ANISOU 2835  O   GLY A 530    17449  13417   9881  -1728   1457    556       O  
ATOM   2836  N   THR A 531      -6.544 -27.263  37.531  1.00 97.30           N  
ANISOU 2836  N   THR A 531    16011  12362   8598  -1271   1374    469       N  
ATOM   2837  CA  THR A 531      -6.002 -26.810  36.261  1.00 89.03           C  
ANISOU 2837  CA  THR A 531    14913  11229   7685  -1268   1221    378       C  
ATOM   2838  C   THR A 531      -4.748 -25.981  36.504  1.00 91.59           C  
ANISOU 2838  C   THR A 531    15400  11377   8023  -1031   1086    294       C  
ATOM   2839  O   THR A 531      -4.515 -25.472  37.605  1.00 92.24           O  
ANISOU 2839  O   THR A 531    15592  11456   7998   -849   1102    293       O  
ATOM   2840  CB  THR A 531      -7.027 -25.979  35.477  1.00 93.60           C  
ANISOU 2840  CB  THR A 531    15201  12073   8290  -1246   1220    362       C  
ATOM   2841  OG1 THR A 531      -7.238 -24.726  36.140  1.00 90.44           O  
ANISOU 2841  OG1 THR A 531    14776  11781   7807   -941   1237    339       O  
ATOM   2842  CG2 THR A 531      -8.352 -26.720  35.373  1.00 92.03           C  
ANISOU 2842  CG2 THR A 531    14787  12139   8042  -1496   1353    462       C  
ATOM   2843  N   TRP A 532      -3.939 -25.846  35.454  1.00 95.92           N  
ANISOU 2843  N   TRP A 532    15965  11791   8688  -1057    951    227       N  
ATOM   2844  CA  TRP A 532      -2.717 -25.057  35.501  1.00 94.35           C  
ANISOU 2844  CA  TRP A 532    15886  11458   8505   -893    808    151       C  
ATOM   2845  C   TRP A 532      -2.953 -23.589  35.163  1.00 87.65           C  
ANISOU 2845  C   TRP A 532    14958  10688   7657   -743    746     72       C  
ATOM   2846  O   TRP A 532      -2.007 -22.894  34.775  1.00 86.51           O  
ANISOU 2846  O   TRP A 532    14887  10433   7550   -683    614      0       O  
ATOM   2847  CB  TRP A 532      -1.673 -25.644  34.550  1.00 92.42           C  
ANISOU 2847  CB  TRP A 532    15701  11045   8369   -982    710    132       C  
ATOM   2848  CG  TRP A 532      -1.233 -27.033  34.893  1.00 93.84           C  
ANISOU 2848  CG  TRP A 532    16037  11096   8521  -1066    771    211       C  
ATOM   2849  CD1 TRP A 532      -1.736 -28.198  34.393  1.00 94.16           C  
ANISOU 2849  CD1 TRP A 532    16109  11084   8585  -1266    864    262       C  
ATOM   2850  CD2 TRP A 532      -0.190 -27.403  35.802  1.00 94.91           C  
ANISOU 2850  CD2 TRP A 532    16350  11135   8576   -946    746    253       C  
ATOM   2851  NE1 TRP A 532      -1.074 -29.271  34.938  1.00 99.31           N  
ANISOU 2851  NE1 TRP A 532    16984  11575   9174  -1255    915    334       N  
ATOM   2852  CE2 TRP A 532      -0.121 -28.810  35.807  1.00 95.62           C  
ANISOU 2852  CE2 TRP A 532    16589  11099   8645  -1041    843    337       C  
ATOM   2853  CE3 TRP A 532       0.690 -26.682  36.615  1.00 94.74           C  
ANISOU 2853  CE3 TRP A 532    16389  11130   8479   -777    648    231       C  
ATOM   2854  CZ2 TRP A 532       0.793 -29.509  36.592  1.00 93.11           C  
ANISOU 2854  CZ2 TRP A 532    16465  10679   8235   -922    852    413       C  
ATOM   2855  CZ3 TRP A 532       1.596 -27.378  37.393  1.00 90.20           C  
ANISOU 2855  CZ3 TRP A 532    15966  10491   7813   -690    640    304       C  
ATOM   2856  CH2 TRP A 532       1.641 -28.777  37.375  1.00 92.84           C  
ANISOU 2856  CH2 TRP A 532    16435  10709   8132   -738    745    399       C  
ATOM   2857  N   ASP A 533      -4.191 -23.105  35.305  1.00 98.41           N  
ANISOU 2857  N   ASP A 533    16182  12246   8964   -675    848     95       N  
ATOM   2858  CA  ASP A 533      -4.520 -21.741  34.904  1.00101.74           C  
ANISOU 2858  CA  ASP A 533    16557  12733   9367   -495    813     35       C  
ATOM   2859  C   ASP A 533      -3.740 -20.693  35.687  1.00101.30           C  
ANISOU 2859  C   ASP A 533    16739  12542   9210   -310    748    -37       C  
ATOM   2860  O   ASP A 533      -3.548 -19.580  35.187  1.00 98.32           O  
ANISOU 2860  O   ASP A 533    16423  12107   8828   -200    677   -109       O  
ATOM   2861  CB  ASP A 533      -6.022 -21.497  35.064  1.00104.52           C  
ANISOU 2861  CB  ASP A 533    16707  13365   9639   -406    959    103       C  
ATOM   2862  CG  ASP A 533      -6.852 -22.319  34.098  1.00111.63           C  
ANISOU 2862  CG  ASP A 533    17345  14446  10624   -627    994    164       C  
ATOM   2863  OD1 ASP A 533      -6.263 -22.968  33.207  1.00110.82           O  
ANISOU 2863  OD1 ASP A 533    17255  14210  10641   -827    902    136       O  
ATOM   2864  OD2 ASP A 533      -8.094 -22.318  34.228  1.00116.60           O  
ANISOU 2864  OD2 ASP A 533    17754  15368  11181   -606   1114    244       O  
ATOM   2865  N   ALA A 534      -3.289 -21.020  36.900  1.00108.28           N  
ANISOU 2865  N   ALA A 534    17781  13367   9992   -287    769    -19       N  
ATOM   2866  CA  ALA A 534      -2.514 -20.068  37.686  1.00100.83           C  
ANISOU 2866  CA  ALA A 534    17083  12304   8925   -159    691    -92       C  
ATOM   2867  C   ALA A 534      -1.122 -19.840  37.113  1.00 98.08           C  
ANISOU 2867  C   ALA A 534    16822  11797   8648   -259    504   -160       C  
ATOM   2868  O   ALA A 534      -0.525 -18.789  37.369  1.00101.31           O  
ANISOU 2868  O   ALA A 534    17416  12113   8966   -202    414   -241       O  
ATOM   2869  CB  ALA A 534      -2.407 -20.545  39.135  1.00 99.77           C  
ANISOU 2869  CB  ALA A 534    17084  12178   8646   -120    755    -46       C  
ATOM   2870  N   TYR A 535      -0.593 -20.795  36.347  1.00 99.03           N  
ANISOU 2870  N   TYR A 535    16828  11888   8911   -413    453   -126       N  
ATOM   2871  CA  TYR A 535       0.733 -20.674  35.752  1.00102.19           C  
ANISOU 2871  CA  TYR A 535    17265  12186   9376   -497    292   -168       C  
ATOM   2872  C   TYR A 535       0.696 -20.716  34.229  1.00104.71           C  
ANISOU 2872  C   TYR A 535    17440  12487   9858   -582    256   -186       C  
ATOM   2873  O   TYR A 535       1.757 -20.731  33.594  1.00100.41           O  
ANISOU 2873  O   TYR A 535    16894  11878   9380   -655    142   -206       O  
ATOM   2874  CB  TYR A 535       1.662 -21.771  36.284  1.00100.89           C  
ANISOU 2874  CB  TYR A 535    17134  12002   9198   -551    259   -101       C  
ATOM   2875  CG  TYR A 535       1.752 -21.835  37.794  1.00100.74           C  
ANISOU 2875  CG  TYR A 535    17259  12011   9006   -470    288    -72       C  
ATOM   2876  CD1 TYR A 535       2.804 -21.229  38.470  1.00101.24           C  
ANISOU 2876  CD1 TYR A 535    17454  12065   8948   -456    153   -110       C  
ATOM   2877  CD2 TYR A 535       0.798 -22.514  38.543  1.00 98.06           C  
ANISOU 2877  CD2 TYR A 535    16923  11724   8610   -431    445     -2       C  
ATOM   2878  CE1 TYR A 535       2.895 -21.286  39.848  1.00 98.26           C  
ANISOU 2878  CE1 TYR A 535    17220  11721   8393   -387    168    -86       C  
ATOM   2879  CE2 TYR A 535       0.881 -22.575  39.922  1.00 98.80           C  
ANISOU 2879  CE2 TYR A 535    17163  11843   8535   -348    477     28       C  
ATOM   2880  CZ  TYR A 535       1.933 -21.959  40.569  1.00 98.18           C  
ANISOU 2880  CZ  TYR A 535    17225  11745   8334   -317    334    -17       C  
ATOM   2881  OH  TYR A 535       2.024 -22.018  41.940  1.00 98.80           O  
ANISOU 2881  OH  TYR A 535    17459  11855   8224   -240    356     10       O  
ATOM   2882  N   ALA A 536      -0.494 -20.733  33.627  1.00100.27           N  
ANISOU 2882  N   ALA A 536    16743  12008   9347   -573    349   -172       N  
ATOM   2883  CA  ALA A 536      -0.628 -20.778  32.170  1.00 95.52           C  
ANISOU 2883  CA  ALA A 536    16007  11407   8881   -656    313   -188       C  
ATOM   2884  C   ALA A 536      -0.562 -19.358  31.607  1.00 97.85           C  
ANISOU 2884  C   ALA A 536    16354  11663   9161   -562    244   -265       C  
ATOM   2885  O   ALA A 536      -1.539 -18.792  31.113  1.00 97.52           O  
ANISOU 2885  O   ALA A 536    16232  11708   9115   -474    296   -268       O  
ATOM   2886  CB  ALA A 536      -1.921 -21.481  31.776  1.00 90.88           C  
ANISOU 2886  CB  ALA A 536    15238  10963   8328   -721    429   -129       C  
ATOM   2887  N   ALA A 537       0.639 -18.780  31.693  1.00111.05           N  
ANISOU 2887  N   ALA A 537    18170  13213  10810   -585    126   -318       N  
ATOM   2888  CA  ALA A 537       0.885 -17.432  31.188  1.00110.89           C  
ANISOU 2888  CA  ALA A 537    18268  13109  10758   -539     55   -393       C  
ATOM   2889  C   ALA A 537       1.951 -17.449  30.101  1.00112.59           C  
ANISOU 2889  C   ALA A 537    18445  13254  11080   -678    -61   -414       C  
ATOM   2890  O   ALA A 537       1.647 -17.128  28.949  1.00112.72           O  
ANISOU 2890  O   ALA A 537    18395  13260  11172   -680    -68   -429       O  
ATOM   2891  CB  ALA A 537       1.268 -16.497  32.336  1.00120.22           C  
ANISOU 2891  CB  ALA A 537    19701  14213  11765   -473     26   -445       C  
ATOM   2892  N   ASN A 538       3.195 -17.813  30.426  1.00113.42           N  
ANISOU 2892  N   ASN A 538    18577  13337  11179   -781   -150   -405       N  
ATOM   2893  CA  ASN A 538       4.237 -17.868  29.407  1.00108.84           C  
ANISOU 2893  CA  ASN A 538    17933  12732  10688   -898   -245   -407       C  
ATOM   2894  C   ASN A 538       3.974 -18.971  28.392  1.00106.43           C  
ANISOU 2894  C   ASN A 538    17459  12455  10526   -926   -193   -358       C  
ATOM   2895  O   ASN A 538       4.390 -18.857  27.233  1.00111.43           O  
ANISOU 2895  O   ASN A 538    18037  13060  11240   -985   -236   -370       O  
ATOM   2896  CB  ASN A 538       5.605 -18.061  30.061  1.00110.71           C  
ANISOU 2896  CB  ASN A 538    18194  13008  10861   -979   -344   -384       C  
ATOM   2897  CG  ASN A 538       5.936 -16.961  31.050  1.00117.44           C  
ANISOU 2897  CG  ASN A 538    19243  13831  11546  -1007   -415   -442       C  
ATOM   2898  OD1 ASN A 538       5.260 -15.934  31.101  1.00112.55           O  
ANISOU 2898  OD1 ASN A 538    18785  13117  10860   -957   -387   -509       O  
ATOM   2899  ND2 ASN A 538       6.982 -17.171  31.841  1.00125.74           N  
ANISOU 2899  ND2 ASN A 538    20301  14967  12506  -1080   -506   -414       N  
ATOM   2900  N   LEU A 539       3.292 -20.043  28.801  1.00 95.85           N  
ANISOU 2900  N   LEU A 539    16062  11158   9199   -902    -97   -305       N  
ATOM   2901  CA  LEU A 539       2.916 -21.077  27.844  1.00 90.39           C  
ANISOU 2901  CA  LEU A 539    15265  10467   8611   -964    -42   -270       C  
ATOM   2902  C   LEU A 539       1.872 -20.558  26.863  1.00 88.16           C  
ANISOU 2902  C   LEU A 539    14903  10219   8376   -967    -20   -304       C  
ATOM   2903  O   LEU A 539       1.913 -20.887  25.673  1.00 94.70           O  
ANISOU 2903  O   LEU A 539    15667  11028   9286  -1038    -34   -308       O  
ATOM   2904  CB  LEU A 539       2.394 -22.313  28.574  1.00 91.31           C  
ANISOU 2904  CB  LEU A 539    15385  10605   8702   -977     62   -205       C  
ATOM   2905  CG  LEU A 539       2.065 -23.506  27.672  1.00 88.46           C  
ANISOU 2905  CG  LEU A 539    14987  10210   8415  -1084    124   -171       C  
ATOM   2906  CD1 LEU A 539       3.333 -24.075  27.051  1.00 92.30           C  
ANISOU 2906  CD1 LEU A 539    15520  10608   8943  -1086     81   -151       C  
ATOM   2907  CD2 LEU A 539       1.298 -24.580  28.424  1.00 90.90           C  
ANISOU 2907  CD2 LEU A 539    15332  10533   8674  -1138    243   -110       C  
ATOM   2908  N   MET A 540       0.931 -19.741  27.344  1.00 94.59           N  
ANISOU 2908  N   MET A 540    15723  11095   9120   -869     19   -322       N  
ATOM   2909  CA  MET A 540      -0.091 -19.193  26.458  1.00101.52           C  
ANISOU 2909  CA  MET A 540    16506  12051  10016   -825     41   -335       C  
ATOM   2910  C   MET A 540       0.477 -18.116  25.542  1.00103.08           C  
ANISOU 2910  C   MET A 540    16773  12159  10233   -798    -46   -388       C  
ATOM   2911  O   MET A 540      -0.053 -17.894  24.447  1.00 96.46           O  
ANISOU 2911  O   MET A 540    15850  11364   9435   -791    -52   -391       O  
ATOM   2912  CB  MET A 540      -1.257 -18.641  27.278  1.00102.49           C  
ANISOU 2912  CB  MET A 540    16613  12296  10034   -673    129   -317       C  
ATOM   2913  CG  MET A 540      -2.083 -19.714  27.970  1.00 99.75           C  
ANISOU 2913  CG  MET A 540    16151  12084   9665   -727    234   -249       C  
ATOM   2914  SD  MET A 540      -2.637 -20.996  26.829  1.00126.51           S  
ANISOU 2914  SD  MET A 540    19353  15563  13151   -949    252   -209       S  
ATOM   2915  CE  MET A 540      -3.351 -22.181  27.966  1.00110.11           C  
ANISOU 2915  CE  MET A 540    17236  13589  11013  -1050    381   -130       C  
ATOM   2916  N   ALA A 541       1.545 -17.439  25.970  1.00120.07           N  
ANISOU 2916  N   ALA A 541    19084  14197  12342   -801   -116   -426       N  
ATOM   2917  CA  ALA A 541       2.230 -16.492  25.097  1.00112.24           C  
ANISOU 2917  CA  ALA A 541    18178  13107  11362   -831   -197   -469       C  
ATOM   2918  C   ALA A 541       3.061 -17.201  24.037  1.00111.18           C  
ANISOU 2918  C   ALA A 541    17945  12959  11341   -962   -246   -453       C  
ATOM   2919  O   ALA A 541       3.176 -16.705  22.911  1.00113.50           O  
ANISOU 2919  O   ALA A 541    18237  13214  11673   -982   -279   -472       O  
ATOM   2920  CB  ALA A 541       3.119 -15.561  25.921  1.00111.04           C  
ANISOU 2920  CB  ALA A 541    18233  12855  11101   -852   -261   -513       C  
ATOM   2921  N   LYS A 542       3.647 -18.351  24.377  1.00 89.30           N  
ANISOU 2921  N   LYS A 542    15111  10213   8607  -1028   -239   -412       N  
ATOM   2922  CA  LYS A 542       4.359 -19.142  23.380  1.00 83.69           C  
ANISOU 2922  CA  LYS A 542    14327   9489   7984  -1106   -255   -387       C  
ATOM   2923  C   LYS A 542       3.396 -19.781  22.388  1.00 77.68           C  
ANISOU 2923  C   LYS A 542    13480   8748   7285  -1130   -201   -382       C  
ATOM   2924  O   LYS A 542       3.757 -19.993  21.225  1.00 81.64           O  
ANISOU 2924  O   LYS A 542    13957   9220   7844  -1180   -220   -385       O  
ATOM   2925  CB  LYS A 542       5.206 -20.213  24.065  1.00 84.61           C  
ANISOU 2925  CB  LYS A 542    14435   9623   8091  -1117   -243   -330       C  
ATOM   2926  CG  LYS A 542       6.518 -19.700  24.639  1.00 82.74           C  
ANISOU 2926  CG  LYS A 542    14226   9417   7794  -1135   -329   -319       C  
ATOM   2927  CD  LYS A 542       7.294 -20.817  25.321  1.00 90.89           C  
ANISOU 2927  CD  LYS A 542    15231  10506   8798  -1094   -311   -241       C  
ATOM   2928  CE  LYS A 542       8.701 -20.373  25.688  1.00 96.72           C  
ANISOU 2928  CE  LYS A 542    15932  11348   9468  -1128   -412   -211       C  
ATOM   2929  NZ  LYS A 542       9.507 -21.497  26.243  1.00 90.51           N  
ANISOU 2929  NZ  LYS A 542    15096  10654   8640  -1038   -392   -111       N  
ATOM   2930  N   LYS A 543       2.175 -20.095  22.827  1.00 87.06           N  
ANISOU 2930  N   LYS A 543    14620  10009   8448  -1110   -135   -370       N  
ATOM   2931  CA  LYS A 543       1.170 -20.620  21.910  1.00 89.86           C  
ANISOU 2931  CA  LYS A 543    14875  10431   8835  -1176   -100   -364       C  
ATOM   2932  C   LYS A 543       0.676 -19.547  20.949  1.00 93.86           C  
ANISOU 2932  C   LYS A 543    15340  10982   9340  -1117   -143   -394       C  
ATOM   2933  O   LYS A 543       0.285 -19.860  19.819  1.00100.08           O  
ANISOU 2933  O   LYS A 543    16058  11809  10160  -1187   -155   -396       O  
ATOM   2934  CB  LYS A 543      -0.006 -21.205  22.692  1.00 95.40           C  
ANISOU 2934  CB  LYS A 543    15505  11253   9491  -1197    -18   -328       C  
ATOM   2935  CG  LYS A 543       0.282 -22.535  23.368  1.00 94.23           C  
ANISOU 2935  CG  LYS A 543    15418  11047   9337  -1288     44   -287       C  
ATOM   2936  CD  LYS A 543      -0.923 -23.024  24.154  1.00103.60           C  
ANISOU 2936  CD  LYS A 543    16534  12364  10466  -1337    133   -245       C  
ATOM   2937  CE  LYS A 543      -0.706 -24.433  24.680  1.00107.82           C  
ANISOU 2937  CE  LYS A 543    17174  12809  10982  -1453    207   -200       C  
ATOM   2938  NZ  LYS A 543      -1.870 -24.914  25.474  1.00117.64           N  
ANISOU 2938  NZ  LYS A 543    18353  14187  12158  -1535    303   -150       N  
ATOM   2939  N   ARG A 544       0.684 -18.284  21.379  1.00 95.45           N  
ANISOU 2939  N   ARG A 544    15615  11166   9486   -986   -164   -415       N  
ATOM   2940  CA  ARG A 544       0.214 -17.204  20.519  1.00 93.48           C  
ANISOU 2940  CA  ARG A 544    15373  10934   9210   -889   -190   -432       C  
ATOM   2941  C   ARG A 544       1.210 -16.914  19.403  1.00 93.10           C  
ANISOU 2941  C   ARG A 544    15390  10769   9215   -959   -258   -457       C  
ATOM   2942  O   ARG A 544       0.813 -16.607  18.272  1.00 92.95           O  
ANISOU 2942  O   ARG A 544    15333  10781   9204   -940   -278   -458       O  
ATOM   2943  CB  ARG A 544      -0.041 -15.949  21.353  1.00 95.08           C  
ANISOU 2943  CB  ARG A 544    15714  11105   9308   -713   -171   -447       C  
ATOM   2944  CG  ARG A 544      -1.080 -15.008  20.771  1.00107.82           C  
ANISOU 2944  CG  ARG A 544    17316  12800  10851   -527   -148   -432       C  
ATOM   2945  CD  ARG A 544      -1.482 -13.946  21.783  1.00108.67           C  
ANISOU 2945  CD  ARG A 544    17594  12873  10824   -312    -92   -437       C  
ATOM   2946  NE  ARG A 544      -2.283 -14.500  22.867  1.00121.09           N  
ANISOU 2946  NE  ARG A 544    19053  14602  12353   -250    -10   -399       N  
ATOM   2947  CZ  ARG A 544      -1.897 -14.551  24.135  1.00120.22           C  
ANISOU 2947  CZ  ARG A 544    19065  14419  12195   -254     16   -418       C  
ATOM   2948  NH1 ARG A 544      -0.718 -14.089  24.518  1.00119.95           N  
ANISOU 2948  NH1 ARG A 544    19256  14178  12142   -333    -47   -475       N  
ATOM   2949  NH2 ARG A 544      -2.714 -15.080  25.042  1.00112.18           N  
ANISOU 2949  NH2 ARG A 544    17931  13560  11132   -194    104   -372       N  
ATOM   2950  N   VAL A 545       2.507 -17.008  19.701  1.00 78.39           N  
ANISOU 2950  N   VAL A 545    13609   8801   7375  -1038   -292   -467       N  
ATOM   2951  CA  VAL A 545       3.524 -16.726  18.693  1.00 73.98           C  
ANISOU 2951  CA  VAL A 545    13090   8164   6855  -1111   -344   -477       C  
ATOM   2952  C   VAL A 545       3.549 -17.823  17.636  1.00 80.68           C  
ANISOU 2952  C   VAL A 545    13840   9039   7775  -1186   -329   -460       C  
ATOM   2953  O   VAL A 545       3.650 -17.543  16.435  1.00 87.63           O  
ANISOU 2953  O   VAL A 545    14723   9897   8674  -1204   -352   -469       O  
ATOM   2954  CB  VAL A 545       4.900 -16.551  19.363  1.00 69.95           C  
ANISOU 2954  CB  VAL A 545    12649   7602   6327  -1184   -385   -474       C  
ATOM   2955  CG1 VAL A 545       5.988 -16.388  18.313  1.00 78.01           C  
ANISOU 2955  CG1 VAL A 545    13666   8592   7382  -1273   -425   -465       C  
ATOM   2956  CG2 VAL A 545       4.881 -15.361  20.307  1.00 70.43           C  
ANISOU 2956  CG2 VAL A 545    12867   7606   6286  -1146   -409   -507       C  
ATOM   2957  N   ILE A 546       3.452 -19.085  18.060  1.00 65.72           N  
ANISOU 2957  N   ILE A 546    11895   7173   5904  -1232   -284   -437       N  
ATOM   2958  CA  ILE A 546       3.522 -20.194  17.114  1.00 64.98           C  
ANISOU 2958  CA  ILE A 546    11780   7062   5849  -1311   -258   -428       C  
ATOM   2959  C   ILE A 546       2.304 -20.198  16.196  1.00 68.97           C  
ANISOU 2959  C   ILE A 546    12220   7642   6343  -1348   -262   -445       C  
ATOM   2960  O   ILE A 546       2.418 -20.467  14.995  1.00 73.47           O  
ANISOU 2960  O   ILE A 546    12802   8187   6926  -1404   -276   -457       O  
ATOM   2961  CB  ILE A 546       3.675 -21.527  17.868  1.00 60.40           C  
ANISOU 2961  CB  ILE A 546    11226   6458   5266  -1347   -194   -395       C  
ATOM   2962  CG1 ILE A 546       5.019 -21.570  18.597  1.00 64.86           C  
ANISOU 2962  CG1 ILE A 546    11829   6990   5826  -1289   -201   -360       C  
ATOM   2963  CG2 ILE A 546       3.557 -22.704  16.913  1.00 64.89           C  
ANISOU 2963  CG2 ILE A 546    11843   6972   5842  -1437   -150   -394       C  
ATOM   2964  CD1 ILE A 546       6.202 -21.211  17.722  1.00 59.30           C  
ANISOU 2964  CD1 ILE A 546    11124   6267   5142  -1281   -235   -351       C  
ATOM   2965  N   ARG A 547       1.123 -19.893  16.740  1.00 92.20           N  
ANISOU 2965  N   ARG A 547    15083  10705   9245  -1310   -251   -439       N  
ATOM   2966  CA  ARG A 547      -0.074 -19.838  15.907  1.00 92.31           C  
ANISOU 2966  CA  ARG A 547    14985  10863   9226  -1337   -267   -438       C  
ATOM   2967  C   ARG A 547       0.021 -18.733  14.863  1.00 97.25           C  
ANISOU 2967  C   ARG A 547    15631  11480   9840  -1245   -324   -451       C  
ATOM   2968  O   ARG A 547      -0.495 -18.886  13.750  1.00 98.16           O  
ANISOU 2968  O   ARG A 547    15687  11673   9935  -1297   -355   -453       O  
ATOM   2969  CB  ARG A 547      -1.318 -19.641  16.774  1.00 99.28           C  
ANISOU 2969  CB  ARG A 547    15743  11930  10050  -1277   -233   -406       C  
ATOM   2970  CG  ARG A 547      -2.093 -20.920  17.042  1.00110.34           C  
ANISOU 2970  CG  ARG A 547    17052  13441  11430  -1457   -187   -382       C  
ATOM   2971  CD  ARG A 547      -3.356 -20.642  17.840  1.00120.85           C  
ANISOU 2971  CD  ARG A 547    18216  15011  12691  -1391   -145   -335       C  
ATOM   2972  NE  ARG A 547      -4.275 -19.769  17.121  1.00123.34           N  
ANISOU 2972  NE  ARG A 547    18380  15539  12946  -1273   -183   -311       N  
ATOM   2973  CZ  ARG A 547      -5.301 -20.194  16.397  1.00121.54           C  
ANISOU 2973  CZ  ARG A 547    17961  15555  12663  -1401   -208   -280       C  
ATOM   2974  NH1 ARG A 547      -5.571 -21.483  16.270  1.00121.65           N  
ANISOU 2974  NH1 ARG A 547    17945  15607  12671  -1692   -198   -281       N  
ATOM   2975  NH2 ARG A 547      -6.077 -19.304  15.784  1.00124.23           N  
ANISOU 2975  NH2 ARG A 547    18155  16113  12932  -1239   -246   -242       N  
ATOM   2976  N   MET A 548       0.671 -17.617  15.199  1.00 92.91           N  
ANISOU 2976  N   MET A 548    15187  10831   9284  -1126   -338   -460       N  
ATOM   2977  CA  MET A 548       0.880 -16.564  14.212  1.00 88.31           C  
ANISOU 2977  CA  MET A 548    14678  10197   8678  -1053   -380   -468       C  
ATOM   2978  C   MET A 548       1.879 -17.001  13.150  1.00 88.69           C  
ANISOU 2978  C   MET A 548    14772  10149   8779  -1167   -401   -480       C  
ATOM   2979  O   MET A 548       1.666 -16.767  11.954  1.00 90.66           O  
ANISOU 2979  O   MET A 548    15020  10416   9009  -1164   -429   -481       O  
ATOM   2980  CB  MET A 548       1.356 -15.284  14.900  1.00 87.84           C  
ANISOU 2980  CB  MET A 548    14778  10023   8574   -942   -381   -477       C  
ATOM   2981  CG  MET A 548       1.930 -14.248  13.945  1.00 91.93           C  
ANISOU 2981  CG  MET A 548    15439  10423   9066   -917   -414   -484       C  
ATOM   2982  SD  MET A 548       2.597 -12.796  14.782  1.00 99.47           S  
ANISOU 2982  SD  MET A 548    16657  11198   9938   -865   -414   -504       S  
ATOM   2983  CE  MET A 548       4.219 -13.392  15.254  1.00 77.81           C  
ANISOU 2983  CE  MET A 548    13905   8397   7264  -1087   -443   -515       C  
ATOM   2984  N   LEU A 549       2.972 -17.644  13.568  1.00 79.07           N  
ANISOU 2984  N   LEU A 549    13589   8844   7609  -1247   -381   -481       N  
ATOM   2985  CA  LEU A 549       3.986 -18.082  12.616  1.00 79.73           C  
ANISOU 2985  CA  LEU A 549    13710   8858   7726  -1316   -379   -478       C  
ATOM   2986  C   LEU A 549       3.449 -19.152  11.674  1.00 84.41           C  
ANISOU 2986  C   LEU A 549    14275   9480   8316  -1391   -363   -488       C  
ATOM   2987  O   LEU A 549       3.894 -19.247  10.525  1.00 84.29           O  
ANISOU 2987  O   LEU A 549    14306   9424   8298  -1417   -366   -493       O  
ATOM   2988  CB  LEU A 549       5.214 -18.601  13.364  1.00 75.87           C  
ANISOU 2988  CB  LEU A 549    13238   8325   7266  -1343   -352   -454       C  
ATOM   2989  CG  LEU A 549       6.063 -17.551  14.082  1.00 75.39           C  
ANISOU 2989  CG  LEU A 549    13217   8242   7187  -1335   -386   -445       C  
ATOM   2990  CD1 LEU A 549       7.421 -18.124  14.460  1.00 77.69           C  
ANISOU 2990  CD1 LEU A 549    13475   8554   7490  -1367   -371   -402       C  
ATOM   2991  CD2 LEU A 549       6.220 -16.302  13.228  1.00 81.63           C  
ANISOU 2991  CD2 LEU A 549    14085   8983   7948  -1340   -421   -456       C  
ATOM   2992  N   ILE A 550       2.498 -19.964  12.139  1.00 80.90           N  
ANISOU 2992  N   ILE A 550    13774   9108   7856  -1446   -344   -491       N  
ATOM   2993  CA  ILE A 550       1.909 -20.980  11.275  1.00 74.69           C  
ANISOU 2993  CA  ILE A 550    12994   8348   7038  -1573   -338   -509       C  
ATOM   2994  C   ILE A 550       0.995 -20.338  10.239  1.00 75.88           C  
ANISOU 2994  C   ILE A 550    13071   8624   7137  -1571   -404   -518       C  
ATOM   2995  O   ILE A 550       0.908 -20.809   9.098  1.00 75.52           O  
ANISOU 2995  O   ILE A 550    13070   8572   7054  -1662   -423   -539       O  
ATOM   2996  CB  ILE A 550       1.173 -22.030  12.131  1.00 73.62           C  
ANISOU 2996  CB  ILE A 550    12832   8258   6882  -1682   -297   -503       C  
ATOM   2997  CG1 ILE A 550       2.179 -22.995  12.761  1.00 72.66           C  
ANISOU 2997  CG1 ILE A 550    12842   7981   6785  -1686   -222   -488       C  
ATOM   2998  CG2 ILE A 550       0.145 -22.795  11.308  1.00 71.66           C  
ANISOU 2998  CG2 ILE A 550    12563   8099   6564  -1865   -316   -523       C  
ATOM   2999  CD1 ILE A 550       1.595 -23.860  13.854  1.00 79.01           C  
ANISOU 2999  CD1 ILE A 550    13653   8801   7567  -1765   -168   -470       C  
ATOM   3000  N   VAL A 551       0.323 -19.243  10.602  1.00 85.13           N  
ANISOU 3000  N   VAL A 551    14151   9909   8285  -1445   -436   -497       N  
ATOM   3001  CA  VAL A 551      -0.591 -18.589   9.670  1.00 87.97           C  
ANISOU 3001  CA  VAL A 551    14429  10421   8574  -1390   -495   -485       C  
ATOM   3002  C   VAL A 551       0.180 -17.912   8.542  1.00 87.28           C  
ANISOU 3002  C   VAL A 551    14459  10218   8485  -1335   -520   -493       C  
ATOM   3003  O   VAL A 551      -0.206 -18.002   7.370  1.00 91.09           O  
ANISOU 3003  O   VAL A 551    14927  10771   8911  -1375   -565   -497       O  
ATOM   3004  CB  VAL A 551      -1.494 -17.593  10.420  1.00 85.94           C  
ANISOU 3004  CB  VAL A 551    14071  10313   8270  -1208   -496   -445       C  
ATOM   3005  CG1 VAL A 551      -2.171 -16.644   9.443  1.00 87.77           C  
ANISOU 3005  CG1 VAL A 551    14260  10673   8415  -1064   -549   -413       C  
ATOM   3006  CG2 VAL A 551      -2.533 -18.339  11.240  1.00 88.61           C  
ANISOU 3006  CG2 VAL A 551    14240  10847   8580  -1286   -473   -422       C  
ATOM   3007  N   ILE A 552       1.281 -17.231   8.869  1.00 88.26           N  
ANISOU 3007  N   ILE A 552    14701  10179   8656  -1264   -495   -491       N  
ATOM   3008  CA  ILE A 552       2.034 -16.529   7.834  1.00 90.92           C  
ANISOU 3008  CA  ILE A 552    15149  10414   8981  -1233   -507   -488       C  
ATOM   3009  C   ILE A 552       2.690 -17.515   6.875  1.00 93.10           C  
ANISOU 3009  C   ILE A 552    15469  10633   9272  -1354   -490   -507       C  
ATOM   3010  O   ILE A 552       2.953 -17.177   5.714  1.00 93.50           O  
ANISOU 3010  O   ILE A 552    15584  10654   9287  -1345   -504   -503       O  
ATOM   3011  CB  ILE A 552       3.071 -15.580   8.465  1.00 92.81           C  
ANISOU 3011  CB  ILE A 552    15502  10516   9247  -1186   -486   -478       C  
ATOM   3012  CG1 ILE A 552       4.155 -16.369   9.199  1.00 97.22           C  
ANISOU 3012  CG1 ILE A 552    16052  11012   9874  -1281   -446   -481       C  
ATOM   3013  CG2 ILE A 552       2.395 -14.606   9.414  1.00 93.59           C  
ANISOU 3013  CG2 ILE A 552    15624  10634   9301  -1053   -490   -468       C  
ATOM   3014  CD1 ILE A 552       5.326 -15.522   9.642  1.00102.95           C  
ANISOU 3014  CD1 ILE A 552    16863  11647  10607  -1298   -442   -466       C  
ATOM   3015  N   VAL A 553       2.961 -18.741   7.329  1.00 80.97           N  
ANISOU 3015  N   VAL A 553    13928   9067   7771  -1450   -447   -522       N  
ATOM   3016  CA  VAL A 553       3.528 -19.750   6.440  1.00 77.22           C  
ANISOU 3016  CA  VAL A 553    13545   8515   7281  -1532   -410   -539       C  
ATOM   3017  C   VAL A 553       2.463 -20.284   5.490  1.00 76.72           C  
ANISOU 3017  C   VAL A 553    13479   8537   7134  -1635   -456   -571       C  
ATOM   3018  O   VAL A 553       2.709 -20.448   4.289  1.00 75.89           O  
ANISOU 3018  O   VAL A 553    13466   8393   6977  -1664   -460   -587       O  
ATOM   3019  CB  VAL A 553       4.180 -20.879   7.260  1.00 73.67           C  
ANISOU 3019  CB  VAL A 553    13142   7982   6867  -1566   -334   -535       C  
ATOM   3020  CG1 VAL A 553       4.499 -22.069   6.370  1.00 72.79           C  
ANISOU 3020  CG1 VAL A 553    13177   7777   6704  -1631   -277   -556       C  
ATOM   3021  CG2 VAL A 553       5.443 -20.374   7.938  1.00 76.53           C  
ANISOU 3021  CG2 VAL A 553    13493   8300   7286  -1476   -300   -493       C  
ATOM   3022  N   VAL A 554       1.265 -20.558   6.008  1.00 78.15           N  
ANISOU 3022  N   VAL A 554    13547   8860   7286  -1706   -494   -577       N  
ATOM   3023  CA  VAL A 554       0.178 -21.037   5.160  1.00 74.02           C  
ANISOU 3023  CA  VAL A 554    12983   8480   6660  -1848   -558   -599       C  
ATOM   3024  C   VAL A 554      -0.240 -19.960   4.167  1.00 83.66           C  
ANISOU 3024  C   VAL A 554    14145   9821   7820  -1743   -636   -579       C  
ATOM   3025  O   VAL A 554      -0.500 -20.247   2.992  1.00 89.88           O  
ANISOU 3025  O   VAL A 554    14981  10653   8518  -1832   -684   -601       O  
ATOM   3026  CB  VAL A 554      -1.006 -21.502   6.027  1.00 77.05           C  
ANISOU 3026  CB  VAL A 554    13215   9045   7016  -1961   -578   -590       C  
ATOM   3027  CG1 VAL A 554      -2.205 -21.844   5.156  1.00 80.37           C  
ANISOU 3027  CG1 VAL A 554    13538   9690   7308  -2134   -667   -599       C  
ATOM   3028  CG2 VAL A 554      -0.601 -22.696   6.879  1.00 80.20           C  
ANISOU 3028  CG2 VAL A 554    13727   9296   7451  -2082   -494   -608       C  
ATOM   3029  N   LEU A 555      -0.309 -18.704   4.616  1.00 82.62           N  
ANISOU 3029  N   LEU A 555    13944   9732   7716  -1547   -646   -535       N  
ATOM   3030  CA  LEU A 555      -0.684 -17.618   3.716  1.00 85.16           C  
ANISOU 3030  CA  LEU A 555    14252  10143   7963  -1407   -704   -501       C  
ATOM   3031  C   LEU A 555       0.385 -17.383   2.655  1.00 88.65           C  
ANISOU 3031  C   LEU A 555    14871  10406   8405  -1395   -683   -513       C  
ATOM   3032  O   LEU A 555       0.064 -17.064   1.504  1.00 87.84           O  
ANISOU 3032  O   LEU A 555    14792  10373   8211  -1369   -736   -502       O  
ATOM   3033  CB  LEU A 555      -0.946 -16.339   4.512  1.00 83.45           C  
ANISOU 3033  CB  LEU A 555    13998   9957   7754  -1182   -694   -451       C  
ATOM   3034  CG  LEU A 555      -2.386 -16.062   4.960  1.00 84.60           C  
ANISOU 3034  CG  LEU A 555    13939  10386   7820  -1081   -734   -403       C  
ATOM   3035  CD1 LEU A 555      -3.278 -15.819   3.753  1.00 93.11           C  
ANISOU 3035  CD1 LEU A 555    14922  11692   8764  -1035   -820   -366       C  
ATOM   3036  CD2 LEU A 555      -2.942 -17.193   5.814  1.00 92.93           C  
ANISOU 3036  CD2 LEU A 555    14845  11564   8900  -1258   -722   -420       C  
ATOM   3037  N   PHE A 556       1.660 -17.539   3.019  1.00 92.13           N  
ANISOU 3037  N   PHE A 556    15422  10648   8936  -1410   -605   -524       N  
ATOM   3038  CA  PHE A 556       2.731 -17.354   2.046  1.00 88.21           C  
ANISOU 3038  CA  PHE A 556    15067  10016   8433  -1402   -567   -520       C  
ATOM   3039  C   PHE A 556       2.700 -18.437   0.975  1.00 85.03           C  
ANISOU 3039  C   PHE A 556    14739   9608   7961  -1522   -567   -560       C  
ATOM   3040  O   PHE A 556       2.895 -18.151  -0.211  1.00 93.69           O  
ANISOU 3040  O   PHE A 556    15923  10688   8987  -1502   -578   -556       O  
ATOM   3041  CB  PHE A 556       4.086 -17.340   2.751  1.00 87.57           C  
ANISOU 3041  CB  PHE A 556    15034   9793   8445  -1397   -484   -505       C  
ATOM   3042  CG  PHE A 556       5.212 -16.865   1.883  1.00 90.64           C  
ANISOU 3042  CG  PHE A 556    15526  10090   8822  -1377   -437   -477       C  
ATOM   3043  CD1 PHE A 556       5.448 -15.512   1.709  1.00 99.75           C  
ANISOU 3043  CD1 PHE A 556    16734  11208   9957  -1314   -449   -438       C  
ATOM   3044  CD2 PHE A 556       6.029 -17.772   1.230  1.00 90.21           C  
ANISOU 3044  CD2 PHE A 556    15538   9982   8757  -1419   -368   -482       C  
ATOM   3045  CE1 PHE A 556       6.483 -15.072   0.908  1.00 98.19           C  
ANISOU 3045  CE1 PHE A 556    16627  10941   9739  -1330   -399   -403       C  
ATOM   3046  CE2 PHE A 556       7.063 -17.339   0.426  1.00 91.46           C  
ANISOU 3046  CE2 PHE A 556    15765  10092   8894  -1396   -312   -442       C  
ATOM   3047  CZ  PHE A 556       7.291 -15.988   0.265  1.00 95.66           C  
ANISOU 3047  CZ  PHE A 556    16323  10608   9416  -1371   -330   -401       C  
ATOM   3048  N   PHE A 557       2.460 -19.688   1.374  1.00 81.24           N  
ANISOU 3048  N   PHE A 557    14264   9123   7482  -1653   -548   -601       N  
ATOM   3049  CA  PHE A 557       2.405 -20.772   0.400  1.00 75.15           C  
ANISOU 3049  CA  PHE A 557    13632   8307   6615  -1788   -540   -650       C  
ATOM   3050  C   PHE A 557       1.152 -20.677  -0.460  1.00 79.29           C  
ANISOU 3050  C   PHE A 557    14096   9019   7011  -1880   -658   -668       C  
ATOM   3051  O   PHE A 557       1.190 -20.982  -1.657  1.00 84.94           O  
ANISOU 3051  O   PHE A 557    14941   9713   7619  -1943   -677   -698       O  
ATOM   3052  CB  PHE A 557       2.466 -22.126   1.110  1.00 74.73           C  
ANISOU 3052  CB  PHE A 557    13658   8163   6572  -1913   -477   -686       C  
ATOM   3053  CG  PHE A 557       3.863 -22.587   1.427  1.00 77.18           C  
ANISOU 3053  CG  PHE A 557    14096   8285   6944  -1816   -347   -667       C  
ATOM   3054  CD1 PHE A 557       4.858 -21.674   1.737  1.00 83.35           C  
ANISOU 3054  CD1 PHE A 557    14806   9050   7814  -1659   -309   -610       C  
ATOM   3055  CD2 PHE A 557       4.181 -23.935   1.409  1.00 76.65           C  
ANISOU 3055  CD2 PHE A 557    14231   8070   6821  -1883   -259   -699       C  
ATOM   3056  CE1 PHE A 557       6.142 -22.096   2.029  1.00 81.55           C  
ANISOU 3056  CE1 PHE A 557    14641   8721   7623  -1567   -197   -574       C  
ATOM   3057  CE2 PHE A 557       5.465 -24.363   1.699  1.00 81.36           C  
ANISOU 3057  CE2 PHE A 557    14927   8534   7453  -1740   -131   -660       C  
ATOM   3058  CZ  PHE A 557       6.445 -23.441   2.010  1.00 76.89           C  
ANISOU 3058  CZ  PHE A 557    14224   8013   6979  -1580   -105   -593       C  
ATOM   3059  N   LEU A 558       0.032 -20.249   0.129  1.00 82.56           N  
ANISOU 3059  N   LEU A 558    14306   9645   7418  -1878   -738   -642       N  
ATOM   3060  CA  LEU A 558      -1.206 -20.134  -0.636  1.00 89.80           C  
ANISOU 3060  CA  LEU A 558    15107  10819   8195  -1952   -862   -637       C  
ATOM   3061  C   LEU A 558      -1.103 -19.080  -1.732  1.00 93.10           C  
ANISOU 3061  C   LEU A 558    15556  11272   8546  -1787   -906   -599       C  
ATOM   3062  O   LEU A 558      -1.810 -19.164  -2.742  1.00 89.39           O  
ANISOU 3062  O   LEU A 558    15063  10971   7931  -1859  -1002   -603       O  
ATOM   3063  CB  LEU A 558      -2.374 -19.807   0.294  1.00 87.37           C  
ANISOU 3063  CB  LEU A 558    14537  10774   7887  -1929   -918   -590       C  
ATOM   3064  CG  LEU A 558      -3.091 -20.984   0.954  1.00 83.11           C  
ANISOU 3064  CG  LEU A 558    13919  10337   7321  -2189   -927   -621       C  
ATOM   3065  CD1 LEU A 558      -4.376 -20.509   1.608  1.00 85.84           C  
ANISOU 3065  CD1 LEU A 558    13957  11032   7626  -2143   -991   -553       C  
ATOM   3066  CD2 LEU A 558      -3.373 -22.073  -0.067  1.00 86.28           C  
ANISOU 3066  CD2 LEU A 558    14451  10751   7581  -2481   -980   -687       C  
ATOM   3067  N   CYS A 559      -0.231 -18.088  -1.553  1.00112.03           N  
ANISOU 3067  N   CYS A 559    18018  13517  11030  -1586   -840   -559       N  
ATOM   3068  CA  CYS A 559      -0.078 -17.003  -2.514  1.00105.46           C  
ANISOU 3068  CA  CYS A 559    17254  12684  10131  -1424   -863   -513       C  
ATOM   3069  C   CYS A 559       0.872 -17.351  -3.654  1.00103.88           C  
ANISOU 3069  C   CYS A 559    17259  12318   9891  -1480   -814   -542       C  
ATOM   3070  O   CYS A 559       0.619 -16.972  -4.802  1.00109.08           O  
ANISOU 3070  O   CYS A 559    17975  13043  10428  -1440   -868   -525       O  
ATOM   3071  CB  CYS A 559       0.417 -15.742  -1.805  1.00106.09           C  
ANISOU 3071  CB  CYS A 559    17357  12657  10295  -1222   -807   -456       C  
ATOM   3072  SG  CYS A 559      -0.807 -14.950  -0.739  1.00110.67           S  
ANISOU 3072  SG  CYS A 559    17749  13441  10861  -1050   -855   -400       S  
ATOM   3073  N   TRP A 560       1.961 -18.065  -3.365  1.00 75.44           N  
ANISOU 3073  N   TRP A 560    13769   8521   6375  -1548   -707   -576       N  
ATOM   3074  CA  TRP A 560       3.001 -18.319  -4.353  1.00 79.67           C  
ANISOU 3074  CA  TRP A 560    14493   8904   6873  -1550   -628   -586       C  
ATOM   3075  C   TRP A 560       2.897 -19.685  -5.019  1.00 81.74           C  
ANISOU 3075  C   TRP A 560    14896   9129   7034  -1710   -619   -660       C  
ATOM   3076  O   TRP A 560       3.675 -19.967  -5.935  1.00 80.54           O  
ANISOU 3076  O   TRP A 560    14924   8860   6819  -1693   -546   -670       O  
ATOM   3077  CB  TRP A 560       4.385 -18.175  -3.711  1.00 72.87           C  
ANISOU 3077  CB  TRP A 560    13666   7883   6139  -1485   -499   -554       C  
ATOM   3078  CG  TRP A 560       4.762 -16.753  -3.461  1.00 82.12           C  
ANISOU 3078  CG  TRP A 560    14802   9038   7360  -1368   -492   -485       C  
ATOM   3079  CD1 TRP A 560       4.667 -16.075  -2.282  1.00 79.56           C  
ANISOU 3079  CD1 TRP A 560    14383   8722   7126  -1321   -504   -460       C  
ATOM   3080  CD2 TRP A 560       5.282 -15.823  -4.419  1.00 87.52           C  
ANISOU 3080  CD2 TRP A 560    15592   9676   7987  -1300   -466   -435       C  
ATOM   3081  NE1 TRP A 560       5.101 -14.782  -2.444  1.00 87.27           N  
ANISOU 3081  NE1 TRP A 560    15428   9638   8094  -1242   -487   -404       N  
ATOM   3082  CE2 TRP A 560       5.484 -14.602  -3.747  1.00 79.86           C  
ANISOU 3082  CE2 TRP A 560    14608   8667   7070  -1232   -462   -383       C  
ATOM   3083  CE3 TRP A 560       5.600 -15.906  -5.778  1.00 85.39           C  
ANISOU 3083  CE3 TRP A 560    15455   9381   7610  -1296   -439   -429       C  
ATOM   3084  CZ2 TRP A 560       5.989 -13.473  -4.387  1.00 79.97           C  
ANISOU 3084  CZ2 TRP A 560    14746   8607   7031  -1182   -430   -322       C  
ATOM   3085  CZ3 TRP A 560       6.100 -14.783  -6.412  1.00 88.18           C  
ANISOU 3085  CZ3 TRP A 560    15900   9683   7922  -1228   -406   -362       C  
ATOM   3086  CH2 TRP A 560       6.289 -13.583  -5.717  1.00 84.60           C  
ANISOU 3086  CH2 TRP A 560    15440   9181   7522  -1182   -401   -308       C  
ATOM   3087  N   MET A 561       1.972 -20.534  -4.589  1.00105.90           N  
ANISOU 3087  N   MET A 561    17904  12276  10057  -1873   -683   -710       N  
ATOM   3088  CA  MET A 561       1.795 -21.832  -5.232  1.00106.81           C  
ANISOU 3088  CA  MET A 561    18214  12327  10041  -2068   -680   -789       C  
ATOM   3089  C   MET A 561       1.117 -21.713  -6.597  1.00109.00           C  
ANISOU 3089  C   MET A 561    18552  12732  10130  -2147   -791   -813       C  
ATOM   3090  O   MET A 561       1.528 -22.412  -7.533  1.00114.75           O  
ANISOU 3090  O   MET A 561    19535  13327  10737  -2218   -746   -867       O  
ATOM   3091  CB  MET A 561       1.002 -22.782  -4.329  1.00109.20           C  
ANISOU 3091  CB  MET A 561    18467  12680  10344  -2271   -712   -833       C  
ATOM   3092  CG  MET A 561       1.861 -23.548  -3.332  1.00111.41           C  
ANISOU 3092  CG  MET A 561    18851  12746  10733  -2244   -570   -839       C  
ATOM   3093  SD  MET A 561       3.285 -24.350  -4.095  1.00115.30           S  
ANISOU 3093  SD  MET A 561    19692  12948  11168  -2152   -400   -863       S  
ATOM   3094  CE  MET A 561       3.699 -25.571  -2.853  1.00108.89           C  
ANISOU 3094  CE  MET A 561    19007  11954  10413  -2179   -274   -874       C  
ATOM   3095  N   PRO A 562       0.082 -20.873  -6.767  1.00 92.77           N  
ANISOU 3095  N   PRO A 562    16283  10940   8024  -2122   -932   -770       N  
ATOM   3096  CA  PRO A 562      -0.532 -20.766  -8.103  1.00 97.37           C  
ANISOU 3096  CA  PRO A 562    16917  11673   8405  -2186  -1047   -782       C  
ATOM   3097  C   PRO A 562       0.437 -20.354  -9.199  1.00 94.75           C  
ANISOU 3097  C   PRO A 562    16797  11177   8027  -2043   -972   -769       C  
ATOM   3098  O   PRO A 562       0.319 -20.839 -10.330  1.00 92.13           O  
ANISOU 3098  O   PRO A 562    16646  10844   7516  -2153  -1011   -819       O  
ATOM   3099  CB  PRO A 562      -1.629 -19.715  -7.890  1.00 91.26           C  
ANISOU 3099  CB  PRO A 562    15843  11219   7611  -2073  -1180   -699       C  
ATOM   3100  CG  PRO A 562      -2.021 -19.902  -6.480  1.00 93.95           C  
ANISOU 3100  CG  PRO A 562    15994  11623   8081  -2109  -1166   -689       C  
ATOM   3101  CD  PRO A 562      -0.724 -20.148  -5.764  1.00 92.58           C  
ANISOU 3101  CD  PRO A 562    15970  11123   8082  -2044   -999   -709       C  
ATOM   3102  N   ILE A 563       1.396 -19.477  -8.901  1.00106.85           N  
ANISOU 3102  N   ILE A 563    18323  12577   9698  -1823   -863   -703       N  
ATOM   3103  CA  ILE A 563       2.298 -19.000  -9.945  1.00103.39           C  
ANISOU 3103  CA  ILE A 563    18062  12015   9207  -1699   -784   -673       C  
ATOM   3104  C   ILE A 563       3.399 -20.018 -10.228  1.00103.58           C  
ANISOU 3104  C   ILE A 563    18322  11810   9222  -1741   -631   -724       C  
ATOM   3105  O   ILE A 563       3.804 -20.201 -11.382  1.00111.38           O  
ANISOU 3105  O   ILE A 563    19514  12729  10075  -1728   -588   -739       O  
ATOM   3106  CB  ILE A 563       2.871 -17.620  -9.570  1.00106.41           C  
ANISOU 3106  CB  ILE A 563    18362  12358   9710  -1490   -729   -574       C  
ATOM   3107  CG1 ILE A 563       3.785 -17.101 -10.682  1.00111.32           C  
ANISOU 3107  CG1 ILE A 563    19164  12869  10262  -1393   -641   -531       C  
ATOM   3108  CG2 ILE A 563       3.602 -17.671  -8.235  1.00107.65           C  
ANISOU 3108  CG2 ILE A 563    18437  12401  10063  -1468   -628   -562       C  
ATOM   3109  CD1 ILE A 563       3.079 -16.903 -12.004  1.00113.43           C  
ANISOU 3109  CD1 ILE A 563    19520  13256  10323  -1388   -746   -531       C  
ATOM   3110  N   PHE A 564       3.894 -20.703  -9.195  1.00107.71           N  
ANISOU 3110  N   PHE A 564    18835  12219   9871  -1766   -538   -743       N  
ATOM   3111  CA  PHE A 564       4.940 -21.698  -9.416  1.00111.19           C  
ANISOU 3111  CA  PHE A 564    19508  12456  10285  -1748   -375   -774       C  
ATOM   3112  C   PHE A 564       4.384 -22.945 -10.093  1.00109.32           C  
ANISOU 3112  C   PHE A 564    19526  12156   9855  -1935   -405   -879       C  
ATOM   3113  O   PHE A 564       5.070 -23.570 -10.910  1.00104.65           O  
ANISOU 3113  O   PHE A 564    19212  11408   9142  -1895   -290   -908       O  
ATOM   3114  CB  PHE A 564       5.616 -22.057  -8.093  1.00111.81           C  
ANISOU 3114  CB  PHE A 564    19503  12448  10531  -1691   -270   -749       C  
ATOM   3115  CG  PHE A 564       6.751 -21.144  -7.728  1.00112.26           C  
ANISOU 3115  CG  PHE A 564    19433  12498  10723  -1515   -171   -651       C  
ATOM   3116  CD1 PHE A 564       6.509 -19.854  -7.286  1.00110.62           C  
ANISOU 3116  CD1 PHE A 564    19023  12396  10612  -1476   -249   -593       C  
ATOM   3117  CD2 PHE A 564       8.064 -21.576  -7.832  1.00114.57           C  
ANISOU 3117  CD2 PHE A 564    19819  12690  11021  -1392      4   -610       C  
ATOM   3118  CE1 PHE A 564       7.553 -19.013  -6.950  1.00107.98           C  
ANISOU 3118  CE1 PHE A 564    18603  12048  10376  -1374   -165   -509       C  
ATOM   3119  CE2 PHE A 564       9.112 -20.740  -7.498  1.00115.35           C  
ANISOU 3119  CE2 PHE A 564    19770  12832  11225  -1279     84   -512       C  
ATOM   3120  CZ  PHE A 564       8.857 -19.457  -7.056  1.00109.79           C  
ANISOU 3120  CZ  PHE A 564    18886  12216  10615  -1299     -7   -467       C  
ATOM   3121  N   SER A 565       3.146 -23.321  -9.767  1.00100.38           N  
ANISOU 3121  N   SER A 565    18318  11150   8673  -2150   -552   -934       N  
ATOM   3122  CA  SER A 565       2.525 -24.458 -10.437  1.00100.88           C  
ANISOU 3122  CA  SER A 565    18640  11168   8522  -2400   -604  -1039       C  
ATOM   3123  C   SER A 565       2.175 -24.121 -11.882  1.00100.47           C  
ANISOU 3123  C   SER A 565    18692  11212   8269  -2436   -698  -1059       C  
ATOM   3124  O   SER A 565       2.298 -24.972 -12.770  1.00100.90           O  
ANISOU 3124  O   SER A 565    19084  11128   8125  -2548   -664  -1139       O  
ATOM   3125  CB  SER A 565       1.281 -24.904  -9.669  1.00 99.35           C  
ANISOU 3125  CB  SER A 565    18297  11134   8319  -2664   -742  -1078       C  
ATOM   3126  OG  SER A 565       0.188 -24.037  -9.921  1.00111.32           O  
ANISOU 3126  OG  SER A 565    19527  12977   9792  -2713   -933  -1040       O  
ATOM   3127  N   ALA A 566       1.740 -22.885 -12.136  1.00 95.75           N  
ANISOU 3127  N   ALA A 566    17841  10839   7699  -2329   -811   -983       N  
ATOM   3128  CA  ALA A 566       1.441 -22.476 -13.505  1.00 90.49           C  
ANISOU 3128  CA  ALA A 566    17267  10278   6837  -2327   -900   -983       C  
ATOM   3129  C   ALA A 566       2.707 -22.350 -14.340  1.00 94.58           C  
ANISOU 3129  C   ALA A 566    18031  10581   7324  -2135   -728   -963       C  
ATOM   3130  O   ALA A 566       2.668 -22.561 -15.558  1.00 93.10           O  
ANISOU 3130  O   ALA A 566    18070  10377   6925  -2179   -750  -1003       O  
ATOM   3131  CB  ALA A 566       0.670 -21.157 -13.508  1.00 85.05           C  
ANISOU 3131  CB  ALA A 566    16264   9876   6175  -2210  -1047   -888       C  
ATOM   3132  N   ASN A 567       3.834 -22.004 -13.712  1.00 91.97           N  
ANISOU 3132  N   ASN A 567    17650  10110   7185  -1931   -558   -896       N  
ATOM   3133  CA  ASN A 567       5.094 -21.953 -14.443  1.00 92.80           C  
ANISOU 3133  CA  ASN A 567    17953  10050   7255  -1756   -375   -861       C  
ATOM   3134  C   ASN A 567       5.588 -23.348 -14.803  1.00 94.23           C  
ANISOU 3134  C   ASN A 567    18486  10018   7301  -1805   -242   -948       C  
ATOM   3135  O   ASN A 567       6.277 -23.519 -15.815  1.00 94.46           O  
ANISOU 3135  O   ASN A 567    18758   9942   7189  -1702   -125   -948       O  
ATOM   3136  CB  ASN A 567       6.149 -21.207 -13.626  1.00 91.56           C  
ANISOU 3136  CB  ASN A 567    17609   9858   7321  -1562   -241   -755       C  
ATOM   3137  CG  ASN A 567       5.994 -19.702 -13.714  1.00 92.50           C  
ANISOU 3137  CG  ASN A 567    17531  10108   7505  -1469   -313   -660       C  
ATOM   3138  OD1 ASN A 567       5.112 -19.198 -14.409  1.00100.35           O  
ANISOU 3138  OD1 ASN A 567    18519  11230   8379  -1499   -455   -661       O  
ATOM   3139  ND2 ASN A 567       6.857 -18.976 -13.014  1.00 94.37           N  
ANISOU 3139  ND2 ASN A 567    17626  10317   7912  -1356   -215   -573       N  
ATOM   3140  N   ALA A 568       5.252 -24.352 -13.990  1.00108.30           N  
ANISOU 3140  N   ALA A 568    20329  11717   9103  -1948   -245  -1018       N  
ATOM   3141  CA  ALA A 568       5.587 -25.727 -14.343  1.00109.41           C  
ANISOU 3141  CA  ALA A 568    20881  11617   9074  -2003   -121  -1109       C  
ATOM   3142  C   ALA A 568       4.703 -26.230 -15.477  1.00114.94           C  
ANISOU 3142  C   ALA A 568    21855  12326   9492  -2246   -251  -1219       C  
ATOM   3143  O   ALA A 568       5.171 -26.953 -16.365  1.00117.12           O  
ANISOU 3143  O   ALA A 568    22532  12407   9562  -2219   -135  -1277       O  
ATOM   3144  CB  ALA A 568       5.462 -26.632 -13.118  1.00105.73           C  
ANISOU 3144  CB  ALA A 568    20436  11039   8696  -2095    -82  -1144       C  
ATOM   3145  N   TRP A 569       3.419 -25.862 -15.459  1.00 87.39           N  
ANISOU 3145  N   TRP A 569    18155   9081   5969  -2480   -490  -1243       N  
ATOM   3146  CA  TRP A 569       2.534 -26.200 -16.569  1.00 85.34           C  
ANISOU 3146  CA  TRP A 569    18094   8907   5426  -2733   -649  -1333       C  
ATOM   3147  C   TRP A 569       3.010 -25.549 -17.859  1.00 85.91           C  
ANISOU 3147  C   TRP A 569    18275   8994   5371  -2553   -618  -1297       C  
ATOM   3148  O   TRP A 569       2.914 -26.144 -18.939  1.00 88.33           O  
ANISOU 3148  O   TRP A 569    18862   9218   5480  -2647   -618  -1356       O  
ATOM   3149  CB  TRP A 569       1.105 -25.765 -16.248  1.00 85.71           C  
ANISOU 3149  CB  TRP A 569    17792   9303   5470  -2969   -912  -1326       C  
ATOM   3150  CG  TRP A 569       0.084 -26.281 -17.208  1.00 88.87           C  
ANISOU 3150  CG  TRP A 569    18304   9848   5616  -3283  -1090  -1401       C  
ATOM   3151  CD1 TRP A 569       0.204 -27.359 -18.034  1.00 91.46           C  
ANISOU 3151  CD1 TRP A 569    18963   9965   5824  -3415  -1018  -1464       C  
ATOM   3152  CD2 TRP A 569      -1.218 -25.734 -17.449  1.00 90.15           C  
ANISOU 3152  CD2 TRP A 569    18161  10422   5669  -3466  -1355  -1379       C  
ATOM   3153  NE1 TRP A 569      -0.944 -27.521 -18.771  1.00 94.26           N  
ANISOU 3153  NE1 TRP A 569    19237  10570   6009  -3705  -1228  -1493       N  
ATOM   3154  CE2 TRP A 569      -1.832 -26.535 -18.431  1.00 93.54           C  
ANISOU 3154  CE2 TRP A 569    18734  10887   5919  -3735  -1440  -1438       C  
ATOM   3155  CE3 TRP A 569      -1.924 -24.646 -16.928  1.00 89.04           C  
ANISOU 3155  CE3 TRP A 569    17574  10637   5621  -3377  -1504  -1280       C  
ATOM   3156  CZ2 TRP A 569      -3.118 -26.283 -18.903  1.00 95.87           C  
ANISOU 3156  CZ2 TRP A 569    18772  11598   6055  -3962  -1696  -1425       C  
ATOM   3157  CZ3 TRP A 569      -3.201 -24.397 -17.398  1.00 91.36           C  
ANISOU 3157  CZ3 TRP A 569    17644  11344   5724  -3575  -1755  -1264       C  
ATOM   3158  CH2 TRP A 569      -3.785 -25.212 -18.375  1.00 94.74           C  
ANISOU 3158  CH2 TRP A 569    18230  11839   5929  -3879  -1859  -1341       C  
ATOM   3159  N   ARG A 570       3.532 -24.325 -17.765  1.00114.62           N  
ANISOU 3159  N   ARG A 570    21638  12729   9185  -2282   -576  -1170       N  
ATOM   3160  CA  ARG A 570       4.039 -23.638 -18.946  1.00111.20           C  
ANISOU 3160  CA  ARG A 570    21306  12305   8640  -2106   -528  -1118       C  
ATOM   3161  C   ARG A 570       5.336 -24.267 -19.442  1.00116.78           C  
ANISOU 3161  C   ARG A 570    22358  12736   9277  -1932   -267  -1129       C  
ATOM   3162  O   ARG A 570       5.649 -24.182 -20.635  1.00126.85           O  
ANISOU 3162  O   ARG A 570    23865  13973  10359  -1860   -218  -1132       O  
ATOM   3163  CB  ARG A 570       4.231 -22.152 -18.626  1.00109.61           C  
ANISOU 3163  CB  ARG A 570    20751  12260   8637  -1895   -544   -976       C  
ATOM   3164  CG  ARG A 570       4.909 -21.332 -19.710  1.00114.06           C  
ANISOU 3164  CG  ARG A 570    21410  12812   9117  -1697   -459   -896       C  
ATOM   3165  CD  ARG A 570       5.737 -20.214 -19.098  1.00119.32           C  
ANISOU 3165  CD  ARG A 570    21841  13477  10020  -1484   -344   -760       C  
ATOM   3166  NE  ARG A 570       6.251 -19.297 -20.108  1.00126.85           N  
ANISOU 3166  NE  ARG A 570    22869  14442  10887  -1331   -280   -669       N  
ATOM   3167  CZ  ARG A 570       5.602 -18.228 -20.549  1.00120.47           C  
ANISOU 3167  CZ  ARG A 570    21966  13786  10023  -1289   -416   -603       C  
ATOM   3168  NH1 ARG A 570       4.398 -17.916 -20.099  1.00119.12           N  
ANISOU 3168  NH1 ARG A 570    21595  13801   9866  -1362   -626   -611       N  
ATOM   3169  NH2 ARG A 570       6.174 -17.455 -21.467  1.00124.08           N  
ANISOU 3169  NH2 ARG A 570    22535  14218  10392  -1153   -330   -516       N  
ATOM   3170  N   ALA A 571       6.093 -24.912 -18.553  1.00105.01           N  
ANISOU 3170  N   ALA A 571    20908  11069   7922  -1841    -92  -1125       N  
ATOM   3171  CA  ALA A 571       7.343 -25.549 -18.950  1.00103.60           C  
ANISOU 3171  CA  ALA A 571    21034  10663   7666  -1623    176  -1114       C  
ATOM   3172  C   ALA A 571       7.136 -26.928 -19.562  1.00105.32           C  
ANISOU 3172  C   ALA A 571    21738  10653   7625  -1753    222  -1246       C  
ATOM   3173  O   ALA A 571       7.991 -27.385 -20.328  1.00111.85           O  
ANISOU 3173  O   ALA A 571    22838  11314   8345  -1557    422  -1228       O  
ATOM   3174  CB  ALA A 571       8.284 -25.652 -17.748  1.00111.97           C  
ANISOU 3174  CB  ALA A 571    21917  11662   8964  -1431    349  -1031       C  
ATOM   3175  N   TYR A 572       6.031 -27.601 -19.244  1.00109.82           N  
ANISOU 3175  N   TYR A 572    22302  11227   8199  -2060     53  -1326       N  
ATOM   3176  CA  TYR A 572       5.735 -28.913 -19.806  1.00113.00           C  
ANISOU 3176  CA  TYR A 572    23049  11415   8471  -2220     83  -1397       C  
ATOM   3177  C   TYR A 572       4.767 -28.862 -20.978  1.00108.37           C  
ANISOU 3177  C   TYR A 572    22499  10957   7718  -2462   -113  -1445       C  
ATOM   3178  O   TYR A 572       4.880 -29.681 -21.896  1.00108.81           O  
ANISOU 3178  O   TYR A 572    22903  10824   7614  -2497    -41  -1484       O  
ATOM   3179  CB  TYR A 572       5.162 -29.838 -18.725  1.00111.73           C  
ANISOU 3179  CB  TYR A 572    22905  11160   8386  -2445     47  -1444       C  
ATOM   3180  CG  TYR A 572       6.205 -30.424 -17.799  1.00108.06           C  
ANISOU 3180  CG  TYR A 572    22584  10462   8013  -2196    292  -1409       C  
ATOM   3181  CD1 TYR A 572       6.927 -31.555 -18.161  1.00116.40           C  
ANISOU 3181  CD1 TYR A 572    24070  11199   8958  -2043    516  -1407       C  
ATOM   3182  CD2 TYR A 572       6.467 -29.848 -16.564  1.00109.57           C  
ANISOU 3182  CD2 TYR A 572    22492  10759   8381  -2095    300  -1370       C  
ATOM   3183  CE1 TYR A 572       7.881 -32.094 -17.319  1.00118.89           C  
ANISOU 3183  CE1 TYR A 572    24512  11329   9332  -1771    744  -1360       C  
ATOM   3184  CE2 TYR A 572       7.419 -30.379 -15.715  1.00112.45           C  
ANISOU 3184  CE2 TYR A 572    22974  10942   8808  -1854    519  -1333       C  
ATOM   3185  CZ  TYR A 572       8.122 -31.502 -16.097  1.00118.16           C  
ANISOU 3185  CZ  TYR A 572    24109  11372   9414  -1680    741  -1324       C  
ATOM   3186  OH  TYR A 572       9.071 -32.035 -15.255  1.00123.19           O  
ANISOU 3186  OH  TYR A 572    24859  11857  10090  -1396    964  -1271       O  
ATOM   3187  N   ASP A 573       3.815 -27.919 -20.970  1.00104.56           N  
ANISOU 3187  N   ASP A 573    21674  10802   7251  -2614   -359  -1436       N  
ATOM   3188  CA  ASP A 573       2.828 -27.762 -22.041  1.00100.27           C  
ANISOU 3188  CA  ASP A 573    21106  10458   6535  -2831   -570  -1469       C  
ATOM   3189  C   ASP A 573       2.631 -26.257 -22.240  1.00104.07           C  
ANISOU 3189  C   ASP A 573    21268  11243   7030  -2692   -701  -1392       C  
ATOM   3190  O   ASP A 573       1.659 -25.665 -21.767  1.00111.14           O  
ANISOU 3190  O   ASP A 573    21841  12434   7955  -2829   -914  -1374       O  
ATOM   3191  CB  ASP A 573       1.517 -28.475 -21.704  1.00105.61           C  
ANISOU 3191  CB  ASP A 573    21700  11261   7167  -3247   -771  -1537       C  
ATOM   3192  CG  ASP A 573       0.602 -28.623 -22.907  1.00119.49           C  
ANISOU 3192  CG  ASP A 573    23508  13189   8702  -3495   -958  -1580       C  
ATOM   3193  OD1 ASP A 573       0.766 -27.867 -23.888  1.00109.52           O  
ANISOU 3193  OD1 ASP A 573    22236  12038   7340  -3337   -993  -1548       O  
ATOM   3194  OD2 ASP A 573      -0.284 -29.503 -22.871  1.00132.21           O  
ANISOU 3194  OD2 ASP A 573    25175  14832  10227  -3861  -1069  -1641       O  
ATOM   3195  N   THR A 574       3.574 -25.638 -22.956  1.00106.13           N  
ANISOU 3195  N   THR A 574    21638  11432   7255  -2404   -558  -1330       N  
ATOM   3196  CA  THR A 574       3.551 -24.188 -23.124  1.00103.43           C  
ANISOU 3196  CA  THR A 574    21057  11318   6922  -2239   -638  -1233       C  
ATOM   3197  C   THR A 574       2.334 -23.727 -23.915  1.00107.43           C  
ANISOU 3197  C   THR A 574    21424  12128   7267  -2398   -906  -1234       C  
ATOM   3198  O   THR A 574       1.807 -22.638 -23.661  1.00113.75           O  
ANISOU 3198  O   THR A 574    21951  13187   8081  -2338  -1053  -1157       O  
ATOM   3199  CB  THR A 574       4.834 -23.718 -23.810  1.00105.16           C  
ANISOU 3199  CB  THR A 574    21452  11391   7113  -1930   -409  -1159       C  
ATOM   3200  OG1 THR A 574       5.954 -24.437 -23.279  1.00105.14           O  
ANISOU 3200  OG1 THR A 574    21622  11128   7200  -1788   -149  -1165       O  
ATOM   3201  CG2 THR A 574       5.046 -22.228 -23.580  1.00109.49           C  
ANISOU 3201  CG2 THR A 574    21755  12105   7742  -1745   -429  -1032       C  
ATOM   3202  N   ALA A 575       1.873 -24.535 -24.871  1.00115.43           N  
ANISOU 3202  N   ALA A 575    22630  13123   8107  -2587   -971  -1311       N  
ATOM   3203  CA  ALA A 575       0.745 -24.127 -25.703  1.00116.03           C  
ANISOU 3203  CA  ALA A 575    22565  13524   7996  -2733  -1228  -1307       C  
ATOM   3204  C   ALA A 575      -0.552 -24.097 -24.904  1.00119.97           C  
ANISOU 3204  C   ALA A 575    22720  14348   8514  -2986  -1474  -1316       C  
ATOM   3205  O   ALA A 575      -1.317 -23.130 -24.982  1.00118.02           O  
ANISOU 3205  O   ALA A 575    22187  14456   8200  -2942  -1668  -1239       O  
ATOM   3206  CB  ALA A 575       0.616 -25.063 -26.905  1.00111.99           C  
ANISOU 3206  CB  ALA A 575    22366  12903   7281  -2897  -1230  -1393       C  
ATOM   3207  N   SER A 576      -0.816 -25.151 -24.128  1.00144.49           N  
ANISOU 3207  N   SER A 576    25855  17348  11698  -3238  -1460  -1395       N  
ATOM   3208  CA  SER A 576      -2.085 -25.232 -23.410  1.00142.41           C  
ANISOU 3208  CA  SER A 576    25259  17415  11435  -3518  -1686  -1402       C  
ATOM   3209  C   SER A 576      -2.104 -24.302 -22.204  1.00142.91           C  
ANISOU 3209  C   SER A 576    25006  17622  11672  -3347  -1706  -1318       C  
ATOM   3210  O   SER A 576      -3.150 -23.732 -21.873  1.00146.02           O  
ANISOU 3210  O   SER A 576    25049  18414  12019  -3424  -1920  -1264       O  
ATOM   3211  CB  SER A 576      -2.352 -26.675 -22.982  1.00145.74           C  
ANISOU 3211  CB  SER A 576    25847  17654  11873  -3861  -1647  -1502       C  
ATOM   3212  OG  SER A 576      -2.563 -27.505 -24.111  1.00150.23           O  
ANISOU 3212  OG  SER A 576    26703  18135  12241  -4069  -1670  -1573       O  
ATOM   3213  N   ALA A 577      -0.962 -24.138 -21.535  1.00112.57           N  
ANISOU 3213  N   ALA A 577    21279  13479   8014  -3107  -1484  -1298       N  
ATOM   3214  CA  ALA A 577      -0.913 -23.274 -20.359  1.00103.23           C  
ANISOU 3214  CA  ALA A 577    19831  12395   6998  -2950  -1489  -1222       C  
ATOM   3215  C   ALA A 577      -1.101 -21.811 -20.739  1.00107.32           C  
ANISOU 3215  C   ALA A 577    20079  13150   7548  -2665  -1563  -1078       C  
ATOM   3216  O   ALA A 577      -1.853 -21.084 -20.080  1.00111.16           O  
ANISOU 3216  O   ALA A 577    20185  13913   8139  -2600  -1683   -989       O  
ATOM   3217  CB  ALA A 577       0.407 -23.474 -19.616  1.00 99.54           C  
ANISOU 3217  CB  ALA A 577    19482  11561   6776  -2743  -1213  -1212       C  
ATOM   3218  N   GLU A 578      -0.427 -21.363 -21.800  1.00110.54           N  
ANISOU 3218  N   GLU A 578    20705  13446   7849  -2476  -1480  -1046       N  
ATOM   3219  CA  GLU A 578      -0.571 -19.979 -22.237  1.00110.80           C  
ANISOU 3219  CA  GLU A 578    20554  13664   7880  -2202  -1536   -904       C  
ATOM   3220  C   GLU A 578      -1.946 -19.720 -22.841  1.00113.20           C  
ANISOU 3220  C   GLU A 578    20681  14391   7939  -2315  -1817   -879       C  
ATOM   3221  O   GLU A 578      -2.454 -18.597 -22.760  1.00108.45           O  
ANISOU 3221  O   GLU A 578    19810  14032   7364  -2093  -1906   -745       O  
ATOM   3222  CB  GLU A 578       0.525 -19.632 -23.243  1.00108.25           C  
ANISOU 3222  CB  GLU A 578    20532  13111   7488  -1998  -1362   -873       C  
ATOM   3223  CG  GLU A 578       1.862 -19.285 -22.611  1.00105.48           C  
ANISOU 3223  CG  GLU A 578    20201  12472   7404  -1780  -1097   -814       C  
ATOM   3224  CD  GLU A 578       2.890 -18.842 -23.633  1.00113.86           C  
ANISOU 3224  CD  GLU A 578    21510  13370   8381  -1587   -927   -758       C  
ATOM   3225  OE1 GLU A 578       2.540 -18.747 -24.829  1.00112.73           O  
ANISOU 3225  OE1 GLU A 578    21536  13320   7975  -1598  -1015   -764       O  
ATOM   3226  OE2 GLU A 578       4.049 -18.590 -23.242  1.00118.69           O  
ANISOU 3226  OE2 GLU A 578    22136  13784   9175  -1435   -706   -701       O  
ATOM   3227  N   ARG A 579      -2.563 -20.739 -23.441  1.00132.29           N  
ANISOU 3227  N   ARG A 579    23256  16912  10095  -2656  -1960  -1000       N  
ATOM   3228  CA  ARG A 579      -3.867 -20.546 -24.068  1.00137.81           C  
ANISOU 3228  CA  ARG A 579    23725  18070  10565  -2780  -2233   -964       C  
ATOM   3229  C   ARG A 579      -4.964 -20.350 -23.028  1.00143.53           C  
ANISOU 3229  C   ARG A 579    24015  19171  11348  -2873  -2404   -908       C  
ATOM   3230  O   ARG A 579      -5.811 -19.461 -23.172  1.00145.24           O  
ANISOU 3230  O   ARG A 579    23911  19790  11484  -2709  -2565   -777       O  
ATOM   3231  CB  ARG A 579      -4.191 -21.735 -24.971  1.00139.44           C  
ANISOU 3231  CB  ARG A 579    24092  18260  10630  -3104  -2284  -1089       C  
ATOM   3232  CG  ARG A 579      -5.605 -21.743 -25.522  1.00142.63           C  
ANISOU 3232  CG  ARG A 579    24214  19178  10800  -3311  -2577  -1067       C  
ATOM   3233  CD  ARG A 579      -5.893 -23.047 -26.248  1.00149.33           C  
ANISOU 3233  CD  ARG A 579    25258  19953  11528  -3692  -2611  -1205       C  
ATOM   3234  NE  ARG A 579      -6.048 -24.158 -25.317  1.00158.65           N  
ANISOU 3234  NE  ARG A 579    26452  20986  12840  -4019  -2562  -1299       N  
ATOM   3235  CZ  ARG A 579      -5.872 -25.433 -25.635  1.00156.73           C  
ANISOU 3235  CZ  ARG A 579    26528  20456  12568  -4312  -2479  -1421       C  
ATOM   3236  NH1 ARG A 579      -5.532 -25.799 -26.860  1.00143.79           N  
ANISOU 3236  NH1 ARG A 579    25216  18645  10771  -4327  -2437  -1477       N  
ATOM   3237  NH2 ARG A 579      -6.039 -26.364 -24.700  1.00160.06           N  
ANISOU 3237  NH2 ARG A 579    26964  20743  13107  -4586  -2427  -1481       N  
ATOM   3238  N   ARG A 580      -4.965 -21.167 -21.973  1.00146.95           N  
ANISOU 3238  N   ARG A 580    24407  19486  11941  -3095  -2348   -987       N  
ATOM   3239  CA  ARG A 580      -6.059 -21.133 -21.008  1.00140.92           C  
ANISOU 3239  CA  ARG A 580    23207  19098  11239  -3219  -2496   -937       C  
ATOM   3240  C   ARG A 580      -5.950 -19.960 -20.045  1.00138.25           C  
ANISOU 3240  C   ARG A 580    22549  18800  11180  -2815  -2409   -788       C  
ATOM   3241  O   ARG A 580      -6.976 -19.435 -19.597  1.00141.08           O  
ANISOU 3241  O   ARG A 580    22504  19579  11521  -2751  -2553   -684       O  
ATOM   3242  CB  ARG A 580      -6.111 -22.445 -20.224  1.00139.01           C  
ANISOU 3242  CB  ARG A 580    23068  18699  11049  -3618  -2459  -1072       C  
ATOM   3243  CG  ARG A 580      -6.406 -23.664 -21.084  1.00150.25           C  
ANISOU 3243  CG  ARG A 580    24686  20064  12337  -3984  -2496  -1190       C  
ATOM   3244  CD  ARG A 580      -6.865 -24.841 -20.237  1.00154.43           C  
ANISOU 3244  CD  ARG A 580    25178  20553  12947  -4376  -2488  -1270       C  
ATOM   3245  NE  ARG A 580      -6.667 -26.117 -20.916  1.00158.68           N  
ANISOU 3245  NE  ARG A 580    26083  20792  13417  -4664  -2410  -1388       N  
ATOM   3246  CZ  ARG A 580      -6.788 -27.302 -20.333  1.00161.14           C  
ANISOU 3246  CZ  ARG A 580    26532  20907  13787  -4989  -2336  -1462       C  
ATOM   3247  NH1 ARG A 580      -7.101 -27.414 -19.052  1.00152.80           N  
ANISOU 3247  NH1 ARG A 580    25257  19928  12871  -5083  -2330  -1440       N  
ATOM   3248  NH2 ARG A 580      -6.593 -28.402 -21.054  1.00169.42           N  
ANISOU 3248  NH2 ARG A 580    27972  21663  14735  -5218  -2259  -1551       N  
ATOM   3249  N   LEU A 581      -4.734 -19.535 -19.716  1.00122.14           N  
ANISOU 3249  N   LEU A 581    20685  16346   9375  -2545  -2174   -772       N  
ATOM   3250  CA  LEU A 581      -4.524 -18.475 -18.732  1.00121.15           C  
ANISOU 3250  CA  LEU A 581    20329  16194   9510  -2206  -2076   -651       C  
ATOM   3251  C   LEU A 581      -3.404 -17.566 -19.233  1.00121.69           C  
ANISOU 3251  C   LEU A 581    20621  15962   9652  -1879  -1906   -586       C  
ATOM   3252  O   LEU A 581      -2.226 -17.930 -19.192  1.00119.56           O  
ANISOU 3252  O   LEU A 581    20611  15314   9504  -1884  -1713   -647       O  
ATOM   3253  CB  LEU A 581      -4.245 -19.076 -17.351  1.00121.80           C  
ANISOU 3253  CB  LEU A 581    20338  16099   9843  -2323  -1965   -706       C  
ATOM   3254  CG  LEU A 581      -3.065 -19.995 -16.994  1.00114.31           C  
ANISOU 3254  CG  LEU A 581    19695  14699   9039  -2439  -1761   -819       C  
ATOM   3255  CD1 LEU A 581      -1.859 -19.241 -16.449  1.00115.48           C  
ANISOU 3255  CD1 LEU A 581    19895  14543   9441  -2130  -1548   -756       C  
ATOM   3256  CD2 LEU A 581      -3.523 -21.079 -16.003  1.00102.17           C  
ANISOU 3256  CD2 LEU A 581    18077  13181   7561  -2747  -1784   -903       C  
ATOM   3257  N   SER A 582      -3.785 -16.394 -19.744  1.00114.81           N  
ANISOU 3257  N   SER A 582    19656  15282   8684  -1596  -1974   -454       N  
ATOM   3258  CA  SER A 582      -2.806 -15.417 -20.205  1.00107.97           C  
ANISOU 3258  CA  SER A 582    19003  14149   7870  -1303  -1815   -374       C  
ATOM   3259  C   SER A 582      -3.371 -14.004 -20.173  1.00105.37           C  
ANISOU 3259  C   SER A 582    18517  14015   7505   -950  -1869   -206       C  
ATOM   3260  O   SER A 582      -2.612 -13.030 -20.151  1.00 99.39           O  
ANISOU 3260  O   SER A 582    17907  13014   6843   -703  -1719   -124       O  
ATOM   3261  CB  SER A 582      -2.326 -15.747 -21.617  1.00 97.80           C  
ANISOU 3261  CB  SER A 582    18036  12755   6368  -1369  -1800   -422       C  
ATOM   3262  OG  SER A 582      -1.397 -14.775 -22.054  1.00103.71           O  
ANISOU 3262  OG  SER A 582    18977  13268   7159  -1104  -1640   -331       O  
ATOM   3263  N   GLY A 583      -4.694 -13.881 -20.179  1.00114.03           N  
ANISOU 3263  N   GLY A 583    19328  15554   8443   -925  -2074   -146       N  
ATOM   3264  CA  GLY A 583      -5.337 -12.586 -20.086  1.00123.28           C  
ANISOU 3264  CA  GLY A 583    20348  16939   9553   -540  -2120     26       C  
ATOM   3265  C   GLY A 583      -5.670 -12.216 -18.656  1.00128.75           C  
ANISOU 3265  C   GLY A 583    20794  17675  10449   -413  -2075     73       C  
ATOM   3266  O   GLY A 583      -4.828 -11.676 -17.934  1.00125.28           O  
ANISOU 3266  O   GLY A 583    20489  16885  10228   -283  -1893     85       O  
ATOM   3267  N   THR A 584      -6.898 -12.512 -18.235  1.00136.35           N  
ANISOU 3267  N   THR A 584    21393  19087  11326   -467  -2241    103       N  
ATOM   3268  CA  THR A 584      -7.356 -12.214 -16.882  1.00134.56           C  
ANISOU 3268  CA  THR A 584    20906  18960  11259   -340  -2205    154       C  
ATOM   3269  C   THR A 584      -6.955 -13.265 -15.842  1.00131.36           C  
ANISOU 3269  C   THR A 584    20455  18368  11086   -678  -2133     13       C  
ATOM   3270  O   THR A 584      -6.677 -12.890 -14.696  1.00129.96           O  
ANISOU 3270  O   THR A 584    20239  18021  11119   -550  -2011     31       O  
ATOM   3271  CB  THR A 584      -8.876 -12.019 -16.873  1.00139.82           C  
ANISOU 3271  CB  THR A 584    21164  20247  11714   -215  -2401    276       C  
ATOM   3272  OG1 THR A 584      -9.533 -13.237 -17.243  1.00138.16           O  
ANISOU 3272  OG1 THR A 584    20761  20371  11362   -646  -2583    187       O  
ATOM   3273  CG2 THR A 584      -9.271 -10.924 -17.854  1.00148.59           C  
ANISOU 3273  CG2 THR A 584    22330  21548  12581    185  -2462    438       C  
ATOM   3274  N   PRO A 585      -6.913 -14.570 -16.162  1.00127.02           N  
ANISOU 3274  N   PRO A 585    19941  17826  10494  -1100  -2199   -126       N  
ATOM   3275  CA  PRO A 585      -6.531 -15.539 -15.115  1.00124.45           C  
ANISOU 3275  CA  PRO A 585    19605  17300  10379  -1380  -2113   -244       C  
ATOM   3276  C   PRO A 585      -5.120 -15.337 -14.585  1.00121.72           C  
ANISOU 3276  C   PRO A 585    19527  16433  10288  -1287  -1885   -287       C  
ATOM   3277  O   PRO A 585      -4.919 -15.315 -13.364  1.00124.17           O  
ANISOU 3277  O   PRO A 585    19745  16628  10805  -1260  -1793   -292       O  
ATOM   3278  CB  PRO A 585      -6.696 -16.893 -15.821  1.00128.18           C  
ANISOU 3278  CB  PRO A 585    20178  17831  10694  -1823  -2216   -379       C  
ATOM   3279  CG  PRO A 585      -7.673 -16.630 -16.900  1.00132.31           C  
ANISOU 3279  CG  PRO A 585    20568  18791  10914  -1807  -2424   -309       C  
ATOM   3280  CD  PRO A 585      -7.288 -15.279 -17.400  1.00132.16           C  
ANISOU 3280  CD  PRO A 585    20656  18676  10883  -1357  -2357   -183       C  
ATOM   3281  N   ILE A 586      -4.129 -15.192 -15.470  1.00105.70           N  
ANISOU 3281  N   ILE A 586    17814  14111   8236  -1245  -1792   -311       N  
ATOM   3282  CA  ILE A 586      -2.772 -14.909 -15.012  1.00100.61           C  
ANISOU 3282  CA  ILE A 586    17380  13036   7810  -1154  -1580   -327       C  
ATOM   3283  C   ILE A 586      -2.652 -13.516 -14.409  1.00101.54           C  
ANISOU 3283  C   ILE A 586    17460  13090   8029   -821  -1506   -205       C  
ATOM   3284  O   ILE A 586      -1.729 -13.265 -13.626  1.00 95.48           O  
ANISOU 3284  O   ILE A 586    16778  12036   7464   -784  -1354   -212       O  
ATOM   3285  CB  ILE A 586      -1.754 -15.099 -16.154  1.00103.23           C  
ANISOU 3285  CB  ILE A 586    18038  13116   8067  -1192  -1488   -367       C  
ATOM   3286  CG1 ILE A 586      -0.352 -15.342 -15.585  1.00 98.84           C  
ANISOU 3286  CG1 ILE A 586    17644  12181   7730  -1220  -1276   -411       C  
ATOM   3287  CG2 ILE A 586      -1.746 -13.895 -17.079  1.00102.52           C  
ANISOU 3287  CG2 ILE A 586    18056  13055   7842   -922  -1496   -250       C  
ATOM   3288  CD1 ILE A 586      -0.220 -16.592 -14.752  1.00 91.88           C  
ANISOU 3288  CD1 ILE A 586    16722  11225   6963  -1458  -1243   -521       C  
ATOM   3289  N   SER A 587      -3.562 -12.598 -14.743  1.00119.56           N  
ANISOU 3289  N   SER A 587    19635  15635  10158   -572  -1607    -87       N  
ATOM   3290  CA  SER A 587      -3.521 -11.277 -14.125  1.00119.05           C  
ANISOU 3290  CA  SER A 587    19593  15480  10159   -239  -1526     28       C  
ATOM   3291  C   SER A 587      -3.916 -11.339 -12.656  1.00122.39           C  
ANISOU 3291  C   SER A 587    19794  15965  10742   -226  -1508     23       C  
ATOM   3292  O   SER A 587      -3.408 -10.557 -11.843  1.00115.62           O  
ANISOU 3292  O   SER A 587    19037  14873  10019    -67  -1384     58       O  
ATOM   3293  CB  SER A 587      -4.431 -10.312 -14.884  1.00128.16           C  
ANISOU 3293  CB  SER A 587    20717  16904  11075     76  -1628    168       C  
ATOM   3294  OG  SER A 587      -4.075 -10.250 -16.254  1.00137.96           O  
ANISOU 3294  OG  SER A 587    22174  18090  12153     66  -1646    177       O  
ATOM   3295  N   PHE A 588      -4.814 -12.258 -12.298  1.00123.51           N  
ANISOU 3295  N   PHE A 588    19653  16419  10858   -414  -1627    -22       N  
ATOM   3296  CA  PHE A 588      -5.210 -12.452 -10.909  1.00118.94           C  
ANISOU 3296  CA  PHE A 588    18854  15917  10422   -432  -1606    -30       C  
ATOM   3297  C   PHE A 588      -4.274 -13.391 -10.164  1.00107.17           C  
ANISOU 3297  C   PHE A 588    17446  14125   9147   -713  -1500   -157       C  
ATOM   3298  O   PHE A 588      -4.101 -13.243  -8.948  1.00108.89           O  
ANISOU 3298  O   PHE A 588    17606  14240   9528   -668  -1419   -158       O  
ATOM   3299  CB  PHE A 588      -6.641 -12.994 -10.837  1.00125.83           C  
ANISOU 3299  CB  PHE A 588    19360  17300  11149   -522  -1776     -1       C  
ATOM   3300  CG  PHE A 588      -7.698 -11.933 -10.965  1.00137.11           C  
ANISOU 3300  CG  PHE A 588    20602  19090  12404   -141  -1850    162       C  
ATOM   3301  CD1 PHE A 588      -7.900 -11.279 -12.171  1.00133.03           C  
ANISOU 3301  CD1 PHE A 588    20182  18686  11679     63  -1918    248       C  
ATOM   3302  CD2 PHE A 588      -8.483 -11.581  -9.878  1.00139.46           C  
ANISOU 3302  CD2 PHE A 588    20640  19619  12730     47  -1839    241       C  
ATOM   3303  CE1 PHE A 588      -8.869 -10.302 -12.291  1.00133.48           C  
ANISOU 3303  CE1 PHE A 588    20080  19084  11553    466  -1976    415       C  
ATOM   3304  CE2 PHE A 588      -9.453 -10.602  -9.993  1.00139.37           C  
ANISOU 3304  CE2 PHE A 588    20465  19953  12535    456  -1887    407       C  
ATOM   3305  CZ  PHE A 588      -9.645  -9.963 -11.202  1.00138.38           C  
ANISOU 3305  CZ  PHE A 588    20440  19940  12198    676  -1956    498       C  
ATOM   3306  N   ILE A 589      -3.668 -14.353 -10.865  1.00 78.71           N  
ANISOU 3306  N   ILE A 589    13996  10382   5527   -979  -1494   -257       N  
ATOM   3307  CA  ILE A 589      -2.703 -15.247 -10.230  1.00 76.59           C  
ANISOU 3307  CA  ILE A 589    13839   9822   5440  -1191  -1377   -361       C  
ATOM   3308  C   ILE A 589      -1.500 -14.459  -9.732  1.00 74.54           C  
ANISOU 3308  C   ILE A 589    13744   9227   5349  -1028  -1212   -332       C  
ATOM   3309  O   ILE A 589      -1.021 -14.668  -8.610  1.00 77.23           O  
ANISOU 3309  O   ILE A 589    14053   9426   5865  -1070  -1127   -361       O  
ATOM   3310  CB  ILE A 589      -2.288 -16.362 -11.207  1.00 77.09           C  
ANISOU 3310  CB  ILE A 589    14090   9791   5408  -1448  -1384   -461       C  
ATOM   3311  CG1 ILE A 589      -3.399 -17.405 -11.332  1.00 79.04           C  
ANISOU 3311  CG1 ILE A 589    14189  10327   5514  -1728  -1536   -520       C  
ATOM   3312  CG2 ILE A 589      -0.989 -17.019 -10.758  1.00 75.04           C  
ANISOU 3312  CG2 ILE A 589    14019   9177   5316  -1544  -1216   -534       C  
ATOM   3313  CD1 ILE A 589      -3.118 -18.471 -12.368  1.00 80.12           C  
ANISOU 3313  CD1 ILE A 589    14570  10367   5505  -1989  -1555   -625       C  
ATOM   3314  N   LEU A 590      -0.992 -13.538 -10.556  1.00 83.88           N  
ANISOU 3314  N   LEU A 590    15110  10292   6467   -859  -1169   -271       N  
ATOM   3315  CA  LEU A 590       0.108 -12.685 -10.118  1.00 85.92           C  
ANISOU 3315  CA  LEU A 590    15527  10261   6856   -745  -1023   -232       C  
ATOM   3316  C   LEU A 590      -0.328 -11.741  -9.006  1.00 86.84           C  
ANISOU 3316  C   LEU A 590    15559  10399   7039   -556  -1014   -168       C  
ATOM   3317  O   LEU A 590       0.467 -11.432  -8.112  1.00 88.97           O  
ANISOU 3317  O   LEU A 590    15891  10456   7456   -565   -909   -174       O  
ATOM   3318  CB  LEU A 590       0.667 -11.888 -11.297  1.00 87.55           C  
ANISOU 3318  CB  LEU A 590    15967  10347   6950   -633   -976   -171       C  
ATOM   3319  CG  LEU A 590       1.799 -12.511 -12.120  1.00 86.02           C  
ANISOU 3319  CG  LEU A 590    15949   9978   6756   -783   -881   -219       C  
ATOM   3320  CD1 LEU A 590       3.030 -12.745 -11.254  1.00 87.08           C  
ANISOU 3320  CD1 LEU A 590    16108   9893   7087   -880   -735   -247       C  
ATOM   3321  CD2 LEU A 590       1.360 -13.799 -12.793  1.00 83.29           C  
ANISOU 3321  CD2 LEU A 590    15575   9766   6305   -960   -964   -308       C  
ATOM   3322  N   LEU A 591      -1.579 -11.275  -9.045  1.00 82.53           N  
ANISOU 3322  N   LEU A 591    14871  10120   6365   -374  -1120   -101       N  
ATOM   3323  CA  LEU A 591      -2.073 -10.390  -7.996  1.00 83.97           C  
ANISOU 3323  CA  LEU A 591    14994  10330   6579   -147  -1096    -35       C  
ATOM   3324  C   LEU A 591      -2.107 -11.100  -6.649  1.00 89.43           C  
ANISOU 3324  C   LEU A 591    15511  11033   7436   -291  -1074   -101       C  
ATOM   3325  O   LEU A 591      -1.837 -10.490  -5.608  1.00 90.08           O  
ANISOU 3325  O   LEU A 591    15647  10967   7613   -189   -995    -85       O  
ATOM   3326  CB  LEU A 591      -3.460  -9.866  -8.368  1.00 87.30           C  
ANISOU 3326  CB  LEU A 591    15263  11103   6803    111  -1209     66       C  
ATOM   3327  CG  LEU A 591      -4.256  -9.141  -7.282  1.00 85.11           C  
ANISOU 3327  CG  LEU A 591    14872  10948   6519    382  -1192    142       C  
ATOM   3328  CD1 LEU A 591      -3.787  -7.701  -7.144  1.00 89.67           C  
ANISOU 3328  CD1 LEU A 591    15777  11230   7064    671  -1076    219       C  
ATOM   3329  CD2 LEU A 591      -5.745  -9.199  -7.583  1.00 83.74           C  
ANISOU 3329  CD2 LEU A 591    14394  11267   6157    547  -1327    229       C  
ATOM   3330  N   LEU A 592      -2.432 -12.395  -6.651  1.00 93.52           N  
ANISOU 3330  N   LEU A 592    15852  11710   7973   -538  -1141   -177       N  
ATOM   3331  CA  LEU A 592      -2.415 -13.165  -5.412  1.00 86.13           C  
ANISOU 3331  CA  LEU A 592    14777  10763   7184   -692  -1110   -237       C  
ATOM   3332  C   LEU A 592      -1.000 -13.291  -4.861  1.00 82.91           C  
ANISOU 3332  C   LEU A 592    14545  10007   6949   -789   -980   -290       C  
ATOM   3333  O   LEU A 592      -0.798 -13.271  -3.642  1.00 93.35           O  
ANISOU 3333  O   LEU A 592    15820  11253   8394   -789   -925   -302       O  
ATOM   3334  CB  LEU A 592      -3.023 -14.547  -5.646  1.00 90.37           C  
ANISOU 3334  CB  LEU A 592    15154  11508   7674   -969  -1200   -306       C  
ATOM   3335  CG  LEU A 592      -3.684 -15.217  -4.442  1.00 91.27           C  
ANISOU 3335  CG  LEU A 592    15044  11777   7857  -1085  -1214   -327       C  
ATOM   3336  CD1 LEU A 592      -4.965 -14.493  -4.061  1.00 92.39           C  
ANISOU 3336  CD1 LEU A 592    14936  12266   7901   -867  -1283   -226       C  
ATOM   3337  CD2 LEU A 592      -3.955 -16.686  -4.729  1.00 91.44           C  
ANISOU 3337  CD2 LEU A 592    15022  11886   7835  -1435  -1273   -413       C  
ATOM   3338  N   SER A 593      -0.008 -13.419  -5.745  1.00 90.77           N  
ANISOU 3338  N   SER A 593    15729  10818   7942   -867   -928   -312       N  
ATOM   3339  CA  SER A 593       1.372 -13.555  -5.293  1.00 94.57           C  
ANISOU 3339  CA  SER A 593    16333  11035   8565   -954   -805   -342       C  
ATOM   3340  C   SER A 593       1.905 -12.254  -4.708  1.00 96.85           C  
ANISOU 3340  C   SER A 593    16733  11164   8903   -813   -736   -282       C  
ATOM   3341  O   SER A 593       2.823 -12.281  -3.880  1.00 98.66           O  
ANISOU 3341  O   SER A 593    16989  11242   9254   -889   -657   -299       O  
ATOM   3342  CB  SER A 593       2.259 -14.021  -6.448  1.00 98.77           C  
ANISOU 3342  CB  SER A 593    17020  11455   9054  -1050   -754   -365       C  
ATOM   3343  OG  SER A 593       2.690 -12.925  -7.238  1.00 98.72           O  
ANISOU 3343  OG  SER A 593    17177  11357   8977   -929   -719   -297       O  
ATOM   3344  N   TYR A 594       1.351 -11.114  -5.119  1.00129.07           N  
ANISOU 3344  N   TYR A 594    20900  15272  12868   -611   -765   -210       N  
ATOM   3345  CA  TYR A 594       1.793  -9.825  -4.606  1.00129.47           C  
ANISOU 3345  CA  TYR A 594    21135  15131  12926   -487   -694   -156       C  
ATOM   3346  C   TYR A 594       1.099  -9.427  -3.313  1.00130.23           C  
ANISOU 3346  C   TYR A 594    21157  15273  13051   -358   -703   -147       C  
ATOM   3347  O   TYR A 594       1.632  -8.594  -2.572  1.00130.19           O  
ANISOU 3347  O   TYR A 594    21319  15071  13078   -327   -634   -133       O  
ATOM   3348  CB  TYR A 594       1.579  -8.737  -5.662  1.00131.93           C  
ANISOU 3348  CB  TYR A 594    21653  15400  13073   -302   -695    -74       C  
ATOM   3349  CG  TYR A 594       2.616  -8.762  -6.761  1.00134.71           C  
ANISOU 3349  CG  TYR A 594    22164  15616  13402   -427   -638    -68       C  
ATOM   3350  CD1 TYR A 594       3.968  -8.693  -6.460  1.00132.26           C  
ANISOU 3350  CD1 TYR A 594    21952  15106  13195   -605   -535    -81       C  
ATOM   3351  CD2 TYR A 594       2.245  -8.862  -8.095  1.00136.02           C  
ANISOU 3351  CD2 TYR A 594    22367  15886  13429   -369   -688    -41       C  
ATOM   3352  CE1 TYR A 594       4.924  -8.719  -7.454  1.00131.88           C  
ANISOU 3352  CE1 TYR A 594    22022  14971  13116   -711   -466    -61       C  
ATOM   3353  CE2 TYR A 594       3.196  -8.888  -9.099  1.00140.15           C  
ANISOU 3353  CE2 TYR A 594    23043  16289  13920   -471   -620    -31       C  
ATOM   3354  CZ  TYR A 594       4.534  -8.816  -8.771  1.00142.83           C  
ANISOU 3354  CZ  TYR A 594    23465  16436  14367   -636   -502    -38       C  
ATOM   3355  OH  TYR A 594       5.489  -8.842  -9.760  1.00153.76           O  
ANISOU 3355  OH  TYR A 594    24974  17737  15709   -729   -420    -13       O  
ATOM   3356  N   THR A 595      -0.072  -9.999  -3.023  1.00 90.81           N  
ANISOU 3356  N   THR A 595    15927  10545   8033   -299   -782   -153       N  
ATOM   3357  CA  THR A 595      -0.730  -9.748  -1.747  1.00 89.47           C  
ANISOU 3357  CA  THR A 595    15659  10447   7890   -177   -776   -142       C  
ATOM   3358  C   THR A 595       0.058 -10.329  -0.579  1.00 90.41           C  
ANISOU 3358  C   THR A 595    15745  10430   8176   -370   -721   -212       C  
ATOM   3359  O   THR A 595      -0.077  -9.844   0.550  1.00 89.87           O  
ANISOU 3359  O   THR A 595    15703  10309   8133   -278   -684   -205       O  
ATOM   3360  CB  THR A 595      -2.150 -10.324  -1.773  1.00 86.98           C  
ANISOU 3360  CB  THR A 595    15050  10503   7497   -107   -871   -119       C  
ATOM   3361  OG1 THR A 595      -2.833  -9.857  -2.943  1.00 83.92           O  
ANISOU 3361  OG1 THR A 595    14667  10284   6935     64   -937    -46       O  
ATOM   3362  CG2 THR A 595      -2.939  -9.891  -0.545  1.00 94.48           C  
ANISOU 3362  CG2 THR A 595    15900  11561   8437     88   -847    -81       C  
ATOM   3363  N   SER A 596       0.897 -11.337  -0.832  1.00 96.14           N  
ANISOU 3363  N   SER A 596    16434  11097   8996   -612   -708   -271       N  
ATOM   3364  CA  SER A 596       1.681 -11.956   0.231  1.00100.71           C  
ANISOU 3364  CA  SER A 596    16972  11575   9717   -770   -658   -323       C  
ATOM   3365  C   SER A 596       2.634 -10.976   0.905  1.00 97.76           C  
ANISOU 3365  C   SER A 596    16783  10981   9382   -762   -589   -307       C  
ATOM   3366  O   SER A 596       3.048 -11.218   2.044  1.00101.87           O  
ANISOU 3366  O   SER A 596    17262  11453   9990   -838   -562   -336       O  
ATOM   3367  CB  SER A 596       2.474 -13.138  -0.326  1.00100.15           C  
ANISOU 3367  CB  SER A 596    16874  11474   9706   -971   -637   -369       C  
ATOM   3368  OG  SER A 596       3.634 -12.691  -1.007  1.00 96.34           O  
ANISOU 3368  OG  SER A 596    16552  10832   9222  -1010   -577   -349       O  
ATOM   3369  N   SER A 597       2.993  -9.882   0.232  1.00100.89           N  
ANISOU 3369  N   SER A 597    17396  11241   9695   -692   -563   -262       N  
ATOM   3370  CA  SER A 597       3.928  -8.927   0.815  1.00107.47           C  
ANISOU 3370  CA  SER A 597    18441  11856  10536   -748   -502   -250       C  
ATOM   3371  C   SER A 597       3.279  -8.064   1.890  1.00109.32           C  
ANISOU 3371  C   SER A 597    18784  12033  10718   -586   -495   -241       C  
ATOM   3372  O   SER A 597       3.975  -7.582   2.790  1.00110.64           O  
ANISOU 3372  O   SER A 597    19084  12046  10907   -683   -459   -258       O  
ATOM   3373  CB  SER A 597       4.523  -8.036  -0.276  1.00107.57           C  
ANISOU 3373  CB  SER A 597    18692  11723  10457   -758   -464   -200       C  
ATOM   3374  OG  SER A 597       3.505  -7.395  -1.025  1.00110.02           O  
ANISOU 3374  OG  SER A 597    19102  12071  10630   -520   -491   -150       O  
ATOM   3375  N   CYS A 598       1.963  -7.858   1.820  1.00100.46           N  
ANISOU 3375  N   CYS A 598    17610  11052   9509   -336   -527   -210       N  
ATOM   3376  CA  CYS A 598       1.284  -6.980   2.763  1.00 99.50           C  
ANISOU 3376  CA  CYS A 598    17619  10881   9305   -115   -498   -188       C  
ATOM   3377  C   CYS A 598       0.539  -7.721   3.863  1.00 97.56           C  
ANISOU 3377  C   CYS A 598    17119  10827   9122    -76   -517   -215       C  
ATOM   3378  O   CYS A 598       0.161  -7.094   4.857  1.00103.60           O  
ANISOU 3378  O   CYS A 598    17995  11536   9833     79   -477   -208       O  
ATOM   3379  CB  CYS A 598       0.293  -6.067   2.030  1.00 95.72           C  
ANISOU 3379  CB  CYS A 598    17272  10448   8648    212   -497   -104       C  
ATOM   3380  SG  CYS A 598      -1.149  -6.917   1.346  1.00 96.14           S  
ANISOU 3380  SG  CYS A 598    16941  10930   8656    371   -589    -62       S  
ATOM   3381  N   VAL A 599       0.320  -9.031   3.718  1.00102.43           N  
ANISOU 3381  N   VAL A 599    17433  11654   9833   -217   -568   -246       N  
ATOM   3382  CA  VAL A 599      -0.466  -9.752   4.714  1.00103.10           C  
ANISOU 3382  CA  VAL A 599    17280  11932   9960   -197   -580   -261       C  
ATOM   3383  C   VAL A 599       0.314  -9.930   6.010  1.00105.83           C  
ANISOU 3383  C   VAL A 599    17675  12130  10404   -333   -538   -312       C  
ATOM   3384  O   VAL A 599      -0.283 -10.040   7.088  1.00106.59           O  
ANISOU 3384  O   VAL A 599    17687  12312  10500   -252   -519   -314       O  
ATOM   3385  CB  VAL A 599      -0.939 -11.106   4.154  1.00 99.47           C  
ANISOU 3385  CB  VAL A 599    16536  11713   9545   -348   -643   -279       C  
ATOM   3386  CG1 VAL A 599      -1.929 -10.895   3.020  1.00104.85           C  
ANISOU 3386  CG1 VAL A 599    17132  12611  10095   -202   -705   -221       C  
ATOM   3387  CG2 VAL A 599       0.248 -11.932   3.685  1.00102.83           C  
ANISOU 3387  CG2 VAL A 599    16992  12003  10075   -612   -639   -334       C  
ATOM   3388  N   ASN A 600       1.650  -9.962   5.939  1.00106.48           N  
ANISOU 3388  N   ASN A 600    17879  12021  10558   -537   -521   -346       N  
ATOM   3389  CA  ASN A 600       2.433 -10.130   7.163  1.00104.57           C  
ANISOU 3389  CA  ASN A 600    17662  11679  10389   -671   -497   -385       C  
ATOM   3390  C   ASN A 600       2.318  -8.925   8.089  1.00107.16           C  
ANISOU 3390  C   ASN A 600    18232  11859  10625   -543   -461   -382       C  
ATOM   3391  O   ASN A 600       2.120  -9.125   9.301  1.00105.28           O  
ANISOU 3391  O   ASN A 600    17951  11647  10405   -528   -447   -405       O  
ATOM   3392  CB  ASN A 600       3.890 -10.451   6.814  1.00100.45           C  
ANISOU 3392  CB  ASN A 600    17169  11055   9942   -908   -490   -400       C  
ATOM   3393  CG  ASN A 600       4.042 -11.786   6.115  1.00106.36           C  
ANISOU 3393  CG  ASN A 600    17715  11927  10770  -1011   -503   -410       C  
ATOM   3394  OD1 ASN A 600       3.219 -12.686   6.287  1.00107.54           O  
ANISOU 3394  OD1 ASN A 600    17696  12221  10945   -987   -521   -424       O  
ATOM   3395  ND2 ASN A 600       5.097 -11.922   5.320  1.00115.00           N  
ANISOU 3395  ND2 ASN A 600    18845  12962  11886  -1135   -484   -399       N  
ATOM   3396  N   PRO A 601       2.435  -7.675   7.621  1.00100.60           N  
ANISOU 3396  N   PRO A 601    17695  10850   9677   -449   -435   -355       N  
ATOM   3397  CA  PRO A 601       2.204  -6.546   8.537  1.00 96.99           C  
ANISOU 3397  CA  PRO A 601    17532  10222   9098   -304   -387   -358       C  
ATOM   3398  C   PRO A 601       0.795  -6.496   9.101  1.00 98.01           C  
ANISOU 3398  C   PRO A 601    17575  10510   9156     11   -361   -328       C  
ATOM   3399  O   PRO A 601       0.612  -6.044  10.239  1.00 93.92           O  
ANISOU 3399  O   PRO A 601    17203   9908   8573    104   -316   -347       O  
ATOM   3400  CB  PRO A 601       2.502  -5.326   7.656  1.00 98.17           C  
ANISOU 3400  CB  PRO A 601    18034  10148   9118   -254   -357   -323       C  
ATOM   3401  CG  PRO A 601       3.498  -5.829   6.680  1.00 97.73           C  
ANISOU 3401  CG  PRO A 601    17873  10103   9156   -515   -389   -324       C  
ATOM   3402  CD  PRO A 601       3.009  -7.209   6.344  1.00 99.65           C  
ANISOU 3402  CD  PRO A 601    17716  10625   9521   -513   -436   -328       C  
ATOM   3403  N   ILE A 602      -0.209  -6.942   8.342  1.00101.43           N  
ANISOU 3403  N   ILE A 602    17766  11192   9579    173   -385   -278       N  
ATOM   3404  CA  ILE A 602      -1.582  -6.921   8.839  1.00105.87           C  
ANISOU 3404  CA  ILE A 602    18183  11983  10059    471   -358   -228       C  
ATOM   3405  C   ILE A 602      -1.739  -7.868  10.023  1.00105.46           C  
ANISOU 3405  C   ILE A 602    17897  12068  10106    360   -356   -266       C  
ATOM   3406  O   ILE A 602      -2.472  -7.576  10.976  1.00108.52           O  
ANISOU 3406  O   ILE A 602    18291  12525  10415    569   -299   -245       O  
ATOM   3407  CB  ILE A 602      -2.569  -7.262   7.707  1.00104.32           C  
ANISOU 3407  CB  ILE A 602    17732  12084   9819    611   -406   -158       C  
ATOM   3408  CG1 ILE A 602      -2.366  -6.324   6.518  1.00 93.97           C  
ANISOU 3408  CG1 ILE A 602    16675  10627   8401    731   -406   -113       C  
ATOM   3409  CG2 ILE A 602      -4.006  -7.182   8.204  1.00108.98           C  
ANISOU 3409  CG2 ILE A 602    18129  12978  10300    929   -376    -82       C  
ATOM   3410  CD1 ILE A 602      -2.599  -4.868   6.844  1.00103.96           C  
ANISOU 3410  CD1 ILE A 602    18338  11677   9484   1054   -315    -66       C  
ATOM   3411  N   ILE A 603      -1.050  -9.010   9.987  1.00 98.99           N  
ANISOU 3411  N   ILE A 603    16889  11281   9441     51   -405   -316       N  
ATOM   3412  CA  ILE A 603      -1.156  -9.970  11.081  1.00100.03           C  
ANISOU 3412  CA  ILE A 603    16825  11523   9658    -61   -398   -346       C  
ATOM   3413  C   ILE A 603      -0.467  -9.436  12.332  1.00103.94           C  
ANISOU 3413  C   ILE A 603    17550  11804  10137    -88   -357   -388       C  
ATOM   3414  O   ILE A 603      -0.957  -9.626  13.451  1.00107.85           O  
ANISOU 3414  O   ILE A 603    17987  12376  10614    -12   -319   -390       O  
ATOM   3415  CB  ILE A 603      -0.589 -11.334  10.647  1.00 93.80           C  
ANISOU 3415  CB  ILE A 603    15831  10799   9011   -349   -448   -379       C  
ATOM   3416  CG1 ILE A 603      -1.467 -11.940   9.549  1.00 98.05           C  
ANISOU 3416  CG1 ILE A 603    16147  11574   9532   -342   -493   -345       C  
ATOM   3417  CG2 ILE A 603      -0.491 -12.283  11.832  1.00 89.16           C  
ANISOU 3417  CG2 ILE A 603    15114  10261   8500   -473   -429   -406       C  
ATOM   3418  CD1 ILE A 603      -0.816 -13.075   8.797  1.00 93.25           C  
ANISOU 3418  CD1 ILE A 603    15454  10956   9021   -602   -532   -382       C  
ATOM   3419  N   TYR A 604       0.670  -8.752  12.165  1.00 98.53           N  
ANISOU 3419  N   TYR A 604    17132  10863   9442   -216   -366   -421       N  
ATOM   3420  CA  TYR A 604       1.353  -8.158  13.312  1.00 92.15           C  
ANISOU 3420  CA  TYR A 604    16569   9857   8586   -283   -344   -465       C  
ATOM   3421  C   TYR A 604       0.436  -7.201  14.063  1.00 99.66           C  
ANISOU 3421  C   TYR A 604    17737  10754   9375     18   -271   -450       C  
ATOM   3422  O   TYR A 604       0.453  -7.152  15.299  1.00108.09           O  
ANISOU 3422  O   TYR A 604    18883  11781  10406     27   -242   -481       O  
ATOM   3423  CB  TYR A 604       2.615  -7.422  12.861  1.00 90.53           C  
ANISOU 3423  CB  TYR A 604    16628   9413   8356   -487   -368   -488       C  
ATOM   3424  CG  TYR A 604       3.643  -8.281  12.164  1.00 87.51           C  
ANISOU 3424  CG  TYR A 604    16048   9091   8110   -756   -420   -491       C  
ATOM   3425  CD1 TYR A 604       3.684  -9.655  12.359  1.00 88.38           C  
ANISOU 3425  CD1 TYR A 604    15842   9387   8351   -843   -442   -494       C  
ATOM   3426  CD2 TYR A 604       4.574  -7.712  11.306  1.00 93.67           C  
ANISOU 3426  CD2 TYR A 604    16983   9737   8869   -912   -432   -482       C  
ATOM   3427  CE1 TYR A 604       4.627 -10.438  11.718  1.00 90.34           C  
ANISOU 3427  CE1 TYR A 604    15946   9680   8699  -1036   -468   -488       C  
ATOM   3428  CE2 TYR A 604       5.517  -8.484  10.662  1.00 95.74           C  
ANISOU 3428  CE2 TYR A 604    17060  10078   9238  -1120   -461   -472       C  
ATOM   3429  CZ  TYR A 604       5.540  -9.845  10.871  1.00 92.35           C  
ANISOU 3429  CZ  TYR A 604    16329   9829   8931  -1161   -475   -475       C  
ATOM   3430  OH  TYR A 604       6.481 -10.612  10.227  1.00 97.29           O  
ANISOU 3430  OH  TYR A 604    16804  10523   9639  -1318   -483   -457       O  
ATOM   3431  N   CYS A 605      -0.371  -6.431  13.331  1.00106.13           N  
ANISOU 3431  N   CYS A 605    18667  11578  10078    294   -233   -394       N  
ATOM   3432  CA  CYS A 605      -1.277  -5.485  13.972  1.00111.83           C  
ANISOU 3432  CA  CYS A 605    19618  12254  10618    651   -140   -363       C  
ATOM   3433  C   CYS A 605      -2.395  -6.212  14.707  1.00119.37           C  
ANISOU 3433  C   CYS A 605    20246  13524  11586    827   -104   -324       C  
ATOM   3434  O   CYS A 605      -2.685  -5.911  15.870  1.00129.22           O  
ANISOU 3434  O   CYS A 605    21623  14730  12745    964    -33   -337       O  
ATOM   3435  CB  CYS A 605      -1.854  -4.524  12.932  1.00115.00           C  
ANISOU 3435  CB  CYS A 605    20209  12609  10877    943   -102   -291       C  
ATOM   3436  SG  CYS A 605      -0.664  -3.330  12.276  1.00113.32           S  
ANISOU 3436  SG  CYS A 605    20521  11960  10576    782   -101   -325       S  
ATOM   3437  N   PHE A 606      -3.017  -7.194  14.052  1.00117.37           N  
ANISOU 3437  N   PHE A 606    19578  13589  11429    798   -149   -279       N  
ATOM   3438  CA  PHE A 606      -4.198  -7.869  14.585  1.00123.66           C  
ANISOU 3438  CA  PHE A 606    20034  14735  12216    942   -114   -222       C  
ATOM   3439  C   PHE A 606      -3.897  -8.688  15.837  1.00127.08           C  
ANISOU 3439  C   PHE A 606    20367  15179  12738    750   -103   -273       C  
ATOM   3440  O   PHE A 606      -4.804  -9.299  16.413  1.00131.19           O  
ANISOU 3440  O   PHE A 606    20619  15976  13251    825    -63   -228       O  
ATOM   3441  CB  PHE A 606      -4.816  -8.772  13.515  1.00123.38           C  
ANISOU 3441  CB  PHE A 606    19606  15024  12250    860   -185   -172       C  
ATOM   3442  CG  PHE A 606      -5.863  -8.097  12.674  1.00127.35           C  
ANISOU 3442  CG  PHE A 606    20049  15736  12603   1197   -170    -70       C  
ATOM   3443  CD1 PHE A 606      -5.556  -6.989  11.904  1.00127.30           C  
ANISOU 3443  CD1 PHE A 606    20364  15507  12498   1369   -162    -54       C  
ATOM   3444  CD2 PHE A 606      -7.161  -8.579  12.657  1.00130.97           C  
ANISOU 3444  CD2 PHE A 606    20122  16638  13002   1339   -163     22       C  
ATOM   3445  CE1 PHE A 606      -6.524  -6.373  11.132  1.00129.52           C  
ANISOU 3445  CE1 PHE A 606    20597  15994  12622   1719   -145     55       C  
ATOM   3446  CE2 PHE A 606      -8.136  -7.969  11.886  1.00133.57           C  
ANISOU 3446  CE2 PHE A 606    20356  17220  13173   1672   -157    135       C  
ATOM   3447  CZ  PHE A 606      -7.815  -6.862  11.122  1.00130.69           C  
ANISOU 3447  CZ  PHE A 606    20328  16621  12709   1885   -147    153       C  
ATOM   3448  N   MET A 607      -2.635  -8.716  16.269  1.00144.63           N  
ANISOU 3448  N   MET A 607    22791  17131  15032    497   -137   -356       N  
ATOM   3449  CA  MET A 607      -2.288  -9.464  17.471  1.00146.89           C  
ANISOU 3449  CA  MET A 607    23003  17426  15384    334   -131   -397       C  
ATOM   3450  C   MET A 607      -2.541  -8.651  18.736  1.00155.45           C  
ANISOU 3450  C   MET A 607    24346  18400  16318    540    -45   -409       C  
ATOM   3451  O   MET A 607      -2.986  -9.200  19.750  1.00161.50           O  
ANISOU 3451  O   MET A 607    24978  19303  17081    570      1   -399       O  
ATOM   3452  CB  MET A 607      -0.826  -9.913  17.410  1.00145.24           C  
ANISOU 3452  CB  MET A 607    22852  17037  15295     -9   -210   -462       C  
ATOM   3453  CG  MET A 607      -0.513 -10.875  16.277  1.00140.00           C  
ANISOU 3453  CG  MET A 607    21950  16472  14771   -206   -276   -453       C  
ATOM   3454  SD  MET A 607      -1.079 -12.556  16.590  1.00150.75           S  
ANISOU 3454  SD  MET A 607    22942  18094  16241   -333   -273   -431       S  
ATOM   3455  CE  MET A 607      -2.401 -12.702  15.388  1.00142.63           C  
ANISOU 3455  CE  MET A 607    21681  17333  15179   -213   -281   -368       C  
ATOM   3456  N   ASN A 608      -2.270  -7.348  18.700  1.00153.91           N  
ANISOU 3456  N   ASN A 608    24556  17943  15981    679    -14   -431       N  
ATOM   3457  CA  ASN A 608      -2.340  -6.498  19.888  1.00151.27           C  
ANISOU 3457  CA  ASN A 608    24571  17429  15474    846     68   -462       C  
ATOM   3458  C   ASN A 608      -3.369  -5.386  19.681  1.00159.38           C  
ANISOU 3458  C   ASN A 608    25821  18440  16298   1294    182   -398       C  
ATOM   3459  O   ASN A 608      -3.070  -4.340  19.100  1.00161.55           O  
ANISOU 3459  O   ASN A 608    26462  18457  16461   1375    194   -407       O  
ATOM   3460  CB  ASN A 608      -0.950  -5.935  20.235  1.00150.31           C  
ANISOU 3460  CB  ASN A 608    24823  16965  15322    563      7   -556       C  
ATOM   3461  CG  ASN A 608      -0.236  -5.347  19.031  1.00157.22           C  
ANISOU 3461  CG  ASN A 608    25870  17657  16209    427    -49   -566       C  
ATOM   3462  OD1 ASN A 608      -0.770  -5.325  17.924  1.00160.32           O  
ANISOU 3462  OD1 ASN A 608    26132  18155  16629    567    -44   -506       O  
ATOM   3463  ND2 ASN A 608       0.982  -4.863  19.247  1.00156.77           N  
ANISOU 3463  ND2 ASN A 608    26102  17347  16118    136   -107   -635       N  
ATOM   3464  N   LYS A 609      -4.589  -5.630  20.160  1.00164.47           N  
ANISOU 3464  N   LYS A 609    26240  19372  16878   1595    276   -321       N  
ATOM   3465  CA  LYS A 609      -5.652  -4.642  20.340  1.00170.09           C  
ANISOU 3465  CA  LYS A 609    27147  20121  17359   2099    419   -244       C  
ATOM   3466  C   LYS A 609      -6.080  -3.944  19.048  1.00175.95           C  
ANISOU 3466  C   LYS A 609    27950  20881  18023   2347    427   -168       C  
ATOM   3467  O   LYS A 609      -6.902  -3.019  19.097  1.00179.25           O  
ANISOU 3467  O   LYS A 609    28578  21305  18222   2815    554    -90       O  
ATOM   3468  CB  LYS A 609      -5.263  -3.607  21.412  1.00156.47           C  
ANISOU 3468  CB  LYS A 609    25996  18021  15435   2218    508   -315       C  
ATOM   3469  CG  LYS A 609      -4.605  -2.327  20.912  1.00163.14           C  
ANISOU 3469  CG  LYS A 609    27419  18431  16134   2244    514   -363       C  
ATOM   3470  CD  LYS A 609      -4.288  -1.395  22.071  1.00164.91           C  
ANISOU 3470  CD  LYS A 609    28232  18292  16135   2324    603   -442       C  
ATOM   3471  CE  LYS A 609      -3.609  -0.121  21.597  1.00161.30           C  
ANISOU 3471  CE  LYS A 609    28408  17369  15509   2291    613   -494       C  
ATOM   3472  NZ  LYS A 609      -3.180   0.728  22.742  1.00141.34           N  
ANISOU 3472  NZ  LYS A 609    26496  14455  12750   2272    679   -592       N  
ATOM   3473  N   ARG A 610      -5.580  -4.372  17.885  1.00169.64           N  
ANISOU 3473  N   ARG A 610    26974  20103  17377   2081    304   -177       N  
ATOM   3474  CA  ARG A 610      -6.096  -3.817  16.636  1.00167.82           C  
ANISOU 3474  CA  ARG A 610    26748  19949  17067   2329    307    -90       C  
ATOM   3475  C   ARG A 610      -7.551  -4.209  16.413  1.00175.57           C  
ANISOU 3475  C   ARG A 610    27276  21438  17993   2655    350     47       C  
ATOM   3476  O   ARG A 610      -8.283  -3.498  15.716  1.00177.86           O  
ANISOU 3476  O   ARG A 610    27613  21841  18126   3039    400    152       O  
ATOM   3477  CB  ARG A 610      -5.241  -4.266  15.453  1.00157.69           C  
ANISOU 3477  CB  ARG A 610    25361  18599  15955   1960    169   -130       C  
ATOM   3478  CG  ARG A 610      -5.433  -3.435  14.191  1.00152.73           C  
ANISOU 3478  CG  ARG A 610    24909  17905  15218   2176    171    -63       C  
ATOM   3479  CD  ARG A 610      -4.953  -2.006  14.384  1.00153.92           C  
ANISOU 3479  CD  ARG A 610    25714  17594  15174   2339    259    -91       C  
ATOM   3480  NE  ARG A 610      -3.532  -1.942  14.700  1.00150.42           N  
ANISOU 3480  NE  ARG A 610    25551  16787  14816   1894    200   -216       N  
ATOM   3481  CZ  ARG A 610      -2.920  -0.872  15.189  1.00145.49           C  
ANISOU 3481  CZ  ARG A 610    25505  15741  14034   1881    260   -274       C  
ATOM   3482  NH1 ARG A 610      -3.580   0.248  15.435  1.00150.65           N  
ANISOU 3482  NH1 ARG A 610    26587  16223  14431   2316    397   -226       N  
ATOM   3483  NH2 ARG A 610      -1.616  -0.928  15.440  1.00134.94           N  
ANISOU 3483  NH2 ARG A 610    24333  14159  12779   1420    185   -377       N  
ATOM   3484  N   PHE A 611      -7.985  -5.328  16.996  1.00186.12           N  
ANISOU 3484  N   PHE A 611    28173  23103  19440   2503    334     59       N  
ATOM   3485  CA  PHE A 611      -9.386  -5.727  16.938  1.00189.61           C  
ANISOU 3485  CA  PHE A 611    28157  24076  19811   2764    380    195       C  
ATOM   3486  C   PHE A 611     -10.300  -4.788  17.715  1.00193.33           C  
ANISOU 3486  C   PHE A 611    28795  24629  20031   3317    558    290       C  
ATOM   3487  O   PHE A 611     -11.524  -4.903  17.592  1.00192.33           O  
ANISOU 3487  O   PHE A 611    28297  24983  19798   3619    614    434       O  
ATOM   3488  CB  PHE A 611      -9.540  -7.161  17.453  1.00186.89           C  
ANISOU 3488  CB  PHE A 611    27362  24014  19634   2408    330    178       C  
ATOM   3489  CG  PHE A 611      -8.848  -7.416  18.764  1.00189.18           C  
ANISOU 3489  CG  PHE A 611    27844  24051  19983   2223    369     79       C  
ATOM   3490  CD1 PHE A 611      -9.490  -7.168  19.965  1.00193.20           C  
ANISOU 3490  CD1 PHE A 611    28386  24663  20359   2495    509    122       C  
ATOM   3491  CD2 PHE A 611      -7.554  -7.915  18.792  1.00183.42           C  
ANISOU 3491  CD2 PHE A 611    27252  23010  19428   1795    268    -46       C  
ATOM   3492  CE1 PHE A 611      -8.854  -7.404  21.170  1.00187.03           C  
ANISOU 3492  CE1 PHE A 611    27791  23657  19616   2324    537     32       C  
ATOM   3493  CE2 PHE A 611      -6.913  -8.153  19.993  1.00184.60           C  
ANISOU 3493  CE2 PHE A 611    27560  22965  19614   1634    292   -126       C  
ATOM   3494  CZ  PHE A 611      -7.564  -7.898  21.183  1.00184.34           C  
ANISOU 3494  CZ  PHE A 611    27576  23017  19446   1890    420    -91       C  
ATOM   3495  N   ARG A 612      -9.740  -3.872  18.511  1.00220.82           N  
ANISOU 3495  N   ARG A 612    32830  27673  23400   3453    652    217       N  
ATOM   3496  CA  ARG A 612     -10.555  -2.859  19.171  1.00226.12           C  
ANISOU 3496  CA  ARG A 612    33767  28354  23795   4030    842    303       C  
ATOM   3497  C   ARG A 612     -11.128  -1.863  18.171  1.00226.78           C  
ANISOU 3497  C   ARG A 612    34011  28472  23684   4495    896    421       C  
ATOM   3498  O   ARG A 612     -12.254  -1.384  18.349  1.00230.55           O  
ANISOU 3498  O   ARG A 612    34409  29247  23944   5042   1039    569       O  
ATOM   3499  CB  ARG A 612      -9.724  -2.133  20.231  1.00226.78           C  
ANISOU 3499  CB  ARG A 612    34476  27906  23785   4004    917    177       C  
ATOM   3500  CG  ARG A 612     -10.384  -0.897  20.822  1.00234.40           C  
ANISOU 3500  CG  ARG A 612    35899  28737  24425   4614   1127    243       C  
ATOM   3501  CD  ARG A 612      -9.522  -0.284  21.913  1.00234.53           C  
ANISOU 3501  CD  ARG A 612    36547  28223  24341   4502   1183     98       C  
ATOM   3502  NE  ARG A 612      -8.183   0.036  21.432  1.00232.85           N  
ANISOU 3502  NE  ARG A 612    36724  27534  24215   4066   1053    -38       N  
ATOM   3503  CZ  ARG A 612      -7.844   1.188  20.869  1.00226.02           C  
ANISOU 3503  CZ  ARG A 612    36427  26271  23180   4213   1093    -51       C  
ATOM   3504  NH1 ARG A 612      -8.725   2.161  20.701  1.00220.64           N  
ANISOU 3504  NH1 ARG A 612    36039  25571  22225   4823   1264     62       N  
ATOM   3505  NH2 ARG A 612      -6.591   1.369  20.463  1.00219.79           N  
ANISOU 3505  NH2 ARG A 612    35925  25102  22484   3745    968   -169       N  
ATOM   3506  N   LEU A 613     -10.376  -1.549  17.118  1.00188.34           N  
ANISOU 3506  N   LEU A 613    29359  23324  18876   4306    792    372       N  
ATOM   3507  CA  LEU A 613     -10.828  -0.582  16.128  1.00182.92           C  
ANISOU 3507  CA  LEU A 613    28879  22625  17998   4736    840    483       C  
ATOM   3508  C   LEU A 613     -12.064  -1.093  15.396  1.00177.66           C  
ANISOU 3508  C   LEU A 613    27578  22622  17304   4978    810    657       C  
ATOM   3509  O   LEU A 613     -12.254  -2.299  15.212  1.00176.79           O  
ANISOU 3509  O   LEU A 613    26892  22896  17386   4622    688    656       O  
ATOM   3510  CB  LEU A 613      -9.710  -0.289  15.125  1.00178.14           C  
ANISOU 3510  CB  LEU A 613    28588  21612  17486   4404    724    393       C  
ATOM   3511  CG  LEU A 613      -8.781   0.885  15.440  1.00173.26           C  
ANISOU 3511  CG  LEU A 613    28765  20334  16731   4407    800    295       C  
ATOM   3512  CD1 LEU A 613      -7.818   0.531  16.563  1.00172.69           C  
ANISOU 3512  CD1 LEU A 613    28855  19980  16781   3965    769    132       C  
ATOM   3513  CD2 LEU A 613      -8.019   1.312  14.194  1.00163.05           C  
ANISOU 3513  CD2 LEU A 613    27724  18760  15468   4216    714    272       C  
ATOM   3514  N   GLY A 614     -12.911  -0.158  14.979  1.00142.76           N  
ANISOU 3514  N   GLY A 614    23285  18338  12620   5589    924    813       N  
ATOM   3515  CA  GLY A 614     -14.131  -0.493  14.269  1.00133.81           C  
ANISOU 3515  CA  GLY A 614    21557  17880  11406   5874    897   1003       C  
ATOM   3516  C   GLY A 614     -14.818   0.713  13.659  1.00125.39           C  
ANISOU 3516  C   GLY A 614    20756  16858  10030   6570   1016   1173       C  
ATOM   3517  O   GLY A 614     -16.043   0.829  13.699  1.00122.29           O  
ANISOU 3517  O   GLY A 614    20009  17015   9442   7074   1106   1366       O  
TER    3518      GLY A 614                                                      
ATOM   3519  N   ASP C   1      -2.955 -10.031 -27.574  1.00153.75           N  
ANISOU 3519  N   ASP C   1    25897  20265  12256    160  -1956    322       N  
ATOM   3520  CA  ASP C   1      -2.004 -11.071 -27.946  1.00156.05           C  
ANISOU 3520  CA  ASP C   1    26404  20296  12591   -140  -1842    165       C  
ATOM   3521  C   ASP C   1      -0.709 -10.912 -27.153  1.00155.24           C  
ANISOU 3521  C   ASP C   1    26414  19766  12806   -150  -1569    147       C  
ATOM   3522  O   ASP C   1       0.384 -11.180 -27.654  1.00152.43           O  
ANISOU 3522  O   ASP C   1    26314  19135  12467   -225  -1390    105       O  
ATOM   3523  CB  ASP C   1      -1.724 -11.033 -29.452  1.00160.36           C  
ANISOU 3523  CB  ASP C   1    27259  20821  12848   -109  -1841    183       C  
ATOM   3524  CG  ASP C   1      -0.977 -12.262 -29.941  1.00159.98           C  
ANISOU 3524  CG  ASP C   1    27435  20579  12770   -408  -1757     12       C  
ATOM   3525  OD1 ASP C   1      -1.537 -13.375 -29.855  1.00162.00           O  
ANISOU 3525  OD1 ASP C   1    27600  20997  12955   -693  -1904   -127       O  
ATOM   3526  OD2 ASP C   1       0.171 -12.112 -30.409  1.00159.68           O  
ANISOU 3526  OD2 ASP C   1    27681  20228  12764   -359  -1532     23       O  
HETATM 3527  N   SMF C   2      -0.838 -10.465 -25.910  1.00123.09           N  
ANISOU 3527  N   SMF C   2    22138  15664   8966    -68  -1537    185       N  
HETATM 3528  CA  SMF C   2       0.303 -10.402 -25.015  1.00119.17           C  
ANISOU 3528  CA  SMF C   2    21694  14820   8767   -122  -1312    159       C  
HETATM 3529  CB  SMF C   2      -0.047  -9.746 -23.676  1.00117.87           C  
ANISOU 3529  CB  SMF C   2    21317  14663   8806      2  -1311    217       C  
HETATM 3530  CG  SMF C   2       1.097  -9.139 -22.947  1.00111.53           C  
ANISOU 3530  CG  SMF C   2    20627  13512   8236     27  -1087    252       C  
HETATM 3531  CD1 SMF C   2       2.300  -8.871 -23.613  1.00113.10           C  
ANISOU 3531  CD1 SMF C   2    21098  13449   8426      2   -898    282       C  
HETATM 3532  CE1 SMF C   2       3.378  -8.304 -22.941  1.00109.79           C  
ANISOU 3532  CE1 SMF C   2    20758  12753   8203    -23   -701    323       C  
HETATM 3533  CD2 SMF C   2       0.999  -8.821 -21.588  1.00108.16           C  
ANISOU 3533  CD2 SMF C   2    20034  13037   8025     58  -1062    259       C  
HETATM 3534  CE2 SMF C   2       2.076  -8.254 -20.912  1.00102.40           C  
ANISOU 3534  CE2 SMF C   2    19416  12002   7488     40   -870    288       C  
HETATM 3535  CZ  SMF C   2       3.277  -7.984 -21.581  1.00 99.74           C  
ANISOU 3535  CZ  SMF C   2    19329  11430   7139    -15   -693    323       C  
HETATM 3536  CH  SMF C   2       4.412  -7.395 -20.854  1.00 95.79           C  
ANISOU 3536  CH  SMF C   2    18912  10660   6822    -86   -504    360       C  
HETATM 3537  S   SMF C   2       5.548  -8.528 -20.069  1.00 96.23           S  
ANISOU 3537  S   SMF C   2    18812  10629   7123   -358   -381    247       S  
HETATM 3538  O1  SMF C   2       4.923  -9.794 -20.117  1.00 91.32           O  
ANISOU 3538  O1  SMF C   2    18032  10182   6483   -435   -501    129       O  
HETATM 3539  O2  SMF C   2       6.776  -8.450 -20.766  1.00 99.23           O  
ANISOU 3539  O2  SMF C   2    19358  10870   7473   -438   -200    290       O  
HETATM 3540  O3  SMF C   2       5.624  -8.000 -18.749  1.00109.49           O  
ANISOU 3540  O3  SMF C   2    20395  12223   8984   -367   -359    261       O  
HETATM 3541  C   SMF C   2       0.876 -11.836 -24.758  1.00116.88           C  
ANISOU 3541  C   SMF C   2    21402  14419   8588   -434  -1254    -12       C  
HETATM 3542  O   SMF C   2       2.120 -11.985 -24.581  1.00117.64           O  
ANISOU 3542  O   SMF C   2    21635  14224   8837   -487  -1038    -35       O  
HETATM 3543  N   NLE C   3      -0.020 -12.825 -24.767  1.00 91.51           N  
ANISOU 3543  N   NLE C   3    18048  11447   5275   -626  -1439   -116       N  
HETATM 3544  CA  NLE C   3       0.256 -14.262 -24.584  1.00 90.93           C  
ANISOU 3544  CA  NLE C   3    18018  11290   5241   -925  -1417   -283       C  
HETATM 3545  C   NLE C   3       1.500 -14.697 -23.799  1.00 89.61           C  
ANISOU 3545  C   NLE C   3    17918  10793   5336   -985  -1182   -336       C  
HETATM 3546  O   NLE C   3       2.637 -14.473 -24.213  1.00 87.83           O  
ANISOU 3546  O   NLE C   3    17896  10336   5141   -906   -984   -303       O  
HETATM 3547  CB  NLE C   3       0.169 -15.023 -25.911  1.00 93.27           C  
ANISOU 3547  CB  NLE C   3    18564  11632   5241  -1069  -1483   -365       C  
HETATM 3548  CG  NLE C   3       0.322 -16.529 -25.753  1.00 93.27           C  
ANISOU 3548  CG  NLE C   3    18676  11531   5233  -1377  -1468   -541       C  
HETATM 3549  CD  NLE C   3      -0.754 -17.285 -26.517  1.00 96.28           C  
ANISOU 3549  CD  NLE C   3    19097  12182   5303  -1621  -1710   -632       C  
HETATM 3550  CE  NLE C   3      -2.140 -16.963 -25.982  1.00 97.26           C  
ANISOU 3550  CE  NLE C   3    18831  12721   5401  -1661  -1961   -578       C  
ATOM   3551  N   GLY C   4       1.258 -15.378 -22.685  1.00112.42           N  
ANISOU 3551  N   GLY C   4    20625  13696   8395  -1133  -1209   -412       N  
ATOM   3552  CA  GLY C   4       2.318 -15.757 -21.776  1.00108.50           C  
ANISOU 3552  CA  GLY C   4    20138  12939   8148  -1165  -1010   -446       C  
ATOM   3553  C   GLY C   4       2.346 -14.771 -20.632  1.00106.00           C  
ANISOU 3553  C   GLY C   4    19599  12616   8062  -1024   -981   -351       C  
ATOM   3554  O   GLY C   4       1.355 -14.083 -20.383  1.00107.77           O  
ANISOU 3554  O   GLY C   4    19647  13047   8255   -928  -1127   -288       O  
ATOM   3555  N   TRP C   5       3.476 -14.692 -19.941  1.00 81.10           N  
ANISOU 3555  N   TRP C   5    16459   9239   5118  -1000   -789   -335       N  
ATOM   3556  CA  TRP C   5       3.611 -13.761 -18.833  1.00 79.56           C  
ANISOU 3556  CA  TRP C   5    16100   9003   5126   -896   -751   -256       C  
ATOM   3557  C   TRP C   5       5.064 -13.575 -18.425  1.00 78.13           C  
ANISOU 3557  C   TRP C   5    15980   8595   5112   -890   -530   -220       C  
ATOM   3558  O   TRP C   5       5.908 -14.442 -18.656  1.00 77.97           O  
ANISOU 3558  O   TRP C   5    16052   8473   5099   -965   -405   -271       O  
ATOM   3559  CB  TRP C   5       2.780 -14.232 -17.633  1.00 79.79           C  
ANISOU 3559  CB  TRP C   5    15883   9157   5277   -982   -864   -313       C  
ATOM   3560  CG  TRP C   5       3.112 -15.617 -17.174  1.00 80.64           C  
ANISOU 3560  CG  TRP C   5    15993   9188   5460  -1177   -815   -431       C  
ATOM   3561  CD1 TRP C   5       4.114 -15.982 -16.324  1.00 82.42           C  
ANISOU 3561  CD1 TRP C   5    16204   9234   5876  -1204   -658   -447       C  
ATOM   3562  CD2 TRP C   5       2.435 -16.826 -17.539  1.00 79.23           C  
ANISOU 3562  CD2 TRP C   5    15858   9104   5140  -1372   -920   -543       C  
ATOM   3563  NE1 TRP C   5       4.106 -17.343 -16.140  1.00 77.93           N  
ANISOU 3563  NE1 TRP C   5    15688   8625   5297  -1363   -647   -556       N  
ATOM   3564  CE2 TRP C   5       3.085 -17.885 -16.875  1.00 78.20           C  
ANISOU 3564  CE2 TRP C   5    15781   8805   5127  -1488   -803   -623       C  
ATOM   3565  CE3 TRP C   5       1.344 -17.116 -18.365  1.00 81.42           C  
ANISOU 3565  CE3 TRP C   5    16148   9602   5185  -1473  -1106   -580       C  
ATOM   3566  CZ2 TRP C   5       2.679 -19.211 -17.009  1.00 83.57           C  
ANISOU 3566  CZ2 TRP C   5    16576   9479   5696  -1705   -852   -743       C  
ATOM   3567  CZ3 TRP C   5       0.945 -18.433 -18.498  1.00 83.86           C  
ANISOU 3567  CZ3 TRP C   5    16545   9933   5384  -1732  -1170   -705       C  
ATOM   3568  CH2 TRP C   5       1.610 -19.464 -17.823  1.00 85.89           C  
ANISOU 3568  CH2 TRP C   5    16904   9969   5760  -1848  -1036   -789       C  
HETATM 3569  N   NLE C   6       5.340 -12.419 -17.832  1.00 88.20           N  
ANISOU 3569  N   NLE C   6    17212   9803   6498   -795   -482   -125       N  
HETATM 3570  CA  NLE C   6       6.641 -12.122 -17.254  1.00 89.34           C  
ANISOU 3570  CA  NLE C   6    17360   9784   6803   -831   -301    -80       C  
HETATM 3571  C   NLE C   6       6.954 -13.135 -16.158  1.00 94.56           C  
ANISOU 3571  C   NLE C   6    17857  10434   7638   -941   -268   -161       C  
HETATM 3572  O   NLE C   6       6.057 -13.545 -15.425  1.00 96.73           O  
ANISOU 3572  O   NLE C   6    17991  10797   7966   -972   -392   -222       O  
HETATM 3573  CB  NLE C   6       6.654 -10.694 -16.700  1.00 91.04           C  
ANISOU 3573  CB  NLE C   6    17586   9928   7077   -750   -290     20       C  
HETATM 3574  CG  NLE C   6       7.987 -10.226 -16.147  1.00 90.90           C  
ANISOU 3574  CG  NLE C   6    17579   9767   7192   -838   -120     79       C  
HETATM 3575  CD  NLE C   6       7.884  -8.800 -15.633  1.00 91.09           C  
ANISOU 3575  CD  NLE C   6    17691   9686   7233   -788   -121    165       C  
HETATM 3576  CE  NLE C   6       9.203  -8.329 -15.051  1.00 93.76           C  
ANISOU 3576  CE  NLE C   6    18037   9906   7682   -943     30    220       C  
HETATM 3577  C   OEM C   7       8.351 -13.961 -13.578  1.00115.55           C  
ANISOU 3577  C   OEM C   7    20203  13001  10698  -1079   -111   -194       C  
HETATM 3578  N   OEM C   7       8.217 -13.546 -16.063  1.00102.55           N  
ANISOU 3578  N   OEM C   7    18882  11359   8722   -987    -97   -148       N  
HETATM 3579  O   OEM C   7       9.058 -12.975 -13.214  1.00120.54           O  
ANISOU 3579  O   OEM C   7    20819  13582  11399  -1085    -39   -109       O  
HETATM 3580  CA  OEM C   7       8.655 -14.510 -15.035  1.00106.55           C  
ANISOU 3580  CA  OEM C   7    19253  11852   9379  -1054    -44   -205       C  
HETATM 3581  CB  OEM C   7       8.310 -15.958 -15.435  1.00105.35           C  
ANISOU 3581  CB  OEM C   7    19186  11709   9135  -1094    -63   -314       C  
HETATM 3582  CG  OEM C   7       9.075 -17.055 -14.698  1.00109.27           C  
ANISOU 3582  CG  OEM C   7    19639  12147   9731  -1114     58   -351       C  
HETATM 3583  CAA OEM C   7       9.138 -13.481 -17.162  1.00 97.25           C  
ANISOU 3583  CAA OEM C   7    18373  10640   7937   -960     48    -94       C  
HETATM 3584  OD1 OEM C   7       9.603 -18.018 -15.343  1.00105.84           O  
ANISOU 3584  OD1 OEM C   7    19371  11652   9190  -1083    173   -385       O  
HETATM 3585  OD2 OEM C   7       9.171 -16.988 -13.432  1.00116.78           O  
ANISOU 3585  OD2 OEM C   7    20408  13108  10855  -1140     48   -343       O  
HETATM 3586  C1  MEA C   8       6.280 -15.399 -12.996  1.00120.42           C  
ANISOU 3586  C1  MEA C   8    20695  13772  11287  -1160   -361   -361       C  
HETATM 3587  N   MEA C   8       7.398 -14.502 -12.802  1.00121.90           N  
ANISOU 3587  N   MEA C   8    20891  13868  11558  -1111   -232   -269       N  
HETATM 3588  CA  MEA C   8       7.125 -13.946 -11.474  1.00117.98           C  
ANISOU 3588  CA  MEA C   8    20239  13379  11208  -1113   -281   -254       C  
HETATM 3589  C   MEA C   8       6.618 -12.517 -11.644  1.00117.62           C  
ANISOU 3589  C   MEA C   8    20252  13330  11108  -1016   -340   -181       C  
HETATM 3590  O   MEA C   8       5.981 -12.131 -12.628  1.00113.83           O  
ANISOU 3590  O   MEA C   8    19875  12901  10476   -934   -406   -158       O  
HETATM 3591  CB  MEA C   8       8.330 -13.946 -10.511  1.00116.62           C  
ANISOU 3591  CB  MEA C   8    19979  13140  11191  -1164   -157   -222       C  
HETATM 3592  CG  MEA C   8       8.925 -15.291 -10.297  1.00116.59           C  
ANISOU 3592  CG  MEA C   8    19937  13134  11227  -1200    -74   -270       C  
HETATM 3593  CD1 MEA C   8      10.314 -15.429 -10.186  1.00115.27           C  
ANISOU 3593  CD1 MEA C   8    19739  12952  11107  -1202     83   -210       C  
HETATM 3594  CE1 MEA C   8      10.883 -16.684  -9.982  1.00114.12           C  
ANISOU 3594  CE1 MEA C   8    19577  12806  10976  -1175    178   -237       C  
HETATM 3595  CZ  MEA C   8      10.068 -17.813  -9.890  1.00114.90           C  
ANISOU 3595  CZ  MEA C   8    19741  12874  11042  -1186    119   -338       C  
HETATM 3596  CE2 MEA C   8       8.683 -17.682 -10.000  1.00114.40           C  
ANISOU 3596  CE2 MEA C   8    19698  12835  10935  -1245    -47   -405       C  
HETATM 3597  CD2 MEA C   8       8.112 -16.427 -10.201  1.00114.11           C  
ANISOU 3597  CD2 MEA C   8    19628  12844  10885  -1233   -144   -365       C  
HETATM 3598  N   NH2 C   9       6.916 -11.703 -10.638  1.00174.01           N  
ANISOU 3598  N   NH2 C   9    27353  20404  18360  -1015   -314   -139       N  
TER    3599      NH2 C   9                                                      
CONECT  620 1267                                                                
CONECT 1267  620                                                                
CONECT 3521 3527                                                                
CONECT 3527 3521 3528                                                           
CONECT 3528 3527 3529 3541                                                      
CONECT 3529 3528 3530                                                           
CONECT 3530 3529 3531 3533                                                      
CONECT 3531 3530 3532                                                           
CONECT 3532 3531 3535                                                           
CONECT 3533 3530 3534                                                           
CONECT 3534 3533 3535                                                           
CONECT 3535 3532 3534 3536                                                      
CONECT 3536 3535 3537                                                           
CONECT 3537 3536 3538 3539 3540                                                 
CONECT 3538 3537                                                                
CONECT 3539 3537                                                                
CONECT 3540 3537                                                                
CONECT 3541 3528 3542 3543                                                      
CONECT 3542 3541                                                                
CONECT 3543 3541 3544                                                           
CONECT 3544 3543 3545 3547                                                      
CONECT 3545 3544 3546 3551                                                      
CONECT 3546 3545                                                                
CONECT 3547 3544 3548                                                           
CONECT 3548 3547 3549                                                           
CONECT 3549 3548 3550                                                           
CONECT 3550 3549                                                                
CONECT 3551 3545                                                                
CONECT 3557 3569                                                                
CONECT 3569 3557 3570                                                           
CONECT 3570 3569 3571 3573                                                      
CONECT 3571 3570 3572 3578                                                      
CONECT 3572 3571                                                                
CONECT 3573 3570 3574                                                           
CONECT 3574 3573 3575                                                           
CONECT 3575 3574 3576                                                           
CONECT 3576 3575                                                                
CONECT 3577 3579 3580 3587                                                      
CONECT 3578 3571 3580 3583                                                      
CONECT 3579 3577                                                                
CONECT 3580 3577 3578 3581                                                      
CONECT 3581 3580 3582                                                           
CONECT 3582 3581 3584 3585                                                      
CONECT 3583 3578                                                                
CONECT 3584 3582                                                                
CONECT 3585 3582                                                                
CONECT 3586 3587                                                                
CONECT 3587 3577 3586 3588                                                      
CONECT 3588 3587 3589 3591                                                      
CONECT 3589 3588 3590 3598                                                      
CONECT 3590 3589                                                                
CONECT 3591 3588 3592                                                           
CONECT 3592 3591 3593 3597                                                      
CONECT 3593 3592 3594                                                           
CONECT 3594 3593 3595                                                           
CONECT 3595 3594 3596                                                           
CONECT 3596 3595 3597                                                           
CONECT 3597 3592 3596                                                           
CONECT 3598 3589                                                                
MASTER      336    0    6   23    5    0    0    6 3597    2   59   43          
END