path: root/plip/test/pdb/3og7.pdb

HEADER    TRANSFERASE                             16-AUG-10   3OG7              
TITLE     B-RAF KINASE V600E ONCOGENIC MUTANT IN COMPLEX WITH PLX4032           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: AKAP9-BRAF FUSION PROTEIN;                                 
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: KINASE DOMAIN (UNP RESIDUES 1175-1446);                    
COMPND   5 SYNONYM: PROTO-ONCOGENE B-RAF, P94, V-RAF MURINE SARCOMA VIRAL       
COMPND   6 ONCOGENE HOMOLOG B1;                                                 
COMPND   7 EC: 2.7.11.1;                                                        
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: BRAF, BRAF1, RAFB1;                                            
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    B-RAF, BRAF, PROTO-ONCOGENE, V600E, KINASE, TRANSFERASE               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.ZHANG,K.Y.ZHANG,C.ZHANG                                             
REVDAT   2   06-OCT-10 3OG7    1       JRNL                                     
REVDAT   1   22-SEP-10 3OG7    0                                                
JRNL        AUTH   G.BOLLAG,P.HIRTH,J.TSAI,J.ZHANG,P.N.IBRAHIM,H.CHO,W.SPEVAK,  
JRNL        AUTH 2 C.ZHANG,Y.ZHANG,G.HABETS,E.A.BURTON,B.WONG,G.TSANG,B.L.WEST, 
JRNL        AUTH 3 B.POWELL,R.SHELLOOE,A.MARIMUTHU,H.NGUYEN,K.Y.ZHANG,          
JRNL        AUTH 4 D.R.ARTIS,J.SCHLESSINGER,F.SU,B.HIGGINS,R.IYER,K.D'ANDREA,   
JRNL        AUTH 5 A.KOEHLER,M.STUMM,P.S.LIN,R.J.LEE,J.GRIPPO,I.PUZANOV,        
JRNL        AUTH 6 K.B.KIM,A.RIBAS,G.A.MCARTHUR,J.A.SOSMAN,P.B.CHAPMAN,         
JRNL        AUTH 7 K.T.FLAHERTY,X.XU,K.L.NATHANSON,K.NOLOP                      
JRNL        TITL   CLINICAL EFFICACY OF A RAF INHIBITOR NEEDS BROAD TARGET      
JRNL        TITL 2 BLOCKADE IN BRAF-MUTANT MELANOMA.                            
JRNL        REF    NATURE                        V. 467   596 2010              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   20823850                                                     
JRNL        DOI    10.1038/NATURE09454                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.45 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.5_2)                        
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : TWIN_LSQ_F                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.45                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 21.30                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 21223                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.214                           
REMARK   3   R VALUE            (WORKING SET) : 0.212                           
REMARK   3   FREE R VALUE                     : 0.258                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.190                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1146                            
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 21.2756 -  4.8839    0.94     2744   156  0.1766 0.2014        
REMARK   3     2  4.8839 -  3.8842    0.95     2646   129  0.1679 0.2228        
REMARK   3     3  3.8842 -  3.3955    0.95     2639   130  0.2012 0.2405        
REMARK   3     4  3.3955 -  3.0861    0.95     2615   142  0.2319 0.2977        
REMARK   3     5  3.0861 -  2.8654    0.95     2581   142  0.2690 0.3498        
REMARK   3     6  2.8654 -  2.6968    0.95     2581   137  0.2837 0.3466        
REMARK   3     7  2.6968 -  2.5620    0.95     2602   129  0.3023 0.3415        
REMARK   3     8  2.5620 -  2.4507    0.94     2570   142  0.3323 0.3173        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 0.33                                          
REMARK   3   B_SOL              : 47.40                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : NULL             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.220           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 65.23                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 24.09380                                             
REMARK   3    B22 (A**2) : -6.25230                                             
REMARK   3    B33 (A**2) : -17.84150                                            
REMARK   3    B12 (A**2) : -0.00000                                             
REMARK   3    B13 (A**2) : -0.00000                                             
REMARK   3    B23 (A**2) : -0.00000                                             
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: 0.0860                                                   
REMARK   3   OPERATOR: -H,L,K                                                   
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.003           4119                                  
REMARK   3   ANGLE     :  0.649           5553                                  
REMARK   3   CHIRALITY :  0.048            600                                  
REMARK   3   PLANARITY :  0.004            707                                  
REMARK   3   DIHEDRAL  : 16.634           1535                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.3512 -12.8290 -19.0118              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2830 T22:   0.1799                                     
REMARK   3      T33:   0.1414 T12:   0.0279                                     
REMARK   3      T13:   0.0065 T23:  -0.0149                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4271 L22:   0.5813                                     
REMARK   3      L33:   0.3905 L12:   0.2092                                     
REMARK   3      L13:   0.1909 L23:   0.5345                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0295 S12:   0.1294 S13:   0.0517                       
REMARK   3      S21:   0.4450 S22:   0.0815 S23:   0.0308                       
REMARK   3      S31:   0.2817 S32:   0.0987 S33:  -0.0896                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN B                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   1.4917   8.6212   6.0490              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0793 T22:   0.1906                                     
REMARK   3      T33:   0.0369 T12:   0.0770                                     
REMARK   3      T13:   0.1264 T23:  -0.0440                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9070 L22:  -0.0294                                     
REMARK   3      L33:   1.4032 L12:   0.0673                                     
REMARK   3      L13:  -0.0545 L23:   0.1136                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0650 S12:  -0.0999 S13:   0.5313                       
REMARK   3      S21:   0.1643 S22:  -0.0917 S23:  -0.0431                       
REMARK   3      S31:   0.6296 S32:   0.1890 S33:   0.1035                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN L AND RESSEQ 1:1                                 
REMARK   3    ORIGIN FOR THE GROUP (A):   1.8508  -2.7808 -20.0870              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2232 T22:   0.2843                                     
REMARK   3      T33:   0.2448 T12:   0.0830                                     
REMARK   3      T13:   0.0676 T23:   0.0568                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3324 L22:   0.2201                                     
REMARK   3      L33:   0.0130 L12:   0.0881                                     
REMARK   3      L13:   0.0256 L23:   0.0536                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0039 S12:  -0.0108 S13:   0.0148                       
REMARK   3      S21:  -0.0181 S22:  -0.0394 S23:   0.0296                       
REMARK   3      S31:   0.0173 S32:   0.0067 S33:   0.0485                       
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 3OG7 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-AUG-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB061075.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-MAR-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.3.1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.1                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 22230                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.450                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 110.128                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 4.500                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.07200                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.45                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.58                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.52400                            
REMARK 200  R SYM FOR SHELL            (I) : 0.52400                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.71                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.35                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM BISTRIS AT PH 6.0, 12.5% 2,5-      
REMARK 280  HEXANEDIOL, AND 12% PEG3350, VAPOR DIFFUSION, SITTING DROP,         
REMARK 280  TEMPERATURE 277K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       25.38500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       55.06400            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.21200            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       55.06400            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       25.38500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.21200            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   432                                                      
REMARK 465     LYS A   433                                                      
REMARK 465     LYS A   434                                                      
REMARK 465     GLY A   435                                                      
REMARK 465     HIS A   436                                                      
REMARK 465     HIS A   437                                                      
REMARK 465     HIS A   438                                                      
REMARK 465     HIS A   439                                                      
REMARK 465     HIS A   440                                                      
REMARK 465     HIS A   441                                                      
REMARK 465     GLY A   442                                                      
REMARK 465     SER A   443                                                      
REMARK 465     ARG A   444                                                      
REMARK 465     ASP A   445                                                      
REMARK 465     ALA A   446                                                      
REMARK 465     ALA A   447                                                      
REMARK 465     ASP A   448                                                      
REMARK 465     GLU A   545                                                      
REMARK 465     THR A   546                                                      
REMARK 465     LYS A   547                                                      
REMARK 465     LEU A   597                                                      
REMARK 465     ALA A   598                                                      
REMARK 465     THR A   599                                                      
REMARK 465     GLU A   600                                                      
REMARK 465     LYS A   601                                                      
REMARK 465     SER A   602                                                      
REMARK 465     ARG A   603                                                      
REMARK 465     TRP A   604                                                      
REMARK 465     SER A   605                                                      
REMARK 465     GLY A   606                                                      
REMARK 465     SER A   607                                                      
REMARK 465     HIS A   608                                                      
REMARK 465     GLN A   609                                                      
REMARK 465     PHE A   610                                                      
REMARK 465     GLU A   611                                                      
REMARK 465     GLN A   612                                                      
REMARK 465     LEU A   613                                                      
REMARK 465     SER A   614                                                      
REMARK 465     MET A   627                                                      
REMARK 465     GLN A   628                                                      
REMARK 465     ASP A   629                                                      
REMARK 465     SER A   630                                                      
REMARK 465     MET B   432                                                      
REMARK 465     LYS B   433                                                      
REMARK 465     LYS B   434                                                      
REMARK 465     GLY B   435                                                      
REMARK 465     HIS B   436                                                      
REMARK 465     HIS B   437                                                      
REMARK 465     HIS B   438                                                      
REMARK 465     HIS B   439                                                      
REMARK 465     HIS B   440                                                      
REMARK 465     HIS B   441                                                      
REMARK 465     GLY B   442                                                      
REMARK 465     SER B   443                                                      
REMARK 465     ARG B   444                                                      
REMARK 465     ASP B   445                                                      
REMARK 465     ALA B   446                                                      
REMARK 465     ALA B   447                                                      
REMARK 465     ASP B   448                                                      
REMARK 465     LYS B   601                                                      
REMARK 465     SER B   602                                                      
REMARK 465     ARG B   603                                                      
REMARK 465     TRP B   604                                                      
REMARK 465     SER B   605                                                      
REMARK 465     GLY B   606                                                      
REMARK 465     SER B   607                                                      
REMARK 465     HIS B   608                                                      
REMARK 465     GLN B   609                                                      
REMARK 465     PHE B   610                                                      
REMARK 465     GLU B   611                                                      
REMARK 465     GLN B   612                                                      
REMARK 465     LEU B   613                                                      
REMARK 465     SER B   614                                                      
REMARK 465     MET B   627                                                      
REMARK 465     GLN B   628                                                      
REMARK 465     ASP B   629                                                      
REMARK 465     SER B   630                                                      
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    PRO A 453      151.21    -47.95                                   
REMARK 500    ARG A 575      -15.01     78.91                                   
REMARK 500    ASP A 576       55.71   -154.93                                   
REMARK 500    ASN A 660       56.53    -91.77                                   
REMARK 500    ASN A 684       36.26    -75.66                                   
REMARK 500    TRP B 476       92.18   -160.90                                   
REMARK 500    THR B 521      -59.15   -129.61                                   
REMARK 500    ALA B 522       21.78    -74.49                                   
REMARK 500    PRO B 523      -87.45   -114.92                                   
REMARK 500    ALA B 543       30.14    -91.55                                   
REMARK 500    ASP B 576       38.22   -154.00                                   
REMARK 500    ASP B 587      -15.42     76.91                                   
REMARK 500    PHE B 595      -84.66    -52.94                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ALA B  522     PRO B  523                  143.03                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 032 A 1                   
DBREF  3OG7 A  449   720  UNP    Q5IBP5   Q5IBP5_HUMAN  1175   1446             
DBREF  3OG7 B  449   720  UNP    Q5IBP5   Q5IBP5_HUMAN  1175   1446             
SEQADV 3OG7 MET A  432  UNP  Q5IBP5              EXPRESSION TAG                 
SEQADV 3OG7 LYS A  433  UNP  Q5IBP5              EXPRESSION TAG                 
SEQADV 3OG7 LYS A  434  UNP  Q5IBP5              EXPRESSION TAG                 
SEQADV 3OG7 GLY A  435  UNP  Q5IBP5              EXPRESSION TAG                 
SEQADV 3OG7 HIS A  436  UNP  Q5IBP5              EXPRESSION TAG                 
SEQADV 3OG7 HIS A  437  UNP  Q5IBP5              EXPRESSION TAG                 
SEQADV 3OG7 HIS A  438  UNP  Q5IBP5              EXPRESSION TAG                 
SEQADV 3OG7 HIS A  439  UNP  Q5IBP5              EXPRESSION TAG                 
SEQADV 3OG7 HIS A  440  UNP  Q5IBP5              EXPRESSION TAG                 
SEQADV 3OG7 HIS A  441  UNP  Q5IBP5              EXPRESSION TAG                 
SEQADV 3OG7 GLY A  442  UNP  Q5IBP5              EXPRESSION TAG                 
SEQADV 3OG7 SER A  443  UNP  Q5IBP5              EXPRESSION TAG                 
SEQADV 3OG7 ARG A  444  UNP  Q5IBP5              EXPRESSION TAG                 
SEQADV 3OG7 ASP A  445  UNP  Q5IBP5              EXPRESSION TAG                 
SEQADV 3OG7 ALA A  446  UNP  Q5IBP5              EXPRESSION TAG                 
SEQADV 3OG7 ALA A  447  UNP  Q5IBP5              EXPRESSION TAG                 
SEQADV 3OG7 ASP A  448  UNP  Q5IBP5              EXPRESSION TAG                 
SEQADV 3OG7 ALA A  522  UNP  Q5IBP5    LYS  1248 ENGINEERED MUTATION            
SEQADV 3OG7 ALA A  543  UNP  Q5IBP5    ILE  1269 ENGINEERED MUTATION            
SEQADV 3OG7 SER A  544  UNP  Q5IBP5    ILE  1270 ENGINEERED MUTATION            
SEQADV 3OG7 LYS A  551  UNP  Q5IBP5    ILE  1277 ENGINEERED MUTATION            
SEQADV 3OG7 ARG A  562  UNP  Q5IBP5    GLN  1288 ENGINEERED MUTATION            
SEQADV 3OG7 ASN A  588  UNP  Q5IBP5    LEU  1314 ENGINEERED MUTATION            
SEQADV 3OG7 GLU A  600  UNP  Q5IBP5    VAL  1326 VARIANT                        
SEQADV 3OG7 SER A  630  UNP  Q5IBP5    LYS  1356 ENGINEERED MUTATION            
SEQADV 3OG7 GLU A  667  UNP  Q5IBP5    PHE  1393 ENGINEERED MUTATION            
SEQADV 3OG7 SER A  673  UNP  Q5IBP5    TYR  1399 ENGINEERED MUTATION            
SEQADV 3OG7 ARG A  688  UNP  Q5IBP5    ALA  1414 ENGINEERED MUTATION            
SEQADV 3OG7 SER A  706  UNP  Q5IBP5    LEU  1432 ENGINEERED MUTATION            
SEQADV 3OG7 ARG A  709  UNP  Q5IBP5    GLN  1435 ENGINEERED MUTATION            
SEQADV 3OG7 GLU A  713  UNP  Q5IBP5    SER  1439 ENGINEERED MUTATION            
SEQADV 3OG7 GLU A  716  UNP  Q5IBP5    LEU  1442 ENGINEERED MUTATION            
SEQADV 3OG7 GLU A  720  UNP  Q5IBP5    SER  1446 ENGINEERED MUTATION            
SEQADV 3OG7 MET B  432  UNP  Q5IBP5              EXPRESSION TAG                 
SEQADV 3OG7 LYS B  433  UNP  Q5IBP5              EXPRESSION TAG                 
SEQADV 3OG7 LYS B  434  UNP  Q5IBP5              EXPRESSION TAG                 
SEQADV 3OG7 GLY B  435  UNP  Q5IBP5              EXPRESSION TAG                 
SEQADV 3OG7 HIS B  436  UNP  Q5IBP5              EXPRESSION TAG                 
SEQADV 3OG7 HIS B  437  UNP  Q5IBP5              EXPRESSION TAG                 
SEQADV 3OG7 HIS B  438  UNP  Q5IBP5              EXPRESSION TAG                 
SEQADV 3OG7 HIS B  439  UNP  Q5IBP5              EXPRESSION TAG                 
SEQADV 3OG7 HIS B  440  UNP  Q5IBP5              EXPRESSION TAG                 
SEQADV 3OG7 HIS B  441  UNP  Q5IBP5              EXPRESSION TAG                 
SEQADV 3OG7 GLY B  442  UNP  Q5IBP5              EXPRESSION TAG                 
SEQADV 3OG7 SER B  443  UNP  Q5IBP5              EXPRESSION TAG                 
SEQADV 3OG7 ARG B  444  UNP  Q5IBP5              EXPRESSION TAG                 
SEQADV 3OG7 ASP B  445  UNP  Q5IBP5              EXPRESSION TAG                 
SEQADV 3OG7 ALA B  446  UNP  Q5IBP5              EXPRESSION TAG                 
SEQADV 3OG7 ALA B  447  UNP  Q5IBP5              EXPRESSION TAG                 
SEQADV 3OG7 ASP B  448  UNP  Q5IBP5              EXPRESSION TAG                 
SEQADV 3OG7 ALA B  522  UNP  Q5IBP5    LYS  1248 ENGINEERED MUTATION            
SEQADV 3OG7 ALA B  543  UNP  Q5IBP5    ILE  1269 ENGINEERED MUTATION            
SEQADV 3OG7 SER B  544  UNP  Q5IBP5    ILE  1270 ENGINEERED MUTATION            
SEQADV 3OG7 LYS B  551  UNP  Q5IBP5    ILE  1277 ENGINEERED MUTATION            
SEQADV 3OG7 ARG B  562  UNP  Q5IBP5    GLN  1288 ENGINEERED MUTATION            
SEQADV 3OG7 ASN B  588  UNP  Q5IBP5    LEU  1314 ENGINEERED MUTATION            
SEQADV 3OG7 GLU B  600  UNP  Q5IBP5    VAL  1326 VARIANT                        
SEQADV 3OG7 SER B  630  UNP  Q5IBP5    LYS  1356 ENGINEERED MUTATION            
SEQADV 3OG7 GLU B  667  UNP  Q5IBP5    PHE  1393 ENGINEERED MUTATION            
SEQADV 3OG7 SER B  673  UNP  Q5IBP5    TYR  1399 ENGINEERED MUTATION            
SEQADV 3OG7 ARG B  688  UNP  Q5IBP5    ALA  1414 ENGINEERED MUTATION            
SEQADV 3OG7 SER B  706  UNP  Q5IBP5    LEU  1432 ENGINEERED MUTATION            
SEQADV 3OG7 ARG B  709  UNP  Q5IBP5    GLN  1435 ENGINEERED MUTATION            
SEQADV 3OG7 GLU B  713  UNP  Q5IBP5    SER  1439 ENGINEERED MUTATION            
SEQADV 3OG7 GLU B  716  UNP  Q5IBP5    LEU  1442 ENGINEERED MUTATION            
SEQADV 3OG7 GLU B  720  UNP  Q5IBP5    SER  1446 ENGINEERED MUTATION            
SEQRES   1 A  289  MET LYS LYS GLY HIS HIS HIS HIS HIS HIS GLY SER ARG          
SEQRES   2 A  289  ASP ALA ALA ASP ASP TRP GLU ILE PRO ASP GLY GLN ILE          
SEQRES   3 A  289  THR VAL GLY GLN ARG ILE GLY SER GLY SER PHE GLY THR          
SEQRES   4 A  289  VAL TYR LYS GLY LYS TRP HIS GLY ASP VAL ALA VAL LYS          
SEQRES   5 A  289  MET LEU ASN VAL THR ALA PRO THR PRO GLN GLN LEU GLN          
SEQRES   6 A  289  ALA PHE LYS ASN GLU VAL GLY VAL LEU ARG LYS THR ARG          
SEQRES   7 A  289  HIS VAL ASN ILE LEU LEU PHE MET GLY TYR SER THR ALA          
SEQRES   8 A  289  PRO GLN LEU ALA ILE VAL THR GLN TRP CYS GLU GLY SER          
SEQRES   9 A  289  SER LEU TYR HIS HIS LEU HIS ALA SER GLU THR LYS PHE          
SEQRES  10 A  289  GLU MET LYS LYS LEU ILE ASP ILE ALA ARG GLN THR ALA          
SEQRES  11 A  289  ARG GLY MET ASP TYR LEU HIS ALA LYS SER ILE ILE HIS          
SEQRES  12 A  289  ARG ASP LEU LYS SER ASN ASN ILE PHE LEU HIS GLU ASP          
SEQRES  13 A  289  ASN THR VAL LYS ILE GLY ASP PHE GLY LEU ALA THR GLU          
SEQRES  14 A  289  LYS SER ARG TRP SER GLY SER HIS GLN PHE GLU GLN LEU          
SEQRES  15 A  289  SER GLY SER ILE LEU TRP MET ALA PRO GLU VAL ILE ARG          
SEQRES  16 A  289  MET GLN ASP SER ASN PRO TYR SER PHE GLN SER ASP VAL          
SEQRES  17 A  289  TYR ALA PHE GLY ILE VAL LEU TYR GLU LEU MET THR GLY          
SEQRES  18 A  289  GLN LEU PRO TYR SER ASN ILE ASN ASN ARG ASP GLN ILE          
SEQRES  19 A  289  ILE GLU MET VAL GLY ARG GLY SER LEU SER PRO ASP LEU          
SEQRES  20 A  289  SER LYS VAL ARG SER ASN CYS PRO LYS ARG MET LYS ARG          
SEQRES  21 A  289  LEU MET ALA GLU CYS LEU LYS LYS LYS ARG ASP GLU ARG          
SEQRES  22 A  289  PRO SER PHE PRO ARG ILE LEU ALA GLU ILE GLU GLU LEU          
SEQRES  23 A  289  ALA ARG GLU                                                  
SEQRES   1 B  289  MET LYS LYS GLY HIS HIS HIS HIS HIS HIS GLY SER ARG          
SEQRES   2 B  289  ASP ALA ALA ASP ASP TRP GLU ILE PRO ASP GLY GLN ILE          
SEQRES   3 B  289  THR VAL GLY GLN ARG ILE GLY SER GLY SER PHE GLY THR          
SEQRES   4 B  289  VAL TYR LYS GLY LYS TRP HIS GLY ASP VAL ALA VAL LYS          
SEQRES   5 B  289  MET LEU ASN VAL THR ALA PRO THR PRO GLN GLN LEU GLN          
SEQRES   6 B  289  ALA PHE LYS ASN GLU VAL GLY VAL LEU ARG LYS THR ARG          
SEQRES   7 B  289  HIS VAL ASN ILE LEU LEU PHE MET GLY TYR SER THR ALA          
SEQRES   8 B  289  PRO GLN LEU ALA ILE VAL THR GLN TRP CYS GLU GLY SER          
SEQRES   9 B  289  SER LEU TYR HIS HIS LEU HIS ALA SER GLU THR LYS PHE          
SEQRES  10 B  289  GLU MET LYS LYS LEU ILE ASP ILE ALA ARG GLN THR ALA          
SEQRES  11 B  289  ARG GLY MET ASP TYR LEU HIS ALA LYS SER ILE ILE HIS          
SEQRES  12 B  289  ARG ASP LEU LYS SER ASN ASN ILE PHE LEU HIS GLU ASP          
SEQRES  13 B  289  ASN THR VAL LYS ILE GLY ASP PHE GLY LEU ALA THR GLU          
SEQRES  14 B  289  LYS SER ARG TRP SER GLY SER HIS GLN PHE GLU GLN LEU          
SEQRES  15 B  289  SER GLY SER ILE LEU TRP MET ALA PRO GLU VAL ILE ARG          
SEQRES  16 B  289  MET GLN ASP SER ASN PRO TYR SER PHE GLN SER ASP VAL          
SEQRES  17 B  289  TYR ALA PHE GLY ILE VAL LEU TYR GLU LEU MET THR GLY          
SEQRES  18 B  289  GLN LEU PRO TYR SER ASN ILE ASN ASN ARG ASP GLN ILE          
SEQRES  19 B  289  ILE GLU MET VAL GLY ARG GLY SER LEU SER PRO ASP LEU          
SEQRES  20 B  289  SER LYS VAL ARG SER ASN CYS PRO LYS ARG MET LYS ARG          
SEQRES  21 B  289  LEU MET ALA GLU CYS LEU LYS LYS LYS ARG ASP GLU ARG          
SEQRES  22 B  289  PRO SER PHE PRO ARG ILE LEU ALA GLU ILE GLU GLU LEU          
SEQRES  23 B  289  ALA ARG GLU                                                  
HET    032  A   1      33                                                       
HETNAM     032 N-(3-{[5-(4-CHLOROPHENYL)-1H-PYRROLO[2,3-B]PYRIDIN-3-            
HETNAM   2 032  YL]CARBONYL}-2,4-DIFLUOROPHENYL)PROPANE-1-SULFONAMIDE           
HETSYN     032 PLX4032                                                          
FORMUL   3  032    C23 H18 CL F2 N3 O3 S                                        
FORMUL   4  HOH   *65(H2 O)                                                     
HELIX    1   1 THR A  491  ARG A  506  1                                  16    
HELIX    2   2 LEU A  537  HIS A  542  1                                   6    
HELIX    3   3 GLU A  549  LYS A  570  1                                  22    
HELIX    4   4 ALA A  621  ARG A  626  1                                   6    
HELIX    5   5 SER A  634  GLY A  652  1                                  19    
HELIX    6   6 ASN A  661  ARG A  671  1                                  11    
HELIX    7   7 PRO A  686  LEU A  697  1                                  12    
HELIX    8   8 LYS A  700  ARG A  704  5                                   5    
HELIX    9   9 SER A  706  LEU A  717  1                                  12    
HELIX   10  10 THR B  491  ARG B  506  1                                  16    
HELIX   11  11 SER B  536  HIS B  542  1                                   7    
HELIX   12  12 GLU B  549  LYS B  570  1                                  22    
HELIX   13  13 GLU B  586  ASN B  588  5                                   3    
HELIX   14  14 GLY B  615  MET B  620  5                                   6    
HELIX   15  15 ALA B  621  ARG B  626  1                                   6    
HELIX   16  16 SER B  634  GLY B  652  1                                  19    
HELIX   17  17 ASN B  661  GLY B  672  1                                  12    
HELIX   18  18 ASP B  677  VAL B  681  5                                   5    
HELIX   19  19 PRO B  686  LEU B  697  1                                  12    
HELIX   20  20 LYS B  700  ARG B  704  5                                   5    
HELIX   21  21 SER B  706  GLU B  720  1                                  15    
SHEET    1   A 5 THR A 458  SER A 465  0                                        
SHEET    2   A 5 GLY A 469  LYS A 475 -1  O  VAL A 471   N  ILE A 463           
SHEET    3   A 5 ASP A 479  LEU A 485 -1  O  VAL A 480   N  GLY A 474           
SHEET    4   A 5 ALA A 526  GLN A 530 -1  O  ILE A 527   N  LYS A 483           
SHEET    5   A 5 PHE A 516  SER A 520 -1  N  GLY A 518   O  VAL A 528           
SHEET    1   B 3 GLY A 534  SER A 536  0                                        
SHEET    2   B 3 ILE A 582  HIS A 585 -1  O  LEU A 584   N  SER A 535           
SHEET    3   B 3 THR A 589  ILE A 592 -1  O  LYS A 591   N  PHE A 583           
SHEET    1   C 5 THR B 458  SER B 465  0                                        
SHEET    2   C 5 THR B 470  LYS B 475 -1  O  LYS B 473   N  GLY B 460           
SHEET    3   C 5 ASP B 479  LEU B 485 -1  O  MET B 484   N  THR B 470           
SHEET    4   C 5 LEU B 525  GLN B 530 -1  O  THR B 529   N  ALA B 481           
SHEET    5   C 5 PHE B 516  SER B 520 -1  N  GLY B 518   O  VAL B 528           
SHEET    1   D 2 ILE B 582  HIS B 585  0                                        
SHEET    2   D 2 THR B 589  ILE B 592 -1  O  THR B 589   N  HIS B 585           
CISPEP   1 ALA A  522    PRO A  523          0        -0.27                     
SITE     1 AC1 13 VAL A 471  ALA A 481  LYS A 483  LEU A 505                    
SITE     2 AC1 13 LEU A 514  THR A 529  GLN A 530  TRP A 531                    
SITE     3 AC1 13 CYS A 532  PHE A 583  ASP A 594  PHE A 595                    
SITE     4 AC1 13 GLY A 596                                                     
CRYST1   50.770  104.424  110.128  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.019697  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009576  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009080        0.00000                         
ATOM      1  N   ASP A 449     -15.047   9.355 -11.670  1.00 80.04           N  
ANISOU    1  N   ASP A 449     9855   9321  11236   -452   1214    -11       N  
ATOM      2  CA  ASP A 449     -14.538   9.164 -13.021  1.00 83.30           C  
ANISOU    2  CA  ASP A 449    10196   9808  11648   -424   1132     64       C  
ATOM      3  C   ASP A 449     -13.017   9.130 -12.998  1.00 76.40           C  
ANISOU    3  C   ASP A 449     9369   8972  10687   -374   1053     98       C  
ATOM      4  O   ASP A 449     -12.381   9.818 -12.197  1.00 67.69           O  
ANISOU    4  O   ASP A 449     8292   7844   9583   -357   1041     80       O  
ATOM      5  CB  ASP A 449     -15.032  10.281 -13.944  1.00 82.63           C  
ANISOU    5  CB  ASP A 449     9947   9738  11710   -431   1094    102       C  
ATOM      6  CG  ASP A 449     -15.551   9.755 -15.271  1.00 81.08           C  
ANISOU    6  CG  ASP A 449     9679   9593  11535   -439   1071    147       C  
ATOM      7  OD1 ASP A 449     -15.391   8.545 -15.536  1.00 78.75           O  
ANISOU    7  OD1 ASP A 449     9454   9328  11139   -435   1078    152       O  
ATOM      8  OD2 ASP A 449     -16.121  10.550 -16.050  1.00 79.01           O  
ANISOU    8  OD2 ASP A 449     9291   9338  11392   -449   1043    175       O  
ATOM      9  N   TRP A 450     -12.436   8.326 -13.881  1.00 63.98           N  
ANISOU    9  N   TRP A 450     7803   7462   9043   -351   1001    142       N  
ATOM     10  CA  TRP A 450     -10.992   8.142 -13.891  1.00 51.35           C  
ANISOU   10  CA  TRP A 450     6249   5904   7356   -304    927    163       C  
ATOM     11  C   TRP A 450     -10.334   8.695 -15.147  1.00 42.87           C  
ANISOU   11  C   TRP A 450     5057   4907   6327   -286    842    231       C  
ATOM     12  O   TRP A 450      -9.221   8.302 -15.494  1.00 39.13           O  
ANISOU   12  O   TRP A 450     4605   4486   5777   -252    780    250       O  
ATOM     13  CB  TRP A 450     -10.640   6.665 -13.711  1.00 46.89           C  
ANISOU   13  CB  TRP A 450     5814   5348   6655   -288    931    145       C  
ATOM     14  CG  TRP A 450     -10.991   6.139 -12.353  1.00 47.22           C  
ANISOU   14  CG  TRP A 450     5998   5313   6629   -303   1002     81       C  
ATOM     15  CD1 TRP A 450     -12.177   5.584 -11.970  1.00 51.48           C  
ANISOU   15  CD1 TRP A 450     6586   5804   7169   -350   1092     44       C  
ATOM     16  CD2 TRP A 450     -10.148   6.126 -11.193  1.00 43.12           C  
ANISOU   16  CD2 TRP A 450     5597   4757   6031   -275    991     45       C  
ATOM     17  NE1 TRP A 450     -12.124   5.223 -10.646  1.00 56.25           N  
ANISOU   17  NE1 TRP A 450     7335   6344   7693   -358   1139    -10       N  
ATOM     18  CE2 TRP A 450     -10.890   5.544 -10.145  1.00 43.95           C  
ANISOU   18  CE2 TRP A 450     5823   4791   6084   -311   1076     -9       C  
ATOM     19  CE3 TRP A 450      -8.839   6.547 -10.939  1.00 30.98           C  
ANISOU   19  CE3 TRP A 450     4074   3240   4459   -226    918     50       C  
ATOM     20  CZ2 TRP A 450     -10.368   5.373  -8.867  1.00 41.72           C  
ANISOU   20  CZ2 TRP A 450     5682   4457   5714   -298   1086    -52       C  
ATOM     21  CZ3 TRP A 450      -8.322   6.376  -9.670  1.00 41.75           C  
ANISOU   21  CZ3 TRP A 450     5570   4552   5740   -208    925      3       C  
ATOM     22  CH2 TRP A 450      -9.085   5.793  -8.648  1.00 48.88           C  
ANISOU   22  CH2 TRP A 450     6599   5384   6589   -243   1007    -45       C  
ATOM     23  N   GLU A 451     -11.019   9.609 -15.823  1.00 40.93           N  
ANISOU   23  N   GLU A 451     4685   4664   6201   -311    838    263       N  
ATOM     24  CA  GLU A 451     -10.452  10.250 -17.000  1.00 44.36           C  
ANISOU   24  CA  GLU A 451     5009   5166   6681   -303    759    331       C  
ATOM     25  C   GLU A 451      -9.395  11.261 -16.588  1.00 35.04           C  
ANISOU   25  C   GLU A 451     3813   3984   5516   -280    713    338       C  
ATOM     26  O   GLU A 451      -9.611  12.062 -15.682  1.00 40.90           O  
ANISOU   26  O   GLU A 451     4560   4665   6314   -285    742    305       O  
ATOM     27  CB  GLU A 451     -11.537  10.937 -17.828  1.00 54.84           C  
ANISOU   27  CB  GLU A 451     6215   6489   8134   -337    763    366       C  
ATOM     28  CG  GLU A 451     -10.984  11.748 -18.985  1.00 63.51           C  
ANISOU   28  CG  GLU A 451     7204   7646   9282   -336    681    440       C  
ATOM     29  CD  GLU A 451     -12.061  12.228 -19.934  1.00 65.27           C  
ANISOU   29  CD  GLU A 451     7318   7869   9614   -366    673    479       C  
ATOM     30  OE1 GLU A 451     -13.218  11.781 -19.796  1.00 70.08           O  
ANISOU   30  OE1 GLU A 451     7931   8441  10253   -385    730    445       O  
ATOM     31  OE2 GLU A 451     -11.746  13.049 -20.821  1.00 62.98           O  
ANISOU   31  OE2 GLU A 451     6939   7613   9377   -373    607    542       O  
ATOM     32  N   ILE A 452      -8.249  11.212 -17.257  1.00 32.41           N  
ANISOU   32  N   ILE A 452     3459   3721   5134   -258    643    374       N  
ATOM     33  CA  ILE A 452      -7.156  12.130 -16.979  1.00 23.88           C  
ANISOU   33  CA  ILE A 452     2358   2650   4065   -238    595    379       C  
ATOM     34  C   ILE A 452      -7.138  13.237 -18.028  1.00 40.15           C  
ANISOU   34  C   ILE A 452     4287   4744   6223   -261    545    447       C  
ATOM     35  O   ILE A 452      -6.853  12.984 -19.199  1.00 51.35           O  
ANISOU   35  O   ILE A 452     5654   6235   7623   -270    501    496       O  
ATOM     36  CB  ILE A 452      -5.805  11.393 -16.961  1.00 27.36           C  
ANISOU   36  CB  ILE A 452     2863   3145   4387   -199    548    364       C  
ATOM     37  CG1 ILE A 452      -5.820  10.291 -15.898  1.00 15.82           C  
ANISOU   37  CG1 ILE A 452     1544   1642   2826   -175    588    301       C  
ATOM     38  CG2 ILE A 452      -4.668  12.367 -16.707  1.00 30.19           C  
ANISOU   38  CG2 ILE A 452     3193   3516   4763   -180    499    364       C  
ATOM     39  CD1 ILE A 452      -4.645   9.338 -15.976  1.00 22.15           C  
ANISOU   39  CD1 ILE A 452     2412   2494   3509   -133    537    281       C  
ATOM     40  N   PRO A 453      -7.455  14.472 -17.608  1.00 41.73           N  
ANISOU   40  N   PRO A 453     4437   4890   6528   -273    552    448       N  
ATOM     41  CA  PRO A 453      -7.568  15.633 -18.501  1.00 36.64           C  
ANISOU   41  CA  PRO A 453     3675   4259   5989   -299    505    512       C  
ATOM     42  C   PRO A 453      -6.383  15.771 -19.455  1.00 44.11           C  
ANISOU   42  C   PRO A 453     4579   5289   6892   -298    433    563       C  
ATOM     43  O   PRO A 453      -5.273  15.352 -19.127  1.00 40.43           O  
ANISOU   43  O   PRO A 453     4168   4858   6337   -270    416    536       O  
ATOM     44  CB  PRO A 453      -7.605  16.813 -17.527  1.00 29.14           C  
ANISOU   44  CB  PRO A 453     2711   3236   5124   -296    518    483       C  
ATOM     45  CG  PRO A 453      -8.222  16.249 -16.297  1.00 29.97           C  
ANISOU   45  CG  PRO A 453     2906   3279   5202   -287    593    407       C  
ATOM     46  CD  PRO A 453      -7.734  14.828 -16.206  1.00 29.84           C  
ANISOU   46  CD  PRO A 453     2990   3304   5046   -265    604    384       C  
ATOM     47  N   ASP A 454      -6.630  16.357 -20.623  1.00 52.80           N  
ANISOU   47  N   ASP A 454     5586   6421   8056   -330    392    634       N  
ATOM     48  CA  ASP A 454      -5.603  16.529 -21.648  1.00 51.35           C  
ANISOU   48  CA  ASP A 454     5355   6321   7833   -342    328    687       C  
ATOM     49  C   ASP A 454      -4.440  17.392 -21.161  1.00 47.70           C  
ANISOU   49  C   ASP A 454     4891   5859   7376   -332    299    676       C  
ATOM     50  O   ASP A 454      -4.644  18.477 -20.617  1.00 47.05           O  
ANISOU   50  O   ASP A 454     4781   5713   7384   -336    301    675       O  
ATOM     51  CB  ASP A 454      -6.221  17.142 -22.911  1.00 63.62           C  
ANISOU   51  CB  ASP A 454     6815   7894   9465   -385    290    768       C  
ATOM     52  CG  ASP A 454      -5.210  17.329 -24.033  1.00 73.69           C  
ANISOU   52  CG  ASP A 454     8043   9259  10695   -410    229    825       C  
ATOM     53  OD1 ASP A 454      -4.080  16.807 -23.925  1.00 77.79           O  
ANISOU   53  OD1 ASP A 454     8599   9836  11121   -392    219    796       O  
ATOM     54  OD2 ASP A 454      -5.553  17.999 -25.031  1.00 68.59           O  
ANISOU   54  OD2 ASP A 454     7325   8627  10110   -449    189    897       O  
ATOM     55  N   GLY A 455      -3.220  16.899 -21.358  1.00 45.78           N  
ANISOU   55  N   GLY A 455     4670   5686   7036   -317    271    662       N  
ATOM     56  CA  GLY A 455      -2.027  17.657 -21.026  1.00 42.94           C  
ANISOU   56  CA  GLY A 455     4301   5339   6676   -309    239    649       C  
ATOM     57  C   GLY A 455      -1.349  17.250 -19.730  1.00 52.32           C  
ANISOU   57  C   GLY A 455     5577   6500   7802   -259    260    565       C  
ATOM     58  O   GLY A 455      -0.195  17.608 -19.493  1.00 50.12           O  
ANISOU   58  O   GLY A 455     5298   6248   7498   -244    230    541       O  
ATOM     59  N   GLN A 456      -2.056  16.503 -18.888  1.00 49.33           N  
ANISOU   59  N   GLN A 456     5277   6070   7397   -233    309    519       N  
ATOM     60  CA  GLN A 456      -1.517  16.112 -17.588  1.00 35.14           C  
ANISOU   60  CA  GLN A 456     3576   4236   5538   -187    328    441       C  
ATOM     61  C   GLN A 456      -0.395  15.079 -17.692  1.00 36.13           C  
ANISOU   61  C   GLN A 456     3755   4429   5543   -152    295    405       C  
ATOM     62  O   GLN A 456       0.510  15.049 -16.858  1.00 36.99           O  
ANISOU   62  O   GLN A 456     3919   4529   5606   -114    280    348       O  
ATOM     63  CB  GLN A 456      -2.629  15.597 -16.670  1.00 35.87           C  
ANISOU   63  CB  GLN A 456     3744   4253   5632   -179    393    403       C  
ATOM     64  CG  GLN A 456      -3.615  16.667 -16.223  1.00 39.85           C  
ANISOU   64  CG  GLN A 456     4205   4680   6258   -203    429    410       C  
ATOM     65  CD  GLN A 456      -4.411  16.247 -15.001  1.00 38.41           C  
ANISOU   65  CD  GLN A 456     4111   4421   6063   -193    497    348       C  
ATOM     66  OE1 GLN A 456      -4.175  15.184 -14.428  1.00 42.30           O  
ANISOU   66  OE1 GLN A 456     4707   4914   6452   -167    516    303       O  
ATOM     67  NE2 GLN A 456      -5.355  17.087 -14.593  1.00 35.26           N  
ANISOU   67  NE2 GLN A 456     3672   3955   5770   -215    534    343       N  
ATOM     68  N   ILE A 457      -0.454  14.237 -18.718  1.00 35.99           N  
ANISOU   68  N   ILE A 457     3720   4477   5476   -164    279    433       N  
ATOM     69  CA  ILE A 457       0.531  13.174 -18.881  1.00 33.89           C  
ANISOU   69  CA  ILE A 457     3500   4275   5100   -131    246    393       C  
ATOM     70  C   ILE A 457       1.624  13.542 -19.880  1.00 41.19           C  
ANISOU   70  C   ILE A 457     4342   5292   6015   -148    190    414       C  
ATOM     71  O   ILE A 457       1.342  13.906 -21.024  1.00 37.76           O  
ANISOU   71  O   ILE A 457     3823   4905   5620   -196    178    479       O  
ATOM     72  CB  ILE A 457      -0.131  11.860 -19.334  1.00 34.08           C  
ANISOU   72  CB  ILE A 457     3565   4319   5065   -130    265    396       C  
ATOM     73  CG1 ILE A 457      -1.301  11.508 -18.416  1.00 46.25           C  
ANISOU   73  CG1 ILE A 457     5184   5770   6617   -126    328    376       C  
ATOM     74  CG2 ILE A 457       0.887  10.733 -19.358  1.00 23.74           C  
ANISOU   74  CG2 ILE A 457     2312   3064   3644    -89    227    344       C  
ATOM     75  CD1 ILE A 457      -2.090  10.303 -18.877  1.00 48.99           C  
ANISOU   75  CD1 ILE A 457     5565   6130   6920   -133    354    383       C  
ATOM     76  N   THR A 458       2.873  13.443 -19.440  1.00 40.82           N  
ANISOU   76  N   THR A 458     4323   5272   5915   -111    155    356       N  
ATOM     77  CA  THR A 458       4.009  13.669 -20.319  1.00 35.47           C  
ANISOU   77  CA  THR A 458     3572   4687   5217   -127    105    358       C  
ATOM     78  C   THR A 458       4.480  12.338 -20.891  1.00 44.63           C  
ANISOU   78  C   THR A 458     4756   5921   6281   -107     80    325       C  
ATOM     79  O   THR A 458       5.099  11.538 -20.190  1.00 42.62           O  
ANISOU   79  O   THR A 458     4578   5659   5955    -51     62    252       O  
ATOM     80  CB  THR A 458       5.174  14.346 -19.579  1.00 30.07           C  
ANISOU   80  CB  THR A 458     2891   3997   4536   -100     78    302       C  
ATOM     81  OG1 THR A 458       4.712  15.550 -18.953  1.00 26.25           O  
ANISOU   81  OG1 THR A 458     2392   3439   4145   -114    103    326       O  
ATOM     82  CG2 THR A 458       6.302  14.678 -20.550  1.00 28.76           C  
ANISOU   82  CG2 THR A 458     2639   3929   4358   -128     34    304       C  
ATOM     83  N   VAL A 459       4.176  12.101 -22.163  1.00 41.08           N  
ANISOU   83  N   VAL A 459     4240   5539   5829   -152     75    379       N  
ATOM     84  CA  VAL A 459       4.559  10.857 -22.821  1.00 35.09           C  
ANISOU   84  CA  VAL A 459     3492   4857   4986   -138     51    350       C  
ATOM     85  C   VAL A 459       6.036  10.889 -23.200  1.00 44.19           C  
ANISOU   85  C   VAL A 459     4599   6094   6095   -132      1    299       C  
ATOM     86  O   VAL A 459       6.534  11.897 -23.700  1.00 54.84           O  
ANISOU   86  O   VAL A 459     5868   7482   7486   -175    -12    326       O  
ATOM     87  CB  VAL A 459       3.709  10.604 -24.072  1.00 38.94           C  
ANISOU   87  CB  VAL A 459     3920   5391   5486   -190     64    421       C  
ATOM     88  CG1 VAL A 459       4.017   9.237 -24.659  1.00 36.62           C  
ANISOU   88  CG1 VAL A 459     3642   5167   5105   -172     43    385       C  
ATOM     89  CG2 VAL A 459       2.236  10.717 -23.731  1.00 36.69           C  
ANISOU   89  CG2 VAL A 459     3663   5020   5257   -200    113    467       C  
ATOM     90  N   GLY A 460       6.733   9.783 -22.960  1.00 45.65           N  
ANISOU   90  N   GLY A 460     4838   6309   6200    -80    -29    222       N  
ATOM     91  CA  GLY A 460       8.162   9.723 -23.208  1.00 43.47           C  
ANISOU   91  CA  GLY A 460     4522   6110   5884    -66    -79    154       C  
ATOM     92  C   GLY A 460       8.567   8.599 -24.140  1.00 55.80           C  
ANISOU   92  C   GLY A 460     6060   7765   7377    -65   -108    122       C  
ATOM     93  O   GLY A 460       8.028   8.464 -25.239  1.00 64.78           O  
ANISOU   93  O   GLY A 460     7139   8957   8518   -118    -94    181       O  
ATOM     94  N   GLN A 461       9.520   7.788 -23.693  1.00 57.20           N  
ANISOU   94  N   GLN A 461     6282   7961   7493     -4   -152     25       N  
ATOM     95  CA  GLN A 461      10.065   6.706 -24.507  1.00 56.72           C  
ANISOU   95  CA  GLN A 461     6194   7989   7368      5   -188    -24       C  
ATOM     96  C   GLN A 461       8.996   5.744 -25.014  1.00 47.12           C  
ANISOU   96  C   GLN A 461     5006   6770   6128     -4   -164     20       C  
ATOM     97  O   GLN A 461       8.163   5.267 -24.246  1.00 48.16           O  
ANISOU   97  O   GLN A 461     5232   6812   6253     29   -140     32       O  
ATOM     98  CB  GLN A 461      11.120   5.927 -23.717  1.00 89.08           C  
ANISOU   98  CB  GLN A 461    10357  12080  11410     87   -244   -142       C  
ATOM     99  CG  GLN A 461      12.397   6.704 -23.443  1.00111.66           C  
ANISOU   99  CG  GLN A 461    13170  14972  14285     97   -279   -208       C  
ATOM    100  CD  GLN A 461      13.397   5.907 -22.627  1.00124.11           C  
ANISOU  100  CD  GLN A 461    14814  16534  15809    185   -343   -328       C  
ATOM    101  OE1 GLN A 461      13.035   4.947 -21.947  1.00127.05           O  
ANISOU  101  OE1 GLN A 461    15294  16840  16138    245   -357   -352       O  
ATOM    102  NE2 GLN A 461      14.663   6.303 -22.689  1.00123.80           N  
ANISOU  102  NE2 GLN A 461    14712  16554  15772    193   -383   -407       N  
ATOM    103  N   ARG A 462       9.027   5.464 -26.313  1.00 49.68           N  
ANISOU  103  N   ARG A 462     5245   7193   6437    -53   -168     42       N  
ATOM    104  CA  ARG A 462       8.182   4.432 -26.896  1.00 49.61           C  
ANISOU  104  CA  ARG A 462     5253   7197   6399    -58   -153     69       C  
ATOM    105  C   ARG A 462       8.757   3.084 -26.493  1.00 58.57           C  
ANISOU  105  C   ARG A 462     6457   8334   7464     15   -197    -28       C  
ATOM    106  O   ARG A 462       9.936   2.818 -26.715  1.00 69.68           O  
ANISOU  106  O   ARG A 462     7827   9809   8837     35   -247   -109       O  
ATOM    107  CB  ARG A 462       8.173   4.548 -28.422  1.00 46.21           C  
ANISOU  107  CB  ARG A 462     4709   6880   5968   -132   -150    113       C  
ATOM    108  CG  ARG A 462       6.974   3.890 -29.096  1.00 53.04           C  
ANISOU  108  CG  ARG A 462     5575   7748   6829   -156   -120    174       C  
ATOM    109  CD  ARG A 462       7.196   3.697 -30.596  1.00 61.93           C  
ANISOU  109  CD  ARG A 462     6599   9001   7932   -217   -131    191       C  
ATOM    110  NE  ARG A 462       7.763   2.385 -30.898  1.00 67.67           N  
ANISOU  110  NE  ARG A 462     7332   9788   8592   -179   -165    107       N  
ATOM    111  CZ  ARG A 462       7.059   1.345 -31.336  1.00 71.66           C  
ANISOU  111  CZ  ARG A 462     7855  10304   9070   -172   -157    115       C  
ATOM    112  NH1 ARG A 462       5.753   1.460 -31.539  1.00 75.34           N  
ANISOU  112  NH1 ARG A 462     8331  10726   9569   -201   -113    201       N  
ATOM    113  NH2 ARG A 462       7.664   0.189 -31.578  1.00 69.00           N  
ANISOU  113  NH2 ARG A 462     7521  10020   8676   -136   -194     32       N  
ATOM    114  N   ILE A 463       7.931   2.231 -25.902  1.00 54.81           N  
ANISOU  114  N   ILE A 463     6080   7778   6965     52   -180    -23       N  
ATOM    115  CA  ILE A 463       8.418   0.959 -25.384  1.00 47.52           C  
ANISOU  115  CA  ILE A 463     5243   6837   5977    125   -226   -111       C  
ATOM    116  C   ILE A 463       8.243  -0.185 -26.378  1.00 51.42           C  
ANISOU  116  C   ILE A 463     5707   7400   6431    118   -239   -122       C  
ATOM    117  O   ILE A 463       9.179  -0.935 -26.647  1.00 51.75           O  
ANISOU  117  O   ILE A 463     5734   7500   6428    153   -296   -206       O  
ATOM    118  CB  ILE A 463       7.733   0.605 -24.054  1.00 50.81           C  
ANISOU  118  CB  ILE A 463     5803   7121   6381    173   -206   -110       C  
ATOM    119  CG1 ILE A 463       8.166   1.585 -22.961  1.00 50.65           C  
ANISOU  119  CG1 ILE A 463     5819   7037   6387    195   -209   -125       C  
ATOM    120  CG2 ILE A 463       8.064  -0.813 -23.640  1.00 60.87           C  
ANISOU  120  CG2 ILE A 463     7174   8370   7584    241   -254   -186       C  
ATOM    121  CD1 ILE A 463       9.667   1.708 -22.805  1.00 54.09           C  
ANISOU  121  CD1 ILE A 463     6228   7522   6803    236   -277   -216       C  
ATOM    122  N   GLY A 464       7.039  -0.313 -26.922  1.00 40.85           N  
ANISOU  122  N   GLY A 464     4357   6054   5111     74   -188    -44       N  
ATOM    123  CA  GLY A 464       6.741  -1.393 -27.842  1.00 45.13           C  
ANISOU  123  CA  GLY A 464     4873   6656   5618     65   -193    -50       C  
ATOM    124  C   GLY A 464       5.355  -1.255 -28.429  1.00 64.84           C  
ANISOU  124  C   GLY A 464     7345   9142   8150      9   -131     46       C  
ATOM    125  O   GLY A 464       4.610  -0.342 -28.077  1.00 61.84           O  
ANISOU  125  O   GLY A 464     6971   8703   7823    -20    -86    113       O  
ATOM    126  N   SER A 465       5.005  -2.170 -29.326  1.00 92.31           N  
ANISOU  126  N   SER A 465    10793  12678  11602     -5   -132     46       N  
ATOM    127  CA  SER A 465       3.726  -2.098 -30.017  1.00 92.81           C  
ANISOU  127  CA  SER A 465    10821  12744  11699    -58    -80    130       C  
ATOM    128  C   SER A 465       2.973  -3.415 -29.920  1.00 95.38           C  
ANISOU  128  C   SER A 465    11218  13030  11991    -30    -65    114       C  
ATOM    129  O   SER A 465       3.510  -4.422 -29.466  1.00 96.59           O  
ANISOU  129  O   SER A 465    11441  13166  12093     26   -103     39       O  
ATOM    130  CB  SER A 465       3.939  -1.740 -31.491  1.00 91.40           C  
ANISOU  130  CB  SER A 465    10509  12692  11527   -122    -88    163       C  
ATOM    131  OG  SER A 465       5.085  -0.921 -31.659  1.00 97.94           O  
ANISOU  131  OG  SER A 465    11275  13582  12357   -138   -120    139       O  
ATOM    132  N   GLY A 466       1.720  -3.392 -30.353  1.00 87.55           N  
ANISOU  132  N   GLY A 466    10209  12023  11033    -71    -14    182       N  
ATOM    133  CA  GLY A 466       0.892  -4.581 -30.398  1.00 97.97           C  
ANISOU  133  CA  GLY A 466    11583  13311  12329    -57      8    173       C  
ATOM    134  C   GLY A 466      -0.296  -4.270 -31.279  1.00115.10           C  
ANISOU  134  C   GLY A 466    13682  15505  14546   -117     55    252       C  
ATOM    135  O   GLY A 466      -0.459  -3.130 -31.706  1.00120.18           O  
ANISOU  135  O   GLY A 466    14250  16174  15239   -162     67    312       O  
ATOM    136  N   SER A 467      -1.126  -5.266 -31.562  1.00165.47           N  
ANISOU  136  N   SER A 467    20085  21874  20913   -116     80    250       N  
ATOM    137  CA  SER A 467      -2.311  -5.030 -32.378  1.00167.27           C  
ANISOU  137  CA  SER A 467    20247  22120  21187   -168    122    318       C  
ATOM    138  C   SER A 467      -3.161  -3.912 -31.779  1.00157.19           C  
ANISOU  138  C   SER A 467    18982  20761  19982   -193    170    377       C  
ATOM    139  O   SER A 467      -3.636  -3.024 -32.487  1.00159.99           O  
ANISOU  139  O   SER A 467    19251  21148  20390   -240    180    441       O  
ATOM    140  CB  SER A 467      -3.140  -6.308 -32.506  1.00140.50           C  
ANISOU  140  CB  SER A 467    16901  18708  17775   -158    149    298       C  
ATOM    141  OG  SER A 467      -4.359  -6.056 -33.184  1.00143.05           O  
ANISOU  141  OG  SER A 467    17166  19038  18150   -204    192    359       O  
ATOM    142  N   PHE A 468      -3.332  -3.966 -30.463  1.00 94.45           N  
ANISOU  142  N   PHE A 468    11145  12706  12036   -160    196    351       N  
ATOM    143  CA  PHE A 468      -4.162  -3.015 -29.733  1.00 82.14           C  
ANISOU  143  CA  PHE A 468     9608  11058  10544   -178    245    391       C  
ATOM    144  C   PHE A 468      -3.701  -1.564 -29.877  1.00 78.20           C  
ANISOU  144  C   PHE A 468     9036  10582  10094   -202    226    434       C  
ATOM    145  O   PHE A 468      -4.471  -0.701 -30.299  1.00 79.69           O  
ANISOU  145  O   PHE A 468     9160  10767  10352   -244    248    495       O  
ATOM    146  CB  PHE A 468      -4.203  -3.405 -28.257  1.00 89.46           C  
ANISOU  146  CB  PHE A 468    10673  11874  11444   -138    271    345       C  
ATOM    147  CG  PHE A 468      -2.943  -4.063 -27.775  1.00 92.61           C  
ANISOU  147  CG  PHE A 468    11139  12282  11766    -84    216    279       C  
ATOM    148  CD1 PHE A 468      -1.818  -3.310 -27.487  1.00 95.00           C  
ANISOU  148  CD1 PHE A 468    11426  12605  12065    -66    171    263       C  
ATOM    149  CD2 PHE A 468      -2.882  -5.437 -27.618  1.00 93.70           C  
ANISOU  149  CD2 PHE A 468    11356  12405  11840    -51    205    228       C  
ATOM    150  CE1 PHE A 468      -0.656  -3.913 -27.048  1.00 93.37           C  
ANISOU  150  CE1 PHE A 468    11277  12406  11793    -13    115    194       C  
ATOM    151  CE2 PHE A 468      -1.723  -6.047 -27.178  1.00 94.73           C  
ANISOU  151  CE2 PHE A 468    11549  12540  11905      3    145    163       C  
ATOM    152  CZ  PHE A 468      -0.608  -5.284 -26.892  1.00 96.14           C  
ANISOU  152  CZ  PHE A 468    11706  12740  12081     24     99    144       C  
ATOM    153  N   GLY A 469      -2.448  -1.301 -29.515  1.00 71.26           N  
ANISOU  153  N   GLY A 469     8170   9725   9182   -176    181    399       N  
ATOM    154  CA  GLY A 469      -1.895   0.041 -29.579  1.00 61.24           C  
ANISOU  154  CA  GLY A 469     6840   8475   7956   -198    162    432       C  
ATOM    155  C   GLY A 469      -0.412   0.082 -29.258  1.00 53.63           C  
ANISOU  155  C   GLY A 469     5888   7546   6943   -164    110    375       C  
ATOM    156  O   GLY A 469       0.254  -0.953 -29.228  1.00 57.80           O  
ANISOU  156  O   GLY A 469     6453   8103   7404   -126     78    312       O  
ATOM    157  N   THR A 470       0.106   1.284 -29.016  1.00 48.27           N  
ANISOU  157  N   THR A 470     5174   6863   6302   -177     98    394       N  
ATOM    158  CA  THR A 470       1.522   1.466 -28.707  1.00 43.91           C  
ANISOU  158  CA  THR A 470     4625   6345   5714   -149     50    338       C  
ATOM    159  C   THR A 470       1.726   1.857 -27.244  1.00 47.95           C  
ANISOU  159  C   THR A 470     5228   6756   6236   -106     58    306       C  
ATOM    160  O   THR A 470       0.988   2.680 -26.702  1.00 31.29           O  
ANISOU  160  O   THR A 470     3131   4572   4186   -122     98    348       O  
ATOM    161  CB  THR A 470       2.165   2.537 -29.608  1.00 44.14           C  
ANISOU  161  CB  THR A 470     4540   6460   5771   -200     25    375       C  
ATOM    162  OG1 THR A 470       1.953   2.199 -30.985  1.00 49.36           O  
ANISOU  162  OG1 THR A 470     5119   7217   6418   -246     18    408       O  
ATOM    163  CG2 THR A 470       3.659   2.635 -29.340  1.00 29.03           C  
ANISOU  163  CG2 THR A 470     2622   4590   3819   -172    -23    304       C  
ATOM    164  N   VAL A 471       2.736   1.265 -26.613  1.00 43.44           N  
ANISOU  164  N   VAL A 471     4718   6181   5606    -50     18    227       N  
ATOM    165  CA  VAL A 471       3.006   1.509 -25.202  1.00 36.99           C  
ANISOU  165  CA  VAL A 471     3999   5271   4786     -4     19    188       C  
ATOM    166  C   VAL A 471       4.186   2.453 -25.003  1.00 40.59           C  
ANISOU  166  C   VAL A 471     4410   5756   5254      3    -20    162       C  
ATOM    167  O   VAL A 471       5.283   2.201 -25.500  1.00 37.34           O  
ANISOU  167  O   VAL A 471     3954   5427   4807     15    -71    112       O  
ATOM    168  CB  VAL A 471       3.282   0.194 -24.449  1.00 47.16           C  
ANISOU  168  CB  VAL A 471     5406   6514   5998     60     -5    115       C  
ATOM    169  CG1 VAL A 471       3.670   0.477 -23.006  1.00 52.79           C  
ANISOU  169  CG1 VAL A 471     6223   7137   6700    107    -12     73       C  
ATOM    170  CG2 VAL A 471       2.068  -0.716 -24.509  1.00 41.19           C  
ANISOU  170  CG2 VAL A 471     4705   5715   5230     51     40    139       C  
ATOM    171  N   TYR A 472       3.948   3.541 -24.275  1.00 44.67           N  
ANISOU  171  N   TYR A 472     4938   6208   5827     -7      7    189       N  
ATOM    172  CA  TYR A 472       4.997   4.494 -23.933  1.00 37.85           C  
ANISOU  172  CA  TYR A 472     4042   5358   4982      1    -24    163       C  
ATOM    173  C   TYR A 472       5.157   4.563 -22.422  1.00 41.84           C  
ANISOU  173  C   TYR A 472     4658   5763   5477     56    -22    116       C  
ATOM    174  O   TYR A 472       4.266   4.159 -21.678  1.00 45.40           O  
ANISOU  174  O   TYR A 472     5200   6128   5921     70     17    124       O  
ATOM    175  CB  TYR A 472       4.648   5.893 -24.444  1.00 38.30           C  
ANISOU  175  CB  TYR A 472     4003   5428   5121    -63      1    240       C  
ATOM    176  CG  TYR A 472       4.415   5.991 -25.932  1.00 35.94           C  
ANISOU  176  CG  TYR A 472     3598   5221   4836   -125      0    298       C  
ATOM    177  CD1 TYR A 472       3.240   5.523 -26.500  1.00 48.96           C  
ANISOU  177  CD1 TYR A 472     5242   6866   6496   -151     33    351       C  
ATOM    178  CD2 TYR A 472       5.359   6.575 -26.766  1.00 48.62           C  
ANISOU  178  CD2 TYR A 472     5110   6921   6444   -161    -32    299       C  
ATOM    179  CE1 TYR A 472       3.016   5.617 -27.858  1.00 57.05           C  
ANISOU  179  CE1 TYR A 472     6172   7974   7529   -208     29    404       C  
ATOM    180  CE2 TYR A 472       5.145   6.675 -28.128  1.00 58.72           C  
ANISOU  180  CE2 TYR A 472     6298   8285   7727   -224    -33    354       C  
ATOM    181  CZ  TYR A 472       3.971   6.194 -28.668  1.00 69.08           C  
ANISOU  181  CZ  TYR A 472     7610   9590   9048   -245     -5    408       C  
ATOM    182  OH  TYR A 472       3.747   6.290 -30.021  1.00 90.27           O  
ANISOU  182  OH  TYR A 472    10207  12358  11734   -307     -9    464       O  
ATOM    183  N   LYS A 473       6.296   5.081 -21.975  1.00 49.09           N  
ANISOU  183  N   LYS A 473     5569   6694   6391     83    -62     65       N  
ATOM    184  CA  LYS A 473       6.494   5.398 -20.567  1.00 44.03           C  
ANISOU  184  CA  LYS A 473     5019   5961   5748    129    -62     25       C  
ATOM    185  C   LYS A 473       6.099   6.855 -20.365  1.00 47.85           C  
ANISOU  185  C   LYS A 473     5450   6411   6319     86    -23     81       C  
ATOM    186  O   LYS A 473       6.333   7.687 -21.240  1.00 40.62           O  
ANISOU  186  O   LYS A 473     4424   5560   5452     38    -27    121       O  
ATOM    187  CB  LYS A 473       7.954   5.175 -20.167  1.00 40.56           C  
ANISOU  187  CB  LYS A 473     4597   5550   5261    186   -132    -68       C  
ATOM    188  CG  LYS A 473       8.261   5.472 -18.708  1.00 36.67           C  
ANISOU  188  CG  LYS A 473     4204   4969   4762    238   -141   -115       C  
ATOM    189  CD  LYS A 473       9.694   5.094 -18.366  1.00 41.26           C  
ANISOU  189  CD  LYS A 473     4805   5580   5292    302   -219   -215       C  
ATOM    190  CE  LYS A 473      10.036   5.439 -16.925  1.00 43.21           C  
ANISOU  190  CE  LYS A 473     5149   5739   5530    354   -233   -262       C  
ATOM    191  NZ  LYS A 473      11.428   5.038 -16.570  1.00 49.15           N  
ANISOU  191  NZ  LYS A 473     5924   6518   6235    422   -317   -367       N  
ATOM    192  N   GLY A 474       5.494   7.167 -19.223  1.00 49.42           N  
ANISOU  192  N   GLY A 474     5729   6511   6538    101     13     83       N  
ATOM    193  CA  GLY A 474       4.974   8.504 -19.000  1.00 38.50           C  
ANISOU  193  CA  GLY A 474     4297   5087   5244     62     53    133       C  
ATOM    194  C   GLY A 474       5.197   9.078 -17.615  1.00 29.10           C  
ANISOU  194  C   GLY A 474     3178   3814   4066     97     60     93       C  
ATOM    195  O   GLY A 474       5.704   8.407 -16.714  1.00 31.67           O  
ANISOU  195  O   GLY A 474     3605   4105   4324    154     35     26       O  
ATOM    196  N   LYS A 475       4.806  10.338 -17.452  1.00 38.64           N  
ANISOU  196  N   LYS A 475     4331   4990   5361     62     90    134       N  
ATOM    197  CA  LYS A 475       4.944  11.041 -16.185  1.00 38.95           C  
ANISOU  197  CA  LYS A 475     4423   4953   5425     87    102    100       C  
ATOM    198  C   LYS A 475       3.592  11.563 -15.713  1.00 35.72           C  
ANISOU  198  C   LYS A 475     4027   4462   5082     55    170    142       C  
ATOM    199  O   LYS A 475       2.995  12.432 -16.348  1.00 37.81           O  
ANISOU  199  O   LYS A 475     4199   4733   5433      4    192    205       O  
ATOM    200  CB  LYS A 475       5.934  12.200 -16.327  1.00 46.69           C  
ANISOU  200  CB  LYS A 475     5316   5969   6454     80     69     92       C  
ATOM    201  CG  LYS A 475       7.347  11.773 -16.699  1.00 51.81           C  
ANISOU  201  CG  LYS A 475     5945   6699   7044    112      3     34       C  
ATOM    202  CD  LYS A 475       8.255  11.720 -15.479  1.00 67.39           C  
ANISOU  202  CD  LYS A 475     7997   8632   8976    178    -31    -53       C  
ATOM    203  CE  LYS A 475       7.768  10.709 -14.452  1.00 73.43           C  
ANISOU  203  CE  LYS A 475     8907   9321   9671    225    -19    -88       C  
ATOM    204  NZ  LYS A 475       8.595  10.733 -13.213  1.00 71.61           N  
ANISOU  204  NZ  LYS A 475     8761   9046   9402    288    -54   -169       N  
ATOM    205  N   TRP A 476       3.113  11.021 -14.599  1.00 33.46           N  
ANISOU  205  N   TRP A 476     3858   4099   4755     82    202    105       N  
ATOM    206  CA  TRP A 476       1.849  11.446 -14.008  1.00 47.11           C  
ANISOU  206  CA  TRP A 476     5609   5748   6542     52    272    128       C  
ATOM    207  C   TRP A 476       1.856  11.136 -12.516  1.00 53.56           C  
ANISOU  207  C   TRP A 476     6560   6486   7306     89    293     65       C  
ATOM    208  O   TRP A 476       1.572  10.009 -12.107  1.00 68.18           O  
ANISOU  208  O   TRP A 476     8521   8309   9076    107    306     39       O  
ATOM    209  CB  TRP A 476       0.675  10.743 -14.693  1.00 36.85           C  
ANISOU  209  CB  TRP A 476     4304   4451   5245     16    314    171       C  
ATOM    210  CG  TRP A 476      -0.648  11.369 -14.392  1.00 34.34           C  
ANISOU  210  CG  TRP A 476     3968   4068   5013    -25    382    198       C  
ATOM    211  CD1 TRP A 476      -1.093  12.585 -14.823  1.00 31.45           C  
ANISOU  211  CD1 TRP A 476     3492   3698   4759    -63    392    245       C  
ATOM    212  CD2 TRP A 476      -1.704  10.813 -13.599  1.00 36.82           C  
ANISOU  212  CD2 TRP A 476     4373   4309   5309    -34    448    176       C  
ATOM    213  NE1 TRP A 476      -2.359  12.823 -14.346  1.00 37.83           N  
ANISOU  213  NE1 TRP A 476     4312   4436   5626    -91    458    247       N  
ATOM    214  CE2 TRP A 476      -2.758  11.750 -13.592  1.00 40.69           C  
ANISOU  214  CE2 TRP A 476     4795   4758   5909    -77    498    203       C  
ATOM    215  CE3 TRP A 476      -1.861   9.616 -12.894  1.00 27.20           C  
ANISOU  215  CE3 TRP A 476     3289   3055   3992    -13    470    133       C  
ATOM    216  CZ2 TRP A 476      -3.953  11.526 -12.908  1.00 25.85           C  
ANISOU  216  CZ2 TRP A 476     2970   2808   4045   -101    572    183       C  
ATOM    217  CZ3 TRP A 476      -3.048   9.395 -12.215  1.00 25.46           C  
ANISOU  217  CZ3 TRP A 476     3130   2762   3780    -41    547    119       C  
ATOM    218  CH2 TRP A 476      -4.078  10.345 -12.227  1.00 20.42           C  
ANISOU  218  CH2 TRP A 476     2414   2089   3254    -86    600    140       C  
ATOM    219  N   HIS A 477       2.178  12.141 -11.706  1.00 50.57           N  
ANISOU  219  N   HIS A 477     6175   6068   6971     98    295     41       N  
ATOM    220  CA  HIS A 477       2.384  11.937 -10.277  1.00 42.88           C  
ANISOU  220  CA  HIS A 477     5326   5025   5939    135    304    -23       C  
ATOM    221  C   HIS A 477       3.378  10.802 -10.086  1.00 43.64           C  
ANISOU  221  C   HIS A 477     5517   5145   5918    193    243    -73       C  
ATOM    222  O   HIS A 477       3.172   9.910  -9.263  1.00 40.89           O  
ANISOU  222  O   HIS A 477     5303   4745   5487    216    254   -109       O  
ATOM    223  CB  HIS A 477       1.070  11.602  -9.573  1.00 30.90           C  
ANISOU  223  CB  HIS A 477     3891   3432   4420    107    383    -24       C  
ATOM    224  CG  HIS A 477      -0.044  12.548  -9.890  1.00 26.09           C  
ANISOU  224  CG  HIS A 477     3184   2801   3929     50    441     21       C  
ATOM    225  ND1 HIS A 477       0.039  13.903  -9.654  1.00 30.99           N  
ANISOU  225  ND1 HIS A 477     3724   3404   4645     38    445     25       N  
ATOM    226  CD2 HIS A 477      -1.274  12.333 -10.415  1.00 28.04           C  
ANISOU  226  CD2 HIS A 477     3400   3037   4217      5    495     60       C  
ATOM    227  CE1 HIS A 477      -1.087  14.484 -10.027  1.00 30.98           C  
ANISOU  227  CE1 HIS A 477     3649   3382   4742    -10    493     65       C  
ATOM    228  NE2 HIS A 477      -1.901  13.552 -10.491  1.00 20.93           N  
ANISOU  228  NE2 HIS A 477     2401   2112   3437    -31    524     85       N  
ATOM    229  N   GLY A 478       4.455  10.841 -10.863  1.00 33.77           N  
ANISOU  229  N   GLY A 478     4195   3973   4663    214    176    -78       N  
ATOM    230  CA  GLY A 478       5.419   9.760 -10.889  1.00 39.71           C  
ANISOU  230  CA  GLY A 478     5014   4759   5316    269    109   -129       C  
ATOM    231  C   GLY A 478       5.301   8.994 -12.191  1.00 47.16           C  
ANISOU  231  C   GLY A 478     5902   5775   6243    250     95    -93       C  
ATOM    232  O   GLY A 478       4.593   9.418 -13.102  1.00 55.39           O  
ANISOU  232  O   GLY A 478     6846   6847   7352    196    130    -29       O  
ATOM    233  N   ASP A 479       5.984   7.859 -12.278  1.00 55.93           N  
ANISOU  233  N   ASP A 479     7076   6911   7265    296     39   -138       N  
ATOM    234  CA  ASP A 479       6.000   7.071 -13.506  1.00 53.69           C  
ANISOU  234  CA  ASP A 479     6738   6701   6959    284     18   -116       C  
ATOM    235  C   ASP A 479       4.654   6.411 -13.807  1.00 45.74           C  
ANISOU  235  C   ASP A 479     5763   5666   5948    244     80    -65       C  
ATOM    236  O   ASP A 479       3.986   5.899 -12.909  1.00 39.96           O  
ANISOU  236  O   ASP A 479     5151   4856   5178    251    117    -76       O  
ATOM    237  CB  ASP A 479       7.096   6.006 -13.436  1.00 45.60           C  
ANISOU  237  CB  ASP A 479     5776   5705   5845    349    -62   -188       C  
ATOM    238  CG  ASP A 479       8.479   6.605 -13.299  1.00 43.87           C  
ANISOU  238  CG  ASP A 479     5507   5527   5633    387   -128   -247       C  
ATOM    239  OD1 ASP A 479       8.648   7.795 -13.637  1.00 58.40           O  
ANISOU  239  OD1 ASP A 479     7238   7400   7551    352   -113   -220       O  
ATOM    240  OD2 ASP A 479       9.399   5.885 -12.858  1.00 44.35           O  
ANISOU  240  OD2 ASP A 479     5640   5587   5625    452   -197   -322       O  
ATOM    241  N   VAL A 480       4.265   6.431 -15.079  1.00 38.67           N  
ANISOU  241  N   VAL A 480     4761   4839   5094    200     92    -11       N  
ATOM    242  CA  VAL A 480       3.081   5.712 -15.536  1.00 28.34           C  
ANISOU  242  CA  VAL A 480     3470   3518   3780    166    142     32       C  
ATOM    243  C   VAL A 480       3.368   5.018 -16.860  1.00 37.94           C  
ANISOU  243  C   VAL A 480     4614   4828   4974    159    107     46       C  
ATOM    244  O   VAL A 480       4.391   5.267 -17.496  1.00 38.76           O  
ANISOU  244  O   VAL A 480     4639   5009   5079    168     52     30       O  
ATOM    245  CB  VAL A 480       1.861   6.640 -15.722  1.00 22.61           C  
ANISOU  245  CB  VAL A 480     2677   2764   3151    105    215     96       C  
ATOM    246  CG1 VAL A 480       1.454   7.270 -14.402  1.00 25.48           C  
ANISOU  246  CG1 VAL A 480     3110   3033   3537    107    258     77       C  
ATOM    247  CG2 VAL A 480       2.156   7.709 -16.766  1.00 17.70           C  
ANISOU  247  CG2 VAL A 480     1903   2213   2608     69    196    144       C  
ATOM    248  N   ALA A 481       2.457   4.143 -17.268  1.00 33.45           N  
ANISOU  248  N   ALA A 481     4072   4253   4386    139    140     71       N  
ATOM    249  CA  ALA A 481       2.539   3.509 -18.574  1.00 31.89           C  
ANISOU  249  CA  ALA A 481     3800   4143   4174    124    116     90       C  
ATOM    250  C   ALA A 481       1.317   3.905 -19.390  1.00 39.31           C  
ANISOU  250  C   ALA A 481     4657   5095   5184     60    174    165       C  
ATOM    251  O   ALA A 481       0.186   3.780 -18.920  1.00 36.69           O  
ANISOU  251  O   ALA A 481     4377   4693   4870     40    236    183       O  
ATOM    252  CB  ALA A 481       2.626   2.006 -18.432  1.00 44.43           C  
ANISOU  252  CB  ALA A 481     5489   5720   5671    163     93     46       C  
ATOM    253  N   VAL A 482       1.546   4.382 -20.610  1.00 40.05           N  
ANISOU  253  N   VAL A 482     4623   5276   5317     26    154    205       N  
ATOM    254  CA  VAL A 482       0.461   4.865 -21.457  1.00 34.13           C  
ANISOU  254  CA  VAL A 482     3787   4541   4638    -33    196    279       C  
ATOM    255  C   VAL A 482       0.325   4.034 -22.730  1.00 35.52           C  
ANISOU  255  C   VAL A 482     3909   4801   4786    -52    181    299       C  
ATOM    256  O   VAL A 482       1.240   3.992 -23.551  1.00 34.97           O  
ANISOU  256  O   VAL A 482     3773   4822   4694    -53    131    291       O  
ATOM    257  CB  VAL A 482       0.681   6.334 -21.857  1.00 35.28           C  
ANISOU  257  CB  VAL A 482     3826   4713   4867    -70    188    325       C  
ATOM    258  CG1 VAL A 482      -0.602   6.924 -22.420  1.00 32.20           C  
ANISOU  258  CG1 VAL A 482     3370   4305   4559   -124    232    397       C  
ATOM    259  CG2 VAL A 482       1.167   7.143 -20.663  1.00 22.59           C  
ANISOU  259  CG2 VAL A 482     2262   3042   3279    -44    187    292       C  
ATOM    260  N   LYS A 483      -0.819   3.376 -22.890  1.00 36.14           N  
ANISOU  260  N   LYS A 483     4014   4851   4868    -69    226    319       N  
ATOM    261  CA  LYS A 483      -1.088   2.613 -24.103  1.00 31.16           C  
ANISOU  261  CA  LYS A 483     3328   4295   4217    -90    217    341       C  
ATOM    262  C   LYS A 483      -1.955   3.419 -25.063  1.00 41.75           C  
ANISOU  262  C   LYS A 483     4560   5664   5639   -148    240    417       C  
ATOM    263  O   LYS A 483      -3.173   3.490 -24.904  1.00 52.40           O  
ANISOU  263  O   LYS A 483     5919   6956   7035   -170    292    444       O  
ATOM    264  CB  LYS A 483      -1.762   1.274 -23.781  1.00 30.76           C  
ANISOU  264  CB  LYS A 483     3373   4202   4113    -71    246    312       C  
ATOM    265  CG  LYS A 483      -1.991   0.395 -25.010  1.00 33.57           C  
ANISOU  265  CG  LYS A 483     3674   4637   4445    -87    234    326       C  
ATOM    266  CD  LYS A 483      -2.928  -0.775 -24.725  1.00 28.54           C  
ANISOU  266  CD  LYS A 483     3122   3947   3776    -82    277    308       C  
ATOM    267  CE  LYS A 483      -2.167  -2.050 -24.392  1.00 32.71           C  
ANISOU  267  CE  LYS A 483     3742   4477   4210    -30    237    243       C  
ATOM    268  NZ  LYS A 483      -3.084  -3.214 -24.206  1.00 32.44           N  
ANISOU  268  NZ  LYS A 483     3789   4393   4144    -31    279    230       N  
ATOM    269  N   MET A 484      -1.316   4.032 -26.053  1.00 45.24           N  
ANISOU  269  N   MET A 484     4900   6192   6096   -175    199    449       N  
ATOM    270  CA  MET A 484      -2.027   4.770 -27.087  1.00 43.97           C  
ANISOU  270  CA  MET A 484     4638   6066   6004   -232    206    525       C  
ATOM    271  C   MET A 484      -2.779   3.795 -27.983  1.00 52.03           C  
ANISOU  271  C   MET A 484     5639   7127   7002   -248    219    541       C  
ATOM    272  O   MET A 484      -2.164   3.013 -28.708  1.00 48.46           O  
ANISOU  272  O   MET A 484     5166   6758   6487   -243    186    520       O  
ATOM    273  CB  MET A 484      -1.044   5.574 -27.937  1.00 41.09           C  
ANISOU  273  CB  MET A 484     4181   5787   5644   -261    157    552       C  
ATOM    274  CG  MET A 484      -0.078   6.436 -27.146  1.00 34.22           C  
ANISOU  274  CG  MET A 484     3324   4893   4784   -243    138    526       C  
ATOM    275  SD  MET A 484      -0.908   7.708 -26.184  1.00 53.62           S  
ANISOU  275  SD  MET A 484     5795   7235   7343   -253    178    560       S  
ATOM    276  CE  MET A 484       0.480   8.754 -25.763  1.00108.04           C  
ANISOU  276  CE  MET A 484    12665  14141  14242   -245    139    537       C  
ATOM    277  N   LEU A 485      -4.106   3.833 -27.935  1.00 51.35           N  
ANISOU  277  N   LEU A 485     5555   6985   6971   -267    266    571       N  
ATOM    278  CA  LEU A 485      -4.900   2.963 -28.792  1.00 50.67           C  
ANISOU  278  CA  LEU A 485     5445   6935   6873   -284    280    585       C  
ATOM    279  C   LEU A 485      -4.709   3.348 -30.252  1.00 65.91           C  
ANISOU  279  C   LEU A 485     7262   8966   8813   -327    239    642       C  
ATOM    280  O   LEU A 485      -4.552   4.526 -30.578  1.00 57.21           O  
ANISOU  280  O   LEU A 485     6097   7875   7763   -358    218    691       O  
ATOM    281  CB  LEU A 485      -6.382   3.008 -28.414  1.00 38.04           C  
ANISOU  281  CB  LEU A 485     3864   5252   5338   -298    340    599       C  
ATOM    282  CG  LEU A 485      -6.741   2.481 -27.025  1.00 41.86           C  
ANISOU  282  CG  LEU A 485     4466   5636   5803   -266    391    542       C  
ATOM    283  CD1 LEU A 485      -8.169   1.972 -27.014  1.00 45.83           C  
ANISOU  283  CD1 LEU A 485     4982   6091   6340   -285    451    542       C  
ATOM    284  CD2 LEU A 485      -5.788   1.374 -26.614  1.00 42.81           C  
ANISOU  284  CD2 LEU A 485     4671   5773   5820   -222    369    483       C  
ATOM    285  N   ASN A 486      -4.715   2.347 -31.125  1.00 76.57           N  
ANISOU  285  N   ASN A 486     8592  10390  10112   -331    227    633       N  
ATOM    286  CA  ASN A 486      -4.555   2.575 -32.555  1.00 81.69           C  
ANISOU  286  CA  ASN A 486     9140  11142  10758   -376    191    683       C  
ATOM    287  C   ASN A 486      -5.810   3.210 -33.150  1.00 70.37           C  
ANISOU  287  C   ASN A 486     7647   9686   9404   -416    207    752       C  
ATOM    288  O   ASN A 486      -6.490   2.611 -33.982  1.00 71.83           O  
ANISOU  288  O   ASN A 486     7798   9910   9584   -433    211    768       O  
ATOM    289  CB  ASN A 486      -4.227   1.259 -33.264  1.00113.06           C  
ANISOU  289  CB  ASN A 486    13108  15198  14651   -366    176    645       C  
ATOM    290  CG  ASN A 486      -3.659   1.467 -34.655  1.00117.89           C  
ANISOU  290  CG  ASN A 486    13623  15933  15238   -411    132    679       C  
ATOM    291  OD1 ASN A 486      -2.535   1.944 -34.817  1.00122.61           O  
ANISOU  291  OD1 ASN A 486    14192  16584  15809   -421     97    671       O  
ATOM    292  ND2 ASN A 486      -4.430   1.094 -35.668  1.00111.65           N  
ANISOU  292  ND2 ASN A 486    12781  15188  14452   -440    135    714       N  
ATOM    293  N   VAL A 487      -6.111   4.427 -32.708  1.00 59.80           N  
ANISOU  293  N   VAL A 487     6296   8283   8143   -430    212    789       N  
ATOM    294  CA  VAL A 487      -7.285   5.160 -33.166  1.00 58.57           C  
ANISOU  294  CA  VAL A 487     6086   8093   8076   -463    218    850       C  
ATOM    295  C   VAL A 487      -6.971   6.649 -33.314  1.00 78.44           C  
ANISOU  295  C   VAL A 487     8552  10599  10653   -494    184    908       C  
ATOM    296  O   VAL A 487      -6.868   7.370 -32.321  1.00 80.16           O  
ANISOU  296  O   VAL A 487     8801  10741  10914   -478    198    895       O  
ATOM    297  CB  VAL A 487      -8.478   4.968 -32.199  1.00 51.38           C  
ANISOU  297  CB  VAL A 487     5228   7073   7222   -441    278    821       C  
ATOM    298  CG1 VAL A 487      -9.558   6.012 -32.450  1.00 38.44           C  
ANISOU  298  CG1 VAL A 487     3530   5383   5694   -470    278    874       C  
ATOM    299  CG2 VAL A 487      -9.044   3.561 -32.327  1.00 53.66           C  
ANISOU  299  CG2 VAL A 487     5551   7374   7464   -425    311    780       C  
ATOM    300  N   THR A 488      -6.808   7.096 -34.558  1.00114.89           N  
ANISOU  300  N   THR A 488    13094  15293  15268   -540    139    970       N  
ATOM    301  CA  THR A 488      -6.555   8.505 -34.850  1.00114.80           C  
ANISOU  301  CA  THR A 488    13034  15273  15312   -578    101   1034       C  
ATOM    302  C   THR A 488      -7.637   9.382 -34.230  1.00111.40           C  
ANISOU  302  C   THR A 488    12603  14730  14995   -573    118   1057       C  
ATOM    303  O   THR A 488      -7.388  10.123 -33.277  1.00108.52           O  
ANISOU  303  O   THR A 488    12263  14296  14672   -558    128   1042       O  
ATOM    304  CB  THR A 488      -6.534   8.782 -36.372  1.00 96.39           C  
ANISOU  304  CB  THR A 488    10627  13031  12965   -636     52   1107       C  
ATOM    305  OG1 THR A 488      -7.778   8.375 -36.956  1.00 95.48           O  
ANISOU  305  OG1 THR A 488    10488  12908  12883   -642     58   1130       O  
ATOM    306  CG2 THR A 488      -5.401   8.034 -37.048  1.00 92.33           C  
ANISOU  306  CG2 THR A 488    10101  12637  12342   -650     35   1082       C  
ATOM    307  N   ALA A 489      -8.839   9.289 -34.789  1.00 85.22           N  
ANISOU  307  N   ALA A 489     9253  11396  11730   -585    119   1087       N  
ATOM    308  CA  ALA A 489      -9.990  10.035 -34.300  1.00 89.99           C  
ANISOU  308  CA  ALA A 489     9847  11897  12449   -581    133   1099       C  
ATOM    309  C   ALA A 489     -11.098   9.068 -33.898  1.00 85.87           C  
ANISOU  309  C   ALA A 489     9353  11332  11942   -553    188   1046       C  
ATOM    310  O   ALA A 489     -11.404   8.131 -34.633  1.00 87.48           O  
ANISOU  310  O   ALA A 489     9545  11594  12100   -558    191   1043       O  
ATOM    311  CB  ALA A 489     -10.483  11.000 -35.366  1.00124.82           C  
ANISOU  311  CB  ALA A 489    14185  16316  16926   -624     74   1184       C  
ATOM    312  N   PRO A 490     -11.699   9.294 -32.721  1.00 83.92           N  
ANISOU  312  N   PRO A 490     9143  10984  11757   -528    236   1000       N  
ATOM    313  CA  PRO A 490     -12.731   8.424 -32.150  1.00 80.01           C  
ANISOU  313  CA  PRO A 490     8685  10438  11278   -507    301    939       C  
ATOM    314  C   PRO A 490     -14.145   8.902 -32.465  1.00 76.07           C  
ANISOU  314  C   PRO A 490     8127   9885  10891   -521    301    955       C  
ATOM    315  O   PRO A 490     -14.460  10.065 -32.222  1.00 68.93           O  
ANISOU  315  O   PRO A 490     7190   8920  10082   -528    281    978       O  
ATOM    316  CB  PRO A 490     -12.494   8.556 -30.638  1.00 76.21           C  
ANISOU  316  CB  PRO A 490     8278   9876  10801   -479    351    879       C  
ATOM    317  CG  PRO A 490     -11.459   9.677 -30.464  1.00 77.25           C  
ANISOU  317  CG  PRO A 490     8398  10011  10943   -484    307    913       C  
ATOM    318  CD  PRO A 490     -11.325  10.361 -31.784  1.00 81.29           C  
ANISOU  318  CD  PRO A 490     8826  10582  11477   -520    237    996       C  
ATOM    319  N   THR A 491     -14.988   8.016 -32.987  1.00 90.34           N  
ANISOU  319  N   THR A 491     9920  11712  12692   -523    322    939       N  
ATOM    320  CA  THR A 491     -16.397   8.338 -33.177  1.00 96.80           C  
ANISOU  320  CA  THR A 491    10686  12475  13620   -530    329    935       C  
ATOM    321  C   THR A 491     -17.145   8.176 -31.865  1.00 99.78           C  
ANISOU  321  C   THR A 491    11110  12756  14047   -513    410    854       C  
ATOM    322  O   THR A 491     -16.712   7.423 -30.993  1.00104.47           O  
ANISOU  322  O   THR A 491    11786  13341  14569   -497    465    801       O  
ATOM    323  CB  THR A 491     -17.057   7.434 -34.226  1.00 85.30           C  
ANISOU  323  CB  THR A 491     9193  11077  12141   -539    324    941       C  
ATOM    324  OG1 THR A 491     -16.877   6.061 -33.857  1.00 75.67           O  
ANISOU  324  OG1 THR A 491     8039   9884  10830   -524    383    883       O  
ATOM    325  CG2 THR A 491     -16.441   7.680 -35.583  1.00 88.91           C  
ANISOU  325  CG2 THR A 491     9597  11629  12555   -564    243   1022       C  
ATOM    326  N   PRO A 492     -18.271   8.888 -31.717  1.00 87.82           N  
ANISOU  326  N   PRO A 492     9545  11168  12655   -518    415    841       N  
ATOM    327  CA  PRO A 492     -19.104   8.753 -30.520  1.00 85.23           C  
ANISOU  327  CA  PRO A 492     9253  10751  12381   -510    497    757       C  
ATOM    328  C   PRO A 492     -19.391   7.287 -30.214  1.00 81.77           C  
ANISOU  328  C   PRO A 492     8878  10327  11864   -506    572    694       C  
ATOM    329  O   PRO A 492     -19.469   6.914 -29.044  1.00 92.13           O  
ANISOU  329  O   PRO A 492    10265  11585  13156   -501    646    628       O  
ATOM    330  CB  PRO A 492     -20.394   9.474 -30.914  1.00 77.95           C  
ANISOU  330  CB  PRO A 492     8241   9778  11597   -520    476    755       C  
ATOM    331  CG  PRO A 492     -19.950  10.506 -31.892  1.00 78.39           C  
ANISOU  331  CG  PRO A 492     8233   9866  11687   -528    374    848       C  
ATOM    332  CD  PRO A 492     -18.805   9.894 -32.653  1.00 76.33           C  
ANISOU  332  CD  PRO A 492     7998   9709  11296   -534    340    903       C  
ATOM    333  N   GLN A 493     -19.537   6.471 -31.255  1.00 56.37           N  
ANISOU  333  N   GLN A 493     5635   7181   8602   -511    552    716       N  
ATOM    334  CA  GLN A 493     -19.777   5.040 -31.081  1.00 73.95           C  
ANISOU  334  CA  GLN A 493     7920   9425  10752   -509    617    661       C  
ATOM    335  C   GLN A 493     -18.520   4.313 -30.598  1.00 62.30           C  
ANISOU  335  C   GLN A 493     6539   7985   9147   -492    628    654       C  
ATOM    336  O   GLN A 493     -18.603   3.361 -29.820  1.00 58.59           O  
ANISOU  336  O   GLN A 493     6153   7487   8621   -486    695    594       O  
ATOM    337  CB  GLN A 493     -20.292   4.407 -32.379  1.00160.88           C  
ANISOU  337  CB  GLN A 493    18868  20503  21755   -518    588    685       C  
ATOM    338  CG  GLN A 493     -21.688   4.850 -32.801  1.00180.89           C  
ANISOU  338  CG  GLN A 493    21318  23000  24414   -529    585    672       C  
ATOM    339  CD  GLN A 493     -22.146   4.183 -34.087  1.00194.82           C  
ANISOU  339  CD  GLN A 493    23024  24835  26164   -536    554    694       C  
ATOM    340  OE1 GLN A 493     -21.330   3.734 -34.892  1.00196.55           O  
ANISOU  340  OE1 GLN A 493    23245  25142  26293   -536    510    742       O  
ATOM    341  NE2 GLN A 493     -23.458   4.117 -34.286  1.00200.76           N  
ANISOU  341  NE2 GLN A 493    23721  25552  27006   -542    576    653       N  
ATOM    342  N   GLN A 494     -17.359   4.761 -31.071  1.00 75.93           N  
ANISOU  342  N   GLN A 494     8252   9770  10827   -487    560    714       N  
ATOM    343  CA  GLN A 494     -16.081   4.241 -30.594  1.00 78.71           C  
ANISOU  343  CA  GLN A 494     8685  10153  11068   -468    559    703       C  
ATOM    344  C   GLN A 494     -15.832   4.682 -29.152  1.00 79.35           C  
ANISOU  344  C   GLN A 494     8839  10151  11159   -455    601    661       C  
ATOM    345  O   GLN A 494     -15.166   3.988 -28.383  1.00 77.04           O  
ANISOU  345  O   GLN A 494     8640   9851  10782   -435    628    622       O  
ATOM    346  CB  GLN A 494     -14.932   4.717 -31.492  1.00 70.27           C  
ANISOU  346  CB  GLN A 494     7572   9170   9957   -471    477    771       C  
ATOM    347  CG  GLN A 494     -14.786   3.953 -32.804  1.00 64.31           C  
ANISOU  347  CG  GLN A 494     6774   8516   9145   -482    440    801       C  
ATOM    348  CD  GLN A 494     -13.687   4.518 -33.691  1.00 55.96           C  
ANISOU  348  CD  GLN A 494     5669   7544   8049   -495    364    865       C  
ATOM    349  OE1 GLN A 494     -13.432   5.724 -33.693  1.00 44.74           O  
ANISOU  349  OE1 GLN A 494     4214   6104   6681   -508    327    908       O  
ATOM    350  NE2 GLN A 494     -13.034   3.647 -34.453  1.00 53.40           N  
ANISOU  350  NE2 GLN A 494     5342   7313   7633   -496    341    867       N  
ATOM    351  N   LEU A 495     -16.377   5.840 -28.793  1.00 76.05           N  
ANISOU  351  N   LEU A 495     8379   9670  10848   -464    602    667       N  
ATOM    352  CA  LEU A 495     -16.180   6.407 -27.465  1.00 67.39           C  
ANISOU  352  CA  LEU A 495     7339   8496   9772   -455    638    628       C  
ATOM    353  C   LEU A 495     -16.838   5.541 -26.395  1.00 65.37           C  
ANISOU  353  C   LEU A 495     7170   8175   9491   -455    731    547       C  
ATOM    354  O   LEU A 495     -16.260   5.299 -25.336  1.00 70.56           O  
ANISOU  354  O   LEU A 495     7922   8799  10089   -441    763    509       O  
ATOM    355  CB  LEU A 495     -16.728   7.835 -27.410  1.00 65.00           C  
ANISOU  355  CB  LEU A 495     6960   8139   9599   -467    616    649       C  
ATOM    356  CG  LEU A 495     -15.883   8.838 -26.626  1.00 72.34           C  
ANISOU  356  CG  LEU A 495     7909   9034  10541   -456    598    656       C  
ATOM    357  CD1 LEU A 495     -14.436   8.774 -27.085  1.00 76.71           C  
ANISOU  357  CD1 LEU A 495     8478   9666  11002   -444    538    703       C  
ATOM    358  CD2 LEU A 495     -16.435  10.246 -26.780  1.00 78.47           C  
ANISOU  358  CD2 LEU A 495     8599   9764  11452   -468    563    685       C  
ATOM    359  N   GLN A 496     -18.050   5.075 -26.681  1.00 56.29           N  
ANISOU  359  N   GLN A 496     5991   7009   8388   -473    773    519       N  
ATOM    360  CA  GLN A 496     -18.762   4.186 -25.771  1.00 57.69           C  
ANISOU  360  CA  GLN A 496     6249   7129   8541   -483    866    441       C  
ATOM    361  C   GLN A 496     -18.076   2.827 -25.721  1.00 64.96           C  
ANISOU  361  C   GLN A 496     7265   8089   9327   -469    878    428       C  
ATOM    362  O   GLN A 496     -17.937   2.227 -24.657  1.00 71.39           O  
ANISOU  362  O   GLN A 496     8189   8856  10078   -467    934    377       O  
ATOM    363  CB  GLN A 496     -20.220   4.026 -26.203  1.00 59.76           C  
ANISOU  363  CB  GLN A 496     6444   7371   8891   -508    905    411       C  
ATOM    364  CG  GLN A 496     -21.069   3.240 -25.218  1.00 69.61           C  
ANISOU  364  CG  GLN A 496     7769   8553  10127   -530   1011    324       C  
ATOM    365  CD  GLN A 496     -21.079   3.865 -23.835  1.00 75.89           C  
ANISOU  365  CD  GLN A 496     8622   9267  10946   -537   1063    275       C  
ATOM    366  OE1 GLN A 496     -20.352   3.434 -22.941  1.00 74.42           O  
ANISOU  366  OE1 GLN A 496     8548   9061  10666   -529   1089    256       O  
ATOM    367  NE2 GLN A 496     -21.903   4.892 -23.656  1.00 75.58           N  
ANISOU  367  NE2 GLN A 496     8505   9179  11034   -552   1074    253       N  
ATOM    368  N   ALA A 497     -17.648   2.346 -26.883  1.00 83.32           N  
ANISOU  368  N   ALA A 497     9549  10501  11609   -461    821    474       N  
ATOM    369  CA  ALA A 497     -16.910   1.094 -26.962  1.00 82.42           C  
ANISOU  369  CA  ALA A 497     9512  10431  11372   -443    817    463       C  
ATOM    370  C   ALA A 497     -15.687   1.142 -26.051  1.00 82.83           C  
ANISOU  370  C   ALA A 497     9657  10468  11347   -416    803    454       C  
ATOM    371  O   ALA A 497     -15.313   0.139 -25.444  1.00 87.58           O  
ANISOU  371  O   ALA A 497    10365  11054  11857   -402    828    415       O  
ATOM    372  CB  ALA A 497     -16.495   0.815 -28.395  1.00 47.45           C  
ANISOU  372  CB  ALA A 497     5007   6105   6916   -439    748    517       C  
ATOM    373  N   PHE A 498     -15.071   2.317 -25.961  1.00 65.89           N  
ANISOU  373  N   PHE A 498     7471   8324   9239   -409    757    488       N  
ATOM    374  CA  PHE A 498     -13.889   2.510 -25.129  1.00 55.10           C  
ANISOU  374  CA  PHE A 498     6179   6946   7811   -382    737    478       C  
ATOM    375  C   PHE A 498     -14.258   2.462 -23.651  1.00 56.42           C  
ANISOU  375  C   PHE A 498     6448   7015   7974   -384    809    417       C  
ATOM    376  O   PHE A 498     -13.652   1.724 -22.873  1.00 62.66           O  
ANISOU  376  O   PHE A 498     7352   7785   8671   -363    822    381       O  
ATOM    377  CB  PHE A 498     -13.217   3.844 -25.468  1.00 47.58           C  
ANISOU  377  CB  PHE A 498     5148   6020   6911   -379    673    530       C  
ATOM    378  CG  PHE A 498     -11.924   4.079 -24.737  1.00 41.86           C  
ANISOU  378  CG  PHE A 498     4487   5293   6125   -350    644    519       C  
ATOM    379  CD1 PHE A 498     -10.870   3.191 -24.867  1.00 37.86           C  
ANISOU  379  CD1 PHE A 498     4034   4841   5511   -322    610    507       C  
ATOM    380  CD2 PHE A 498     -11.757   5.198 -23.938  1.00 33.31           C  
ANISOU  380  CD2 PHE A 498     3404   4157   5098   -348    647    516       C  
ATOM    381  CE1 PHE A 498      -9.678   3.407 -24.202  1.00 34.08           C  
ANISOU  381  CE1 PHE A 498     3609   4360   4980   -292    579    490       C  
ATOM    382  CE2 PHE A 498     -10.566   5.421 -23.272  1.00 30.83           C  
ANISOU  382  CE2 PHE A 498     3144   3841   4729   -320    619    502       C  
ATOM    383  CZ  PHE A 498      -9.525   4.524 -23.404  1.00 28.01           C  
ANISOU  383  CZ  PHE A 498     2841   3538   4265   -291    584    488       C  
ATOM    384  N   LYS A 499     -15.260   3.248 -23.275  1.00 42.85           N  
ANISOU  384  N   LYS A 499     4689   5236   6357   -409    854    403       N  
ATOM    385  CA  LYS A 499     -15.724   3.305 -21.894  1.00 58.95           C  
ANISOU  385  CA  LYS A 499     6814   7184   8401   -421    930    341       C  
ATOM    386  C   LYS A 499     -16.095   1.926 -21.355  1.00 73.59           C  
ANISOU  386  C   LYS A 499     8782   9008  10170   -430    996    288       C  
ATOM    387  O   LYS A 499     -15.852   1.623 -20.187  1.00 86.64           O  
ANISOU  387  O   LYS A 499    10553  10605  11762   -427   1036    245       O  
ATOM    388  CB  LYS A 499     -16.917   4.255 -21.769  1.00 70.78           C  
ANISOU  388  CB  LYS A 499     8231   8631  10032   -452    970    325       C  
ATOM    389  CG  LYS A 499     -16.583   5.704 -22.078  1.00 78.32           C  
ANISOU  389  CG  LYS A 499     9089   9594  11077   -444    908    372       C  
ATOM    390  CD  LYS A 499     -17.806   6.593 -21.940  1.00 88.84           C  
ANISOU  390  CD  LYS A 499    10342  10869  12546   -471    943    348       C  
ATOM    391  CE  LYS A 499     -17.469   8.040 -22.252  1.00 93.87           C  
ANISOU  391  CE  LYS A 499    10887  11507  13274   -463    875    397       C  
ATOM    392  NZ  LYS A 499     -18.670   8.912 -22.154  1.00100.85           N  
ANISOU  392  NZ  LYS A 499    11687  12331  14299   -485    899    369       N  
ATOM    393  N   ASN A 500     -16.688   1.096 -22.208  1.00 78.59           N  
ANISOU  393  N   ASN A 500     9385   9677  10797   -442   1005    292       N  
ATOM    394  CA  ASN A 500     -17.090  -0.248 -21.808  1.00 83.44           C  
ANISOU  394  CA  ASN A 500    10103  10265  11335   -455   1066    245       C  
ATOM    395  C   ASN A 500     -15.892  -1.109 -21.423  1.00 85.66           C  
ANISOU  395  C   ASN A 500    10503  10559  11486   -420   1032    242       C  
ATOM    396  O   ASN A 500     -15.963  -1.903 -20.485  1.00 89.30           O  
ANISOU  396  O   ASN A 500    11094  10963  11874   -427   1082    197       O  
ATOM    397  CB  ASN A 500     -17.896  -0.926 -22.919  1.00 89.46           C  
ANISOU  397  CB  ASN A 500    10796  11072  12123   -472   1074    253       C  
ATOM    398  CG  ASN A 500     -19.212  -0.224 -23.201  1.00 81.66           C  
ANISOU  398  CG  ASN A 500     9703  10059  11263   -506   1114    240       C  
ATOM    399  OD1 ASN A 500     -19.416   0.923 -22.804  1.00 79.26           O  
ANISOU  399  OD1 ASN A 500     9354   9720  11042   -513   1116    239       O  
ATOM    400  ND2 ASN A 500     -20.112  -0.913 -23.892  1.00 77.81           N  
ANISOU  400  ND2 ASN A 500     9175   9591  10798   -527   1143    226       N  
ATOM    401  N   GLU A 501     -14.793  -0.946 -22.154  1.00 90.19           N  
ANISOU  401  N   GLU A 501    11031  11207  12031   -384    943    288       N  
ATOM    402  CA  GLU A 501     -13.563  -1.676 -21.868  1.00 95.27           C  
ANISOU  402  CA  GLU A 501    11770  11869  12560   -344    896    281       C  
ATOM    403  C   GLU A 501     -12.885  -1.143 -20.608  1.00 91.45           C  
ANISOU  403  C   GLU A 501    11374  11327  12047   -326    896    259       C  
ATOM    404  O   GLU A 501     -12.290  -1.903 -19.845  1.00 94.53           O  
ANISOU  404  O   GLU A 501    11891  11685  12341   -303    892    227       O  
ATOM    405  CB  GLU A 501     -12.604  -1.609 -23.060  1.00106.17           C  
ANISOU  405  CB  GLU A 501    13064  13352  13925   -317    804    328       C  
ATOM    406  CG  GLU A 501     -13.100  -2.336 -24.302  1.00108.92           C  
ANISOU  406  CG  GLU A 501    13341  13765  14278   -330    796    346       C  
ATOM    407  CD  GLU A 501     -12.148  -2.207 -25.477  1.00115.64           C  
ANISOU  407  CD  GLU A 501    14105  14722  15113   -310    710    390       C  
ATOM    408  OE1 GLU A 501     -11.204  -1.394 -25.395  1.00120.02           O  
ANISOU  408  OE1 GLU A 501    14636  15299  15668   -292    659    410       O  
ATOM    409  OE2 GLU A 501     -12.348  -2.916 -26.485  1.00116.17           O  
ANISOU  409  OE2 GLU A 501    14124  14851  15164   -315    695    401       O  
ATOM    410  N   VAL A 502     -12.978   0.167 -20.395  1.00 82.41           N  
ANISOU  410  N   VAL A 502    10160  10165  10985   -335    895    274       N  
ATOM    411  CA  VAL A 502     -12.426   0.787 -19.193  1.00 69.64           C  
ANISOU  411  CA  VAL A 502     8615   8492   9352   -320    900    250       C  
ATOM    412  C   VAL A 502     -13.242   0.399 -17.966  1.00 71.45           C  
ANISOU  412  C   VAL A 502     8959   8628   9561   -350    992    193       C  
ATOM    413  O   VAL A 502     -12.690   0.154 -16.894  1.00 70.00           O  
ANISOU  413  O   VAL A 502     8898   8396   9302   -334    998    161       O  
ATOM    414  CB  VAL A 502     -12.383   2.323 -19.308  1.00 49.22           C  
ANISOU  414  CB  VAL A 502     5919   5911   6870   -325    878    280       C  
ATOM    415  CG1 VAL A 502     -12.027   2.947 -17.968  1.00 42.52           C  
ANISOU  415  CG1 VAL A 502     5146   4994   6014   -317    898    245       C  
ATOM    416  CG2 VAL A 502     -11.388   2.746 -20.374  1.00 44.26           C  
ANISOU  416  CG2 VAL A 502     5198   5371   6246   -300    786    334       C  
ATOM    417  N   GLY A 503     -14.560   0.344 -18.133  1.00 76.74           N  
ANISOU  417  N   GLY A 503     9588   9273  10297   -395   1063    177       N  
ATOM    418  CA  GLY A 503     -15.452  -0.057 -17.061  1.00 73.78           C  
ANISOU  418  CA  GLY A 503     9313   8814   9906   -435   1161    118       C  
ATOM    419  C   GLY A 503     -15.149  -1.456 -16.560  1.00 74.09           C  
ANISOU  419  C   GLY A 503     9508   8828   9814   -429   1176     91       C  
ATOM    420  O   GLY A 503     -15.485  -1.806 -15.429  1.00 79.77           O  
ANISOU  420  O   GLY A 503    10351   9473  10485   -455   1243     44       O  
ATOM    421  N   VAL A 504     -14.514  -2.259 -17.409  1.00 67.53           N  
ANISOU  421  N   VAL A 504     8673   8058   8927   -396   1112    120       N  
ATOM    422  CA  VAL A 504     -14.113  -3.613 -17.038  1.00 62.72           C  
ANISOU  422  CA  VAL A 504     8208   7427   8195   -382   1108     98       C  
ATOM    423  C   VAL A 504     -12.778  -3.617 -16.294  1.00 58.02           C  
ANISOU  423  C   VAL A 504     7713   6818   7513   -332   1043     93       C  
ATOM    424  O   VAL A 504     -12.592  -4.374 -15.343  1.00 55.44           O  
ANISOU  424  O   VAL A 504     7543   6429   7092   -331   1062     60       O  
ATOM    425  CB  VAL A 504     -14.045  -4.542 -18.267  1.00 52.25           C  
ANISOU  425  CB  VAL A 504     6833   6171   6849   -368   1068    121       C  
ATOM    426  CG1 VAL A 504     -13.110  -5.715 -18.005  1.00 46.48           C  
ANISOU  426  CG1 VAL A 504     6232   5434   5993   -329   1018    108       C  
ATOM    427  CG2 VAL A 504     -15.437  -5.032 -18.637  1.00 50.12           C  
ANISOU  427  CG2 VAL A 504     6532   5886   6624   -421   1149    104       C  
ATOM    428  N   LEU A 505     -11.853  -2.769 -16.732  1.00 41.49           N  
ANISOU  428  N   LEU A 505     5531   4781   5451   -293    966    125       N  
ATOM    429  CA  LEU A 505     -10.589  -2.592 -16.030  1.00 38.00           C  
ANISOU  429  CA  LEU A 505     5166   4329   4944   -245    903    115       C  
ATOM    430  C   LEU A 505     -10.851  -1.925 -14.686  1.00 46.72           C  
ANISOU  430  C   LEU A 505     6345   5350   6054   -265    959     83       C  
ATOM    431  O   LEU A 505     -10.072  -2.055 -13.743  1.00 45.11           O  
ANISOU  431  O   LEU A 505     6258   5107   5774   -235    932     59       O  
ATOM    432  CB  LEU A 505      -9.636  -1.720 -16.849  1.00 32.36           C  
ANISOU  432  CB  LEU A 505     4323   3697   4275   -209    818    153       C  
ATOM    433  CG  LEU A 505      -9.174  -2.229 -18.213  1.00 34.41           C  
ANISOU  433  CG  LEU A 505     4496   4051   4526   -188    753    184       C  
ATOM    434  CD1 LEU A 505      -8.315  -1.180 -18.904  1.00 33.70           C  
ANISOU  434  CD1 LEU A 505     4281   4035   4487   -167    684    219       C  
ATOM    435  CD2 LEU A 505      -8.413  -3.533 -18.068  1.00 31.76           C  
ANISOU  435  CD2 LEU A 505     4274   3716   4077   -148    707    155       C  
ATOM    436  N   ARG A 506     -11.966  -1.209 -14.615  1.00 51.40           N  
ANISOU  436  N   ARG A 506     6870   5919   6741   -315   1034     80       N  
ATOM    437  CA  ARG A 506     -12.305  -0.401 -13.453  1.00 50.16           C  
ANISOU  437  CA  ARG A 506     6753   5692   6611   -340   1091     47       C  
ATOM    438  C   ARG A 506     -12.495  -1.253 -12.202  1.00 51.79           C  
ANISOU  438  C   ARG A 506     7147   5817   6714   -360   1148     -2       C  
ATOM    439  O   ARG A 506     -12.362  -0.764 -11.080  1.00 60.30           O  
ANISOU  439  O   ARG A 506     8299   6839   7773   -367   1174    -32       O  
ATOM    440  CB  ARG A 506     -13.578   0.394 -13.742  1.00 54.27           C  
ANISOU  440  CB  ARG A 506     7156   6206   7259   -392   1161     44       C  
ATOM    441  CG  ARG A 506     -13.690   1.705 -12.999  1.00 58.09           C  
ANISOU  441  CG  ARG A 506     7602   6653   7818   -403   1185     27       C  
ATOM    442  CD  ARG A 506     -15.014   2.379 -13.311  1.00 69.64           C  
ANISOU  442  CD  ARG A 506     8948   8104   9409   -453   1250     16       C  
ATOM    443  NE  ARG A 506     -15.208   3.586 -12.516  1.00 79.87           N  
ANISOU  443  NE  ARG A 506    10212   9355  10778   -467   1279    -12       N  
ATOM    444  CZ  ARG A 506     -15.550   3.584 -11.231  1.00 70.43           C  
ANISOU  444  CZ  ARG A 506     9121   8089   9551   -498   1353    -71       C  
ATOM    445  NH1 ARG A 506     -15.732   2.439 -10.590  1.00 66.24           N  
ANISOU  445  NH1 ARG A 506     8739   7520   8911   -521   1405   -105       N  
ATOM    446  NH2 ARG A 506     -15.705   4.728 -10.584  1.00 66.00           N  
ANISOU  446  NH2 ARG A 506     8516   7495   9065   -509   1375    -97       N  
ATOM    447  N   LYS A 507     -12.803  -2.530 -12.400  1.00 52.87           N  
ANISOU  447  N   LYS A 507     7364   5944   6781   -373   1167    -10       N  
ATOM    448  CA  LYS A 507     -13.107  -3.417 -11.282  1.00 60.87           C  
ANISOU  448  CA  LYS A 507     8561   6874   7693   -403   1226    -52       C  
ATOM    449  C   LYS A 507     -11.965  -4.367 -10.956  1.00 55.14           C  
ANISOU  449  C   LYS A 507     7976   6136   6837   -349   1147    -52       C  
ATOM    450  O   LYS A 507     -12.189  -5.468 -10.461  1.00 55.30           O  
ANISOU  450  O   LYS A 507     8144   6103   6764   -369   1176    -74       O  
ATOM    451  CB  LYS A 507     -14.381  -4.212 -11.563  1.00 88.87           C  
ANISOU  451  CB  LYS A 507    12117  10400  11250   -465   1315    -70       C  
ATOM    452  CG  LYS A 507     -14.444  -4.813 -12.949  1.00 97.15           C  
ANISOU  452  CG  LYS A 507    13069  11520  12323   -447   1274    -36       C  
ATOM    453  CD  LYS A 507     -15.832  -5.342 -13.242  1.00102.47           C  
ANISOU  453  CD  LYS A 507    13723  12177  13035   -513   1371    -59       C  
ATOM    454  CE  LYS A 507     -16.890  -4.277 -12.985  1.00110.08           C  
ANISOU  454  CE  LYS A 507    14593  13119  14112   -565   1454    -84       C  
ATOM    455  NZ  LYS A 507     -18.154  -4.578 -13.715  1.00114.39           N  
ANISOU  455  NZ  LYS A 507    15052  13679  14731   -613   1521    -99       N  
ATOM    456  N   THR A 508     -10.741  -3.933 -11.234  1.00 61.79           N  
ANISOU  456  N   THR A 508     8775   7028   7676   -283   1046    -31       N  
ATOM    457  CA  THR A 508      -9.559  -4.732 -10.924  1.00 60.10           C  
ANISOU  457  CA  THR A 508     8682   6805   7349   -223    958    -38       C  
ATOM    458  C   THR A 508      -8.683  -4.088  -9.848  1.00 58.68           C  
ANISOU  458  C   THR A 508     8577   6588   7131   -189    920    -59       C  
ATOM    459  O   THR A 508      -7.902  -3.181 -10.129  1.00 65.15           O  
ANISOU  459  O   THR A 508     9296   7457   8000   -149    859    -46       O  
ATOM    460  CB  THR A 508      -8.709  -5.023 -12.184  1.00 44.57           C  
ANISOU  460  CB  THR A 508     6614   4930   5391   -167    859     -9       C  
ATOM    461  OG1 THR A 508      -8.409  -3.797 -12.861  1.00 38.07           O  
ANISOU  461  OG1 THR A 508     5620   4177   4668   -154    829     19       O  
ATOM    462  CG2 THR A 508      -9.458  -5.947 -13.131  1.00 39.40           C  
ANISOU  462  CG2 THR A 508     5923   4303   4745   -194    887      4       C  
ATOM    463  N   ARG A 509      -8.826  -4.566  -8.614  1.00 47.77           N  
ANISOU  463  N   ARG A 509     7373   5117   5658   -208    956    -93       N  
ATOM    464  CA  ARG A 509      -7.993  -4.110  -7.506  1.00 34.97           C  
ANISOU  464  CA  ARG A 509     5848   3454   3984   -175    917   -117       C  
ATOM    465  C   ARG A 509      -7.283  -5.286  -6.846  1.00 39.72           C  
ANISOU  465  C   ARG A 509     6646   4001   4444   -137    857   -137       C  
ATOM    466  O   ARG A 509      -7.791  -5.876  -5.890  1.00 38.10           O  
ANISOU  466  O   ARG A 509     6605   3712   4158   -179    913   -159       O  
ATOM    467  CB  ARG A 509      -8.826  -3.354  -6.470  1.00 36.32           C  
ANISOU  467  CB  ARG A 509     6054   3564   4180   -237   1020   -143       C  
ATOM    468  CG  ARG A 509      -9.217  -1.950  -6.889  1.00 32.24           C  
ANISOU  468  CG  ARG A 509     5352   3094   3805   -255   1053   -131       C  
ATOM    469  CD  ARG A 509      -9.997  -1.244  -5.794  1.00 33.83           C  
ANISOU  469  CD  ARG A 509     5593   3232   4029   -315   1151   -167       C  
ATOM    470  NE  ARG A 509     -10.228   0.164  -6.107  1.00 34.95           N  
ANISOU  470  NE  ARG A 509     5563   3410   4306   -322   1166   -160       N  
ATOM    471  CZ  ARG A 509      -9.400   1.151  -5.775  1.00 39.21           C  
ANISOU  471  CZ  ARG A 509     6061   3962   4875   -281   1114   -161       C  
ATOM    472  NH1 ARG A 509      -8.279   0.889  -5.115  1.00 40.89           N  
ANISOU  472  NH1 ARG A 509     6389   4157   4991   -228   1042   -174       N  
ATOM    473  NH2 ARG A 509      -9.693   2.403  -6.103  1.00 31.35           N  
ANISOU  473  NH2 ARG A 509     4909   2994   4006   -292   1130   -152       N  
ATOM    474  N   HIS A 510      -6.103  -5.615  -7.362  1.00 45.32           N  
ANISOU  474  N   HIS A 510     7338   4756   5126    -60    739   -132       N  
ATOM    475  CA  HIS A 510      -5.337  -6.758  -6.884  1.00 41.83           C  
ANISOU  475  CA  HIS A 510     7067   4266   4559    -12    660   -153       C  
ATOM    476  C   HIS A 510      -3.845  -6.516  -7.110  1.00 51.88           C  
ANISOU  476  C   HIS A 510     8299   5589   5825     80    529   -165       C  
ATOM    477  O   HIS A 510      -3.455  -5.847  -8.068  1.00 58.62           O  
ANISOU  477  O   HIS A 510     8977   6532   6765    103    496   -149       O  
ATOM    478  CB  HIS A 510      -5.786  -8.022  -7.618  1.00 40.76           C  
ANISOU  478  CB  HIS A 510     6958   4135   4393    -26    665   -141       C  
ATOM    479  CG  HIS A 510      -5.335  -9.294  -6.972  1.00 45.06           C  
ANISOU  479  CG  HIS A 510     7709   4605   4807      3    608   -163       C  
ATOM    480  ND1 HIS A 510      -4.052  -9.779  -7.100  1.00 55.88           N  
ANISOU  480  ND1 HIS A 510     9116   5991   6126     90    475   -181       N  
ATOM    481  CD2 HIS A 510      -6.003 -10.189  -6.207  1.00 47.67           C  
ANISOU  481  CD2 HIS A 510     8221   4842   5048    -46    663   -172       C  
ATOM    482  CE1 HIS A 510      -3.946 -10.915  -6.433  1.00 54.84           C  
ANISOU  482  CE1 HIS A 510     9182   5774   5880     99    444   -197       C  
ATOM    483  NE2 HIS A 510      -5.115 -11.187  -5.883  1.00 41.73           N  
ANISOU  483  NE2 HIS A 510     7618   4047   4193     14    558   -189       N  
ATOM    484  N   VAL A 511      -3.016  -7.066  -6.228  1.00 46.78           N  
ANISOU  484  N   VAL A 511     7816   4883   5074    129    454   -197       N  
ATOM    485  CA  VAL A 511      -1.574  -6.832  -6.270  1.00 41.52           C  
ANISOU  485  CA  VAL A 511     7124   4254   4397    218    329   -223       C  
ATOM    486  C   VAL A 511      -0.897  -7.555  -7.436  1.00 44.17           C  
ANISOU  486  C   VAL A 511     7382   4661   4739    271    239   -224       C  
ATOM    487  O   VAL A 511       0.185  -7.164  -7.880  1.00 45.63           O  
ANISOU  487  O   VAL A 511     7473   4912   4953    333    150   -243       O  
ATOM    488  CB  VAL A 511      -0.906  -7.245  -4.945  1.00 39.56           C  
ANISOU  488  CB  VAL A 511     7082   3914   4033    259    268   -261       C  
ATOM    489  CG1 VAL A 511      -1.136  -8.724  -4.675  1.00 34.82           C  
ANISOU  489  CG1 VAL A 511     6663   3241   3325    256    250   -266       C  
ATOM    490  CG2 VAL A 511       0.580  -6.920  -4.966  1.00 46.86           C  
ANISOU  490  CG2 VAL A 511     7970   4880   4956    353    139   -297       C  
ATOM    491  N   ASN A 512      -1.540  -8.606  -7.935  1.00 50.35           N  
ANISOU  491  N   ASN A 512     8200   5433   5496    244    265   -209       N  
ATOM    492  CA  ASN A 512      -0.985  -9.389  -9.036  1.00 51.27           C  
ANISOU  492  CA  ASN A 512     8248   5615   5615    289    185   -215       C  
ATOM    493  C   ASN A 512      -1.589  -9.020 -10.389  1.00 45.47           C  
ANISOU  493  C   ASN A 512     7314   4978   4983    249    238   -177       C  
ATOM    494  O   ASN A 512      -1.179  -9.537 -11.428  1.00 38.42           O  
ANISOU  494  O   ASN A 512     6338   4156   4105    279    181   -180       O  
ATOM    495  CB  ASN A 512      -1.149 -10.885  -8.764  1.00 47.33           C  
ANISOU  495  CB  ASN A 512     7923   5044   5018    296    160   -228       C  
ATOM    496  CG  ASN A 512      -0.372 -11.340  -7.543  1.00 47.43           C  
ANISOU  496  CG  ASN A 512     8134   4963   4923    348     79   -267       C  
ATOM    497  OD1 ASN A 512      -0.907 -12.025  -6.670  1.00 50.90           O  
ANISOU  497  OD1 ASN A 512     8760   5302   5278    316    114   -266       O  
ATOM    498  ND2 ASN A 512       0.897 -10.954  -7.472  1.00 42.22           N  
ANISOU  498  ND2 ASN A 512     7440   4337   4264    427    -29   -303       N  
ATOM    499  N   ILE A 513      -2.569  -8.123 -10.362  1.00 41.20           N  
ANISOU  499  N   ILE A 513     6700   4441   4514    182    344   -145       N  
ATOM    500  CA  ILE A 513      -3.153  -7.584 -11.579  1.00 35.79           C  
ANISOU  500  CA  ILE A 513     5823   3843   3933    144    391   -107       C  
ATOM    501  C   ILE A 513      -2.616  -6.177 -11.811  1.00 34.07           C  
ANISOU  501  C   ILE A 513     5461   3688   3797    158    373    -96       C  
ATOM    502  O   ILE A 513      -2.737  -5.311 -10.944  1.00 40.19           O  
ANISOU  502  O   ILE A 513     6263   4421   4589    143    409   -100       O  
ATOM    503  CB  ILE A 513      -4.689  -7.538 -11.495  1.00 34.12           C  
ANISOU  503  CB  ILE A 513     5615   3594   3758     59    519    -81       C  
ATOM    504  CG1 ILE A 513      -5.252  -8.938 -11.257  1.00 32.21           C  
ANISOU  504  CG1 ILE A 513     5518   3286   3432     39    544    -92       C  
ATOM    505  CG2 ILE A 513      -5.276  -6.946 -12.764  1.00 40.91           C  
ANISOU  505  CG2 ILE A 513     6276   4542   4727     25    557    -42       C  
ATOM    506  CD1 ILE A 513      -4.938  -9.910 -12.367  1.00 27.21           C  
ANISOU  506  CD1 ILE A 513     4837   2712   2789     70    484    -89       C  
ATOM    507  N   LEU A 514      -2.011  -5.958 -12.975  1.00 49.76           N  
ANISOU  507  N   LEU A 514     7298   5777   5833    183    316    -85       N  
ATOM    508  CA  LEU A 514      -1.473  -4.648 -13.329  1.00 46.86           C  
ANISOU  508  CA  LEU A 514     6787   5474   5545    190    296    -72       C  
ATOM    509  C   LEU A 514      -2.427  -3.542 -12.886  1.00 49.02           C  
ANISOU  509  C   LEU A 514     7022   5713   5890    132    391    -44       C  
ATOM    510  O   LEU A 514      -3.631  -3.623 -13.128  1.00 55.05           O  
ANISOU  510  O   LEU A 514     7765   6462   6691     74    475    -17       O  
ATOM    511  CB  LEU A 514      -1.239  -4.561 -14.837  1.00 44.15           C  
ANISOU  511  CB  LEU A 514     6272   5244   5257    189    265    -47       C  
ATOM    512  CG  LEU A 514      -0.621  -3.265 -15.360  1.00 42.69           C  
ANISOU  512  CG  LEU A 514     5936   5135   5150    191    238    -31       C  
ATOM    513  CD1 LEU A 514       0.834  -3.161 -14.929  1.00 43.31           C  
ANISOU  513  CD1 LEU A 514     6044   5225   5186    259    144    -82       C  
ATOM    514  CD2 LEU A 514      -0.741  -3.188 -16.873  1.00 35.26           C  
ANISOU  514  CD2 LEU A 514     4835   4297   4265    167    232      6       C  
ATOM    515  N   LEU A 515      -1.889  -2.512 -12.239  1.00 32.24           N  
ANISOU  515  N   LEU A 515     4885   3576   3790    148    377    -55       N  
ATOM    516  CA  LEU A 515      -2.718  -1.443 -11.690  1.00 30.60           C  
ANISOU  516  CA  LEU A 515     4649   3328   3649     99    460    -38       C  
ATOM    517  C   LEU A 515      -3.226  -0.471 -12.754  1.00 36.90           C  
ANISOU  517  C   LEU A 515     5260   4194   4565     59    491     10       C  
ATOM    518  O   LEU A 515      -2.456   0.305 -13.318  1.00 30.10           O  
ANISOU  518  O   LEU A 515     4286   3399   3752     80    439     22       O  
ATOM    519  CB  LEU A 515      -1.960  -0.673 -10.603  1.00 40.33           C  
ANISOU  519  CB  LEU A 515     5934   4522   4867    131    432    -71       C  
ATOM    520  CG  LEU A 515      -2.721   0.507  -9.988  1.00 44.17           C  
ANISOU  520  CG  LEU A 515     6385   4968   5428     84    513    -61       C  
ATOM    521  CD1 LEU A 515      -3.992   0.027  -9.300  1.00 36.59           C  
ANISOU  521  CD1 LEU A 515     5530   3929   4444     27    611    -67       C  
ATOM    522  CD2 LEU A 515      -1.844   1.290  -9.021  1.00 36.86           C  
ANISOU  522  CD2 LEU A 515     5497   4015   4491    121    475    -94       C  
ATOM    523  N   PHE A 516      -4.528  -0.523 -13.020  1.00 35.64           N  
ANISOU  523  N   PHE A 516     5072   4018   4453      1    575     35       N  
ATOM    524  CA  PHE A 516      -5.177   0.453 -13.884  1.00 28.07           C  
ANISOU  524  CA  PHE A 516     3950   3105   3610    -40    609     79       C  
ATOM    525  C   PHE A 516      -5.291   1.775 -13.139  1.00 42.21           C  
ANISOU  525  C   PHE A 516     5712   4858   5468    -54    639     76       C  
ATOM    526  O   PHE A 516      -5.853   1.827 -12.046  1.00 59.59           O  
ANISOU  526  O   PHE A 516     8007   6981   7654    -76    700     47       O  
ATOM    527  CB  PHE A 516      -6.562  -0.043 -14.296  1.00 37.86           C  
ANISOU  527  CB  PHE A 516     5176   4330   4880    -94    687     96       C  
ATOM    528  CG  PHE A 516      -7.486   1.048 -14.758  1.00 44.58           C  
ANISOU  528  CG  PHE A 516     5893   5192   5853   -141    738    129       C  
ATOM    529  CD1 PHE A 516      -7.362   1.592 -16.026  1.00 43.05           C  
ANISOU  529  CD1 PHE A 516     5546   5080   5731   -145    699    176       C  
ATOM    530  CD2 PHE A 516      -8.491   1.518 -13.927  1.00 46.83           C  
ANISOU  530  CD2 PHE A 516     6206   5404   6182   -184    823    109       C  
ATOM    531  CE1 PHE A 516      -8.217   2.591 -16.452  1.00 43.82           C  
ANISOU  531  CE1 PHE A 516     5526   5180   5942   -185    736    207       C  
ATOM    532  CE2 PHE A 516      -9.349   2.516 -14.346  1.00 43.27           C  
ANISOU  532  CE2 PHE A 516     5630   4959   5851   -223    863    132       C  
ATOM    533  CZ  PHE A 516      -9.213   3.054 -15.611  1.00 37.89           C  
ANISOU  533  CZ  PHE A 516     4801   4354   5242   -221    815    183       C  
ATOM    534  N   MET A 517      -4.758   2.843 -13.726  1.00 29.33           N  
ANISOU  534  N   MET A 517     3951   3283   3910    -46    598    103       N  
ATOM    535  CA  MET A 517      -4.708   4.133 -13.042  1.00 21.17           C  
ANISOU  535  CA  MET A 517     2885   2216   2942    -53    614     98       C  
ATOM    536  C   MET A 517      -5.648   5.189 -13.621  1.00 23.54           C  
ANISOU  536  C   MET A 517     3048   2525   3370   -101    658    138       C  
ATOM    537  O   MET A 517      -6.176   6.023 -12.885  1.00 36.57           O  
ANISOU  537  O   MET A 517     4695   4121   5079   -124    707    124       O  
ATOM    538  CB  MET A 517      -3.272   4.666 -12.998  1.00 23.85           C  
ANISOU  538  CB  MET A 517     3199   2595   3267     -3    531     87       C  
ATOM    539  CG  MET A 517      -2.344   3.867 -12.095  1.00 23.13           C  
ANISOU  539  CG  MET A 517     3254   2474   3062     51    486     34       C  
ATOM    540  SD  MET A 517      -0.730   4.640 -11.870  1.00 39.06           S  
ANISOU  540  SD  MET A 517     5237   4528   5075    108    396      7       S  
ATOM    541  CE  MET A 517      -1.202   6.212 -11.154  1.00 24.48           C  
ANISOU  541  CE  MET A 517     3337   2633   3329     76    450     13       C  
ATOM    542  N   GLY A 518      -5.851   5.159 -14.934  1.00 35.49           N  
ANISOU  542  N   GLY A 518     4451   4107   4927   -117    637    185       N  
ATOM    543  CA  GLY A 518      -6.711   6.133 -15.581  1.00 33.55           C  
ANISOU  543  CA  GLY A 518     4075   3870   4802   -159    665    227       C  
ATOM    544  C   GLY A 518      -6.836   5.905 -17.072  1.00 35.70           C  
ANISOU  544  C   GLY A 518     4243   4223   5099   -172    632    279       C  
ATOM    545  O   GLY A 518      -6.265   4.960 -17.616  1.00 40.48           O  
ANISOU  545  O   GLY A 518     4871   4880   5628   -150    592    279       O  
ATOM    546  N   TYR A 519      -7.591   6.772 -17.737  1.00 29.92           N  
ANISOU  546  N   TYR A 519     3395   3500   4475   -208    645    320       N  
ATOM    547  CA  TYR A 519      -7.767   6.675 -19.179  1.00 32.48           C  
ANISOU  547  CA  TYR A 519     3614   3898   4827   -225    612    374       C  
ATOM    548  C   TYR A 519      -7.835   8.058 -19.810  1.00 40.99           C  
ANISOU  548  C   TYR A 519     4566   4995   6014   -247    583    426       C  
ATOM    549  O   TYR A 519      -8.267   9.021 -19.179  1.00 37.24           O  
ANISOU  549  O   TYR A 519     4072   4460   5617   -259    610    419       O  
ATOM    550  CB  TYR A 519      -9.026   5.875 -19.526  1.00 43.27           C  
ANISOU  550  CB  TYR A 519     4987   5251   6204   -254    667    372       C  
ATOM    551  CG  TYR A 519     -10.325   6.608 -19.271  1.00 41.48           C  
ANISOU  551  CG  TYR A 519     4713   4963   6086   -291    727    370       C  
ATOM    552  CD1 TYR A 519     -10.891   7.418 -20.247  1.00 34.61           C  
ANISOU  552  CD1 TYR A 519     3714   4117   5317   -317    707    420       C  
ATOM    553  CD2 TYR A 519     -10.992   6.477 -18.060  1.00 50.51           C  
ANISOU  553  CD2 TYR A 519     5941   6022   7228   -302    801    314       C  
ATOM    554  CE1 TYR A 519     -12.080   8.085 -20.021  1.00 45.28           C  
ANISOU  554  CE1 TYR A 519     5018   5411   6776   -346    754    410       C  
ATOM    555  CE2 TYR A 519     -12.182   7.139 -17.825  1.00 56.63           C  
ANISOU  555  CE2 TYR A 519     6666   6744   8108   -337    857    300       C  
ATOM    556  CZ  TYR A 519     -12.722   7.941 -18.808  1.00 57.41           C  
ANISOU  556  CZ  TYR A 519     6631   6867   8314   -356    830    346       C  
ATOM    557  OH  TYR A 519     -13.906   8.600 -18.574  1.00 60.01           O  
ANISOU  557  OH  TYR A 519     6907   7140   8754   -387    879    325       O  
ATOM    558  N   SER A 520      -7.406   8.145 -21.062  1.00 56.94           N  
ANISOU  558  N   SER A 520     6501   7098   8037   -255    527    477       N  
ATOM    559  CA  SER A 520      -7.408   9.407 -21.779  1.00 53.82           C  
ANISOU  559  CA  SER A 520     5990   6724   7734   -280    491    535       C  
ATOM    560  C   SER A 520      -8.347   9.384 -22.969  1.00 52.99           C  
ANISOU  560  C   SER A 520     5799   6650   7683   -315    487    586       C  
ATOM    561  O   SER A 520      -8.518   8.359 -23.622  1.00 44.37           O  
ANISOU  561  O   SER A 520     4715   5605   6536   -316    488    589       O  
ATOM    562  CB  SER A 520      -5.998   9.754 -22.245  1.00 59.23           C  
ANISOU  562  CB  SER A 520     6645   7481   8381   -268    422    555       C  
ATOM    563  OG  SER A 520      -5.246  10.303 -21.183  1.00 64.29           O  
ANISOU  563  OG  SER A 520     7331   8081   9015   -242    419    518       O  
ATOM    564  N   THR A 521      -8.952  10.532 -23.244  1.00 72.79           N  
ANISOU  564  N   THR A 521     8226   9130  10302   -341    480    624       N  
ATOM    565  CA  THR A 521      -9.800  10.696 -24.412  1.00 76.31           C  
ANISOU  565  CA  THR A 521     8582   9602  10809   -372    462    678       C  
ATOM    566  C   THR A 521      -9.145  11.695 -25.353  1.00 81.92           C  
ANISOU  566  C   THR A 521     9207  10364  11554   -392    391    748       C  
ATOM    567  O   THR A 521      -9.364  11.665 -26.561  1.00 89.12           O  
ANISOU  567  O   THR A 521    10054  11332  12474   -417    355    802       O  
ATOM    568  CB  THR A 521     -11.198  11.194 -24.026  1.00 72.80           C  
ANISOU  568  CB  THR A 521     8111   9075  10475   -389    508    663       C  
ATOM    569  OG1 THR A 521     -12.123  10.100 -24.060  1.00 68.41           O  
ANISOU  569  OG1 THR A 521     7587   8512   9895   -393    559    630       O  
ATOM    570  CG2 THR A 521     -11.664  12.267 -24.991  1.00 72.05           C  
ANISOU  570  CG2 THR A 521     7905   8985  10485   -416    457    730       C  
ATOM    571  N   ALA A 522      -8.338  12.583 -24.784  1.00 67.22           N  
ANISOU  571  N   ALA A 522     7349   8482   9709   -384    371    746       N  
ATOM    572  CA  ALA A 522      -7.611  13.571 -25.564  1.00 59.61           C  
ANISOU  572  CA  ALA A 522     6314   7563   8773   -408    307    808       C  
ATOM    573  C   ALA A 522      -6.194  13.671 -25.027  1.00 64.45           C  
ANISOU  573  C   ALA A 522     6965   8202   9319   -386    289    780       C  
ATOM    574  O   ALA A 522      -5.989  13.606 -23.820  1.00 65.36           O  
ANISOU  574  O   ALA A 522     7148   8264   9422   -355    322    721       O  
ATOM    575  CB  ALA A 522      -8.297  14.909 -25.475  1.00 43.28           C  
ANISOU  575  CB  ALA A 522     4186   5425   6835   -428    296    841       C  
ATOM    576  N   PRO A 523      -5.204  13.831 -25.917  1.00 76.95           N  
ANISOU  576  N   PRO A 523     8508   9870  10861   -404    237    818       N  
ATOM    577  CA  PRO A 523      -5.321  13.918 -27.377  1.00 83.87           C  
ANISOU  577  CA  PRO A 523     9311  10818  11739   -447    195    889       C  
ATOM    578  C   PRO A 523      -5.997  12.702 -28.001  1.00 92.50           C  
ANISOU  578  C   PRO A 523    10412  11950  12785   -447    212    886       C  
ATOM    579  O   PRO A 523      -7.031  12.852 -28.644  1.00102.22           O  
ANISOU  579  O   PRO A 523    11598  13168  14074   -470    209    928       O  
ATOM    580  CB  PRO A 523      -3.862  14.001 -27.845  1.00 49.22           C  
ANISOU  580  CB  PRO A 523     4906   6515   7279   -458    153    894       C  
ATOM    581  CG  PRO A 523      -3.040  13.641 -26.671  1.00 43.87           C  
ANISOU  581  CG  PRO A 523     4302   5818   6550   -411    172    816       C  
ATOM    582  CD  PRO A 523      -3.817  14.021 -25.473  1.00 42.32           C  
ANISOU  582  CD  PRO A 523     4147   5513   6421   -386    215    786       C  
ATOM    583  N   GLN A 524      -5.422  11.519 -27.824  1.00 64.98           N  
ANISOU  583  N   GLN A 524     6983   8510   9198   -418    225    835       N  
ATOM    584  CA  GLN A 524      -6.025  10.305 -28.361  1.00 60.54           C  
ANISOU  584  CA  GLN A 524     6432   7982   8587   -416    243    826       C  
ATOM    585  C   GLN A 524      -6.420   9.357 -27.241  1.00 60.76           C  
ANISOU  585  C   GLN A 524     6555   7950   8582   -375    299    754       C  
ATOM    586  O   GLN A 524      -6.079   9.580 -26.083  1.00 64.25           O  
ANISOU  586  O   GLN A 524     7056   8334   9022   -347    320    710       O  
ATOM    587  CB  GLN A 524      -5.055   9.607 -29.307  1.00 64.67           C  
ANISOU  587  CB  GLN A 524     6936   8619   9016   -424    205    830       C  
ATOM    588  CG  GLN A 524      -3.629   9.645 -28.819  1.00 64.61           C  
ANISOU  588  CG  GLN A 524     6959   8642   8948   -401    184    787       C  
ATOM    589  CD  GLN A 524      -2.712   8.796 -29.660  1.00 69.12           C  
ANISOU  589  CD  GLN A 524     7514   9323   9425   -405    152    770       C  
ATOM    590  OE1 GLN A 524      -3.151   7.850 -30.314  1.00 65.04           O  
ANISOU  590  OE1 GLN A 524     6992   8848   8870   -408    157    771       O  
ATOM    591  NE2 GLN A 524      -1.426   9.125 -29.648  1.00 75.35           N  
ANISOU  591  NE2 GLN A 524     8292  10161  10178   -404    119    749       N  
ATOM    592  N   LEU A 525      -7.139   8.296 -27.592  1.00 60.62           N  
ANISOU  592  N   LEU A 525     6553   7947   8535   -373    325    742       N  
ATOM    593  CA  LEU A 525      -7.558   7.310 -26.605  1.00 47.60           C  
ANISOU  593  CA  LEU A 525     4999   6240   6845   -342    380    677       C  
ATOM    594  C   LEU A 525      -6.350   6.586 -26.025  1.00 37.87           C  
ANISOU  594  C   LEU A 525     3846   5031   5511   -303    366    624       C  
ATOM    595  O   LEU A 525      -5.459   6.159 -26.759  1.00 33.21           O  
ANISOU  595  O   LEU A 525     3233   4527   4858   -300    322    627       O  
ATOM    596  CB  LEU A 525      -8.528   6.301 -27.221  1.00 42.71           C  
ANISOU  596  CB  LEU A 525     4375   5638   6214   -353    407    677       C  
ATOM    597  CG  LEU A 525      -9.853   6.850 -27.744  1.00 42.28           C  
ANISOU  597  CG  LEU A 525     4250   5555   6261   -386    423    716       C  
ATOM    598  CD1 LEU A 525     -10.821   5.710 -28.005  1.00 32.84           C  
ANISOU  598  CD1 LEU A 525     3073   4359   5047   -388    464    693       C  
ATOM    599  CD2 LEU A 525     -10.443   7.830 -26.749  1.00 51.88           C  
ANISOU  599  CD2 LEU A 525     5474   6672   7568   -387    456    702       C  
ATOM    600  N   ALA A 526      -6.320   6.448 -24.705  1.00 37.01           N  
ANISOU  600  N   ALA A 526     3829   4845   5386   -273    401    570       N  
ATOM    601  CA  ALA A 526      -5.210   5.771 -24.050  1.00 36.68           C  
ANISOU  601  CA  ALA A 526     3873   4814   5251   -230    382    515       C  
ATOM    602  C   ALA A 526      -5.620   5.156 -22.721  1.00 43.61           C  
ANISOU  602  C   ALA A 526     4872   5601   6096   -205    434    457       C  
ATOM    603  O   ALA A 526      -6.535   5.636 -22.052  1.00 35.94           O  
ANISOU  603  O   ALA A 526     3917   4553   5186   -221    487    454       O  
ATOM    604  CB  ALA A 526      -4.037   6.723 -23.858  1.00 24.96           C  
ANISOU  604  CB  ALA A 526     2360   3350   3773   -220    336    516       C  
ATOM    605  N   ILE A 527      -4.932   4.081 -22.356  1.00 49.96           N  
ANISOU  605  N   ILE A 527     5764   6415   6802   -167    418    409       N  
ATOM    606  CA  ILE A 527      -5.101   3.453 -21.058  1.00 38.77           C  
ANISOU  606  CA  ILE A 527     4482   4915   5335   -141    457    353       C  
ATOM    607  C   ILE A 527      -3.866   3.743 -20.215  1.00 39.85           C  
ANISOU  607  C   ILE A 527     4674   5038   5427    -99    415    314       C  
ATOM    608  O   ILE A 527      -2.745   3.450 -20.629  1.00 37.11           O  
ANISOU  608  O   ILE A 527     4314   4757   5030    -71    352    300       O  
ATOM    609  CB  ILE A 527      -5.281   1.930 -21.190  1.00 44.66           C  
ANISOU  609  CB  ILE A 527     5303   5667   5998   -127    464    325       C  
ATOM    610  CG1 ILE A 527      -6.530   1.609 -22.012  1.00 48.67           C  
ANISOU  610  CG1 ILE A 527     5755   6187   6550   -168    507    358       C  
ATOM    611  CG2 ILE A 527      -5.363   1.279 -19.819  1.00 44.80           C  
ANISOU  611  CG2 ILE A 527     5474   5595   5953   -103    498    270       C  
ATOM    612  CD1 ILE A 527      -7.807   2.168 -21.421  1.00 56.79           C  
ANISOU  612  CD1 ILE A 527     6787   7135   7654   -203    583    362       C  
ATOM    613  N   VAL A 528      -4.074   4.330 -19.041  1.00 44.22           N  
ANISOU  613  N   VAL A 528     5285   5510   6004    -95    450    292       N  
ATOM    614  CA  VAL A 528      -2.974   4.652 -18.139  1.00 41.34           C  
ANISOU  614  CA  VAL A 528     4979   5126   5602    -54    413    251       C  
ATOM    615  C   VAL A 528      -2.897   3.642 -16.998  1.00 44.19           C  
ANISOU  615  C   VAL A 528     5499   5420   5871    -21    428    193       C  
ATOM    616  O   VAL A 528      -3.896   3.370 -16.333  1.00 44.29           O  
ANISOU  616  O   VAL A 528     5583   5361   5885    -42    495    183       O  
ATOM    617  CB  VAL A 528      -3.123   6.066 -17.555  1.00 29.26           C  
ANISOU  617  CB  VAL A 528     3408   3553   4157    -70    434    263       C  
ATOM    618  CG1 VAL A 528      -1.915   6.418 -16.703  1.00 26.53           C  
ANISOU  618  CG1 VAL A 528     3112   3194   3774    -26    391    219       C  
ATOM    619  CG2 VAL A 528      -3.298   7.077 -18.670  1.00 34.33           C  
ANISOU  619  CG2 VAL A 528     3902   4249   4892   -108    419    325       C  
ATOM    620  N   THR A 529      -1.712   3.082 -16.779  1.00 35.18           N  
ANISOU  620  N   THR A 529     4416   4302   4651     30    363    152       N  
ATOM    621  CA  THR A 529      -1.504   2.127 -15.698  1.00 34.91           C  
ANISOU  621  CA  THR A 529     4541   4201   4522     68    361     98       C  
ATOM    622  C   THR A 529      -0.229   2.452 -14.937  1.00 35.06           C  
ANISOU  622  C   THR A 529     4605   4212   4502    121    299     52       C  
ATOM    623  O   THR A 529       0.398   3.483 -15.171  1.00 34.43           O  
ANISOU  623  O   THR A 529     4434   4173   4477    123    270     61       O  
ATOM    624  CB  THR A 529      -1.401   0.682 -16.224  1.00 31.83           C  
ANISOU  624  CB  THR A 529     4200   3839   4054     87    333     84       C  
ATOM    625  OG1 THR A 529      -0.142   0.500 -16.884  1.00 35.96           O  
ANISOU  625  OG1 THR A 529     4671   4443   4549    127    246     64       O  
ATOM    626  CG2 THR A 529      -2.532   0.380 -17.191  1.00 31.03           C  
ANISOU  626  CG2 THR A 529     4030   3765   3995     37    383    129       C  
ATOM    627  N   GLN A 530       0.150   1.564 -14.027  1.00 38.07           N  
ANISOU  627  N   GLN A 530     5134   4540   4791    162    276      1       N  
ATOM    628  CA  GLN A 530       1.396   1.713 -13.292  1.00 34.77           C  
ANISOU  628  CA  GLN A 530     4771   4112   4328    221    207    -51       C  
ATOM    629  C   GLN A 530       2.570   1.392 -14.205  1.00 32.47           C  
ANISOU  629  C   GLN A 530     4407   3913   4017    260    119    -72       C  
ATOM    630  O   GLN A 530       2.397   0.790 -15.265  1.00 40.47           O  
ANISOU  630  O   GLN A 530     5361   4986   5029    246    111    -51       O  
ATOM    631  CB  GLN A 530       1.419   0.773 -12.090  1.00 36.31           C  
ANISOU  631  CB  GLN A 530     5154   4218   4423    254    201    -98       C  
ATOM    632  CG  GLN A 530       1.367  -0.697 -12.469  1.00 41.92           C  
ANISOU  632  CG  GLN A 530     5937   4932   5058    272    174   -110       C  
ATOM    633  CD  GLN A 530       1.586  -1.618 -11.286  1.00 40.98           C  
ANISOU  633  CD  GLN A 530     6013   4725   4834    310    149   -157       C  
ATOM    634  OE1 GLN A 530       0.711  -2.405 -10.929  1.00 45.52           O  
ANISOU  634  OE1 GLN A 530     6694   5238   5364    283    200   -149       O  
ATOM    635  NE2 GLN A 530       2.757  -1.522 -10.670  1.00 44.60           N  
ANISOU  635  NE2 GLN A 530     6521   5174   5250    373     69   -208       N  
ATOM    636  N   TRP A 531       3.767   1.791 -13.790  1.00 33.91           N  
ANISOU  636  N   TRP A 531     4591   4108   4185    308     53   -119       N  
ATOM    637  CA  TRP A 531       4.976   1.447 -14.526  1.00 20.67           C  
ANISOU  637  CA  TRP A 531     2854   2516   2485    348    -33   -157       C  
ATOM    638  C   TRP A 531       5.691   0.266 -13.876  1.00 35.11           C  
ANISOU  638  C   TRP A 531     4818   4307   4214    418   -104   -227       C  
ATOM    639  O   TRP A 531       6.065   0.323 -12.705  1.00 39.27           O  
ANISOU  639  O   TRP A 531     5454   4764   4701    457   -126   -269       O  
ATOM    640  CB  TRP A 531       5.917   2.646 -14.618  1.00 31.26           C  
ANISOU  640  CB  TRP A 531     4091   3905   3880    355    -65   -172       C  
ATOM    641  CG  TRP A 531       7.171   2.327 -15.357  1.00 45.66           C  
ANISOU  641  CG  TRP A 531     5848   5819   5682    391   -148   -221       C  
ATOM    642  CD1 TRP A 531       8.436   2.273 -14.847  1.00 55.21           C  
ANISOU  642  CD1 TRP A 531     7086   7034   6856    454   -226   -300       C  
ATOM    643  CD2 TRP A 531       7.281   1.988 -16.742  1.00 47.52           C  
ANISOU  643  CD2 TRP A 531     5973   6153   5930    365   -162   -203       C  
ATOM    644  NE1 TRP A 531       9.328   1.933 -15.834  1.00 58.12           N  
ANISOU  644  NE1 TRP A 531     7365   7501   7218    467   -285   -336       N  
ATOM    645  CE2 TRP A 531       8.643   1.752 -17.007  1.00 55.62           C  
ANISOU  645  CE2 TRP A 531     6963   7244   6928    411   -246   -276       C  
ATOM    646  CE3 TRP A 531       6.359   1.867 -17.786  1.00 50.77           C  
ANISOU  646  CE3 TRP A 531     6311   6606   6373    306   -113   -135       C  
ATOM    647  CZ2 TRP A 531       9.107   1.402 -18.274  1.00 66.32           C  
ANISOU  647  CZ2 TRP A 531     8210   8705   8283    396   -276   -286       C  
ATOM    648  CZ3 TRP A 531       6.820   1.520 -19.040  1.00 62.50           C  
ANISOU  648  CZ3 TRP A 531     7695   8196   7856    293   -146   -139       C  
ATOM    649  CH2 TRP A 531       8.181   1.291 -19.275  1.00 68.08           C  
ANISOU  649  CH2 TRP A 531     8368   8968   8533    336   -225   -214       C  
ATOM    650  N   CYS A 532       5.878  -0.804 -14.644  1.00 58.01           N  
ANISOU  650  N   CYS A 532     7712   7253   7075    433   -143   -242       N  
ATOM    651  CA  CYS A 532       6.542  -2.005 -14.145  1.00 53.71           C  
ANISOU  651  CA  CYS A 532     7293   6673   6440    501   -220   -309       C  
ATOM    652  C   CYS A 532       8.019  -2.029 -14.517  1.00 55.19           C  
ANISOU  652  C   CYS A 532     7416   6934   6620    558   -320   -381       C  
ATOM    653  O   CYS A 532       8.371  -2.128 -15.693  1.00 66.28           O  
ANISOU  653  O   CYS A 532     8697   8437   8050    545   -341   -383       O  
ATOM    654  CB  CYS A 532       5.862  -3.263 -14.687  1.00 44.95           C  
ANISOU  654  CB  CYS A 532     6227   5561   5291    489   -207   -293       C  
ATOM    655  SG  CYS A 532       4.158  -3.491 -14.142  1.00 51.16           S  
ANISOU  655  SG  CYS A 532     7114   6253   6073    427    -93   -228       S  
ATOM    656  N   GLU A 533       8.877  -1.942 -13.506  1.00 40.92           N  
ANISOU  656  N   GLU A 533     5693   5080   4776    619   -382   -444       N  
ATOM    657  CA  GLU A 533      10.317  -2.025 -13.710  1.00 49.52           C  
ANISOU  657  CA  GLU A 533     6733   6228   5856    681   -483   -528       C  
ATOM    658  C   GLU A 533      10.698  -3.463 -14.042  1.00 60.99           C  
ANISOU  658  C   GLU A 533     8241   7689   7244    730   -558   -580       C  
ATOM    659  O   GLU A 533       9.938  -4.392 -13.768  1.00 60.94           O  
ANISOU  659  O   GLU A 533     8351   7616   7188    728   -539   -557       O  
ATOM    660  CB  GLU A 533      11.058  -1.558 -12.458  1.00 70.56           C  
ANISOU  660  CB  GLU A 533     9482   8830   8499    736   -530   -584       C  
ATOM    661  CG  GLU A 533      10.437  -0.334 -11.801  1.00 91.12           C  
ANISOU  661  CG  GLU A 533    12082  11390  11150    691   -449   -531       C  
ATOM    662  CD  GLU A 533      11.325   0.892 -11.876  1.00111.58           C  
ANISOU  662  CD  GLU A 533    14555  14036  13804    695   -468   -559       C  
ATOM    663  OE1 GLU A 533      10.852   1.940 -12.364  1.00117.27           O  
ANISOU  663  OE1 GLU A 533    15163  14794  14601    631   -399   -499       O  
ATOM    664  OE2 GLU A 533      12.495   0.810 -11.443  1.00122.10           O  
ANISOU  664  OE2 GLU A 533    15909  15373  15110    763   -555   -644       O  
ATOM    665  N   GLY A 534      11.873  -3.647 -14.634  1.00 74.02           N  
ANISOU  665  N   GLY A 534     9807   9419   8898    772   -641   -655       N  
ATOM    666  CA  GLY A 534      12.311  -4.968 -15.040  1.00 75.72           C  
ANISOU  666  CA  GLY A 534    10055   9651   9064    820   -719   -714       C  
ATOM    667  C   GLY A 534      11.809  -5.325 -16.425  1.00 73.73           C  
ANISOU  667  C   GLY A 534     9686   9488   8839    765   -679   -673       C  
ATOM    668  O   GLY A 534      11.926  -4.532 -17.359  1.00 64.82           O  
ANISOU  668  O   GLY A 534     8401   8458   7771    715   -644   -649       O  
ATOM    669  N   SER A 535      11.240  -6.517 -16.560  1.00 84.78           N  
ANISOU  669  N   SER A 535    11167  10852  10193    772   -683   -664       N  
ATOM    670  CA  SER A 535      10.781  -6.991 -17.859  1.00 86.17           C  
ANISOU  670  CA  SER A 535    11241  11111  10389    727   -653   -633       C  
ATOM    671  C   SER A 535       9.642  -7.996 -17.727  1.00 96.50           C  
ANISOU  671  C   SER A 535    12662  12347  11657    710   -611   -586       C  
ATOM    672  O   SER A 535       9.206  -8.313 -16.622  1.00106.63           O  
ANISOU  672  O   SER A 535    14105  13514  12894    729   -603   -575       O  
ATOM    673  CB  SER A 535      11.945  -7.617 -18.627  1.00 67.85           C  
ANISOU  673  CB  SER A 535     8839   8880   8061    773   -748   -728       C  
ATOM    674  OG  SER A 535      12.648  -8.533 -17.807  1.00 68.92           O  
ANISOU  674  OG  SER A 535     9105   8945   8138    862   -850   -813       O  
ATOM    675  N   SER A 536       9.164  -8.490 -18.865  1.00 87.00           N  
ANISOU  675  N   SER A 536    11374  11212  10469    671   -583   -559       N  
ATOM    676  CA  SER A 536       8.092  -9.480 -18.884  1.00 71.99           C  
ANISOU  676  CA  SER A 536     9563   9254   8535    651   -542   -518       C  
ATOM    677  C   SER A 536       8.611 -10.846 -18.454  1.00 64.70           C  
ANISOU  677  C   SER A 536     8767   8273   7542    726   -636   -592       C  
ATOM    678  O   SER A 536       9.819 -11.080 -18.432  1.00 68.05           O  
ANISOU  678  O   SER A 536     9176   8727   7953    791   -737   -679       O  
ATOM    679  CB  SER A 536       7.475  -9.572 -20.282  1.00 60.08           C  
ANISOU  679  CB  SER A 536     7917   7844   7068    589   -489   -472       C  
ATOM    680  OG  SER A 536       8.456  -9.875 -21.258  1.00 54.57           O  
ANISOU  680  OG  SER A 536     7102   7256   6377    612   -559   -536       O  
ATOM    681  N   LEU A 537       7.694 -11.744 -18.107  1.00 55.21           N  
ANISOU  681  N   LEU A 537     7691   6987   6298    715   -604   -560       N  
ATOM    682  CA  LEU A 537       8.063 -13.110 -17.752  1.00 58.30           C  
ANISOU  682  CA  LEU A 537     8212   7315   6623    779   -692   -621       C  
ATOM    683  C   LEU A 537       8.652 -13.822 -18.964  1.00 53.70           C  
ANISOU  683  C   LEU A 537     7512   6836   6055    801   -754   -676       C  
ATOM    684  O   LEU A 537       9.430 -14.767 -18.828  1.00 51.79           O  
ANISOU  684  O   LEU A 537     7330   6574   5776    872   -859   -756       O  
ATOM    685  CB  LEU A 537       6.851 -13.881 -17.226  1.00 59.30           C  
ANISOU  685  CB  LEU A 537     8491   7336   6706    748   -630   -567       C  
ATOM    686  CG  LEU A 537       7.109 -15.340 -16.841  1.00 48.23           C  
ANISOU  686  CG  LEU A 537     7239   5854   5232    807   -716   -619       C  
ATOM    687  CD1 LEU A 537       8.236 -15.421 -15.829  1.00 55.84           C  
ANISOU  687  CD1 LEU A 537     8313   6754   6149    892   -830   -692       C  
ATOM    688  CD2 LEU A 537       5.851 -15.993 -16.294  1.00 46.65           C  
ANISOU  688  CD2 LEU A 537     7191   5547   4988    762   -640   -561       C  
ATOM    689  N   TYR A 538       8.270 -13.357 -20.149  1.00 66.70           N  
ANISOU  689  N   TYR A 538     8992   8593   7759    739   -690   -635       N  
ATOM    690  CA  TYR A 538       8.774 -13.909 -21.400  1.00 73.20           C  
ANISOU  690  CA  TYR A 538     9685   9530   8599    745   -735   -684       C  
ATOM    691  C   TYR A 538      10.259 -13.604 -21.558  1.00 69.74           C  
ANISOU  691  C   TYR A 538     9163   9164   8173    800   -831   -780       C  
ATOM    692  O   TYR A 538      11.047 -14.481 -21.912  1.00 68.91           O  
ANISOU  692  O   TYR A 538     9042   9090   8050    854   -922   -868       O  
ATOM    693  CB  TYR A 538       7.991 -13.331 -22.581  1.00 79.53           C  
ANISOU  693  CB  TYR A 538    10332  10431   9455    659   -640   -610       C  
ATOM    694  CG  TYR A 538       8.294 -13.978 -23.916  1.00 76.47           C  
ANISOU  694  CG  TYR A 538     9816  10159   9079    653   -670   -650       C  
ATOM    695  CD1 TYR A 538       7.510 -15.016 -24.399  1.00 68.17           C  
ANISOU  695  CD1 TYR A 538     8790   9098   8013    637   -648   -632       C  
ATOM    696  CD2 TYR A 538       9.356 -13.543 -24.697  1.00 79.68           C  
ANISOU  696  CD2 TYR A 538    10075  10687   9512    658   -717   -709       C  
ATOM    697  CE1 TYR A 538       7.776 -15.607 -25.618  1.00 74.19           C  
ANISOU  697  CE1 TYR A 538     9435   9969   8787    631   -675   -671       C  
ATOM    698  CE2 TYR A 538       9.632 -14.128 -25.918  1.00 82.86           C  
ANISOU  698  CE2 TYR A 538    10359  11200   9924    647   -741   -750       C  
ATOM    699  CZ  TYR A 538       8.840 -15.159 -26.374  1.00 83.21           C  
ANISOU  699  CZ  TYR A 538    10431  11233   9953    635   -721   -730       C  
ATOM    700  OH  TYR A 538       9.112 -15.742 -27.589  1.00 90.64           O  
ANISOU  700  OH  TYR A 538    11252  12286  10902    624   -745   -774       O  
ATOM    701  N   HIS A 539      10.636 -12.357 -21.291  1.00 63.99           N  
ANISOU  701  N   HIS A 539     8377   8459   7476    784   -810   -767       N  
ATOM    702  CA  HIS A 539      12.022 -11.929 -21.435  1.00 57.31           C  
ANISOU  702  CA  HIS A 539     7442   7685   6647    827   -889   -858       C  
ATOM    703  C   HIS A 539      12.949 -12.667 -20.476  1.00 61.63           C  
ANISOU  703  C   HIS A 539     8117   8154   7148    928  -1009   -957       C  
ATOM    704  O   HIS A 539      14.108 -12.921 -20.795  1.00 76.15           O  
ANISOU  704  O   HIS A 539     9888  10053   8992    979  -1101  -1062       O  
ATOM    705  CB  HIS A 539      12.150 -10.419 -21.226  1.00 60.05           C  
ANISOU  705  CB  HIS A 539     7719   8059   7038    788   -837   -818       C  
ATOM    706  CG  HIS A 539      13.559  -9.919 -21.297  1.00 79.54           C  
ANISOU  706  CG  HIS A 539    10099  10597   9525    827   -912   -913       C  
ATOM    707  ND1 HIS A 539      14.426  -9.975 -20.225  1.00 86.89           N  
ANISOU  707  ND1 HIS A 539    11126  11459  10431    907   -996   -990       N  
ATOM    708  CD2 HIS A 539      14.255  -9.350 -22.310  1.00 88.86           C  
ANISOU  708  CD2 HIS A 539    11106  11909  10747    794   -914   -948       C  
ATOM    709  CE1 HIS A 539      15.591  -9.465 -20.575  1.00 90.64           C  
ANISOU  709  CE1 HIS A 539    11483  12021  10935    924  -1047  -1072       C  
ATOM    710  NE2 HIS A 539      15.515  -9.078 -21.838  1.00 91.45           N  
ANISOU  710  NE2 HIS A 539    11422  12247  11077    854   -995  -1048       N  
ATOM    711  N   HIS A 540      12.439 -13.004 -19.297  1.00 58.03           N  
ANISOU  711  N   HIS A 540     7845   7560   6645    954  -1009   -927       N  
ATOM    712  CA  HIS A 540      13.230 -13.738 -18.317  1.00 61.33           C  
ANISOU  712  CA  HIS A 540     8406   7886   7010   1049  -1126  -1012       C  
ATOM    713  C   HIS A 540      13.376 -15.204 -18.711  1.00 60.37           C  
ANISOU  713  C   HIS A 540     8327   7753   6856   1095  -1204  -1070       C  
ATOM    714  O   HIS A 540      14.477 -15.754 -18.700  1.00 63.50           O  
ANISOU  714  O   HIS A 540     8719   8162   7245   1173  -1324  -1180       O  
ATOM    715  CB  HIS A 540      12.605 -13.631 -16.923  1.00 71.26           C  
ANISOU  715  CB  HIS A 540     9857   8999   8219   1055  -1098   -958       C  
ATOM    716  CG  HIS A 540      12.872 -12.327 -16.238  1.00 74.21           C  
ANISOU  716  CG  HIS A 540    10216   9364   8615   1046  -1070   -942       C  
ATOM    717  ND1 HIS A 540      14.141 -11.913 -15.897  1.00 85.37           N  
ANISOU  717  ND1 HIS A 540    11598  10800  10038   1110  -1160  -1032       N  
ATOM    718  CD2 HIS A 540      12.031 -11.354 -15.812  1.00 77.78           C  
ANISOU  718  CD2 HIS A 540    10681   9786   9086    983   -963   -853       C  
ATOM    719  CE1 HIS A 540      14.072 -10.735 -15.301  1.00 91.63           C  
ANISOU  719  CE1 HIS A 540    12385  11578  10853   1085  -1108   -995       C  
ATOM    720  NE2 HIS A 540      12.804 -10.375 -15.236  1.00 89.07           N  
ANISOU  720  NE2 HIS A 540    12087  11221  10534   1009   -989   -887       N  
ATOM    721  N   LEU A 541      12.258 -15.827 -19.065  1.00 61.49           N  
ANISOU  721  N   LEU A 541     8507   7872   6986   1047  -1136   -999       N  
ATOM    722  CA  LEU A 541      12.241 -17.247 -19.405  1.00 63.14           C  
ANISOU  722  CA  LEU A 541     8768   8058   7164   1083  -1200  -1043       C  
ATOM    723  C   LEU A 541      12.943 -17.586 -20.724  1.00 66.98           C  
ANISOU  723  C   LEU A 541     9076   8683   7691   1092  -1246  -1120       C  
ATOM    724  O   LEU A 541      13.490 -18.681 -20.871  1.00 74.60           O  
ANISOU  724  O   LEU A 541    10070   9636   8637   1155  -1347  -1204       O  
ATOM    725  CB  LEU A 541      10.801 -17.782 -19.412  1.00 64.49           C  
ANISOU  725  CB  LEU A 541     9026   8166   7313   1023  -1105   -946       C  
ATOM    726  CG  LEU A 541      10.250 -18.388 -18.116  1.00 67.39           C  
ANISOU  726  CG  LEU A 541     9629   8367   7609   1043  -1112   -916       C  
ATOM    727  CD1 LEU A 541      10.661 -17.563 -16.914  1.00 69.59           C  
ANISOU  727  CD1 LEU A 541     9998   8576   7867   1070  -1129   -917       C  
ATOM    728  CD2 LEU A 541       8.734 -18.537 -18.169  1.00 62.24           C  
ANISOU  728  CD2 LEU A 541     9028   7671   6949    960   -985   -812       C  
ATOM    729  N   HIS A 542      12.942 -16.650 -21.671  1.00 68.55           N  
ANISOU  729  N   HIS A 542     9091   9010   7944   1028  -1177  -1093       N  
ATOM    730  CA  HIS A 542      13.378 -16.950 -23.038  1.00 62.98           C  
ANISOU  730  CA  HIS A 542     8212   8444   7273   1013  -1195  -1148       C  
ATOM    731  C   HIS A 542      14.392 -15.953 -23.624  1.00 73.47           C  
ANISOU  731  C   HIS A 542     9367   9901   8647   1000  -1207  -1204       C  
ATOM    732  O   HIS A 542      15.198 -16.313 -24.477  1.00 91.57           O  
ANISOU  732  O   HIS A 542    11539  12296  10958   1016  -1264  -1296       O  
ATOM    733  CB  HIS A 542      12.155 -17.067 -23.960  1.00 56.75           C  
ANISOU  733  CB  HIS A 542     7362   7702   6499    927  -1086  -1054       C  
ATOM    734  CG  HIS A 542      11.031 -17.869 -23.377  1.00 58.68           C  
ANISOU  734  CG  HIS A 542     7770   7823   6704    922  -1050   -988       C  
ATOM    735  ND1 HIS A 542      11.175 -19.186 -22.994  1.00 69.49           N  
ANISOU  735  ND1 HIS A 542     9264   9109   8030    986  -1134  -1044       N  
ATOM    736  CD2 HIS A 542       9.741 -17.544 -23.120  1.00 55.58           C  
ANISOU  736  CD2 HIS A 542     7435   7374   6309    857   -939   -876       C  
ATOM    737  CE1 HIS A 542      10.026 -19.635 -22.521  1.00 69.23           C  
ANISOU  737  CE1 HIS A 542     9362   8975   7966    957  -1072   -965       C  
ATOM    738  NE2 HIS A 542       9.139 -18.658 -22.586  1.00 57.62           N  
ANISOU  738  NE2 HIS A 542     7850   7520   6521    878   -952   -866       N  
ATOM    739  N   ALA A 543      14.350 -14.706 -23.163  1.00 62.13           N  
ANISOU  739  N   ALA A 543     7919   8459   7230    968  -1152  -1152       N  
ATOM    740  CA  ALA A 543      15.216 -13.659 -23.707  1.00 76.72           C  
ANISOU  740  CA  ALA A 543     9605  10423   9121    943  -1150  -1191       C  
ATOM    741  C   ALA A 543      16.570 -13.575 -23.001  1.00 69.22           C  
ANISOU  741  C   ALA A 543     8676   9456   8168   1028  -1260  -1312       C  
ATOM    742  O   ALA A 543      17.613 -13.555 -23.650  1.00 74.39           O  
ANISOU  742  O   ALA A 543     9204  10215   8847   1043  -1315  -1415       O  
ATOM    743  CB  ALA A 543      14.515 -12.319 -23.697  1.00131.35           C  
ANISOU  743  CB  ALA A 543    16482  17354  16071    862  -1037  -1078       C  
ATOM    744  N   SER A 544      16.554 -13.503 -21.675  1.00 83.33           N  
ANISOU  744  N   SER A 544    10622  11114   9925   1080  -1291  -1303       N  
ATOM    745  CA  SER A 544      17.797 -13.398 -20.912  1.00 88.90           C  
ANISOU  745  CA  SER A 544    11358  11792  10626   1165  -1399  -1416       C  
ATOM    746  C   SER A 544      18.141 -14.693 -20.184  1.00 84.72           C  
ANISOU  746  C   SER A 544    10984  11157  10048   1265  -1520  -1493       C  
ATOM    747  O   SER A 544      19.312 -15.010 -19.985  1.00 79.88           O  
ANISOU  747  O   SER A 544    10359  10553   9438   1345  -1638  -1621       O  
ATOM    748  CB  SER A 544      17.741 -12.229 -19.920  1.00104.37           C  
ANISOU  748  CB  SER A 544    13372  13692  12590   1156  -1359  -1366       C  
ATOM    749  OG  SER A 544      16.781 -12.459 -18.903  1.00107.21           O  
ANISOU  749  OG  SER A 544    13916  13914  12906   1160  -1326  -1281       O  
ATOM    750  N   PHE A 548      15.921 -18.528 -12.677  1.00 64.72           N  
ANISOU  750  N   PHE A 548     9861   7647   7081   1532  -1778  -1341       N  
ATOM    751  CA  PHE A 548      15.268 -18.477 -11.374  1.00 81.02           C  
ANISOU  751  CA  PHE A 548    12141   9571   9072   1519  -1747  -1271       C  
ATOM    752  C   PHE A 548      15.419 -19.798 -10.633  1.00 84.30           C  
ANISOU  752  C   PHE A 548    12777   9849   9406   1589  -1868  -1306       C  
ATOM    753  O   PHE A 548      15.573 -20.852 -11.248  1.00 86.69           O  
ANISOU  753  O   PHE A 548    13071  10158   9711   1620  -1935  -1349       O  
ATOM    754  CB  PHE A 548      13.777 -18.162 -11.521  1.00123.18           C  
ANISOU  754  CB  PHE A 548    17490  14904  14409   1404  -1574  -1140       C  
ATOM    755  CG  PHE A 548      13.492 -16.834 -12.159  1.00138.10           C  
ANISOU  755  CG  PHE A 548    19185  16911  16375   1330  -1453  -1093       C  
ATOM    756  CD1 PHE A 548      12.478 -16.708 -13.093  1.00143.09           C  
ANISOU  756  CD1 PHE A 548    19710  17611  17047   1241  -1328  -1015       C  
ATOM    757  CD2 PHE A 548      14.231 -15.714 -11.823  1.00146.24           C  
ANISOU  757  CD2 PHE A 548    20144  17982  17438   1351  -1467  -1125       C  
ATOM    758  CE1 PHE A 548      12.205 -15.491 -13.681  1.00147.10           C  
ANISOU  758  CE1 PHE A 548    20047  18220  17624   1174  -1224   -968       C  
ATOM    759  CE2 PHE A 548      13.964 -14.492 -12.410  1.00151.09           C  
ANISOU  759  CE2 PHE A 548    20587  18698  18123   1281  -1359  -1078       C  
ATOM    760  CZ  PHE A 548      12.949 -14.381 -13.340  1.00151.07           C  
ANISOU  760  CZ  PHE A 548    20484  18758  18158   1193  -1240   -998       C  
ATOM    761  N   GLU A 549      15.364 -19.736  -9.308  1.00 92.47           N  
ANISOU  761  N   GLU A 549    14011  10756  10367   1610  -1896  -1285       N  
ATOM    762  CA  GLU A 549      15.386 -20.935  -8.486  1.00 90.73           C  
ANISOU  762  CA  GLU A 549    14029  10388  10058   1665  -2003  -1301       C  
ATOM    763  C   GLU A 549      14.001 -21.571  -8.529  1.00 71.23           C  
ANISOU  763  C   GLU A 549    11666   7855   7544   1578  -1892  -1197       C  
ATOM    764  O   GLU A 549      13.006 -20.874  -8.720  1.00 64.40           O  
ANISOU  764  O   GLU A 549    10741   7028   6699   1479  -1732  -1107       O  
ATOM    765  CB  GLU A 549      15.767 -20.573  -7.052  1.00125.18           C  
ANISOU  765  CB  GLU A 549    18571  14641  14352   1709  -2062  -1310       C  
ATOM    766  CG  GLU A 549      16.362 -21.712  -6.252  1.00132.04           C  
ANISOU  766  CG  GLU A 549    19654  15373  15140   1804  -2234  -1371       C  
ATOM    767  CD  GLU A 549      17.380 -21.224  -5.243  1.00134.66           C  
ANISOU  767  CD  GLU A 549    20060  15657  15445   1888  -2349  -1440       C  
ATOM    768  OE1 GLU A 549      18.134 -20.283  -5.571  1.00134.72           O  
ANISOU  768  OE1 GLU A 549    19890  15773  15527   1913  -2355  -1498       O  
ATOM    769  OE2 GLU A 549      17.429 -21.780  -4.126  1.00133.15           O  
ANISOU  769  OE2 GLU A 549    20109  15322  15160   1928  -2433  -1437       O  
ATOM    770  N   MET A 550      13.931 -22.888  -8.366  1.00 72.51           N  
ANISOU  770  N   MET A 550    11981   7920   7649   1613  -1977  -1212       N  
ATOM    771  CA  MET A 550      12.647 -23.580  -8.445  1.00 78.54           C  
ANISOU  771  CA  MET A 550    12846   8623   8372   1531  -1876  -1122       C  
ATOM    772  C   MET A 550      11.627 -22.962  -7.494  1.00 79.74           C  
ANISOU  772  C   MET A 550    13128   8701   8467   1444  -1743  -1021       C  
ATOM    773  O   MET A 550      10.431 -22.933  -7.785  1.00 62.94           O  
ANISOU  773  O   MET A 550    10989   6582   6344   1345  -1597   -937       O  
ATOM    774  CB  MET A 550      12.809 -25.077  -8.168  1.00 92.63           C  
ANISOU  774  CB  MET A 550    14815  10288  10090   1589  -2003  -1156       C  
ATOM    775  CG  MET A 550      11.501 -25.860  -8.172  1.00101.04           C  
ANISOU  775  CG  MET A 550    16004  11279  11107   1503  -1903  -1066       C  
ATOM    776  SD  MET A 550      10.465 -25.548  -9.618  1.00 78.60           S  
ANISOU  776  SD  MET A 550    12926   8583   8356   1398  -1726  -1006       S  
ATOM    777  CE  MET A 550      11.596 -25.916 -10.959  1.00 67.49           C  
ANISOU  777  CE  MET A 550    11295   7310   7040   1483  -1846  -1120       C  
ATOM    778  N   LYS A 551      12.109 -22.461  -6.361  1.00 94.05           N  
ANISOU  778  N   LYS A 551    15060  10445  10230   1480  -1793  -1036       N  
ATOM    779  CA  LYS A 551      11.250 -21.800  -5.387  1.00 96.14           C  
ANISOU  779  CA  LYS A 551    15445  10643  10441   1401  -1673   -953       C  
ATOM    780  C   LYS A 551      10.609 -20.558  -5.992  1.00 82.48           C  
ANISOU  780  C   LYS A 551    13511   9033   8795   1315  -1509   -899       C  
ATOM    781  O   LYS A 551       9.409 -20.328  -5.839  1.00 73.32           O  
ANISOU  781  O   LYS A 551    12386   7851   7622   1215  -1362   -815       O  
ATOM    782  CB  LYS A 551      12.054 -21.413  -4.148  1.00113.98           C  
ANISOU  782  CB  LYS A 551    17841  12824  12641   1467  -1771   -994       C  
ATOM    783  CG  LYS A 551      11.252 -20.663  -3.102  1.00111.32           C  
ANISOU  783  CG  LYS A 551    17623  12424  12249   1388  -1651   -919       C  
ATOM    784  CD  LYS A 551      12.137 -20.233  -1.948  1.00106.88           C  
ANISOU  784  CD  LYS A 551    17177  11798  11634   1459  -1755   -966       C  
ATOM    785  CE  LYS A 551      11.358 -19.422  -0.931  1.00105.16           C  
ANISOU  785  CE  LYS A 551    17062  11527  11365   1378  -1631   -898       C  
ATOM    786  NZ  LYS A 551      12.233 -18.953   0.177  1.00108.46           N  
ANISOU  786  NZ  LYS A 551    17586  11890  11733   1447  -1731   -946       N  
ATOM    787  N   LYS A 552      11.424 -19.762  -6.676  1.00 79.69           N  
ANISOU  787  N   LYS A 552    12946   8804   8529   1354  -1537   -951       N  
ATOM    788  CA  LYS A 552      10.962 -18.538  -7.320  1.00 78.79           C  
ANISOU  788  CA  LYS A 552    12627   8808   8501   1281  -1399   -906       C  
ATOM    789  C   LYS A 552       9.960 -18.836  -8.432  1.00 78.21           C  
ANISOU  789  C   LYS A 552    12442   8800   8475   1202  -1288   -849       C  
ATOM    790  O   LYS A 552       8.920 -18.185  -8.535  1.00 74.59           O  
ANISOU  790  O   LYS A 552    11935   8363   8041   1109  -1140   -771       O  
ATOM    791  CB  LYS A 552      12.150 -17.749  -7.873  1.00 87.63           C  
ANISOU  791  CB  LYS A 552    13551  10045   9700   1342  -1468   -982       C  
ATOM    792  CG  LYS A 552      13.134 -17.290  -6.807  1.00104.20           C  
ANISOU  792  CG  LYS A 552    15736  12091  11764   1417  -1568  -1042       C  
ATOM    793  CD  LYS A 552      14.236 -16.427  -7.400  1.00113.38           C  
ANISOU  793  CD  LYS A 552    16690  13378  13013   1464  -1617  -1117       C  
ATOM    794  CE  LYS A 552      15.193 -15.930  -6.325  1.00121.72           C  
ANISOU  794  CE  LYS A 552    17826  14383  14039   1538  -1714  -1180       C  
ATOM    795  NZ  LYS A 552      16.259 -15.057  -6.891  1.00124.73           N  
ANISOU  795  NZ  LYS A 552    18001  14886  14506   1578  -1754  -1257       N  
ATOM    796  N   LEU A 553      10.284 -19.824  -9.260  1.00 82.38           N  
ANISOU  796  N   LEU A 553    12927   9359   9016   1241  -1363   -892       N  
ATOM    797  CA  LEU A 553       9.398 -20.252 -10.337  1.00 71.54           C  
ANISOU  797  CA  LEU A 553    11455   8044   7682   1175  -1273   -847       C  
ATOM    798  C   LEU A 553       8.003 -20.572  -9.812  1.00 62.44           C  
ANISOU  798  C   LEU A 553    10451   6797   6477   1087  -1153   -758       C  
ATOM    799  O   LEU A 553       7.001 -20.208 -10.425  1.00 66.53           O  
ANISOU  799  O   LEU A 553    10868   7371   7041   1001  -1018   -695       O  
ATOM    800  CB  LEU A 553       9.981 -21.470 -11.058  1.00 65.70           C  
ANISOU  800  CB  LEU A 553    10698   7319   6945   1240  -1391   -916       C  
ATOM    801  CG  LEU A 553      11.317 -21.250 -11.771  1.00 57.33           C  
ANISOU  801  CG  LEU A 553     9466   6369   5946   1320  -1503  -1015       C  
ATOM    802  CD1 LEU A 553      11.845 -22.559 -12.343  1.00 51.86           C  
ANISOU  802  CD1 LEU A 553     8782   5672   5249   1386  -1624  -1090       C  
ATOM    803  CD2 LEU A 553      11.187 -20.187 -12.858  1.00 55.53           C  
ANISOU  803  CD2 LEU A 553     8987   6299   5812   1263  -1403   -993       C  
ATOM    804  N   ILE A 554       7.946 -21.259  -8.676  1.00 60.96           N  
ANISOU  804  N   ILE A 554    10505   6466   6191   1106  -1203   -756       N  
ATOM    805  CA  ILE A 554       6.671 -21.582  -8.049  1.00 71.12           C  
ANISOU  805  CA  ILE A 554    11953   7654   7416   1018  -1090   -680       C  
ATOM    806  C   ILE A 554       5.970 -20.313  -7.588  1.00 74.62           C  
ANISOU  806  C   ILE A 554    12358   8114   7880    940   -950   -621       C  
ATOM    807  O   ILE A 554       4.757 -20.182  -7.729  1.00 86.01           O  
ANISOU  807  O   ILE A 554    13790   9555   9335    845   -809   -557       O  
ATOM    808  CB  ILE A 554       6.849 -22.528  -6.846  1.00 80.76           C  
ANISOU  808  CB  ILE A 554    13455   8713   8518   1054  -1180   -692       C  
ATOM    809  CG1 ILE A 554       7.407 -23.875  -7.309  1.00 79.27           C  
ANISOU  809  CG1 ILE A 554    13314   8494   8310   1126  -1316   -746       C  
ATOM    810  CG2 ILE A 554       5.526 -22.719  -6.113  1.00 80.92           C  
ANISOU  810  CG2 ILE A 554    13643   8633   8470    950  -1048   -613       C  
ATOM    811  CD1 ILE A 554       7.608 -24.861  -6.188  1.00 85.52           C  
ANISOU  811  CD1 ILE A 554    14387   9120   8985   1164  -1419   -757       C  
ATOM    812  N   ASP A 555       6.739 -19.379  -7.038  1.00 67.07           N  
ANISOU  812  N   ASP A 555    11378   7173   6933    982   -992   -650       N  
ATOM    813  CA  ASP A 555       6.181 -18.109  -6.589  1.00 67.64           C  
ANISOU  813  CA  ASP A 555    11404   7263   7031    916   -871   -604       C  
ATOM    814  C   ASP A 555       5.522 -17.382  -7.754  1.00 62.38           C  
ANISOU  814  C   ASP A 555    10507   6723   6473    850   -753   -563       C  
ATOM    815  O   ASP A 555       4.374 -16.948  -7.661  1.00 70.11           O  
ANISOU  815  O   ASP A 555    11478   7694   7468    759   -613   -501       O  
ATOM    816  CB  ASP A 555       7.267 -17.226  -5.974  1.00 72.40           C  
ANISOU  816  CB  ASP A 555    11991   7879   7640    983   -950   -652       C  
ATOM    817  CG  ASP A 555       6.701 -15.975  -5.332  1.00 74.86           C  
ANISOU  817  CG  ASP A 555    12285   8189   7969    918   -833   -608       C  
ATOM    818  OD1 ASP A 555       5.542 -16.021  -4.868  1.00 79.77           O  
ANISOU  818  OD1 ASP A 555    13003   8750   8557    832   -716   -549       O  
ATOM    819  OD2 ASP A 555       7.412 -14.948  -5.289  1.00 70.75           O  
ANISOU  819  OD2 ASP A 555    11655   7729   7499    952   -858   -636       O  
ATOM    820  N   ILE A 556       6.264 -17.252  -8.849  1.00 44.18           N  
ANISOU  820  N   ILE A 556     8013   4533   4241    896   -812   -602       N  
ATOM    821  CA  ILE A 556       5.755 -16.618 -10.058  1.00 39.16           C  
ANISOU  821  CA  ILE A 556     7154   4022   3704    840   -718   -567       C  
ATOM    822  C   ILE A 556       4.499 -17.330 -10.542  1.00 41.94           C  
ANISOU  822  C   ILE A 556     7526   4357   4053    765   -621   -513       C  
ATOM    823  O   ILE A 556       3.519 -16.696 -10.925  1.00 50.66           O  
ANISOU  823  O   ILE A 556     8535   5503   5211    685   -494   -456       O  
ATOM    824  CB  ILE A 556       6.810 -16.639 -11.174  1.00 48.34           C  
ANISOU  824  CB  ILE A 556     8138   5304   4927    902   -811   -627       C  
ATOM    825  CG1 ILE A 556       8.033 -15.818 -10.758  1.00 46.41           C  
ANISOU  825  CG1 ILE A 556     7851   5087   4697    968   -896   -684       C  
ATOM    826  CG2 ILE A 556       6.222 -16.107 -12.467  1.00 61.35           C  
ANISOU  826  CG2 ILE A 556     9571   7074   6664    838   -716   -585       C  
ATOM    827  CD1 ILE A 556       9.209 -15.942 -11.704  1.00 52.22           C  
ANISOU  827  CD1 ILE A 556     8434   5928   5480   1036  -1002   -762       C  
ATOM    828  N   ALA A 557       4.539 -18.657 -10.517  1.00 55.02           N  
ANISOU  828  N   ALA A 557     9306   5950   5650    794   -686   -535       N  
ATOM    829  CA  ALA A 557       3.388 -19.469 -10.889  1.00 50.15           C  
ANISOU  829  CA  ALA A 557     8729   5303   5021    727   -602   -491       C  
ATOM    830  C   ALA A 557       2.256 -19.283  -9.885  1.00 51.39           C  
ANISOU  830  C   ALA A 557     9034   5360   5129    644   -482   -435       C  
ATOM    831  O   ALA A 557       1.080 -19.364 -10.235  1.00 45.66           O  
ANISOU  831  O   ALA A 557     8281   4640   4428    562   -362   -388       O  
ATOM    832  CB  ALA A 557       3.783 -20.929 -10.970  1.00 51.07           C  
ANISOU  832  CB  ALA A 557     8963   5363   5081    782   -710   -533       C  
ATOM    833  N   ARG A 558       2.627 -19.039  -8.633  1.00 66.66           N  
ANISOU  833  N   ARG A 558    11126   7205   6996    666   -517   -446       N  
ATOM    834  CA  ARG A 558       1.666 -18.892  -7.549  1.00 66.38           C  
ANISOU  834  CA  ARG A 558    11251   7069   6901    590   -413   -403       C  
ATOM    835  C   ARG A 558       0.909 -17.575  -7.663  1.00 64.89           C  
ANISOU  835  C   ARG A 558    10924   6942   6791    516   -276   -362       C  
ATOM    836  O   ARG A 558      -0.317 -17.541  -7.563  1.00 73.99           O  
ANISOU  836  O   ARG A 558    12098   8068   7948    425   -146   -320       O  
ATOM    837  CB  ARG A 558       2.382 -18.961  -6.199  1.00 75.36           C  
ANISOU  837  CB  ARG A 558    12591   8100   7943    639   -500   -431       C  
ATOM    838  CG  ARG A 558       1.464 -19.163  -5.003  1.00 85.78           C  
ANISOU  838  CG  ARG A 558    14126   9295   9172    562   -412   -395       C  
ATOM    839  CD  ARG A 558       1.834 -18.222  -3.867  1.00 86.16           C  
ANISOU  839  CD  ARG A 558    14246   9306   9187    571   -416   -403       C  
ATOM    840  NE  ARG A 558       3.280 -18.108  -3.696  1.00 89.03           N  
ANISOU  840  NE  ARG A 558    14605   9681   9540    685   -575   -460       N  
ATOM    841  CZ  ARG A 558       3.970 -18.694  -2.722  1.00102.51           C  
ANISOU  841  CZ  ARG A 558    16518  11285  11146    743   -690   -491       C  
ATOM    842  NH1 ARG A 558       3.349 -19.438  -1.817  1.00107.46           N  
ANISOU  842  NH1 ARG A 558    17380  11785  11664    694   -661   -466       N  
ATOM    843  NH2 ARG A 558       5.285 -18.530  -2.651  1.00108.73           N  
ANISOU  843  NH2 ARG A 558    17279  12094  11939    849   -834   -551       N  
ATOM    844  N   GLN A 559       1.650 -16.491  -7.869  1.00 47.52           N  
ANISOU  844  N   GLN A 559     8580   4823   4654    555   -309   -379       N  
ATOM    845  CA  GLN A 559       1.055 -15.166  -7.980  1.00 37.03           C  
ANISOU  845  CA  GLN A 559     7113   3552   3405    495   -196   -344       C  
ATOM    846  C   GLN A 559       0.118 -15.078  -9.181  1.00 43.35           C  
ANISOU  846  C   GLN A 559     7745   4435   4290    432    -99   -305       C  
ATOM    847  O   GLN A 559      -0.941 -14.454  -9.108  1.00 48.52           O  
ANISOU  847  O   GLN A 559     8359   5091   4987    353     27   -265       O  
ATOM    848  CB  GLN A 559       2.143 -14.093  -8.076  1.00 43.64           C  
ANISOU  848  CB  GLN A 559     7823   4463   4295    555   -263   -373       C  
ATOM    849  CG  GLN A 559       3.097 -14.061  -6.891  1.00 44.15           C  
ANISOU  849  CG  GLN A 559     8040   4452   4283    621   -360   -417       C  
ATOM    850  CD  GLN A 559       4.052 -12.883  -6.942  1.00 49.07           C  
ANISOU  850  CD  GLN A 559     8529   5147   4966    668   -407   -446       C  
ATOM    851  OE1 GLN A 559       3.651 -11.757  -7.232  1.00 46.38           O  
ANISOU  851  OE1 GLN A 559     8048   4869   4707    622   -322   -415       O  
ATOM    852  NE2 GLN A 559       5.323 -13.138  -6.653  1.00 57.18           N  
ANISOU  852  NE2 GLN A 559     9602   6166   5958    762   -546   -508       N  
ATOM    853  N   THR A 560       0.509 -15.708 -10.284  1.00 58.54           N  
ANISOU  853  N   THR A 560     9571   6429   6242    469   -161   -320       N  
ATOM    854  CA  THR A 560      -0.306 -15.694 -11.495  1.00 56.37           C  
ANISOU  854  CA  THR A 560     9136   6238   6045    416    -83   -287       C  
ATOM    855  C   THR A 560      -1.674 -16.327 -11.246  1.00 49.10           C  
ANISOU  855  C   THR A 560     8316   5245   5095    334     28   -252       C  
ATOM    856  O   THR A 560      -2.686 -15.863 -11.766  1.00 50.10           O  
ANISOU  856  O   THR A 560     8335   5413   5290    265    138   -216       O  
ATOM    857  CB  THR A 560       0.392 -16.419 -12.664  1.00 47.49           C  
ANISOU  857  CB  THR A 560     7908   5194   4940    471   -176   -317       C  
ATOM    858  OG1 THR A 560       1.674 -15.826 -12.903  1.00 37.75           O  
ANISOU  858  OG1 THR A 560     6576   4032   3734    541   -275   -358       O  
ATOM    859  CG2 THR A 560      -0.448 -16.322 -13.928  1.00 37.95           C  
ANISOU  859  CG2 THR A 560     6530   4078   3811    414    -95   -281       C  
ATOM    860  N   ALA A 561      -1.699 -17.386 -10.445  1.00 43.88           N  
ANISOU  860  N   ALA A 561     7865   4474   4335    342     -3   -267       N  
ATOM    861  CA  ALA A 561      -2.953 -18.048 -10.106  1.00 40.67           C  
ANISOU  861  CA  ALA A 561     7574   3988   3890    260    103   -241       C  
ATOM    862  C   ALA A 561      -3.807 -17.143  -9.226  1.00 58.56           C  
ANISOU  862  C   ALA A 561     9880   6209   6161    184    225   -216       C  
ATOM    863  O   ALA A 561      -5.029 -17.100  -9.365  1.00 63.96           O  
ANISOU  863  O   ALA A 561    10541   6887   6876    100    349   -190       O  
ATOM    864  CB  ALA A 561      -2.690 -19.372  -9.419  1.00 39.01           C  
ANISOU  864  CB  ALA A 561     7589   3664   3566    287     32   -262       C  
ATOM    865  N   ARG A 562      -3.154 -16.428  -8.315  1.00 65.58           N  
ANISOU  865  N   ARG A 562    10827   7068   7022    215    187   -229       N  
ATOM    866  CA  ARG A 562      -3.838 -15.446  -7.483  1.00 57.59           C  
ANISOU  866  CA  ARG A 562     9836   6023   6022    150    294   -213       C  
ATOM    867  C   ARG A 562      -4.533 -14.420  -8.367  1.00 46.94           C  
ANISOU  867  C   ARG A 562     8263   4772   4799    103    386   -187       C  
ATOM    868  O   ARG A 562      -5.720 -14.143  -8.196  1.00 54.57           O  
ANISOU  868  O   ARG A 562     9223   5718   5794     18    513   -168       O  
ATOM    869  CB  ARG A 562      -2.853 -14.757  -6.533  1.00 56.19           C  
ANISOU  869  CB  ARG A 562     9724   5818   5808    204    222   -237       C  
ATOM    870  CG  ARG A 562      -2.403 -15.629  -5.370  1.00 62.46           C  
ANISOU  870  CG  ARG A 562    10772   6491   6468    232    153   -259       C  
ATOM    871  CD  ARG A 562      -1.368 -14.931  -4.504  1.00 71.87           C  
ANISOU  871  CD  ARG A 562    12014   7664   7629    294     71   -287       C  
ATOM    872  NE  ARG A 562      -1.071 -15.699  -3.297  1.00 77.15           N  
ANISOU  872  NE  ARG A 562    12940   8208   8164    309     15   -304       N  
ATOM    873  CZ  ARG A 562      -0.023 -15.483  -2.507  1.00 77.96           C  
ANISOU  873  CZ  ARG A 562    13133   8275   8214    381    -91   -336       C  
ATOM    874  NH1 ARG A 562       0.844 -14.523  -2.796  1.00 71.59           N  
ANISOU  874  NH1 ARG A 562    12175   7550   7478    442   -148   -358       N  
ATOM    875  NH2 ARG A 562       0.162 -16.235  -1.431  1.00 83.44           N  
ANISOU  875  NH2 ARG A 562    14071   8851   8782    389   -142   -347       N  
ATOM    876  N   GLY A 563      -3.788 -13.869  -9.320  1.00 38.19           N  
ANISOU  876  N   GLY A 563     6974   3770   3766    158    320   -188       N  
ATOM    877  CA  GLY A 563      -4.332 -12.902 -10.255  1.00 34.30           C  
ANISOU  877  CA  GLY A 563     6267   3374   3392    121    388   -159       C  
ATOM    878  C   GLY A 563      -5.442 -13.478 -11.115  1.00 50.62           C  
ANISOU  878  C   GLY A 563     8272   5464   5497     62    467   -136       C  
ATOM    879  O   GLY A 563      -6.483 -12.846 -11.302  1.00 62.70           O  
ANISOU  879  O   GLY A 563     9716   7010   7097     -5    575   -114       O  
ATOM    880  N   MET A 564      -5.224 -14.681 -11.637  1.00 39.74           N  
ANISOU  880  N   MET A 564     6936   4088   4078     90    412   -147       N  
ATOM    881  CA  MET A 564      -6.205 -15.328 -12.503  1.00 40.59           C  
ANISOU  881  CA  MET A 564     6984   4220   4218     40    477   -131       C  
ATOM    882  C   MET A 564      -7.479 -15.704 -11.756  1.00 39.67           C  
ANISOU  882  C   MET A 564     6995   4009   4067    -46    599   -125       C  
ATOM    883  O   MET A 564      -8.581 -15.554 -12.282  1.00 43.81           O  
ANISOU  883  O   MET A 564     7428   4560   4656   -111    698   -109       O  
ATOM    884  CB  MET A 564      -5.606 -16.563 -13.173  1.00 47.34           C  
ANISOU  884  CB  MET A 564     7861   5093   5032     93    383   -150       C  
ATOM    885  CG  MET A 564      -4.565 -16.246 -14.228  1.00 47.56           C  
ANISOU  885  CG  MET A 564     7721   5237   5111    161    284   -160       C  
ATOM    886  SD  MET A 564      -5.162 -15.037 -15.424  1.00 44.64           S  
ANISOU  886  SD  MET A 564     7096   4993   4874    117    356   -120       S  
ATOM    887  CE  MET A 564      -6.641 -15.851 -16.025  1.00 30.59           C  
ANISOU  887  CE  MET A 564     5304   3202   3115     43    461   -100       C  
ATOM    888  N   ASP A 565      -7.323 -16.199 -10.532  1.00 48.40           N  
ANISOU  888  N   ASP A 565     8313   5006   5071    -48    589   -142       N  
ATOM    889  CA  ASP A 565      -8.473 -16.552  -9.711  1.00 51.93           C  
ANISOU  889  CA  ASP A 565     8899   5360   5474   -137    707   -141       C  
ATOM    890  C   ASP A 565      -9.282 -15.311  -9.350  1.00 50.67           C  
ANISOU  890  C   ASP A 565     8659   5209   5383   -202    821   -134       C  
ATOM    891  O   ASP A 565     -10.511 -15.354  -9.307  1.00 52.23           O  
ANISOU  891  O   ASP A 565     8853   5384   5608   -286    942   -133       O  
ATOM    892  CB  ASP A 565      -8.032 -17.277  -8.439  1.00 61.71           C  
ANISOU  892  CB  ASP A 565    10390   6478   6578   -126    664   -159       C  
ATOM    893  CG  ASP A 565      -9.205 -17.723  -7.588  1.00 67.56           C  
ANISOU  893  CG  ASP A 565    11288   7121   7262   -226    788   -161       C  
ATOM    894  OD1 ASP A 565     -10.321 -17.862  -8.132  1.00 63.24           O  
ANISOU  894  OD1 ASP A 565    10665   6594   6770   -296    893   -154       O  
ATOM    895  OD2 ASP A 565      -9.010 -17.936  -6.374  1.00 75.07           O  
ANISOU  895  OD2 ASP A 565    12438   7974   8112   -238    781   -171       O  
ATOM    896  N   TYR A 566      -8.588 -14.206  -9.088  1.00 45.55           N  
ANISOU  896  N   TYR A 566     7946   4593   4767   -162    780   -133       N  
ATOM    897  CA  TYR A 566      -9.254 -12.945  -8.788  1.00 37.59           C  
ANISOU  897  CA  TYR A 566     6848   3599   3836   -215    875   -129       C  
ATOM    898  C   TYR A 566     -10.070 -12.477  -9.984  1.00 53.30           C  
ANISOU  898  C   TYR A 566     8627   5675   5949   -248    936   -109       C  
ATOM    899  O   TYR A 566     -11.224 -12.071  -9.839  1.00 62.88           O  
ANISOU  899  O   TYR A 566     9805   6873   7215   -324   1052   -112       O  
ATOM    900  CB  TYR A 566      -8.241 -11.866  -8.399  1.00 38.50           C  
ANISOU  900  CB  TYR A 566     6921   3740   3969   -157    805   -132       C  
ATOM    901  CG  TYR A 566      -8.856 -10.495  -8.202  1.00 47.98           C  
ANISOU  901  CG  TYR A 566     8006   4961   5261   -203    891   -127       C  
ATOM    902  CD1 TYR A 566      -9.421 -10.132  -6.984  1.00 51.63           C  
ANISOU  902  CD1 TYR A 566     8581   5345   5691   -260    975   -148       C  
ATOM    903  CD2 TYR A 566      -8.873  -9.565  -9.233  1.00 45.14           C  
ANISOU  903  CD2 TYR A 566     7430   4699   5023   -191    886   -105       C  
ATOM    904  CE1 TYR A 566      -9.986  -8.881  -6.800  1.00 39.67           C  
ANISOU  904  CE1 TYR A 566     6958   3849   4267   -301   1051   -150       C  
ATOM    905  CE2 TYR A 566      -9.435  -8.313  -9.058  1.00 42.95           C  
ANISOU  905  CE2 TYR A 566     7050   4435   4835   -230    957   -102       C  
ATOM    906  CZ  TYR A 566      -9.990  -7.976  -7.840  1.00 40.82           C  
ANISOU  906  CZ  TYR A 566     6887   4087   4537   -283   1039   -127       C  
ATOM    907  OH  TYR A 566     -10.549  -6.731  -7.663  1.00 45.75           O  
ANISOU  907  OH  TYR A 566     7403   4722   5256   -320   1106   -131       O  
ATOM    908  N   LEU A 567      -9.460 -12.535 -11.165  1.00 55.54           N  
ANISOU  908  N   LEU A 567     8774   6050   6279   -192    854    -92       N  
ATOM    909  CA  LEU A 567     -10.124 -12.109 -12.392  1.00 48.74           C  
ANISOU  909  CA  LEU A 567     7713   5277   5529   -217    895    -69       C  
ATOM    910  C   LEU A 567     -11.416 -12.885 -12.625  1.00 40.39           C  
ANISOU  910  C   LEU A 567     6679   4190   4478   -288    994    -74       C  
ATOM    911  O   LEU A 567     -12.457 -12.297 -12.913  1.00 47.85           O  
ANISOU  911  O   LEU A 567     7520   5154   5508   -346   1086    -70       O  
ATOM    912  CB  LEU A 567      -9.192 -12.259 -13.600  1.00 42.84           C  
ANISOU  912  CB  LEU A 567     6841   4629   4808   -148    787    -55       C  
ATOM    913  CG  LEU A 567      -7.979 -11.328 -13.684  1.00 44.89           C  
ANISOU  913  CG  LEU A 567     7022   4945   5091    -83    695    -50       C  
ATOM    914  CD1 LEU A 567      -7.189 -11.582 -14.961  1.00 35.99           C  
ANISOU  914  CD1 LEU A 567     5767   3920   3987    -30    603    -42       C  
ATOM    915  CD2 LEU A 567      -8.407  -9.871 -13.602  1.00 38.68           C  
ANISOU  915  CD2 LEU A 567     6117   4181   4397   -116    753    -32       C  
ATOM    916  N   HIS A 568     -11.343 -14.205 -12.491  1.00 46.97           N  
ANISOU  916  N   HIS A 568     7649   4974   5223   -284    973    -87       N  
ATOM    917  CA  HIS A 568     -12.501 -15.063 -12.720  1.00 52.41           C  
ANISOU  917  CA  HIS A 568     8370   5633   5910   -351   1063    -95       C  
ATOM    918  C   HIS A 568     -13.557 -14.917 -11.628  1.00 61.62           C  
ANISOU  918  C   HIS A 568     9646   6710   7056   -439   1190   -117       C  
ATOM    919  O   HIS A 568     -14.749 -15.084 -11.884  1.00 62.65           O  
ANISOU  919  O   HIS A 568     9737   6836   7233   -509   1294   -128       O  
ATOM    920  CB  HIS A 568     -12.069 -16.523 -12.856  1.00 46.11           C  
ANISOU  920  CB  HIS A 568     7694   4802   5021   -320    999   -104       C  
ATOM    921  CG  HIS A 568     -11.301 -16.808 -14.109  1.00 37.59           C  
ANISOU  921  CG  HIS A 568     6488   3821   3975   -250    896    -92       C  
ATOM    922  ND1 HIS A 568     -10.561 -17.957 -14.282  1.00 40.71           N  
ANISOU  922  ND1 HIS A 568     6971   4201   4297   -198    803   -104       N  
ATOM    923  CD2 HIS A 568     -11.160 -16.094 -15.250  1.00 35.97           C  
ANISOU  923  CD2 HIS A 568     6074   3728   3866   -227    870    -72       C  
ATOM    924  CE1 HIS A 568      -9.998 -17.939 -15.478  1.00 49.81           C  
ANISOU  924  CE1 HIS A 568     7969   5457   5500   -147    729    -97       C  
ATOM    925  NE2 HIS A 568     -10.346 -16.819 -16.085  1.00 43.06           N  
ANISOU  925  NE2 HIS A 568     6935   4681   4743   -166    770    -75       N  
ATOM    926  N   ALA A 569     -13.115 -14.616 -10.411  1.00 59.26           N  
ANISOU  926  N   ALA A 569     9485   6343   6690   -436   1183   -129       N  
ATOM    927  CA  ALA A 569     -14.039 -14.299  -9.329  1.00 50.33           C  
ANISOU  927  CA  ALA A 569     8446   5134   5541   -522   1304   -154       C  
ATOM    928  C   ALA A 569     -14.805 -13.038  -9.707  1.00 54.58           C  
ANISOU  928  C   ALA A 569     8796   5729   6213   -558   1380   -155       C  
ATOM    929  O   ALA A 569     -15.964 -12.860  -9.333  1.00 50.68           O  
ANISOU  929  O   ALA A 569     8305   5200   5750   -642   1502   -182       O  
ATOM    930  CB  ALA A 569     -13.289 -14.101  -8.028  1.00 52.96           C  
ANISOU  930  CB  ALA A 569     8947   5395   5779   -503   1267   -164       C  
ATOM    931  N   LYS A 570     -14.137 -12.166 -10.455  1.00 63.44           N  
ANISOU  931  N   LYS A 570     9754   6937   7413   -495   1304   -129       N  
ATOM    932  CA  LYS A 570     -14.761 -10.972 -11.005  1.00 58.91           C  
ANISOU  932  CA  LYS A 570     8987   6424   6973   -517   1352   -123       C  
ATOM    933  C   LYS A 570     -15.380 -11.294 -12.361  1.00 64.60           C  
ANISOU  933  C   LYS A 570     9560   7215   7772   -525   1363   -108       C  
ATOM    934  O   LYS A 570     -15.747 -10.394 -13.118  1.00 58.73           O  
ANISOU  934  O   LYS A 570     8637   6536   7141   -527   1373    -93       O  
ATOM    935  CB  LYS A 570     -13.727  -9.856 -11.157  1.00 56.21           C  
ANISOU  935  CB  LYS A 570     8545   6137   6674   -450   1263    -99       C  
ATOM    936  CG  LYS A 570     -13.172  -9.329  -9.843  1.00 60.28           C  
ANISOU  936  CG  LYS A 570     9180   6590   7132   -441   1256   -117       C  
ATOM    937  CD  LYS A 570     -14.172  -8.433  -9.135  1.00 61.05           C  
ANISOU  937  CD  LYS A 570     9256   6651   7290   -513   1371   -145       C  
ATOM    938  CE  LYS A 570     -13.504  -7.662  -8.009  1.00 64.13           C  
ANISOU  938  CE  LYS A 570     9721   7001   7643   -495   1350   -159       C  
ATOM    939  NZ  LYS A 570     -14.385  -6.602  -7.451  1.00 73.65           N  
ANISOU  939  NZ  LYS A 570    10869   8186   8929   -556   1450   -187       N  
ATOM    940  N   SER A 571     -15.486 -12.588 -12.656  1.00 66.45           N  
ANISOU  940  N   SER A 571     9874   7433   7942   -529   1357   -112       N  
ATOM    941  CA  SER A 571     -16.028 -13.071 -13.926  1.00 73.17           C  
ANISOU  941  CA  SER A 571    10601   8347   8852   -535   1363   -101       C  
ATOM    942  C   SER A 571     -15.375 -12.402 -15.135  1.00 74.39           C  
ANISOU  942  C   SER A 571    10568   8613   9085   -473   1273    -63       C  
ATOM    943  O   SER A 571     -16.052 -12.039 -16.097  1.00 78.42           O  
ANISOU  943  O   SER A 571    10920   9186   9692   -491   1300    -52       O  
ATOM    944  CB  SER A 571     -17.551 -12.899 -13.970  1.00116.67           C  
ANISOU  944  CB  SER A 571    16053  13840  14437   -621   1495   -129       C  
ATOM    945  OG  SER A 571     -17.916 -11.529 -13.909  1.00130.12           O  
ANISOU  945  OG  SER A 571    17631  15566  16241   -636   1529   -130       O  
ATOM    946  N   ILE A 572     -14.056 -12.250 -15.080  1.00 64.70           N  
ANISOU  946  N   ILE A 572     9360   7410   7813   -401   1165    -46       N  
ATOM    947  CA  ILE A 572     -13.309 -11.641 -16.174  1.00 45.23           C  
ANISOU  947  CA  ILE A 572     6729   5049   5407   -345   1076    -12       C  
ATOM    948  C   ILE A 572     -12.401 -12.654 -16.864  1.00 43.85           C  
ANISOU  948  C   ILE A 572     6571   4918   5172   -287    978     -8       C  
ATOM    949  O   ILE A 572     -11.472 -13.187 -16.258  1.00 40.59           O  
ANISOU  949  O   ILE A 572     6286   4466   4670   -242    912    -22       O  
ATOM    950  CB  ILE A 572     -12.463 -10.448 -15.688  1.00 48.65           C  
ANISOU  950  CB  ILE A 572     7135   5493   5859   -309   1028     -1       C  
ATOM    951  CG1 ILE A 572     -13.367  -9.342 -15.143  1.00 49.99           C  
ANISOU  951  CG1 ILE A 572     7259   5629   6105   -364   1120     -7       C  
ATOM    952  CG2 ILE A 572     -11.589  -9.917 -16.816  1.00 32.13           C  
ANISOU  952  CG2 ILE A 572     4885   3507   3814   -255    934     31       C  
ATOM    953  CD1 ILE A 572     -12.618  -8.138 -14.610  1.00 40.33           C  
ANISOU  953  CD1 ILE A 572     6009   4409   4904   -334   1081      1       C  
ATOM    954  N   ILE A 573     -12.682 -12.919 -18.135  1.00 58.20           N  
ANISOU  954  N   ILE A 573     8258   6815   7041   -286    967      8       N  
ATOM    955  CA  ILE A 573     -11.855 -13.818 -18.927  1.00 54.52           C  
ANISOU  955  CA  ILE A 573     7780   6404   6531   -233    875      7       C  
ATOM    956  C   ILE A 573     -10.711 -13.033 -19.558  1.00 63.01           C  
ANISOU  956  C   ILE A 573     8736   7571   7635   -177    778     28       C  
ATOM    957  O   ILE A 573     -10.942 -12.140 -20.374  1.00 72.21           O  
ANISOU  957  O   ILE A 573     9742   8811   8886   -189    785     58       O  
ATOM    958  CB  ILE A 573     -12.673 -14.490 -20.044  1.00 45.11           C  
ANISOU  958  CB  ILE A 573     6499   5262   5379   -261    907     11       C  
ATOM    959  CG1 ILE A 573     -13.990 -15.035 -19.487  1.00 38.19           C  
ANISOU  959  CG1 ILE A 573     5710   4302   4498   -331   1023    -11       C  
ATOM    960  CG2 ILE A 573     -11.865 -15.596 -20.708  1.00 43.16           C  
ANISOU  960  CG2 ILE A 573     6266   5057   5075   -210    819      0       C  
ATOM    961  CD1 ILE A 573     -14.915 -15.598 -20.546  1.00 43.39           C  
ANISOU  961  CD1 ILE A 573     6272   5008   5207   -364   1065    -11       C  
ATOM    962  N   HIS A 574      -9.480 -13.359 -19.179  1.00 46.60           N  
ANISOU  962  N   HIS A 574     6738   5485   5485   -116    687     10       N  
ATOM    963  CA  HIS A 574      -8.323 -12.667 -19.735  1.00 42.74           C  
ANISOU  963  CA  HIS A 574     6140   5081   5017    -64    596     20       C  
ATOM    964  C   HIS A 574      -8.312 -12.783 -21.255  1.00 39.32           C  
ANISOU  964  C   HIS A 574     5543   4764   4633    -62    566     38       C  
ATOM    965  O   HIS A 574      -8.099 -11.798 -21.960  1.00 46.55           O  
ANISOU  965  O   HIS A 574     6314   5759   5613    -64    549     67       O  
ATOM    966  CB  HIS A 574      -7.019 -13.219 -19.160  1.00 34.40           C  
ANISOU  966  CB  HIS A 574     5197   3999   3874      5    497    -16       C  
ATOM    967  CG  HIS A 574      -5.818 -12.393 -19.501  1.00 38.95           C  
ANISOU  967  CG  HIS A 574     5676   4652   4472     53    413    -16       C  
ATOM    968  ND1 HIS A 574      -5.332 -12.280 -20.785  1.00 38.31           N  
ANISOU  968  ND1 HIS A 574     5440   4687   4428     69    361     -8       N  
ATOM    969  CD2 HIS A 574      -5.006 -11.637 -18.723  1.00 37.26           C  
ANISOU  969  CD2 HIS A 574     5497   4416   4245     85    374    -27       C  
ATOM    970  CE1 HIS A 574      -4.272 -11.489 -20.785  1.00 33.88           C  
ANISOU  970  CE1 HIS A 574     4823   4172   3877    106    297    -14       C  
ATOM    971  NE2 HIS A 574      -4.054 -11.087 -19.547  1.00 31.08           N  
ANISOU  971  NE2 HIS A 574     4579   3734   3494    119    302    -26       N  
ATOM    972  N   ARG A 575      -8.536 -14.002 -21.742  1.00 52.34           N  
ANISOU  972  N   ARG A 575     7220   6418   6247    -60    560     20       N  
ATOM    973  CA  ARG A 575      -8.629 -14.296 -23.176  1.00 44.49           C  
ANISOU  973  CA  ARG A 575     6084   5530   5292    -62    538     32       C  
ATOM    974  C   ARG A 575      -7.287 -14.398 -23.900  1.00 35.22           C  
ANISOU  974  C   ARG A 575     4838   4448   4097     -5    429     16       C  
ATOM    975  O   ARG A 575      -7.225 -14.903 -25.019  1.00 28.88           O  
ANISOU  975  O   ARG A 575     3942   3728   3304     -1    401     13       O  
ATOM    976  CB  ARG A 575      -9.546 -13.298 -23.892  1.00 40.42           C  
ANISOU  976  CB  ARG A 575     5418   5067   4873   -113    600     76       C  
ATOM    977  CG  ARG A 575     -11.022 -13.525 -23.629  1.00 40.47           C  
ANISOU  977  CG  ARG A 575     5456   5009   4910   -173    708     78       C  
ATOM    978  CD  ARG A 575     -11.895 -12.583 -24.443  1.00 38.39           C  
ANISOU  978  CD  ARG A 575     5035   4801   4748   -216    754    116       C  
ATOM    979  NE  ARG A 575     -13.314 -12.801 -24.179  1.00 54.08           N  
ANISOU  979  NE  ARG A 575     7047   6728   6772   -272    857    107       N  
ATOM    980  CZ  ARG A 575     -13.962 -12.309 -23.127  1.00 69.49           C  
ANISOU  980  CZ  ARG A 575     9069   8593   8741   -307    931     97       C  
ATOM    981  NH1 ARG A 575     -13.317 -11.571 -22.233  1.00 67.95           N  
ANISOU  981  NH1 ARG A 575     8928   8360   8529   -288    912     99       N  
ATOM    982  NH2 ARG A 575     -15.255 -12.558 -22.964  1.00 77.59           N  
ANISOU  982  NH2 ARG A 575    10107   9571   9802   -362   1026     80       N  
ATOM    983  N   ASP A 576      -6.220 -13.921 -23.267  1.00 45.09           N  
ANISOU  983  N   ASP A 576     6130   5686   5318     39    368      0       N  
ATOM    984  CA  ASP A 576      -4.894 -13.988 -23.875  1.00 48.34           C  
ANISOU  984  CA  ASP A 576     6474   6183   5711     92    265    -26       C  
ATOM    985  C   ASP A 576      -3.793 -13.978 -22.821  1.00 37.16           C  
ANISOU  985  C   ASP A 576     5173   4710   4237    149    196    -66       C  
ATOM    986  O   ASP A 576      -2.904 -13.129 -22.848  1.00 40.42           O  
ANISOU  986  O   ASP A 576     5523   5171   4666    174    149    -70       O  
ATOM    987  CB  ASP A 576      -4.694 -12.836 -24.866  1.00 50.01           C  
ANISOU  987  CB  ASP A 576     6504   6506   5992     72    258     11       C  
ATOM    988  CG  ASP A 576      -3.429 -12.989 -25.697  1.00 50.47           C  
ANISOU  988  CG  ASP A 576     6475   6669   6033    113    163    -21       C  
ATOM    989  OD1 ASP A 576      -3.187 -12.138 -26.579  1.00 64.09           O  
ANISOU  989  OD1 ASP A 576     8056   8491   7805     93    154      6       O  
ATOM    990  OD2 ASP A 576      -2.675 -13.958 -25.474  1.00 50.57           O  
ANISOU  990  OD2 ASP A 576     6563   6666   5985    165     97    -77       O  
ATOM    991  N   LEU A 577      -3.858 -14.920 -21.887  1.00 34.52           N  
ANISOU  991  N   LEU A 577     5010   4273   3834    169    190    -96       N  
ATOM    992  CA  LEU A 577      -2.804 -15.063 -20.894  1.00 33.06           C  
ANISOU  992  CA  LEU A 577     4947   4029   3586    230    113   -138       C  
ATOM    993  C   LEU A 577      -1.588 -15.738 -21.514  1.00 37.04           C  
ANISOU  993  C   LEU A 577     5413   4599   4062    295     -2   -193       C  
ATOM    994  O   LEU A 577      -1.683 -16.836 -22.065  1.00 34.56           O  
ANISOU  994  O   LEU A 577     5106   4298   3726    305    -25   -215       O  
ATOM    995  CB  LEU A 577      -3.289 -15.866 -19.685  1.00 33.69           C  
ANISOU  995  CB  LEU A 577     5234   3971   3596    226    141   -150       C  
ATOM    996  CG  LEU A 577      -2.233 -16.066 -18.591  1.00 34.04           C  
ANISOU  996  CG  LEU A 577     5422   3943   3568    290     55   -194       C  
ATOM    997  CD1 LEU A 577      -1.856 -14.734 -17.960  1.00 27.83           C  
ANISOU  997  CD1 LEU A 577     4612   3155   2808    293     62   -182       C  
ATOM    998  CD2 LEU A 577      -2.709 -17.050 -17.532  1.00 27.80           C  
ANISOU  998  CD2 LEU A 577     4846   3019   2698    283     73   -204       C  
ATOM    999  N   LYS A 578      -0.450 -15.060 -21.430  1.00 46.90           N  
ANISOU  999  N   LYS A 578     6613   5891   5315    338    -72   -218       N  
ATOM   1000  CA  LYS A 578       0.821 -15.598 -21.899  1.00 41.77           C  
ANISOU 1000  CA  LYS A 578     5926   5302   4641    404   -185   -284       C  
ATOM   1001  C   LYS A 578       1.959 -14.920 -21.143  1.00 43.46           C  
ANISOU 1001  C   LYS A 578     6170   5503   4841    455   -253   -320       C  
ATOM   1002  O   LYS A 578       1.745 -13.909 -20.475  1.00 48.11           O  
ANISOU 1002  O   LYS A 578     6774   6056   5449    433   -207   -286       O  
ATOM   1003  CB  LYS A 578       0.971 -15.410 -23.412  1.00 36.32           C  
ANISOU 1003  CB  LYS A 578     5040   4756   4003    383   -191   -279       C  
ATOM   1004  CG  LYS A 578       0.444 -14.086 -23.937  1.00 43.85           C  
ANISOU 1004  CG  LYS A 578     5859   5775   5029    321   -117   -213       C  
ATOM   1005  CD  LYS A 578       0.702 -13.939 -25.430  1.00 52.39           C  
ANISOU 1005  CD  LYS A 578     6759   6999   6150    300   -133   -211       C  
ATOM   1006  CE  LYS A 578       0.275 -12.564 -25.925  1.00 59.49           C  
ANISOU 1006  CE  LYS A 578     7532   7957   7117    241    -73   -144       C  
ATOM   1007  NZ  LYS A 578       0.840 -12.249 -27.270  1.00 61.36           N  
ANISOU 1007  NZ  LYS A 578     7599   8335   7380    225   -104   -147       N  
ATOM   1008  N   SER A 579       3.163 -15.474 -21.247  1.00 42.58           N  
ANISOU 1008  N   SER A 579     6061   5418   4699    524   -364   -394       N  
ATOM   1009  CA  SER A 579       4.289 -15.010 -20.436  1.00 44.37           C  
ANISOU 1009  CA  SER A 579     6335   5620   4905    583   -441   -443       C  
ATOM   1010  C   SER A 579       4.683 -13.556 -20.697  1.00 54.00           C  
ANISOU 1010  C   SER A 579     7418   6918   6183    560   -419   -423       C  
ATOM   1011  O   SER A 579       5.289 -12.914 -19.840  1.00 58.15           O  
ANISOU 1011  O   SER A 579     7990   7405   6700    591   -448   -442       O  
ATOM   1012  CB  SER A 579       5.505 -15.922 -20.615  1.00 46.83           C  
ANISOU 1012  CB  SER A 579     6659   5953   5181    663   -569   -537       C  
ATOM   1013  OG  SER A 579       6.105 -15.729 -21.883  1.00 56.40           O  
ANISOU 1013  OG  SER A 579     7686   7307   6438    660   -598   -566       O  
ATOM   1014  N   ASN A 580       4.345 -13.040 -21.875  1.00 48.06           N  
ANISOU 1014  N   ASN A 580     6499   6273   5489    507   -371   -384       N  
ATOM   1015  CA  ASN A 580       4.670 -11.654 -22.207  1.00 41.16           C  
ANISOU 1015  CA  ASN A 580     5494   5474   4672    477   -349   -358       C  
ATOM   1016  C   ASN A 580       3.594 -10.661 -21.772  1.00 45.61           C  
ANISOU 1016  C   ASN A 580     6066   5989   5276    416   -246   -275       C  
ATOM   1017  O   ASN A 580       3.787  -9.448 -21.860  1.00 43.63           O  
ANISOU 1017  O   ASN A 580     5728   5777   5073    392   -225   -249       O  
ATOM   1018  CB  ASN A 580       5.002 -11.495 -23.696  1.00 60.25           C  
ANISOU 1018  CB  ASN A 580     7728   8037   7129    450   -359   -361       C  
ATOM   1019  CG  ASN A 580       4.355 -12.560 -24.559  1.00 80.20           C  
ANISOU 1019  CG  ASN A 580    10234  10594   9646    431   -344   -355       C  
ATOM   1020  OD1 ASN A 580       4.876 -13.666 -24.699  1.00 87.65           O  
ANISOU 1020  OD1 ASN A 580    11213  11541  10550    479   -413   -420       O  
ATOM   1021  ND2 ASN A 580       3.219 -12.225 -25.155  1.00 88.15           N  
ANISOU 1021  ND2 ASN A 580    11178  11623  10693    362   -256   -279       N  
ATOM   1022  N   ASN A 581       2.464 -11.182 -21.304  1.00 42.76           N  
ANISOU 1022  N   ASN A 581     5809   5540   4896    390   -181   -240       N  
ATOM   1023  CA  ASN A 581       1.432 -10.349 -20.695  1.00 45.33           C  
ANISOU 1023  CA  ASN A 581     6164   5803   5255    338    -86   -177       C  
ATOM   1024  C   ASN A 581       1.472 -10.490 -19.177  1.00 49.25           C  
ANISOU 1024  C   ASN A 581     6842   6174   5699    367    -90   -198       C  
ATOM   1025  O   ASN A 581       0.509 -10.180 -18.476  1.00 46.96           O  
ANISOU 1025  O   ASN A 581     6621   5807   5415    326     -8   -160       O  
ATOM   1026  CB  ASN A 581       0.047 -10.684 -21.254  1.00 47.07           C  
ANISOU 1026  CB  ASN A 581     6360   6021   5503    276      2   -124       C  
ATOM   1027  CG  ASN A 581      -0.184 -10.088 -22.633  1.00 53.25           C  
ANISOU 1027  CG  ASN A 581     6957   6921   6353    232     24    -83       C  
ATOM   1028  OD1 ASN A 581       0.609  -9.278 -23.113  1.00 53.67           O  
ANISOU 1028  OD1 ASN A 581     6902   7054   6438    236    -13    -86       O  
ATOM   1029  ND2 ASN A 581      -1.278 -10.485 -23.273  1.00 61.81           N  
ANISOU 1029  ND2 ASN A 581     8008   8017   7462    186     85    -47       N  
ATOM   1030  N   ILE A 582       2.614 -10.969 -18.692  1.00 43.11           N  
ANISOU 1030  N   ILE A 582     6137   5377   4866    438   -187   -264       N  
ATOM   1031  CA  ILE A 582       2.896 -11.083 -17.270  1.00 27.88           C  
ANISOU 1031  CA  ILE A 582     4380   3336   2879    477   -213   -292       C  
ATOM   1032  C   ILE A 582       4.189 -10.331 -16.982  1.00 43.13           C  
ANISOU 1032  C   ILE A 582     6270   5300   4817    529   -291   -338       C  
ATOM   1033  O   ILE A 582       5.265 -10.752 -17.407  1.00 49.74           O  
ANISOU 1033  O   ILE A 582     7068   6192   5640    584   -386   -399       O  
ATOM   1034  CB  ILE A 582       3.077 -12.552 -16.856  1.00 39.62           C  
ANISOU 1034  CB  ILE A 582     6022   4750   4283    523   -275   -336       C  
ATOM   1035  CG1 ILE A 582       1.767 -13.322 -17.033  1.00 40.95           C  
ANISOU 1035  CG1 ILE A 582     6245   4875   4440    468   -193   -294       C  
ATOM   1036  CG2 ILE A 582       3.568 -12.647 -15.420  1.00 39.54           C  
ANISOU 1036  CG2 ILE A 582     6190   4630   4205    570   -323   -371       C  
ATOM   1037  CD1 ILE A 582       1.905 -14.814 -16.830  1.00 30.92           C  
ANISOU 1037  CD1 ILE A 582     5111   3543   3095    507   -253   -333       C  
ATOM   1038  N   PHE A 583       4.082  -9.214 -16.270  1.00 52.23           N  
ANISOU 1038  N   PHE A 583     7427   6420   5996    511   -249   -314       N  
ATOM   1039  CA  PHE A 583       5.238  -8.359 -16.018  1.00 57.81           C  
ANISOU 1039  CA  PHE A 583     8083   7163   6721    552   -311   -355       C  
ATOM   1040  C   PHE A 583       5.777  -8.540 -14.604  1.00 64.55           C  
ANISOU 1040  C   PHE A 583     9105   7913   7508    609   -364   -401       C  
ATOM   1041  O   PHE A 583       5.042  -8.408 -13.626  1.00 64.82           O  
ANISOU 1041  O   PHE A 583     9260   7853   7518    584   -305   -371       O  
ATOM   1042  CB  PHE A 583       4.874  -6.894 -16.270  1.00 62.02           C  
ANISOU 1042  CB  PHE A 583     8489   7740   7336    496   -238   -300       C  
ATOM   1043  CG  PHE A 583       4.099  -6.678 -17.539  1.00 70.19           C  
ANISOU 1043  CG  PHE A 583     9380   8856   8432    431   -175   -242       C  
ATOM   1044  CD1 PHE A 583       2.715  -6.603 -17.517  1.00 63.85           C  
ANISOU 1044  CD1 PHE A 583     8594   8011   7654    369    -76   -179       C  
ATOM   1045  CD2 PHE A 583       4.751  -6.573 -18.756  1.00 71.76           C  
ANISOU 1045  CD2 PHE A 583     9429   9174   8663    432   -216   -254       C  
ATOM   1046  CE1 PHE A 583       1.997  -6.416 -18.684  1.00 54.12           C  
ANISOU 1046  CE1 PHE A 583     7232   6851   6479    313    -25   -127       C  
ATOM   1047  CE2 PHE A 583       4.039  -6.385 -19.927  1.00 66.81           C  
ANISOU 1047  CE2 PHE A 583     8677   8620   8087    371   -163   -199       C  
ATOM   1048  CZ  PHE A 583       2.660  -6.307 -19.890  1.00 55.36           C  
ANISOU 1048  CZ  PHE A 583     7246   7124   6662    315    -71   -134       C  
ATOM   1049  N   LEU A 584       7.066  -8.852 -14.504  1.00 62.51           N  
ANISOU 1049  N   LEU A 584     8857   7674   7220    685   -477   -477       N  
ATOM   1050  CA  LEU A 584       7.716  -9.004 -13.209  1.00 60.66           C  
ANISOU 1050  CA  LEU A 584     8777   7347   6923    747   -545   -528       C  
ATOM   1051  C   LEU A 584       8.199  -7.661 -12.683  1.00 70.65           C  
ANISOU 1051  C   LEU A 584     9991   8623   8228    750   -537   -534       C  
ATOM   1052  O   LEU A 584       9.359  -7.292 -12.875  1.00 74.13           O  
ANISOU 1052  O   LEU A 584    10355   9123   8690    798   -614   -593       O  
ATOM   1053  CB  LEU A 584       8.892  -9.979 -13.299  1.00 66.22           C  
ANISOU 1053  CB  LEU A 584     9519   8060   7582    835   -680   -618       C  
ATOM   1054  CG  LEU A 584       8.551 -11.463 -13.427  1.00 79.53           C  
ANISOU 1054  CG  LEU A 584    11312   9698   9208    851   -713   -627       C  
ATOM   1055  CD1 LEU A 584       9.808 -12.315 -13.324  1.00 79.10           C  
ANISOU 1055  CD1 LEU A 584    11305   9637   9111    948   -860   -726       C  
ATOM   1056  CD2 LEU A 584       7.549 -11.865 -12.359  1.00 86.11           C  
ANISOU 1056  CD2 LEU A 584    12339  10400   9978    822   -654   -581       C  
ATOM   1057  N   HIS A 585       7.307  -6.931 -12.019  1.00 73.69           N  
ANISOU 1057  N   HIS A 585    10418   8953   8629    697   -443   -477       N  
ATOM   1058  CA  HIS A 585       7.657  -5.635 -11.450  1.00 73.41           C  
ANISOU 1058  CA  HIS A 585    10341   8918   8634    696   -428   -479       C  
ATOM   1059  C   HIS A 585       8.661  -5.779 -10.313  1.00 76.53           C  
ANISOU 1059  C   HIS A 585    10862   9249   8967    774   -522   -551       C  
ATOM   1060  O   HIS A 585       8.411  -6.487  -9.338  1.00 75.95           O  
ANISOU 1060  O   HIS A 585    10971   9072   8814    794   -536   -560       O  
ATOM   1061  CB  HIS A 585       6.414  -4.897 -10.954  1.00 66.75           C  
ANISOU 1061  CB  HIS A 585     9520   8023   7820    622   -306   -409       C  
ATOM   1062  CG  HIS A 585       6.724  -3.665 -10.164  1.00 58.24           C  
ANISOU 1062  CG  HIS A 585     8429   6925   6774    624   -293   -416       C  
ATOM   1063  ND1 HIS A 585       7.500  -2.641 -10.661  1.00 54.40           N  
ANISOU 1063  ND1 HIS A 585     7791   6520   6357    632   -318   -430       N  
ATOM   1064  CD2 HIS A 585       6.365  -3.293  -8.913  1.00 60.57           C  
ANISOU 1064  CD2 HIS A 585     8844   7130   7041    616   -256   -413       C  
ATOM   1065  CE1 HIS A 585       7.608  -1.691  -9.750  1.00 55.63           C  
ANISOU 1065  CE1 HIS A 585     7972   6635   6530    633   -298   -436       C  
ATOM   1066  NE2 HIS A 585       6.927  -2.062  -8.680  1.00 58.31           N  
ANISOU 1066  NE2 HIS A 585     8473   6871   6810    624   -261   -427       N  
ATOM   1067  N   GLU A 586       9.794  -5.096 -10.447  1.00 75.48           N  
ANISOU 1067  N   GLU A 586    10633   9176   8869    816   -586   -603       N  
ATOM   1068  CA  GLU A 586      10.874  -5.189  -9.474  1.00 83.25           C  
ANISOU 1068  CA  GLU A 586    11716  10112   9804    898   -688   -683       C  
ATOM   1069  C   GLU A 586      11.462  -6.599  -9.477  1.00 84.43           C  
ANISOU 1069  C   GLU A 586    11964  10234   9880    969   -797   -745       C  
ATOM   1070  O   GLU A 586      12.310  -6.934  -8.649  1.00 80.72           O  
ANISOU 1070  O   GLU A 586    11603   9709   9357   1045   -896   -814       O  
ATOM   1071  CB  GLU A 586      10.376  -4.810  -8.077  1.00107.05           C  
ANISOU 1071  CB  GLU A 586    14880  13016  12777    888   -646   -662       C  
ATOM   1072  CG  GLU A 586      11.471  -4.660  -7.035  1.00119.50           C  
ANISOU 1072  CG  GLU A 586    16545  14547  14311    968   -744   -739       C  
ATOM   1073  CD  GLU A 586      10.922  -4.279  -5.677  1.00126.14           C  
ANISOU 1073  CD  GLU A 586    17534  15283  15108    951   -695   -717       C  
ATOM   1074  OE1 GLU A 586       9.716  -3.968  -5.592  1.00126.77           O  
ANISOU 1074  OE1 GLU A 586    17624  15338  15205    872   -578   -644       O  
ATOM   1075  OE2 GLU A 586      11.695  -4.288  -4.696  1.00128.89           O  
ANISOU 1075  OE2 GLU A 586    17989  15578  15406   1015   -775   -776       O  
ATOM   1076  N   ASP A 587      11.002  -7.415 -10.422  1.00 99.83           N  
ANISOU 1076  N   ASP A 587    13876  12221  11832    944   -782   -721       N  
ATOM   1077  CA  ASP A 587      11.488  -8.782 -10.598  1.00 95.84           C  
ANISOU 1077  CA  ASP A 587    13446  11697  11270   1006   -882   -778       C  
ATOM   1078  C   ASP A 587      11.031  -9.714  -9.477  1.00 80.77           C  
ANISOU 1078  C   ASP A 587    11773   9651   9265   1026   -902   -771       C  
ATOM   1079  O   ASP A 587      11.506 -10.844  -9.367  1.00 79.22           O  
ANISOU 1079  O   ASP A 587    11674   9414   9011   1088  -1001   -823       O  
ATOM   1080  CB  ASP A 587      13.015  -8.810 -10.729  1.00 98.14           C  
ANISOU 1080  CB  ASP A 587    13679  12041  11570   1092  -1012   -885       C  
ATOM   1081  CG  ASP A 587      13.524  -7.915 -11.844  1.00 93.37           C  
ANISOU 1081  CG  ASP A 587    12846  11575  11054   1065   -992   -898       C  
ATOM   1082  OD1 ASP A 587      13.095  -6.745 -11.911  1.00 98.37           O  
ANISOU 1082  OD1 ASP A 587    13395  12238  11742   1004   -902   -840       O  
ATOM   1083  OD2 ASP A 587      14.359  -8.380 -12.648  1.00 85.34           O  
ANISOU 1083  OD2 ASP A 587    11737  10636  10053   1103  -1068   -968       O  
ATOM   1084  N   ASN A 588      10.106  -9.233  -8.653  1.00 68.40           N  
ANISOU 1084  N   ASN A 588    10297   8012   7680    972   -808   -708       N  
ATOM   1085  CA  ASN A 588       9.552 -10.032  -7.567  1.00 77.27           C  
ANISOU 1085  CA  ASN A 588    11648   9003   8708    973   -807   -693       C  
ATOM   1086  C   ASN A 588       8.050 -10.251  -7.713  1.00 66.34           C  
ANISOU 1086  C   ASN A 588    10297   7587   7320    879   -675   -608       C  
ATOM   1087  O   ASN A 588       7.560 -11.369  -7.570  1.00 64.37           O  
ANISOU 1087  O   ASN A 588    10179   7271   7007    873   -680   -597       O  
ATOM   1088  CB  ASN A 588       9.851  -9.383  -6.211  1.00104.02           C  
ANISOU 1088  CB  ASN A 588    15153  12315  12057    995   -821   -711       C  
ATOM   1089  CG  ASN A 588      11.318  -9.453  -5.836  1.00115.59           C  
ANISOU 1089  CG  ASN A 588    16638  13781  13501   1099   -969   -805       C  
ATOM   1090  OD1 ASN A 588      12.072 -10.266  -6.369  1.00128.57           O  
ANISOU 1090  OD1 ASN A 588    18263  15451  15136   1162  -1074   -863       O  
ATOM   1091  ND2 ASN A 588      11.729  -8.597  -4.907  1.00107.65           N  
ANISOU 1091  ND2 ASN A 588    15668  12745  12490   1120   -980   -826       N  
ATOM   1092  N   THR A 589       7.325  -9.176  -8.003  1.00 50.52           N  
ANISOU 1092  N   THR A 589     8173   5630   5390    806   -560   -553       N  
ATOM   1093  CA  THR A 589       5.870  -9.236  -8.076  1.00 44.62           C  
ANISOU 1093  CA  THR A 589     7448   4853   4651    716   -429   -479       C  
ATOM   1094  C   THR A 589       5.373  -9.447  -9.506  1.00 45.58           C  
ANISOU 1094  C   THR A 589     7412   5068   4838    676   -385   -445       C  
ATOM   1095  O   THR A 589       5.933  -8.902 -10.458  1.00 63.73           O  
ANISOU 1095  O   THR A 589     9535   7473   7208    687   -410   -456       O  
ATOM   1096  CB  THR A 589       5.223  -7.964  -7.487  1.00 56.47           C  
ANISOU 1096  CB  THR A 589     8921   6339   6196    656   -324   -440       C  
ATOM   1097  OG1 THR A 589       5.945  -7.554  -6.319  1.00 67.71           O  
ANISOU 1097  OG1 THR A 589    10446   7705   7575    703   -379   -482       O  
ATOM   1098  CG2 THR A 589       3.770  -8.222  -7.117  1.00 46.00           C  
ANISOU 1098  CG2 THR A 589     7685   4946   4849    572   -202   -385       C  
ATOM   1099  N   VAL A 590       4.317 -10.244  -9.644  1.00 41.21           N  
ANISOU 1099  N   VAL A 590     6926   4473   4258    625   -320   -407       N  
ATOM   1100  CA  VAL A 590       3.716 -10.530 -10.942  1.00 43.26           C  
ANISOU 1100  CA  VAL A 590     7053   4812   4573    584   -273   -373       C  
ATOM   1101  C   VAL A 590       2.583  -9.559 -11.262  1.00 44.87           C  
ANISOU 1101  C   VAL A 590     7148   5045   4855    497   -142   -308       C  
ATOM   1102  O   VAL A 590       1.690  -9.345 -10.443  1.00 38.86           O  
ANISOU 1102  O   VAL A 590     6481   4208   4078    447    -56   -280       O  
ATOM   1103  CB  VAL A 590       3.176 -11.975 -11.003  1.00 57.27           C  
ANISOU 1103  CB  VAL A 590     8951   6528   6282    577   -276   -371       C  
ATOM   1104  CG1 VAL A 590       2.093 -12.103 -12.067  1.00 60.37           C  
ANISOU 1104  CG1 VAL A 590     9230   6976   6731    507   -183   -320       C  
ATOM   1105  CG2 VAL A 590       4.307 -12.956 -11.261  1.00 56.17           C  
ANISOU 1105  CG2 VAL A 590     8845   6399   6098    663   -415   -435       C  
ATOM   1106  N   LYS A 591       2.626  -8.978 -12.457  1.00 46.37           N  
ANISOU 1106  N   LYS A 591     7143   5346   5131    479   -128   -287       N  
ATOM   1107  CA  LYS A 591       1.590  -8.050 -12.899  1.00 49.20           C  
ANISOU 1107  CA  LYS A 591     7383   5738   5571    403    -17   -227       C  
ATOM   1108  C   LYS A 591       0.960  -8.528 -14.202  1.00 48.22           C  
ANISOU 1108  C   LYS A 591     7150   5685   5488    366     16   -195       C  
ATOM   1109  O   LYS A 591       1.578  -8.454 -15.265  1.00 51.48           O  
ANISOU 1109  O   LYS A 591     7427   6197   5936    385    -34   -203       O  
ATOM   1110  CB  LYS A 591       2.169  -6.646 -13.083  1.00 46.01           C  
ANISOU 1110  CB  LYS A 591     6841   5399   5242    406    -25   -223       C  
ATOM   1111  CG  LYS A 591       2.820  -6.068 -11.835  1.00 37.31           C  
ANISOU 1111  CG  LYS A 591     5831   4235   4109    443    -57   -257       C  
ATOM   1112  CD  LYS A 591       1.812  -5.885 -10.711  1.00 33.66           C  
ANISOU 1112  CD  LYS A 591     5494   3670   3624    396     32   -235       C  
ATOM   1113  CE  LYS A 591       2.463  -5.272  -9.481  1.00 33.85           C  
ANISOU 1113  CE  LYS A 591     5606   3637   3617    432      1   -270       C  
ATOM   1114  NZ  LYS A 591       1.458  -4.868  -8.458  1.00 40.01           N  
ANISOU 1114  NZ  LYS A 591     6479   4332   4389    375    100   -249       N  
ATOM   1115  N   ILE A 592      -0.272  -9.021 -14.115  1.00 38.30           N  
ANISOU 1115  N   ILE A 592     5952   4378   4223    310    102   -163       N  
ATOM   1116  CA  ILE A 592      -0.985  -9.517 -15.286  1.00 39.64           C  
ANISOU 1116  CA  ILE A 592     6027   4606   4429    273    139   -134       C  
ATOM   1117  C   ILE A 592      -1.764  -8.401 -15.976  1.00 40.22           C  
ANISOU 1117  C   ILE A 592     5939   4738   4603    212    219    -82       C  
ATOM   1118  O   ILE A 592      -2.631  -7.772 -15.369  1.00 35.56           O  
ANISOU 1118  O   ILE A 592     5373   4095   4044    164    303    -58       O  
ATOM   1119  CB  ILE A 592      -1.962 -10.644 -14.910  1.00 44.30           C  
ANISOU 1119  CB  ILE A 592     6754   5113   4964    241    193   -130       C  
ATOM   1120  CG1 ILE A 592      -1.200 -11.853 -14.367  1.00 29.05           C  
ANISOU 1120  CG1 ILE A 592     4982   3123   2933    302    104   -179       C  
ATOM   1121  CG2 ILE A 592      -2.806 -11.042 -16.111  1.00 58.87           C  
ANISOU 1121  CG2 ILE A 592     8491   7021   6858    197    242   -100       C  
ATOM   1122  CD1 ILE A 592      -2.103 -12.954 -13.856  1.00 29.18           C  
ANISOU 1122  CD1 ILE A 592     5157   3045   2886    267    155   -175       C  
ATOM   1123  N   GLY A 593      -1.453  -8.161 -17.245  1.00 58.81           N  
ANISOU 1123  N   GLY A 593     8133   7203   7011    213    189    -67       N  
ATOM   1124  CA  GLY A 593      -2.113  -7.114 -18.003  1.00 59.77           C  
ANISOU 1124  CA  GLY A 593     8099   7383   7227    159    249    -14       C  
ATOM   1125  C   GLY A 593      -2.473  -7.529 -19.416  1.00 63.34           C  
ANISOU 1125  C   GLY A 593     8430   7923   7712    135    252     10       C  
ATOM   1126  O   GLY A 593      -2.231  -8.666 -19.822  1.00 69.03           O  
ANISOU 1126  O   GLY A 593     9183   8662   8383    160    212    -16       O  
ATOM   1127  N   ASP A 594      -3.062  -6.596 -20.158  1.00 49.21           N  
ANISOU 1127  N   ASP A 594     6504   6188   6007     88    297     60       N  
ATOM   1128  CA  ASP A 594      -3.430  -6.799 -21.559  1.00 34.54           C  
ANISOU 1128  CA  ASP A 594     4517   4421   4187     60    300     90       C  
ATOM   1129  C   ASP A 594      -4.695  -7.644 -21.715  1.00 30.31           C  
ANISOU 1129  C   ASP A 594     4020   3847   3650     23    369    101       C  
ATOM   1130  O   ASP A 594      -4.966  -8.184 -22.788  1.00 44.21           O  
ANISOU 1130  O   ASP A 594     5705   5673   5419     10    364    112       O  
ATOM   1131  CB  ASP A 594      -2.264  -7.398 -22.353  1.00 53.71           C  
ANISOU 1131  CB  ASP A 594     6897   6937   6574    103    209     56       C  
ATOM   1132  CG  ASP A 594      -2.298  -7.013 -23.820  1.00 76.59           C  
ANISOU 1132  CG  ASP A 594     9625   9951   9523     72    201     93       C  
ATOM   1133  OD1 ASP A 594      -3.341  -6.502 -24.280  1.00 83.04           O  
ANISOU 1133  OD1 ASP A 594    10373  10775  10403     19    263    145       O  
ATOM   1134  OD2 ASP A 594      -1.279  -7.218 -24.513  1.00 80.76           O  
ANISOU 1134  OD2 ASP A 594    10091  10565  10031     98    131     65       O  
ATOM   1135  N   PHE A 595      -5.468  -7.748 -20.638  1.00 47.08           N  
ANISOU 1135  N   PHE A 595     6260   5867   5760      4    435     95       N  
ATOM   1136  CA  PHE A 595      -6.761  -8.419 -20.684  1.00 55.10           C  
ANISOU 1136  CA  PHE A 595     7312   6840   6783    -41    514    102       C  
ATOM   1137  C   PHE A 595      -7.856  -7.422 -21.053  1.00 62.24           C  
ANISOU 1137  C   PHE A 595     8107   7755   7787    -98    587    144       C  
ATOM   1138  O   PHE A 595      -8.986  -7.807 -21.355  1.00 66.01           O  
ANISOU 1138  O   PHE A 595     8570   8218   8292   -140    652    152       O  
ATOM   1139  CB  PHE A 595      -7.075  -9.084 -19.339  1.00 48.76           C  
ANISOU 1139  CB  PHE A 595     6697   5919   5912    -42    553     68       C  
ATOM   1140  CG  PHE A 595      -6.995  -8.150 -18.162  1.00 47.87           C  
ANISOU 1140  CG  PHE A 595     6644   5739   5806    -46    578     64       C  
ATOM   1141  CD1 PHE A 595      -5.789  -7.927 -17.520  1.00 43.58           C  
ANISOU 1141  CD1 PHE A 595     6160   5184   5215      8    505     39       C  
ATOM   1142  CD2 PHE A 595      -8.127  -7.501 -17.696  1.00 52.64           C  
ANISOU 1142  CD2 PHE A 595     7244   6292   6466   -102    674     77       C  
ATOM   1143  CE1 PHE A 595      -5.711  -7.071 -16.438  1.00 38.05           C  
ANISOU 1143  CE1 PHE A 595     5514   4424   4521      5    528     33       C  
ATOM   1144  CE2 PHE A 595      -8.056  -6.643 -16.615  1.00 41.78           C  
ANISOU 1144  CE2 PHE A 595     5919   4857   5097   -107    699     68       C  
ATOM   1145  CZ  PHE A 595      -6.846  -6.428 -15.985  1.00 34.81           C  
ANISOU 1145  CZ  PHE A 595     5097   3965   4165    -54    626     48       C  
ATOM   1146  N   GLY A 596      -7.500  -6.140 -21.035  1.00 62.49           N  
ANISOU 1146  N   GLY A 596     8058   7810   7874    -98    572    168       N  
ATOM   1147  CA  GLY A 596      -8.440  -5.059 -21.282  1.00 61.37           C  
ANISOU 1147  CA  GLY A 596     7817   7670   7833   -146    630    205       C  
ATOM   1148  C   GLY A 596      -9.400  -5.313 -22.426  1.00 61.41           C  
ANISOU 1148  C   GLY A 596     7720   7724   7889   -183    660    233       C  
ATOM   1149  O   GLY A 596      -9.387  -4.598 -23.429  1.00 58.98           O  
ANISOU 1149  O   GLY A 596     7276   7491   7644   -195    634    274       O  
ATOM   1150  N   GLY A 615      -2.203 -14.091 -33.910  1.00 61.85           N  
ANISOU 1150  N   GLY A 615     7109   8853   7538     13     10    -31       N  
ATOM   1151  CA  GLY A 615      -1.047 -13.702 -33.124  1.00 67.49           C  
ANISOU 1151  CA  GLY A 615     7870   9544   8229     55    -41    -70       C  
ATOM   1152  C   GLY A 615      -0.407 -14.870 -32.397  1.00 70.90           C  
ANISOU 1152  C   GLY A 615     8416   9916   8608    123    -96   -152       C  
ATOM   1153  O   GLY A 615       0.113 -15.793 -33.023  1.00 68.78           O  
ANISOU 1153  O   GLY A 615     8112   9709   8310    146   -146   -212       O  
ATOM   1154  N   SER A 616      -0.443 -14.827 -31.068  1.00 97.53           N  
ANISOU 1154  N   SER A 616    11925  13166  11965    154    -90   -156       N  
ATOM   1155  CA  SER A 616       0.139 -15.884 -30.245  1.00 91.96           C  
ANISOU 1155  CA  SER A 616    11350  12386  11207    221   -147   -228       C  
ATOM   1156  C   SER A 616      -0.808 -17.075 -30.108  1.00 81.37           C  
ANISOU 1156  C   SER A 616    10097  10974   9846    220   -115   -230       C  
ATOM   1157  O   SER A 616      -1.874 -16.968 -29.501  1.00 75.49           O  
ANISOU 1157  O   SER A 616     9429  10139   9113    191    -41   -182       O  
ATOM   1158  CB  SER A 616       0.514 -15.344 -28.865  1.00 71.41           C  
ANISOU 1158  CB  SER A 616     8865   9679   8588    253   -157   -232       C  
ATOM   1159  OG  SER A 616      -0.591 -14.705 -28.251  1.00 67.33           O  
ANISOU 1159  OG  SER A 616     8400   9084   8101    211    -71   -162       O  
ATOM   1160  N   ILE A 617      -0.403 -18.210 -30.669  1.00 52.21           N  
ANISOU 1160  N   ILE A 617     6391   7321   6124    251   -169   -290       N  
ATOM   1161  CA  ILE A 617      -1.244 -19.400 -30.705  1.00 43.99           C  
ANISOU 1161  CA  ILE A 617     5420   6227   5068    248   -142   -296       C  
ATOM   1162  C   ILE A 617      -0.748 -20.490 -29.761  1.00 41.05           C  
ANISOU 1162  C   ILE A 617     5207   5750   4639    312   -205   -359       C  
ATOM   1163  O   ILE A 617      -1.396 -21.525 -29.606  1.00 35.83           O  
ANISOU 1163  O   ILE A 617     4631   5024   3958    313   -187   -367       O  
ATOM   1164  CB  ILE A 617      -1.297 -19.992 -32.124  1.00 50.80           C  
ANISOU 1164  CB  ILE A 617     6149   7209   5943    231   -155   -317       C  
ATOM   1165  CG1 ILE A 617       0.121 -20.181 -32.661  1.00 55.61           C  
ANISOU 1165  CG1 ILE A 617     6680   7915   6534    274   -253   -394       C  
ATOM   1166  CG2 ILE A 617      -2.093 -19.092 -33.052  1.00 45.53           C  
ANISOU 1166  CG2 ILE A 617     5346   6625   5327    160    -84   -244       C  
ATOM   1167  CD1 ILE A 617       0.213 -21.127 -33.831  1.00 69.30           C  
ANISOU 1167  CD1 ILE A 617     8321   9745   8265    274   -281   -441       C  
ATOM   1168  N   LEU A 618       0.403 -20.260 -29.139  1.00 42.50           N  
ANISOU 1168  N   LEU A 618     5432   5917   4798    366   -282   -406       N  
ATOM   1169  CA  LEU A 618       1.017 -21.269 -28.281  1.00 39.74           C  
ANISOU 1169  CA  LEU A 618     5233   5474   4395    436   -361   -472       C  
ATOM   1170  C   LEU A 618       0.240 -21.518 -26.988  1.00 36.54           C  
ANISOU 1170  C   LEU A 618     5018   4910   3956    430   -314   -437       C  
ATOM   1171  O   LEU A 618       0.355 -22.587 -26.388  1.00 43.49           O  
ANISOU 1171  O   LEU A 618     6038   5699   4789    471   -361   -476       O  
ATOM   1172  CB  LEU A 618       2.468 -20.900 -27.966  1.00 46.75           C  
ANISOU 1172  CB  LEU A 618     6107   6387   5268    497   -459   -536       C  
ATOM   1173  CG  LEU A 618       3.451 -21.036 -29.128  1.00 40.24           C  
ANISOU 1173  CG  LEU A 618     5123   5705   4460    516   -528   -604       C  
ATOM   1174  CD1 LEU A 618       4.848 -20.604 -28.714  1.00 34.30           C  
ANISOU 1174  CD1 LEU A 618     4363   4972   3698    573   -618   -672       C  
ATOM   1175  CD2 LEU A 618       3.467 -22.467 -29.634  1.00 50.02           C  
ANISOU 1175  CD2 LEU A 618     6375   6949   5680    545   -577   -663       C  
ATOM   1176  N   TRP A 619      -0.550 -20.535 -26.566  1.00 46.12           N  
ANISOU 1176  N   TRP A 619     6237   6091   5194    378   -224   -366       N  
ATOM   1177  CA  TRP A 619      -1.299 -20.641 -25.315  1.00 51.24           C  
ANISOU 1177  CA  TRP A 619     7060   6596   5811    362   -169   -334       C  
ATOM   1178  C   TRP A 619      -2.778 -20.939 -25.543  1.00 46.37           C  
ANISOU 1178  C   TRP A 619     6452   5950   5216    294    -60   -284       C  
ATOM   1179  O   TRP A 619      -3.565 -20.982 -24.595  1.00 34.12           O  
ANISOU 1179  O   TRP A 619     5032   4288   3645    265      5   -257       O  
ATOM   1180  CB  TRP A 619      -1.150 -19.359 -24.493  1.00 55.29           C  
ANISOU 1180  CB  TRP A 619     7592   7078   6336    353   -142   -301       C  
ATOM   1181  CG  TRP A 619       0.255 -19.088 -24.055  1.00 58.89           C  
ANISOU 1181  CG  TRP A 619     8066   7543   6767    421   -245   -355       C  
ATOM   1182  CD1 TRP A 619       0.819 -19.423 -22.859  1.00 52.95           C  
ANISOU 1182  CD1 TRP A 619     7478   6684   5957    473   -304   -390       C  
ATOM   1183  CD2 TRP A 619       1.278 -18.426 -24.810  1.00 58.50           C  
ANISOU 1183  CD2 TRP A 619     7864   7615   6750    442   -302   -383       C  
ATOM   1184  NE1 TRP A 619       2.128 -19.012 -22.822  1.00 52.52           N  
ANISOU 1184  NE1 TRP A 619     7378   6677   5901    530   -396   -442       N  
ATOM   1185  CE2 TRP A 619       2.435 -18.397 -24.007  1.00 61.87           C  
ANISOU 1185  CE2 TRP A 619     8366   8001   7140    510   -394   -440       C  
ATOM   1186  CE3 TRP A 619       1.328 -17.856 -26.085  1.00 55.82           C  
ANISOU 1186  CE3 TRP A 619     7334   7412   6463    407   -285   -366       C  
ATOM   1187  CZ2 TRP A 619       3.629 -17.819 -24.438  1.00 60.15           C  
ANISOU 1187  CZ2 TRP A 619     8034   7878   6942    543   -463   -487       C  
ATOM   1188  CZ3 TRP A 619       2.513 -17.283 -26.510  1.00 53.07           C  
ANISOU 1188  CZ3 TRP A 619     6879   7157   6128    435   -352   -408       C  
ATOM   1189  CH2 TRP A 619       3.647 -17.269 -25.689  1.00 47.30           C  
ANISOU 1189  CH2 TRP A 619     6222   6386   5365    502   -438   -470       C  
ATOM   1190  N   MET A 620      -3.145 -21.154 -26.803  1.00 50.82           N  
ANISOU 1190  N   MET A 620     6875   6614   5818    268    -41   -278       N  
ATOM   1191  CA  MET A 620      -4.543 -21.333 -27.187  1.00 51.67           C  
ANISOU 1191  CA  MET A 620     6960   6713   5959    203     61   -234       C  
ATOM   1192  C   MET A 620      -5.048 -22.763 -27.008  1.00 59.18           C  
ANISOU 1192  C   MET A 620     8027   7588   6870    206     66   -262       C  
ATOM   1193  O   MET A 620      -4.462 -23.712 -27.529  1.00 56.36           O  
ANISOU 1193  O   MET A 620     7657   7264   6492    247     -8   -313       O  
ATOM   1194  CB  MET A 620      -4.756 -20.883 -28.635  1.00 38.33           C  
ANISOU 1194  CB  MET A 620     5069   5166   4329    170     78   -212       C  
ATOM   1195  CG  MET A 620      -4.622 -19.384 -28.837  1.00 37.02           C  
ANISOU 1195  CG  MET A 620     4793   5063   4211    145     99   -166       C  
ATOM   1196  SD  MET A 620      -4.761 -18.895 -30.563  1.00 59.10           S  
ANISOU 1196  SD  MET A 620     7365   8026   7064    106    106   -140       S  
ATOM   1197  CE  MET A 620      -6.214 -19.814 -31.057  1.00 57.26           C  
ANISOU 1197  CE  MET A 620     7135   7772   6851     62    183   -125       C  
ATOM   1198  N   ALA A 621      -6.149 -22.903 -26.275  1.00 62.89           N  
ANISOU 1198  N   ALA A 621     8607   7956   7334    159    156   -232       N  
ATOM   1199  CA  ALA A 621      -6.785 -24.198 -26.073  1.00 54.69           C  
ANISOU 1199  CA  ALA A 621     7683   6838   6261    148    179   -251       C  
ATOM   1200  C   ALA A 621      -7.319 -24.747 -27.389  1.00 54.88           C  
ANISOU 1200  C   ALA A 621     7574   6953   6326    125    199   -256       C  
ATOM   1201  O   ALA A 621      -7.687 -23.984 -28.281  1.00 51.93           O  
ANISOU 1201  O   ALA A 621     7039   6680   6013     93    238   -225       O  
ATOM   1202  CB  ALA A 621      -7.905 -24.084 -25.056  1.00 36.46           C  
ANISOU 1202  CB  ALA A 621     5503   4411   3940     89    285   -218       C  
ATOM   1203  N   PRO A 622      -7.366 -26.082 -27.508  1.00 45.25           N  
ANISOU 1203  N   PRO A 622     6425   5695   5073    142    170   -296       N  
ATOM   1204  CA  PRO A 622      -7.840 -26.744 -28.726  1.00 44.84           C  
ANISOU 1204  CA  PRO A 622     6258   5725   5055    125    184   -309       C  
ATOM   1205  C   PRO A 622      -9.192 -26.211 -29.182  1.00 51.61           C  
ANISOU 1205  C   PRO A 622     7026   6611   5973     50    303   -261       C  
ATOM   1206  O   PRO A 622      -9.358 -25.931 -30.368  1.00 39.01           O  
ANISOU 1206  O   PRO A 622     5261   5133   4426     36    309   -252       O  
ATOM   1207  CB  PRO A 622      -7.969 -28.205 -28.295  1.00 40.55           C  
ANISOU 1207  CB  PRO A 622     5866   5080   4460    142    162   -348       C  
ATOM   1208  CG  PRO A 622      -6.953 -28.358 -27.226  1.00 33.28           C  
ANISOU 1208  CG  PRO A 622     5095   4072   3476    199     76   -374       C  
ATOM   1209  CD  PRO A 622      -6.935 -27.053 -26.487  1.00 31.27           C  
ANISOU 1209  CD  PRO A 622     4855   3799   3229    182    115   -331       C  
ATOM   1210  N   GLU A 623     -10.136 -26.070 -28.255  1.00 53.67           N  
ANISOU 1210  N   GLU A 623     7400   6765   6229      2    394   -234       N  
ATOM   1211  CA  GLU A 623     -11.468 -25.572 -28.590  1.00 51.80           C  
ANISOU 1211  CA  GLU A 623     7086   6544   6054    -69    508   -199       C  
ATOM   1212  C   GLU A 623     -11.422 -24.123 -29.071  1.00 51.98           C  
ANISOU 1212  C   GLU A 623     6956   6658   6137    -81    520   -157       C  
ATOM   1213  O   GLU A 623     -12.323 -23.662 -29.772  1.00 51.12           O  
ANISOU 1213  O   GLU A 623     6729   6603   6091   -126    584   -131       O  
ATOM   1214  CB  GLU A 623     -12.422 -25.709 -27.398  1.00 39.66           C  
ANISOU 1214  CB  GLU A 623     5706   4868   4495   -120    604   -190       C  
ATOM   1215  CG  GLU A 623     -12.150 -24.749 -26.249  1.00 47.39           C  
ANISOU 1215  CG  GLU A 623     6771   5782   5455   -121    616   -167       C  
ATOM   1216  CD  GLU A 623     -11.109 -25.268 -25.276  1.00 43.38           C  
ANISOU 1216  CD  GLU A 623     6431   5190   4861    -68    533   -192       C  
ATOM   1217  OE1 GLU A 623     -10.479 -26.305 -25.568  1.00 45.67           O  
ANISOU 1217  OE1 GLU A 623     6758   5483   5113    -22    453   -228       O  
ATOM   1218  OE2 GLU A 623     -10.923 -24.637 -24.215  1.00 39.75           O  
ANISOU 1218  OE2 GLU A 623     6067   4661   4374    -70    545   -178       O  
ATOM   1219  N   VAL A 624     -10.366 -23.412 -28.690  1.00 51.85           N  
ANISOU 1219  N   VAL A 624     6945   6655   6101    -41    454   -152       N  
ATOM   1220  CA  VAL A 624     -10.171 -22.031 -29.118  1.00 50.63           C  
ANISOU 1220  CA  VAL A 624     6655   6585   5999    -50    454   -112       C  
ATOM   1221  C   VAL A 624      -9.639 -21.968 -30.547  1.00 60.59           C  
ANISOU 1221  C   VAL A 624     7743   7993   7287    -33    395   -116       C  
ATOM   1222  O   VAL A 624     -10.037 -21.105 -31.329  1.00 71.58           O  
ANISOU 1222  O   VAL A 624     8996   9466   8736    -66    423    -78       O  
ATOM   1223  CB  VAL A 624      -9.204 -21.281 -28.181  1.00 34.70           C  
ANISOU 1223  CB  VAL A 624     4705   4528   3950    -15    407   -110       C  
ATOM   1224  CG1 VAL A 624      -8.801 -19.945 -28.784  1.00 34.78           C  
ANISOU 1224  CG1 VAL A 624     4565   4639   4012    -18    389    -74       C  
ATOM   1225  CG2 VAL A 624      -9.837 -21.084 -26.819  1.00 36.09           C  
ANISOU 1225  CG2 VAL A 624     5032   4571   4108    -44    478    -97       C  
ATOM   1226  N   ILE A 625      -8.741 -22.889 -30.884  1.00 60.96           N  
ANISOU 1226  N   ILE A 625     7800   8071   7290     15    311   -165       N  
ATOM   1227  CA  ILE A 625      -8.150 -22.936 -32.219  1.00 50.51           C  
ANISOU 1227  CA  ILE A 625     6318   6889   5983     30    253   -181       C  
ATOM   1228  C   ILE A 625      -9.190 -23.233 -33.300  1.00 69.18           C  
ANISOU 1228  C   ILE A 625     8575   9318   8392    -15    308   -166       C  
ATOM   1229  O   ILE A 625      -9.309 -22.493 -34.279  1.00 82.27           O  
ANISOU 1229  O   ILE A 625    10083  11083  10092    -41    314   -135       O  
ATOM   1230  CB  ILE A 625      -7.000 -23.961 -32.298  1.00 35.84           C  
ANISOU 1230  CB  ILE A 625     4499   5045   4072     94    151   -250       C  
ATOM   1231  CG1 ILE A 625      -5.772 -23.441 -31.544  1.00 22.96           C  
ANISOU 1231  CG1 ILE A 625     2923   3393   2408    143     78   -269       C  
ATOM   1232  CG2 ILE A 625      -6.642 -24.248 -33.744  1.00 39.95           C  
ANISOU 1232  CG2 ILE A 625     4859   5710   4610     97    108   -275       C  
ATOM   1233  CD1 ILE A 625      -4.551 -24.339 -31.643  1.00 24.11           C  
ANISOU 1233  CD1 ILE A 625     3092   3558   2510    210    -33   -346       C  
ATOM   1234  N   ARG A 626      -9.939 -24.317 -33.121  1.00 66.80           N  
ANISOU 1234  N   ARG A 626     8353   8949   8079    -26    347   -188       N  
ATOM   1235  CA  ARG A 626     -11.009 -24.671 -34.049  1.00 68.44           C  
ANISOU 1235  CA  ARG A 626     8470   9205   8330    -68    405   -180       C  
ATOM   1236  C   ARG A 626     -12.251 -23.812 -33.825  1.00 67.25           C  
ANISOU 1236  C   ARG A 626     8298   9018   8235   -127    505   -129       C  
ATOM   1237  O   ARG A 626     -12.429 -22.778 -34.468  1.00 65.87           O  
ANISOU 1237  O   ARG A 626     7996   8922   8108   -150    515    -88       O  
ATOM   1238  CB  ARG A 626     -11.359 -26.159 -33.932  1.00 64.43           C  
ANISOU 1238  CB  ARG A 626     8053   8635   7791    -60    411   -228       C  
ATOM   1239  CG  ARG A 626     -11.218 -26.728 -32.528  1.00 60.34           C  
ANISOU 1239  CG  ARG A 626     7739   7969   7219    -42    412   -247       C  
ATOM   1240  CD  ARG A 626     -11.646 -28.188 -32.478  1.00 50.81           C  
ANISOU 1240  CD  ARG A 626     6622   6698   5986    -42    422   -289       C  
ATOM   1241  NE  ARG A 626     -11.251 -28.837 -31.230  1.00 59.38           N  
ANISOU 1241  NE  ARG A 626     7907   7649   7006    -16    395   -312       N  
ATOM   1242  CZ  ARG A 626     -11.985 -28.850 -30.121  1.00 54.61           C  
ANISOU 1242  CZ  ARG A 626     7449   6917   6382    -54    470   -294       C  
ATOM   1243  NH1 ARG A 626     -13.164 -28.241 -30.090  1.00 61.73           N  
ANISOU 1243  NH1 ARG A 626     8313   7810   7332   -119    580   -260       N  
ATOM   1244  NH2 ARG A 626     -11.538 -29.471 -29.038  1.00 51.35           N  
ANISOU 1244  NH2 ARG A 626     7223   6386   5901    -28    434   -314       N  
ATOM   1245  N   ASN A 631     -19.380 -20.852 -27.145  1.00103.54           N  
ANISOU 1245  N   ASN A 631    13410  12920  13011   -480   1204    -87       N  
ATOM   1246  CA  ASN A 631     -18.563 -20.280 -26.081  1.00104.19           C  
ANISOU 1246  CA  ASN A 631    13595  12948  13045   -458   1176    -73       C  
ATOM   1247  C   ASN A 631     -17.101 -20.715 -26.159  1.00 98.42           C  
ANISOU 1247  C   ASN A 631    12912  12245  12239   -388   1059    -66       C  
ATOM   1248  O   ASN A 631     -16.600 -21.382 -25.254  1.00 99.10           O  
ANISOU 1248  O   ASN A 631    13161  12249  12242   -374   1041    -84       O  
ATOM   1249  CB  ASN A 631     -19.157 -20.629 -24.712  1.00114.71           C  
ANISOU 1249  CB  ASN A 631    15101  14149  14333   -508   1265   -103       C  
ATOM   1250  CG  ASN A 631     -20.464 -19.907 -24.443  1.00121.88           C  
ANISOU 1250  CG  ASN A 631    15959  15028  15322   -576   1378   -117       C  
ATOM   1251  OD1 ASN A 631     -20.731 -18.851 -25.018  1.00128.92           O  
ANISOU 1251  OD1 ASN A 631    16700  15983  16299   -576   1376    -95       O  
ATOM   1252  ND2 ASN A 631     -21.284 -20.471 -23.563  1.00119.18           N  
ANISOU 1252  ND2 ASN A 631    15743  14588  14952   -637   1477   -156       N  
ATOM   1253  N   PRO A 632     -16.411 -20.337 -27.249  1.00 84.27           N  
ANISOU 1253  N   PRO A 632    10977  10569  10474   -346    977    -42       N  
ATOM   1254  CA  PRO A 632     -15.006 -20.711 -27.449  1.00 77.65           C  
ANISOU 1254  CA  PRO A 632    10158   9771   9573   -280    864    -46       C  
ATOM   1255  C   PRO A 632     -14.096 -20.186 -26.341  1.00 75.05           C  
ANISOU 1255  C   PRO A 632     9937   9384   9195   -250    825    -41       C  
ATOM   1256  O   PRO A 632     -13.291 -20.947 -25.806  1.00 73.42           O  
ANISOU 1256  O   PRO A 632     9854   9130   8911   -210    767    -65       O  
ATOM   1257  CB  PRO A 632     -14.655 -20.050 -28.785  1.00 73.11           C  
ANISOU 1257  CB  PRO A 632     9391   9334   9054   -262    809    -18       C  
ATOM   1258  CG  PRO A 632     -15.963 -19.879 -29.481  1.00 75.16           C  
ANISOU 1258  CG  PRO A 632     9545   9622   9390   -313    885     -8       C  
ATOM   1259  CD  PRO A 632     -16.945 -19.575 -28.391  1.00 77.75           C  
ANISOU 1259  CD  PRO A 632     9962   9841   9738   -363    986    -16       C  
ATOM   1260  N   TYR A 633     -14.221 -18.905 -26.006  1.00 68.21           N  
ANISOU 1260  N   TYR A 633     9023   8518   8375   -265    851    -12       N  
ATOM   1261  CA  TYR A 633     -13.415 -18.314 -24.939  1.00 48.37           C  
ANISOU 1261  CA  TYR A 633     6606   5952   5822   -239    820     -9       C  
ATOM   1262  C   TYR A 633     -14.083 -18.445 -23.574  1.00 47.74           C  
ANISOU 1262  C   TYR A 633     6687   5741   5709   -280    903    -25       C  
ATOM   1263  O   TYR A 633     -15.183 -17.936 -23.357  1.00 56.10           O  
ANISOU 1263  O   TYR A 633     7720   6772   6824   -338    998    -21       O  
ATOM   1264  CB  TYR A 633     -13.102 -16.848 -25.237  1.00 44.15           C  
ANISOU 1264  CB  TYR A 633     5942   5483   5351   -233    799     29       C  
ATOM   1265  CG  TYR A 633     -11.956 -16.666 -26.205  1.00 42.61           C  
ANISOU 1265  CG  TYR A 633     5638   5399   5154   -183    696     39       C  
ATOM   1266  CD1 TYR A 633     -12.178 -16.217 -27.499  1.00 47.88           C  
ANISOU 1266  CD1 TYR A 633     6132   6176   5885   -195    686     67       C  
ATOM   1267  CD2 TYR A 633     -10.654 -16.955 -25.825  1.00 40.83           C  
ANISOU 1267  CD2 TYR A 633     5483   5170   4861   -125    608     18       C  
ATOM   1268  CE1 TYR A 633     -11.132 -16.052 -28.386  1.00 40.52           C  
ANISOU 1268  CE1 TYR A 633     5102   5349   4946   -158    597     74       C  
ATOM   1269  CE2 TYR A 633      -9.602 -16.796 -26.702  1.00 45.91           C  
ANISOU 1269  CE2 TYR A 633     6022   5919   5503    -84    518     18       C  
ATOM   1270  CZ  TYR A 633      -9.846 -16.344 -27.982  1.00 46.02           C  
ANISOU 1270  CZ  TYR A 633     5866   6042   5577   -104    517     46       C  
ATOM   1271  OH  TYR A 633      -8.799 -16.183 -28.860  1.00 54.92           O  
ANISOU 1271  OH  TYR A 633     6892   7278   6699    -72    434     43       O  
ATOM   1272  N   SER A 634     -13.404 -19.121 -22.653  1.00 42.82           N  
ANISOU 1272  N   SER A 634     6233   5041   4996   -252    864    -47       N  
ATOM   1273  CA  SER A 634     -13.977 -19.426 -21.348  1.00 50.22           C  
ANISOU 1273  CA  SER A 634     7346   5851   5883   -295    939    -64       C  
ATOM   1274  C   SER A 634     -12.940 -19.341 -20.236  1.00 49.12           C  
ANISOU 1274  C   SER A 634     7353   5646   5664   -253    877    -71       C  
ATOM   1275  O   SER A 634     -11.756 -19.121 -20.489  1.00 68.04           O  
ANISOU 1275  O   SER A 634     9713   8094   8045   -186    773    -68       O  
ATOM   1276  CB  SER A 634     -14.581 -20.830 -21.362  1.00 54.07           C  
ANISOU 1276  CB  SER A 634     7933   6285   6327   -323    976    -91       C  
ATOM   1277  OG  SER A 634     -13.578 -21.805 -21.590  1.00 60.61           O  
ANISOU 1277  OG  SER A 634     8820   7119   7089   -261    871   -107       O  
ATOM   1278  N   PHE A 635     -13.396 -19.522 -19.002  1.00 44.60           N  
ANISOU 1278  N   PHE A 635     6947   4960   5039   -294    942    -84       N  
ATOM   1279  CA  PHE A 635     -12.496 -19.591 -17.863  1.00 49.86           C  
ANISOU 1279  CA  PHE A 635     7777   5549   5617   -258    885    -93       C  
ATOM   1280  C   PHE A 635     -11.558 -20.777 -18.049  1.00 46.27           C  
ANISOU 1280  C   PHE A 635     7408   5085   5089   -195    776   -112       C  
ATOM   1281  O   PHE A 635     -10.402 -20.743 -17.629  1.00 44.23           O  
ANISOU 1281  O   PHE A 635     7211   4814   4779   -130    677   -121       O  
ATOM   1282  CB  PHE A 635     -13.290 -19.751 -16.562  1.00 65.09           C  
ANISOU 1282  CB  PHE A 635     9881   7356   7494   -326    983   -106       C  
ATOM   1283  CG  PHE A 635     -14.275 -18.641 -16.303  1.00 77.01           C  
ANISOU 1283  CG  PHE A 635    11313   8867   9079   -392   1095   -100       C  
ATOM   1284  CD1 PHE A 635     -15.577 -18.723 -16.772  1.00 83.10           C  
ANISOU 1284  CD1 PHE A 635    12009   9650   9916   -461   1202   -107       C  
ATOM   1285  CD2 PHE A 635     -13.902 -17.522 -15.581  1.00 77.15           C  
ANISOU 1285  CD2 PHE A 635    11334   8874   9107   -383   1092    -92       C  
ATOM   1286  CE1 PHE A 635     -16.483 -17.704 -16.528  1.00 80.91           C  
ANISOU 1286  CE1 PHE A 635    11656   9372   9714   -518   1299   -110       C  
ATOM   1287  CE2 PHE A 635     -14.801 -16.501 -15.334  1.00 72.87           C  
ANISOU 1287  CE2 PHE A 635    10717   8331   8638   -441   1191    -92       C  
ATOM   1288  CZ  PHE A 635     -16.093 -16.593 -15.808  1.00 75.83           C  
ANISOU 1288  CZ  PHE A 635    11015   8716   9081   -508   1293   -103       C  
ATOM   1289  N   GLN A 636     -12.068 -21.821 -18.697  1.00 53.08           N  
ANISOU 1289  N   GLN A 636     8265   5953   5949   -212    792   -124       N  
ATOM   1290  CA  GLN A 636     -11.321 -23.058 -18.907  1.00 58.63           C  
ANISOU 1290  CA  GLN A 636     9049   6639   6588   -157    695   -147       C  
ATOM   1291  C   GLN A 636     -10.234 -22.915 -19.972  1.00 57.76           C  
ANISOU 1291  C   GLN A 636     8789   6647   6511    -80    580   -153       C  
ATOM   1292  O   GLN A 636      -9.208 -23.595 -19.917  1.00 47.43           O  
ANISOU 1292  O   GLN A 636     7547   5326   5148    -14    470   -179       O  
ATOM   1293  CB  GLN A 636     -12.272 -24.197 -19.282  1.00 64.55           C  
ANISOU 1293  CB  GLN A 636     9835   7359   7333   -205    756   -160       C  
ATOM   1294  CG  GLN A 636     -13.417 -24.403 -18.302  1.00 76.48           C  
ANISOU 1294  CG  GLN A 636    11488   8758   8813   -293    881   -161       C  
ATOM   1295  CD  GLN A 636     -14.753 -23.941 -18.854  1.00 83.43           C  
ANISOU 1295  CD  GLN A 636    12235   9682   9783   -368   1007   -155       C  
ATOM   1296  OE1 GLN A 636     -15.378 -24.633 -19.658  1.00 88.66           O  
ANISOU 1296  OE1 GLN A 636    12837  10374  10476   -391   1039   -166       O  
ATOM   1297  NE2 GLN A 636     -15.201 -22.768 -18.419  1.00 80.04           N  
ANISOU 1297  NE2 GLN A 636    11758   9255   9398   -406   1077   -143       N  
ATOM   1298  N   SER A 637     -10.464 -22.039 -20.946  1.00 68.94           N  
ANISOU 1298  N   SER A 637    10003   8174   8015    -91    604   -131       N  
ATOM   1299  CA  SER A 637      -9.457 -21.757 -21.963  1.00 55.83           C  
ANISOU 1299  CA  SER A 637     8193   6634   6387    -30    505   -135       C  
ATOM   1300  C   SER A 637      -8.365 -20.874 -21.370  1.00 59.06           C  
ANISOU 1300  C   SER A 637     8615   7046   6779     19    437   -135       C  
ATOM   1301  O   SER A 637      -7.214 -20.914 -21.808  1.00 66.70           O  
ANISOU 1301  O   SER A 637     9529   8076   7738     83    331   -156       O  
ATOM   1302  CB  SER A 637     -10.083 -21.087 -23.186  1.00 37.60           C  
ANISOU 1302  CB  SER A 637     5674   4439   4172    -63    553   -108       C  
ATOM   1303  OG  SER A 637     -10.620 -19.823 -22.855  1.00 52.89           O  
ANISOU 1303  OG  SER A 637     7559   6375   6162   -104    624    -75       O  
ATOM   1304  N   ASP A 638      -8.738 -20.076 -20.372  1.00 47.22           N  
ANISOU 1304  N   ASP A 638     7184   5480   5278    -14    499   -116       N  
ATOM   1305  CA  ASP A 638      -7.775 -19.302 -19.597  1.00 37.03           C  
ANISOU 1305  CA  ASP A 638     5936   4172   3964     28    441   -119       C  
ATOM   1306  C   ASP A 638      -6.906 -20.247 -18.778  1.00 35.00           C  
ANISOU 1306  C   ASP A 638     5861   3829   3608     84    352   -156       C  
ATOM   1307  O   ASP A 638      -5.706 -20.024 -18.619  1.00 37.77           O  
ANISOU 1307  O   ASP A 638     6214   4200   3936    151    251   -178       O  
ATOM   1308  CB  ASP A 638      -8.494 -18.320 -18.667  1.00 46.57           C  
ANISOU 1308  CB  ASP A 638     7184   5319   5190    -26    536    -95       C  
ATOM   1309  CG  ASP A 638      -8.617 -16.927 -19.260  1.00 45.72           C  
ANISOU 1309  CG  ASP A 638     6892   5302   5177    -42    564    -63       C  
ATOM   1310  OD1 ASP A 638      -7.840 -16.593 -20.177  1.00 50.80           O  
ANISOU 1310  OD1 ASP A 638     7400   6047   5854     -1    491    -60       O  
ATOM   1311  OD2 ASP A 638      -9.487 -16.160 -18.797  1.00 43.64           O  
ANISOU 1311  OD2 ASP A 638     6622   5006   4955    -97    657    -44       O  
ATOM   1312  N   VAL A 639      -7.527 -21.303 -18.259  1.00 36.38           N  
ANISOU 1312  N   VAL A 639     6190   3907   3725     54    388   -165       N  
ATOM   1313  CA  VAL A 639      -6.820 -22.314 -17.479  1.00 40.95           C  
ANISOU 1313  CA  VAL A 639     6960   4391   4207    102    303   -198       C  
ATOM   1314  C   VAL A 639      -5.757 -23.011 -18.324  1.00 48.70           C  
ANISOU 1314  C   VAL A 639     7880   5439   5185    181    175   -235       C  
ATOM   1315  O   VAL A 639      -4.650 -23.276 -17.852  1.00 53.42           O  
ANISOU 1315  O   VAL A 639     8562   6005   5732    252     63   -268       O  
ATOM   1316  CB  VAL A 639      -7.789 -23.365 -16.902  1.00 49.22           C  
ANISOU 1316  CB  VAL A 639     8179   5326   5198     45    374   -197       C  
ATOM   1317  CG1 VAL A 639      -7.024 -24.444 -16.156  1.00 59.31           C  
ANISOU 1317  CG1 VAL A 639     9659   6503   6375     97    272   -227       C  
ATOM   1318  CG2 VAL A 639      -8.803 -22.705 -15.983  1.00 44.49           C  
ANISOU 1318  CG2 VAL A 639     7650   4659   4597    -37    502   -171       C  
ATOM   1319  N   TYR A 640      -6.100 -23.306 -19.575  1.00 44.36           N  
ANISOU 1319  N   TYR A 640     7181   4981   4692    169    190   -234       N  
ATOM   1320  CA  TYR A 640      -5.158 -23.916 -20.506  1.00 48.57           C  
ANISOU 1320  CA  TYR A 640     7629   5593   5231    237     78   -274       C  
ATOM   1321  C   TYR A 640      -3.960 -23.002 -20.741  1.00 46.66           C  
ANISOU 1321  C   TYR A 640     7277   5438   5016    295     -5   -291       C  
ATOM   1322  O   TYR A 640      -2.811 -23.441 -20.697  1.00 43.20           O  
ANISOU 1322  O   TYR A 640     6867   5003   4544    369   -124   -340       O  
ATOM   1323  CB  TYR A 640      -5.841 -24.230 -21.837  1.00 55.55           C  
ANISOU 1323  CB  TYR A 640     8357   6573   6178    203    125   -266       C  
ATOM   1324  CG  TYR A 640      -4.929 -24.902 -22.839  1.00 62.96           C  
ANISOU 1324  CG  TYR A 640     9202   7597   7123    265     17   -314       C  
ATOM   1325  CD1 TYR A 640      -4.880 -26.285 -22.943  1.00 61.95           C  
ANISOU 1325  CD1 TYR A 640     9161   7422   6955    289    -31   -351       C  
ATOM   1326  CD2 TYR A 640      -4.110 -24.153 -23.674  1.00 67.30           C  
ANISOU 1326  CD2 TYR A 640     9577   8276   7719    297    -37   -324       C  
ATOM   1327  CE1 TYR A 640      -4.046 -26.905 -23.855  1.00 61.14           C  
ANISOU 1327  CE1 TYR A 640     8968   7400   6863    346   -130   -402       C  
ATOM   1328  CE2 TYR A 640      -3.271 -24.762 -24.588  1.00 62.89           C  
ANISOU 1328  CE2 TYR A 640     8928   7801   7166    349   -131   -376       C  
ATOM   1329  CZ  TYR A 640      -3.244 -26.139 -24.675  1.00 57.29           C  
ANISOU 1329  CZ  TYR A 640     8303   7045   6421    375   -178   -417       C  
ATOM   1330  OH  TYR A 640      -2.412 -26.753 -25.582  1.00 47.45           O  
ANISOU 1330  OH  TYR A 640     6962   5883   5185    427   -272   -476       O  
ATOM   1331  N   ALA A 641      -4.239 -21.728 -20.998  1.00 45.56           N  
ANISOU 1331  N   ALA A 641     7008   5366   4938    259     57   -253       N  
ATOM   1332  CA  ALA A 641      -3.190 -20.734 -21.188  1.00 41.41           C  
ANISOU 1332  CA  ALA A 641     6376   4919   4440    301     -7   -263       C  
ATOM   1333  C   ALA A 641      -2.260 -20.692 -19.980  1.00 41.65           C  
ANISOU 1333  C   ALA A 641     6554   4864   4406    358    -84   -293       C  
ATOM   1334  O   ALA A 641      -1.061 -20.445 -20.113  1.00 35.97           O  
ANISOU 1334  O   ALA A 641     5785   4194   3686    421   -182   -333       O  
ATOM   1335  CB  ALA A 641      -3.796 -19.366 -21.441  1.00 42.04           C  
ANISOU 1335  CB  ALA A 641     6327   5054   4590    246     82   -209       C  
ATOM   1336  N   PHE A 642      -2.822 -20.925 -18.799  1.00 59.75           N  
ANISOU 1336  N   PHE A 642     9029   7029   6645    332    -38   -278       N  
ATOM   1337  CA  PHE A 642      -2.029 -20.979 -17.578  1.00 62.64           C  
ANISOU 1337  CA  PHE A 642     9560   7301   6940    383   -110   -306       C  
ATOM   1338  C   PHE A 642      -1.136 -22.216 -17.590  1.00 57.63           C  
ANISOU 1338  C   PHE A 642     9015   6634   6249    458   -238   -364       C  
ATOM   1339  O   PHE A 642       0.027 -22.156 -17.192  1.00 47.61           O  
ANISOU 1339  O   PHE A 642     7782   5356   4952    531   -348   -409       O  
ATOM   1340  CB  PHE A 642      -2.937 -20.982 -16.345  1.00 60.49           C  
ANISOU 1340  CB  PHE A 642     9466   6899   6617    326    -22   -274       C  
ATOM   1341  CG  PHE A 642      -2.191 -20.969 -15.040  1.00 65.81           C  
ANISOU 1341  CG  PHE A 642    10317   7474   7213    372    -90   -297       C  
ATOM   1342  CD1 PHE A 642      -1.533 -19.826 -14.616  1.00 61.50           C  
ANISOU 1342  CD1 PHE A 642     9727   6954   6686    398   -113   -300       C  
ATOM   1343  CD2 PHE A 642      -2.154 -22.097 -14.235  1.00 71.22           C  
ANISOU 1343  CD2 PHE A 642    11217   8038   7806    387   -134   -316       C  
ATOM   1344  CE1 PHE A 642      -0.848 -19.809 -13.415  1.00 64.03           C  
ANISOU 1344  CE1 PHE A 642    10210   7185   6935    441   -179   -323       C  
ATOM   1345  CE2 PHE A 642      -1.470 -22.087 -13.032  1.00 72.13           C  
ANISOU 1345  CE2 PHE A 642    11502   8059   7846    430   -203   -335       C  
ATOM   1346  CZ  PHE A 642      -0.816 -20.941 -12.623  1.00 69.97           C  
ANISOU 1346  CZ  PHE A 642    11177   7817   7592    458   -226   -341       C  
ATOM   1347  N   GLY A 643      -1.686 -23.333 -18.058  1.00 47.47           N  
ANISOU 1347  N   GLY A 643     7759   5329   4950    441   -226   -368       N  
ATOM   1348  CA  GLY A 643      -0.934 -24.570 -18.169  1.00 43.88           C  
ANISOU 1348  CA  GLY A 643     7379   4843   4450    510   -346   -425       C  
ATOM   1349  C   GLY A 643       0.303 -24.414 -19.032  1.00 52.76           C  
ANISOU 1349  C   GLY A 643     8347   6083   5614    583   -457   -482       C  
ATOM   1350  O   GLY A 643       1.367 -24.945 -18.711  1.00 57.01           O  
ANISOU 1350  O   GLY A 643     8956   6589   6114    663   -585   -542       O  
ATOM   1351  N   ILE A 644       0.163 -23.686 -20.136  1.00 50.32           N  
ANISOU 1351  N   ILE A 644     7827   5910   5382    553   -410   -465       N  
ATOM   1352  CA  ILE A 644       1.295 -23.406 -21.010  1.00 48.82           C  
ANISOU 1352  CA  ILE A 644     7474   5844   5232    608   -499   -517       C  
ATOM   1353  C   ILE A 644       2.314 -22.548 -20.274  1.00 51.03           C  
ANISOU 1353  C   ILE A 644     7773   6114   5500    656   -562   -541       C  
ATOM   1354  O   ILE A 644       3.521 -22.762 -20.388  1.00 51.43           O  
ANISOU 1354  O   ILE A 644     7799   6197   5544    731   -680   -613       O  
ATOM   1355  CB  ILE A 644       0.857 -22.679 -22.294  1.00 42.17           C  
ANISOU 1355  CB  ILE A 644     6410   5144   4468    554   -424   -483       C  
ATOM   1356  CG1 ILE A 644      -0.196 -23.500 -23.041  1.00 34.99           C  
ANISOU 1356  CG1 ILE A 644     5476   4247   3574    505   -359   -460       C  
ATOM   1357  CG2 ILE A 644       2.058 -22.405 -23.190  1.00 36.75           C  
ANISOU 1357  CG2 ILE A 644     5560   4587   3815    602   -513   -541       C  
ATOM   1358  CD1 ILE A 644       0.318 -24.823 -23.543  1.00 35.00           C  
ANISOU 1358  CD1 ILE A 644     5490   4255   3552    557   -452   -526       C  
ATOM   1359  N   VAL A 645       1.817 -21.572 -19.519  1.00 54.17           N  
ANISOU 1359  N   VAL A 645     8212   6469   5899    614   -482   -487       N  
ATOM   1360  CA  VAL A 645       2.676 -20.722 -18.708  1.00 43.71           C  
ANISOU 1360  CA  VAL A 645     6919   5126   4563    654   -531   -506       C  
ATOM   1361  C   VAL A 645       3.438 -21.576 -17.702  1.00 42.45           C  
ANISOU 1361  C   VAL A 645     6952   4854   4325    729   -646   -562       C  
ATOM   1362  O   VAL A 645       4.643 -21.407 -17.517  1.00 47.68           O  
ANISOU 1362  O   VAL A 645     7600   5535   4982    802   -754   -623       O  
ATOM   1363  CB  VAL A 645       1.868 -19.636 -17.977  1.00 45.34           C  
ANISOU 1363  CB  VAL A 645     7157   5290   4780    591   -419   -438       C  
ATOM   1364  CG1 VAL A 645       2.768 -18.842 -17.043  1.00 45.31           C  
ANISOU 1364  CG1 VAL A 645     7203   5255   4758    636   -475   -462       C  
ATOM   1365  CG2 VAL A 645       1.192 -18.716 -18.983  1.00 35.38           C  
ANISOU 1365  CG2 VAL A 645     5702   4140   3603    524   -322   -386       C  
ATOM   1366  N   LEU A 646       2.729 -22.502 -17.062  1.00 39.28           N  
ANISOU 1366  N   LEU A 646     6729   4333   3863    710   -623   -542       N  
ATOM   1367  CA  LEU A 646       3.361 -23.464 -16.169  1.00 43.37           C  
ANISOU 1367  CA  LEU A 646     7443   4733   4301    778   -737   -590       C  
ATOM   1368  C   LEU A 646       4.477 -24.180 -16.913  1.00 58.12           C  
ANISOU 1368  C   LEU A 646     9236   6662   6184    862   -874   -675       C  
ATOM   1369  O   LEU A 646       5.577 -24.353 -16.390  1.00 67.76           O  
ANISOU 1369  O   LEU A 646    10523   7849   7376    945  -1000   -739       O  
ATOM   1370  CB  LEU A 646       2.344 -24.490 -15.664  1.00 49.20           C  
ANISOU 1370  CB  LEU A 646     8364   5350   4979    734   -686   -555       C  
ATOM   1371  CG  LEU A 646       1.174 -23.981 -14.820  1.00 53.53           C  
ANISOU 1371  CG  LEU A 646     9016   5822   5502    646   -549   -482       C  
ATOM   1372  CD1 LEU A 646       0.286 -25.136 -14.375  1.00 39.51           C  
ANISOU 1372  CD1 LEU A 646     7423   3928   3661    603   -510   -460       C  
ATOM   1373  CD2 LEU A 646       1.684 -23.203 -13.618  1.00 65.97           C  
ANISOU 1373  CD2 LEU A 646    10695   7335   7037    669   -575   -484       C  
ATOM   1374  N   TYR A 647       4.179 -24.593 -18.141  1.00 56.57           N  
ANISOU 1374  N   TYR A 647     8898   6559   6036    840   -850   -679       N  
ATOM   1375  CA  TYR A 647       5.140 -25.292 -18.982  1.00 57.43           C  
ANISOU 1375  CA  TYR A 647     8914   6740   6168    910   -967   -764       C  
ATOM   1376  C   TYR A 647       6.375 -24.436 -19.240  1.00 56.29           C  
ANISOU 1376  C   TYR A 647     8633   6694   6062    962  -1041   -822       C  
ATOM   1377  O   TYR A 647       7.502 -24.929 -19.198  1.00 57.08           O  
ANISOU 1377  O   TYR A 647     8743   6793   6152   1047  -1176   -912       O  
ATOM   1378  CB  TYR A 647       4.489 -25.689 -20.307  1.00 60.79           C  
ANISOU 1378  CB  TYR A 647     9191   7263   6643    862   -906   -749       C  
ATOM   1379  CG  TYR A 647       5.426 -26.385 -21.268  1.00 62.63           C  
ANISOU 1379  CG  TYR A 647     9310   7584   6904    924  -1016   -840       C  
ATOM   1380  CD1 TYR A 647       5.523 -27.769 -21.293  1.00 51.58           C  
ANISOU 1380  CD1 TYR A 647     8006   6118   5474    967  -1095   -887       C  
ATOM   1381  CD2 TYR A 647       6.212 -25.656 -22.150  1.00 60.08           C  
ANISOU 1381  CD2 TYR A 647     8783   7407   6638    937  -1040   -881       C  
ATOM   1382  CE1 TYR A 647       6.376 -28.409 -22.168  1.00 43.11           C  
ANISOU 1382  CE1 TYR A 647     6823   5126   4431   1024  -1197   -978       C  
ATOM   1383  CE2 TYR A 647       7.068 -26.286 -23.029  1.00 53.49           C  
ANISOU 1383  CE2 TYR A 647     7838   6656   5828    989  -1136   -972       C  
ATOM   1384  CZ  TYR A 647       7.146 -27.662 -23.035  1.00 51.26           C  
ANISOU 1384  CZ  TYR A 647     7648   6309   5519   1035  -1215  -1023       C  
ATOM   1385  OH  TYR A 647       7.999 -28.289 -23.911  1.00 59.55           O  
ANISOU 1385  OH  TYR A 647     8583   7444   6598   1087  -1312  -1122       O  
ATOM   1386  N   GLU A 648       6.156 -23.154 -19.512  1.00 55.21           N  
ANISOU 1386  N   GLU A 648     8365   6640   5972    910   -952   -776       N  
ATOM   1387  CA  GLU A 648       7.257 -22.224 -19.728  1.00 57.84           C  
ANISOU 1387  CA  GLU A 648     8569   7066   6344    947  -1006   -824       C  
ATOM   1388  C   GLU A 648       8.161 -22.185 -18.508  1.00 63.51           C  
ANISOU 1388  C   GLU A 648     9430   7688   7012   1023  -1108   -874       C  
ATOM   1389  O   GLU A 648       9.381 -22.272 -18.624  1.00 64.45           O  
ANISOU 1389  O   GLU A 648     9500   7847   7141   1098  -1225   -965       O  
ATOM   1390  CB  GLU A 648       6.731 -20.815 -20.001  1.00 58.05           C  
ANISOU 1390  CB  GLU A 648     8469   7167   6420    873   -887   -751       C  
ATOM   1391  CG  GLU A 648       5.905 -20.677 -21.261  1.00 50.82           C  
ANISOU 1391  CG  GLU A 648     7395   6356   5558    799   -792   -702       C  
ATOM   1392  CD  GLU A 648       5.624 -19.229 -21.602  1.00 57.19           C  
ANISOU 1392  CD  GLU A 648     8065   7245   6421    738   -702   -642       C  
ATOM   1393  OE1 GLU A 648       6.589 -18.484 -21.871  1.00 51.65           O  
ANISOU 1393  OE1 GLU A 648     7252   6624   5748    762   -747   -682       O  
ATOM   1394  OE2 GLU A 648       4.440 -18.833 -21.599  1.00 64.40           O  
ANISOU 1394  OE2 GLU A 648     8980   8139   7352    665   -587   -560       O  
ATOM   1395  N   LEU A 649       7.549 -22.047 -17.337  1.00 74.42           N  
ANISOU 1395  N   LEU A 649    10988   8946   8343   1002  -1063   -818       N  
ATOM   1396  CA  LEU A 649       8.288 -21.946 -16.085  1.00 74.17           C  
ANISOU 1396  CA  LEU A 649    11108   8815   8258   1066  -1150   -855       C  
ATOM   1397  C   LEU A 649       9.050 -23.228 -15.765  1.00 80.36           C  
ANISOU 1397  C   LEU A 649    12020   9520   8991   1156  -1301   -936       C  
ATOM   1398  O   LEU A 649      10.212 -23.184 -15.364  1.00 83.81           O  
ANISOU 1398  O   LEU A 649    12476   9948   9420   1240  -1424  -1015       O  
ATOM   1399  CB  LEU A 649       7.341 -21.597 -14.932  1.00 51.14           C  
ANISOU 1399  CB  LEU A 649     8360   5782   5291   1011  -1058   -774       C  
ATOM   1400  CG  LEU A 649       6.626 -20.243 -14.984  1.00 44.71           C  
ANISOU 1400  CG  LEU A 649     7444   5020   4523    930   -919   -699       C  
ATOM   1401  CD1 LEU A 649       5.457 -20.214 -14.013  1.00 36.77           C  
ANISOU 1401  CD1 LEU A 649     6605   3899   3468    864   -815   -624       C  
ATOM   1402  CD2 LEU A 649       7.590 -19.099 -14.701  1.00 50.64           C  
ANISOU 1402  CD2 LEU A 649     8118   5821   5303    968   -960   -733       C  
ATOM   1403  N   MET A 650       8.396 -24.370 -15.950  1.00 77.42           N  
ANISOU 1403  N   MET A 650    11735   9092   8591   1141  -1295   -920       N  
ATOM   1404  CA  MET A 650       8.971 -25.648 -15.536  1.00 77.61           C  
ANISOU 1404  CA  MET A 650    11910   9016   8561   1221  -1435   -986       C  
ATOM   1405  C   MET A 650       9.951 -26.259 -16.536  1.00 77.47           C  
ANISOU 1405  C   MET A 650    11755   9090   8591   1291  -1552  -1089       C  
ATOM   1406  O   MET A 650      10.716 -27.159 -16.189  1.00 86.84           O  
ANISOU 1406  O   MET A 650    13043  10207   9747   1377  -1696  -1167       O  
ATOM   1407  CB  MET A 650       7.863 -26.642 -15.189  1.00 65.47           C  
ANISOU 1407  CB  MET A 650    10547   7363   6967   1173  -1383   -926       C  
ATOM   1408  CG  MET A 650       7.040 -26.205 -13.987  1.00 69.83           C  
ANISOU 1408  CG  MET A 650    11275   7802   7456   1115  -1292   -844       C  
ATOM   1409  SD  MET A 650       8.087 -25.714 -12.597  1.00 98.36           S  
ANISOU 1409  SD  MET A 650    15035  11326  11012   1192  -1404   -884       S  
ATOM   1410  CE  MET A 650       6.898 -24.924 -11.511  1.00 69.32           C  
ANISOU 1410  CE  MET A 650    11490   7564   7283   1092  -1247   -778       C  
ATOM   1411  N   THR A 651       9.932 -25.767 -17.770  1.00 65.69           N  
ANISOU 1411  N   THR A 651    10033   7753   7173   1254  -1492  -1094       N  
ATOM   1412  CA  THR A 651      10.836 -26.270 -18.797  1.00 71.09           C  
ANISOU 1412  CA  THR A 651    10566   8540   7905   1309  -1588  -1195       C  
ATOM   1413  C   THR A 651      11.828 -25.199 -19.235  1.00 77.51           C  
ANISOU 1413  C   THR A 651    11194   9483   8774   1329  -1611  -1252       C  
ATOM   1414  O   THR A 651      12.912 -25.508 -19.725  1.00 81.89           O  
ANISOU 1414  O   THR A 651    11654  10103   9358   1396  -1722  -1363       O  
ATOM   1415  CB  THR A 651      10.068 -26.765 -20.036  1.00 60.22           C  
ANISOU 1415  CB  THR A 651     9067   7248   6566   1249  -1512  -1169       C  
ATOM   1416  OG1 THR A 651       9.595 -25.641 -20.787  1.00 65.46           O  
ANISOU 1416  OG1 THR A 651     9553   8038   7282   1168  -1384  -1108       O  
ATOM   1417  CG2 THR A 651       8.893 -27.641 -19.623  1.00 55.89           C  
ANISOU 1417  CG2 THR A 651     8689   6578   5967   1208  -1455  -1097       C  
ATOM   1418  N   GLY A 652      11.451 -23.938 -19.058  1.00 80.68           N  
ANISOU 1418  N   GLY A 652    11542   9920   9191   1268  -1504  -1180       N  
ATOM   1419  CA  GLY A 652      12.302 -22.834 -19.460  1.00 78.47           C  
ANISOU 1419  CA  GLY A 652    11091   9761   8963   1274  -1510  -1222       C  
ATOM   1420  C   GLY A 652      12.261 -22.603 -20.957  1.00 74.70           C  
ANISOU 1420  C   GLY A 652    10384   9449   8550   1223  -1456  -1230       C  
ATOM   1421  O   GLY A 652      13.104 -21.897 -21.511  1.00 73.86           O  
ANISOU 1421  O   GLY A 652    10118   9458   8489   1230  -1476  -1286       O  
ATOM   1422  N   GLN A 653      11.272 -23.199 -21.615  1.00 73.42           N  
ANISOU 1422  N   GLN A 653    10208   9299   8391   1168  -1384  -1175       N  
ATOM   1423  CA  GLN A 653      11.131 -23.062 -23.059  1.00 71.17           C  
ANISOU 1423  CA  GLN A 653     9716   9167   8160   1116  -1330  -1177       C  
ATOM   1424  C   GLN A 653       9.680 -23.193 -23.504  1.00 62.06           C  
ANISOU 1424  C   GLN A 653     8562   8010   7009   1029  -1201  -1070       C  
ATOM   1425  O   GLN A 653       8.844 -23.747 -22.790  1.00 53.72           O  
ANISOU 1425  O   GLN A 653     7671   6830   5911   1019  -1171  -1016       O  
ATOM   1426  CB  GLN A 653      11.994 -24.099 -23.776  1.00 64.06           C  
ANISOU 1426  CB  GLN A 653     8746   8321   7271   1178  -1445  -1297       C  
ATOM   1427  CG  GLN A 653      11.665 -25.529 -23.404  1.00 64.40           C  
ANISOU 1427  CG  GLN A 653     8949   8247   7274   1222  -1507  -1314       C  
ATOM   1428  CD  GLN A 653      12.768 -26.488 -23.790  1.00 72.82           C  
ANISOU 1428  CD  GLN A 653     9974   9341   8352   1308  -1654  -1453       C  
ATOM   1429  OE1 GLN A 653      13.898 -26.076 -24.049  1.00 83.48           O  
ANISOU 1429  OE1 GLN A 653    11211  10775   9733   1349  -1724  -1547       O  
ATOM   1430  NE2 GLN A 653      12.449 -27.775 -23.826  1.00 71.44           N  
ANISOU 1430  NE2 GLN A 653     9893   9095   8156   1336  -1702  -1473       N  
ATOM   1431  N   LEU A 654       9.396 -22.681 -24.696  1.00 54.49           N  
ANISOU 1431  N   LEU A 654     7417   7188   6098    964  -1127  -1042       N  
ATOM   1432  CA  LEU A 654       8.051 -22.710 -25.256  1.00 53.80           C  
ANISOU 1432  CA  LEU A 654     7302   7115   6023    881  -1006   -947       C  
ATOM   1433  C   LEU A 654       7.710 -24.085 -25.820  1.00 56.34           C  
ANISOU 1433  C   LEU A 654     7643   7429   6335    893  -1033   -978       C  
ATOM   1434  O   LEU A 654       8.602 -24.855 -26.175  1.00 73.95           O  
ANISOU 1434  O   LEU A 654     9840   9691   8565    954  -1139  -1079       O  
ATOM   1435  CB  LEU A 654       7.914 -21.647 -26.348  1.00 50.89           C  
ANISOU 1435  CB  LEU A 654     6731   6897   5709    810   -927   -908       C  
ATOM   1436  CG  LEU A 654       7.986 -20.190 -25.891  1.00 52.65           C  
ANISOU 1436  CG  LEU A 654     6925   7128   5950    779   -875   -855       C  
ATOM   1437  CD1 LEU A 654       8.244 -19.254 -27.066  1.00 43.41           C  
ANISOU 1437  CD1 LEU A 654     5547   6118   4831    725   -836   -846       C  
ATOM   1438  CD2 LEU A 654       6.710 -19.804 -25.157  1.00 57.37           C  
ANISOU 1438  CD2 LEU A 654     7633   7625   6539    727   -770   -748       C  
ATOM   1439  N   PRO A 655       6.409 -24.400 -25.894  1.00 45.52           N  
ANISOU 1439  N   PRO A 655     6323   6014   4958    833   -937   -897       N  
ATOM   1440  CA  PRO A 655       5.953 -25.662 -26.482  1.00 48.41           C  
ANISOU 1440  CA  PRO A 655     6700   6374   5318    834   -948   -917       C  
ATOM   1441  C   PRO A 655       6.219 -25.697 -27.981  1.00 52.99           C  
ANISOU 1441  C   PRO A 655     7069   7120   5945    813   -948   -956       C  
ATOM   1442  O   PRO A 655       6.303 -24.647 -28.619  1.00 55.51           O  
ANISOU 1442  O   PRO A 655     7240   7552   6300    767   -897   -929       O  
ATOM   1443  CB  PRO A 655       4.441 -25.644 -26.226  1.00 46.13           C  
ANISOU 1443  CB  PRO A 655     6490   6015   5023    760   -821   -812       C  
ATOM   1444  CG  PRO A 655       4.241 -24.659 -25.123  1.00 52.12           C  
ANISOU 1444  CG  PRO A 655     7343   6695   5764    744   -775   -754       C  
ATOM   1445  CD  PRO A 655       5.298 -23.623 -25.323  1.00 52.94           C  
ANISOU 1445  CD  PRO A 655     7325   6893   5896    766   -817   -788       C  
ATOM   1446  N   TYR A 656       6.359 -26.898 -28.529  1.00 52.47           N  
ANISOU 1446  N   TYR A 656     6993   7067   5877    844  -1007  -1021       N  
ATOM   1447  CA  TYR A 656       6.498 -27.074 -29.969  1.00 49.00           C  
ANISOU 1447  CA  TYR A 656     6362   6781   5476    818  -1001  -1059       C  
ATOM   1448  C   TYR A 656       7.685 -26.301 -30.545  1.00 47.41           C  
ANISOU 1448  C   TYR A 656     6000   6714   5301    831  -1050  -1125       C  
ATOM   1449  O   TYR A 656       7.628 -25.816 -31.674  1.00 42.87           O  
ANISOU 1449  O   TYR A 656     5251   6279   4756    776  -1001  -1115       O  
ATOM   1450  CB  TYR A 656       5.206 -26.654 -30.676  1.00 57.83           C  
ANISOU 1450  CB  TYR A 656     7404   7952   6618    724   -867   -957       C  
ATOM   1451  CG  TYR A 656       3.951 -26.912 -29.867  1.00 60.29           C  
ANISOU 1451  CG  TYR A 656     7875   8126   6906    693   -788   -872       C  
ATOM   1452  CD1 TYR A 656       3.633 -28.190 -29.430  1.00 55.80           C  
ANISOU 1452  CD1 TYR A 656     7449   7447   6307    725   -823   -895       C  
ATOM   1453  CD2 TYR A 656       3.079 -25.876 -29.550  1.00 58.20           C  
ANISOU 1453  CD2 TYR A 656     7620   7842   6653    628   -679   -771       C  
ATOM   1454  CE1 TYR A 656       2.488 -28.430 -28.694  1.00 54.08           C  
ANISOU 1454  CE1 TYR A 656     7378   7106   6065    688   -745   -822       C  
ATOM   1455  CE2 TYR A 656       1.930 -26.107 -28.815  1.00 49.30           C  
ANISOU 1455  CE2 TYR A 656     6632   6594   5507    594   -602   -703       C  
ATOM   1456  CZ  TYR A 656       1.640 -27.386 -28.391  1.00 49.22           C  
ANISOU 1456  CZ  TYR A 656     6762   6478   5461    621   -632   -729       C  
ATOM   1457  OH  TYR A 656       0.500 -27.625 -27.660  1.00 47.45           O  
ANISOU 1457  OH  TYR A 656     6679   6135   5215    580   -550   -665       O  
ATOM   1458  N   SER A 657       8.757 -26.188 -29.767  1.00 71.23           N  
ANISOU 1458  N   SER A 657     9076   9686   8304    902  -1145  -1194       N  
ATOM   1459  CA  SER A 657       9.965 -25.516 -30.234  1.00 76.81           C  
ANISOU 1459  CA  SER A 657     9637  10511   9035    919  -1197  -1272       C  
ATOM   1460  C   SER A 657      10.583 -26.279 -31.400  1.00 79.48           C  
ANISOU 1460  C   SER A 657     9832  10970   9395    934  -1257  -1378       C  
ATOM   1461  O   SER A 657      11.036 -25.682 -32.376  1.00 80.32           O  
ANISOU 1461  O   SER A 657     9762  11228   9530    894  -1237  -1406       O  
ATOM   1462  CB  SER A 657      10.979 -25.368 -29.099  1.00 79.38           C  
ANISOU 1462  CB  SER A 657    10066  10752   9341   1000  -1297  -1337       C  
ATOM   1463  OG  SER A 657      10.504 -24.475 -28.108  1.00 77.50           O  
ANISOU 1463  OG  SER A 657     9933  10426   9086    978  -1236  -1244       O  
ATOM   1464  N   ASN A 658      10.595 -27.603 -31.290  1.00 69.44           N  
ANISOU 1464  N   ASN A 658     8641   9632   8111    990  -1330  -1438       N  
ATOM   1465  CA  ASN A 658      11.093 -28.454 -32.361  1.00 68.49           C  
ANISOU 1465  CA  ASN A 658     8395   9615   8013   1007  -1388  -1542       C  
ATOM   1466  C   ASN A 658      10.288 -28.249 -33.642  1.00 76.62           C  
ANISOU 1466  C   ASN A 658     9275  10773   9063    915  -1281  -1483       C  
ATOM   1467  O   ASN A 658      10.836 -28.282 -34.744  1.00 85.94           O  
ANISOU 1467  O   ASN A 658    10285  12100  10267    897  -1296  -1555       O  
ATOM   1468  CB  ASN A 658      11.048 -29.923 -31.937  1.00 79.71           C  
ANISOU 1468  CB  ASN A 658     9950  10919   9418   1079  -1477  -1598       C  
ATOM   1469  CG  ASN A 658      12.272 -30.695 -32.383  1.00 90.16           C  
ANISOU 1469  CG  ASN A 658    11192  12301  10763   1153  -1610  -1760       C  
ATOM   1470  OD1 ASN A 658      13.368 -30.142 -32.479  1.00 90.49           O  
ANISOU 1470  OD1 ASN A 658    11140  12420  10823   1179  -1665  -1844       O  
ATOM   1471  ND2 ASN A 658      12.094 -31.984 -32.649  1.00 93.15           N  
ANISOU 1471  ND2 ASN A 658    11604  12643  11144   1188  -1664  -1811       N  
ATOM   1472  N   ILE A 659       8.986 -28.032 -33.487  1.00 88.19           N  
ANISOU 1472  N   ILE A 659    10806  12183  10520    856  -1174  -1356       N  
ATOM   1473  CA  ILE A 659       8.098 -27.799 -34.621  1.00 81.27           C  
ANISOU 1473  CA  ILE A 659     9804  11414   9662    769  -1071  -1289       C  
ATOM   1474  C   ILE A 659       7.896 -26.304 -34.854  1.00 93.81           C  
ANISOU 1474  C   ILE A 659    11304  13077  11263    696   -982  -1204       C  
ATOM   1475  O   ILE A 659       7.008 -25.696 -34.256  1.00102.93           O  
ANISOU 1475  O   ILE A 659    12541  14153  12413    660   -903  -1095       O  
ATOM   1476  CB  ILE A 659       6.715 -28.441 -34.385  1.00 51.46           C  
ANISOU 1476  CB  ILE A 659     6140   7537   5875    742  -1001  -1204       C  
ATOM   1477  CG1 ILE A 659       6.857 -29.926 -34.044  1.00 48.72           C  
ANISOU 1477  CG1 ILE A 659     5904   7096   5513    812  -1089  -1279       C  
ATOM   1478  CG2 ILE A 659       5.819 -28.246 -35.599  1.00 40.02           C  
ANISOU 1478  CG2 ILE A 659     4555   6201   4448    658   -904  -1145       C  
ATOM   1479  CD1 ILE A 659       5.540 -30.607 -33.727  1.00 52.67           C  
ANISOU 1479  CD1 ILE A 659     6528   7486   6000    785  -1023  -1203       C  
ATOM   1480  N   ASN A 660       8.712 -25.710 -35.719  1.00 80.02           N  
ANISOU 1480  N   ASN A 660     9392  11479   9534    672   -995  -1255       N  
ATOM   1481  CA  ASN A 660       8.594 -24.281 -36.001  1.00 65.24           C  
ANISOU 1481  CA  ASN A 660     7433   9681   7674    601   -918  -1176       C  
ATOM   1482  C   ASN A 660       7.679 -23.980 -37.185  1.00 58.82           C  
ANISOU 1482  C   ASN A 660     6501   8973   6875    510   -824  -1100       C  
ATOM   1483  O   ASN A 660       8.087 -23.339 -38.153  1.00 62.63           O  
ANISOU 1483  O   ASN A 660     6831   9598   7367    458   -806  -1110       O  
ATOM   1484  CB  ASN A 660       9.970 -23.646 -36.221  1.00 60.25           C  
ANISOU 1484  CB  ASN A 660     6695   9147   7049    614   -976  -1264       C  
ATOM   1485  CG  ASN A 660       9.890 -22.145 -36.447  1.00 61.90           C  
ANISOU 1485  CG  ASN A 660     6826   9423   7271    540   -901  -1183       C  
ATOM   1486  OD1 ASN A 660       8.907 -21.501 -36.077  1.00 73.55           O  
ANISOU 1486  OD1 ASN A 660     8359  10835   8749    499   -820  -1063       O  
ATOM   1487  ND2 ASN A 660      10.925 -21.581 -37.059  1.00 51.29           N  
ANISOU 1487  ND2 ASN A 660     5348   8205   5935    521   -927  -1251       N  
ATOM   1488  N   ASN A 661       6.440 -24.451 -37.101  1.00 42.10           N  
ANISOU 1488  N   ASN A 661     4455   6783   4756    490   -765  -1025       N  
ATOM   1489  CA  ASN A 661       5.444 -24.162 -38.123  1.00 43.46           C  
ANISOU 1489  CA  ASN A 661     4530   7038   4944    408   -676   -945       C  
ATOM   1490  C   ASN A 661       4.083 -23.851 -37.519  1.00 49.14           C  
ANISOU 1490  C   ASN A 661     5354   7648   5671    376   -587   -826       C  
ATOM   1491  O   ASN A 661       3.427 -24.717 -36.941  1.00 47.37           O  
ANISOU 1491  O   ASN A 661     5249   7311   5437    403   -581   -818       O  
ATOM   1492  CB  ASN A 661       5.329 -25.311 -39.121  1.00 57.46           C  
ANISOU 1492  CB  ASN A 661     6231   8886   6718    409   -697  -1007       C  
ATOM   1493  CG  ASN A 661       4.372 -25.001 -40.260  1.00 66.22           C  
ANISOU 1493  CG  ASN A 661     7228  10091   7840    325   -612   -932       C  
ATOM   1494  OD1 ASN A 661       3.302 -24.425 -40.055  1.00 71.29           O  
ANISOU 1494  OD1 ASN A 661     7909  10683   8495    281   -531   -824       O  
ATOM   1495  ND2 ASN A 661       4.755 -25.387 -41.470  1.00 62.70           N  
ANISOU 1495  ND2 ASN A 661     6641   9786   7394    302   -632   -995       N  
ATOM   1496  N   ARG A 662       3.669 -22.601 -37.672  1.00 63.81           N  
ANISOU 1496  N   ARG A 662     7160   9538   7546    315   -518   -736       N  
ATOM   1497  CA  ARG A 662       2.405 -22.128 -37.136  1.00 66.94           C  
ANISOU 1497  CA  ARG A 662     7636   9841   7959    279   -431   -627       C  
ATOM   1498  C   ARG A 662       1.232 -22.989 -37.598  1.00 65.37           C  
ANISOU 1498  C   ARG A 662     7446   9625   7767    255   -382   -600       C  
ATOM   1499  O   ARG A 662       0.573 -23.635 -36.786  1.00 68.88           O  
ANISOU 1499  O   ARG A 662     8025   9943   8204    278   -364   -587       O  
ATOM   1500  CB  ARG A 662       2.193 -20.675 -37.547  1.00 66.98           C  
ANISOU 1500  CB  ARG A 662     7547   9914   7989    212   -374   -546       C  
ATOM   1501  CG  ARG A 662       1.041 -19.997 -36.860  1.00 74.90           C  
ANISOU 1501  CG  ARG A 662     8628  10816   9015    181   -293   -443       C  
ATOM   1502  CD  ARG A 662       1.397 -18.566 -36.527  1.00 83.67           C  
ANISOU 1502  CD  ARG A 662     9715  11935  10143    157   -279   -395       C  
ATOM   1503  NE  ARG A 662       0.201 -17.771 -36.280  1.00 92.14           N  
ANISOU 1503  NE  ARG A 662    10809  12950  11250    109   -194   -293       N  
ATOM   1504  CZ  ARG A 662       0.212 -16.496 -35.911  1.00 98.35           C  
ANISOU 1504  CZ  ARG A 662    11586  13722  12061     84   -168   -236       C  
ATOM   1505  NH1 ARG A 662       1.363 -15.863 -35.736  1.00 98.97           N  
ANISOU 1505  NH1 ARG A 662    11636  13838  12130    100   -216   -269       N  
ATOM   1506  NH2 ARG A 662      -0.931 -15.855 -35.713  1.00 99.67           N  
ANISOU 1506  NH2 ARG A 662    11769  13835  12265     42    -94   -152       N  
ATOM   1507  N   ASP A 663       0.980 -22.997 -38.904  1.00 58.20           N  
ANISOU 1507  N   ASP A 663     6397   8845   6872    207   -360   -593       N  
ATOM   1508  CA  ASP A 663      -0.113 -23.781 -39.471  1.00 51.52           C  
ANISOU 1508  CA  ASP A 663     5540   7998   6036    181   -314   -571       C  
ATOM   1509  C   ASP A 663      -0.070 -25.238 -39.027  1.00 44.92           C  
ANISOU 1509  C   ASP A 663     4806   7081   5181    241   -358   -643       C  
ATOM   1510  O   ASP A 663      -1.107 -25.877 -38.860  1.00 48.20           O  
ANISOU 1510  O   ASP A 663     5288   7423   5603    231   -311   -614       O  
ATOM   1511  CB  ASP A 663      -0.109 -23.698 -40.998  1.00 63.49           C  
ANISOU 1511  CB  ASP A 663     6884   9679   7560    130   -306   -576       C  
ATOM   1512  CG  ASP A 663      -0.738 -22.421 -41.512  1.00 66.54           C  
ANISOU 1512  CG  ASP A 663     7190  10120   7971     58   -240   -477       C  
ATOM   1513  OD1 ASP A 663      -0.539 -21.363 -40.880  1.00 69.27           O  
ANISOU 1513  OD1 ASP A 663     7567  10427   8325     51   -228   -431       O  
ATOM   1514  OD2 ASP A 663      -1.434 -22.479 -42.547  1.00 59.47           O  
ANISOU 1514  OD2 ASP A 663     6203   9305   7089      9   -203   -445       O  
ATOM   1515  N   GLN A 664       1.133 -25.760 -38.836  1.00 47.78           N  
ANISOU 1515  N   GLN A 664     5180   7454   5521    301   -451   -739       N  
ATOM   1516  CA  GLN A 664       1.296 -27.129 -38.380  1.00 51.09           C  
ANISOU 1516  CA  GLN A 664     5701   7789   5922    363   -509   -812       C  
ATOM   1517  C   GLN A 664       0.775 -27.266 -36.948  1.00 51.90           C  
ANISOU 1517  C   GLN A 664     5998   7711   6010    390   -489   -771       C  
ATOM   1518  O   GLN A 664      -0.033 -28.144 -36.649  1.00 53.95           O  
ANISOU 1518  O   GLN A 664     6354   7882   6265    393   -464   -761       O  
ATOM   1519  CB  GLN A 664       2.767 -27.531 -38.470  1.00 51.22           C  
ANISOU 1519  CB  GLN A 664     5681   7857   5925    425   -620   -930       C  
ATOM   1520  CG  GLN A 664       2.997 -28.968 -38.892  1.00 61.35           C  
ANISOU 1520  CG  GLN A 664     6959   9149   7203    468   -684  -1024       C  
ATOM   1521  CD  GLN A 664       4.423 -29.224 -39.348  1.00 64.15           C  
ANISOU 1521  CD  GLN A 664     7218   9599   7555    513   -785  -1147       C  
ATOM   1522  OE1 GLN A 664       5.384 -28.837 -38.681  1.00 55.90           O  
ANISOU 1522  OE1 GLN A 664     6211   8528   6501    557   -846  -1190       O  
ATOM   1523  NE2 GLN A 664       4.564 -29.884 -40.491  1.00 63.83           N  
ANISOU 1523  NE2 GLN A 664     7053   9675   7524    501   -803  -1212       N  
ATOM   1524  N   ILE A 665       1.231 -26.377 -36.071  1.00 48.60           N  
ANISOU 1524  N   ILE A 665     5640   7243   5584    403   -498   -747       N  
ATOM   1525  CA  ILE A 665       0.801 -26.371 -34.675  1.00 46.39           C  
ANISOU 1525  CA  ILE A 665     5544   6798   5284    423   -478   -707       C  
ATOM   1526  C   ILE A 665      -0.700 -26.102 -34.542  1.00 43.87           C  
ANISOU 1526  C   ILE A 665     5262   6423   4983    359   -362   -611       C  
ATOM   1527  O   ILE A 665      -1.389 -26.749 -33.753  1.00 48.17           O  
ANISOU 1527  O   ILE A 665     5951   6841   5510    364   -335   -595       O  
ATOM   1528  CB  ILE A 665       1.582 -25.321 -33.855  1.00 41.11           C  
ANISOU 1528  CB  ILE A 665     4909   6103   4607    444   -504   -700       C  
ATOM   1529  CG1 ILE A 665       3.069 -25.681 -33.799  1.00 41.77           C  
ANISOU 1529  CG1 ILE A 665     4978   6220   4673    516   -625   -808       C  
ATOM   1530  CG2 ILE A 665       1.016 -25.210 -32.450  1.00 35.44           C  
ANISOU 1530  CG2 ILE A 665     4376   5221   3867    452   -469   -650       C  
ATOM   1531  CD1 ILE A 665       3.943 -24.571 -33.246  1.00 42.53           C  
ANISOU 1531  CD1 ILE A 665     5068   6324   4769    532   -652   -811       C  
ATOM   1532  N   ILE A 666      -1.196 -25.141 -35.316  1.00 38.32           N  
ANISOU 1532  N   ILE A 666     4430   5814   4314    296   -296   -549       N  
ATOM   1533  CA  ILE A 666      -2.618 -24.812 -35.325  1.00 40.15           C  
ANISOU 1533  CA  ILE A 666     4672   6008   4574    235   -189   -464       C  
ATOM   1534  C   ILE A 666      -3.460 -26.013 -35.750  1.00 42.31           C  
ANISOU 1534  C   ILE A 666     4963   6264   4850    225   -162   -480       C  
ATOM   1535  O   ILE A 666      -4.500 -26.299 -35.158  1.00 44.08           O  
ANISOU 1535  O   ILE A 666     5288   6384   5077    202    -96   -443       O  
ATOM   1536  CB  ILE A 666      -2.915 -23.638 -36.276  1.00 45.85           C  
ANISOU 1536  CB  ILE A 666     5236   6850   5336    174   -141   -404       C  
ATOM   1537  CG1 ILE A 666      -2.111 -22.404 -35.873  1.00 41.99           C  
ANISOU 1537  CG1 ILE A 666     4728   6378   4849    179   -163   -386       C  
ATOM   1538  CG2 ILE A 666      -4.403 -23.324 -36.291  1.00 51.25           C  
ANISOU 1538  CG2 ILE A 666     5926   7491   6056    116    -38   -326       C  
ATOM   1539  CD1 ILE A 666      -2.330 -21.214 -36.781  1.00 40.93           C  
ANISOU 1539  CD1 ILE A 666     4447   6355   4751    118   -124   -324       C  
ATOM   1540  N   GLU A 667      -3.002 -26.713 -36.782  1.00 33.57           N  
ANISOU 1540  N   GLU A 667     3754   5259   3742    239   -213   -540       N  
ATOM   1541  CA  GLU A 667      -3.709 -27.882 -37.293  1.00 49.60           C  
ANISOU 1541  CA  GLU A 667     5785   7284   5776    232   -195   -563       C  
ATOM   1542  C   GLU A 667      -3.642 -29.064 -36.329  1.00 53.13           C  
ANISOU 1542  C   GLU A 667     6405   7592   6190    282   -232   -610       C  
ATOM   1543  O   GLU A 667      -4.643 -29.738 -36.090  1.00 52.29           O  
ANISOU 1543  O   GLU A 667     6377   7405   6086    261   -177   -591       O  
ATOM   1544  CB  GLU A 667      -3.141 -28.291 -38.656  1.00 60.02           C  
ANISOU 1544  CB  GLU A 667     6945   8757   7104    234   -244   -622       C  
ATOM   1545  CG  GLU A 667      -3.608 -29.654 -39.152  1.00 75.96           C  
ANISOU 1545  CG  GLU A 667     8967  10771   9123    243   -248   -669       C  
ATOM   1546  CD  GLU A 667      -5.068 -29.665 -39.562  1.00 89.23           C  
ANISOU 1546  CD  GLU A 667    10622  12446  10834    182   -148   -606       C  
ATOM   1547  OE1 GLU A 667      -5.538 -28.656 -40.128  1.00 88.92           O  
ANISOU 1547  OE1 GLU A 667    10482  12483  10823    130    -93   -543       O  
ATOM   1548  OE2 GLU A 667      -5.743 -30.690 -39.328  1.00 97.57           O  
ANISOU 1548  OE2 GLU A 667    11760  13422  11889    186   -126   -622       O  
ATOM   1549  N   MET A 668      -2.459 -29.308 -35.774  1.00 53.91           N  
ANISOU 1549  N   MET A 668     6565   7660   6258    347   -328   -671       N  
ATOM   1550  CA  MET A 668      -2.224 -30.503 -34.968  1.00 36.10           C  
ANISOU 1550  CA  MET A 668     4468   5280   3968    402   -388   -725       C  
ATOM   1551  C   MET A 668      -2.753 -30.396 -33.536  1.00 39.21           C  
ANISOU 1551  C   MET A 668     5058   5507   4333    399   -348   -675       C  
ATOM   1552  O   MET A 668      -3.203 -31.387 -32.960  1.00 54.09           O  
ANISOU 1552  O   MET A 668     7082   7275   6193    409   -347   -686       O  
ATOM   1553  CB  MET A 668      -0.736 -30.870 -34.982  1.00 26.49           C  
ANISOU 1553  CB  MET A 668     3236   4098   2733    477   -518   -821       C  
ATOM   1554  CG  MET A 668      -0.192 -31.115 -36.387  1.00 30.16           C  
ANISOU 1554  CG  MET A 668     3512   4726   3221    478   -558   -885       C  
ATOM   1555  SD  MET A 668       1.391 -31.982 -36.448  1.00 52.40           S  
ANISOU 1555  SD  MET A 668     6318   7567   6023    571   -713  -1024       S  
ATOM   1556  CE  MET A 668       2.517 -30.744 -35.809  1.00 84.27           C  
ANISOU 1556  CE  MET A 668    10352  11619  10050    597   -758  -1029       C  
ATOM   1557  N   VAL A 669      -2.702 -29.199 -32.963  1.00 37.38           N  
ANISOU 1557  N   VAL A 669     4838   5261   4102    381   -314   -622       N  
ATOM   1558  CA  VAL A 669      -3.236 -28.983 -31.622  1.00 41.66           C  
ANISOU 1558  CA  VAL A 669     5556   5655   4618    370   -267   -574       C  
ATOM   1559  C   VAL A 669      -4.762 -28.898 -31.652  1.00 51.08           C  
ANISOU 1559  C   VAL A 669     6763   6812   5835    295   -140   -507       C  
ATOM   1560  O   VAL A 669      -5.439 -29.327 -30.716  1.00 49.55           O  
ANISOU 1560  O   VAL A 669     6728   6486   5615    279    -95   -487       O  
ATOM   1561  CB  VAL A 669      -2.657 -27.713 -30.974  1.00 38.71           C  
ANISOU 1561  CB  VAL A 669     5188   5280   4242    377   -275   -546       C  
ATOM   1562  CG1 VAL A 669      -3.434 -27.353 -29.718  1.00 33.85           C  
ANISOU 1562  CG1 VAL A 669     4730   4526   3605    347   -201   -488       C  
ATOM   1563  CG2 VAL A 669      -1.181 -27.904 -30.660  1.00 39.36           C  
ANISOU 1563  CG2 VAL A 669     5296   5364   4294    457   -402   -621       C  
ATOM   1564  N   GLY A 670      -5.295 -28.346 -32.737  1.00 48.76           N  
ANISOU 1564  N   GLY A 670     6302   6635   5591    247    -84   -475       N  
ATOM   1565  CA  GLY A 670      -6.730 -28.197 -32.896  1.00 42.52           C  
ANISOU 1565  CA  GLY A 670     5497   5825   4834    178     32   -419       C  
ATOM   1566  C   GLY A 670      -7.461 -29.517 -33.050  1.00 44.26           C  
ANISOU 1566  C   GLY A 670     5777   5992   5046    168     56   -445       C  
ATOM   1567  O   GLY A 670      -8.626 -29.634 -32.668  1.00 46.92           O  
ANISOU 1567  O   GLY A 670     6179   6254   5394    118    149   -411       O  
ATOM   1568  N   ARG A 671      -6.778 -30.512 -33.610  1.00 45.51           N  
ANISOU 1568  N   ARG A 671     5910   6192   5191    214    -27   -511       N  
ATOM   1569  CA  ARG A 671      -7.372 -31.830 -33.828  1.00 50.04           C  
ANISOU 1569  CA  ARG A 671     6533   6720   5759    209    -16   -544       C  
ATOM   1570  C   ARG A 671      -7.066 -32.787 -32.678  1.00 62.29           C  
ANISOU 1570  C   ARG A 671     8294   8119   7255    249    -65   -576       C  
ATOM   1571  O   ARG A 671      -7.692 -33.840 -32.552  1.00 65.90           O  
ANISOU 1571  O   ARG A 671     8838   8500   7701    236    -42   -591       O  
ATOM   1572  CB  ARG A 671      -6.893 -32.424 -35.156  1.00 48.71           C  
ANISOU 1572  CB  ARG A 671     6213   6684   5611    232    -76   -601       C  
ATOM   1573  CG  ARG A 671      -5.397 -32.694 -35.224  1.00 53.89           C  
ANISOU 1573  CG  ARG A 671     6854   7380   6242    306   -205   -672       C  
ATOM   1574  CD  ARG A 671      -4.963 -33.027 -36.645  1.00 49.10           C  
ANISOU 1574  CD  ARG A 671     6066   6930   5662    315   -249   -726       C  
ATOM   1575  NE  ARG A 671      -3.550 -33.387 -36.724  1.00 49.04           N  
ANISOU 1575  NE  ARG A 671     6040   6959   5635    386   -373   -810       N  
ATOM   1576  CZ  ARG A 671      -2.905 -33.646 -37.857  1.00 51.47           C  
ANISOU 1576  CZ  ARG A 671     6193   7404   5959    401   -428   -873       C  
ATOM   1577  NH1 ARG A 671      -3.542 -33.581 -39.017  1.00 48.15           N  
ANISOU 1577  NH1 ARG A 671     5627   7097   5569    351   -371   -857       N  
ATOM   1578  NH2 ARG A 671      -1.620 -33.968 -37.831  1.00 61.61           N  
ANISOU 1578  NH2 ARG A 671     7468   8714   7229    466   -540   -958       N  
ATOM   1579  N   GLY A 672      -6.099 -32.417 -31.844  1.00 69.77           N  
ANISOU 1579  N   GLY A 672     9326   9019   8166    297   -135   -586       N  
ATOM   1580  CA  GLY A 672      -5.766 -33.198 -30.666  1.00 56.72           C  
ANISOU 1580  CA  GLY A 672     7883   7213   6454    336   -189   -611       C  
ATOM   1581  C   GLY A 672      -4.617 -34.169 -30.855  1.00 55.05           C  
ANISOU 1581  C   GLY A 672     7689   7005   6221    416   -328   -695       C  
ATOM   1582  O   GLY A 672      -4.439 -35.090 -30.059  1.00 64.03           O  
ANISOU 1582  O   GLY A 672     9001   8015   7313    450   -381   -722       O  
ATOM   1583  N   SER A 673      -3.831 -33.966 -31.905  1.00 55.91           N  
ANISOU 1583  N   SER A 673     7621   7260   6362    447   -388   -740       N  
ATOM   1584  CA  SER A 673      -2.702 -34.846 -32.185  1.00 51.89           C  
ANISOU 1584  CA  SER A 673     7103   6769   5842    524   -521   -833       C  
ATOM   1585  C   SER A 673      -1.417 -34.319 -31.556  1.00 57.49           C  
ANISOU 1585  C   SER A 673     7846   7468   6528    588   -621   -868       C  
ATOM   1586  O   SER A 673      -0.408 -35.021 -31.502  1.00 63.38           O  
ANISOU 1586  O   SER A 673     8619   8201   7261    662   -743   -951       O  
ATOM   1587  CB  SER A 673      -2.513 -35.019 -33.693  1.00 32.98           C  
ANISOU 1587  CB  SER A 673     4495   4542   3494    520   -535   -878       C  
ATOM   1588  OG  SER A 673      -2.056 -33.816 -34.288  1.00 39.31           O  
ANISOU 1588  OG  SER A 673     5136   5478   4320    505   -524   -864       O  
ATOM   1589  N   LEU A 674      -1.458 -33.083 -31.073  1.00 49.58           N  
ANISOU 1589  N   LEU A 674     6842   6472   5525    562   -570   -809       N  
ATOM   1590  CA  LEU A 674      -0.269 -32.458 -30.514  1.00 46.08           C  
ANISOU 1590  CA  LEU A 674     6416   6029   5064    618   -655   -840       C  
ATOM   1591  C   LEU A 674      -0.520 -31.853 -29.136  1.00 48.11           C  
ANISOU 1591  C   LEU A 674     6840   6156   5282    608   -619   -781       C  
ATOM   1592  O   LEU A 674      -1.568 -31.257 -28.882  1.00 52.73           O  
ANISOU 1592  O   LEU A 674     7446   6714   5874    539   -502   -701       O  
ATOM   1593  CB  LEU A 674       0.276 -31.397 -31.472  1.00 34.92           C  
ANISOU 1593  CB  LEU A 674     4791   4786   3693    604   -650   -846       C  
ATOM   1594  CG  LEU A 674       1.606 -30.749 -31.095  1.00 37.40           C  
ANISOU 1594  CG  LEU A 674     5087   5125   3997    661   -741   -893       C  
ATOM   1595  CD1 LEU A 674       2.662 -31.808 -30.870  1.00 39.81           C  
ANISOU 1595  CD1 LEU A 674     5456   5388   4280    750   -882   -999       C  
ATOM   1596  CD2 LEU A 674       2.058 -29.774 -32.169  1.00 32.10           C  
ANISOU 1596  CD2 LEU A 674     4201   4629   3366    634   -726   -898       C  
ATOM   1597  N   SER A 675       0.456 -32.022 -28.252  1.00 44.55           N  
ANISOU 1597  N   SER A 675     6508   5627   4792    678   -724   -826       N  
ATOM   1598  CA  SER A 675       0.401 -31.468 -26.906  1.00 39.64           C  
ANISOU 1598  CA  SER A 675     6049   4885   4127    677   -708   -781       C  
ATOM   1599  C   SER A 675       1.823 -31.201 -26.426  1.00 46.38           C  
ANISOU 1599  C   SER A 675     6922   5736   4962    760   -835   -846       C  
ATOM   1600  O   SER A 675       2.763 -31.847 -26.885  1.00 51.50           O  
ANISOU 1600  O   SER A 675     7522   6427   5620    825   -949   -934       O  
ATOM   1601  CB  SER A 675      -0.302 -32.437 -25.956  1.00 41.24           C  
ANISOU 1601  CB  SER A 675     6476   4919   4275    667   -692   -760       C  
ATOM   1602  OG  SER A 675       0.438 -33.636 -25.810  1.00 48.22           O  
ANISOU 1602  OG  SER A 675     7450   5740   5130    741   -822   -836       O  
ATOM   1603  N   PRO A 676       1.987 -30.244 -25.502  1.00 70.98           N  
ANISOU 1603  N   PRO A 676    10106   8805   8057    757   -817   -808       N  
ATOM   1604  CA  PRO A 676       3.324 -29.892 -25.008  1.00 70.97           C  
ANISOU 1604  CA  PRO A 676    10120   8803   8042    834   -933   -870       C  
ATOM   1605  C   PRO A 676       4.113 -31.110 -24.521  1.00 62.82           C  
ANISOU 1605  C   PRO A 676     9224   7675   6970    922  -1077   -952       C  
ATOM   1606  O   PRO A 676       3.538 -32.023 -23.928  1.00 49.30           O  
ANISOU 1606  O   PRO A 676     7684   5834   5213    918  -1077   -934       O  
ATOM   1607  CB  PRO A 676       3.025 -28.940 -23.848  1.00 51.79           C  
ANISOU 1607  CB  PRO A 676     7804   6291   5583    808   -875   -803       C  
ATOM   1608  CG  PRO A 676       1.711 -28.326 -24.204  1.00 42.80           C  
ANISOU 1608  CG  PRO A 676     6602   5187   4475    710   -718   -712       C  
ATOM   1609  CD  PRO A 676       0.933 -29.407 -24.901  1.00 52.63           C  
ANISOU 1609  CD  PRO A 676     7837   6432   5727    681   -686   -713       C  
ATOM   1610  N   ASP A 677       5.418 -31.112 -24.781  1.00 52.97           N  
ANISOU 1610  N   ASP A 677     7898   6490   5739    998  -1200  -1046       N  
ATOM   1611  CA  ASP A 677       6.295 -32.216 -24.396  1.00 59.39           C  
ANISOU 1611  CA  ASP A 677     8819   7222   6525   1092  -1354  -1138       C  
ATOM   1612  C   ASP A 677       6.745 -32.082 -22.944  1.00 65.47           C  
ANISOU 1612  C   ASP A 677     9792   7849   7235   1141  -1422  -1136       C  
ATOM   1613  O   ASP A 677       7.583 -31.241 -22.618  1.00 71.71           O  
ANISOU 1613  O   ASP A 677    10543   8672   8031   1176  -1466  -1165       O  
ATOM   1614  CB  ASP A 677       7.515 -32.266 -25.321  1.00 91.24           C  
ANISOU 1614  CB  ASP A 677    12670  11388  10607   1152  -1458  -1252       C  
ATOM   1615  CG  ASP A 677       8.425 -33.445 -25.029  1.00103.38           C  
ANISOU 1615  CG  ASP A 677    14301  12850  12129   1253  -1625  -1360       C  
ATOM   1616  OD1 ASP A 677       8.036 -34.323 -24.230  1.00 99.57           O  
ANISOU 1616  OD1 ASP A 677    14022  12212  11597   1272  -1658  -1340       O  
ATOM   1617  OD2 ASP A 677       9.532 -33.495 -25.606  1.00113.04           O  
ANISOU 1617  OD2 ASP A 677    15393  14167  13391   1313  -1723  -1468       O  
ATOM   1618  N   LEU A 678       6.192 -32.924 -22.078  1.00 72.77           N  
ANISOU 1618  N   LEU A 678    10936   8614   8100   1141  -1432  -1104       N  
ATOM   1619  CA  LEU A 678       6.446 -32.829 -20.644  1.00 70.55           C  
ANISOU 1619  CA  LEU A 678    10870   8185   7750   1174  -1483  -1088       C  
ATOM   1620  C   LEU A 678       7.724 -33.548 -20.210  1.00 68.44           C  
ANISOU 1620  C   LEU A 678    10688   7854   7462   1291  -1675  -1193       C  
ATOM   1621  O   LEU A 678       7.990 -33.690 -19.017  1.00 74.04           O  
ANISOU 1621  O   LEU A 678    11598   8426   8107   1329  -1743  -1189       O  
ATOM   1622  CB  LEU A 678       5.241 -33.351 -19.857  1.00 63.71           C  
ANISOU 1622  CB  LEU A 678    10213   7174   6821   1111  -1399  -1002       C  
ATOM   1623  CG  LEU A 678       3.901 -32.704 -20.211  1.00 56.21           C  
ANISOU 1623  CG  LEU A 678     9190   6274   5893    996  -1210   -904       C  
ATOM   1624  CD1 LEU A 678       2.775 -33.277 -19.368  1.00 60.74           C  
ANISOU 1624  CD1 LEU A 678     9978   6699   6402    933  -1132   -833       C  
ATOM   1625  CD2 LEU A 678       3.973 -31.196 -20.047  1.00 48.10           C  
ANISOU 1625  CD2 LEU A 678     8065   5320   4889    966  -1138   -864       C  
ATOM   1626  N   SER A 679       8.513 -33.999 -21.180  1.00 66.07           N  
ANISOU 1626  N   SER A 679    10235   7652   7216   1346  -1766  -1292       N  
ATOM   1627  CA  SER A 679       9.804 -34.607 -20.880  1.00 62.92           C  
ANISOU 1627  CA  SER A 679     9884   7210   6814   1462  -1954  -1409       C  
ATOM   1628  C   SER A 679      10.863 -33.518 -20.768  1.00 68.26           C  
ANISOU 1628  C   SER A 679    10450   7969   7516   1505  -2000  -1461       C  
ATOM   1629  O   SER A 679      12.037 -33.798 -20.527  1.00 64.74           O  
ANISOU 1629  O   SER A 679    10017   7506   7076   1603  -2154  -1568       O  
ATOM   1630  CB  SER A 679      10.200 -35.613 -21.962  1.00 63.20           C  
ANISOU 1630  CB  SER A 679     9799   7313   6900   1504  -2034  -1504       C  
ATOM   1631  OG  SER A 679      10.497 -34.962 -23.184  1.00 62.24           O  
ANISOU 1631  OG  SER A 679     9413   7385   6850   1479  -1986  -1542       O  
ATOM   1632  N   LYS A 680      10.434 -32.272 -20.945  1.00 82.26           N  
ANISOU 1632  N   LYS A 680    12116   9830   9308   1431  -1866  -1389       N  
ATOM   1633  CA  LYS A 680      11.341 -31.133 -20.895  1.00 85.57           C  
ANISOU 1633  CA  LYS A 680    12421  10337   9756   1457  -1889  -1429       C  
ATOM   1634  C   LYS A 680      11.434 -30.545 -19.490  1.00 98.10           C  
ANISOU 1634  C   LYS A 680    14184  11804  11285   1473  -1900  -1387       C  
ATOM   1635  O   LYS A 680      12.432 -29.914 -19.139  1.00100.72           O  
ANISOU 1635  O   LYS A 680    14482  12160  11626   1528  -1974  -1447       O  
ATOM   1636  CB  LYS A 680      10.904 -30.057 -21.890  1.00 74.37           C  
ANISOU 1636  CB  LYS A 680    10783   9082   8393   1369  -1747  -1378       C  
ATOM   1637  CG  LYS A 680      10.872 -30.524 -23.338  1.00 77.91           C  
ANISOU 1637  CG  LYS A 680    11040   9666   8898   1349  -1734  -1422       C  
ATOM   1638  CD  LYS A 680      12.252 -30.934 -23.825  1.00 79.51           C  
ANISOU 1638  CD  LYS A 680    11136   9938   9136   1438  -1882  -1571       C  
ATOM   1639  CE  LYS A 680      12.239 -31.240 -25.313  1.00 76.18           C  
ANISOU 1639  CE  LYS A 680    10504   9670   8770   1408  -1855  -1616       C  
ATOM   1640  NZ  LYS A 680      13.588 -31.618 -25.813  1.00 85.32           N  
ANISOU 1640  NZ  LYS A 680    11546  10904   9967   1489  -1994  -1771       N  
ATOM   1641  N   VAL A 681      10.392 -30.751 -18.689  1.00 99.72           N  
ANISOU 1641  N   VAL A 681    14577  11883  11429   1421  -1825  -1288       N  
ATOM   1642  CA  VAL A 681      10.395 -30.274 -17.313  1.00 91.88           C  
ANISOU 1642  CA  VAL A 681    13769  10768  10371   1430  -1831  -1245       C  
ATOM   1643  C   VAL A 681      11.596 -30.870 -16.588  1.00 97.37           C  
ANISOU 1643  C   VAL A 681    14588  11374  11035   1548  -2023  -1345       C  
ATOM   1644  O   VAL A 681      11.961 -32.024 -16.818  1.00101.80           O  
ANISOU 1644  O   VAL A 681    15193  11893  11595   1608  -2137  -1413       O  
ATOM   1645  CB  VAL A 681       9.093 -30.650 -16.568  1.00 72.27           C  
ANISOU 1645  CB  VAL A 681    11487   8152   7819   1356  -1731  -1137       C  
ATOM   1646  CG1 VAL A 681       7.925 -30.734 -17.541  1.00 69.21           C  
ANISOU 1646  CG1 VAL A 681    10987   7839   7470   1260  -1585  -1072       C  
ATOM   1647  CG2 VAL A 681       9.259 -31.965 -15.829  1.00 70.97           C  
ANISOU 1647  CG2 VAL A 681    11554   7825   7586   1414  -1854  -1167       C  
ATOM   1648  N   ARG A 682      12.222 -30.078 -15.725  1.00 83.52           N  
ANISOU 1648  N   ARG A 682    12885   9590   9260   1585  -2064  -1358       N  
ATOM   1649  CA  ARG A 682      13.408 -30.536 -15.014  1.00 92.78           C  
ANISOU 1649  CA  ARG A 682    14166  10681  10406   1702  -2252  -1458       C  
ATOM   1650  C   ARG A 682      13.041 -31.450 -13.852  1.00 92.28           C  
ANISOU 1650  C   ARG A 682    14397  10419  10246   1721  -2313  -1420       C  
ATOM   1651  O   ARG A 682      11.928 -31.391 -13.329  1.00 88.83           O  
ANISOU 1651  O   ARG A 682    14091   9907   9754   1637  -2194  -1310       O  
ATOM   1652  CB  ARG A 682      14.233 -29.348 -14.518  1.00126.33           C  
ANISOU 1652  CB  ARG A 682    18359  14972  14667   1735  -2276  -1490       C  
ATOM   1653  CG  ARG A 682      14.819 -28.499 -15.631  1.00138.08           C  
ANISOU 1653  CG  ARG A 682    19565  16651  16248   1727  -2243  -1546       C  
ATOM   1654  CD  ARG A 682      15.672 -27.377 -15.069  1.00148.98           C  
ANISOU 1654  CD  ARG A 682    20906  18061  17640   1763  -2275  -1583       C  
ATOM   1655  NE  ARG A 682      16.278 -26.568 -16.122  1.00158.66           N  
ANISOU 1655  NE  ARG A 682    21867  19466  18950   1751  -2245  -1640       N  
ATOM   1656  CZ  ARG A 682      17.039 -25.503 -15.897  1.00167.12           C  
ANISOU 1656  CZ  ARG A 682    22853  20596  20049   1771  -2257  -1679       C  
ATOM   1657  NH1 ARG A 682      17.290 -25.116 -14.654  1.00169.66           N  
ANISOU 1657  NH1 ARG A 682    23328  20814  20322   1808  -2299  -1669       N  
ATOM   1658  NH2 ARG A 682      17.551 -24.824 -16.915  1.00169.44           N  
ANISOU 1658  NH2 ARG A 682    22910  21054  20417   1751  -2225  -1729       N  
ATOM   1659  N   SER A 683      13.985 -32.302 -13.463  1.00109.11           N  
ANISOU 1659  N   SER A 683    16633  12467  12358   1830  -2500  -1516       N  
ATOM   1660  CA  SER A 683      13.793 -33.210 -12.340  1.00109.17           C  
ANISOU 1660  CA  SER A 683    16931  12279  12270   1859  -2585  -1490       C  
ATOM   1661  C   SER A 683      13.428 -32.428 -11.085  1.00111.08           C  
ANISOU 1661  C   SER A 683    17339  12433  12435   1820  -2523  -1407       C  
ATOM   1662  O   SER A 683      12.593 -32.863 -10.292  1.00107.55           O  
ANISOU 1662  O   SER A 683    17112  11851  11902   1769  -2478  -1323       O  
ATOM   1663  CB  SER A 683      15.059 -34.034 -12.096  1.00 98.27           C  
ANISOU 1663  CB  SER A 683    15616  10832  10891   1997  -2815  -1619       C  
ATOM   1664  OG  SER A 683      15.392 -34.809 -13.234  1.00103.39           O  
ANISOU 1664  OG  SER A 683    16114  11558  11610   2033  -2876  -1703       O  
ATOM   1665  N   ASN A 684      14.057 -31.268 -10.916  1.00 99.62           N  
ANISOU 1665  N   ASN A 684    15779  11059  11013   1840  -2517  -1434       N  
ATOM   1666  CA  ASN A 684      13.789 -30.414  -9.766  1.00 93.17           C  
ANISOU 1666  CA  ASN A 684    15094  10175  10133   1806  -2457  -1365       C  
ATOM   1667  C   ASN A 684      12.467 -29.668  -9.887  1.00 85.78           C  
ANISOU 1667  C   ASN A 684    14117   9281   9195   1671  -2237  -1242       C  
ATOM   1668  O   ASN A 684      12.359 -28.515  -9.472  1.00 83.68           O  
ANISOU 1668  O   ASN A 684    13814   9049   8930   1634  -2154  -1203       O  
ATOM   1669  CB  ASN A 684      14.932 -29.417  -9.553  1.00100.04           C  
ANISOU 1669  CB  ASN A 684    15856  11115  11041   1875  -2528  -1442       C  
ATOM   1670  CG  ASN A 684      15.135 -28.491 -10.739  1.00104.03           C  
ANISOU 1670  CG  ASN A 684    16058  11815  11652   1845  -2442  -1468       C  
ATOM   1671  OD1 ASN A 684      14.228 -28.275 -11.541  1.00108.57           O  
ANISOU 1671  OD1 ASN A 684    16515  12472  12263   1752  -2294  -1399       O  
ATOM   1672  ND2 ASN A 684      16.335 -27.934 -10.850  1.00102.96           N  
ANISOU 1672  ND2 ASN A 684    15798  11756  11568   1921  -2537  -1570       N  
ATOM   1673  N   CYS A 685      11.469 -30.327 -10.467  1.00100.11           N  
ANISOU 1673  N   CYS A 685    15933  11094  11012   1600  -2147  -1185       N  
ATOM   1674  CA  CYS A 685      10.135 -29.750 -10.588  1.00108.60           C  
ANISOU 1674  CA  CYS A 685    16979  12198  12086   1472  -1942  -1074       C  
ATOM   1675  C   CYS A 685       9.161 -30.494  -9.682  1.00112.21           C  
ANISOU 1675  C   CYS A 685    17700  12493  12443   1414  -1897   -996       C  
ATOM   1676  O   CYS A 685       8.945 -31.691  -9.865  1.00111.51           O  
ANISOU 1676  O   CYS A 685    17706  12334  12329   1424  -1948  -1004       O  
ATOM   1677  CB  CYS A 685       9.644 -29.810 -12.037  1.00 98.67           C  
ANISOU 1677  CB  CYS A 685    15496  11079  10916   1422  -1851  -1067       C  
ATOM   1678  SG  CYS A 685       7.960 -29.175 -12.265  1.00 77.37           S  
ANISOU 1678  SG  CYS A 685    12755   8417   8227   1270  -1608   -938       S  
ATOM   1679  N   PRO A 686       8.580 -29.792  -8.695  1.00108.68           N  
ANISOU 1679  N   PRO A 686    17372  11984  11937   1351  -1802   -924       N  
ATOM   1680  CA  PRO A 686       7.604 -30.453  -7.825  1.00106.92           C  
ANISOU 1680  CA  PRO A 686    17400  11611  11614   1281  -1743   -851       C  
ATOM   1681  C   PRO A 686       6.614 -31.269  -8.626  1.00111.87           C  
ANISOU 1681  C   PRO A 686    17998  12247  12261   1212  -1656   -813       C  
ATOM   1682  O   PRO A 686       5.779 -30.714  -9.324  1.00115.45           O  
ANISOU 1682  O   PRO A 686    18294  12799  12773   1129  -1502   -767       O  
ATOM   1683  CB  PRO A 686       6.869 -29.284  -7.197  1.00 94.43           C  
ANISOU 1683  CB  PRO A 686    15826  10039  10015   1191  -1587   -777       C  
ATOM   1684  CG  PRO A 686       7.896 -28.218  -7.104  1.00 94.51           C  
ANISOU 1684  CG  PRO A 686    15713  10129  10069   1258  -1648   -828       C  
ATOM   1685  CD  PRO A 686       8.827 -28.397  -8.286  1.00 92.38           C  
ANISOU 1685  CD  PRO A 686    15229   9978   9892   1341  -1748   -913       C  
ATOM   1686  N   LYS A 687       6.682 -32.582  -8.493  1.00117.11           N  
ANISOU 1686  N   LYS A 687    18821  12802  12874   1245  -1754   -833       N  
ATOM   1687  CA  LYS A 687       5.820 -33.444  -9.275  1.00122.04           C  
ANISOU 1687  CA  LYS A 687    19419  13432  13520   1187  -1685   -807       C  
ATOM   1688  C   LYS A 687       4.359 -33.379  -8.807  1.00123.08           C  
ANISOU 1688  C   LYS A 687    19665  13501  13599   1053  -1501   -708       C  
ATOM   1689  O   LYS A 687       3.511 -34.149  -9.267  1.00125.39           O  
ANISOU 1689  O   LYS A 687    19976  13774  13893    993  -1433   -680       O  
ATOM   1690  CB  LYS A 687       6.380 -34.867  -9.320  1.00128.32           C  
ANISOU 1690  CB  LYS A 687    20339  14131  14286   1267  -1853   -864       C  
ATOM   1691  CG  LYS A 687       7.744 -34.943 -10.022  1.00126.69           C  
ANISOU 1691  CG  LYS A 687    19970  14012  14154   1394  -2019   -976       C  
ATOM   1692  CD  LYS A 687       8.294 -36.364 -10.033  1.00124.18           C  
ANISOU 1692  CD  LYS A 687    19779  13592  13812   1477  -2193  -1039       C  
ATOM   1693  CE  LYS A 687       9.684 -36.463 -10.640  1.00123.10           C  
ANISOU 1693  CE  LYS A 687    19491  13534  13748   1606  -2366  -1162       C  
ATOM   1694  NZ  LYS A 687      10.108 -37.880 -10.491  1.00125.69           N  
ANISOU 1694  NZ  LYS A 687    19977  13736  14044   1681  -2535  -1217       N  
ATOM   1695  N   ARG A 688       4.069 -32.435  -7.914  1.00107.16           N  
ANISOU 1695  N   ARG A 688    17716  11461  11541   1003  -1419   -662       N  
ATOM   1696  CA  ARG A 688       2.691 -32.073  -7.624  1.00 96.62           C  
ANISOU 1696  CA  ARG A 688    16423  10107  10182    870  -1223   -579       C  
ATOM   1697  C   ARG A 688       2.240 -31.013  -8.618  1.00 86.31           C  
ANISOU 1697  C   ARG A 688    14836   8969   8988    823  -1089   -563       C  
ATOM   1698  O   ARG A 688       1.046 -30.853  -8.867  1.00 68.44           O  
ANISOU 1698  O   ARG A 688    12533   6728   6743    719   -928   -509       O  
ATOM   1699  CB  ARG A 688       2.555 -31.538  -6.199  1.00103.53           C  
ANISOU 1699  CB  ARG A 688    17497  10878  10960    834  -1193   -541       C  
ATOM   1700  CG  ARG A 688       2.934 -32.540  -5.138  1.00108.38           C  
ANISOU 1700  CG  ARG A 688    18410  11317  11452    871  -1320   -548       C  
ATOM   1701  CD  ARG A 688       1.771 -32.832  -4.215  1.00115.93           C  
ANISOU 1701  CD  ARG A 688    19592  12151  12307    749  -1194   -476       C  
ATOM   1702  NE  ARG A 688       1.773 -31.916  -3.084  1.00117.50           N  
ANISOU 1702  NE  ARG A 688    19892  12310  12442    719  -1151   -452       N  
ATOM   1703  CZ  ARG A 688       0.682 -31.395  -2.536  1.00119.47           C  
ANISOU 1703  CZ  ARG A 688    20196  12540  12657    597   -976   -394       C  
ATOM   1704  NH1 ARG A 688      -0.516 -31.696  -3.016  1.00118.29           N  
ANISOU 1704  NH1 ARG A 688    20010  12405  12531    492   -826   -356       N  
ATOM   1705  NH2 ARG A 688       0.797 -30.568  -1.507  1.00123.66           N  
ANISOU 1705  NH2 ARG A 688    20815  13037  13132    580   -953   -381       N  
ATOM   1706  N   MET A 689       3.215 -30.287  -9.161  1.00102.42           N  
ANISOU 1706  N   MET A 689    16687  11127  11102    900  -1161   -613       N  
ATOM   1707  CA  MET A 689       3.003 -29.254 -10.169  1.00 97.85           C  
ANISOU 1707  CA  MET A 689    15834  10713  10631    870  -1063   -605       C  
ATOM   1708  C   MET A 689       2.626 -29.872 -11.507  1.00 93.86           C  
ANISOU 1708  C   MET A 689    15173  10294  10196    855  -1035   -615       C  
ATOM   1709  O   MET A 689       1.624 -29.502 -12.111  1.00 93.27           O  
ANISOU 1709  O   MET A 689    14979  10287  10171    770   -890   -568       O  
ATOM   1710  CB  MET A 689       4.297 -28.450 -10.340  1.00 90.15           C  
ANISOU 1710  CB  MET A 689    14723   9827   9704    963  -1169   -665       C  
ATOM   1711  CG  MET A 689       4.208 -27.278 -11.298  1.00 85.43           C  
ANISOU 1711  CG  MET A 689    13853   9395   9211    934  -1079   -656       C  
ATOM   1712  SD  MET A 689       3.186 -25.938 -10.668  1.00 99.67           S  
ANISOU 1712  SD  MET A 689    15651  11202  11017    828   -898   -574       S  
ATOM   1713  CE  MET A 689       4.046 -25.517  -9.160  1.00126.71           C  
ANISOU 1713  CE  MET A 689    19262  14523  14360    886   -991   -596       C  
ATOM   1714  N   LYS A 690       3.437 -30.823 -11.961  1.00 79.25           N  
ANISOU 1714  N   LYS A 690    13322   8440   8351    940  -1180   -680       N  
ATOM   1715  CA  LYS A 690       3.244 -31.429 -13.274  1.00 70.75           C  
ANISOU 1715  CA  LYS A 690    12085   7453   7343    939  -1172   -703       C  
ATOM   1716  C   LYS A 690       1.865 -32.065 -13.395  1.00 65.69           C  
ANISOU 1716  C   LYS A 690    11514   6761   6684    840  -1043   -643       C  
ATOM   1717  O   LYS A 690       1.223 -31.971 -14.440  1.00 73.45           O  
ANISOU 1717  O   LYS A 690    12324   7847   7737    790   -950   -627       O  
ATOM   1718  CB  LYS A 690       4.336 -32.457 -13.570  1.00 87.13           C  
ANISOU 1718  CB  LYS A 690    14180   9507   9417   1048  -1358   -791       C  
ATOM   1719  CG  LYS A 690       4.233 -33.072 -14.956  1.00103.56           C  
ANISOU 1719  CG  LYS A 690    16085  11691  11572   1052  -1358   -825       C  
ATOM   1720  CD  LYS A 690       5.394 -34.011 -15.250  1.00115.37           C  
ANISOU 1720  CD  LYS A 690    17584  13174  13076   1166  -1548   -925       C  
ATOM   1721  CE  LYS A 690       5.243 -34.657 -16.622  1.00124.93           C  
ANISOU 1721  CE  LYS A 690    18623  14488  14359   1164  -1543   -961       C  
ATOM   1722  NZ  LYS A 690       6.363 -35.582 -16.966  1.00128.44           N  
ANISOU 1722  NZ  LYS A 690    19055  14926  14819   1274  -1726  -1069       N  
ATOM   1723  N   ARG A 691       1.414 -32.711 -12.325  1.00 61.96           N  
ANISOU 1723  N   ARG A 691    11297   6129   6115    808  -1039   -611       N  
ATOM   1724  CA  ARG A 691       0.058 -33.239 -12.284  1.00 74.79           C  
ANISOU 1724  CA  ARG A 691    13007   7696   7715    702   -903   -553       C  
ATOM   1725  C   ARG A 691      -0.930 -32.110 -12.537  1.00 70.74           C  
ANISOU 1725  C   ARG A 691    12353   7272   7255    606   -720   -497       C  
ATOM   1726  O   ARG A 691      -1.874 -32.255 -13.312  1.00 63.48           O  
ANISOU 1726  O   ARG A 691    11329   6407   6385    538   -609   -473       O  
ATOM   1727  CB  ARG A 691      -0.239 -33.872 -10.927  1.00118.48           C  
ANISOU 1727  CB  ARG A 691    18847  13044  13126    672   -914   -523       C  
ATOM   1728  CG  ARG A 691      -1.585 -34.576 -10.867  1.00138.01           C  
ANISOU 1728  CG  ARG A 691    21424  15446  15568    562   -783   -473       C  
ATOM   1729  CD  ARG A 691      -2.040 -34.781  -9.434  1.00154.08           C  
ANISOU 1729  CD  ARG A 691    23743  17318  17482    501   -747   -430       C  
ATOM   1730  NE  ARG A 691      -0.912 -34.791  -8.508  1.00166.68           N  
ANISOU 1730  NE  ARG A 691    25493  18830  19006    589   -903   -457       N  
ATOM   1731  CZ  ARG A 691      -0.079 -35.815  -8.355  1.00173.65           C  
ANISOU 1731  CZ  ARG A 691    26505  19629  19847    676  -1076   -499       C  
ATOM   1732  NH1 ARG A 691      -0.240 -36.916  -9.076  1.00173.75           N  
ANISOU 1732  NH1 ARG A 691    26508  19628  19881    687  -1112   -519       N  
ATOM   1733  NH2 ARG A 691       0.920 -35.733  -7.488  1.00177.66           N  
ANISOU 1733  NH2 ARG A 691    27147  20062  20292    756  -1216   -525       N  
ATOM   1734  N   LEU A 692      -0.701 -30.981 -11.874  1.00 74.50           N  
ANISOU 1734  N   LEU A 692    12826   7759   7723    602   -694   -481       N  
ATOM   1735  CA  LEU A 692      -1.557 -29.812 -12.024  1.00 75.69           C  
ANISOU 1735  CA  LEU A 692    12846   7986   7926    518   -533   -433       C  
ATOM   1736  C   LEU A 692      -1.400 -29.203 -13.413  1.00 64.56           C  
ANISOU 1736  C   LEU A 692    11147   6750   6632    535   -516   -448       C  
ATOM   1737  O   LEU A 692      -2.381 -28.812 -14.045  1.00 59.17           O  
ANISOU 1737  O   LEU A 692    10337   6136   6008    459   -384   -412       O  
ATOM   1738  CB  LEU A 692      -1.233 -28.774 -10.948  1.00 75.11           C  
ANISOU 1738  CB  LEU A 692    12843   7879   7815    520   -527   -419       C  
ATOM   1739  CG  LEU A 692      -2.075 -27.498 -10.949  1.00 66.67           C  
ANISOU 1739  CG  LEU A 692    11655   6877   6800    437   -368   -373       C  
ATOM   1740  CD1 LEU A 692      -3.555 -27.821 -10.821  1.00 65.35           C  
ANISOU 1740  CD1 LEU A 692    11554   6659   6618    320   -211   -327       C  
ATOM   1741  CD2 LEU A 692      -1.632 -26.579  -9.830  1.00 63.14           C  
ANISOU 1741  CD2 LEU A 692    11293   6388   6311    450   -381   -368       C  
ATOM   1742  N   MET A 693      -0.158 -29.126 -13.880  1.00 48.22           N  
ANISOU 1742  N   MET A 693     8977   4750   4594    633   -650   -504       N  
ATOM   1743  CA  MET A 693       0.134 -28.626 -15.217  1.00 41.92           C  
ANISOU 1743  CA  MET A 693     7914   4118   3896    652   -649   -525       C  
ATOM   1744  C   MET A 693      -0.630 -29.430 -16.260  1.00 51.10           C  
ANISOU 1744  C   MET A 693     8995   5324   5098    612   -596   -520       C  
ATOM   1745  O   MET A 693      -1.358 -28.874 -17.080  1.00 50.03           O  
ANISOU 1745  O   MET A 693     8692   5287   5030    552   -487   -488       O  
ATOM   1746  CB  MET A 693       1.635 -28.713 -15.494  1.00 44.28           C  
ANISOU 1746  CB  MET A 693     8150   4465   4208    765   -816   -602       C  
ATOM   1747  CG  MET A 693       2.036 -28.244 -16.880  1.00 42.01           C  
ANISOU 1747  CG  MET A 693     7595   4352   4017    782   -822   -631       C  
ATOM   1748  SD  MET A 693       3.790 -28.490 -17.212  1.00 54.25           S  
ANISOU 1748  SD  MET A 693     9074   5956   5581    910  -1017   -739       S  
ATOM   1749  CE  MET A 693       4.508 -27.697 -15.777  1.00 37.93           C  
ANISOU 1749  CE  MET A 693     7149   3804   3459    952  -1072   -742       C  
ATOM   1750  N   ALA A 694      -0.457 -30.747 -16.217  1.00 54.19           N  
ANISOU 1750  N   ALA A 694     9508   5636   5445    646   -678   -552       N  
ATOM   1751  CA  ALA A 694      -1.138 -31.643 -17.142  1.00 59.93           C  
ANISOU 1751  CA  ALA A 694    10176   6391   6203    613   -639   -554       C  
ATOM   1752  C   ALA A 694      -2.651 -31.534 -16.990  1.00 65.96           C  
ANISOU 1752  C   ALA A 694    10976   7120   6965    498   -466   -487       C  
ATOM   1753  O   ALA A 694      -3.397 -31.729 -17.950  1.00 64.74           O  
ANISOU 1753  O   ALA A 694    10694   7038   6867    452   -388   -476       O  
ATOM   1754  CB  ALA A 694      -0.680 -33.072 -16.927  1.00 45.18           C  
ANISOU 1754  CB  ALA A 694     8464   4420   4281    671   -763   -600       C  
ATOM   1755  N   GLU A 695      -3.097 -31.229 -15.775  1.00 75.92           N  
ANISOU 1755  N   GLU A 695    12413   8272   8162    451   -406   -447       N  
ATOM   1756  CA  GLU A 695      -4.519 -31.061 -15.495  1.00 74.01           C  
ANISOU 1756  CA  GLU A 695    12214   7992   7916    337   -238   -392       C  
ATOM   1757  C   GLU A 695      -5.089 -29.828 -16.191  1.00 73.18           C  
ANISOU 1757  C   GLU A 695    11888   8016   7902    288   -123   -362       C  
ATOM   1758  O   GLU A 695      -6.246 -29.822 -16.613  1.00 73.44           O  
ANISOU 1758  O   GLU A 695    11860   8072   7973    208      3   -334       O  
ATOM   1759  CB  GLU A 695      -4.765 -30.975 -13.987  1.00 66.94           C  
ANISOU 1759  CB  GLU A 695    11558   6952   6924    299   -207   -364       C  
ATOM   1760  CG  GLU A 695      -4.934 -32.322 -13.307  1.00 67.97           C  
ANISOU 1760  CG  GLU A 695    11935   6930   6960    289   -246   -368       C  
ATOM   1761  CD  GLU A 695      -6.199 -33.036 -13.744  1.00 78.34           C  
ANISOU 1761  CD  GLU A 695    13254   8225   8288    199   -127   -349       C  
ATOM   1762  OE1 GLU A 695      -6.122 -34.239 -14.069  1.00 85.63           O  
ANISOU 1762  OE1 GLU A 695    14242   9104   9192    221   -189   -371       O  
ATOM   1763  OE2 GLU A 695      -7.269 -32.390 -13.769  1.00 76.75           O  
ANISOU 1763  OE2 GLU A 695    12988   8054   8120    107     28   -315       O  
ATOM   1764  N   CYS A 696      -4.272 -28.786 -16.303  1.00 67.49           N  
ANISOU 1764  N   CYS A 696    11049   7377   7217    337   -171   -371       N  
ATOM   1765  CA  CYS A 696      -4.680 -27.557 -16.974  1.00 58.42           C  
ANISOU 1765  CA  CYS A 696     9689   6350   6155    298    -80   -342       C  
ATOM   1766  C   CYS A 696      -4.484 -27.666 -18.484  1.00 47.12           C  
ANISOU 1766  C   CYS A 696     8038   5061   4804    323   -107   -363       C  
ATOM   1767  O   CYS A 696      -5.141 -26.970 -19.256  1.00 40.03           O  
ANISOU 1767  O   CYS A 696     6972   4258   3980    274    -17   -334       O  
ATOM   1768  CB  CYS A 696      -3.892 -26.361 -16.431  1.00 54.84           C  
ANISOU 1768  CB  CYS A 696     9208   5922   5707    335   -117   -341       C  
ATOM   1769  SG  CYS A 696      -4.111 -26.046 -14.663  1.00 59.29           S  
ANISOU 1769  SG  CYS A 696    10012   6334   6179    302    -79   -318       S  
ATOM   1770  N   LEU A 697      -3.577 -28.548 -18.894  1.00 48.53           N  
ANISOU 1770  N   LEU A 697     8221   5251   4968    398   -235   -415       N  
ATOM   1771  CA  LEU A 697      -3.266 -28.737 -20.308  1.00 49.34           C  
ANISOU 1771  CA  LEU A 697     8122   5487   5137    426   -273   -445       C  
ATOM   1772  C   LEU A 697      -4.166 -29.778 -20.969  1.00 50.11           C  
ANISOU 1772  C   LEU A 697     8214   5580   5247    384   -221   -444       C  
ATOM   1773  O   LEU A 697      -3.876 -30.248 -22.069  1.00 56.56           O  
ANISOU 1773  O   LEU A 697     8898   6487   6103    413   -267   -479       O  
ATOM   1774  CB  LEU A 697      -1.798 -29.135 -20.486  1.00 48.06           C  
ANISOU 1774  CB  LEU A 697     7946   5353   4962    530   -437   -515       C  
ATOM   1775  CG  LEU A 697      -0.751 -28.041 -20.292  1.00 42.08           C  
ANISOU 1775  CG  LEU A 697     7114   4654   4220    579   -497   -532       C  
ATOM   1776  CD1 LEU A 697       0.649 -28.595 -20.502  1.00 28.29           C  
ANISOU 1776  CD1 LEU A 697     5356   2931   2464    680   -661   -616       C  
ATOM   1777  CD2 LEU A 697      -1.018 -26.897 -21.249  1.00 47.10           C  
ANISOU 1777  CD2 LEU A 697     7523   5435   4937    537   -419   -502       C  
ATOM   1778  N   LYS A 698      -5.255 -30.135 -20.296  1.00 50.78           N  
ANISOU 1778  N   LYS A 698     8440   5558   5296    313   -122   -408       N  
ATOM   1779  CA  LYS A 698      -6.193 -31.124 -20.822  1.00 55.06           C  
ANISOU 1779  CA  LYS A 698     8991   6083   5847    266    -63   -407       C  
ATOM   1780  C   LYS A 698      -6.767 -30.700 -22.173  1.00 53.00           C  
ANISOU 1780  C   LYS A 698     8493   5967   5678    231      8   -396       C  
ATOM   1781  O   LYS A 698      -7.215 -29.565 -22.338  1.00 50.01           O  
ANISOU 1781  O   LYS A 698     8002   5652   5347    189     90   -358       O  
ATOM   1782  CB  LYS A 698      -7.328 -31.365 -19.822  1.00 53.09           C  
ANISOU 1782  CB  LYS A 698     8922   5702   5548    182     51   -369       C  
ATOM   1783  CG  LYS A 698      -6.953 -32.256 -18.647  1.00 51.98           C  
ANISOU 1783  CG  LYS A 698     9043   5403   5306    205    -18   -382       C  
ATOM   1784  CD  LYS A 698      -7.343 -33.701 -18.912  1.00 66.64           C  
ANISOU 1784  CD  LYS A 698    10986   7195   7137    194    -31   -403       C  
ATOM   1785  CE  LYS A 698      -6.821 -34.634 -17.832  1.00 76.44           C  
ANISOU 1785  CE  LYS A 698    12487   8280   8277    228   -126   -418       C  
ATOM   1786  NZ  LYS A 698      -5.346 -34.813 -17.923  1.00 82.89           N  
ANISOU 1786  NZ  LYS A 698    13294   9116   9084    345   -304   -467       N  
ATOM   1787  N   LYS A 699      -6.749 -31.617 -23.138  1.00 45.86           N  
ANISOU 1787  N   LYS A 699     7515   5112   4796    250    -29   -429       N  
ATOM   1788  CA  LYS A 699      -7.334 -31.351 -24.448  1.00 47.52           C  
ANISOU 1788  CA  LYS A 699     7513   5455   5087    216     33   -421       C  
ATOM   1789  C   LYS A 699      -8.810 -31.026 -24.277  1.00 46.55           C  
ANISOU 1789  C   LYS A 699     7397   5302   4988    119    189   -373       C  
ATOM   1790  O   LYS A 699      -9.346 -30.132 -24.934  1.00 47.09           O  
ANISOU 1790  O   LYS A 699     7303   5465   5122     80    262   -344       O  
ATOM   1791  CB  LYS A 699      -7.187 -32.564 -25.373  1.00 70.36           C  
ANISOU 1791  CB  LYS A 699    10358   8385   7991    245    -25   -469       C  
ATOM   1792  CG  LYS A 699      -5.756 -33.031 -25.623  1.00 81.01           C  
ANISOU 1792  CG  LYS A 699    11692   9766   9324    342   -183   -532       C  
ATOM   1793  CD  LYS A 699      -5.741 -34.292 -26.487  1.00 74.08           C  
ANISOU 1793  CD  LYS A 699    10774   8913   8458    364   -231   -583       C  
ATOM   1794  CE  LYS A 699      -4.332 -34.832 -26.693  1.00 65.34           C  
ANISOU 1794  CE  LYS A 699     9658   7831   7339    462   -392   -658       C  
ATOM   1795  NZ  LYS A 699      -3.480 -33.908 -27.490  1.00 68.54           N  
ANISOU 1795  NZ  LYS A 699     9862   8389   7789    495   -436   -679       N  
ATOM   1796  N   LYS A 700      -9.458 -31.762 -23.381  1.00 56.09           N  
ANISOU 1796  N   LYS A 700     8797   6372   6141     78    238   -367       N  
ATOM   1797  CA  LYS A 700     -10.886 -31.618 -23.143  1.00 56.79           C  
ANISOU 1797  CA  LYS A 700     8911   6420   6248    -18    388   -335       C  
ATOM   1798  C   LYS A 700     -11.170 -30.528 -22.117  1.00 61.93           C  
ANISOU 1798  C   LYS A 700     9625   7020   6884    -58    458   -298       C  
ATOM   1799  O   LYS A 700     -10.662 -30.558 -20.997  1.00 55.93           O  
ANISOU 1799  O   LYS A 700     9037   6161   6053    -39    418   -297       O  
ATOM   1800  CB  LYS A 700     -11.480 -32.950 -22.690  1.00 48.70           C  
ANISOU 1800  CB  LYS A 700     8062   5273   5170    -53    416   -350       C  
ATOM   1801  CG  LYS A 700     -10.956 -34.134 -23.487  1.00 54.73           C  
ANISOU 1801  CG  LYS A 700     8800   6062   5932      3    318   -394       C  
ATOM   1802  CD  LYS A 700     -11.655 -35.427 -23.106  1.00 60.67           C  
ANISOU 1802  CD  LYS A 700     9718   6695   6640    -40    355   -407       C  
ATOM   1803  CE  LYS A 700     -11.086 -36.602 -23.889  1.00 67.17           C  
ANISOU 1803  CE  LYS A 700    10515   7540   7466     20    249   -455       C  
ATOM   1804  NZ  LYS A 700     -11.785 -37.884 -23.588  1.00 71.14           N  
ANISOU 1804  NZ  LYS A 700    11172   7926   7930    -24    285   -466       N  
ATOM   1805  N   ARG A 701     -11.994 -29.572 -22.526  1.00 69.27           N  
ANISOU 1805  N   ARG A 701    10415   8019   7886   -112    560   -271       N  
ATOM   1806  CA  ARG A 701     -12.327 -28.399 -21.729  1.00 64.36           C  
ANISOU 1806  CA  ARG A 701     9811   7370   7271   -152    632   -239       C  
ATOM   1807  C   ARG A 701     -12.760 -28.706 -20.294  1.00 74.19           C  
ANISOU 1807  C   ARG A 701    11288   8464   8438   -201    690   -236       C  
ATOM   1808  O   ARG A 701     -12.230 -28.134 -19.340  1.00 68.37           O  
ANISOU 1808  O   ARG A 701    10646   7675   7657   -184    664   -226       O  
ATOM   1809  CB  ARG A 701     -13.431 -27.614 -22.436  1.00 61.92           C  
ANISOU 1809  CB  ARG A 701     9331   7142   7056   -214    745   -219       C  
ATOM   1810  CG  ARG A 701     -14.247 -26.746 -21.511  1.00 70.92           C  
ANISOU 1810  CG  ARG A 701    10523   8221   8204   -283    856   -198       C  
ATOM   1811  CD  ARG A 701     -15.541 -26.321 -22.165  1.00 73.99           C  
ANISOU 1811  CD  ARG A 701    10770   8661   8681   -351    973   -191       C  
ATOM   1812  NE  ARG A 701     -15.314 -25.392 -23.264  1.00 78.93           N  
ANISOU 1812  NE  ARG A 701    11177   9423   9391   -322    941   -172       N  
ATOM   1813  CZ  ARG A 701     -16.280 -24.720 -23.878  1.00 80.12           C  
ANISOU 1813  CZ  ARG A 701    11181   9632   9629   -368   1021   -160       C  
ATOM   1814  NH1 ARG A 701     -17.540 -24.875 -23.497  1.00 78.05           N  
ANISOU 1814  NH1 ARG A 701    10961   9309   9387   -445   1141   -173       N  
ATOM   1815  NH2 ARG A 701     -15.986 -23.893 -24.870  1.00 80.64           N  
ANISOU 1815  NH2 ARG A 701    11061   9817   9762   -340    980   -138       N  
ATOM   1816  N   ASP A 702     -13.727 -29.608 -20.153  1.00 87.96           N  
ANISOU 1816  N   ASP A 702    13121  10136  10162   -264    770   -246       N  
ATOM   1817  CA  ASP A 702     -14.374 -29.863 -18.867  1.00 91.81           C  
ANISOU 1817  CA  ASP A 702    13818  10486  10580   -335    853   -242       C  
ATOM   1818  C   ASP A 702     -13.523 -30.697 -17.913  1.00 85.85           C  
ANISOU 1818  C   ASP A 702    13293   9613   9713   -294    757   -251       C  
ATOM   1819  O   ASP A 702     -13.866 -30.852 -16.741  1.00 89.44           O  
ANISOU 1819  O   ASP A 702    13941   9949  10094   -347    809   -244       O  
ATOM   1820  CB  ASP A 702     -15.738 -30.527 -19.079  1.00104.10           C  
ANISOU 1820  CB  ASP A 702    15387  12010  12158   -424    979   -254       C  
ATOM   1821  CG  ASP A 702     -16.746 -29.590 -19.712  1.00112.43           C  
ANISOU 1821  CG  ASP A 702    16249  13153  13317   -478   1091   -247       C  
ATOM   1822  OD1 ASP A 702     -16.422 -28.395 -19.870  1.00117.39           O  
ANISOU 1822  OD1 ASP A 702    16753  13855  13994   -452   1075   -228       O  
ATOM   1823  OD2 ASP A 702     -17.859 -30.046 -20.047  1.00113.58           O  
ANISOU 1823  OD2 ASP A 702    16368  13292  13497   -546   1190   -264       O  
ATOM   1824  N   GLU A 703     -12.414 -31.228 -18.419  1.00 72.64           N  
ANISOU 1824  N   GLU A 703    11599   7974   8028   -202    615   -268       N  
ATOM   1825  CA  GLU A 703     -11.501 -32.019 -17.601  1.00 68.22           C  
ANISOU 1825  CA  GLU A 703    11245   7307   7370   -148    501   -282       C  
ATOM   1826  C   GLU A 703     -10.459 -31.148 -16.896  1.00 53.93           C  
ANISOU 1826  C   GLU A 703     9469   5492   5528    -89    420   -275       C  
ATOM   1827  O   GLU A 703      -9.491 -31.660 -16.331  1.00 57.32           O  
ANISOU 1827  O   GLU A 703    10039   5853   5888    -24    299   -291       O  
ATOM   1828  CB  GLU A 703     -10.804 -33.089 -18.450  1.00 90.43           C  
ANISOU 1828  CB  GLU A 703    14024  10150  10187    -75    380   -316       C  
ATOM   1829  CG  GLU A 703     -11.725 -34.202 -18.932  1.00 95.73           C  
ANISOU 1829  CG  GLU A 703    14717  10791  10867   -128    442   -328       C  
ATOM   1830  CD  GLU A 703     -10.988 -35.306 -19.675  1.00 94.28           C  
ANISOU 1830  CD  GLU A 703    14515  10625  10683    -52    315   -367       C  
ATOM   1831  OE1 GLU A 703     -11.644 -36.287 -20.080  1.00 93.26           O  
ANISOU 1831  OE1 GLU A 703    14407  10469  10559    -88    352   -380       O  
ATOM   1832  OE2 GLU A 703      -9.756 -35.197 -19.854  1.00 91.28           O  
ANISOU 1832  OE2 GLU A 703    14096  10287  10301     42    179   -389       O  
ATOM   1833  N   ARG A 704     -10.667 -29.833 -16.934  1.00 49.66           N  
ANISOU 1833  N   ARG A 704     8800   5024   5045   -110    484   -254       N  
ATOM   1834  CA  ARG A 704      -9.743 -28.881 -16.323  1.00 50.62           C  
ANISOU 1834  CA  ARG A 704     8931   5154   5149    -59    419   -248       C  
ATOM   1835  C   ARG A 704     -10.267 -28.372 -14.985  1.00 61.74           C  
ANISOU 1835  C   ARG A 704    10497   6460   6501   -125    506   -226       C  
ATOM   1836  O   ARG A 704     -11.463 -28.119 -14.832  1.00 55.67           O  
ANISOU 1836  O   ARG A 704     9720   5676   5756   -218    647   -212       O  
ATOM   1837  CB  ARG A 704      -9.493 -27.697 -17.257  1.00 39.16           C  
ANISOU 1837  CB  ARG A 704     7231   3852   3798    -33    419   -239       C  
ATOM   1838  CG  ARG A 704      -8.923 -28.071 -18.609  1.00 35.44           C  
ANISOU 1838  CG  ARG A 704     6591   3495   3381     27    335   -262       C  
ATOM   1839  CD  ARG A 704      -8.553 -26.820 -19.381  1.00 41.44           C  
ANISOU 1839  CD  ARG A 704     7130   4392   4223     50    328   -250       C  
ATOM   1840  NE  ARG A 704      -8.030 -27.115 -20.710  1.00 54.49           N  
ANISOU 1840  NE  ARG A 704     8614   6163   5926     99    256   -273       N  
ATOM   1841  CZ  ARG A 704      -8.626 -26.758 -21.843  1.00 56.05           C  
ANISOU 1841  CZ  ARG A 704     8622   6471   6204     67    314   -258       C  
ATOM   1842  NH1 ARG A 704      -9.769 -26.088 -21.812  1.00 61.82           N  
ANISOU 1842  NH1 ARG A 704     9303   7205   6980    -10    440   -223       N  
ATOM   1843  NH2 ARG A 704      -8.075 -27.066 -23.008  1.00 43.58           N  
ANISOU 1843  NH2 ARG A 704     6901   4999   4659    110    243   -283       N  
ATOM   1844  N   PRO A 705      -9.365 -28.233 -14.005  1.00 53.70           N  
ANISOU 1844  N   PRO A 705     9621   5374   5409    -77    421   -230       N  
ATOM   1845  CA  PRO A 705      -9.709 -27.747 -12.666  1.00 50.96           C  
ANISOU 1845  CA  PRO A 705     9435   4930   4998   -133    489   -214       C  
ATOM   1846  C   PRO A 705      -9.851 -26.231 -12.650  1.00 61.88           C  
ANISOU 1846  C   PRO A 705    10669   6391   6451   -149    553   -198       C  
ATOM   1847  O   PRO A 705      -9.077 -25.544 -13.314  1.00 63.64           O  
ANISOU 1847  O   PRO A 705    10728   6717   6736    -81    481   -201       O  
ATOM   1848  CB  PRO A 705      -8.499 -28.169 -11.818  1.00 73.48           C  
ANISOU 1848  CB  PRO A 705    12468   7697   7753    -54    345   -228       C  
ATOM   1849  CG  PRO A 705      -7.755 -29.171 -12.652  1.00 75.60           C  
ANISOU 1849  CG  PRO A 705    12704   7992   8027     27    216   -256       C  
ATOM   1850  CD  PRO A 705      -7.991 -28.751 -14.060  1.00 69.97           C  
ANISOU 1850  CD  PRO A 705    11726   7429   7431     31    249   -258       C  
ATOM   1851  N   SER A 706     -10.831 -25.718 -11.912  1.00 71.17           N  
ANISOU 1851  N   SER A 706    11902   7520   7621   -241    686   -184       N  
ATOM   1852  CA  SER A 706     -11.011 -24.274 -11.803  1.00 62.82           C  
ANISOU 1852  CA  SER A 706    10715   6524   6630   -259    748   -172       C  
ATOM   1853  C   SER A 706      -9.816 -23.638 -11.098  1.00 57.39           C  
ANISOU 1853  C   SER A 706    10080   5824   5902   -187    645   -174       C  
ATOM   1854  O   SER A 706      -9.007 -24.332 -10.482  1.00 51.88           O  
ANISOU 1854  O   SER A 706     9551   5050   5113   -136    543   -186       O  
ATOM   1855  CB  SER A 706     -12.314 -23.935 -11.071  1.00105.18           C  
ANISOU 1855  CB  SER A 706    16141  11830  11991   -374    911   -168       C  
ATOM   1856  OG  SER A 706     -12.290 -24.388  -9.728  1.00113.62           O  
ANISOU 1856  OG  SER A 706    17462  12768  12941   -408    920   -172       O  
ATOM   1857  N   PHE A 707      -9.706 -22.318 -11.199  1.00 67.43           N  
ANISOU 1857  N   PHE A 707    11205   7169   7245   -180    668   -165       N  
ATOM   1858  CA  PHE A 707      -8.588 -21.598 -10.597  1.00 67.75           C  
ANISOU 1858  CA  PHE A 707    11271   7210   7261   -112    576   -170       C  
ATOM   1859  C   PHE A 707      -8.574 -21.635  -9.067  1.00 76.76           C  
ANISOU 1859  C   PHE A 707    12644   8226   8296   -141    593   -174       C  
ATOM   1860  O   PHE A 707      -7.503 -21.661  -8.464  1.00 87.99           O  
ANISOU 1860  O   PHE A 707    14165   9611   9655    -71    481   -186       O  
ATOM   1861  CB  PHE A 707      -8.521 -20.154 -11.103  1.00 55.18           C  
ANISOU 1861  CB  PHE A 707     9464   5725   5775   -104    602   -158       C  
ATOM   1862  CG  PHE A 707      -7.587 -19.965 -12.266  1.00 48.69           C  
ANISOU 1862  CG  PHE A 707     8464   5020   5017    -22    497   -163       C  
ATOM   1863  CD1 PHE A 707      -6.220 -20.124 -12.103  1.00 45.35           C  
ANISOU 1863  CD1 PHE A 707     8082   4599   4551     71    356   -186       C  
ATOM   1864  CD2 PHE A 707      -8.072 -19.622 -13.517  1.00 43.74           C  
ANISOU 1864  CD2 PHE A 707     7627   4501   4492    -40    539   -148       C  
ATOM   1865  CE1 PHE A 707      -5.354 -19.951 -13.169  1.00 40.49           C  
ANISOU 1865  CE1 PHE A 707     7299   4093   3992    140    264   -198       C  
ATOM   1866  CE2 PHE A 707      -7.210 -19.445 -14.587  1.00 47.10           C  
ANISOU 1866  CE2 PHE A 707     7892   5036   4969     27    446   -153       C  
ATOM   1867  CZ  PHE A 707      -5.851 -19.610 -14.412  1.00 45.22           C  
ANISOU 1867  CZ  PHE A 707     7694   4801   4687    115    312   -180       C  
ATOM   1868  N   PRO A 708      -9.759 -21.623  -8.430  1.00 71.49           N  
ANISOU 1868  N   PRO A 708    12061   7494   7607   -245    733   -168       N  
ATOM   1869  CA  PRO A 708      -9.747 -21.815  -6.977  1.00 68.18           C  
ANISOU 1869  CA  PRO A 708    11882   6951   7071   -279    747   -172       C  
ATOM   1870  C   PRO A 708      -8.988 -23.090  -6.624  1.00 62.41           C  
ANISOU 1870  C   PRO A 708    11351   6132   6229   -226    626   -180       C  
ATOM   1871  O   PRO A 708      -8.154 -23.086  -5.717  1.00 49.82           O  
ANISOU 1871  O   PRO A 708     9905   4474   4552   -180    539   -186       O  
ATOM   1872  CB  PRO A 708     -11.231 -21.964  -6.635  1.00 52.30           C  
ANISOU 1872  CB  PRO A 708     9923   4891   5056   -407    918   -172       C  
ATOM   1873  CG  PRO A 708     -11.932 -21.181  -7.691  1.00 49.45           C  
ANISOU 1873  CG  PRO A 708     9309   4644   4835   -431    998   -168       C  
ATOM   1874  CD  PRO A 708     -11.114 -21.354  -8.943  1.00 52.70           C  
ANISOU 1874  CD  PRO A 708     9562   5152   5307   -336    881   -161       C  
ATOM   1875  N   ARG A 709      -9.273 -24.166  -7.352  1.00 63.46           N  
ANISOU 1875  N   ARG A 709    11484   6263   6363   -230    615   -180       N  
ATOM   1876  CA  ARG A 709      -8.571 -25.430  -7.171  1.00 74.31           C  
ANISOU 1876  CA  ARG A 709    13029   7558   7646   -175    492   -189       C  
ATOM   1877  C   ARG A 709      -7.083 -25.268  -7.473  1.00 71.74           C  
ANISOU 1877  C   ARG A 709    12644   7281   7332    -44    319   -208       C  
ATOM   1878  O   ARG A 709      -6.233 -25.705  -6.699  1.00 73.34           O  
ANISOU 1878  O   ARG A 709    13021   7401   7443     11    206   -221       O  
ATOM   1879  CB  ARG A 709      -9.166 -26.506  -8.081  1.00 90.90           C  
ANISOU 1879  CB  ARG A 709    15098   9668   9772   -200    516   -190       C  
ATOM   1880  CG  ARG A 709     -10.673 -26.699  -7.951  1.00101.20           C  
ANISOU 1880  CG  ARG A 709    16434  10938  11081   -329    691   -181       C  
ATOM   1881  CD  ARG A 709     -11.053 -27.469  -6.693  1.00108.05           C  
ANISOU 1881  CD  ARG A 709    17589  11652  11814   -399    729   -176       C  
ATOM   1882  NE  ARG A 709     -12.338 -28.149  -6.846  1.00113.59           N  
ANISOU 1882  NE  ARG A 709    18327  12316  12514   -507    863   -176       N  
ATOM   1883  CZ  ARG A 709     -12.472 -29.423  -7.205  1.00116.40           C  
ANISOU 1883  CZ  ARG A 709    18767  12623  12836   -511    833   -179       C  
ATOM   1884  NH1 ARG A 709     -11.397 -30.164  -7.443  1.00112.26           N  
ANISOU 1884  NH1 ARG A 709    18298  12079  12277   -409    669   -183       N  
ATOM   1885  NH2 ARG A 709     -13.679 -29.959  -7.324  1.00117.21           N  
ANISOU 1885  NH2 ARG A 709    18896  12696  12943   -615    966   -182       N  
ATOM   1886  N   ILE A 710      -6.778 -24.640  -8.604  1.00 70.37           N  
ANISOU 1886  N   ILE A 710    12224   7242   7270      2    298   -213       N  
ATOM   1887  CA  ILE A 710      -5.397 -24.419  -9.017  1.00 69.74           C  
ANISOU 1887  CA  ILE A 710    12057   7226   7214    118    145   -239       C  
ATOM   1888  C   ILE A 710      -4.635 -23.591  -7.987  1.00 76.75           C  
ANISOU 1888  C   ILE A 710    13020   8081   8060    156     94   -246       C  
ATOM   1889  O   ILE A 710      -3.462 -23.845  -7.716  1.00 74.96           O  
ANISOU 1889  O   ILE A 710    12860   7832   7791    247    -51   -275       O  
ATOM   1890  CB  ILE A 710      -5.331 -23.694 -10.373  1.00 57.44           C  
ANISOU 1890  CB  ILE A 710    10215   5824   5784    139    157   -238       C  
ATOM   1891  CG1 ILE A 710      -6.289 -24.341 -11.374  1.00 52.52           C  
ANISOU 1891  CG1 ILE A 710     9503   5240   5210     87    233   -228       C  
ATOM   1892  CG2 ILE A 710      -3.908 -23.687 -10.907  1.00 62.99           C  
ANISOU 1892  CG2 ILE A 710    10831   6594   6507    254     -2   -274       C  
ATOM   1893  CD1 ILE A 710      -6.258 -23.705 -12.741  1.00 47.96           C  
ANISOU 1893  CD1 ILE A 710     8657   4814   4751    104    242   -225       C  
ATOM   1894  N   LEU A 711      -5.309 -22.594  -7.421  1.00 74.49           N  
ANISOU 1894  N   LEU A 711    12718   7794   7791     86    212   -226       N  
ATOM   1895  CA  LEU A 711      -4.705 -21.730  -6.413  1.00 72.63           C  
ANISOU 1895  CA  LEU A 711    12547   7528   7520    111    181   -232       C  
ATOM   1896  C   LEU A 711      -4.454 -22.515  -5.131  1.00 71.10           C  
ANISOU 1896  C   LEU A 711    12641   7190   7186    113    128   -239       C  
ATOM   1897  O   LEU A 711      -3.331 -22.567  -4.631  1.00 67.11           O  
ANISOU 1897  O   LEU A 711    12219   6651   6629    198     -6   -263       O  
ATOM   1898  CB  LEU A 711      -5.603 -20.522  -6.131  1.00 75.62           C  
ANISOU 1898  CB  LEU A 711    12840   7938   7955     28    328   -212       C  
ATOM   1899  CG  LEU A 711      -5.085 -19.496  -5.121  1.00 76.82           C  
ANISOU 1899  CG  LEU A 711    13037   8069   8083     46    314   -220       C  
ATOM   1900  CD1 LEU A 711      -3.726 -18.958  -5.545  1.00 77.64           C  
ANISOU 1900  CD1 LEU A 711    13020   8250   8230    157    177   -242       C  
ATOM   1901  CD2 LEU A 711      -6.084 -18.360  -4.938  1.00 74.58           C  
ANISOU 1901  CD2 LEU A 711    12654   7816   7865    -42    466   -204       C  
ATOM   1902  N   ALA A 712      -5.509 -23.129  -4.606  1.00 75.72           N  
ANISOU 1902  N   ALA A 712    13377   7686   7707     16    232   -220       N  
ATOM   1903  CA  ALA A 712      -5.396 -23.966  -3.420  1.00 72.82           C  
ANISOU 1903  CA  ALA A 712    13299   7173   7198      1    192   -219       C  
ATOM   1904  C   ALA A 712      -4.292 -24.998  -3.599  1.00 70.73           C  
ANISOU 1904  C   ALA A 712    13123   6868   6884    107     10   -242       C  
ATOM   1905  O   ALA A 712      -3.453 -25.182  -2.719  1.00 75.70           O  
ANISOU 1905  O   ALA A 712    13920   7419   7425    164   -101   -256       O  
ATOM   1906  CB  ALA A 712      -6.718 -24.652  -3.128  1.00 47.68           C  
ANISOU 1906  CB  ALA A 712    10239   3913   3966   -121    330   -198       C  
ATOM   1907  N   GLU A 713      -4.297 -25.671  -4.744  1.00 59.88           N  
ANISOU 1907  N   GLU A 713    11634   5549   5568    135    -21   -249       N  
ATOM   1908  CA  GLU A 713      -3.290 -26.683  -5.033  1.00 66.20           C  
ANISOU 1908  CA  GLU A 713    12497   6320   6336    236   -193   -278       C  
ATOM   1909  C   GLU A 713      -1.878 -26.125  -4.910  1.00 69.63           C  
ANISOU 1909  C   GLU A 713    12881   6792   6782    354   -342   -315       C  
ATOM   1910  O   GLU A 713      -1.092 -26.596  -4.093  1.00 77.83           O  
ANISOU 1910  O   GLU A 713    14105   7736   7731    414   -467   -335       O  
ATOM   1911  CB  GLU A 713      -3.511 -27.283  -6.421  1.00101.89           C  
ANISOU 1911  CB  GLU A 713    16852  10922  10940    248   -193   -286       C  
ATOM   1912  CG  GLU A 713      -4.776 -28.110  -6.521  1.00118.10           C  
ANISOU 1912  CG  GLU A 713    18984  12919  12969    145    -73   -259       C  
ATOM   1913  CD  GLU A 713      -4.781 -29.265  -5.546  1.00127.47           C  
ANISOU 1913  CD  GLU A 713    20468  13943  14022    129   -124   -254       C  
ATOM   1914  OE1 GLU A 713      -3.700 -29.847  -5.317  1.00125.13           O  
ANISOU 1914  OE1 GLU A 713    20273  13595  13676    226   -291   -280       O  
ATOM   1915  OE2 GLU A 713      -5.861 -29.593  -5.012  1.00133.12           O  
ANISOU 1915  OE2 GLU A 713    21316  14581  14683     19      1   -226       O  
ATOM   1916  N   ILE A 714      -1.561 -25.117  -5.715  1.00 79.50           N  
ANISOU 1916  N   ILE A 714    13883   8180   8143    386   -332   -327       N  
ATOM   1917  CA  ILE A 714      -0.227 -24.526  -5.701  1.00 79.06           C  
ANISOU 1917  CA  ILE A 714    13753   8174   8111    493   -464   -368       C  
ATOM   1918  C   ILE A 714       0.138 -23.973  -4.324  1.00 77.70           C  
ANISOU 1918  C   ILE A 714    13744   7920   7859    500   -487   -369       C  
ATOM   1919  O   ILE A 714       1.284 -24.081  -3.885  1.00 80.97           O  
ANISOU 1919  O   ILE A 714    14231   8302   8233    595   -635   -409       O  
ATOM   1920  CB  ILE A 714      -0.088 -23.419  -6.763  1.00 71.79           C  
ANISOU 1920  CB  ILE A 714    12541   7414   7321    505   -424   -372       C  
ATOM   1921  CG1 ILE A 714      -0.425 -23.975  -8.148  1.00 58.40           C  
ANISOU 1921  CG1 ILE A 714    10685   5804   5700    498   -406   -373       C  
ATOM   1922  CG2 ILE A 714       1.316 -22.841  -6.750  1.00 73.28           C  
ANISOU 1922  CG2 ILE A 714    12655   7655   7534    612   -560   -421       C  
ATOM   1923  CD1 ILE A 714      -0.101 -23.034  -9.283  1.00 58.48           C  
ANISOU 1923  CD1 ILE A 714    10418   5972   5830    522   -396   -382       C  
ATOM   1924  N   GLU A 715      -0.843 -23.389  -3.645  1.00 73.42           N  
ANISOU 1924  N   GLU A 715    13258   7344   7294    400   -342   -330       N  
ATOM   1925  CA  GLU A 715      -0.632 -22.817  -2.321  1.00 81.55           C  
ANISOU 1925  CA  GLU A 715    14440   8300   8247    392   -343   -329       C  
ATOM   1926  C   GLU A 715      -0.316 -23.924  -1.322  1.00 87.69           C  
ANISOU 1926  C   GLU A 715    15510   8925   8882    412   -440   -335       C  
ATOM   1927  O   GLU A 715       0.572 -23.787  -0.479  1.00 97.77           O  
ANISOU 1927  O   GLU A 715    16907  10147  10094    477   -550   -359       O  
ATOM   1928  CB  GLU A 715      -1.877 -22.049  -1.874  1.00 90.14           C  
ANISOU 1928  CB  GLU A 715    15520   9385   9344    268   -155   -291       C  
ATOM   1929  CG  GLU A 715      -1.617 -20.968  -0.835  1.00 94.80           C  
ANISOU 1929  CG  GLU A 715    16154   9959   9909    264   -137   -297       C  
ATOM   1930  CD  GLU A 715      -1.371 -19.605  -1.457  1.00 89.81           C  
ANISOU 1930  CD  GLU A 715    15262   9458   9403    288   -107   -305       C  
ATOM   1931  OE1 GLU A 715      -0.199 -19.281  -1.743  1.00 90.69           O  
ANISOU 1931  OE1 GLU A 715    15285   9624   9550    390   -232   -338       O  
ATOM   1932  OE2 GLU A 715      -2.350 -18.856  -1.658  1.00 83.14           O  
ANISOU 1932  OE2 GLU A 715    14302   8661   8625    203     41   -281       O  
ATOM   1933  N   GLU A 716      -1.053 -25.025  -1.427  1.00 85.10           N  
ANISOU 1933  N   GLU A 716    15299   8528   8506    355   -401   -312       N  
ATOM   1934  CA  GLU A 716      -0.825 -26.184  -0.575  1.00 93.70           C  
ANISOU 1934  CA  GLU A 716    16673   9467   9460    367   -494   -312       C  
ATOM   1935  C   GLU A 716       0.494 -26.889  -0.893  1.00 93.25           C  
ANISOU 1935  C   GLU A 716    16634   9399   9399    504   -705   -359       C  
ATOM   1936  O   GLU A 716       1.217 -27.287   0.017  1.00101.91           O  
ANISOU 1936  O   GLU A 716    17934  10391  10398    560   -831   -376       O  
ATOM   1937  CB  GLU A 716      -1.997 -27.165  -0.663  1.00 97.24           C  
ANISOU 1937  CB  GLU A 716    17233   9847   9865    263   -389   -277       C  
ATOM   1938  CG  GLU A 716      -3.229 -26.746   0.132  1.00 96.45           C  
ANISOU 1938  CG  GLU A 716    17228   9702   9718    122   -204   -239       C  
ATOM   1939  CD  GLU A 716      -4.414 -27.656  -0.124  1.00 91.48           C  
ANISOU 1939  CD  GLU A 716    16668   9024   9066     17    -89   -212       C  
ATOM   1940  OE1 GLU A 716      -4.480 -28.242  -1.225  1.00 83.32           O  
ANISOU 1940  OE1 GLU A 716    15511   8043   8102     43   -110   -219       O  
ATOM   1941  OE2 GLU A 716      -5.277 -27.784   0.771  1.00 89.28           O  
ANISOU 1941  OE2 GLU A 716    16565   8658   8700    -94     24   -188       O  
ATOM   1942  N   LEU A 717       0.818 -27.046  -2.172  1.00 83.74           N  
ANISOU 1942  N   LEU A 717    15220   8300   8299    560   -747   -385       N  
ATOM   1943  CA  LEU A 717       2.094 -27.662  -2.527  1.00 80.59           C  
ANISOU 1943  CA  LEU A 717    14813   7900   7908    691   -946   -443       C  
ATOM   1944  C   LEU A 717       3.238 -26.665  -2.377  1.00 83.46           C  
ANISOU 1944  C   LEU A 717    15070   8331   8312    784  -1038   -488       C  
ATOM   1945  O   LEU A 717       4.384 -26.967  -2.706  1.00 90.28           O  
ANISOU 1945  O   LEU A 717    15890   9215   9197    898  -1200   -549       O  
ATOM   1946  CB  LEU A 717       2.063 -28.232  -3.947  1.00 75.82           C  
ANISOU 1946  CB  LEU A 717    14025   7387   7398    716   -960   -462       C  
ATOM   1947  CG  LEU A 717       1.829 -27.242  -5.089  1.00 63.55           C  
ANISOU 1947  CG  LEU A 717    12164   6004   5978    696   -863   -460       C  
ATOM   1948  CD1 LEU A 717       3.141 -26.853  -5.766  1.00 58.18           C  
ANISOU 1948  CD1 LEU A 717    11305   5428   5374    814   -998   -526       C  
ATOM   1949  CD2 LEU A 717       0.856 -27.846  -6.089  1.00 65.19           C  
ANISOU 1949  CD2 LEU A 717    12281   6253   6235    630   -765   -435       C  
ATOM   1950  N   ALA A 718       2.920 -25.479  -1.868  1.00 68.17           N  
ANISOU 1950  N   ALA A 718    13089   6427   6385    733   -934   -465       N  
ATOM   1951  CA  ALA A 718       3.912 -24.422  -1.724  1.00 75.01           C  
ANISOU 1951  CA  ALA A 718    13843   7362   7297    808  -1002   -505       C  
ATOM   1952  C   ALA A 718       4.562 -24.403  -0.342  1.00 98.12           C  
ANISOU 1952  C   ALA A 718    16995  10173  10112    852  -1100   -522       C  
ATOM   1953  O   ALA A 718       5.775 -24.234  -0.230  1.00103.28           O  
ANISOU 1953  O   ALA A 718    17625  10840  10775    962  -1249   -581       O  
ATOM   1954  CB  ALA A 718       3.295 -23.071  -2.037  1.00 73.52           C  
ANISOU 1954  CB  ALA A 718    13456   7283   7197    738   -845   -475       C  
ATOM   1955  N   ARG A 719       3.756 -24.575   0.703  1.00113.87           N  
ANISOU 1955  N   ARG A 719    19205  12056  12002    764  -1018   -475       N  
ATOM   1956  CA  ARG A 719       4.231 -24.456   2.086  1.00113.34           C  
ANISOU 1956  CA  ARG A 719    19361  11881  11822    788  -1090   -483       C  
ATOM   1957  C   ARG A 719       5.662 -24.955   2.297  1.00107.55           C  
ANISOU 1957  C   ARG A 719    18703  11105  11058    931  -1316   -548       C  
ATOM   1958  O   ARG A 719       6.440 -24.337   3.024  1.00100.11           O  
ANISOU 1958  O   ARG A 719    17799  10148  10089    990  -1393   -581       O  
ATOM   1959  CB  ARG A 719       3.279 -25.165   3.057  1.00120.17           C  
ANISOU 1959  CB  ARG A 719    20502  12604  12552    685  -1015   -431       C  
ATOM   1960  CG  ARG A 719       1.924 -24.496   3.210  1.00122.92           C  
ANISOU 1960  CG  ARG A 719    20810  12980  12915    541   -792   -379       C  
ATOM   1961  CD  ARG A 719       1.086 -25.182   4.279  1.00130.05           C  
ANISOU 1961  CD  ARG A 719    22001  13738  13673    438   -724   -336       C  
ATOM   1962  NE  ARG A 719      -0.199 -24.520   4.493  1.00135.42           N  
ANISOU 1962  NE  ARG A 719    22643  14443  14366    299   -509   -298       N  
ATOM   1963  CZ  ARG A 719      -1.115 -24.939   5.361  1.00139.56           C  
ANISOU 1963  CZ  ARG A 719    23384  14863  14778    183   -408   -264       C  
ATOM   1964  NH1 ARG A 719      -0.887 -26.019   6.094  1.00141.90           N  
ANISOU 1964  NH1 ARG A 719    23959  15020  14938    189   -503   -254       N  
ATOM   1965  NH2 ARG A 719      -2.258 -24.281   5.496  1.00140.45           N  
ANISOU 1965  NH2 ARG A 719    23437  15010  14918     60   -213   -242       N  
ATOM   1966  N   GLU A 720       5.999 -26.072   1.662  1.00105.75           N  
ANISOU 1966  N   GLU A 720    18491  10854  10836    988  -1424   -573       N  
ATOM   1967  CA  GLU A 720       7.333 -26.651   1.776  1.00106.33           C  
ANISOU 1967  CA  GLU A 720    18628  10884  10889   1127  -1646   -644       C  
ATOM   1968  C   GLU A 720       8.428 -25.606   1.568  1.00107.96           C  
ANISOU 1968  C   GLU A 720    18642  11197  11179   1220  -1720   -709       C  
ATOM   1969  O   GLU A 720       9.088 -25.576   0.529  1.00108.06           O  
ANISOU 1969  O   GLU A 720    18448  11314  11295   1291  -1784   -764       O  
ATOM   1970  CB  GLU A 720       7.503 -27.804   0.782  1.00113.46           C  
ANISOU 1970  CB  GLU A 720    19486  11793  11832   1173  -1729   -670       C  
ATOM   1971  CG  GLU A 720       6.517 -28.949   0.978  1.00121.28           C  
ANISOU 1971  CG  GLU A 720    20675  12667  12738   1090  -1676   -612       C  
ATOM   1972  CD  GLU A 720       5.091 -28.568   0.619  1.00127.43           C  
ANISOU 1972  CD  GLU A 720    21371  13500  13548    946  -1446   -542       C  
ATOM   1973  OE1 GLU A 720       4.906 -27.597  -0.145  1.00129.36           O  
ANISOU 1973  OE1 GLU A 720    21361  13886  13903    926  -1346   -542       O  
ATOM   1974  OE2 GLU A 720       4.154 -29.242   1.095  1.00129.80           O  
ANISOU 1974  OE2 GLU A 720    21860  13696  13761    853  -1367   -488       O  
TER    1975      GLU A 720                                                      
ATOM   1976  N   ASP B 449     -19.744  -2.620  -7.379  1.00 84.65           N  
ANISOU 1976  N   ASP B 449    11150  11526   9486  -1909   1102   -808       N  
ATOM   1977  CA  ASP B 449     -19.689  -2.892  -5.948  1.00 82.57           C  
ANISOU 1977  CA  ASP B 449    10987  11169   9215  -1963   1142   -855       C  
ATOM   1978  C   ASP B 449     -18.336  -3.454  -5.526  1.00 66.83           C  
ANISOU 1978  C   ASP B 449     9132   9015   7244  -1818   1179   -773       C  
ATOM   1979  O   ASP B 449     -17.879  -4.468  -6.053  1.00 60.47           O  
ANISOU 1979  O   ASP B 449     8494   8109   6372  -1807   1239   -728       O  
ATOM   1980  CB  ASP B 449     -20.802  -3.864  -5.538  1.00 89.16           C  
ANISOU 1980  CB  ASP B 449    11973  11985   9920  -2217   1221   -949       C  
ATOM   1981  CG  ASP B 449     -22.188  -3.276  -5.717  1.00 92.57           C  
ANISOU 1981  CG  ASP B 449    12261  12593  10318  -2367   1184  -1043       C  
ATOM   1982  OD1 ASP B 449     -22.898  -3.109  -4.703  1.00 88.89           O  
ANISOU 1982  OD1 ASP B 449    11781  12164   9831  -2486   1192  -1126       O  
ATOM   1983  OD2 ASP B 449     -22.566  -2.979  -6.868  1.00 95.98           O  
ANISOU 1983  OD2 ASP B 449    12592  13138  10739  -2360   1146  -1031       O  
ATOM   1984  N   TRP B 450     -17.697  -2.781  -4.577  1.00 51.73           N  
ANISOU 1984  N   TRP B 450     7154   7084   5417  -1703   1145   -756       N  
ATOM   1985  CA  TRP B 450     -16.477  -3.294  -3.973  1.00 57.82           C  
ANISOU 1985  CA  TRP B 450     8057   7718   6195  -1572   1180   -687       C  
ATOM   1986  C   TRP B 450     -16.833  -4.055  -2.706  1.00 52.61           C  
ANISOU 1986  C   TRP B 450     7572   6967   5451  -1701   1252   -742       C  
ATOM   1987  O   TRP B 450     -15.964  -4.414  -1.911  1.00 39.21           O  
ANISOU 1987  O   TRP B 450     5986   5167   3745  -1605   1279   -699       O  
ATOM   1988  CB  TRP B 450     -15.502  -2.158  -3.669  1.00 63.98           C  
ANISOU 1988  CB  TRP B 450     8668   8537   7105  -1372   1104   -630       C  
ATOM   1989  CG  TRP B 450     -15.007  -1.489  -4.903  1.00 54.96           C  
ANISOU 1989  CG  TRP B 450     7381   7469   6033  -1233   1040   -553       C  
ATOM   1990  CD1 TRP B 450     -15.390  -0.273  -5.389  1.00 63.15           C  
ANISOU 1990  CD1 TRP B 450     8216   8635   7144  -1200    958   -557       C  
ATOM   1991  CD2 TRP B 450     -14.052  -2.010  -5.832  1.00 59.28           C  
ANISOU 1991  CD2 TRP B 450     7985   7968   6569  -1104   1054   -457       C  
ATOM   1992  NE1 TRP B 450     -14.723   0.000  -6.557  1.00 73.80           N  
ANISOU 1992  NE1 TRP B 450     9490  10018   8532  -1065    921   -459       N  
ATOM   1993  CE2 TRP B 450     -13.896  -1.051  -6.851  1.00 72.05           C  
ANISOU 1993  CE2 TRP B 450     9414   9697   8263  -1007    978   -400       C  
ATOM   1994  CE3 TRP B 450     -13.310  -3.192  -5.897  1.00 65.25           C  
ANISOU 1994  CE3 TRP B 450     8946   8598   7249  -1053   1126   -410       C  
ATOM   1995  CZ2 TRP B 450     -13.026  -1.239  -7.925  1.00 68.29           C  
ANISOU 1995  CZ2 TRP B 450     8926   9223   7798   -874    970   -300       C  
ATOM   1996  CZ3 TRP B 450     -12.449  -3.377  -6.962  1.00 58.90           C  
ANISOU 1996  CZ3 TRP B 450     8133   7794   6453   -911   1119   -320       C  
ATOM   1997  CH2 TRP B 450     -12.314  -2.407  -7.961  1.00 61.85           C  
ANISOU 1997  CH2 TRP B 450     8296   8293   6912   -829   1041   -266       C  
ATOM   1998  N   GLU B 451     -18.129  -4.291  -2.529  1.00 59.11           N  
ANISOU 1998  N   GLU B 451     8416   7839   6203  -1920   1280   -836       N  
ATOM   1999  CA  GLU B 451     -18.624  -5.060  -1.398  1.00 64.63           C  
ANISOU 1999  CA  GLU B 451     9286   8464   6805  -2075   1352   -890       C  
ATOM   2000  C   GLU B 451     -18.249  -6.528  -1.544  1.00 68.46           C  
ANISOU 2000  C   GLU B 451    10072   8780   7161  -2101   1445   -849       C  
ATOM   2001  O   GLU B 451     -18.811  -7.242  -2.374  1.00 74.83           O  
ANISOU 2001  O   GLU B 451    10982   9571   7880  -2221   1488   -869       O  
ATOM   2002  CB  GLU B 451     -20.144  -4.919  -1.272  1.00 68.43           C  
ANISOU 2002  CB  GLU B 451     9701   9062   7236  -2311   1358  -1002       C  
ATOM   2003  CG  GLU B 451     -20.751  -5.800  -0.189  1.00 76.89           C  
ANISOU 2003  CG  GLU B 451    10959  10066   8189  -2500   1440  -1056       C  
ATOM   2004  CD  GLU B 451     -22.227  -5.530   0.037  1.00 79.06           C  
ANISOU 2004  CD  GLU B 451    11134  10484   8421  -2727   1439  -1169       C  
ATOM   2005  OE1 GLU B 451     -22.743  -5.924   1.105  1.00 77.13           O  
ANISOU 2005  OE1 GLU B 451    10977  10224   8104  -2871   1489  -1219       O  
ATOM   2006  OE2 GLU B 451     -22.869  -4.923  -0.847  1.00 79.40           O  
ANISOU 2006  OE2 GLU B 451    11013  10664   8492  -2757   1387  -1207       O  
ATOM   2007  N   ILE B 452     -17.288  -6.971  -0.742  1.00 69.35           N  
ANISOU 2007  N   ILE B 452    10331   8767   7251  -1981   1474   -794       N  
ATOM   2008  CA  ILE B 452     -16.898  -8.374  -0.719  1.00 65.63           C  
ANISOU 2008  CA  ILE B 452    10177   8119   6639  -1987   1561   -757       C  
ATOM   2009  C   ILE B 452     -17.885  -9.160   0.134  1.00 79.73           C  
ANISOU 2009  C   ILE B 452    12147   9855   8293  -2220   1634   -830       C  
ATOM   2010  O   ILE B 452     -17.989  -8.929   1.339  1.00 90.09           O  
ANISOU 2010  O   ILE B 452    13445  11178   9607  -2248   1633   -855       O  
ATOM   2011  CB  ILE B 452     -15.479  -8.557  -0.151  1.00 48.47           C  
ANISOU 2011  CB  ILE B 452     8102   5840   4475  -1753   1559   -671       C  
ATOM   2012  CG1 ILE B 452     -14.472  -7.714  -0.939  1.00 50.64           C  
ANISOU 2012  CG1 ILE B 452     8178   6182   4881  -1528   1485   -598       C  
ATOM   2013  CG2 ILE B 452     -15.080 -10.027  -0.163  1.00 44.91           C  
ANISOU 2013  CG2 ILE B 452     8001   5201   3863  -1742   1646   -636       C  
ATOM   2014  CD1 ILE B 452     -13.050  -7.805  -0.415  1.00 51.72           C  
ANISOU 2014  CD1 ILE B 452     8381   6243   5028  -1292   1475   -515       C  
ATOM   2015  N   PRO B 453     -18.620 -10.091  -0.491  1.00 78.51           N  
ANISOU 2015  N   PRO B 453    12163   9651   8015  -2395   1698   -865       N  
ATOM   2016  CA  PRO B 453     -19.603 -10.901   0.234  1.00 78.42           C  
ANISOU 2016  CA  PRO B 453    12341   9593   7862  -2639   1773   -933       C  
ATOM   2017  C   PRO B 453     -18.939 -11.632   1.393  1.00 86.59           C  
ANISOU 2017  C   PRO B 453    13622  10471   8808  -2574   1821   -895       C  
ATOM   2018  O   PRO B 453     -17.980 -12.374   1.182  1.00 86.31           O  
ANISOU 2018  O   PRO B 453    13797  10284   8715  -2424   1851   -824       O  
ATOM   2019  CB  PRO B 453     -20.079 -11.906  -0.821  1.00 66.46           C  
ANISOU 2019  CB  PRO B 453    11013   8014   6225  -2774   1837   -949       C  
ATOM   2020  CG  PRO B 453     -19.781 -11.257  -2.128  1.00 65.56           C  
ANISOU 2020  CG  PRO B 453    10696   7995   6219  -2655   1776   -919       C  
ATOM   2021  CD  PRO B 453     -18.521 -10.482  -1.907  1.00 68.90           C  
ANISOU 2021  CD  PRO B 453    10984   8418   6777  -2375   1709   -839       C  
ATOM   2022  N   ASP B 454     -19.438 -11.416   2.605  1.00 95.95           N  
ANISOU 2022  N   ASP B 454    14781  11700   9977  -2677   1825   -942       N  
ATOM   2023  CA  ASP B 454     -18.834 -12.018   3.785  1.00 94.14           C  
ANISOU 2023  CA  ASP B 454    14764  11342   9661  -2612   1862   -908       C  
ATOM   2024  C   ASP B 454     -18.813 -13.538   3.670  1.00 88.84           C  
ANISOU 2024  C   ASP B 454    14484  10474   8798  -2687   1955   -891       C  
ATOM   2025  O   ASP B 454     -19.776 -14.149   3.206  1.00 86.12           O  
ANISOU 2025  O   ASP B 454    14250  10119   8354  -2910   2009   -945       O  
ATOM   2026  CB  ASP B 454     -19.581 -11.597   5.048  1.00 96.99           C  
ANISOU 2026  CB  ASP B 454    15032  11802  10017  -2755   1859   -974       C  
ATOM   2027  CG  ASP B 454     -18.706 -11.653   6.281  1.00 95.75           C  
ANISOU 2027  CG  ASP B 454    14957  11579   9844  -2606   1855   -931       C  
ATOM   2028  OD1 ASP B 454     -17.701 -10.912   6.328  1.00 83.17           O  
ANISOU 2028  OD1 ASP B 454    13211  10018   8373  -2375   1792   -877       O  
ATOM   2029  OD2 ASP B 454     -19.028 -12.425   7.208  1.00 96.70           O  
ANISOU 2029  OD2 ASP B 454    15292  11625   9824  -2723   1913   -952       O  
ATOM   2030  N   GLY B 455     -17.707 -14.141   4.091  1.00 76.64           N  
ANISOU 2030  N   GLY B 455    13152   8775   7193  -2497   1973   -818       N  
ATOM   2031  CA  GLY B 455     -17.561 -15.584   4.039  1.00 69.71           C  
ANISOU 2031  CA  GLY B 455    12670   7691   6124  -2534   2060   -797       C  
ATOM   2032  C   GLY B 455     -16.543 -16.017   3.004  1.00 76.27           C  
ANISOU 2032  C   GLY B 455    13612   8414   6952  -2325   2063   -723       C  
ATOM   2033  O   GLY B 455     -16.166 -17.186   2.938  1.00 85.74           O  
ANISOU 2033  O   GLY B 455    15150   9428   7999  -2293   2129   -693       O  
ATOM   2034  N   GLN B 456     -16.098 -15.068   2.188  1.00 73.46           N  
ANISOU 2034  N   GLN B 456    12973   8177   6759  -2182   1992   -695       N  
ATOM   2035  CA  GLN B 456     -15.098 -15.346   1.168  1.00 64.86           C  
ANISOU 2035  CA  GLN B 456    11943   7018   5682  -1973   1988   -624       C  
ATOM   2036  C   GLN B 456     -13.702 -15.064   1.704  1.00 58.38           C  
ANISOU 2036  C   GLN B 456    11100   6169   4911  -1676   1943   -544       C  
ATOM   2037  O   GLN B 456     -12.702 -15.422   1.082  1.00 63.68           O  
ANISOU 2037  O   GLN B 456    11862   6767   5566  -1472   1944   -477       O  
ATOM   2038  CB  GLN B 456     -15.357 -14.498  -0.078  1.00 68.48           C  
ANISOU 2038  CB  GLN B 456    12110   7629   6278  -1980   1935   -634       C  
ATOM   2039  CG  GLN B 456     -16.695 -14.766  -0.738  1.00 76.08           C  
ANISOU 2039  CG  GLN B 456    13079   8641   7188  -2259   1974   -714       C  
ATOM   2040  CD  GLN B 456     -16.988 -13.805  -1.872  1.00 80.32           C  
ANISOU 2040  CD  GLN B 456    13302   9353   7864  -2259   1910   -727       C  
ATOM   2041  OE1 GLN B 456     -16.180 -12.930  -2.187  1.00 79.42           O  
ANISOU 2041  OE1 GLN B 456    12970   9318   7889  -2052   1837   -674       O  
ATOM   2042  NE2 GLN B 456     -18.151 -13.963  -2.493  1.00 80.84           N  
ANISOU 2042  NE2 GLN B 456    13344   9487   7885  -2493   1936   -799       N  
ATOM   2043  N   ILE B 457     -13.640 -14.424   2.866  1.00 53.89           N  
ANISOU 2043  N   ILE B 457    10408   5670   4397  -1655   1904   -553       N  
ATOM   2044  CA  ILE B 457     -12.363 -14.021   3.439  1.00 61.75           C  
ANISOU 2044  CA  ILE B 457    11342   6672   5448  -1387   1854   -485       C  
ATOM   2045  C   ILE B 457     -11.984 -14.863   4.655  1.00 64.14           C  
ANISOU 2045  C   ILE B 457    11927   6842   5603  -1340   1897   -469       C  
ATOM   2046  O   ILE B 457     -12.714 -14.905   5.643  1.00 55.60           O  
ANISOU 2046  O   ILE B 457    10879   5774   4474  -1503   1916   -521       O  
ATOM   2047  CB  ILE B 457     -12.386 -12.540   3.850  1.00 54.70           C  
ANISOU 2047  CB  ILE B 457    10074   5973   4737  -1359   1768   -502       C  
ATOM   2048  CG1 ILE B 457     -13.325 -11.747   2.938  1.00 51.54           C  
ANISOU 2048  CG1 ILE B 457     9420   5712   4453  -1511   1738   -554       C  
ATOM   2049  CG2 ILE B 457     -10.979 -11.966   3.830  1.00 56.27           C  
ANISOU 2049  CG2 ILE B 457    10146   6210   5024  -1068   1706   -424       C  
ATOM   2050  CD1 ILE B 457     -13.494 -10.298   3.347  1.00 43.38           C  
ANISOU 2050  CD1 ILE B 457     8037   4861   3586  -1506   1658   -582       C  
ATOM   2051  N   THR B 458     -10.839 -15.534   4.573  1.00 67.93           N  
ANISOU 2051  N   THR B 458    12606   7201   6003  -1111   1910   -398       N  
ATOM   2052  CA  THR B 458     -10.323 -16.311   5.696  1.00 71.18           C  
ANISOU 2052  CA  THR B 458    13285   7490   6270  -1021   1942   -374       C  
ATOM   2053  C   THR B 458      -9.379 -15.459   6.535  1.00 78.45           C  
ANISOU 2053  C   THR B 458    14007   8518   7283   -815   1869   -337       C  
ATOM   2054  O   THR B 458      -8.276 -15.129   6.103  1.00 82.12           O  
ANISOU 2054  O   THR B 458    14374   9018   7810   -574   1825   -275       O  
ATOM   2055  CB  THR B 458      -9.599 -17.587   5.221  1.00 82.53           C  
ANISOU 2055  CB  THR B 458    15080   8731   7545   -876   2001   -320       C  
ATOM   2056  OG1 THR B 458     -10.561 -18.625   4.994  1.00 87.98           O  
ANISOU 2056  OG1 THR B 458    16055   9285   8089  -1104   2087   -365       O  
ATOM   2057  CG2 THR B 458      -8.594 -18.061   6.265  1.00 76.18           C  
ANISOU 2057  CG2 THR B 458    14464   7846   6636   -663   2001   -270       C  
ATOM   2058  N   VAL B 459      -9.825 -15.102   7.736  1.00 89.58           N  
ANISOU 2058  N   VAL B 459    15352   9990   8694   -916   1858   -380       N  
ATOM   2059  CA  VAL B 459      -9.054 -14.230   8.615  1.00 79.37           C  
ANISOU 2059  CA  VAL B 459    13852   8817   7487   -753   1790   -360       C  
ATOM   2060  C   VAL B 459      -8.035 -14.994   9.454  1.00 70.16           C  
ANISOU 2060  C   VAL B 459    12931   7548   6181   -549   1804   -308       C  
ATOM   2061  O   VAL B 459      -8.363 -15.992  10.093  1.00 72.19           O  
ANISOU 2061  O   VAL B 459    13485   7673   6269   -628   1865   -320       O  
ATOM   2062  CB  VAL B 459      -9.971 -13.396   9.530  1.00 74.24           C  
ANISOU 2062  CB  VAL B 459    12991   8306   6912   -945   1766   -434       C  
ATOM   2063  CG1 VAL B 459     -10.489 -12.190   8.781  1.00 66.44           C  
ANISOU 2063  CG1 VAL B 459    11655   7477   6113  -1028   1714   -468       C  
ATOM   2064  CG2 VAL B 459     -11.127 -14.240  10.050  1.00 75.02           C  
ANISOU 2064  CG2 VAL B 459    13318   8318   6867  -1201   1839   -493       C  
ATOM   2065  N   GLY B 460      -6.796 -14.511   9.443  1.00 71.56           N  
ANISOU 2065  N   GLY B 460    12979   7791   6420   -287   1747   -250       N  
ATOM   2066  CA  GLY B 460      -5.713 -15.143  10.172  1.00 73.84           C  
ANISOU 2066  CA  GLY B 460    13467   8008   6581    -59   1751   -197       C  
ATOM   2067  C   GLY B 460      -5.281 -14.353  11.393  1.00 84.28           C  
ANISOU 2067  C   GLY B 460    14599   9470   7953     16   1693   -208       C  
ATOM   2068  O   GLY B 460      -6.102 -13.708  12.047  1.00 92.97           O  
ANISOU 2068  O   GLY B 460    15537  10667   9119   -167   1679   -272       O  
ATOM   2069  N   GLN B 461      -3.986 -14.392  11.694  1.00 96.40           N  
ANISOU 2069  N   GLN B 461    16150  11026   9454    288   1661   -150       N  
ATOM   2070  CA  GLN B 461      -3.460 -13.801  12.926  1.00110.41           C  
ANISOU 2070  CA  GLN B 461    17785  12923  11241    379   1611   -159       C  
ATOM   2071  C   GLN B 461      -3.594 -12.280  13.001  1.00119.85           C  
ANISOU 2071  C   GLN B 461    18569  14327  12640    322   1537   -198       C  
ATOM   2072  O   GLN B 461      -3.644 -11.594  11.980  1.00134.13           O  
ANISOU 2072  O   GLN B 461    20177  16199  14589    307   1506   -190       O  
ATOM   2073  CB  GLN B 461      -1.999 -14.206  13.138  1.00102.28           C  
ANISOU 2073  CB  GLN B 461    16860  11881  10120    694   1592    -88       C  
ATOM   2074  CG  GLN B 461      -1.066 -13.787  12.016  1.00100.57           C  
ANISOU 2074  CG  GLN B 461    16493  11724   9996    886   1551    -31       C  
ATOM   2075  CD  GLN B 461       0.180 -13.090  12.528  1.00100.78           C  
ANISOU 2075  CD  GLN B 461    16323  11908  10061   1119   1480      1       C  
ATOM   2076  OE1 GLN B 461       0.106 -12.225  13.402  1.00 93.33           O  
ANISOU 2076  OE1 GLN B 461    15165  11104   9192   1068   1434    -40       O  
ATOM   2077  NE2 GLN B 461       1.332 -13.459  11.981  1.00108.36           N  
ANISOU 2077  NE2 GLN B 461    17350  12856  10966   1374   1471     70       N  
ATOM   2078  N   ARG B 462      -3.635 -11.767  14.229  1.00104.05           N  
ANISOU 2078  N   ARG B 462    16454  12431  10648    294   1508   -240       N  
ATOM   2079  CA  ARG B 462      -3.785 -10.337  14.486  1.00 99.60           C  
ANISOU 2079  CA  ARG B 462    15521  12061  10261    234   1441   -289       C  
ATOM   2080  C   ARG B 462      -2.477  -9.573  14.292  1.00 98.19           C  
ANISOU 2080  C   ARG B 462    15137  12005  10167    472   1369   -243       C  
ATOM   2081  O   ARG B 462      -1.391 -10.111  14.513  1.00 94.21           O  
ANISOU 2081  O   ARG B 462    14762  11473   9560    694   1365   -186       O  
ATOM   2082  CB  ARG B 462      -4.308 -10.112  15.908  1.00103.92           C  
ANISOU 2082  CB  ARG B 462    16031  12681  10774    116   1440   -360       C  
ATOM   2083  CG  ARG B 462      -4.538  -8.652  16.274  1.00104.55           C  
ANISOU 2083  CG  ARG B 462    15742  12955  11026     43   1376   -426       C  
ATOM   2084  CD  ARG B 462      -4.742  -8.473  17.773  1.00100.38           C  
ANISOU 2084  CD  ARG B 462    15182  12513  10446    -14   1371   -491       C  
ATOM   2085  NE  ARG B 462      -5.868  -9.255  18.277  1.00103.33           N  
ANISOU 2085  NE  ARG B 462    15756  12798  10705   -221   1437   -533       N  
ATOM   2086  CZ  ARG B 462      -5.751 -10.442  18.865  1.00106.77           C  
ANISOU 2086  CZ  ARG B 462    16505  13112  10952   -191   1488   -505       C  
ATOM   2087  NH1 ARG B 462      -4.555 -10.990  19.029  1.00108.20           N  
ANISOU 2087  NH1 ARG B 462    16832  13243  11035     53   1480   -436       N  
ATOM   2088  NH2 ARG B 462      -6.832 -11.081  19.291  1.00107.42           N  
ANISOU 2088  NH2 ARG B 462    16756  13123  10934   -404   1547   -548       N  
ATOM   2089  N   ILE B 463      -2.594  -8.313  13.881  1.00120.37           N  
ANISOU 2089  N   ILE B 463    17626  14953  13156    422   1313   -269       N  
ATOM   2090  CA  ILE B 463      -1.438  -7.440  13.710  1.00109.34           C  
ANISOU 2090  CA  ILE B 463    16004  13690  11849    612   1240   -235       C  
ATOM   2091  C   ILE B 463      -1.545  -6.236  14.643  1.00110.58           C  
ANISOU 2091  C   ILE B 463    15888  14018  12111    547   1185   -309       C  
ATOM   2092  O   ILE B 463      -0.542  -5.607  14.981  1.00110.28           O  
ANISOU 2092  O   ILE B 463    15696  14100  12106    699   1128   -298       O  
ATOM   2093  CB  ILE B 463      -1.297  -6.955  12.250  1.00 66.88           C  
ANISOU 2093  CB  ILE B 463    10490   8330   6592    635   1217   -192       C  
ATOM   2094  CG1 ILE B 463      -0.971  -8.128  11.322  1.00 68.88           C  
ANISOU 2094  CG1 ILE B 463    11003   8431   6738    739   1267   -120       C  
ATOM   2095  CG2 ILE B 463      -0.218  -5.888  12.134  1.00 47.66           C  
ANISOU 2095  CG2 ILE B 463     7792   6055   4261    791   1138   -166       C  
ATOM   2096  CD1 ILE B 463      -2.155  -9.012  11.004  1.00 65.86           C  
ANISOU 2096  CD1 ILE B 463    10843   7895   6288    547   1341   -147       C  
ATOM   2097  N   GLY B 464      -2.766  -5.923  15.062  1.00 80.93           N  
ANISOU 2097  N   GLY B 464    12073  10278   8400    319   1203   -390       N  
ATOM   2098  CA  GLY B 464      -2.989  -4.831  15.992  1.00 86.86           C  
ANISOU 2098  CA  GLY B 464    12579  11182   9243    244   1158   -476       C  
ATOM   2099  C   GLY B 464      -4.357  -4.198  15.842  1.00 99.56           C  
ANISOU 2099  C   GLY B 464    14046  12823  10958     -1   1167   -556       C  
ATOM   2100  O   GLY B 464      -5.271  -4.796  15.274  1.00 91.90           O  
ANISOU 2100  O   GLY B 464    13208  11752   9957   -139   1219   -554       O  
ATOM   2101  N   SER B 465      -4.506  -2.983  16.356  1.00162.81           N  
ANISOU 2101  N   SER B 465    21788  20980  19091    -54   1117   -634       N  
ATOM   2102  CA  SER B 465      -5.784  -2.294  16.272  1.00167.73           C  
ANISOU 2102  CA  SER B 465    22259  21653  19819   -271   1121   -720       C  
ATOM   2103  C   SER B 465      -5.592  -0.832  15.894  1.00171.32           C  
ANISOU 2103  C   SER B 465    22408  22231  20456   -257   1050   -759       C  
ATOM   2104  O   SER B 465      -4.973  -0.065  16.629  1.00177.30           O  
ANISOU 2104  O   SER B 465    23008  23097  21261   -185   1001   -804       O  
ATOM   2105  CB  SER B 465      -6.571  -2.426  17.580  1.00100.44           C  
ANISOU 2105  CB  SER B 465    13759  13171  11231   -411   1151   -811       C  
ATOM   2106  OG  SER B 465      -5.993  -1.665  18.627  1.00 90.59           O  
ANISOU 2106  OG  SER B 465    12346  12055  10019   -340   1103   -872       O  
ATOM   2107  N   GLY B 466      -6.124  -0.454  14.739  1.00103.18           N  
ANISOU 2107  N   GLY B 466    13699  13581  11923   -328   1044   -745       N  
ATOM   2108  CA  GLY B 466      -5.931   0.887  14.227  1.00 89.91           C  
ANISOU 2108  CA  GLY B 466    11759  11995  10409   -311    976   -772       C  
ATOM   2109  C   GLY B 466      -7.153   1.769  14.369  1.00 87.28           C  
ANISOU 2109  C   GLY B 466    11253  11729  10182   -496    966   -884       C  
ATOM   2110  O   GLY B 466      -7.626   2.028  15.476  1.00 93.27           O  
ANISOU 2110  O   GLY B 466    11950  12553  10934   -579    972   -980       O  
ATOM   2111  N   SER B 467      -7.666   2.228  13.234  1.00 84.11           N  
ANISOU 2111  N   SER B 467    10771  11314   9871   -553    949   -875       N  
ATOM   2112  CA  SER B 467      -8.788   3.157  13.212  1.00 81.81           C  
ANISOU 2112  CA  SER B 467    10309  11088   9686   -707    929   -982       C  
ATOM   2113  C   SER B 467     -10.123   2.496  13.550  1.00 96.73           C  
ANISOU 2113  C   SER B 467    12292  12962  11500   -893    995  -1036       C  
ATOM   2114  O   SER B 467     -10.793   2.889  14.505  1.00 99.63           O  
ANISOU 2114  O   SER B 467    12570  13406  11880   -997   1001  -1142       O  
ATOM   2115  CB  SER B 467      -8.878   3.844  11.848  1.00 66.32           C  
ANISOU 2115  CB  SER B 467     8251   9117   7831   -693    883   -952       C  
ATOM   2116  OG  SER B 467     -10.002   4.701  11.783  1.00 64.97           O  
ANISOU 2116  OG  SER B 467     7943   8998   7747   -828    859  -1061       O  
ATOM   2117  N   PHE B 468     -10.512   1.501  12.761  1.00132.66           N  
ANISOU 2117  N   PHE B 468    17020  17418  15968   -941   1046   -970       N  
ATOM   2118  CA  PHE B 468     -11.811   0.862  12.942  1.00145.66           C  
ANISOU 2118  CA  PHE B 468    18762  19048  17536  -1135   1109  -1021       C  
ATOM   2119  C   PHE B 468     -11.761  -0.318  13.905  1.00149.51           C  
ANISOU 2119  C   PHE B 468    19474  19473  17860  -1161   1175  -1006       C  
ATOM   2120  O   PHE B 468     -12.719  -1.078  14.014  1.00150.64           O  
ANISOU 2120  O   PHE B 468    19750  19578  17907  -1320   1235  -1031       O  
ATOM   2121  CB  PHE B 468     -12.382   0.400  11.600  1.00140.17           C  
ANISOU 2121  CB  PHE B 468    18147  18285  16829  -1201   1130   -978       C  
ATOM   2122  CG  PHE B 468     -13.022   1.499  10.796  1.00141.17           C  
ANISOU 2122  CG  PHE B 468    18066  18487  17085  -1253   1074  -1031       C  
ATOM   2123  CD1 PHE B 468     -12.874   1.541   9.419  1.00142.10           C  
ANISOU 2123  CD1 PHE B 468    18184  18566  17241  -1201   1050   -969       C  
ATOM   2124  CD2 PHE B 468     -13.775   2.481  11.411  1.00141.17           C  
ANISOU 2124  CD2 PHE B 468    17879  18597  17160  -1345   1043  -1150       C  
ATOM   2125  CE1 PHE B 468     -13.465   2.541   8.670  1.00143.29           C  
ANISOU 2125  CE1 PHE B 468    18169  18782  17493  -1235    992  -1020       C  
ATOM   2126  CE2 PHE B 468     -14.367   3.485  10.668  1.00141.76           C  
ANISOU 2126  CE2 PHE B 468    17795  18730  17337  -1375    984  -1209       C  
ATOM   2127  CZ  PHE B 468     -14.207   3.514   9.296  1.00141.90           C  
ANISOU 2127  CZ  PHE B 468    17832  18703  17381  -1317    957  -1142       C  
ATOM   2128  N   GLY B 469     -10.645  -0.477  14.602  1.00136.79           N  
ANISOU 2128  N   GLY B 469    17912  17852  16208  -1006   1161   -969       N  
ATOM   2129  CA  GLY B 469     -10.510  -1.587  15.522  1.00133.43           C  
ANISOU 2129  CA  GLY B 469    17716  17362  15619  -1008   1214   -952       C  
ATOM   2130  C   GLY B 469      -9.378  -2.512  15.136  1.00124.82           C  
ANISOU 2130  C   GLY B 469    16840  16151  14436   -829   1225   -838       C  
ATOM   2131  O   GLY B 469      -8.259  -2.067  14.900  1.00123.74           O  
ANISOU 2131  O   GLY B 469    16621  16040  14356   -648   1174   -789       O  
ATOM   2132  N   THR B 470      -9.673  -3.802  15.050  1.00108.31           N  
ANISOU 2132  N   THR B 470    15027  13928  12196   -881   1291   -800       N  
ATOM   2133  CA  THR B 470      -8.627  -4.802  14.891  1.00 95.22           C  
ANISOU 2133  CA  THR B 470    13608  12148  10424   -706   1309   -704       C  
ATOM   2134  C   THR B 470      -8.377  -5.225  13.442  1.00 81.30           C  
ANISOU 2134  C   THR B 470    11933  10285   8672   -645   1319   -625       C  
ATOM   2135  O   THR B 470      -9.305  -5.325  12.637  1.00 61.51           O  
ANISOU 2135  O   THR B 470     9432   7750   6191   -794   1345   -643       O  
ATOM   2136  CB  THR B 470      -8.905  -6.018  15.785  1.00 85.10           C  
ANISOU 2136  CB  THR B 470    12612  10769   8955   -767   1374   -708       C  
ATOM   2137  OG1 THR B 470     -10.183  -6.575  15.457  1.00 85.88           O  
ANISOU 2137  OG1 THR B 470    12825  10806   9002   -992   1433   -743       O  
ATOM   2138  CG2 THR B 470      -8.924  -5.575  17.229  1.00 80.33           C  
ANISOU 2138  CG2 THR B 470    11908  10277   8335   -788   1356   -778       C  
ATOM   2139  N   VAL B 471      -7.106  -5.461  13.123  1.00 75.11           N  
ANISOU 2139  N   VAL B 471    11210   9462   7866   -422   1297   -542       N  
ATOM   2140  CA  VAL B 471      -6.704  -5.872  11.783  1.00 78.39           C  
ANISOU 2140  CA  VAL B 471    11706   9794   8286   -334   1304   -465       C  
ATOM   2141  C   VAL B 471      -6.046  -7.251  11.784  1.00 85.99           C  
ANISOU 2141  C   VAL B 471    12992  10603   9077   -206   1354   -397       C  
ATOM   2142  O   VAL B 471      -5.164  -7.531  12.595  1.00 87.41           O  
ANISOU 2142  O   VAL B 471    13253  10782   9178    -53   1345   -371       O  
ATOM   2143  CB  VAL B 471      -5.758  -4.839  11.125  1.00 73.70           C  
ANISOU 2143  CB  VAL B 471    10871   9301   7829   -173   1230   -423       C  
ATOM   2144  CG1 VAL B 471      -6.358  -3.445  11.204  1.00 68.05           C  
ANISOU 2144  CG1 VAL B 471     9852   8729   7277   -287   1178   -495       C  
ATOM   2145  CG2 VAL B 471      -4.381  -4.869  11.780  1.00 68.29           C  
ANISOU 2145  CG2 VAL B 471    10201   8649   7096     53   1198   -376       C  
ATOM   2146  N   TYR B 472      -6.487  -8.111  10.872  1.00 81.63           N  
ANISOU 2146  N   TYR B 472    12629   9924   8462   -270   1407   -373       N  
ATOM   2147  CA  TYR B 472      -5.928  -9.449  10.755  1.00 76.59           C  
ANISOU 2147  CA  TYR B 472    12319   9124   7659   -154   1460   -315       C  
ATOM   2148  C   TYR B 472      -5.502  -9.745   9.322  1.00 65.59           C  
ANISOU 2148  C   TYR B 472    10968   7671   6284    -57   1465   -253       C  
ATOM   2149  O   TYR B 472      -6.202  -9.394   8.371  1.00 56.26           O  
ANISOU 2149  O   TYR B 472     9674   6512   5189   -182   1464   -273       O  
ATOM   2150  CB  TYR B 472      -6.943 -10.502  11.207  1.00 92.28           C  
ANISOU 2150  CB  TYR B 472    14578  10984   9501   -347   1538   -356       C  
ATOM   2151  CG  TYR B 472      -7.565 -10.245  12.560  1.00105.52           C  
ANISOU 2151  CG  TYR B 472    16212  12727  11154   -482   1540   -425       C  
ATOM   2152  CD1 TYR B 472      -8.774  -9.568  12.674  1.00108.26           C  
ANISOU 2152  CD1 TYR B 472    16379  13168  11587   -715   1537   -506       C  
ATOM   2153  CD2 TYR B 472      -6.952 -10.691  13.727  1.00107.98           C  
ANISOU 2153  CD2 TYR B 472    16662  13016  11349   -373   1544   -413       C  
ATOM   2154  CE1 TYR B 472      -9.347  -9.338  13.910  1.00113.17           C  
ANISOU 2154  CE1 TYR B 472    16956  13862  12182   -837   1541   -573       C  
ATOM   2155  CE2 TYR B 472      -7.525 -10.459  14.964  1.00106.48           C  
ANISOU 2155  CE2 TYR B 472    16427  12898  11134   -499   1546   -479       C  
ATOM   2156  CZ  TYR B 472      -8.718  -9.785  15.049  1.00108.99           C  
ANISOU 2156  CZ  TYR B 472    16562  13310  11539   -731   1546   -560       C  
ATOM   2157  OH  TYR B 472      -9.286  -9.558  16.286  1.00109.21           O  
ANISOU 2157  OH  TYR B 472    16538  13419  11536   -854   1549   -629       O  
ATOM   2158  N   LYS B 473      -4.349 -10.389   9.174  1.00 69.11           N  
ANISOU 2158  N   LYS B 473    11570   8049   6641    173   1470   -181       N  
ATOM   2159  CA  LYS B 473      -3.920 -10.896   7.880  1.00 64.48           C  
ANISOU 2159  CA  LYS B 473    11075   7388   6035    274   1487   -125       C  
ATOM   2160  C   LYS B 473      -4.894 -11.984   7.459  1.00 61.70           C  
ANISOU 2160  C   LYS B 473    10994   6876   5573    101   1569   -151       C  
ATOM   2161  O   LYS B 473      -5.152 -12.914   8.218  1.00 68.47           O  
ANISOU 2161  O   LYS B 473    12119   7614   6281     53   1623   -167       O  
ATOM   2162  CB  LYS B 473      -2.508 -11.469   7.982  1.00 54.58           C  
ANISOU 2162  CB  LYS B 473     9962   6095   4683    561   1482    -50       C  
ATOM   2163  CG  LYS B 473      -1.944 -12.003   6.675  1.00 50.65           C  
ANISOU 2163  CG  LYS B 473     9557   5532   4156    693   1500      9       C  
ATOM   2164  CD  LYS B 473      -0.489 -12.404   6.852  1.00 47.84           C  
ANISOU 2164  CD  LYS B 473     9293   5174   3711    993   1484     79       C  
ATOM   2165  CE  LYS B 473       0.143 -12.823   5.538  1.00 47.47           C  
ANISOU 2165  CE  LYS B 473     9302   5092   3645   1140   1496    136       C  
ATOM   2166  NZ  LYS B 473       1.609 -13.042   5.693  1.00 52.14           N  
ANISOU 2166  NZ  LYS B 473     9929   5721   4162   1444   1471    202       N  
ATOM   2167  N   GLY B 474      -5.441 -11.867   6.255  1.00 57.92           N  
ANISOU 2167  N   GLY B 474    10448   6398   5160      1   1578   -159       N  
ATOM   2168  CA  GLY B 474      -6.418 -12.827   5.778  1.00 41.64           C  
ANISOU 2168  CA  GLY B 474     8621   4202   2998   -185   1653   -193       C  
ATOM   2169  C   GLY B 474      -6.052 -13.490   4.465  1.00 53.18           C  
ANISOU 2169  C   GLY B 474    10212   5579   4416    -99   1683   -149       C  
ATOM   2170  O   GLY B 474      -4.931 -13.356   3.971  1.00 55.77           O  
ANISOU 2170  O   GLY B 474    10484   5937   4769    132   1651    -84       O  
ATOM   2171  N   LYS B 475      -7.013 -14.216   3.903  1.00 59.06           N  
ANISOU 2171  N   LYS B 475    11129   6225   5088   -291   1747   -187       N  
ATOM   2172  CA  LYS B 475      -6.841 -14.872   2.616  1.00 52.82           C  
ANISOU 2172  CA  LYS B 475    10464   5355   4249   -247   1783   -160       C  
ATOM   2173  C   LYS B 475      -8.049 -14.612   1.727  1.00 56.47           C  
ANISOU 2173  C   LYS B 475    10813   5868   4776   -491   1796   -217       C  
ATOM   2174  O   LYS B 475      -9.183 -14.907   2.101  1.00 70.00           O  
ANISOU 2174  O   LYS B 475    12615   7546   6438   -733   1838   -283       O  
ATOM   2175  CB  LYS B 475      -6.645 -16.377   2.798  1.00 63.19           C  
ANISOU 2175  CB  LYS B 475    12203   6457   5349   -208   1865   -144       C  
ATOM   2176  CG  LYS B 475      -5.258 -16.776   3.268  1.00 67.07           C  
ANISOU 2176  CG  LYS B 475    12828   6895   5759     92   1854    -74       C  
ATOM   2177  CD  LYS B 475      -4.203 -16.388   2.245  1.00 66.50           C  
ANISOU 2177  CD  LYS B 475    12598   6904   5764    321   1810    -11       C  
ATOM   2178  CE  LYS B 475      -3.148 -17.473   2.106  1.00 63.32           C  
ANISOU 2178  CE  LYS B 475    12493   6367   5199    565   1848     47       C  
ATOM   2179  NZ  LYS B 475      -2.024 -17.049   1.224  1.00 57.36           N  
ANISOU 2179  NZ  LYS B 475    11565   5715   4514    806   1799    111       N  
ATOM   2180  N   TRP B 476      -7.794 -14.055   0.549  1.00 50.73           N  
ANISOU 2180  N   TRP B 476     9885   5234   4156   -427   1758   -192       N  
ATOM   2181  CA  TRP B 476      -8.847 -13.775  -0.416  1.00 51.02           C  
ANISOU 2181  CA  TRP B 476     9797   5335   4252   -631   1763   -241       C  
ATOM   2182  C   TRP B 476      -8.230 -13.596  -1.798  1.00 60.34           C  
ANISOU 2182  C   TRP B 476    10868   6569   5491   -494   1740   -191       C  
ATOM   2183  O   TRP B 476      -7.826 -12.493  -2.171  1.00 57.41           O  
ANISOU 2183  O   TRP B 476    10195   6348   5268   -400   1665   -162       O  
ATOM   2184  CB  TRP B 476      -9.621 -12.523  -0.008  1.00 54.72           C  
ANISOU 2184  CB  TRP B 476     9953   5968   4870   -772   1704   -293       C  
ATOM   2185  CG  TRP B 476     -10.840 -12.272  -0.838  1.00 63.05           C  
ANISOU 2185  CG  TRP B 476    10894   7095   5968   -998   1710   -356       C  
ATOM   2186  CD1 TRP B 476     -12.007 -12.980  -0.816  1.00 62.57           C  
ANISOU 2186  CD1 TRP B 476    10999   6972   5803  -1245   1775   -425       C  
ATOM   2187  CD2 TRP B 476     -11.020 -11.232  -1.806  1.00 62.57           C  
ANISOU 2187  CD2 TRP B 476    10527   7193   6054   -999   1646   -356       C  
ATOM   2188  NE1 TRP B 476     -12.899 -12.450  -1.714  1.00 61.95           N  
ANISOU 2188  NE1 TRP B 476    10729   7012   5797  -1395   1754   -471       N  
ATOM   2189  CE2 TRP B 476     -12.318 -11.375  -2.335  1.00 64.60           C  
ANISOU 2189  CE2 TRP B 476    10777   7482   6287  -1243   1674   -429       C  
ATOM   2190  CE3 TRP B 476     -10.208 -10.196  -2.279  1.00 51.57           C  
ANISOU 2190  CE3 TRP B 476     8870   5923   4803   -819   1567   -301       C  
ATOM   2191  CZ2 TRP B 476     -12.824 -10.521  -3.313  1.00 63.80           C  
ANISOU 2191  CZ2 TRP B 476    10415   7531   6295  -1299   1622   -448       C  
ATOM   2192  CZ3 TRP B 476     -10.711  -9.349  -3.249  1.00 45.96           C  
ANISOU 2192  CZ3 TRP B 476     7909   5350   4202   -880   1518   -316       C  
ATOM   2193  CH2 TRP B 476     -12.007  -9.516  -3.756  1.00 54.36           C  
ANISOU 2193  CH2 TRP B 476     8973   6443   5236  -1112   1544   -389       C  
ATOM   2194  N   HIS B 477      -8.158 -14.690  -2.549  1.00 73.04           N  
ANISOU 2194  N   HIS B 477    12728   8053   6971   -486   1805   -180       N  
ATOM   2195  CA  HIS B 477      -7.469 -14.702  -3.833  1.00 66.77           C  
ANISOU 2195  CA  HIS B 477    11872   7297   6202   -338   1792   -127       C  
ATOM   2196  C   HIS B 477      -6.007 -14.327  -3.620  1.00 72.63           C  
ANISOU 2196  C   HIS B 477    12528   8083   6986    -38   1740    -46       C  
ATOM   2197  O   HIS B 477      -5.393 -13.664  -4.457  1.00 74.28           O  
ANISOU 2197  O   HIS B 477    12516   8414   7295     90   1688      0       O  
ATOM   2198  CB  HIS B 477      -8.135 -13.741  -4.820  1.00 40.56           C  
ANISOU 2198  CB  HIS B 477     8242   4144   3024   -456   1744   -152       C  
ATOM   2199  CG  HIS B 477      -9.624 -13.874  -4.880  1.00 50.43           C  
ANISOU 2199  CG  HIS B 477     9514   5397   4252   -756   1779   -239       C  
ATOM   2200  ND1 HIS B 477     -10.253 -14.981  -5.409  1.00 57.18           N  
ANISOU 2200  ND1 HIS B 477    10624   6137   4965   -903   1861   -276       N  
ATOM   2201  CD2 HIS B 477     -10.612 -13.036  -4.483  1.00 57.09           C  
ANISOU 2201  CD2 HIS B 477    10154   6351   5186   -937   1744   -300       C  
ATOM   2202  CE1 HIS B 477     -11.562 -14.821  -5.331  1.00 57.00           C  
ANISOU 2202  CE1 HIS B 477    10548   6162   4948  -1167   1874   -356       C  
ATOM   2203  NE2 HIS B 477     -11.806 -13.648  -4.774  1.00 58.18           N  
ANISOU 2203  NE2 HIS B 477    10418   6450   5237  -1186   1802   -372       N  
ATOM   2204  N   GLY B 478      -5.459 -14.761  -2.489  1.00 49.24           N  
ANISOU 2204  N   GLY B 478     9740   5029   3939     68   1754    -29       N  
ATOM   2205  CA  GLY B 478      -4.095 -14.437  -2.115  1.00 43.49           C  
ANISOU 2205  CA  GLY B 478     8940   4351   3234    345   1705     40       C  
ATOM   2206  C   GLY B 478      -4.045 -13.770  -0.753  1.00 46.79           C  
ANISOU 2206  C   GLY B 478     9248   4823   3706    343   1663     27       C  
ATOM   2207  O   GLY B 478      -5.033 -13.772  -0.020  1.00 52.79           O  
ANISOU 2207  O   GLY B 478    10048   5554   4457    139   1683    -34       O  
ATOM   2208  N   ASP B 479      -2.897 -13.197  -0.413  1.00 49.56           N  
ANISOU 2208  N   ASP B 479     9456   5266   4108    566   1605     83       N  
ATOM   2209  CA  ASP B 479      -2.737 -12.513   0.865  1.00 61.73           C  
ANISOU 2209  CA  ASP B 479    10878   6877   5702    581   1560     72       C  
ATOM   2210  C   ASP B 479      -3.505 -11.195   0.900  1.00 67.46           C  
ANISOU 2210  C   ASP B 479    11276   7751   6603    412   1504     29       C  
ATOM   2211  O   ASP B 479      -3.502 -10.441  -0.071  1.00 63.71           O  
ANISOU 2211  O   ASP B 479    10573   7386   6247    411   1462     45       O  
ATOM   2212  CB  ASP B 479      -1.256 -12.263   1.155  1.00 71.23           C  
ANISOU 2212  CB  ASP B 479    12012   8150   6901    868   1513    141       C  
ATOM   2213  CG  ASP B 479      -0.519 -13.525   1.547  1.00 78.64           C  
ANISOU 2213  CG  ASP B 479    13286   8943   7649   1044   1564    174       C  
ATOM   2214  OD1 ASP B 479      -1.188 -14.499   1.947  1.00 82.43           O  
ANISOU 2214  OD1 ASP B 479    14054   9263   8002    929   1632    138       O  
ATOM   2215  OD2 ASP B 479       0.727 -13.540   1.461  1.00 83.10           O  
ANISOU 2215  OD2 ASP B 479    13830   9557   8185   1298   1536    234       O  
ATOM   2216  N   VAL B 480      -4.167 -10.926   2.023  1.00 81.81           N  
ANISOU 2216  N   VAL B 480    13077   9575   8430    274   1502    -26       N  
ATOM   2217  CA  VAL B 480      -4.868  -9.662   2.219  1.00 69.49           C  
ANISOU 2217  CA  VAL B 480    11219   8158   7028    129   1448    -72       C  
ATOM   2218  C   VAL B 480      -4.733  -9.192   3.664  1.00 65.79           C  
ANISOU 2218  C   VAL B 480    10690   7737   6571    136   1420    -96       C  
ATOM   2219  O   VAL B 480      -4.407  -9.978   4.550  1.00 73.91           O  
ANISOU 2219  O   VAL B 480    11938   8673   7472    197   1454    -91       O  
ATOM   2220  CB  VAL B 480      -6.368  -9.766   1.865  1.00 55.90           C  
ANISOU 2220  CB  VAL B 480     9511   6414   5315   -146   1484   -147       C  
ATOM   2221  CG1 VAL B 480      -6.548 -10.237   0.431  1.00 48.55           C  
ANISOU 2221  CG1 VAL B 480     8635   5445   4365   -166   1512   -130       C  
ATOM   2222  CG2 VAL B 480      -7.087 -10.697   2.834  1.00 54.72           C  
ANISOU 2222  CG2 VAL B 480     9625   6139   5026   -292   1551   -198       C  
ATOM   2223  N   ALA B 481      -4.976  -7.906   3.890  1.00 54.58           N  
ANISOU 2223  N   ALA B 481     8975   6463   5299     78   1356   -125       N  
ATOM   2224  CA  ALA B 481      -5.005  -7.353   5.239  1.00 46.41           C  
ANISOU 2224  CA  ALA B 481     7856   5492   4288     53   1330   -164       C  
ATOM   2225  C   ALA B 481      -6.399  -6.809   5.521  1.00 49.48           C  
ANISOU 2225  C   ALA B 481     8129   5930   4743   -200   1332   -252       C  
ATOM   2226  O   ALA B 481      -6.938  -6.029   4.737  1.00 53.39           O  
ANISOU 2226  O   ALA B 481     8427   6506   5354   -285   1299   -272       O  
ATOM   2227  CB  ALA B 481      -3.959  -6.266   5.398  1.00 56.10           C  
ANISOU 2227  CB  ALA B 481     8837   6857   5621    220   1251   -125       C  
ATOM   2228  N   VAL B 482      -6.983  -7.225   6.640  1.00 57.97           N  
ANISOU 2228  N   VAL B 482     9327   6962   5736   -315   1369   -306       N  
ATOM   2229  CA  VAL B 482      -8.357  -6.855   6.960  1.00 67.90           C  
ANISOU 2229  CA  VAL B 482    10501   8266   7030   -561   1380   -395       C  
ATOM   2230  C   VAL B 482      -8.433  -5.949   8.184  1.00 77.97           C  
ANISOU 2230  C   VAL B 482    11598   9658   8370   -587   1340   -447       C  
ATOM   2231  O   VAL B 482      -7.751  -6.178   9.179  1.00 82.64           O  
ANISOU 2231  O   VAL B 482    12265  10237   8897   -482   1339   -433       O  
ATOM   2232  CB  VAL B 482      -9.225  -8.103   7.214  1.00 62.75           C  
ANISOU 2232  CB  VAL B 482    10139   7481   6222   -726   1465   -429       C  
ATOM   2233  CG1 VAL B 482     -10.691  -7.717   7.323  1.00 65.85           C  
ANISOU 2233  CG1 VAL B 482    10426   7942   6654   -988   1477   -520       C  
ATOM   2234  CG2 VAL B 482      -9.026  -9.128   6.109  1.00 51.43           C  
ANISOU 2234  CG2 VAL B 482     8921   5916   4702   -684   1512   -380       C  
ATOM   2235  N   LYS B 483      -9.266  -4.917   8.100  1.00 78.16           N  
ANISOU 2235  N   LYS B 483    11385   9798   8516   -722   1305   -512       N  
ATOM   2236  CA  LYS B 483      -9.559  -4.059   9.242  1.00 81.05           C  
ANISOU 2236  CA  LYS B 483    11580  10274   8940   -781   1274   -583       C  
ATOM   2237  C   LYS B 483     -11.014  -4.258   9.639  1.00 79.25           C  
ANISOU 2237  C   LYS B 483    11382  10057   8672  -1029   1318   -672       C  
ATOM   2238  O   LYS B 483     -11.919  -3.888   8.891  1.00 79.37           O  
ANISOU 2238  O   LYS B 483    11294  10116   8748  -1160   1313   -712       O  
ATOM   2239  CB  LYS B 483      -9.318  -2.591   8.887  1.00 90.38           C  
ANISOU 2239  CB  LYS B 483    12453  11591  10295   -728   1193   -597       C  
ATOM   2240  CG  LYS B 483      -9.971  -1.610   9.851  1.00 96.98           C  
ANISOU 2240  CG  LYS B 483    13094  12546  11207   -838   1164   -697       C  
ATOM   2241  CD  LYS B 483     -10.072  -0.210   9.255  1.00102.65           C  
ANISOU 2241  CD  LYS B 483    13538  13372  12091   -830   1090   -726       C  
ATOM   2242  CE  LYS B 483      -8.722   0.490   9.195  1.00 99.54           C  
ANISOU 2242  CE  LYS B 483    13029  13020  11771   -630   1027   -670       C  
ATOM   2243  NZ  LYS B 483      -8.856   1.891   8.702  1.00 94.13           N  
ANISOU 2243  NZ  LYS B 483    12101  12427  11238   -635    952   -708       N  
ATOM   2244  N   MET B 484     -11.241  -4.837  10.814  1.00 63.04           N  
ANISOU 2244  N   MET B 484     9468   7976   6510  -1093   1360   -705       N  
ATOM   2245  CA  MET B 484     -12.595  -5.188  11.234  1.00 67.56           C  
ANISOU 2245  CA  MET B 484    10099   8555   7015  -1335   1410   -785       C  
ATOM   2246  C   MET B 484     -13.042  -4.516  12.532  1.00 74.36           C  
ANISOU 2246  C   MET B 484    10813   9538   7902  -1416   1396   -869       C  
ATOM   2247  O   MET B 484     -12.388  -4.627  13.570  1.00 73.98           O  
ANISOU 2247  O   MET B 484    10811   9492   7804  -1324   1392   -863       O  
ATOM   2248  CB  MET B 484     -12.735  -6.706  11.351  1.00 83.97           C  
ANISOU 2248  CB  MET B 484    12525  10473   8908  -1392   1490   -756       C  
ATOM   2249  CG  MET B 484     -11.421  -7.455  11.208  1.00 89.76           C  
ANISOU 2249  CG  MET B 484    13458  11082   9565  -1168   1496   -660       C  
ATOM   2250  SD  MET B 484     -11.641  -9.232  11.388  1.00192.94           S  
ANISOU 2250  SD  MET B 484    26959  23947  22404  -1239   1591   -636       S  
ATOM   2251  CE  MET B 484     -13.003  -9.490  10.257  1.00 57.21           C  
ANISOU 2251  CE  MET B 484     9785   6738   5214  -1486   1633   -683       C  
ATOM   2252  N   LEU B 485     -14.173  -3.825  12.457  1.00103.00           N  
ANISOU 2252  N   LEU B 485    14261  13274  11601  -1587   1388   -954       N  
ATOM   2253  CA  LEU B 485     -14.763  -3.177  13.615  1.00105.18           C  
ANISOU 2253  CA  LEU B 485    14385  13677  11900  -1685   1381  -1049       C  
ATOM   2254  C   LEU B 485     -15.645  -4.164  14.372  1.00105.05           C  
ANISOU 2254  C   LEU B 485    14564  13625  11724  -1872   1456  -1089       C  
ATOM   2255  O   LEU B 485     -16.775  -4.437  13.965  1.00105.69           O  
ANISOU 2255  O   LEU B 485    14671  13719  11768  -2064   1492  -1133       O  
ATOM   2256  CB  LEU B 485     -15.590  -1.975  13.165  1.00 83.01           C  
ANISOU 2256  CB  LEU B 485    11299  11006   9236  -1773   1336  -1128       C  
ATOM   2257  CG  LEU B 485     -16.344  -1.206  14.244  1.00 80.34           C  
ANISOU 2257  CG  LEU B 485    10777  10814   8934  -1883   1328  -1243       C  
ATOM   2258  CD1 LEU B 485     -15.420  -0.210  14.924  1.00 81.35           C  
ANISOU 2258  CD1 LEU B 485    10727  11015   9166  -1722   1267  -1260       C  
ATOM   2259  CD2 LEU B 485     -17.540  -0.500  13.631  1.00 74.85           C  
ANISOU 2259  CD2 LEU B 485     9904  10221   8316  -2027   1311  -1324       C  
ATOM   2260  N   ASN B 486     -15.123  -4.700  15.471  1.00 86.64           N  
ANISOU 2260  N   ASN B 486    12374  11257   9290  -1818   1476  -1076       N  
ATOM   2261  CA  ASN B 486     -15.851  -5.694  16.254  1.00 81.34           C  
ANISOU 2261  CA  ASN B 486    11915  10542   8449  -1986   1545  -1107       C  
ATOM   2262  C   ASN B 486     -16.802  -5.095  17.290  1.00 69.11           C  
ANISOU 2262  C   ASN B 486    10195   9153   6910  -2146   1549  -1218       C  
ATOM   2263  O   ASN B 486     -16.658  -5.335  18.488  1.00 61.88           O  
ANISOU 2263  O   ASN B 486     9340   8262   5910  -2148   1563  -1242       O  
ATOM   2264  CB  ASN B 486     -14.881  -6.675  16.923  1.00 84.60           C  
ANISOU 2264  CB  ASN B 486    12594  10829   8722  -1854   1568  -1039       C  
ATOM   2265  CG  ASN B 486     -13.847  -5.979  17.785  1.00 88.56           C  
ANISOU 2265  CG  ASN B 486    12957  11410   9283  -1665   1511  -1037       C  
ATOM   2266  OD1 ASN B 486     -12.814  -5.524  17.293  1.00 94.39           O  
ANISOU 2266  OD1 ASN B 486    13611  12143  10112  -1467   1461   -982       O  
ATOM   2267  ND2 ASN B 486     -14.118  -5.896  19.082  1.00 88.69           N  
ANISOU 2267  ND2 ASN B 486    12946  11510   9241  -1729   1519  -1102       N  
ATOM   2268  N   VAL B 487     -17.775  -4.318  16.824  1.00 76.42           N  
ANISOU 2268  N   VAL B 487    10906  10196   7933  -2275   1536  -1289       N  
ATOM   2269  CA  VAL B 487     -18.808  -3.783  17.705  1.00 77.24           C  
ANISOU 2269  CA  VAL B 487    10846  10461   8039  -2439   1547  -1402       C  
ATOM   2270  C   VAL B 487     -20.169  -4.398  17.365  1.00 88.47           C  
ANISOU 2270  C   VAL B 487    12356  11894   9365  -2692   1607  -1446       C  
ATOM   2271  O   VAL B 487     -20.589  -4.388  16.208  1.00102.02           O  
ANISOU 2271  O   VAL B 487    14054  13588  11121  -2742   1604  -1435       O  
ATOM   2272  CB  VAL B 487     -18.870  -2.237  17.645  1.00 65.26           C  
ANISOU 2272  CB  VAL B 487     8980   9103   6714  -2379   1479  -1473       C  
ATOM   2273  CG1 VAL B 487     -17.507  -1.638  17.970  1.00 66.00           C  
ANISOU 2273  CG1 VAL B 487     8991   9189   6896  -2143   1419  -1435       C  
ATOM   2274  CG2 VAL B 487     -19.355  -1.761  16.285  1.00 58.64           C  
ANISOU 2274  CG2 VAL B 487     8027   8276   5976  -2410   1452  -1473       C  
ATOM   2275  N   THR B 488     -20.845  -4.947  18.372  1.00 87.67           N  
ANISOU 2275  N   THR B 488    12351  11832   9128  -2853   1658  -1498       N  
ATOM   2276  CA  THR B 488     -22.112  -5.651  18.157  1.00 84.73           C  
ANISOU 2276  CA  THR B 488    12089  11470   8636  -3110   1721  -1540       C  
ATOM   2277  C   THR B 488     -23.044  -4.881  17.228  1.00 92.97           C  
ANISOU 2277  C   THR B 488    12905  12633   9786  -3207   1699  -1600       C  
ATOM   2278  O   THR B 488     -23.474  -5.400  16.198  1.00100.02           O  
ANISOU 2278  O   THR B 488    13900  13461  10643  -3296   1721  -1578       O  
ATOM   2279  CB  THR B 488     -22.839  -5.956  19.486  1.00 73.23           C  
ANISOU 2279  CB  THR B 488    10666  10108   7049  -3279   1766  -1615       C  
ATOM   2280  OG1 THR B 488     -22.013  -6.792  20.305  1.00 73.95           O  
ANISOU 2280  OG1 THR B 488    11002  10077   7019  -3196   1785  -1557       O  
ATOM   2281  CG2 THR B 488     -24.161  -6.664  19.223  1.00 65.22           C  
ANISOU 2281  CG2 THR B 488     9758   9117   5906  -3557   1830  -1661       C  
ATOM   2282  N   ALA B 489     -23.345  -3.640  17.597  1.00 81.34           N  
ANISOU 2282  N   ALA B 489    11128  11336   8440  -3184   1655  -1682       N  
ATOM   2283  CA  ALA B 489     -24.182  -2.772  16.778  1.00 86.08           C  
ANISOU 2283  CA  ALA B 489    11496  12063   9149  -3248   1621  -1747       C  
ATOM   2284  C   ALA B 489     -23.523  -1.410  16.603  1.00 79.38           C  
ANISOU 2284  C   ALA B 489    10387  11277   8497  -3048   1537  -1761       C  
ATOM   2285  O   ALA B 489     -23.460  -0.621  17.546  1.00 70.93           O  
ANISOU 2285  O   ALA B 489     9143  10320   7487  -3004   1516  -1829       O  
ATOM   2286  CB  ALA B 489     -25.556  -2.619  17.401  1.00129.83           C  
ANISOU 2286  CB  ALA B 489    16922  17783  14625  -3471   1657  -1864       C  
ATOM   2287  N   PRO B 490     -23.027  -1.132  15.390  1.00 81.67           N  
ANISOU 2287  N   PRO B 490    10656  11492   8882  -2929   1489  -1702       N  
ATOM   2288  CA  PRO B 490     -22.310   0.111  15.084  1.00 77.72           C  
ANISOU 2288  CA  PRO B 490     9943  11026   8561  -2736   1403  -1706       C  
ATOM   2289  C   PRO B 490     -23.155   1.368  15.261  1.00 76.64           C  
ANISOU 2289  C   PRO B 490     9569  11084   8465  -2688   1376  -1818       C  
ATOM   2290  O   PRO B 490     -24.276   1.446  14.755  1.00 72.20           O  
ANISOU 2290  O   PRO B 490     8976  10615   7843  -2773   1395  -1867       O  
ATOM   2291  CB  PRO B 490     -21.938  -0.056  13.608  1.00105.73           C  
ANISOU 2291  CB  PRO B 490    13558  14468  12147  -2659   1373  -1626       C  
ATOM   2292  CG  PRO B 490     -21.930  -1.522  13.382  1.00107.55           C  
ANISOU 2292  CG  PRO B 490    14081  14562  12221  -2742   1448  -1551       C  
ATOM   2293  CD  PRO B 490     -23.027  -2.060  14.247  1.00108.20           C  
ANISOU 2293  CD  PRO B 490    14218  14719  12173  -2965   1515  -1625       C  
ATOM   2294  N   THR B 491     -22.605   2.348  15.969  1.00 80.73           N  
ANISOU 2294  N   THR B 491     9932  11661   9082  -2547   1334  -1861       N  
ATOM   2295  CA  THR B 491     -23.261   3.635  16.145  1.00 84.57           C  
ANISOU 2295  CA  THR B 491    10213  12297   9621  -2468   1307  -1971       C  
ATOM   2296  C   THR B 491     -23.258   4.386  14.819  1.00 90.69           C  
ANISOU 2296  C   THR B 491    10932  13053  10474  -2335   1254  -1947       C  
ATOM   2297  O   THR B 491     -22.512   4.027  13.907  1.00 87.34           O  
ANISOU 2297  O   THR B 491    10597  12507  10082  -2273   1226  -1845       O  
ATOM   2298  CB  THR B 491     -22.532   4.491  17.203  1.00 81.21           C  
ANISOU 2298  CB  THR B 491     9658  11910   9289  -2341   1274  -2027       C  
ATOM   2299  OG1 THR B 491     -21.257   4.902  16.694  1.00 67.06           O  
ANISOU 2299  OG1 THR B 491     7859  10010   7612  -2162   1210  -1953       O  
ATOM   2300  CG2 THR B 491     -22.334   3.706  18.494  1.00 89.39           C  
ANISOU 2300  CG2 THR B 491    10756  12955  10252  -2460   1320  -2035       C  
ATOM   2301  N   PRO B 492     -24.098   5.426  14.701  1.00115.99           N  
ANISOU 2301  N   PRO B 492    13991  16376  13704  -2293   1240  -2042       N  
ATOM   2302  CA  PRO B 492     -24.111   6.250  13.488  1.00111.63           C  
ANISOU 2302  CA  PRO B 492    13384  15803  13226  -2164   1188  -2025       C  
ATOM   2303  C   PRO B 492     -22.733   6.842  13.195  1.00108.69           C  
ANISOU 2303  C   PRO B 492    12998  15315  12986  -1971   1122  -1962       C  
ATOM   2304  O   PRO B 492     -22.425   7.137  12.041  1.00115.95           O  
ANISOU 2304  O   PRO B 492    13930  16170  13954  -1880   1080  -1901       O  
ATOM   2305  CB  PRO B 492     -25.105   7.361  13.833  1.00 87.43           C  
ANISOU 2305  CB  PRO B 492    10164  12877  10180  -2144   1189  -2159       C  
ATOM   2306  CG  PRO B 492     -26.003   6.760  14.856  1.00 87.44           C  
ANISOU 2306  CG  PRO B 492    10163  12996  10065  -2323   1254  -2234       C  
ATOM   2307  CD  PRO B 492     -25.136   5.838  15.663  1.00 91.50           C  
ANISOU 2307  CD  PRO B 492    10780  13431  10554  -2375   1276  -2174       C  
ATOM   2308  N   GLN B 493     -21.917   7.003  14.232  1.00 74.71           N  
ANISOU 2308  N   GLN B 493     8663  10991   8732  -1918   1114  -1978       N  
ATOM   2309  CA  GLN B 493     -20.584   7.581  14.079  1.00 74.75           C  
ANISOU 2309  CA  GLN B 493     8646  10900   8856  -1748   1052  -1930       C  
ATOM   2310  C   GLN B 493     -19.619   6.631  13.369  1.00 79.39           C  
ANISOU 2310  C   GLN B 493     9369  11363   9432  -1737   1037  -1790       C  
ATOM   2311  O   GLN B 493     -18.990   7.001  12.376  1.00 87.74           O  
ANISOU 2311  O   GLN B 493    10433  12348  10557  -1622    986  -1726       O  
ATOM   2312  CB  GLN B 493     -20.016   8.003  15.438  1.00 95.62           C  
ANISOU 2312  CB  GLN B 493    11210  13574  11546  -1705   1047  -1999       C  
ATOM   2313  CG  GLN B 493     -20.925   8.939  16.220  1.00100.63           C  
ANISOU 2313  CG  GLN B 493    11710  14328  12198  -1713   1064  -2152       C  
ATOM   2314  CD  GLN B 493     -20.182   9.731  17.279  1.00104.18           C  
ANISOU 2314  CD  GLN B 493    12059  14786  12738  -1616   1036  -2230       C  
ATOM   2315  OE1 GLN B 493     -19.299   9.209  17.961  1.00 96.14           O  
ANISOU 2315  OE1 GLN B 493    11073  13745  11711  -1616   1031  -2191       O  
ATOM   2316  NE2 GLN B 493     -20.540  11.003  17.422  1.00111.38           N  
ANISOU 2316  NE2 GLN B 493    12851  15727  13740  -1537   1018  -2348       N  
ATOM   2317  N   GLN B 494     -19.504   5.409  13.881  1.00 86.63           N  
ANISOU 2317  N   GLN B 494    10402  12250  10265  -1861   1083  -1747       N  
ATOM   2318  CA  GLN B 494     -18.639   4.401  13.276  1.00 79.97           C  
ANISOU 2318  CA  GLN B 494     9707  11272   9405  -1867   1081  -1625       C  
ATOM   2319  C   GLN B 494     -19.096   4.096  11.855  1.00 70.82           C  
ANISOU 2319  C   GLN B 494     8616  10074   8218  -1889   1079  -1572       C  
ATOM   2320  O   GLN B 494     -18.302   3.695  11.007  1.00 59.57           O  
ANISOU 2320  O   GLN B 494     7272   8541   6819  -1832   1053  -1479       O  
ATOM   2321  CB  GLN B 494     -18.657   3.120  14.110  1.00 76.78           C  
ANISOU 2321  CB  GLN B 494     9447  10823   8902  -2026   1148  -1602       C  
ATOM   2322  CG  GLN B 494     -18.526   3.347  15.604  1.00 75.87           C  
ANISOU 2322  CG  GLN B 494     9258  10783   8785  -2043   1162  -1672       C  
ATOM   2323  CD  GLN B 494     -18.858   2.108  16.412  1.00 73.88           C  
ANISOU 2323  CD  GLN B 494     9199  10509   8365  -2160   1252  -1649       C  
ATOM   2324  OE1 GLN B 494     -17.967   1.416  16.901  1.00 71.97           O  
ANISOU 2324  OE1 GLN B 494     9113  10185   8048  -2072   1275  -1577       O  
ATOM   2325  NE2 GLN B 494     -20.144   1.819  16.548  1.00 72.85           N  
ANISOU 2325  NE2 GLN B 494     9069  10450   8163  -2357   1299  -1717       N  
ATOM   2326  N   LEU B 495     -20.387   4.293  11.609  1.00 79.81           N  
ANISOU 2326  N   LEU B 495     9714  11309   9300  -1975   1106  -1639       N  
ATOM   2327  CA  LEU B 495     -20.977   4.048  10.300  1.00 71.19           C  
ANISOU 2327  CA  LEU B 495     8668  10210   8169  -2010   1104  -1606       C  
ATOM   2328  C   LEU B 495     -20.477   5.055   9.269  1.00 73.65           C  
ANISOU 2328  C   LEU B 495     8898  10503   8584  -1833   1030  -1575       C  
ATOM   2329  O   LEU B 495     -19.969   4.676   8.215  1.00 80.63           O  
ANISOU 2329  O   LEU B 495     9852  11306   9478  -1794   1004  -1491       O  
ATOM   2330  CB  LEU B 495     -22.501   4.120  10.395  1.00 47.34           C  
ANISOU 2330  CB  LEU B 495     5602   7324   5060  -2145   1148  -1697       C  
ATOM   2331  CG  LEU B 495     -23.291   3.760   9.138  1.00 57.28           C  
ANISOU 2331  CG  LEU B 495     6906   8603   6254  -2217   1155  -1678       C  
ATOM   2332  CD1 LEU B 495     -23.369   2.250   8.977  1.00 52.73           C  
ANISOU 2332  CD1 LEU B 495     6522   7943   5571  -2385   1213  -1627       C  
ATOM   2333  CD2 LEU B 495     -24.683   4.365   9.203  1.00 66.10           C  
ANISOU 2333  CD2 LEU B 495     7911   9884   7321  -2286   1172  -1781       C  
ATOM   2334  N   GLN B 496     -20.630   6.340   9.579  1.00 65.72           N  
ANISOU 2334  N   GLN B 496     7753   9564   7653  -1732    998  -1648       N  
ATOM   2335  CA  GLN B 496     -20.196   7.409   8.682  1.00 71.15           C  
ANISOU 2335  CA  GLN B 496     8376  10221   8439  -1574    933  -1628       C  
ATOM   2336  C   GLN B 496     -18.683   7.418   8.517  1.00 65.09           C  
ANISOU 2336  C   GLN B 496     7641   9341   7750  -1450    884  -1542       C  
ATOM   2337  O   GLN B 496     -18.168   7.751   7.450  1.00 68.22           O  
ANISOU 2337  O   GLN B 496     8046   9682   8193  -1355    835  -1480       O  
ATOM   2338  CB  GLN B 496     -20.680   8.770   9.188  1.00 88.86           C  
ANISOU 2338  CB  GLN B 496    10484  12530  10749  -1507    922  -1740       C  
ATOM   2339  CG  GLN B 496     -22.157   9.039   8.936  1.00101.03           C  
ANISOU 2339  CG  GLN B 496    11973  14186  12228  -1592    951  -1820       C  
ATOM   2340  CD  GLN B 496     -22.457   9.357   7.481  1.00 96.34           C  
ANISOU 2340  CD  GLN B 496    11385  13583  11636  -1549    918  -1776       C  
ATOM   2341  OE1 GLN B 496     -23.495   8.962   6.948  1.00 85.87           O  
ANISOU 2341  OE1 GLN B 496    10070  12341  10218  -1653    941  -1789       O  
ATOM   2342  NE2 GLN B 496     -21.547  10.075   6.832  1.00 94.61           N  
ANISOU 2342  NE2 GLN B 496    11159  13270  11518  -1404    862  -1726       N  
ATOM   2343  N   ALA B 497     -17.975   7.060   9.582  1.00 55.19           N  
ANISOU 2343  N   ALA B 497     6402   8063   6504  -1456    895  -1541       N  
ATOM   2344  CA  ALA B 497     -16.527   6.927   9.519  1.00 57.00           C  
ANISOU 2344  CA  ALA B 497     6665   8201   6793  -1355    851  -1461       C  
ATOM   2345  C   ALA B 497     -16.164   5.826   8.532  1.00 64.12           C  
ANISOU 2345  C   ALA B 497     7695   9020   7649  -1390    854  -1353       C  
ATOM   2346  O   ALA B 497     -15.151   5.905   7.836  1.00 57.06           O  
ANISOU 2346  O   ALA B 497     6818   8060   6802  -1273    813  -1268       O  
ATOM   2347  CB  ALA B 497     -15.962   6.616  10.890  1.00 38.37           C  
ANISOU 2347  CB  ALA B 497     4300   5847   4430  -1377    869  -1485       C  
ATOM   2348  N   PHE B 498     -17.003   4.797   8.482  1.00 69.20           N  
ANISOU 2348  N   PHE B 498     8433   9667   8193  -1542    916  -1354       N  
ATOM   2349  CA  PHE B 498     -16.808   3.687   7.561  1.00 62.55           C  
ANISOU 2349  CA  PHE B 498     7736   8736   7293  -1577    945  -1259       C  
ATOM   2350  C   PHE B 498     -17.041   4.128   6.120  1.00 67.68           C  
ANISOU 2350  C   PHE B 498     8350   9398   7967  -1525    897  -1237       C  
ATOM   2351  O   PHE B 498     -16.215   3.872   5.244  1.00 66.77           O  
ANISOU 2351  O   PHE B 498     8285   9220   7866  -1411    890  -1127       O  
ATOM   2352  CB  PHE B 498     -17.729   2.521   7.926  1.00 41.51           C  
ANISOU 2352  CB  PHE B 498     5203   6063   4505  -1770   1032  -1282       C  
ATOM   2353  CG  PHE B 498     -17.508   1.291   7.094  1.00 47.91           C  
ANISOU 2353  CG  PHE B 498     6209   6768   5228  -1781   1088  -1183       C  
ATOM   2354  CD1 PHE B 498     -16.293   0.629   7.127  1.00 48.28           C  
ANISOU 2354  CD1 PHE B 498     6389   6704   5250  -1647   1114  -1075       C  
ATOM   2355  CD2 PHE B 498     -18.518   0.791   6.288  1.00 56.18           C  
ANISOU 2355  CD2 PHE B 498     7311   7829   6206  -1921   1113  -1209       C  
ATOM   2356  CE1 PHE B 498     -16.084  -0.505   6.366  1.00 39.90           C  
ANISOU 2356  CE1 PHE B 498     5523   5536   4100  -1647   1165   -997       C  
ATOM   2357  CE2 PHE B 498     -18.316  -0.345   5.525  1.00 54.09           C  
ANISOU 2357  CE2 PHE B 498     7234   7461   5857  -1935   1166  -1132       C  
ATOM   2358  CZ  PHE B 498     -17.097  -0.993   5.565  1.00 51.53           C  
ANISOU 2358  CZ  PHE B 498     7053   7015   5511  -1795   1193  -1028       C  
ATOM   2359  N   LYS B 499     -18.165   4.798   5.881  1.00 64.93           N  
ANISOU 2359  N   LYS B 499     7918   9151   7602  -1563    892  -1311       N  
ATOM   2360  CA  LYS B 499     -18.496   5.289   4.546  1.00 72.42           C  
ANISOU 2360  CA  LYS B 499     8830  10128   8560  -1511    850  -1291       C  
ATOM   2361  C   LYS B 499     -17.444   6.270   4.030  1.00 67.99           C  
ANISOU 2361  C   LYS B 499     8206   9524   8102  -1328    776  -1241       C  
ATOM   2362  O   LYS B 499     -17.018   6.188   2.877  1.00 67.15           O  
ANISOU 2362  O   LYS B 499     8117   9390   8007  -1243    764  -1137       O  
ATOM   2363  CB  LYS B 499     -19.882   5.944   4.539  1.00 83.62           C  
ANISOU 2363  CB  LYS B 499    10162  11669   9940  -1568    867  -1379       C  
ATOM   2364  CG  LYS B 499     -21.032   4.963   4.721  1.00 85.76           C  
ANISOU 2364  CG  LYS B 499    10496  11999  10089  -1761    938  -1420       C  
ATOM   2365  CD  LYS B 499     -22.388   5.662   4.698  1.00 86.16           C  
ANISOU 2365  CD  LYS B 499    10447  12189  10099  -1813    950  -1510       C  
ATOM   2366  CE  LYS B 499     -22.952   5.845   6.101  1.00 87.62           C  
ANISOU 2366  CE  LYS B 499    10582  12445  10263  -1882    996  -1604       C  
ATOM   2367  NZ  LYS B 499     -24.354   6.356   6.081  1.00 88.20           N  
ANISOU 2367  NZ  LYS B 499    10567  12665  10280  -1955   1016  -1698       N  
ATOM   2368  N   ASN B 500     -17.031   7.195   4.891  1.00 64.66           N  
ANISOU 2368  N   ASN B 500     7708   9106   7756  -1249    756  -1289       N  
ATOM   2369  CA  ASN B 500     -16.030   8.189   4.527  1.00 61.69           C  
ANISOU 2369  CA  ASN B 500     7272   8683   7483  -1070    716  -1223       C  
ATOM   2370  C   ASN B 500     -14.709   7.567   4.086  1.00 58.57           C  
ANISOU 2370  C   ASN B 500     6934   8217   7104   -976    711  -1080       C  
ATOM   2371  O   ASN B 500     -14.181   7.904   3.026  1.00 55.46           O  
ANISOU 2371  O   ASN B 500     6522   7799   6750   -866    690   -974       O  
ATOM   2372  CB  ASN B 500     -15.795   9.165   5.682  1.00 63.32           C  
ANISOU 2372  CB  ASN B 500     7402   8893   7766  -1027    705  -1318       C  
ATOM   2373  CG  ASN B 500     -16.993  10.056   5.944  1.00 66.32           C  
ANISOU 2373  CG  ASN B 500     7709   9336   8154  -1067    717  -1448       C  
ATOM   2374  OD1 ASN B 500     -18.038   9.915   5.309  1.00 66.00           O  
ANISOU 2374  OD1 ASN B 500     7671   9354   8051  -1131    734  -1461       O  
ATOM   2375  ND2 ASN B 500     -16.846  10.982   6.885  1.00 64.10           N  
ANISOU 2375  ND2 ASN B 500     7350   9049   7955  -1019    718  -1534       N  
ATOM   2376  N   GLU B 501     -14.178   6.660   4.900  1.00 57.24           N  
ANISOU 2376  N   GLU B 501     6830   8017   6901  -1014    738  -1066       N  
ATOM   2377  CA  GLU B 501     -12.912   6.010   4.580  1.00 55.97           C  
ANISOU 2377  CA  GLU B 501     6733   7795   6739   -908    747   -933       C  
ATOM   2378  C   GLU B 501     -13.045   5.094   3.367  1.00 57.42           C  
ANISOU 2378  C   GLU B 501     7009   7948   6862   -920    774   -846       C  
ATOM   2379  O   GLU B 501     -12.099   4.923   2.601  1.00 59.08           O  
ANISOU 2379  O   GLU B 501     7239   8123   7086   -799    763   -732       O  
ATOM   2380  CB  GLU B 501     -12.370   5.229   5.780  1.00 80.45           C  
ANISOU 2380  CB  GLU B 501     9901  10868   9797   -926    790   -931       C  
ATOM   2381  CG  GLU B 501     -10.998   4.619   5.530  1.00 88.51           C  
ANISOU 2381  CG  GLU B 501    10998  11832  10800   -784    802   -799       C  
ATOM   2382  CD  GLU B 501     -10.421   3.927   6.751  1.00100.22           C  
ANISOU 2382  CD  GLU B 501    12562  13293  12223   -767    846   -794       C  
ATOM   2383  OE1 GLU B 501      -9.284   3.418   6.657  1.00100.56           O  
ANISOU 2383  OE1 GLU B 501    12681  13297  12232   -633    856   -697       O  
ATOM   2384  OE2 GLU B 501     -11.098   3.891   7.800  1.00103.57           O  
ANISOU 2384  OE2 GLU B 501    12981  13748  12625   -878    871   -888       O  
ATOM   2385  N   VAL B 502     -14.224   4.506   3.196  1.00 73.22           N  
ANISOU 2385  N   VAL B 502     9062   9967   8790  -1072    810   -906       N  
ATOM   2386  CA  VAL B 502     -14.483   3.652   2.044  1.00 72.05           C  
ANISOU 2386  CA  VAL B 502     9002   9795   8580  -1104    839   -846       C  
ATOM   2387  C   VAL B 502     -14.565   4.482   0.768  1.00 74.98           C  
ANISOU 2387  C   VAL B 502     9278  10216   8997  -1021    783   -803       C  
ATOM   2388  O   VAL B 502     -14.091   4.066  -0.289  1.00 80.97           O  
ANISOU 2388  O   VAL B 502    10070  10950   9745   -955    784   -706       O  
ATOM   2389  CB  VAL B 502     -15.777   2.833   2.223  1.00 56.16           C  
ANISOU 2389  CB  VAL B 502     7072   7796   6468  -1309    895   -929       C  
ATOM   2390  CG1 VAL B 502     -16.636   2.895   0.968  1.00 48.92           C  
ANISOU 2390  CG1 VAL B 502     6129   6937   5520  -1362    879   -938       C  
ATOM   2391  CG2 VAL B 502     -15.444   1.395   2.583  1.00 49.39           C  
ANISOU 2391  CG2 VAL B 502     6411   6836   5521  -1359    981   -884       C  
ATOM   2392  N   GLY B 503     -15.163   5.662   0.877  1.00 59.40           N  
ANISOU 2392  N   GLY B 503     7192   8308   7070  -1015    743   -869       N  
ATOM   2393  CA  GLY B 503     -15.308   6.550  -0.260  1.00 58.24           C  
ANISOU 2393  CA  GLY B 503     6963   8201   6965   -928    706   -812       C  
ATOM   2394  C   GLY B 503     -13.994   7.164  -0.700  1.00 63.60           C  
ANISOU 2394  C   GLY B 503     7596   8835   7735   -754    672   -687       C  
ATOM   2395  O   GLY B 503     -13.798   7.439  -1.883  1.00 74.18           O  
ANISOU 2395  O   GLY B 503     8902  10186   9097   -680    653   -585       O  
ATOM   2396  N   VAL B 504     -13.090   7.380   0.251  1.00 53.37           N  
ANISOU 2396  N   VAL B 504     6294   7495   6487   -695    666   -690       N  
ATOM   2397  CA  VAL B 504     -11.800   7.996  -0.050  1.00 50.40           C  
ANISOU 2397  CA  VAL B 504     5873   7083   6194   -545    636   -578       C  
ATOM   2398  C   VAL B 504     -10.816   6.980  -0.626  1.00 50.76           C  
ANISOU 2398  C   VAL B 504     5988   7103   6196   -481    643   -465       C  
ATOM   2399  O   VAL B 504      -9.956   7.323  -1.438  1.00 52.62           O  
ANISOU 2399  O   VAL B 504     6188   7332   6473   -367    617   -346       O  
ATOM   2400  CB  VAL B 504     -11.181   8.674   1.193  1.00 39.27           C  
ANISOU 2400  CB  VAL B 504     4422   5649   4852   -509    626   -632       C  
ATOM   2401  CG1 VAL B 504     -10.935   7.657   2.287  1.00 53.76           C  
ANISOU 2401  CG1 VAL B 504     6331   7478   6619   -566    651   -685       C  
ATOM   2402  CG2 VAL B 504      -9.885   9.376   0.828  1.00 44.46           C  
ANISOU 2402  CG2 VAL B 504     5027   6271   5594   -373    598   -517       C  
ATOM   2403  N   LEU B 505     -10.952   5.728  -0.205  1.00 45.78           N  
ANISOU 2403  N   LEU B 505     5463   6449   5483   -554    688   -498       N  
ATOM   2404  CA  LEU B 505     -10.084   4.659  -0.683  1.00 40.81           C  
ANISOU 2404  CA  LEU B 505     4926   5777   4804   -486    717   -401       C  
ATOM   2405  C   LEU B 505     -10.374   4.311  -2.140  1.00 43.62           C  
ANISOU 2405  C   LEU B 505     5292   6150   5132   -482    718   -337       C  
ATOM   2406  O   LEU B 505      -9.456   4.114  -2.935  1.00 49.94           O  
ANISOU 2406  O   LEU B 505     6093   6944   5938   -366    708   -228       O  
ATOM   2407  CB  LEU B 505     -10.241   3.414   0.193  1.00 46.41           C  
ANISOU 2407  CB  LEU B 505     5780   6428   5425   -566    788   -448       C  
ATOM   2408  CG  LEU B 505      -9.640   3.472   1.598  1.00 43.77           C  
ANISOU 2408  CG  LEU B 505     5456   6077   5095   -537    796   -477       C  
ATOM   2409  CD1 LEU B 505     -10.148   2.318   2.444  1.00 43.15           C  
ANISOU 2409  CD1 LEU B 505     5535   5942   4917   -647    874   -529       C  
ATOM   2410  CD2 LEU B 505      -8.121   3.468   1.536  1.00 40.42           C  
ANISOU 2410  CD2 LEU B 505     5031   5642   4685   -359    779   -369       C  
ATOM   2411  N   ARG B 506     -11.656   4.240  -2.484  1.00 50.84           N  
ANISOU 2411  N   ARG B 506     6208   7098   6011   -610    728   -410       N  
ATOM   2412  CA  ARG B 506     -12.070   3.831  -3.822  1.00 53.59           C  
ANISOU 2412  CA  ARG B 506     6567   7474   6319   -629    733   -366       C  
ATOM   2413  C   ARG B 506     -11.631   4.835  -4.885  1.00 54.67           C  
ANISOU 2413  C   ARG B 506     6583   7663   6525   -507    673   -259       C  
ATOM   2414  O   ARG B 506     -11.627   4.529  -6.078  1.00 57.84           O  
ANISOU 2414  O   ARG B 506     6980   8095   6904   -484    670   -190       O  
ATOM   2415  CB  ARG B 506     -13.586   3.630  -3.876  1.00 51.21           C  
ANISOU 2415  CB  ARG B 506     6283   7219   5957   -802    754   -473       C  
ATOM   2416  CG  ARG B 506     -14.391   4.918  -3.907  1.00 56.20           C  
ANISOU 2416  CG  ARG B 506     6789   7933   6633   -812    707   -516       C  
ATOM   2417  CD  ARG B 506     -15.875   4.625  -4.043  1.00 71.43           C  
ANISOU 2417  CD  ARG B 506     8733   9927   8480   -979    729   -617       C  
ATOM   2418  NE  ARG B 506     -16.130   3.555  -5.004  1.00 83.62           N  
ANISOU 2418  NE  ARG B 506    10354  11474   9945  -1048    762   -592       N  
ATOM   2419  CZ  ARG B 506     -16.215   3.731  -6.319  1.00 89.94           C  
ANISOU 2419  CZ  ARG B 506    11099  12333  10741  -1003    737   -518       C  
ATOM   2420  NH1 ARG B 506     -16.063   4.941  -6.841  1.00 96.69           N  
ANISOU 2420  NH1 ARG B 506    11830  13241  11668   -886    684   -444       N  
ATOM   2421  NH2 ARG B 506     -16.450   2.696  -7.114  1.00 85.26           N  
ANISOU 2421  NH2 ARG B 506    10584  11740  10072  -1079    775   -510       N  
ATOM   2422  N   LYS B 507     -11.255   6.031  -4.446  1.00 39.49           N  
ANISOU 2422  N   LYS B 507     4572   5745   4688   -434    634   -241       N  
ATOM   2423  CA  LYS B 507     -10.822   7.078  -5.363  1.00 42.63           C  
ANISOU 2423  CA  LYS B 507     4871   6167   5160   -328    591   -123       C  
ATOM   2424  C   LYS B 507      -9.315   7.079  -5.568  1.00 44.39           C  
ANISOU 2424  C   LYS B 507     5087   6364   5416   -194    573     -2       C  
ATOM   2425  O   LYS B 507      -8.772   7.982  -6.204  1.00 47.35           O  
ANISOU 2425  O   LYS B 507     5387   6746   5859   -112    543    107       O  
ATOM   2426  CB  LYS B 507     -11.279   8.445  -4.862  1.00 54.93           C  
ANISOU 2426  CB  LYS B 507     6347   7720   6803   -332    577   -161       C  
ATOM   2427  CG  LYS B 507     -12.782   8.599  -4.849  1.00 68.89           C  
ANISOU 2427  CG  LYS B 507     8101   9538   8537   -443    592   -262       C  
ATOM   2428  CD  LYS B 507     -13.203   9.999  -4.455  1.00 83.00           C  
ANISOU 2428  CD  LYS B 507     9799  11310  10427   -426    589   -288       C  
ATOM   2429  CE  LYS B 507     -14.719  10.123  -4.463  1.00 96.77           C  
ANISOU 2429  CE  LYS B 507    11523  13121  12124   -529    608   -386       C  
ATOM   2430  NZ  LYS B 507     -15.176  11.530  -4.271  1.00106.68           N  
ANISOU 2430  NZ  LYS B 507    12678  14357  13498   -499    612   -395       N  
ATOM   2431  N   THR B 508      -8.642   6.066  -5.032  1.00 42.76           N  
ANISOU 2431  N   THR B 508     4964   6125   5159   -175    600    -15       N  
ATOM   2432  CA  THR B 508      -7.190   5.984  -5.136  1.00 46.94           C  
ANISOU 2432  CA  THR B 508     5490   6645   5701    -42    587     93       C  
ATOM   2433  C   THR B 508      -6.716   4.784  -5.952  1.00 41.57           C  
ANISOU 2433  C   THR B 508     4880   5965   4950     11    616    154       C  
ATOM   2434  O   THR B 508      -7.121   3.647  -5.710  1.00 41.50           O  
ANISOU 2434  O   THR B 508     4985   5914   4870    -51    674     88       O  
ATOM   2435  CB  THR B 508      -6.519   5.946  -3.746  1.00 56.11           C  
ANISOU 2435  CB  THR B 508     6682   7772   6866    -19    597     46       C  
ATOM   2436  OG1 THR B 508      -6.857   4.723  -3.078  1.00 55.74           O  
ANISOU 2436  OG1 THR B 508     6754   7684   6740    -80    654    -33       O  
ATOM   2437  CG2 THR B 508      -6.974   7.126  -2.904  1.00 56.17           C  
ANISOU 2437  CG2 THR B 508     6620   7774   6948    -73    576    -32       C  
ATOM   2438  N   ARG B 509      -5.854   5.062  -6.925  1.00 39.12           N  
ANISOU 2438  N   ARG B 509     4512   5694   4657    121    584    283       N  
ATOM   2439  CA  ARG B 509      -5.196   4.032  -7.717  1.00 35.22           C  
ANISOU 2439  CA  ARG B 509     4071   5208   4103    201    611    349       C  
ATOM   2440  C   ARG B 509      -3.775   4.473  -8.040  1.00 23.84           C  
ANISOU 2440  C   ARG B 509     2569   3809   2681    349    574    481       C  
ATOM   2441  O   ARG B 509      -3.500   4.962  -9.135  1.00 25.95           O  
ANISOU 2441  O   ARG B 509     2759   4134   2968    393    538    587       O  
ATOM   2442  CB  ARG B 509      -5.968   3.756  -9.008  1.00 41.81           C  
ANISOU 2442  CB  ARG B 509     4888   6082   4915    150    615    363       C  
ATOM   2443  CG  ARG B 509      -7.214   2.910  -8.820  1.00 35.75           C  
ANISOU 2443  CG  ARG B 509     4219   5277   4088      3    671    238       C  
ATOM   2444  CD  ARG B 509      -7.937   2.688 -10.136  1.00 30.76           C  
ANISOU 2444  CD  ARG B 509     3560   4702   3425    -51    671    255       C  
ATOM   2445  NE  ARG B 509      -9.031   1.732  -9.997  1.00 38.14           N  
ANISOU 2445  NE  ARG B 509     4612   5598   4282   -204    735    139       N  
ATOM   2446  CZ  ARG B 509      -8.891   0.416 -10.110  1.00 35.02           C  
ANISOU 2446  CZ  ARG B 509     4372   5133   3801   -225    811    115       C  
ATOM   2447  NH1 ARG B 509      -7.700  -0.109 -10.367  1.00 35.13           N  
ANISOU 2447  NH1 ARG B 509     4436   5116   3796    -84    833    192       N  
ATOM   2448  NH2 ARG B 509      -9.943  -0.379  -9.965  1.00 31.56           N  
ANISOU 2448  NH2 ARG B 509     4054   4651   3284   -387    870     15       N  
ATOM   2449  N   HIS B 510      -2.879   4.304  -7.072  1.00 32.42           N  
ANISOU 2449  N   HIS B 510     3693   4874   3750    418    583    478       N  
ATOM   2450  CA  HIS B 510      -1.491   4.724  -7.219  1.00 30.12           C  
ANISOU 2450  CA  HIS B 510     3352   4636   3457    546    550    594       C  
ATOM   2451  C   HIS B 510      -0.578   3.681  -6.590  1.00 31.98           C  
ANISOU 2451  C   HIS B 510     3683   4855   3613    657    590    588       C  
ATOM   2452  O   HIS B 510      -0.936   3.058  -5.592  1.00 35.83           O  
ANISOU 2452  O   HIS B 510     4269   5276   4070    621    635    491       O  
ATOM   2453  CB  HIS B 510      -1.274   6.081  -6.546  1.00 25.55           C  
ANISOU 2453  CB  HIS B 510     2698   4063   2948    509    513    600       C  
ATOM   2454  CG  HIS B 510       0.013   6.748  -6.921  1.00 12.44           C  
ANISOU 2454  CG  HIS B 510      978   2461   1287    594    488    727       C  
ATOM   2455  ND1 HIS B 510       1.205   6.478  -6.283  1.00 21.18           N  
ANISOU 2455  ND1 HIS B 510     2108   3604   2336    688    491    750       N  
ATOM   2456  CD2 HIS B 510       0.290   7.678  -7.862  1.00 14.31           C  
ANISOU 2456  CD2 HIS B 510     1138   2730   1570    591    469    838       C  
ATOM   2457  CE1 HIS B 510       2.162   7.213  -6.821  1.00 29.66           C  
ANISOU 2457  CE1 HIS B 510     3118   4738   3413    727    477    862       C  
ATOM   2458  NE2 HIS B 510       1.636   7.950  -7.780  1.00 26.97           N  
ANISOU 2458  NE2 HIS B 510     2718   4388   3142    666    468    920       N  
ATOM   2459  N   VAL B 511       0.602   3.495  -7.170  1.00 40.15           N  
ANISOU 2459  N   VAL B 511     4700   5950   4605    796    578    695       N  
ATOM   2460  CA  VAL B 511       1.526   2.470  -6.694  1.00 40.09           C  
ANISOU 2460  CA  VAL B 511     4794   5929   4508    935    620    698       C  
ATOM   2461  C   VAL B 511       2.117   2.811  -5.324  1.00 41.64           C  
ANISOU 2461  C   VAL B 511     4998   6132   4689    961    606    668       C  
ATOM   2462  O   VAL B 511       2.629   1.937  -4.625  1.00 46.58           O  
ANISOU 2462  O   VAL B 511     5736   6726   5237   1058    647    641       O  
ATOM   2463  CB  VAL B 511       2.665   2.214  -7.706  1.00 49.43           C  
ANISOU 2463  CB  VAL B 511     5946   7197   5640   1089    607    819       C  
ATOM   2464  CG1 VAL B 511       3.750   3.268  -7.568  1.00 51.50           C  
ANISOU 2464  CG1 VAL B 511     6106   7564   5897   1135    543    917       C  
ATOM   2465  CG2 VAL B 511       3.249   0.831  -7.500  1.00 67.60           C  
ANISOU 2465  CG2 VAL B 511     8397   9450   7838   1232    676    796       C  
ATOM   2466  N   ASN B 512       2.044   4.082  -4.942  1.00 44.40           N  
ANISOU 2466  N   ASN B 512     5245   6517   5107    875    557    667       N  
ATOM   2467  CA  ASN B 512       2.544   4.515  -3.639  1.00 38.03           C  
ANISOU 2467  CA  ASN B 512     4431   5725   4293    878    546    621       C  
ATOM   2468  C   ASN B 512       1.427   4.744  -2.627  1.00 25.78           C  
ANISOU 2468  C   ASN B 512     2894   4103   2799    741    559    488       C  
ATOM   2469  O   ASN B 512       1.640   5.354  -1.581  1.00 29.98           O  
ANISOU 2469  O   ASN B 512     3390   4648   3352    711    545    432       O  
ATOM   2470  CB  ASN B 512       3.398   5.776  -3.776  1.00 40.43           C  
ANISOU 2470  CB  ASN B 512     4625   6109   4626    873    506    691       C  
ATOM   2471  CG  ASN B 512       4.696   5.521  -4.511  1.00 39.71           C  
ANISOU 2471  CG  ASN B 512     4527   6116   4446   1011    499    815       C  
ATOM   2472  OD1 ASN B 512       5.060   6.257  -5.428  1.00 35.61           O  
ANISOU 2472  OD1 ASN B 512     3934   5647   3949    991    488    907       O  
ATOM   2473  ND2 ASN B 512       5.402   4.467  -4.115  1.00 39.58           N  
ANISOU 2473  ND2 ASN B 512     4591   6121   4325   1158    513    818       N  
ATOM   2474  N   ILE B 513       0.237   4.254  -2.951  1.00 28.26           N  
ANISOU 2474  N   ILE B 513     3257   4350   3131    651    590    431       N  
ATOM   2475  CA  ILE B 513      -0.900   4.326  -2.045  1.00 27.73           C  
ANISOU 2475  CA  ILE B 513     3216   4224   3096    514    610    303       C  
ATOM   2476  C   ILE B 513      -1.350   2.912  -1.707  1.00 38.55           C  
ANISOU 2476  C   ILE B 513     4751   5516   4381    506    685    248       C  
ATOM   2477  O   ILE B 513      -1.530   2.086  -2.602  1.00 46.03           O  
ANISOU 2477  O   ILE B 513     5776   6429   5284    526    722    278       O  
ATOM   2478  CB  ILE B 513      -2.080   5.096  -2.673  1.00 26.94           C  
ANISOU 2478  CB  ILE B 513     3043   4114   3077    384    589    270       C  
ATOM   2479  CG1 ILE B 513      -1.664   6.525  -3.027  1.00 22.10           C  
ANISOU 2479  CG1 ILE B 513     2309   3541   2547    388    538    331       C  
ATOM   2480  CG2 ILE B 513      -3.278   5.105  -1.734  1.00 27.35           C  
ANISOU 2480  CG2 ILE B 513     3124   4122   3148    245    612    131       C  
ATOM   2481  CD1 ILE B 513      -1.256   7.354  -1.833  1.00 36.84           C  
ANISOU 2481  CD1 ILE B 513     4130   5410   4459    372    525    271       C  
ATOM   2482  N   LEU B 514      -1.510   2.631  -0.416  1.00 62.90           N  
ANISOU 2482  N   LEU B 514     7902   8564   7432    472    712    168       N  
ATOM   2483  CA  LEU B 514      -2.003   1.334   0.038  1.00 64.98           C  
ANISOU 2483  CA  LEU B 514     8359   8731   7599    440    791    116       C  
ATOM   2484  C   LEU B 514      -3.165   0.893  -0.847  1.00 62.17           C  
ANISOU 2484  C   LEU B 514     8056   8324   7242    315    826     86       C  
ATOM   2485  O   LEU B 514      -4.117   1.647  -1.043  1.00 72.83           O  
ANISOU 2485  O   LEU B 514     9302   9704   8668    186    797     35       O  
ATOM   2486  CB  LEU B 514      -2.458   1.421   1.497  1.00 76.30           C  
ANISOU 2486  CB  LEU B 514     9821  10146   9023    353    804     19       C  
ATOM   2487  CG  LEU B 514      -2.943   0.135   2.170  1.00 83.31           C  
ANISOU 2487  CG  LEU B 514    10932  10928   9796    306    885    -29       C  
ATOM   2488  CD1 LEU B 514      -1.777  -0.800   2.463  1.00 88.61           C  
ANISOU 2488  CD1 LEU B 514    11758  11559  10351    488    914     34       C  
ATOM   2489  CD2 LEU B 514      -3.705   0.457   3.448  1.00 77.55           C  
ANISOU 2489  CD2 LEU B 514    10183  10203   9080    174    890   -133       C  
ATOM   2490  N   LEU B 515      -3.085  -0.323  -1.383  1.00 36.62           N  
ANISOU 2490  N   LEU B 515     4992   5012   3911    356    888    112       N  
ATOM   2491  CA  LEU B 515      -4.095  -0.806  -2.324  1.00 34.24           C  
ANISOU 2491  CA  LEU B 515     4746   4670   3593    239    924     84       C  
ATOM   2492  C   LEU B 515      -5.382  -1.274  -1.645  1.00 44.96           C  
ANISOU 2492  C   LEU B 515     6216   5957   4908     49    974    -22       C  
ATOM   2493  O   LEU B 515      -5.433  -2.355  -1.058  1.00 46.17           O  
ANISOU 2493  O   LEU B 515     6582   6009   4953     34   1041    -46       O  
ATOM   2494  CB  LEU B 515      -3.530  -1.925  -3.205  1.00 47.66           C  
ANISOU 2494  CB  LEU B 515     6596   6312   5199    345    974    145       C  
ATOM   2495  CG  LEU B 515      -4.471  -2.478  -4.280  1.00 37.62           C  
ANISOU 2495  CG  LEU B 515     5386   5008   3900    229   1012    120       C  
ATOM   2496  CD1 LEU B 515      -4.970  -1.357  -5.176  1.00 30.81           C  
ANISOU 2496  CD1 LEU B 515     4297   4259   3150    170    943    132       C  
ATOM   2497  CD2 LEU B 515      -3.788  -3.559  -5.103  1.00 43.73           C  
ANISOU 2497  CD2 LEU B 515     6314   5725   4577    348   1062    177       C  
ATOM   2498  N   PHE B 516      -6.416  -0.445  -1.740  1.00 44.42           N  
ANISOU 2498  N   PHE B 516     6013   5948   4918    -93    939    -84       N  
ATOM   2499  CA  PHE B 516      -7.752  -0.797  -1.276  1.00 40.12           C  
ANISOU 2499  CA  PHE B 516     5544   5365   4334   -290    980   -187       C  
ATOM   2500  C   PHE B 516      -8.355  -1.855  -2.197  1.00 43.35           C  
ANISOU 2500  C   PHE B 516     6103   5711   4657   -369   1040   -193       C  
ATOM   2501  O   PHE B 516      -8.370  -1.684  -3.414  1.00 45.21           O  
ANISOU 2501  O   PHE B 516     6265   5994   4921   -344   1017   -153       O  
ATOM   2502  CB  PHE B 516      -8.631   0.456  -1.239  1.00 44.65           C  
ANISOU 2502  CB  PHE B 516     5921   6034   5008   -393    917   -251       C  
ATOM   2503  CG  PHE B 516     -10.106   0.181  -1.357  1.00 58.19           C  
ANISOU 2503  CG  PHE B 516     7675   7750   6686   -591    947   -345       C  
ATOM   2504  CD1 PHE B 516     -10.863  -0.127  -0.238  1.00 67.30           C  
ANISOU 2504  CD1 PHE B 516     8902   8875   7793   -729    987   -435       C  
ATOM   2505  CD2 PHE B 516     -10.741   0.261  -2.587  1.00 58.38           C  
ANISOU 2505  CD2 PHE B 516     7650   7818   6713   -642    932   -341       C  
ATOM   2506  CE1 PHE B 516     -12.222  -0.369  -0.348  1.00 61.55           C  
ANISOU 2506  CE1 PHE B 516     8202   8164   7022   -919   1013   -522       C  
ATOM   2507  CE2 PHE B 516     -12.098   0.021  -2.702  1.00 53.72           C  
ANISOU 2507  CE2 PHE B 516     7087   7247   6076   -826    957   -430       C  
ATOM   2508  CZ  PHE B 516     -12.839  -0.294  -1.582  1.00 44.51           C  
ANISOU 2508  CZ  PHE B 516     5995   6053   4863   -968    997   -522       C  
ATOM   2509  N   MET B 517      -8.847  -2.946  -1.617  1.00 40.03           N  
ANISOU 2509  N   MET B 517     5898   5188   4124   -470   1116   -241       N  
ATOM   2510  CA  MET B 517      -9.352  -4.062  -2.412  1.00 44.76           C  
ANISOU 2510  CA  MET B 517     6677   5709   4620   -551   1182   -249       C  
ATOM   2511  C   MET B 517     -10.850  -4.332  -2.247  1.00 53.84           C  
ANISOU 2511  C   MET B 517     7879   6854   5725   -794   1218   -349       C  
ATOM   2512  O   MET B 517     -11.450  -5.012  -3.081  1.00 58.80           O  
ANISOU 2512  O   MET B 517     8602   7453   6285   -892   1258   -367       O  
ATOM   2513  CB  MET B 517      -8.548  -5.332  -2.116  1.00 39.61           C  
ANISOU 2513  CB  MET B 517     6292   4917   3841   -449   1250   -205       C  
ATOM   2514  CG  MET B 517      -7.087  -5.244  -2.520  1.00 36.06           C  
ANISOU 2514  CG  MET B 517     5809   4482   3411   -206   1222   -105       C  
ATOM   2515  SD  MET B 517      -6.213  -6.803  -2.292  1.00 56.32           S  
ANISOU 2515  SD  MET B 517     8711   6882   5805    -71   1302    -61       S  
ATOM   2516  CE  MET B 517      -7.179  -7.889  -3.339  1.00 68.66           C  
ANISOU 2516  CE  MET B 517    10467   8356   7267   -230   1376    -98       C  
ATOM   2517  N   GLY B 518     -11.448  -3.809  -1.178  1.00 57.99           N  
ANISOU 2517  N   GLY B 518     8337   7417   6280   -894   1203   -418       N  
ATOM   2518  CA  GLY B 518     -12.870  -3.995  -0.935  1.00 60.79           C  
ANISOU 2518  CA  GLY B 518     8720   7789   6589  -1125   1234   -517       C  
ATOM   2519  C   GLY B 518     -13.290  -3.773   0.505  1.00 63.43           C  
ANISOU 2519  C   GLY B 518     9052   8132   6918  -1214   1242   -582       C  
ATOM   2520  O   GLY B 518     -12.457  -3.515   1.376  1.00 59.45           O  
ANISOU 2520  O   GLY B 518     8533   7614   6441  -1094   1226   -552       O  
ATOM   2521  N   TYR B 519     -14.593  -3.878   0.748  1.00 72.76           N  
ANISOU 2521  N   TYR B 519    10240   9349   8057  -1427   1266   -674       N  
ATOM   2522  CA  TYR B 519     -15.151  -3.672   2.075  1.00 72.46           C  
ANISOU 2522  CA  TYR B 519    10185   9338   8007  -1535   1278   -746       C  
ATOM   2523  C   TYR B 519     -16.245  -4.696   2.387  1.00 72.75           C  
ANISOU 2523  C   TYR B 519    10409   9326   7907  -1761   1358   -810       C  
ATOM   2524  O   TYR B 519     -16.533  -5.574   1.565  1.00 73.78           O  
ANISOU 2524  O   TYR B 519    10690   9391   7951  -1832   1405   -800       O  
ATOM   2525  CB  TYR B 519     -15.714  -2.262   2.191  1.00 60.09           C  
ANISOU 2525  CB  TYR B 519     8347   7925   6561  -1562   1199   -811       C  
ATOM   2526  CG  TYR B 519     -16.991  -2.038   1.420  1.00 61.05           C  
ANISOU 2526  CG  TYR B 519     8387   8139   6671  -1720   1186   -883       C  
ATOM   2527  CD1 TYR B 519     -18.229  -2.331   1.987  1.00 53.67           C  
ANISOU 2527  CD1 TYR B 519     7485   7245   5662  -1936   1225   -979       C  
ATOM   2528  CD2 TYR B 519     -16.960  -1.513   0.136  1.00 63.91           C  
ANISOU 2528  CD2 TYR B 519     8634   8562   7088  -1649   1131   -854       C  
ATOM   2529  CE1 TYR B 519     -19.390  -2.119   1.298  1.00 55.82           C  
ANISOU 2529  CE1 TYR B 519     7678   7620   5912  -2074   1209  -1049       C  
ATOM   2530  CE2 TYR B 519     -18.116  -1.296  -0.562  1.00 61.06           C  
ANISOU 2530  CE2 TYR B 519     8198   8299   6701  -1779   1114   -919       C  
ATOM   2531  CZ  TYR B 519     -19.330  -1.602   0.027  1.00 60.97           C  
ANISOU 2531  CZ  TYR B 519     8221   8332   6613  -1991   1153  -1019       C  
ATOM   2532  OH  TYR B 519     -20.499  -1.388  -0.656  1.00 61.13           O  
ANISOU 2532  OH  TYR B 519     8164   8469   6594  -2119   1134  -1088       O  
ATOM   2533  N   SER B 520     -16.852  -4.577   3.570  1.00 72.33           N  
ANISOU 2533  N   SER B 520    10345   9309   7830  -1880   1375   -877       N  
ATOM   2534  CA  SER B 520     -17.937  -5.473   3.996  1.00 75.17           C  
ANISOU 2534  CA  SER B 520    10870   9639   8054  -2112   1450   -942       C  
ATOM   2535  C   SER B 520     -18.753  -4.834   5.133  1.00 74.04           C  
ANISOU 2535  C   SER B 520    10590   9610   7931  -2239   1439  -1032       C  
ATOM   2536  O   SER B 520     -18.216  -4.050   5.910  1.00 71.32           O  
ANISOU 2536  O   SER B 520    10114   9312   7671  -2128   1397  -1030       O  
ATOM   2537  CB  SER B 520     -17.361  -6.827   4.433  1.00 70.09           C  
ANISOU 2537  CB  SER B 520    10546   8817   7269  -2090   1529   -889       C  
ATOM   2538  OG  SER B 520     -18.373  -7.815   4.521  1.00 72.35           O  
ANISOU 2538  OG  SER B 520    11025   9054   7409  -2318   1605   -941       O  
ATOM   2539  N   THR B 521     -20.045  -5.159   5.224  1.00 67.96           N  
ANISOU 2539  N   THR B 521     9847   8895   7080  -2472   1478  -1115       N  
ATOM   2540  CA  THR B 521     -20.925  -4.546   6.229  1.00 72.36           C  
ANISOU 2540  CA  THR B 521    10260   9584   7651  -2603   1470  -1209       C  
ATOM   2541  C   THR B 521     -21.737  -5.560   7.047  1.00 79.89           C  
ANISOU 2541  C   THR B 521    11407  10504   8444  -2822   1557  -1255       C  
ATOM   2542  O   THR B 521     -21.608  -5.617   8.272  1.00 88.46           O  
ANISOU 2542  O   THR B 521    12526  11587   9498  -2831   1578  -1267       O  
ATOM   2543  CB  THR B 521     -21.924  -3.530   5.607  1.00 92.83           C  
ANISOU 2543  CB  THR B 521    12603  12351  10319  -2681   1408  -1293       C  
ATOM   2544  OG1 THR B 521     -22.971  -4.235   4.927  1.00 94.99           O  
ANISOU 2544  OG1 THR B 521    12965  12645  10484  -2881   1451  -1336       O  
ATOM   2545  CG2 THR B 521     -21.219  -2.588   4.639  1.00 94.78           C  
ANISOU 2545  CG2 THR B 521    12686  12625  10700  -2479   1320  -1249       C  
ATOM   2546  N   ALA B 522     -22.555  -6.371   6.372  1.00 87.09           N  
ANISOU 2546  N   ALA B 522    12450  11393   9246  -3001   1607  -1281       N  
ATOM   2547  CA  ALA B 522     -23.580  -7.174   7.063  1.00 91.74           C  
ANISOU 2547  CA  ALA B 522    13184  11991   9683  -3252   1683  -1345       C  
ATOM   2548  C   ALA B 522     -23.138  -8.419   7.866  1.00100.60           C  
ANISOU 2548  C   ALA B 522    14630  12939  10656  -3278   1763  -1299       C  
ATOM   2549  O   ALA B 522     -23.932  -9.338   8.098  1.00111.56           O  
ANISOU 2549  O   ALA B 522    16205  14294  11889  -3494   1834  -1338       O  
ATOM   2550  CB  ALA B 522     -24.765  -7.493   6.128  1.00 79.64           C  
ANISOU 2550  CB  ALA B 522    11651  10531   8079  -3464   1705  -1408       C  
ATOM   2551  N   PRO B 523     -21.861  -8.457   8.266  1.00 93.61           N  
ANISOU 2551  N   PRO B 523    13818  11944   9805  -3055   1747  -1218       N  
ATOM   2552  CA  PRO B 523     -21.527  -9.028   9.571  1.00 93.53           C  
ANISOU 2552  CA  PRO B 523    13984  11858   9696  -3054   1788  -1204       C  
ATOM   2553  C   PRO B 523     -20.970  -7.893  10.422  1.00 91.20           C  
ANISOU 2553  C   PRO B 523    13452  11669   9532  -2899   1724  -1208       C  
ATOM   2554  O   PRO B 523     -21.734  -7.245  11.142  1.00 76.51           O  
ANISOU 2554  O   PRO B 523    11413   9959   7699  -3012   1713  -1288       O  
ATOM   2555  CB  PRO B 523     -20.417 -10.025   9.247  1.00 65.30           C  
ANISOU 2555  CB  PRO B 523    10696   8071   6044  -2897   1819  -1107       C  
ATOM   2556  CG  PRO B 523     -19.800  -9.512   7.930  1.00 60.87           C  
ANISOU 2556  CG  PRO B 523    10004   7511   5612  -2730   1765  -1057       C  
ATOM   2557  CD  PRO B 523     -20.685  -8.411   7.382  1.00 65.48           C  
ANISOU 2557  CD  PRO B 523    10276   8285   6318  -2821   1713  -1127       C  
ATOM   2558  N   GLN B 524     -19.659  -7.660  10.327  1.00 93.62           N  
ANISOU 2558  N   GLN B 524    13754  11905   9913  -2648   1684  -1127       N  
ATOM   2559  CA  GLN B 524     -19.000  -6.530  10.982  1.00 83.59           C  
ANISOU 2559  CA  GLN B 524    12251  10733   8776  -2485   1617  -1127       C  
ATOM   2560  C   GLN B 524     -18.689  -5.507   9.905  1.00 70.96           C  
ANISOU 2560  C   GLN B 524    10417   9200   7343  -2361   1543  -1111       C  
ATOM   2561  O   GLN B 524     -18.933  -5.753   8.724  1.00 75.17           O  
ANISOU 2561  O   GLN B 524    10982   9702   7877  -2392   1546  -1095       O  
ATOM   2562  CB  GLN B 524     -17.678  -6.955  11.628  1.00 86.79           C  
ANISOU 2562  CB  GLN B 524    12810  11025   9140  -2281   1617  -1048       C  
ATOM   2563  CG  GLN B 524     -17.747  -8.164  12.544  1.00 89.83           C  
ANISOU 2563  CG  GLN B 524    13495  11298   9338  -2360   1687  -1042       C  
ATOM   2564  CD  GLN B 524     -17.683  -7.796  14.010  1.00 89.48           C  
ANISOU 2564  CD  GLN B 524    13379  11340   9280  -2356   1677  -1083       C  
ATOM   2565  OE1 GLN B 524     -18.530  -7.061  14.517  1.00 92.47           O  
ANISOU 2565  OE1 GLN B 524    13552  11873   9708  -2486   1666  -1168       O  
ATOM   2566  NE2 GLN B 524     -16.680  -8.315  14.705  1.00 88.25           N  
ANISOU 2566  NE2 GLN B 524    13391  11091   9048  -2203   1682  -1026       N  
ATOM   2567  N   LEU B 525     -18.152  -4.359  10.301  1.00 54.97           N  
ANISOU 2567  N   LEU B 525     8162   7272   5454  -2225   1476  -1118       N  
ATOM   2568  CA  LEU B 525     -17.663  -3.408   9.312  1.00 55.31           C  
ANISOU 2568  CA  LEU B 525     8010   7359   5645  -2082   1402  -1091       C  
ATOM   2569  C   LEU B 525     -16.212  -3.765   8.981  1.00 66.17           C  
ANISOU 2569  C   LEU B 525     9501   8616   7025  -1856   1391   -979       C  
ATOM   2570  O   LEU B 525     -15.391  -3.946   9.886  1.00 71.88           O  
ANISOU 2570  O   LEU B 525    10294   9301   7716  -1746   1396   -947       O  
ATOM   2571  CB  LEU B 525     -17.820  -1.957   9.779  1.00 53.41           C  
ANISOU 2571  CB  LEU B 525     7473   7273   5546  -2052   1332  -1161       C  
ATOM   2572  CG  LEU B 525     -19.237  -1.498  10.099  1.00 48.44           C  
ANISOU 2572  CG  LEU B 525     6708   6780   4918  -2254   1336  -1280       C  
ATOM   2573  CD1 LEU B 525     -19.354   0.010  10.119  1.00 36.17           C  
ANISOU 2573  CD1 LEU B 525     4867   5359   3515  -2192   1251  -1349       C  
ATOM   2574  CD2 LEU B 525     -20.225  -2.072   9.115  1.00 59.40           C  
ANISOU 2574  CD2 LEU B 525     8171   8163   6236  -2413   1365  -1299       C  
ATOM   2575  N   ALA B 526     -15.909  -3.897   7.688  1.00 60.70           N  
ANISOU 2575  N   ALA B 526     8828   7875   6360  -1786   1376   -924       N  
ATOM   2576  CA  ALA B 526     -14.600  -4.382   7.247  1.00 57.64           C  
ANISOU 2576  CA  ALA B 526     8568   7376   5957  -1581   1375   -818       C  
ATOM   2577  C   ALA B 526     -13.993  -3.526   6.139  1.00 55.05           C  
ANISOU 2577  C   ALA B 526     8058   7098   5761  -1435   1305   -772       C  
ATOM   2578  O   ALA B 526     -14.689  -3.085   5.225  1.00 47.65           O  
ANISOU 2578  O   ALA B 526     7003   6224   4878  -1511   1279   -803       O  
ATOM   2579  CB  ALA B 526     -14.705  -5.830   6.789  1.00 60.59           C  
ANISOU 2579  CB  ALA B 526     9243   7599   6178  -1637   1452   -783       C  
ATOM   2580  N   ILE B 527     -12.687  -3.306   6.237  1.00 65.27           N  
ANISOU 2580  N   ILE B 527     9334   8371   7095  -1223   1272   -698       N  
ATOM   2581  CA  ILE B 527     -11.916  -2.652   5.189  1.00 63.03           C  
ANISOU 2581  CA  ILE B 527     8914   8121   6915  -1067   1211   -635       C  
ATOM   2582  C   ILE B 527     -10.768  -3.565   4.773  1.00 68.52           C  
ANISOU 2582  C   ILE B 527     9796   8704   7535   -897   1239   -534       C  
ATOM   2583  O   ILE B 527      -9.778  -3.713   5.494  1.00 68.13           O  
ANISOU 2583  O   ILE B 527     9802   8627   7456   -754   1235   -492       O  
ATOM   2584  CB  ILE B 527     -11.374  -1.282   5.644  1.00 62.41           C  
ANISOU 2584  CB  ILE B 527     8590   8154   6970   -965   1132   -646       C  
ATOM   2585  CG1 ILE B 527     -12.451  -0.210   5.473  1.00 70.19           C  
ANISOU 2585  CG1 ILE B 527     9367   9251   8051  -1094   1086   -737       C  
ATOM   2586  CG2 ILE B 527     -10.133  -0.901   4.856  1.00 54.50           C  
ANISOU 2586  CG2 ILE B 527     7519   7156   6032   -760   1083   -551       C  
ATOM   2587  CD1 ILE B 527     -11.958   1.195   5.723  1.00 68.14           C  
ANISOU 2587  CD1 ILE B 527     8881   9084   7923   -996   1003   -755       C  
ATOM   2588  N   VAL B 528     -10.923  -4.193   3.612  1.00 73.08           N  
ANISOU 2588  N   VAL B 528    10472   9223   8073   -912   1266   -503       N  
ATOM   2589  CA  VAL B 528      -9.935  -5.130   3.096  1.00 63.53           C  
ANISOU 2589  CA  VAL B 528     9453   7905   6782   -757   1298   -417       C  
ATOM   2590  C   VAL B 528      -8.960  -4.420   2.167  1.00 55.83           C  
ANISOU 2590  C   VAL B 528     8310   6995   5908   -574   1235   -342       C  
ATOM   2591  O   VAL B 528      -9.368  -3.651   1.298  1.00 52.32           O  
ANISOU 2591  O   VAL B 528     7683   6636   5559   -614   1191   -352       O  
ATOM   2592  CB  VAL B 528     -10.607  -6.271   2.314  1.00 56.81           C  
ANISOU 2592  CB  VAL B 528     8815   6950   5818   -876   1368   -427       C  
ATOM   2593  CG1 VAL B 528      -9.623  -7.406   2.087  1.00 62.12           C  
ANISOU 2593  CG1 VAL B 528     9741   7486   6375   -721   1414   -353       C  
ATOM   2594  CG2 VAL B 528     -11.835  -6.770   3.056  1.00 52.76           C  
ANISOU 2594  CG2 VAL B 528     8420   6406   5221  -1108   1422   -512       C  
ATOM   2595  N   THR B 529      -7.671  -4.675   2.359  1.00 38.98           N  
ANISOU 2595  N   THR B 529     6240   4827   3744   -371   1229   -268       N  
ATOM   2596  CA  THR B 529      -6.643  -4.102   1.501  1.00 38.24           C  
ANISOU 2596  CA  THR B 529     6003   4797   3727   -191   1175   -188       C  
ATOM   2597  C   THR B 529      -5.563  -5.137   1.224  1.00 40.54           C  
ANISOU 2597  C   THR B 529     6497   4997   3910    -10   1212   -112       C  
ATOM   2598  O   THR B 529      -5.607  -6.247   1.754  1.00 40.01           O  
ANISOU 2598  O   THR B 529     6685   4808   3709    -19   1275   -121       O  
ATOM   2599  CB  THR B 529      -5.989  -2.859   2.137  1.00 45.64           C  
ANISOU 2599  CB  THR B 529     6715   5852   4775   -101   1099   -179       C  
ATOM   2600  OG1 THR B 529      -5.130  -3.261   3.211  1.00 49.76           O  
ANISOU 2600  OG1 THR B 529     7344   6341   5223     18   1111   -159       O  
ATOM   2601  CG2 THR B 529      -7.048  -1.902   2.661  1.00 46.12           C  
ANISOU 2601  CG2 THR B 529     6609   5990   4924   -271   1068   -270       C  
ATOM   2602  N   GLN B 530      -4.595  -4.768   0.393  1.00 38.06           N  
ANISOU 2602  N   GLN B 530     6072   4743   3647    157   1171    -35       N  
ATOM   2603  CA  GLN B 530      -3.486  -5.657   0.080  1.00 47.49           C  
ANISOU 2603  CA  GLN B 530     7432   5871   4740    352   1199     38       C  
ATOM   2604  C   GLN B 530      -2.689  -5.969   1.338  1.00 40.03           C  
ANISOU 2604  C   GLN B 530     6595   4896   3718    476   1203     49       C  
ATOM   2605  O   GLN B 530      -2.714  -5.206   2.303  1.00 42.89           O  
ANISOU 2605  O   GLN B 530     6828   5329   4138    447   1164     18       O  
ATOM   2606  CB  GLN B 530      -2.570  -5.025  -0.969  1.00 48.44           C  
ANISOU 2606  CB  GLN B 530     7369   6096   4938    505   1145    117       C  
ATOM   2607  CG  GLN B 530      -2.036  -3.657  -0.572  1.00 49.40           C  
ANISOU 2607  CG  GLN B 530     7226   6360   5183    560   1061    137       C  
ATOM   2608  CD  GLN B 530      -0.878  -3.207  -1.440  1.00 46.97           C  
ANISOU 2608  CD  GLN B 530     6781   6149   4916    738   1013    232       C  
ATOM   2609  OE1 GLN B 530      -0.791  -2.040  -1.823  1.00 50.90           O  
ANISOU 2609  OE1 GLN B 530     7048   6762   5532    725    945    257       O  
ATOM   2610  NE2 GLN B 530       0.019  -4.134  -1.756  1.00 40.98           N  
ANISOU 2610  NE2 GLN B 530     6175   5344   4052    907   1047    287       N  
ATOM   2611  N   TRP B 531      -1.988  -7.096   1.330  1.00 59.53           N  
ANISOU 2611  N   TRP B 531     9305   7264   6051    618   1249     90       N  
ATOM   2612  CA  TRP B 531      -1.089  -7.430   2.426  1.00 73.03           C  
ANISOU 2612  CA  TRP B 531    11120   8954   7673    773   1248    110       C  
ATOM   2613  C   TRP B 531       0.303  -6.876   2.146  1.00 67.07           C  
ANISOU 2613  C   TRP B 531    10209   8319   6957   1003   1189    186       C  
ATOM   2614  O   TRP B 531       0.859  -7.085   1.068  1.00 67.56           O  
ANISOU 2614  O   TRP B 531    10266   8392   7012   1115   1189    242       O  
ATOM   2615  CB  TRP B 531      -1.031  -8.943   2.647  1.00 79.42           C  
ANISOU 2615  CB  TRP B 531    12288   9589   8298    821   1326    114       C  
ATOM   2616  CG  TRP B 531       0.081  -9.353   3.561  1.00 78.67           C  
ANISOU 2616  CG  TRP B 531    12308   9483   8100   1031   1321    150       C  
ATOM   2617  CD1 TRP B 531       1.214 -10.032   3.219  1.00 84.02           C  
ANISOU 2617  CD1 TRP B 531    13118  10130   8678   1268   1331    215       C  
ATOM   2618  CD2 TRP B 531       0.179  -9.090   4.965  1.00 79.62           C  
ANISOU 2618  CD2 TRP B 531    12413   9637   8203   1031   1301    121       C  
ATOM   2619  NE1 TRP B 531       2.006 -10.217   4.325  1.00 90.10           N  
ANISOU 2619  NE1 TRP B 531    13957  10912   9364   1418   1318    228       N  
ATOM   2620  CE2 TRP B 531       1.395  -9.646   5.410  1.00 87.40           C  
ANISOU 2620  CE2 TRP B 531    13526  10611   9072   1274   1300    171       C  
ATOM   2621  CE3 TRP B 531      -0.644  -8.440   5.890  1.00 89.96           C  
ANISOU 2621  CE3 TRP B 531    13610  10995   9577    852   1286     52       C  
ATOM   2622  CZ2 TRP B 531       1.806  -9.575   6.739  1.00100.63           C  
ANISOU 2622  CZ2 TRP B 531    15218  12324  10695   1341   1282    157       C  
ATOM   2623  CZ3 TRP B 531      -0.234  -8.370   7.208  1.00 99.45           C  
ANISOU 2623  CZ3 TRP B 531    14827  12231  10729    915   1269     37       C  
ATOM   2624  CH2 TRP B 531       0.980  -8.934   7.621  1.00103.68           C  
ANISOU 2624  CH2 TRP B 531    15489  12756  11149   1155   1267     89       C  
ATOM   2625  N   CYS B 532       0.864  -6.167   3.120  1.00 64.97           N  
ANISOU 2625  N   CYS B 532     9812   8150   6726   1066   1138    183       N  
ATOM   2626  CA  CYS B 532       2.160  -5.522   2.940  1.00 66.96           C  
ANISOU 2626  CA  CYS B 532     9891   8537   7013   1262   1076    249       C  
ATOM   2627  C   CYS B 532       3.298  -6.230   3.665  1.00 73.22           C  
ANISOU 2627  C   CYS B 532    10837   9316   7669   1481   1085    284       C  
ATOM   2628  O   CYS B 532       3.232  -6.466   4.872  1.00 80.92           O  
ANISOU 2628  O   CYS B 532    11904  10261   8579   1473   1095    245       O  
ATOM   2629  CB  CYS B 532       2.100  -4.059   3.383  1.00 67.66           C  
ANISOU 2629  CB  CYS B 532     9690   8773   7244   1184   1002    225       C  
ATOM   2630  SG  CYS B 532       1.760  -2.902   2.045  1.00 76.68           S  
ANISOU 2630  SG  CYS B 532    10567  10014   8552   1093    950    252       S  
ATOM   2631  N   GLU B 533       4.344  -6.557   2.913  1.00 61.56           N  
ANISOU 2631  N   GLU B 533     9377   7871   6140   1683   1079    356       N  
ATOM   2632  CA  GLU B 533       5.558  -7.122   3.484  1.00 73.33           C  
ANISOU 2632  CA  GLU B 533    10979   9380   7502   1922   1077    395       C  
ATOM   2633  C   GLU B 533       6.376  -6.019   4.145  1.00 75.19           C  
ANISOU 2633  C   GLU B 533    10968   9801   7800   1993    998    406       C  
ATOM   2634  O   GLU B 533       6.096  -4.835   3.960  1.00 76.21           O  
ANISOU 2634  O   GLU B 533    10848  10037   8072   1872    945    395       O  
ATOM   2635  CB  GLU B 533       6.390  -7.807   2.398  1.00 99.20           C  
ANISOU 2635  CB  GLU B 533    14345  12646  10703   2114   1097    464       C  
ATOM   2636  CG  GLU B 533       5.704  -8.990   1.732  1.00112.40           C  
ANISOU 2636  CG  GLU B 533    16286  14132  12288   2062   1177    451       C  
ATOM   2637  CD  GLU B 533       5.458 -10.137   2.692  1.00120.08           C  
ANISOU 2637  CD  GLU B 533    17581  14940  13105   2076   1238    418       C  
ATOM   2638  OE1 GLU B 533       4.331 -10.244   3.214  1.00117.25           O  
ANISOU 2638  OE1 GLU B 533    17303  14488  12759   1866   1269    358       O  
ATOM   2639  OE2 GLU B 533       6.393 -10.931   2.926  1.00126.59           O  
ANISOU 2639  OE2 GLU B 533    18580  15732  13786   2298   1256    454       O  
ATOM   2640  N   GLY B 534       7.384  -6.410   4.918  1.00 85.26           N  
ANISOU 2640  N   GLY B 534    12320  11115   8960   2188    989    425       N  
ATOM   2641  CA  GLY B 534       8.269  -5.453   5.560  1.00 83.41           C  
ANISOU 2641  CA  GLY B 534    11866  11066   8760   2268    915    434       C  
ATOM   2642  C   GLY B 534       7.612  -4.662   6.675  1.00 83.42           C  
ANISOU 2642  C   GLY B 534    11754  11106   8837   2094    888    356       C  
ATOM   2643  O   GLY B 534       6.467  -4.921   7.047  1.00 76.59           O  
ANISOU 2643  O   GLY B 534    10991  10122   7987   1920    930    297       O  
ATOM   2644  N   SER B 535       8.344  -3.690   7.211  1.00 95.04           N  
ANISOU 2644  N   SER B 535    13013  12750  10348   2137    818    353       N  
ATOM   2645  CA  SER B 535       7.843  -2.863   8.302  1.00 90.33           C  
ANISOU 2645  CA  SER B 535    12291  12209   9820   1987    788    270       C  
ATOM   2646  C   SER B 535       7.670  -1.414   7.858  1.00 80.01           C  
ANISOU 2646  C   SER B 535    10706  11020   8676   1849    724    257       C  
ATOM   2647  O   SER B 535       8.070  -1.045   6.754  1.00 76.39           O  
ANISOU 2647  O   SER B 535    10148  10615   8262   1883    697    325       O  
ATOM   2648  CB  SER B 535       8.786  -2.937   9.507  1.00 86.71           C  
ANISOU 2648  CB  SER B 535    11837  11850   9259   2136    763    252       C  
ATOM   2649  OG  SER B 535       8.857  -4.255  10.023  1.00 88.64           O  
ANISOU 2649  OG  SER B 535    12358  11975   9348   2252    823    259       O  
ATOM   2650  N   SER B 536       7.073  -0.597   8.722  1.00 70.21           N  
ANISOU 2650  N   SER B 536     9346   9816   7514   1692    700    168       N  
ATOM   2651  CA  SER B 536       6.855   0.813   8.415  1.00 64.93           C  
ANISOU 2651  CA  SER B 536     8436   9241   6994   1550    642    140       C  
ATOM   2652  C   SER B 536       8.174   1.573   8.394  1.00 63.77           C  
ANISOU 2652  C   SER B 536     8132   9264   6833   1662    574    175       C  
ATOM   2653  O   SER B 536       9.206   1.060   8.829  1.00 60.87           O  
ANISOU 2653  O   SER B 536     7820   8962   6344   1845    568    206       O  
ATOM   2654  CB  SER B 536       5.908   1.454   9.433  1.00 46.69           C  
ANISOU 2654  CB  SER B 536     6052   6924   4764   1366    638     19       C  
ATOM   2655  OG  SER B 536       6.572   1.706  10.660  1.00 54.13           O  
ANISOU 2655  OG  SER B 536     6943   7966   5659   1429    609    -37       O  
ATOM   2656  N   LEU B 537       8.133   2.799   7.887  1.00 53.85           N  
ANISOU 2656  N   LEU B 537     6692   8076   5693   1544    528    167       N  
ATOM   2657  CA  LEU B 537       9.316   3.645   7.841  1.00 51.37           C  
ANISOU 2657  CA  LEU B 537     6234   7917   5367   1603    473    187       C  
ATOM   2658  C   LEU B 537       9.740   4.006   9.257  1.00 53.84           C  
ANISOU 2658  C   LEU B 537     6486   8316   5655   1618    448     89       C  
ATOM   2659  O   LEU B 537      10.904   4.311   9.514  1.00 61.60           O  
ANISOU 2659  O   LEU B 537     7398   9434   6573   1721    415     99       O  
ATOM   2660  CB  LEU B 537       9.033   4.911   7.034  1.00 52.61           C  
ANISOU 2660  CB  LEU B 537     6242   8086   5663   1443    448    184       C  
ATOM   2661  CG  LEU B 537      10.250   5.764   6.686  1.00 46.14           C  
ANISOU 2661  CG  LEU B 537     5297   7399   4834   1482    415    219       C  
ATOM   2662  CD1 LEU B 537      11.263   4.936   5.918  1.00 42.86           C  
ANISOU 2662  CD1 LEU B 537     4955   7058   4272   1673    419    347       C  
ATOM   2663  CD2 LEU B 537       9.832   6.983   5.883  1.00 43.36           C  
ANISOU 2663  CD2 LEU B 537     4828   7008   4640   1314    412    215       C  
ATOM   2664  N   TYR B 538       8.777   3.968  10.172  1.00 61.42           N  
ANISOU 2664  N   TYR B 538     7471   9204   6660   1509    468    -10       N  
ATOM   2665  CA  TYR B 538       9.034   4.226  11.581  1.00 60.86           C  
ANISOU 2665  CA  TYR B 538     7350   9207   6566   1516    450   -113       C  
ATOM   2666  C   TYR B 538       9.964   3.160  12.141  1.00 59.60           C  
ANISOU 2666  C   TYR B 538     7315   9098   6232   1735    462    -65       C  
ATOM   2667  O   TYR B 538      10.994   3.468  12.739  1.00 65.43           O  
ANISOU 2667  O   TYR B 538     7973   9977   6911   1833    425    -86       O  
ATOM   2668  CB  TYR B 538       7.717   4.230  12.359  1.00 55.73           C  
ANISOU 2668  CB  TYR B 538     6725   8465   5983   1357    479   -219       C  
ATOM   2669  CG  TYR B 538       7.835   4.769  13.764  1.00 63.32           C  
ANISOU 2669  CG  TYR B 538     7593   9511   6956   1322    454   -345       C  
ATOM   2670  CD1 TYR B 538       7.747   6.132  14.011  1.00 65.31           C  
ANISOU 2670  CD1 TYR B 538     7658   9814   7344   1192    412   -449       C  
ATOM   2671  CD2 TYR B 538       8.029   3.917  14.843  1.00 72.39           C  
ANISOU 2671  CD2 TYR B 538     8851  10676   7978   1420    478   -366       C  
ATOM   2672  CE1 TYR B 538       7.853   6.632  15.293  1.00 75.36           C  
ANISOU 2672  CE1 TYR B 538     8839  11162   8631   1160    389   -577       C  
ATOM   2673  CE2 TYR B 538       8.136   4.408  16.130  1.00 74.51           C  
ANISOU 2673  CE2 TYR B 538     9024  11034   8251   1389    454   -485       C  
ATOM   2674  CZ  TYR B 538       8.047   5.768  16.349  1.00 74.26           C  
ANISOU 2674  CZ  TYR B 538     8791  11062   8361   1258    409   -593       C  
ATOM   2675  OH  TYR B 538       8.152   6.268  17.626  1.00 73.96           O  
ANISOU 2675  OH  TYR B 538     8654  11113   8333   1226    386   -723       O  
ATOM   2676  N   HIS B 539       9.591   1.902  11.935  1.00 61.26           N  
ANISOU 2676  N   HIS B 539     7733   9185   6358   1811    519     -7       N  
ATOM   2677  CA  HIS B 539      10.384   0.770  12.396  1.00 67.43           C  
ANISOU 2677  CA  HIS B 539     8677   9974   6969   2029    543     40       C  
ATOM   2678  C   HIS B 539      11.799   0.809  11.824  1.00 59.41           C  
ANISOU 2678  C   HIS B 539     7604   9095   5875   2221    504    127       C  
ATOM   2679  O   HIS B 539      12.776   0.635  12.550  1.00 57.96           O  
ANISOU 2679  O   HIS B 539     7413   9029   5581   2376    483    123       O  
ATOM   2680  CB  HIS B 539       9.700  -0.542  12.004  1.00 80.66           C  
ANISOU 2680  CB  HIS B 539    10608  11460   8580   2057    620     88       C  
ATOM   2681  CG  HIS B 539      10.414  -1.768  12.484  1.00 82.48           C  
ANISOU 2681  CG  HIS B 539    11046  11662   8630   2276    655    130       C  
ATOM   2682  ND1 HIS B 539      11.669  -2.122  12.035  1.00 78.17           N  
ANISOU 2682  ND1 HIS B 539    10515  11202   7985   2505    637    212       N  
ATOM   2683  CD2 HIS B 539      10.041  -2.730  13.358  1.00 86.18           C  
ANISOU 2683  CD2 HIS B 539    11728  12027   8991   2302    708    102       C  
ATOM   2684  CE1 HIS B 539      12.041  -3.245  12.621  1.00 88.16           C  
ANISOU 2684  CE1 HIS B 539    11993  12411   9093   2673    678    229       C  
ATOM   2685  NE2 HIS B 539      11.073  -3.637  13.428  1.00 91.58           N  
ANISOU 2685  NE2 HIS B 539    12556  12725   9516   2551    721    166       N  
ATOM   2686  N   HIS B 540      11.900   1.038  10.518  1.00 60.47           N  
ANISOU 2686  N   HIS B 540     7694   9224   6056   2209    494    205       N  
ATOM   2687  CA  HIS B 540      13.190   1.015   9.835  1.00 67.56           C  
ANISOU 2687  CA  HIS B 540     8548  10253   6867   2382    462    296       C  
ATOM   2688  C   HIS B 540      14.099   2.175  10.233  1.00 78.19           C  
ANISOU 2688  C   HIS B 540     9688  11800   8219   2358    399    255       C  
ATOM   2689  O   HIS B 540      15.323   2.043  10.227  1.00 85.29           O  
ANISOU 2689  O   HIS B 540    10562  12846   8999   2528    375    301       O  
ATOM   2690  CB  HIS B 540      12.995   0.996   8.317  1.00 66.44           C  
ANISOU 2690  CB  HIS B 540     8410  10060   6774   2353    471    387       C  
ATOM   2691  CG  HIS B 540      12.506  -0.315   7.787  1.00 68.90           C  
ANISOU 2691  CG  HIS B 540     8940  10199   7041   2440    538    436       C  
ATOM   2692  ND1 HIS B 540      13.349  -1.376   7.534  1.00 70.52           N  
ANISOU 2692  ND1 HIS B 540     9285  10404   7107   2681    563    504       N  
ATOM   2693  CD2 HIS B 540      11.262  -0.737   7.455  1.00 73.41           C  
ANISOU 2693  CD2 HIS B 540     9621  10589   7681   2312    593    414       C  
ATOM   2694  CE1 HIS B 540      12.646  -2.395   7.073  1.00 77.83           C  
ANISOU 2694  CE1 HIS B 540    10411  11141   8019   2691    634    516       C  
ATOM   2695  NE2 HIS B 540      11.376  -2.033   7.015  1.00 74.78           N  
ANISOU 2695  NE2 HIS B 540    10011  10649   7755   2462    652    464       N  
ATOM   2696  N   LEU B 541      13.499   3.309  10.576  1.00 90.06           N  
ANISOU 2696  N   LEU B 541    11052  13305   9863   2146    380    159       N  
ATOM   2697  CA  LEU B 541      14.267   4.488  10.955  1.00 84.94           C  
ANISOU 2697  CA  LEU B 541    10216  12809   9248   2093    338     95       C  
ATOM   2698  C   LEU B 541      14.590   4.512  12.444  1.00 83.47           C  
ANISOU 2698  C   LEU B 541     9996  12706   9011   2141    320     -6       C  
ATOM   2699  O   LEU B 541      15.677   4.930  12.845  1.00 80.19           O  
ANISOU 2699  O   LEU B 541     9479  12454   8535   2217    290    -29       O  
ATOM   2700  CB  LEU B 541      13.515   5.763  10.569  1.00 58.01           C  
ANISOU 2700  CB  LEU B 541     6674   9335   6033   1852    333     31       C  
ATOM   2701  CG  LEU B 541      13.901   6.409   9.239  1.00 62.04           C  
ANISOU 2701  CG  LEU B 541     7111   9864   6598   1804    335    109       C  
ATOM   2702  CD1 LEU B 541      14.074   5.361   8.149  1.00 69.82           C  
ANISOU 2702  CD1 LEU B 541     8227  10831   7470   1936    356    251       C  
ATOM   2703  CD2 LEU B 541      12.873   7.454   8.835  1.00 57.06           C  
ANISOU 2703  CD2 LEU B 541     6397   9111   6171   1579    342     56       C  
ATOM   2704  N   HIS B 542      13.647   4.054  13.260  1.00 69.67           N  
ANISOU 2704  N   HIS B 542     8334  10854   7284   2092    344    -68       N  
ATOM   2705  CA  HIS B 542      13.759   4.210  14.707  1.00 77.21           C  
ANISOU 2705  CA  HIS B 542     9241  11882   8213   2097    331   -179       C  
ATOM   2706  C   HIS B 542      14.004   2.901  15.459  1.00 86.39           C  
ANISOU 2706  C   HIS B 542    10579  13035   9209   2288    361   -147       C  
ATOM   2707  O   HIS B 542      14.957   2.791  16.229  1.00 82.55           O  
ANISOU 2707  O   HIS B 542    10060  12692   8612   2429    339   -165       O  
ATOM   2708  CB  HIS B 542      12.516   4.915  15.259  1.00 74.63           C  
ANISOU 2708  CB  HIS B 542     8849  11465   8041   1869    336   -304       C  
ATOM   2709  CG  HIS B 542      12.175   6.186  14.534  1.00 71.70           C  
ANISOU 2709  CG  HIS B 542     8331  11066   7845   1686    316   -342       C  
ATOM   2710  ND1 HIS B 542      13.130   7.064  14.089  1.00 64.90           N  
ANISOU 2710  ND1 HIS B 542     7338  10306   7016   1690    286   -335       N  
ATOM   2711  CD2 HIS B 542      10.975   6.717  14.194  1.00 62.79           C  
ANISOU 2711  CD2 HIS B 542     7178   9811   6869   1495    330   -388       C  
ATOM   2712  CE1 HIS B 542      12.538   8.092  13.494  1.00 54.47           C  
ANISOU 2712  CE1 HIS B 542     5927   8900   5870   1513    286   -372       C  
ATOM   2713  NE2 HIS B 542      11.236   7.903  13.546  1.00 57.47           N  
ANISOU 2713  NE2 HIS B 542     6367   9147   6320   1399    308   -405       N  
ATOM   2714  N   ALA B 543      13.140   1.915  15.239  1.00104.06           N  
ANISOU 2714  N   ALA B 543    13012  15099  11429   2288    418   -103       N  
ATOM   2715  CA  ALA B 543      13.221   0.654  15.970  1.00 90.66           C  
ANISOU 2715  CA  ALA B 543    11521  13346   9580   2442    464    -82       C  
ATOM   2716  C   ALA B 543      14.074  -0.372  15.236  1.00 91.68           C  
ANISOU 2716  C   ALA B 543    11800  13461   9572   2680    484     43       C  
ATOM   2717  O   ALA B 543      13.845  -1.578  15.349  1.00101.74           O  
ANISOU 2717  O   ALA B 543    13312  14602  10743   2781    544     82       O  
ATOM   2718  CB  ALA B 543      11.829   0.101  16.228  1.00 47.45           C  
ANISOU 2718  CB  ALA B 543     6205   7680   4143   2299    525   -117       C  
ATOM   2719  N   SER B 544      15.058   0.109  14.486  1.00 66.21           N  
ANISOU 2719  N   SER B 544     8446  10372   6339   2764    438    100       N  
ATOM   2720  CA  SER B 544      15.916  -0.780  13.717  1.00 75.31           C  
ANISOU 2720  CA  SER B 544     9716  11533   7367   2996    452    215       C  
ATOM   2721  C   SER B 544      17.378  -0.351  13.749  1.00 87.02           C  
ANISOU 2721  C   SER B 544    11050  13257   8757   3153    393    242       C  
ATOM   2722  O   SER B 544      17.698   0.818  13.973  1.00 82.54           O  
ANISOU 2722  O   SER B 544    10273  12839   8251   3038    341    182       O  
ATOM   2723  CB  SER B 544      15.428  -0.885  12.271  1.00 84.42           C  
ANISOU 2723  CB  SER B 544    10910  12568   8598   2933    473    290       C  
ATOM   2724  OG  SER B 544      16.241  -1.770  11.522  1.00 85.08           O  
ANISOU 2724  OG  SER B 544    11107  12656   8563   3163    490    391       O  
ATOM   2725  N   GLU B 545      18.256  -1.321  13.524  1.00125.06           N  
ANISOU 2725  N   GLU B 545    15990  18106  13422   3413    410    323       N  
ATOM   2726  CA  GLU B 545      19.692  -1.095  13.492  1.00146.54           C  
ANISOU 2726  CA  GLU B 545    18590  21064  16023   3591    359    360       C  
ATOM   2727  C   GLU B 545      20.177  -1.117  12.046  1.00146.25           C  
ANISOU 2727  C   GLU B 545    18535  21061  15973   3652    348    465       C  
ATOM   2728  O   GLU B 545      21.366  -0.954  11.771  1.00150.05           O  
ANISOU 2728  O   GLU B 545    18926  21735  16351   3771    339    488       O  
ATOM   2729  CB  GLU B 545      20.412  -2.161  14.326  1.00173.35           C  
ANISOU 2729  CB  GLU B 545    22127  24498  19239   3864    385    373       C  
ATOM   2730  CG  GLU B 545      20.137  -2.072  15.826  1.00183.23           C  
ANISOU 2730  CG  GLU B 545    23376  25771  20473   3818    388    273       C  
ATOM   2731  CD  GLU B 545      20.811  -3.177  16.627  1.00197.81           C  
ANISOU 2731  CD  GLU B 545    25387  27646  22127   4088    421    292       C  
ATOM   2732  OE1 GLU B 545      21.352  -4.123  16.017  1.00205.71           O  
ANISOU 2732  OE1 GLU B 545    26538  28606  23015   4310    453    378       O  
ATOM   2733  OE2 GLU B 545      20.795  -3.098  17.874  1.00201.43           O  
ANISOU 2733  OE2 GLU B 545    25826  28167  22541   4079    417    217       O  
ATOM   2734  N   THR B 546      19.240  -1.330  11.127  1.00153.86           N  
ANISOU 2734  N   THR B 546    19585  21836  17041   3541    385    500       N  
ATOM   2735  CA  THR B 546      19.524  -1.267   9.699  1.00145.45           C  
ANISOU 2735  CA  THR B 546    18492  20783  15989   3533    410    564       C  
ATOM   2736  C   THR B 546      19.334   0.160   9.202  1.00136.62           C  
ANISOU 2736  C   THR B 546    17167  19751  14993   3282    369    542       C  
ATOM   2737  O   THR B 546      18.215   0.673   9.153  1.00131.13           O  
ANISOU 2737  O   THR B 546    16452  18937  14435   3077    350    519       O  
ATOM   2738  CB  THR B 546      18.615  -2.214   8.893  1.00 95.93           C  
ANISOU 2738  CB  THR B 546    12416  14269   9764   3541    471    610       C  
ATOM   2739  OG1 THR B 546      18.937  -3.573   9.214  1.00 92.79           O  
ANISOU 2739  OG1 THR B 546    12242  13784   9230   3793    519    635       O  
ATOM   2740  CG2 THR B 546      18.802  -1.993   7.398  1.00 89.46           C  
ANISOU 2740  CG2 THR B 546    11536  13474   8980   3488    501    659       C  
ATOM   2741  N   LYS B 547      20.440   0.800   8.840  1.00123.23           N  
ANISOU 2741  N   LYS B 547    15325  18259  13236   3305    358    551       N  
ATOM   2742  CA  LYS B 547      20.412   2.192   8.420  1.00110.37           C  
ANISOU 2742  CA  LYS B 547    13518  16716  11700   3083    324    532       C  
ATOM   2743  C   LYS B 547      20.538   2.315   6.905  1.00109.37           C  
ANISOU 2743  C   LYS B 547    13366  16580  11607   3041    366    607       C  
ATOM   2744  O   LYS B 547      21.383   1.669   6.284  1.00116.70           O  
ANISOU 2744  O   LYS B 547    14325  17583  12433   3215    405    660       O  
ATOM   2745  CB  LYS B 547      21.519   2.978   9.127  1.00 81.77           C  
ANISOU 2745  CB  LYS B 547     9745  13331   7993   3108    279    484       C  
ATOM   2746  CG  LYS B 547      21.371   3.025  10.643  1.00 85.92           C  
ANISOU 2746  CG  LYS B 547    10251  13867   8529   3114    255    378       C  
ATOM   2747  CD  LYS B 547      22.551   3.732  11.292  1.00 90.52           C  
ANISOU 2747  CD  LYS B 547    10665  14681   9046   3152    233    313       C  
ATOM   2748  CE  LYS B 547      22.445   3.722  12.810  1.00 91.38           C  
ANISOU 2748  CE  LYS B 547    10753  14819   9148   3172    208    208       C  
ATOM   2749  NZ  LYS B 547      23.631   4.353  13.454  1.00 93.92           N  
ANISOU 2749  NZ  LYS B 547    10907  15379   9400   3222    184    144       N  
ATOM   2750  N   PHE B 548      19.683   3.143   6.315  1.00 82.40           N  
ANISOU 2750  N   PHE B 548     9897  13079   8333   2814    356    611       N  
ATOM   2751  CA  PHE B 548      19.680   3.332   4.871  1.00 71.41           C  
ANISOU 2751  CA  PHE B 548     8475  11672   6987   2754    395    685       C  
ATOM   2752  C   PHE B 548      20.760   4.309   4.436  1.00 75.29           C  
ANISOU 2752  C   PHE B 548     8809  12362   7435   2723    385    711       C  
ATOM   2753  O   PHE B 548      21.244   5.114   5.231  1.00 73.98           O  
ANISOU 2753  O   PHE B 548     8513  12287   7307   2674    364    634       O  
ATOM   2754  CB  PHE B 548      18.316   3.835   4.396  1.00 73.49           C  
ANISOU 2754  CB  PHE B 548     8745  11764   7413   2532    390    687       C  
ATOM   2755  CG  PHE B 548      17.211   2.838   4.567  1.00 76.08           C  
ANISOU 2755  CG  PHE B 548     9227  11892   7787   2554    410    676       C  
ATOM   2756  CD1 PHE B 548      16.175   3.075   5.454  1.00 81.68           C  
ANISOU 2756  CD1 PHE B 548     9956  12491   8586   2431    381    606       C  
ATOM   2757  CD2 PHE B 548      17.212   1.658   3.844  1.00 78.99           C  
ANISOU 2757  CD2 PHE B 548     9721  12180   8112   2697    466    725       C  
ATOM   2758  CE1 PHE B 548      15.156   2.155   5.612  1.00 87.77           C  
ANISOU 2758  CE1 PHE B 548    10874  13081   9395   2449    403    602       C  
ATOM   2759  CE2 PHE B 548      16.198   0.735   3.997  1.00 85.29           C  
ANISOU 2759  CE2 PHE B 548    10677  12782   8946   2716    490    715       C  
ATOM   2760  CZ  PHE B 548      15.168   0.983   4.883  1.00 90.04           C  
ANISOU 2760  CZ  PHE B 548    11300  13280   9631   2593    455    661       C  
ATOM   2761  N   GLU B 549      21.137   4.229   3.166  1.00 86.63           N  
ANISOU 2761  N   GLU B 549    10219  13834   8862   2746    426    791       N  
ATOM   2762  CA  GLU B 549      22.052   5.197   2.587  1.00 78.46           C  
ANISOU 2762  CA  GLU B 549     9029  12964   7818   2693    427    828       C  
ATOM   2763  C   GLU B 549      21.236   6.278   1.901  1.00 69.93           C  
ANISOU 2763  C   GLU B 549     7849  11750   6972   2448    437    831       C  
ATOM   2764  O   GLU B 549      20.022   6.141   1.748  1.00 69.05           O  
ANISOU 2764  O   GLU B 549     7819  11461   6956   2343    440    827       O  
ATOM   2765  CB  GLU B 549      23.006   4.520   1.604  1.00 74.89           C  
ANISOU 2765  CB  GLU B 549     8577  12634   7242   2868    469    906       C  
ATOM   2766  CG  GLU B 549      23.779   3.365   2.218  1.00 82.20           C  
ANISOU 2766  CG  GLU B 549     9582  13639   8013   3133    479    881       C  
ATOM   2767  CD  GLU B 549      25.109   3.119   1.537  1.00 97.69           C  
ANISOU 2767  CD  GLU B 549    11475  15807   9835   3302    505    935       C  
ATOM   2768  OE1 GLU B 549      25.266   3.531   0.369  1.00111.24           O  
ANISOU 2768  OE1 GLU B 549    13117  17566  11583   3230    527   1003       O  
ATOM   2769  OE2 GLU B 549      25.997   2.513   2.173  1.00 96.25           O  
ANISOU 2769  OE2 GLU B 549    11312  15752   9507   3513    502    912       O  
ATOM   2770  N   MET B 550      21.899   7.353   1.494  1.00 70.17           N  
ANISOU 2770  N   MET B 550     7703  11861   7098   2363    437    845       N  
ATOM   2771  CA  MET B 550      21.204   8.486   0.897  1.00 69.48           C  
ANISOU 2771  CA  MET B 550     7515  11638   7245   2143    438    855       C  
ATOM   2772  C   MET B 550      20.333   8.108  -0.295  1.00 70.56           C  
ANISOU 2772  C   MET B 550     7741  11661   7406   2089    469    942       C  
ATOM   2773  O   MET B 550      19.171   8.507  -0.367  1.00 73.77           O  
ANISOU 2773  O   MET B 550     8165  11893   7973   1936    467    919       O  
ATOM   2774  CB  MET B 550      22.196   9.581   0.506  1.00 64.80           C  
ANISOU 2774  CB  MET B 550     6730  11157   6732   2092    429    885       C  
ATOM   2775  CG  MET B 550      22.254  10.701   1.517  1.00 65.59           C  
ANISOU 2775  CG  MET B 550     6701  11224   6996   1979    391    779       C  
ATOM   2776  SD  MET B 550      20.610  11.391   1.767  1.00 67.79           S  
ANISOU 2776  SD  MET B 550     7008  11227   7524   1763    383    710       S  
ATOM   2777  CE  MET B 550      20.818  12.214   3.341  1.00 50.61           C  
ANISOU 2777  CE  MET B 550     4725   9055   5447   1711    341    551       C  
ATOM   2778  N   LYS B 551      20.889   7.338  -1.224  1.00 68.24           N  
ANISOU 2778  N   LYS B 551     7500  11475   6951   2221    499   1038       N  
ATOM   2779  CA  LYS B 551      20.171   6.998  -2.447  1.00 65.12           C  
ANISOU 2779  CA  LYS B 551     7174  10997   6572   2177    529   1125       C  
ATOM   2780  C   LYS B 551      18.765   6.481  -2.150  1.00 55.65           C  
ANISOU 2780  C   LYS B 551     6113   9606   5424   2115    522   1087       C  
ATOM   2781  O   LYS B 551      17.815   6.801  -2.862  1.00 59.60           O  
ANISOU 2781  O   LYS B 551     6614   9981   6051   1979    530   1119       O  
ATOM   2782  CB  LYS B 551      20.942   5.970  -3.278  1.00 68.48           C  
ANISOU 2782  CB  LYS B 551     7650  11550   6819   2366    564   1195       C  
ATOM   2783  CG  LYS B 551      20.619   6.047  -4.763  1.00 78.45           C  
ANISOU 2783  CG  LYS B 551     8880  12779   8147   2300    596   1286       C  
ATOM   2784  CD  LYS B 551      20.745   4.701  -5.458  1.00 76.67           C  
ANISOU 2784  CD  LYS B 551     8732  12551   7846   2474    634   1290       C  
ATOM   2785  CE  LYS B 551      20.332   4.810  -6.920  1.00 65.34           C  
ANISOU 2785  CE  LYS B 551     7258  11086   6483   2396    660   1371       C  
ATOM   2786  NZ  LYS B 551      20.228   3.480  -7.583  1.00 59.27           N  
ANISOU 2786  NZ  LYS B 551     6583  10282   5654   2550    695   1363       N  
ATOM   2787  N   LYS B 552      18.638   5.687  -1.093  1.00 43.34           N  
ANISOU 2787  N   LYS B 552     4660   8021   3787   2219    505   1015       N  
ATOM   2788  CA  LYS B 552      17.349   5.110  -0.728  1.00 52.71           C  
ANISOU 2788  CA  LYS B 552     5958   9017   5052   2174    500    964       C  
ATOM   2789  C   LYS B 552      16.492   6.101   0.054  1.00 64.66           C  
ANISOU 2789  C   LYS B 552     7420  10429   6721   1984    470    886       C  
ATOM   2790  O   LYS B 552      15.277   6.162  -0.131  1.00 67.58           O  
ANISOU 2790  O   LYS B 552     7827  10646   7205   1862    470    872       O  
ATOM   2791  CB  LYS B 552      17.545   3.822   0.075  1.00 60.21           C  
ANISOU 2791  CB  LYS B 552     7030   9945   5902   2368    509    910       C  
ATOM   2792  CG  LYS B 552      16.273   3.020   0.276  1.00 59.98           C  
ANISOU 2792  CG  LYS B 552     7135   9715   5940   2347    518    875       C  
ATOM   2793  CD  LYS B 552      16.594   1.575   0.605  1.00 59.93           C  
ANISOU 2793  CD  LYS B 552     7279   9672   5821   2574    550    862       C  
ATOM   2794  CE  LYS B 552      15.361   0.700   0.495  1.00 71.78           C  
ANISOU 2794  CE  LYS B 552     8929  10962   7384   2557    575    847       C  
ATOM   2795  NZ  LYS B 552      15.695  -0.746   0.629  1.00 81.74           N  
ANISOU 2795  NZ  LYS B 552    10371  12159   8526   2787    619    848       N  
ATOM   2796  N   LEU B 553      17.133   6.872   0.927  1.00 71.67           N  
ANISOU 2796  N   LEU B 553     8195  11388   7650   1962    452    813       N  
ATOM   2797  CA  LEU B 553      16.446   7.900   1.702  1.00 52.84           C  
ANISOU 2797  CA  LEU B 553     5724   8896   5459   1789    433    708       C  
ATOM   2798  C   LEU B 553      15.773   8.909   0.781  1.00 55.12           C  
ANISOU 2798  C   LEU B 553     5928   9072   5942   1609    444    741       C  
ATOM   2799  O   LEU B 553      14.613   9.269   0.979  1.00 61.59           O  
ANISOU 2799  O   LEU B 553     6759   9742   6900   1476    439    687       O  
ATOM   2800  CB  LEU B 553      17.428   8.613   2.631  1.00 37.32           C  
ANISOU 2800  CB  LEU B 553     3632   7041   3506   1809    409    633       C  
ATOM   2801  CG  LEU B 553      18.045   7.744   3.728  1.00 46.60           C  
ANISOU 2801  CG  LEU B 553     4877   8327   4503   1982    392    586       C  
ATOM   2802  CD1 LEU B 553      19.009   8.555   4.580  1.00 43.96           C  
ANISOU 2802  CD1 LEU B 553     4396   8113   4192   1988    366    510       C  
ATOM   2803  CD2 LEU B 553      16.958   7.120   4.592  1.00 46.81           C  
ANISOU 2803  CD2 LEU B 553     5024   8228   4534   1967    381    516       C  
ATOM   2804  N   ILE B 554      16.515   9.362  -0.225  1.00 43.89           N  
ANISOU 2804  N   ILE B 554     4420   7728   4528   1613    457    835       N  
ATOM   2805  CA  ILE B 554      15.983  10.280  -1.222  1.00 37.78           C  
ANISOU 2805  CA  ILE B 554     3570   6855   3929   1467    466    894       C  
ATOM   2806  C   ILE B 554      14.856   9.605  -1.995  1.00 49.78           C  
ANISOU 2806  C   ILE B 554     5207   8273   5435   1436    485    944       C  
ATOM   2807  O   ILE B 554      13.830  10.221  -2.279  1.00 65.14           O  
ANISOU 2807  O   ILE B 554     7133  10077   7540   1297    484    934       O  
ATOM   2808  CB  ILE B 554      17.068  10.720  -2.220  1.00 54.66           C  
ANISOU 2808  CB  ILE B 554     5602   9117   6051   1499    476   1003       C  
ATOM   2809  CG1 ILE B 554      18.338  11.164  -1.490  1.00 58.46           C  
ANISOU 2809  CG1 ILE B 554     5973   9737   6501   1563    455    961       C  
ATOM   2810  CG2 ILE B 554      16.542  11.827  -3.122  1.00 52.21           C  
ANISOU 2810  CG2 ILE B 554     5200   8692   5944   1346    476   1065       C  
ATOM   2811  CD1 ILE B 554      18.234  12.524  -0.837  1.00 58.97           C  
ANISOU 2811  CD1 ILE B 554     5908   9716   6784   1428    423    882       C  
ATOM   2812  N   ASP B 555      15.059   8.335  -2.332  1.00 51.59           N  
ANISOU 2812  N   ASP B 555     5556   8572   5473   1577    501    996       N  
ATOM   2813  CA  ASP B 555      14.067   7.558  -3.069  1.00 45.87           C  
ANISOU 2813  CA  ASP B 555     4947   7761   4722   1569    513   1044       C  
ATOM   2814  C   ASP B 555      12.766   7.435  -2.278  1.00 35.20           C  
ANISOU 2814  C   ASP B 555     3660   6254   3459   1482    496    948       C  
ATOM   2815  O   ASP B 555      11.686   7.701  -2.803  1.00 38.53           O  
ANISOU 2815  O   ASP B 555     4086   6561   3994   1364    498    955       O  
ATOM   2816  CB  ASP B 555      14.621   6.170  -3.405  1.00 61.13           C  
ANISOU 2816  CB  ASP B 555     6988   9777   6461   1764    528   1091       C  
ATOM   2817  CG  ASP B 555      13.697   5.371  -4.307  1.00 67.66           C  
ANISOU 2817  CG  ASP B 555     7879  10489   7341   1759    554   1102       C  
ATOM   2818  OD1 ASP B 555      13.331   5.876  -5.389  1.00 73.89           O  
ANISOU 2818  OD1 ASP B 555     8610  11259   8205   1662    563   1169       O  
ATOM   2819  OD2 ASP B 555      13.346   4.232  -3.937  1.00 67.76           O  
ANISOU 2819  OD2 ASP B 555     8002  10429   7316   1858    567   1047       O  
ATOM   2820  N   ILE B 556      12.877   7.031  -1.015  1.00 33.53           N  
ANISOU 2820  N   ILE B 556     3496   6050   3194   1543    479    858       N  
ATOM   2821  CA  ILE B 556      11.719   6.932  -0.131  1.00 42.95           C  
ANISOU 2821  CA  ILE B 556     4739   7113   4468   1460    466    756       C  
ATOM   2822  C   ILE B 556      10.985   8.265  -0.041  1.00 41.74           C  
ANISOU 2822  C   ILE B 556     4475   6863   4521   1267    463    693       C  
ATOM   2823  O   ILE B 556       9.756   8.309  -0.033  1.00 39.22           O  
ANISOU 2823  O   ILE B 556     4187   6423   4291   1164    464    651       O  
ATOM   2824  CB  ILE B 556      12.123   6.485   1.288  1.00 42.94           C  
ANISOU 2824  CB  ILE B 556     4777   7153   4384   1553    449    669       C  
ATOM   2825  CG1 ILE B 556      12.607   5.034   1.273  1.00 39.70           C  
ANISOU 2825  CG1 ILE B 556     4507   6786   3790   1763    449    729       C  
ATOM   2826  CG2 ILE B 556      10.956   6.641   2.249  1.00 37.86           C  
ANISOU 2826  CG2 ILE B 556     4150   6389   3847   1437    442    552       C  
ATOM   2827  CD1 ILE B 556      13.032   4.519   2.633  1.00 36.62           C  
ANISOU 2827  CD1 ILE B 556     4168   6432   3314   1879    434    659       C  
ATOM   2828  N   ALA B 557      11.749   9.350   0.027  1.00 48.42           N  
ANISOU 2828  N   ALA B 557     5191   7757   5450   1230    457    687       N  
ATOM   2829  CA  ALA B 557      11.176  10.690   0.059  1.00 38.91           C  
ANISOU 2829  CA  ALA B 557     3880   6444   4461   1073    449    638       C  
ATOM   2830  C   ALA B 557      10.470  10.996  -1.255  1.00 40.39           C  
ANISOU 2830  C   ALA B 557     4063   6552   4734    995    464    731       C  
ATOM   2831  O   ALA B 557       9.406  11.617  -1.272  1.00 48.94           O  
ANISOU 2831  O   ALA B 557     5127   7505   5962    878    461    688       O  
ATOM   2832  CB  ALA B 557      12.257  11.719   0.330  1.00 28.97           C  
ANISOU 2832  CB  ALA B 557     2483   5248   3276   1070    434    626       C  
ATOM   2833  N   ARG B 558      11.075  10.557  -2.354  1.00 33.92           N  
ANISOU 2833  N   ARG B 558     3256   5816   3815   1068    480    857       N  
ATOM   2834  CA  ARG B 558      10.522  10.773  -3.684  1.00 28.20           C  
ANISOU 2834  CA  ARG B 558     2523   5042   3150   1011    493    960       C  
ATOM   2835  C   ARG B 558       9.215  10.019  -3.879  1.00 28.03           C  
ANISOU 2835  C   ARG B 558     2610   4931   3108    980    495    941       C  
ATOM   2836  O   ARG B 558       8.257  10.555  -4.435  1.00 36.52           O  
ANISOU 2836  O   ARG B 558     3665   5908   4304    880    494    954       O  
ATOM   2837  CB  ARG B 558      11.524  10.345  -4.760  1.00 49.00           C  
ANISOU 2837  CB  ARG B 558     5149   7810   5658   1109    510   1092       C  
ATOM   2838  CG  ARG B 558      10.947  10.335  -6.170  1.00 51.85           C  
ANISOU 2838  CG  ARG B 558     5516   8139   6045   1069    522   1203       C  
ATOM   2839  CD  ARG B 558      12.038  10.204  -7.221  1.00 54.50           C  
ANISOU 2839  CD  ARG B 558     5807   8616   6284   1148    541   1331       C  
ATOM   2840  NE  ARG B 558      12.586   8.853  -7.308  1.00 61.42           N  
ANISOU 2840  NE  ARG B 558     6786   9608   6943   1301    554   1352       N  
ATOM   2841  CZ  ARG B 558      13.650   8.528  -8.037  1.00 68.82           C  
ANISOU 2841  CZ  ARG B 558     7700  10696   7754   1404    574   1441       C  
ATOM   2842  NH1 ARG B 558      14.286   9.460  -8.733  1.00 63.68           N  
ANISOU 2842  NH1 ARG B 558     6917  10102   7175   1358    582   1521       N  
ATOM   2843  NH2 ARG B 558      14.083   7.276  -8.065  1.00 72.07           N  
ANISOU 2843  NH2 ARG B 558     8170  11170   8044   1556    595   1400       N  
ATOM   2844  N   GLN B 559       9.183   8.770  -3.429  1.00 24.11           N  
ANISOU 2844  N   GLN B 559     2228   4468   2464   1077    494    912       N  
ATOM   2845  CA  GLN B 559       7.997   7.941  -3.591  1.00 29.90           C  
ANISOU 2845  CA  GLN B 559     3060   5117   3183   1060    491    890       C  
ATOM   2846  C   GLN B 559       6.836   8.472  -2.757  1.00 39.02           C  
ANISOU 2846  C   GLN B 559     4205   6154   4468    930    484    767       C  
ATOM   2847  O   GLN B 559       5.683   8.434  -3.188  1.00 35.70           O  
ANISOU 2847  O   GLN B 559     3806   5649   4109    853    484    754       O  
ATOM   2848  CB  GLN B 559       8.298   6.487  -3.222  1.00 20.31           C  
ANISOU 2848  CB  GLN B 559     1967   3939   1812   1212    489    888       C  
ATOM   2849  CG  GLN B 559       9.430   5.865  -4.021  1.00 30.37           C  
ANISOU 2849  CG  GLN B 559     3262   5331   2947   1365    496    998       C  
ATOM   2850  CD  GLN B 559       9.498   4.359  -3.860  1.00 41.10           C  
ANISOU 2850  CD  GLN B 559     4729   6659   4229   1516    526    958       C  
ATOM   2851  OE1 GLN B 559       8.473   3.681  -3.819  1.00 45.52           O  
ANISOU 2851  OE1 GLN B 559     5369   7101   4827   1500    530    918       O  
ATOM   2852  NE2 GLN B 559      10.711   3.827  -3.775  1.00 42.66           N  
ANISOU 2852  NE2 GLN B 559     4940   6955   4314   1673    549    972       N  
ATOM   2853  N   THR B 560       7.147   8.969  -1.565  1.00 42.65           N  
ANISOU 2853  N   THR B 560     4624   6618   4965    911    476    671       N  
ATOM   2854  CA  THR B 560       6.123   9.515  -0.682  1.00 40.48           C  
ANISOU 2854  CA  THR B 560     4329   6244   4808    795    470    543       C  
ATOM   2855  C   THR B 560       5.525  10.781  -1.288  1.00 41.27           C  
ANISOU 2855  C   THR B 560     4339   6256   5084    679    470    553       C  
ATOM   2856  O   THR B 560       4.316  10.999  -1.224  1.00 52.00           O  
ANISOU 2856  O   THR B 560     5710   7525   6524    591    471    491       O  
ATOM   2857  CB  THR B 560       6.684   9.822   0.722  1.00 40.43           C  
ANISOU 2857  CB  THR B 560     4286   6272   4805    809    458    436       C  
ATOM   2858  OG1 THR B 560       7.409   8.687   1.210  1.00 35.37           O  
ANISOU 2858  OG1 THR B 560     3725   5720   3993    946    457    450       O  
ATOM   2859  CG2 THR B 560       5.557  10.144   1.690  1.00 27.07           C  
ANISOU 2859  CG2 THR B 560     2591   4489   3205    702    453    295       C  
ATOM   2860  N   ALA B 561       6.378  11.609  -1.880  1.00 33.76           N  
ANISOU 2860  N   ALA B 561     3298   5335   4195    688    469    633       N  
ATOM   2861  CA  ALA B 561       5.927  12.832  -2.533  1.00 32.55           C  
ANISOU 2861  CA  ALA B 561     3057   5090   4221    601    468    667       C  
ATOM   2862  C   ALA B 561       4.995  12.522  -3.702  1.00 33.69           C  
ANISOU 2862  C   ALA B 561     3245   5195   4358    575    476    746       C  
ATOM   2863  O   ALA B 561       4.069  13.283  -3.979  1.00 28.67           O  
ANISOU 2863  O   ALA B 561     2574   4463   3857    497    474    732       O  
ATOM   2864  CB  ALA B 561       7.115  13.654  -3.000  1.00 30.57           C  
ANISOU 2864  CB  ALA B 561     2700   4885   4029    625    464    755       C  
ATOM   2865  N   ARG B 562       5.249  11.409  -4.385  1.00 35.33           N  
ANISOU 2865  N   ARG B 562     3529   5484   4411    650    483    826       N  
ATOM   2866  CA  ARG B 562       4.415  10.982  -5.505  1.00 26.42           C  
ANISOU 2866  CA  ARG B 562     2442   4336   3261    637    484    895       C  
ATOM   2867  C   ARG B 562       3.030  10.585  -5.016  1.00 31.34           C  
ANISOU 2867  C   ARG B 562     3126   4881   3899    575    480    783       C  
ATOM   2868  O   ARG B 562       2.019  10.975  -5.599  1.00 50.94           O  
ANISOU 2868  O   ARG B 562     5592   7304   6458    510    478    788       O  
ATOM   2869  CB  ARG B 562       5.054   9.802  -6.240  1.00 31.68           C  
ANISOU 2869  CB  ARG B 562     3173   5105   3760    746    488    988       C  
ATOM   2870  CG  ARG B 562       6.357  10.125  -6.955  1.00 35.13           C  
ANISOU 2870  CG  ARG B 562     3547   5642   4161    807    497   1110       C  
ATOM   2871  CD  ARG B 562       6.869   8.913  -7.721  1.00 44.74           C  
ANISOU 2871  CD  ARG B 562     4833   6960   5208    925    501   1194       C  
ATOM   2872  NE  ARG B 562       8.141   9.174  -8.389  1.00 55.35           N  
ANISOU 2872  NE  ARG B 562     6114   8420   6497    986    516   1305       N  
ATOM   2873  CZ  ARG B 562       8.786   8.287  -9.141  1.00 60.23           C  
ANISOU 2873  CZ  ARG B 562     6755   9140   6991   1094    531   1364       C  
ATOM   2874  NH1 ARG B 562       8.277   7.078  -9.326  1.00 60.72           N  
ANISOU 2874  NH1 ARG B 562     6883   9175   7012   1153    541   1299       N  
ATOM   2875  NH2 ARG B 562       9.938   8.611  -9.709  1.00 63.82           N  
ANISOU 2875  NH2 ARG B 562     7135   9711   7404   1140    550   1451       N  
ATOM   2876  N   GLY B 563       2.993   9.797  -3.946  1.00 23.31           N  
ANISOU 2876  N   GLY B 563     2176   3874   2806    599    481    684       N  
ATOM   2877  CA  GLY B 563       1.740   9.391  -3.339  1.00 21.67           C  
ANISOU 2877  CA  GLY B 563     2022   3603   2610    532    483    566       C  
ATOM   2878  C   GLY B 563       0.945  10.576  -2.822  1.00 32.50           C  
ANISOU 2878  C   GLY B 563     3327   4892   4127    426    482    475       C  
ATOM   2879  O   GLY B 563      -0.253  10.685  -3.076  1.00 41.52           O  
ANISOU 2879  O   GLY B 563     4477   5983   5314    356    485    432       O  
ATOM   2880  N   MET B 564       1.614  11.468  -2.096  1.00 35.64           N  
ANISOU 2880  N   MET B 564     3655   5282   4604    420    478    439       N  
ATOM   2881  CA  MET B 564       0.964  12.657  -1.549  1.00 34.23           C  
ANISOU 2881  CA  MET B 564     3404   5016   4587    337    476    345       C  
ATOM   2882  C   MET B 564       0.544  13.631  -2.642  1.00 30.88           C  
ANISOU 2882  C   MET B 564     2912   4529   4292    305    477    430       C  
ATOM   2883  O   MET B 564      -0.504  14.270  -2.547  1.00 39.92           O  
ANISOU 2883  O   MET B 564     4029   5598   5542    242    480    366       O  
ATOM   2884  CB  MET B 564       1.876  13.364  -0.545  1.00 29.80           C  
ANISOU 2884  CB  MET B 564     2773   4459   4091    348    467    283       C  
ATOM   2885  CG  MET B 564       2.054  12.618   0.761  1.00 29.90           C  
ANISOU 2885  CG  MET B 564     2836   4522   4002    366    464    172       C  
ATOM   2886  SD  MET B 564       0.474  12.208   1.525  1.00 37.86           S  
ANISOU 2886  SD  MET B 564     3903   5480   5002    278    474     25       S  
ATOM   2887  CE  MET B 564      -0.268  13.832   1.681  1.00 23.73           C  
ANISOU 2887  CE  MET B 564     2007   3580   3430    195    472    -56       C  
ATOM   2888  N   ASP B 565       1.372  13.748  -3.674  1.00 36.25           N  
ANISOU 2888  N   ASP B 565     3562   5249   4963    353    475    576       N  
ATOM   2889  CA  ASP B 565       1.054  14.597  -4.814  1.00 39.92           C  
ANISOU 2889  CA  ASP B 565     3961   5666   5541    331    475    683       C  
ATOM   2890  C   ASP B 565      -0.194  14.074  -5.509  1.00 33.20           C  
ANISOU 2890  C   ASP B 565     3164   4809   4642    306    478    690       C  
ATOM   2891  O   ASP B 565      -1.030  14.846  -5.977  1.00 39.01           O  
ANISOU 2891  O   ASP B 565     3851   5482   5490    265    479    705       O  
ATOM   2892  CB  ASP B 565       2.221  14.626  -5.800  1.00 35.77           C  
ANISOU 2892  CB  ASP B 565     3398   5209   4982    388    474    842       C  
ATOM   2893  CG  ASP B 565       1.965  15.540  -6.977  1.00 35.00           C  
ANISOU 2893  CG  ASP B 565     3224   5068   5008    366    472    966       C  
ATOM   2894  OD1 ASP B 565       1.491  16.673  -6.753  1.00 44.02           O  
ANISOU 2894  OD1 ASP B 565     4290   6109   6326    317    468    934       O  
ATOM   2895  OD2 ASP B 565       2.243  15.128  -8.123  1.00 40.24           O  
ANISOU 2895  OD2 ASP B 565     3896   5800   5592    402    474   1097       O  
ATOM   2896  N   TYR B 566      -0.307  12.751  -5.573  1.00 28.78           N  
ANISOU 2896  N   TYR B 566     2700   4316   3919    336    479    678       N  
ATOM   2897  CA  TYR B 566      -1.458  12.105  -6.184  1.00 30.09           C  
ANISOU 2897  CA  TYR B 566     2916   4489   4028    311    478    667       C  
ATOM   2898  C   TYR B 566      -2.720  12.385  -5.379  1.00 34.93           C  
ANISOU 2898  C   TYR B 566     3534   5041   4696    232    485    521       C  
ATOM   2899  O   TYR B 566      -3.766  12.711  -5.940  1.00 34.03           O  
ANISOU 2899  O   TYR B 566     3399   4907   4625    190    486    520       O  
ATOM   2900  CB  TYR B 566      -1.230  10.595  -6.294  1.00 24.91           C  
ANISOU 2900  CB  TYR B 566     2353   3903   3208    364    475    668       C  
ATOM   2901  CG  TYR B 566      -2.445   9.828  -6.771  1.00 38.92           C  
ANISOU 2901  CG  TYR B 566     4175   5682   4930    326    475    623       C  
ATOM   2902  CD1 TYR B 566      -2.772   9.775  -8.121  1.00 37.34           C  
ANISOU 2902  CD1 TYR B 566     3951   5515   4719    336    465    719       C  
ATOM   2903  CD2 TYR B 566      -3.265   9.157  -5.872  1.00 34.89           C  
ANISOU 2903  CD2 TYR B 566     3726   5150   4381    270    488    481       C  
ATOM   2904  CE1 TYR B 566      -3.882   9.076  -8.562  1.00 27.89           C  
ANISOU 2904  CE1 TYR B 566     2787   4334   3475    292    467    664       C  
ATOM   2905  CE2 TYR B 566      -4.377   8.456  -6.304  1.00 36.11           C  
ANISOU 2905  CE2 TYR B 566     3918   5312   4489    215    497    428       C  
ATOM   2906  CZ  TYR B 566      -4.680   8.419  -7.650  1.00 37.71           C  
ANISOU 2906  CZ  TYR B 566     4094   5552   4684    227    486    515       C  
ATOM   2907  OH  TYR B 566      -5.784   7.723  -8.085  1.00 43.06           O  
ANISOU 2907  OH  TYR B 566     4803   6247   5312    161    498    452       O  
ATOM   2908  N   LEU B 567      -2.610  12.257  -4.060  1.00 40.54           N  
ANISOU 2908  N   LEU B 567     4267   5738   5399    213    490    397       N  
ATOM   2909  CA  LEU B 567      -3.738  12.479  -3.163  1.00 22.53           C  
ANISOU 2909  CA  LEU B 567     1990   3414   3158    136    499    246       C  
ATOM   2910  C   LEU B 567      -4.222  13.923  -3.227  1.00 34.33           C  
ANISOU 2910  C   LEU B 567     3388   4832   4826    102    502    234       C  
ATOM   2911  O   LEU B 567      -5.418  14.180  -3.356  1.00 42.52           O  
ANISOU 2911  O   LEU B 567     4414   5848   5895     53    510    181       O  
ATOM   2912  CB  LEU B 567      -3.358  12.112  -1.729  1.00 21.27           C  
ANISOU 2912  CB  LEU B 567     1861   3264   2958    129    502    128       C  
ATOM   2913  CG  LEU B 567      -2.962  10.651  -1.502  1.00 26.10           C  
ANISOU 2913  CG  LEU B 567     2568   3938   3413    166    504    132       C  
ATOM   2914  CD1 LEU B 567      -2.391  10.450  -0.109  1.00 23.15           C  
ANISOU 2914  CD1 LEU B 567     2207   3580   3011    175    505     42       C  
ATOM   2915  CD2 LEU B 567      -4.148   9.729  -1.736  1.00 32.99           C  
ANISOU 2915  CD2 LEU B 567     3509   4816   4210    108    518     79       C  
ATOM   2916  N   HIS B 568      -3.289  14.863  -3.136  1.00 39.19           N  
ANISOU 2916  N   HIS B 568     3927   5406   5558    130    495    283       N  
ATOM   2917  CA  HIS B 568      -3.626  16.280  -3.214  1.00 36.20           C  
ANISOU 2917  CA  HIS B 568     3445   4937   5374    107    495    283       C  
ATOM   2918  C   HIS B 568      -4.233  16.631  -4.572  1.00 42.38           C  
ANISOU 2918  C   HIS B 568     4194   5709   6199    108    495    406       C  
ATOM   2919  O   HIS B 568      -5.064  17.531  -4.676  1.00 47.74           O  
ANISOU 2919  O   HIS B 568     4808   6324   7007     80    499    386       O  
ATOM   2920  CB  HIS B 568      -2.391  17.142  -2.935  1.00 35.42           C  
ANISOU 2920  CB  HIS B 568     3266   4799   5392    134    483    320       C  
ATOM   2921  CG  HIS B 568      -1.989  17.172  -1.492  1.00 30.71           C  
ANISOU 2921  CG  HIS B 568     2667   4199   4802    124    480    175       C  
ATOM   2922  ND1 HIS B 568      -1.173  18.152  -0.968  1.00 32.95           N  
ANISOU 2922  ND1 HIS B 568     2861   4435   5225    131    468    153       N  
ATOM   2923  CD2 HIS B 568      -2.299  16.351  -0.462  1.00 33.31           C  
ANISOU 2923  CD2 HIS B 568     3067   4573   5016    105    485     45       C  
ATOM   2924  CE1 HIS B 568      -0.991  17.929   0.322  1.00 34.36           C  
ANISOU 2924  CE1 HIS B 568     3054   4634   5367    121    464     11       C  
ATOM   2925  NE2 HIS B 568      -1.666  16.841   0.654  1.00 36.15           N  
ANISOU 2925  NE2 HIS B 568     3378   4918   5439    105    475    -52       N  
ATOM   2926  N   ALA B 569      -3.815  15.911  -5.609  1.00 39.63           N  
ANISOU 2926  N   ALA B 569     3886   5431   5741    146    490    534       N  
ATOM   2927  CA  ALA B 569      -4.353  16.116  -6.951  1.00 33.34           C  
ANISOU 2927  CA  ALA B 569     3060   4648   4961    151    488    658       C  
ATOM   2928  C   ALA B 569      -5.794  15.626  -7.045  1.00 37.20           C  
ANISOU 2928  C   ALA B 569     3590   5165   5380    109    495    578       C  
ATOM   2929  O   ALA B 569      -6.562  16.081  -7.894  1.00 29.16           O  
ANISOU 2929  O   ALA B 569     2525   4146   4410     97    495    640       O  
ATOM   2930  CB  ALA B 569      -3.488  15.419  -7.983  1.00 17.57           C  
ANISOU 2930  CB  ALA B 569     1091   2731   2854    205    479    802       C  
ATOM   2931  N   LYS B 570      -6.148  14.686  -6.174  1.00 44.71           N  
ANISOU 2931  N   LYS B 570     4624   6150   6215     82    501    443       N  
ATOM   2932  CA  LYS B 570      -7.502  14.151  -6.122  1.00 46.97           C  
ANISOU 2932  CA  LYS B 570     4949   6473   6424     25    510    346       C  
ATOM   2933  C   LYS B 570      -8.319  14.886  -5.064  1.00 51.83           C  
ANISOU 2933  C   LYS B 570     5528   7035   7130    -28    526    202       C  
ATOM   2934  O   LYS B 570      -9.450  14.503  -4.763  1.00 65.58           O  
ANISOU 2934  O   LYS B 570     7298   8812   8806    -87    539     94       O  
ATOM   2935  CB  LYS B 570      -7.475  12.650  -5.815  1.00 46.71           C  
ANISOU 2935  CB  LYS B 570     5024   6507   6218     14    511    281       C  
ATOM   2936  CG  LYS B 570      -6.720  11.810  -6.837  1.00 44.21           C  
ANISOU 2936  CG  LYS B 570     4742   6248   5810     73    496    406       C  
ATOM   2937  CD  LYS B 570      -7.564  11.502  -8.070  1.00 42.36           C  
ANISOU 2937  CD  LYS B 570     4500   6070   5526     56    490    460       C  
ATOM   2938  CE  LYS B 570      -8.621  10.444  -7.777  1.00 49.81           C  
ANISOU 2938  CE  LYS B 570     5513   7056   6359    -21    502    328       C  
ATOM   2939  NZ  LYS B 570      -9.256   9.915  -9.020  1.00 57.89           N  
ANISOU 2939  NZ  LYS B 570     6532   8150   7312    -38    495    376       N  
ATOM   2940  N   SER B 571      -7.736  15.944  -4.505  1.00 35.05           N  
ANISOU 2940  N   SER B 571     3332   4828   5157    -11    524    195       N  
ATOM   2941  CA  SER B 571      -8.386  16.726  -3.459  1.00 30.52           C  
ANISOU 2941  CA  SER B 571     2710   4197   4690    -52    536     53       C  
ATOM   2942  C   SER B 571      -8.581  15.905  -2.186  1.00 44.29           C  
ANISOU 2942  C   SER B 571     4528   5980   6321    -93    545   -110       C  
ATOM   2943  O   SER B 571      -9.597  16.034  -1.502  1.00 42.84           O  
ANISOU 2943  O   SER B 571     4337   5802   6139   -147    560   -244       O  
ATOM   2944  CB  SER B 571      -9.726  17.273  -3.950  1.00 43.37           C  
ANISOU 2944  CB  SER B 571     4284   5823   6370    -84    547     42       C  
ATOM   2945  OG  SER B 571      -9.554  18.036  -5.131  1.00 66.31           O  
ANISOU 2945  OG  SER B 571     7116   8695   9383    -47    537    204       O  
ATOM   2946  N   ILE B 572      -7.598  15.062  -1.880  1.00 54.56           N  
ANISOU 2946  N   ILE B 572     5893   7314   7522    -68    536    -94       N  
ATOM   2947  CA  ILE B 572      -7.629  14.226  -0.682  1.00 41.34           C  
ANISOU 2947  CA  ILE B 572     4287   5678   5742   -104    543   -228       C  
ATOM   2948  C   ILE B 572      -6.544  14.627   0.315  1.00 43.08           C  
ANISOU 2948  C   ILE B 572     4476   5869   6023    -76    533   -268       C  
ATOM   2949  O   ILE B 572      -5.354  14.601  -0.002  1.00 39.77           O  
ANISOU 2949  O   ILE B 572     4051   5453   5606    -17    519   -165       O  
ATOM   2950  CB  ILE B 572      -7.453  12.733  -1.029  1.00 35.25           C  
ANISOU 2950  CB  ILE B 572     3619   4979   4794   -101    541   -188       C  
ATOM   2951  CG1 ILE B 572      -8.667  12.210  -1.798  1.00 34.42           C  
ANISOU 2951  CG1 ILE B 572     3547   4915   4614   -153    551   -193       C  
ATOM   2952  CG2 ILE B 572      -7.246  11.913   0.234  1.00 27.17           C  
ANISOU 2952  CG2 ILE B 572     2657   3984   3682   -131    546   -297       C  
ATOM   2953  CD1 ILE B 572      -8.532  10.767  -2.245  1.00 34.70           C  
ANISOU 2953  CD1 ILE B 572     3675   5005   4505   -156    551   -156       C  
ATOM   2954  N   ILE B 573      -6.966  14.996   1.522  1.00 49.08           N  
ANISOU 2954  N   ILE B 573     5210   6612   6824   -119    539   -422       N  
ATOM   2955  CA  ILE B 573      -6.040  15.337   2.597  1.00 40.42           C  
ANISOU 2955  CA  ILE B 573     4080   5503   5776   -101    528   -487       C  
ATOM   2956  C   ILE B 573      -5.877  14.137   3.526  1.00 40.63           C  
ANISOU 2956  C   ILE B 573     4189   5606   5643   -122    529   -560       C  
ATOM   2957  O   ILE B 573      -6.864  13.589   4.014  1.00 50.89           O  
ANISOU 2957  O   ILE B 573     5531   6938   6865   -190    544   -660       O  
ATOM   2958  CB  ILE B 573      -6.549  16.538   3.417  1.00 47.29           C  
ANISOU 2958  CB  ILE B 573     4856   6308   6803   -131    531   -620       C  
ATOM   2959  CG1 ILE B 573      -7.042  17.651   2.491  1.00 45.28           C  
ANISOU 2959  CG1 ILE B 573     4522   5974   6711   -120    534   -552       C  
ATOM   2960  CG2 ILE B 573      -5.463  17.052   4.349  1.00 51.94           C  
ANISOU 2960  CG2 ILE B 573     5390   6878   7465   -104    513   -673       C  
ATOM   2961  CD1 ILE B 573      -7.609  18.849   3.220  1.00 42.91           C  
ANISOU 2961  CD1 ILE B 573     4121   5601   6581   -143    537   -679       C  
ATOM   2962  N   HIS B 574      -4.635  13.728   3.766  1.00 37.85           N  
ANISOU 2962  N   HIS B 574     3852   5288   5240    -66    514   -505       N  
ATOM   2963  CA  HIS B 574      -4.364  12.570   4.615  1.00 34.43           C  
ANISOU 2963  CA  HIS B 574     3490   4927   4664    -71    514   -549       C  
ATOM   2964  C   HIS B 574      -4.606  12.893   6.086  1.00 38.57           C  
ANISOU 2964  C   HIS B 574     3977   5463   5214   -119    512   -714       C  
ATOM   2965  O   HIS B 574      -5.258  12.128   6.799  1.00 43.56           O  
ANISOU 2965  O   HIS B 574     4658   6137   5756   -180    524   -797       O  
ATOM   2966  CB  HIS B 574      -2.931  12.081   4.410  1.00 43.28           C  
ANISOU 2966  CB  HIS B 574     4630   6094   5721     23    500   -433       C  
ATOM   2967  CG  HIS B 574      -2.682  10.704   4.940  1.00 38.49           C  
ANISOU 2967  CG  HIS B 574     4111   5553   4961     45    507   -428       C  
ATOM   2968  ND1 HIS B 574      -2.237  10.468   6.222  1.00 38.46           N  
ANISOU 2968  ND1 HIS B 574     4103   5595   4917     55    503   -507       N  
ATOM   2969  CD2 HIS B 574      -2.812   9.488   4.359  1.00 42.95           C  
ANISOU 2969  CD2 HIS B 574     4769   6134   5414     66    525   -349       C  
ATOM   2970  CE1 HIS B 574      -2.104   9.168   6.409  1.00 30.62           C  
ANISOU 2970  CE1 HIS B 574     3203   4638   3795     89    522   -465       C  
ATOM   2971  NE2 HIS B 574      -2.448   8.550   5.292  1.00 37.21           N  
ANISOU 2971  NE2 HIS B 574     4101   5446   4590     95    539   -372       N  
ATOM   2972  N   ARG B 575      -4.063  14.022   6.534  1.00 45.26           N  
ANISOU 2972  N   ARG B 575     4732   6274   6192    -97    499   -762       N  
ATOM   2973  CA  ARG B 575      -4.310  14.531   7.883  1.00 39.24           C  
ANISOU 2973  CA  ARG B 575     3914   5516   5479   -138    495   -932       C  
ATOM   2974  C   ARG B 575      -3.602  13.747   8.981  1.00 47.76           C  
ANISOU 2974  C   ARG B 575     5017   6685   6444   -122    482   -974       C  
ATOM   2975  O   ARG B 575      -3.748  14.061  10.162  1.00 60.48           O  
ANISOU 2975  O   ARG B 575     6582   8319   8078   -156    477  -1115       O  
ATOM   2976  CB  ARG B 575      -5.811  14.571   8.179  1.00 32.81           C  
ANISOU 2976  CB  ARG B 575     3108   4693   4664   -225    517  -1050       C  
ATOM   2977  CG  ARG B 575      -6.568  15.667   7.462  1.00 43.33           C  
ANISOU 2977  CG  ARG B 575     4380   5940   6145   -232    529  -1052       C  
ATOM   2978  CD  ARG B 575      -8.027  15.292   7.331  1.00 64.35           C  
ANISOU 2978  CD  ARG B 575     7083   8626   8742   -305    555  -1113       C  
ATOM   2979  NE  ARG B 575      -8.644  15.031   8.627  1.00 75.70           N  
ANISOU 2979  NE  ARG B 575     8522  10121  10121   -376    564  -1281       N  
ATOM   2980  CZ  ARG B 575      -9.472  15.869   9.241  1.00 80.31           C  
ANISOU 2980  CZ  ARG B 575     9035  10688  10790   -410    576  -1424       C  
ATOM   2981  NH1 ARG B 575      -9.792  17.026   8.673  1.00 82.84           N  
ANISOU 2981  NH1 ARG B 575     9276  10926  11274   -378    581  -1412       N  
ATOM   2982  NH2 ARG B 575      -9.985  15.547  10.420  1.00 77.40           N  
ANISOU 2982  NH2 ARG B 575     8669  10388  10351   -478    584  -1573       N  
ATOM   2983  N   ASP B 576      -2.846  12.726   8.602  1.00 44.36           N  
ANISOU 2983  N   ASP B 576     4655   6308   5890    -63    480   -851       N  
ATOM   2984  CA  ASP B 576      -2.135  11.928   9.592  1.00 53.46           C  
ANISOU 2984  CA  ASP B 576     5833   7548   6932    -24    472   -868       C  
ATOM   2985  C   ASP B 576      -0.898  11.278   8.988  1.00 46.49           C  
ANISOU 2985  C   ASP B 576     4994   6709   5962     92    465   -714       C  
ATOM   2986  O   ASP B 576      -0.568  10.135   9.305  1.00 54.97           O  
ANISOU 2986  O   ASP B 576     6145   7839   6904    145    477   -667       O  
ATOM   2987  CB  ASP B 576      -3.059  10.864  10.194  1.00 72.57           C  
ANISOU 2987  CB  ASP B 576     8326  10003   9246    -94    497   -917       C  
ATOM   2988  CG  ASP B 576      -2.518  10.286  11.492  1.00 75.62           C  
ANISOU 2988  CG  ASP B 576     8716  10469   9548    -64    496   -964       C  
ATOM   2989  OD1 ASP B 576      -2.873   9.136  11.828  1.00 74.81           O  
ANISOU 2989  OD1 ASP B 576     8702  10388   9336    -79    532   -937       O  
ATOM   2990  OD2 ASP B 576      -1.737  10.982  12.176  1.00 68.52           O  
ANISOU 2990  OD2 ASP B 576     7737   9604   8693    -22    467  -1024       O  
ATOM   2991  N   LEU B 577      -0.215  12.012   8.116  1.00 39.59           N  
ANISOU 2991  N   LEU B 577     4073   5805   5166    139    453   -633       N  
ATOM   2992  CA  LEU B 577       1.010  11.512   7.507  1.00 46.71           C  
ANISOU 2992  CA  LEU B 577     5003   6761   5985    251    446   -492       C  
ATOM   2993  C   LEU B 577       2.153  11.493   8.518  1.00 47.99           C  
ANISOU 2993  C   LEU B 577     5128   7010   6097    326    426   -529       C  
ATOM   2994  O   LEU B 577       2.402  12.480   9.214  1.00 45.12           O  
ANISOU 2994  O   LEU B 577     4669   6641   5834    299    408   -630       O  
ATOM   2995  CB  LEU B 577       1.400  12.348   6.287  1.00 39.54           C  
ANISOU 2995  CB  LEU B 577     4043   5803   5176    266    442   -391       C  
ATOM   2996  CG  LEU B 577       2.660  11.861   5.565  1.00 32.80           C  
ANISOU 2996  CG  LEU B 577     3211   5020   4231    378    437   -244       C  
ATOM   2997  CD1 LEU B 577       2.436  10.480   4.962  1.00 27.59           C  
ANISOU 2997  CD1 LEU B 577     2671   4388   3425    428    455   -150       C  
ATOM   2998  CD2 LEU B 577       3.090  12.849   4.498  1.00 40.78           C  
ANISOU 2998  CD2 LEU B 577     4148   5987   5358    378    434   -153       C  
ATOM   2999  N   LYS B 578       2.840  10.358   8.590  1.00 44.99           N  
ANISOU 2999  N   LYS B 578     4825   6706   5561    431    430   -449       N  
ATOM   3000  CA  LYS B 578       3.974  10.181   9.490  1.00 48.25           C  
ANISOU 3000  CA  LYS B 578     5217   7219   5896    529    412   -468       C  
ATOM   3001  C   LYS B 578       4.704   8.898   9.113  1.00 55.43           C  
ANISOU 3001  C   LYS B 578     6237   8188   6638    674    425   -338       C  
ATOM   3002  O   LYS B 578       4.152   8.055   8.405  1.00 63.05           O  
ANISOU 3002  O   LYS B 578     7302   9102   7553    681    453   -262       O  
ATOM   3003  CB  LYS B 578       3.502  10.121  10.944  1.00 52.03           C  
ANISOU 3003  CB  LYS B 578     5679   7722   6366    481    409   -613       C  
ATOM   3004  CG  LYS B 578       2.693   8.880  11.285  1.00 49.81           C  
ANISOU 3004  CG  LYS B 578     5518   7426   5980    473    445   -605       C  
ATOM   3005  CD  LYS B 578       2.230   8.888  12.735  1.00 44.09           C  
ANISOU 3005  CD  LYS B 578     4767   6734   5250    416    447   -746       C  
ATOM   3006  CE  LYS B 578       0.749   9.212  12.840  1.00 46.99           C  
ANISOU 3006  CE  LYS B 578     5117   7033   5703    254    464   -843       C  
ATOM   3007  NZ  LYS B 578       0.237   9.018  14.225  1.00 54.22           N  
ANISOU 3007  NZ  LYS B 578     6021   7990   6589    198    476   -966       N  
ATOM   3008  N   SER B 579       5.942   8.752   9.579  1.00 52.99           N  
ANISOU 3008  N   SER B 579     5911   7980   6244    798    407   -318       N  
ATOM   3009  CA  SER B 579       6.749   7.581   9.253  1.00 50.02           C  
ANISOU 3009  CA  SER B 579     5643   7659   5705    965    418   -198       C  
ATOM   3010  C   SER B 579       6.026   6.303   9.669  1.00 57.26           C  
ANISOU 3010  C   SER B 579     6710   8516   6531    993    458   -194       C  
ATOM   3011  O   SER B 579       6.277   5.230   9.122  1.00 64.36           O  
ANISOU 3011  O   SER B 579     7738   9392   7326   1109    485    -92       O  
ATOM   3012  CB  SER B 579       8.117   7.659   9.932  1.00 36.83           C  
ANISOU 3012  CB  SER B 579     3926   6119   3949   1095    391   -204       C  
ATOM   3013  OG  SER B 579       7.985   7.591  11.338  1.00 41.49           O  
ANISOU 3013  OG  SER B 579     4505   6742   4518   1089    384   -318       O  
ATOM   3014  N   ASN B 580       5.119   6.430  10.633  1.00 47.84           N  
ANISOU 3014  N   ASN B 580     5506   7288   5383    883    469   -312       N  
ATOM   3015  CA  ASN B 580       4.326   5.301  11.109  1.00 50.99           C  
ANISOU 3015  CA  ASN B 580     6054   7615   5705    875    522   -322       C  
ATOM   3016  C   ASN B 580       3.298   4.831  10.073  1.00 41.81           C  
ANISOU 3016  C   ASN B 580     4977   6338   4571    794    563   -271       C  
ATOM   3017  O   ASN B 580       3.023   3.635   9.953  1.00 51.87           O  
ANISOU 3017  O   ASN B 580     6424   7534   5749    839    617   -223       O  
ATOM   3018  CB  ASN B 580       3.634   5.658  12.428  1.00 84.25           C  
ANISOU 3018  CB  ASN B 580    10216  11839   9956    764    523   -466       C  
ATOM   3019  CG  ASN B 580       2.927   4.473  13.052  1.00 98.89           C  
ANISOU 3019  CG  ASN B 580    12241  13624  11709    752    586   -475       C  
ATOM   3020  OD1 ASN B 580       3.568   3.558  13.570  1.00101.08           O  
ANISOU 3020  OD1 ASN B 580    12646  13910  11851    887    608   -434       O  
ATOM   3021  ND2 ASN B 580       1.600   4.482  13.007  1.00104.71           N  
ANISOU 3021  ND2 ASN B 580    12994  14287  12504    589    618   -530       N  
ATOM   3022  N   ASN B 581       2.740   5.778   9.321  1.00 44.74           N  
ANISOU 3022  N   ASN B 581     5240   6690   5070    676    540   -287       N  
ATOM   3023  CA  ASN B 581       1.749   5.463   8.292  1.00 47.89           C  
ANISOU 3023  CA  ASN B 581     5696   6998   5503    594    571   -247       C  
ATOM   3024  C   ASN B 581       2.321   5.199   6.896  1.00 49.21           C  
ANISOU 3024  C   ASN B 581     5891   7159   5647    686    568   -112       C  
ATOM   3025  O   ASN B 581       1.577   5.159   5.910  1.00 44.53           O  
ANISOU 3025  O   ASN B 581     5313   6508   5100    617    582    -80       O  
ATOM   3026  CB  ASN B 581       0.688   6.566   8.213  1.00 46.44           C  
ANISOU 3026  CB  ASN B 581     5396   6788   5460    422    552   -342       C  
ATOM   3027  CG  ASN B 581      -0.183   6.635   9.444  1.00 43.96           C  
ANISOU 3027  CG  ASN B 581     5071   6470   5162    312    567   -478       C  
ATOM   3028  OD1 ASN B 581      -1.097   7.453   9.518  1.00 43.77           O  
ANISOU 3028  OD1 ASN B 581     4966   6425   5240    183    555   -571       O  
ATOM   3029  ND2 ASN B 581       0.089   5.785  10.414  1.00 42.80           N  
ANISOU 3029  ND2 ASN B 581     5013   6342   4909    369    596   -490       N  
ATOM   3030  N   ILE B 582       3.635   5.009   6.825  1.00 49.38           N  
ANISOU 3030  N   ILE B 582     5918   7252   5593    844    548    -36       N  
ATOM   3031  CA  ILE B 582       4.303   4.751   5.553  1.00 27.94           C  
ANISOU 3031  CA  ILE B 582     3222   4552   2842    945    544     92       C  
ATOM   3032  C   ILE B 582       4.925   3.363   5.547  1.00 39.57           C  
ANISOU 3032  C   ILE B 582     4858   6006   4170   1120    581    161       C  
ATOM   3033  O   ILE B 582       6.014   3.167   6.085  1.00 50.26           O  
ANISOU 3033  O   ILE B 582     6222   7438   5436   1262    565    182       O  
ATOM   3034  CB  ILE B 582       5.406   5.797   5.252  1.00 24.32           C  
ANISOU 3034  CB  ILE B 582     2629   4198   2412    984    494    131       C  
ATOM   3035  CG1 ILE B 582       4.826   7.206   5.257  1.00 34.53           C  
ANISOU 3035  CG1 ILE B 582     3790   5469   3862    820    472     55       C  
ATOM   3036  CG2 ILE B 582       6.089   5.512   3.909  1.00 29.04           C  
ANISOU 3036  CG2 ILE B 582     3246   4827   2960   1082    493    270       C  
ATOM   3037  CD1 ILE B 582       5.856   8.298   5.084  1.00 38.61           C  
ANISOU 3037  CD1 ILE B 582     4187   6052   4430    836    444     73       C  
ATOM   3038  N   PHE B 583       4.260   2.417   4.916  1.00 43.35           N  
ANISOU 3038  N   PHE B 583     5474   6376   4622   1112    635    189       N  
ATOM   3039  CA  PHE B 583       4.730   1.053   4.865  1.00 51.58           C  
ANISOU 3039  CA  PHE B 583     6710   7359   5530   1273    685    241       C  
ATOM   3040  C   PHE B 583       5.811   0.821   3.807  1.00 48.93           C  
ANISOU 3040  C   PHE B 583     6351   7089   5151   1435    663    355       C  
ATOM   3041  O   PHE B 583       5.604   1.074   2.663  1.00 56.01           O  
ANISOU 3041  O   PHE B 583     7169   7998   6114   1390    648    407       O  
ATOM   3042  CB  PHE B 583       3.544   0.154   4.612  1.00 93.46           C  
ANISOU 3042  CB  PHE B 583    12190  12509  10813   1185    759    216       C  
ATOM   3043  CG  PHE B 583       3.365  -0.918   5.630  1.00118.87           C  
ANISOU 3043  CG  PHE B 583    15467  15662  14035   1035    790    112       C  
ATOM   3044  CD1 PHE B 583       4.042  -2.113   5.520  1.00124.80           C  
ANISOU 3044  CD1 PHE B 583    16391  16360  14666   1096    830     83       C  
ATOM   3045  CD2 PHE B 583       2.507  -0.739   6.693  1.00132.59           C  
ANISOU 3045  CD2 PHE B 583    17094  17395  15887    836    780     43       C  
ATOM   3046  CE1 PHE B 583       3.875  -3.097   6.465  1.00135.76           C  
ANISOU 3046  CE1 PHE B 583    17833  17699  16049    950    859     -7       C  
ATOM   3047  CE2 PHE B 583       2.341  -1.718   7.643  1.00137.62           C  
ANISOU 3047  CE2 PHE B 583    17778  17990  16522    696    810    -54       C  
ATOM   3048  CZ  PHE B 583       3.020  -2.896   7.532  1.00141.31           C  
ANISOU 3048  CZ  PHE B 583    18412  18411  16870    748    849    -77       C  
ATOM   3049  N   LEU B 584       6.977   0.351   4.203  1.00 51.81           N  
ANISOU 3049  N   LEU B 584     6782   7505   5398   1629    661    393       N  
ATOM   3050  CA  LEU B 584       8.048   0.066   3.257  1.00 54.65           C  
ANISOU 3050  CA  LEU B 584     7137   7933   5694   1803    647    497       C  
ATOM   3051  C   LEU B 584       7.914  -1.353   2.711  1.00 66.74           C  
ANISOU 3051  C   LEU B 584     8889   9330   7138   1910    721    523       C  
ATOM   3052  O   LEU B 584       8.688  -2.241   3.066  1.00 73.40           O  
ANISOU 3052  O   LEU B 584     9874  10161   7854   2095    746    543       O  
ATOM   3053  CB  LEU B 584       9.422   0.263   3.903  1.00 49.57           C  
ANISOU 3053  CB  LEU B 584     6439   7436   4958   1965    601    523       C  
ATOM   3054  CG  LEU B 584      10.045   1.657   3.817  1.00 50.59           C  
ANISOU 3054  CG  LEU B 584     6353   7734   5136   1899    528    539       C  
ATOM   3055  CD1 LEU B 584      11.500   1.619   4.261  1.00 51.36           C  
ANISOU 3055  CD1 LEU B 584     6424   7985   5105   2080    495    572       C  
ATOM   3056  CD2 LEU B 584       9.941   2.189   2.399  1.00 51.55           C  
ANISOU 3056  CD2 LEU B 584     6389   7879   5320   1829    514    617       C  
ATOM   3057  N   HIS B 585       6.923  -1.557   1.846  1.00 65.17           N  
ANISOU 3057  N   HIS B 585     8729   9031   7002   1789    758    517       N  
ATOM   3058  CA  HIS B 585       6.655  -2.874   1.272  1.00 65.20           C  
ANISOU 3058  CA  HIS B 585     8958   8894   6922   1849    835    524       C  
ATOM   3059  C   HIS B 585       7.905  -3.461   0.626  1.00 71.18           C  
ANISOU 3059  C   HIS B 585     9761   9704   7579   2087    836    606       C  
ATOM   3060  O   HIS B 585       8.484  -2.865  -0.283  1.00 61.97           O  
ANISOU 3060  O   HIS B 585     8430   8659   6459   2135    791    675       O  
ATOM   3061  CB  HIS B 585       5.523  -2.790   0.246  1.00 77.05           C  
ANISOU 3061  CB  HIS B 585    10439  10325   8512   1679    859    511       C  
ATOM   3062  CG  HIS B 585       5.047  -4.121  -0.249  1.00 91.84           C  
ANISOU 3062  CG  HIS B 585    12561  12041  10293   1688    942    497       C  
ATOM   3063  ND1 HIS B 585       5.766  -5.284  -0.071  1.00 99.04           N  
ANISOU 3063  ND1 HIS B 585    13694  12884  11053   1871    988    517       N  
ATOM   3064  CD2 HIS B 585       3.927  -4.471  -0.924  1.00 97.75           C  
ANISOU 3064  CD2 HIS B 585    13382  12690  11068   1534    987    462       C  
ATOM   3065  CE1 HIS B 585       5.106  -6.293  -0.611  1.00103.87           C  
ANISOU 3065  CE1 HIS B 585    14516  13348  11601   1820   1058    496       C  
ATOM   3066  NE2 HIS B 585       3.987  -5.828  -1.136  1.00101.83           N  
ANISOU 3066  NE2 HIS B 585    14167  13075  11449   1612   1059    461       N  
ATOM   3067  N   GLU B 586       8.315  -4.632   1.106  1.00 90.43           N  
ANISOU 3067  N   GLU B 586    12431  12055   9872   2237    888    598       N  
ATOM   3068  CA  GLU B 586       9.495  -5.313   0.584  1.00 89.54           C  
ANISOU 3068  CA  GLU B 586    12391  11985   9646   2484    897    664       C  
ATOM   3069  C   GLU B 586      10.739  -4.431   0.668  1.00 78.85           C  
ANISOU 3069  C   GLU B 586    10812  10846   8300   2613    816    723       C  
ATOM   3070  O   GLU B 586      11.699  -4.624  -0.079  1.00 71.64           O  
ANISOU 3070  O   GLU B 586     9866  10024   7332   2786    805    791       O  
ATOM   3071  CB  GLU B 586       9.259  -5.779  -0.855  1.00113.53           C  
ANISOU 3071  CB  GLU B 586    15473  14971  12691   2486    935    697       C  
ATOM   3072  CG  GLU B 586       8.259  -6.922  -0.981  1.00120.94           C  
ANISOU 3072  CG  GLU B 586    16689  15696  13566   2399   1021    645       C  
ATOM   3073  CD  GLU B 586       7.800  -7.137  -2.409  1.00123.01           C  
ANISOU 3073  CD  GLU B 586    16947  15925  13864   2339   1050    664       C  
ATOM   3074  OE1 GLU B 586       8.437  -6.577  -3.325  1.00118.31           O  
ANISOU 3074  OE1 GLU B 586    16161  15471  13321   2414   1009    726       O  
ATOM   3075  OE2 GLU B 586       6.804  -7.862  -2.617  1.00124.44           O  
ANISOU 3075  OE2 GLU B 586    17316  15949  14016   2210   1112    616       O  
ATOM   3076  N   ASP B 587      10.705  -3.462   1.580  1.00 81.11           N  
ANISOU 3076  N   ASP B 587    10950  11221   8646   2516    761    694       N  
ATOM   3077  CA  ASP B 587      11.839  -2.579   1.850  1.00 85.18           C  
ANISOU 3077  CA  ASP B 587    11272  11945   9147   2601    680    739       C  
ATOM   3078  C   ASP B 587      12.051  -1.478   0.812  1.00 92.00           C  
ANISOU 3078  C   ASP B 587    11916  12950  10091   2490    639    785       C  
ATOM   3079  O   ASP B 587      12.770  -0.514   1.071  1.00100.00           O  
ANISOU 3079  O   ASP B 587    12770  14129  11097   2451    597    786       O  
ATOM   3080  CB  ASP B 587      13.133  -3.384   2.027  1.00 93.47           C  
ANISOU 3080  CB  ASP B 587    12416  13063  10035   2873    692    774       C  
ATOM   3081  CG  ASP B 587      13.226  -4.050   3.384  1.00 99.44           C  
ANISOU 3081  CG  ASP B 587    13335  13754  10693   2964    716    721       C  
ATOM   3082  OD1 ASP B 587      12.194  -4.559   3.871  1.00 97.95           O  
ANISOU 3082  OD1 ASP B 587    13309  13393  10516   2848    771    657       O  
ATOM   3083  OD2 ASP B 587      14.332  -4.066   3.963  1.00103.32           O  
ANISOU 3083  OD2 ASP B 587    13795  14379  11084   3140    683    740       O  
ATOM   3084  N   ASN B 588      11.425  -1.608  -0.353  1.00 85.43           N  
ANISOU 3084  N   ASN B 588    11086  12049   9325   2418    666    811       N  
ATOM   3085  CA  ASN B 588      11.718  -0.698  -1.459  1.00 78.48           C  
ANISOU 3085  CA  ASN B 588    10024  11298   8496   2320    652    855       C  
ATOM   3086  C   ASN B 588      10.541   0.120  -1.992  1.00 70.96           C  
ANISOU 3086  C   ASN B 588     8977  10291   7693   2096    627    854       C  
ATOM   3087  O   ASN B 588      10.742   1.176  -2.589  1.00 76.08           O  
ANISOU 3087  O   ASN B 588     9471  11044   8393   1984    603    888       O  
ATOM   3088  CB  ASN B 588      12.386  -1.459  -2.608  1.00 95.05           C  
ANISOU 3088  CB  ASN B 588    12169  13432  10514   2464    700    903       C  
ATOM   3089  CG  ASN B 588      13.742  -2.018  -2.224  1.00101.08           C  
ANISOU 3089  CG  ASN B 588    12984  14301  11120   2686    716    912       C  
ATOM   3090  OD1 ASN B 588      14.748  -1.308  -2.248  1.00 99.41           O  
ANISOU 3090  OD1 ASN B 588    12632  14272  10867   2703    693    935       O  
ATOM   3091  ND2 ASN B 588      13.775  -3.297  -1.868  1.00103.07           N  
ANISOU 3091  ND2 ASN B 588    13452  14432  11276   2861    756    897       N  
ATOM   3092  N   THR B 589       9.320  -0.359  -1.781  1.00 58.76           N  
ANISOU 3092  N   THR B 589     7536   8577   6212   2036    637    820       N  
ATOM   3093  CA  THR B 589       8.154   0.320  -2.338  1.00 59.96           C  
ANISOU 3093  CA  THR B 589     7606   8681   6495   1829    626    804       C  
ATOM   3094  C   THR B 589       7.309   1.018  -1.275  1.00 61.20           C  
ANISOU 3094  C   THR B 589     7727   8797   6729   1651    614    712       C  
ATOM   3095  O   THR B 589       6.643   0.371  -0.467  1.00 62.19           O  
ANISOU 3095  O   THR B 589     7980   8809   6840   1617    663    627       O  
ATOM   3096  CB  THR B 589       7.279  -0.642  -3.156  1.00 63.46           C  
ANISOU 3096  CB  THR B 589     8173   8988   6951   1805    697    779       C  
ATOM   3097  OG1 THR B 589       8.103  -1.371  -4.074  1.00 68.22           O  
ANISOU 3097  OG1 THR B 589     8821   9624   7474   1984    718    847       O  
ATOM   3098  CG2 THR B 589       6.219   0.128  -3.934  1.00 57.52           C  
ANISOU 3098  CG2 THR B 589     7306   8225   6324   1612    677    776       C  
ATOM   3099  N   VAL B 590       7.341   2.348  -1.287  1.00 62.91           N  
ANISOU 3099  N   VAL B 590     7786   9102   7015   1530    557    725       N  
ATOM   3100  CA  VAL B 590       6.556   3.142  -0.343  1.00 50.36           C  
ANISOU 3100  CA  VAL B 590     6144   7478   5512   1363    547    626       C  
ATOM   3101  C   VAL B 590       5.061   2.933  -0.538  1.00 52.97           C  
ANISOU 3101  C   VAL B 590     6516   7682   5928   1218    581    559       C  
ATOM   3102  O   VAL B 590       4.544   3.024  -1.652  1.00 55.70           O  
ANISOU 3102  O   VAL B 590     6834   8007   6323   1165    582    599       O  
ATOM   3103  CB  VAL B 590       6.856   4.651  -0.460  1.00 38.23           C  
ANISOU 3103  CB  VAL B 590     4452   6028   4047   1253    504    638       C  
ATOM   3104  CG1 VAL B 590       5.795   5.468   0.262  1.00 36.04           C  
ANISOU 3104  CG1 VAL B 590     4121   5681   3891   1075    501    525       C  
ATOM   3105  CG2 VAL B 590       8.232   4.965   0.097  1.00 35.52           C  
ANISOU 3105  CG2 VAL B 590     4064   5811   3620   1352    485    656       C  
ATOM   3106  N   LYS B 591       4.370   2.655   0.562  1.00 55.15           N  
ANISOU 3106  N   LYS B 591     6859   7886   6209   1150    610    455       N  
ATOM   3107  CA  LYS B 591       2.919   2.493   0.552  1.00 45.71           C  
ANISOU 3107  CA  LYS B 591     5706   6586   5075    991    645    376       C  
ATOM   3108  C   LYS B 591       2.267   3.427   1.589  1.00 43.02           C  
ANISOU 3108  C   LYS B 591     5280   6252   4813    845    622    273       C  
ATOM   3109  O   LYS B 591       2.313   3.160   2.791  1.00 49.04           O  
ANISOU 3109  O   LYS B 591     6094   7006   5535    852    637    206       O  
ATOM   3110  CB  LYS B 591       2.546   1.022   0.807  1.00 33.21           C  
ANISOU 3110  CB  LYS B 591     4337   4886   3395   1028    725    343       C  
ATOM   3111  CG  LYS B 591       2.880   0.067  -0.349  1.00 37.09           C  
ANISOU 3111  CG  LYS B 591     4933   5339   3823   1138    764    416       C  
ATOM   3112  CD  LYS B 591       1.791   0.099  -1.434  1.00 38.69           C  
ANISOU 3112  CD  LYS B 591     5114   5496   4091   1004    780    405       C  
ATOM   3113  CE  LYS B 591       2.287  -0.527  -2.743  1.00 40.45           C  
ANISOU 3113  CE  LYS B 591     5376   5723   4270   1117    800    485       C  
ATOM   3114  NZ  LYS B 591       1.249  -0.533  -3.818  1.00 49.85           N  
ANISOU 3114  NZ  LYS B 591     6544   6884   5513    990    814    471       N  
ATOM   3115  N   ILE B 592       1.680   4.528   1.123  1.00 40.32           N  
ANISOU 3115  N   ILE B 592     4816   5923   4581    723    586    258       N  
ATOM   3116  CA  ILE B 592       1.022   5.478   2.023  1.00 40.19           C  
ANISOU 3116  CA  ILE B 592     4721   5902   4649    591    567    148       C  
ATOM   3117  C   ILE B 592      -0.395   5.056   2.388  1.00 46.46           C  
ANISOU 3117  C   ILE B 592     5574   6619   5458    459    606     49       C  
ATOM   3118  O   ILE B 592      -1.229   4.848   1.503  1.00 40.97           O  
ANISOU 3118  O   ILE B 592     4901   5883   4783    394    621     59       O  
ATOM   3119  CB  ILE B 592       0.987   6.898   1.441  1.00 43.66           C  
ANISOU 3119  CB  ILE B 592     5028   6359   5201    524    527    163       C  
ATOM   3120  CG1 ILE B 592       2.378   7.513   1.472  1.00 34.23           C  
ANISOU 3120  CG1 ILE B 592     3767   5240   4000    613    501    224       C  
ATOM   3121  CG2 ILE B 592       0.020   7.799   2.220  1.00 41.70           C  
ANISOU 3121  CG2 ILE B 592     4719   6070   5055    387    520     31       C  
ATOM   3122  CD1 ILE B 592       2.411   8.943   0.971  1.00 27.44           C  
ANISOU 3122  CD1 ILE B 592     2794   4363   3269    544    483    238       C  
ATOM   3123  N   GLY B 593      -0.681   4.932   3.684  1.00 59.64           N  
ANISOU 3123  N   GLY B 593     7269   8281   7110    412    622    -49       N  
ATOM   3124  CA  GLY B 593      -1.997   4.456   4.106  1.00 63.41           C  
ANISOU 3124  CA  GLY B 593     7816   8696   7580    276    667   -141       C  
ATOM   3125  C   GLY B 593      -2.315   4.649   5.588  1.00 65.77           C  
ANISOU 3125  C   GLY B 593     8101   9011   7880    208    672   -255       C  
ATOM   3126  O   GLY B 593      -1.995   5.705   6.140  1.00 45.39           O  
ANISOU 3126  O   GLY B 593     5394   6484   5369    201    625   -307       O  
ATOM   3127  N   ASP B 594      -2.918   3.645   6.237  1.00102.07           N  
ANISOU 3127  N   ASP B 594    12835  13554  12394    155    734   -298       N  
ATOM   3128  CA  ASP B 594      -3.568   3.840   7.535  1.00110.17           C  
ANISOU 3128  CA  ASP B 594    13839  14596  13423     48    745   -415       C  
ATOM   3129  C   ASP B 594      -4.280   5.170   7.406  1.00114.57           C  
ANISOU 3129  C   ASP B 594    14226  15192  14112    -61    695   -499       C  
ATOM   3130  O   ASP B 594      -4.082   6.066   8.227  1.00121.23           O  
ANISOU 3130  O   ASP B 594    14958  16088  15017    -72    657   -577       O  
ATOM   3131  CB  ASP B 594      -2.559   3.847   8.704  1.00 77.57           C  
ANISOU 3131  CB  ASP B 594     9705  10520   9247    153    731   -429       C  
ATOM   3132  CG  ASP B 594      -3.181   3.388  10.015  1.00 92.41           C  
ANISOU 3132  CG  ASP B 594    11654  12391  11066     69    772   -519       C  
ATOM   3133  OD1 ASP B 594      -4.386   3.599  10.163  1.00 99.09           O  
ANISOU 3133  OD1 ASP B 594    12470  13227  11953    -91    789   -600       O  
ATOM   3134  OD2 ASP B 594      -2.497   2.836  10.903  1.00 89.36           O  
ANISOU 3134  OD2 ASP B 594    11351  12016  10586    162    786   -511       O  
ATOM   3135  N   PHE B 595      -5.070   5.313   6.341  1.00110.91           N  
ANISOU 3135  N   PHE B 595    13753  14699  13689   -131    694   -486       N  
ATOM   3136  CA  PHE B 595      -5.789   6.562   6.109  1.00123.69           C  
ANISOU 3136  CA  PHE B 595    15243  16336  15418   -213    651   -563       C  
ATOM   3137  C   PHE B 595      -6.598   6.964   7.336  1.00131.28           C  
ANISOU 3137  C   PHE B 595    16155  17322  16402   -327    654   -710       C  
ATOM   3138  O   PHE B 595      -6.133   7.778   8.119  1.00136.06           O  
ANISOU 3138  O   PHE B 595    16673  17960  17063   -300    621   -773       O  
ATOM   3139  CB  PHE B 595      -6.718   6.486   4.886  1.00108.82           C  
ANISOU 3139  CB  PHE B 595    13378  14423  13543   -276    658   -540       C  
ATOM   3140  CG  PHE B 595      -6.014   6.578   3.542  1.00 94.72           C  
ANISOU 3140  CG  PHE B 595    11586  12630  11774   -170    635   -408       C  
ATOM   3141  CD1 PHE B 595      -5.715   5.419   2.820  1.00 84.38           C  
ANISOU 3141  CD1 PHE B 595    10384  11293  10383   -118    671   -316       C  
ATOM   3142  CD2 PHE B 595      -5.700   7.821   2.980  1.00 81.29           C  
ANISOU 3142  CD2 PHE B 595     9782  10937  10168   -125    590   -378       C  
ATOM   3143  CE1 PHE B 595      -5.091   5.492   1.578  1.00 68.66           C  
ANISOU 3143  CE1 PHE B 595     8375   9309   8404    -23    649   -199       C  
ATOM   3144  CE2 PHE B 595      -5.072   7.906   1.736  1.00 68.14           C  
ANISOU 3144  CE2 PHE B 595     8107   9272   8513    -38    573   -247       C  
ATOM   3145  CZ  PHE B 595      -4.770   6.741   1.036  1.00 61.86           C  
ANISOU 3145  CZ  PHE B 595     7398   8475   7632     13    596   -160       C  
ATOM   3146  N   GLY B 596      -7.812   6.428   7.473  1.00130.86           N  
ANISOU 3146  N   GLY B 596    16155  17258  16307   -458    695   -772       N  
ATOM   3147  CA  GLY B 596      -8.580   6.560   8.702  1.00129.65           C  
ANISOU 3147  CA  GLY B 596    15969  17141  16150   -572    710   -903       C  
ATOM   3148  C   GLY B 596      -9.079   7.959   9.010  1.00125.50           C  
ANISOU 3148  C   GLY B 596    15309  16647  15729   -611    661  -1030       C  
ATOM   3149  O   GLY B 596     -10.239   8.140   9.362  1.00123.40           O  
ANISOU 3149  O   GLY B 596    15019  16406  15462   -730    673  -1141       O  
ATOM   3150  N   LEU B 597      -8.202   8.947   8.885  1.00150.40           N  
ANISOU 3150  N   LEU B 597    18386  19792  18966   -506    616  -1018       N  
ATOM   3151  CA  LEU B 597      -8.554  10.334   9.138  1.00145.83           C  
ANISOU 3151  CA  LEU B 597    17708  19204  18497   -514    590  -1133       C  
ATOM   3152  C   LEU B 597      -8.634  11.109   7.830  1.00136.04           C  
ANISOU 3152  C   LEU B 597    16446  17906  17335   -458    581  -1064       C  
ATOM   3153  O   LEU B 597      -8.896  12.313   7.826  1.00128.76           O  
ANISOU 3153  O   LEU B 597    15447  16947  16528   -442    577  -1126       O  
ATOM   3154  CB  LEU B 597      -7.504  10.967  10.043  1.00101.05           C  
ANISOU 3154  CB  LEU B 597    11966  13546  12883   -444    563  -1174       C  
ATOM   3155  CG  LEU B 597      -7.292  10.312  11.402  1.00 97.53           C  
ANISOU 3155  CG  LEU B 597    11522  13169  12366   -477    570  -1233       C  
ATOM   3156  CD1 LEU B 597      -6.095  10.925  12.106  1.00 95.13           C  
ANISOU 3156  CD1 LEU B 597    11148  12887  12109   -388    537  -1258       C  
ATOM   3157  CD2 LEU B 597      -8.542  10.448  12.258  1.00 92.01           C  
ANISOU 3157  CD2 LEU B 597    10789  12507  11663   -608    585  -1388       C  
ATOM   3158  N   ALA B 598      -8.372  10.421   6.724  1.00 81.88           N  
ANISOU 3158  N   ALA B 598     9651  11035  10425   -421    586   -926       N  
ATOM   3159  CA  ALA B 598      -8.385  11.054   5.408  1.00 85.42           C  
ANISOU 3159  CA  ALA B 598    10075  11440  10939   -366    578   -834       C  
ATOM   3160  C   ALA B 598      -9.727  11.709   5.120  1.00 96.57           C  
ANISOU 3160  C   ALA B 598    11453  12844  12395   -429    593   -912       C  
ATOM   3161  O   ALA B 598     -10.762  11.269   5.616  1.00 93.60           O  
ANISOU 3161  O   ALA B 598    11104  12509  11950   -529    612  -1016       O  
ATOM   3162  CB  ALA B 598      -8.048  10.043   4.322  1.00106.42           C  
ANISOU 3162  CB  ALA B 598    12813  14106  13517   -331    582   -692       C  
ATOM   3163  N   THR B 599      -9.699  12.754   4.300  1.00106.08           N  
ANISOU 3163  N   THR B 599    12591  13997  13716   -371    588   -852       N  
ATOM   3164  CA  THR B 599     -10.906  13.477   3.923  1.00131.35           C  
ANISOU 3164  CA  THR B 599    15744  17190  16975   -406    605   -902       C  
ATOM   3165  C   THR B 599     -10.799  13.971   2.492  1.00115.49           C  
ANISOU 3165  C   THR B 599    13702  15142  15035   -345    598   -752       C  
ATOM   3166  O   THR B 599      -9.771  13.799   1.838  1.00113.78           O  
ANISOU 3166  O   THR B 599    13501  14907  14825   -279    581   -620       O  
ATOM   3167  CB  THR B 599     -11.143  14.698   4.828  1.00192.99           C  
ANISOU 3167  CB  THR B 599    23453  24956  24919   -406    609  -1025       C  
ATOM   3168  OG1 THR B 599     -12.335  15.377   4.412  1.00190.13           O  
ANISOU 3168  OG1 THR B 599    23036  24589  24615   -430    627  -1061       O  
ATOM   3169  CG2 THR B 599      -9.971  15.665   4.732  1.00195.49           C  
ANISOU 3169  CG2 THR B 599    23697  25189  25393   -320    587   -955       C  
ATOM   3170  N   GLU B 600     -11.864  14.603   2.014  1.00100.98           N  
ANISOU 3170  N   GLU B 600    11813  13303  13251   -367    612   -771       N  
ATOM   3171  CA  GLU B 600     -11.876  15.162   0.672  1.00102.95           C  
ANISOU 3171  CA  GLU B 600    12018  13521  13579   -316    604   -626       C  
ATOM   3172  C   GLU B 600     -13.005  16.170   0.507  1.00100.19           C  
ANISOU 3172  C   GLU B 600    11579  13157  13333   -335    619   -671       C  
ATOM   3173  O   GLU B 600     -13.104  16.838  -0.520  1.00104.43           O  
ANISOU 3173  O   GLU B 600    12055  13660  13962   -297    612   -555       O  
ATOM   3174  CB  GLU B 600     -12.028  14.048  -0.356  1.00104.01           C  
ANISOU 3174  CB  GLU B 600    12231  13721  13566   -328    602   -534       C  
ATOM   3175  CG  GLU B 600     -13.260  13.207  -0.133  1.00107.36           C  
ANISOU 3175  CG  GLU B 600    12711  14231  13849   -429    621   -643       C  
ATOM   3176  CD  GLU B 600     -13.677  12.456  -1.370  1.00111.79           C  
ANISOU 3176  CD  GLU B 600    13315  14851  14310   -446    618   -556       C  
ATOM   3177  OE1 GLU B 600     -14.744  12.798  -1.919  1.00115.08           O  
ANISOU 3177  OE1 GLU B 600    13690  15312  14725   -481    629   -566       O  
ATOM   3178  OE2 GLU B 600     -12.944  11.535  -1.795  1.00113.04           O  
ANISOU 3178  OE2 GLU B 600    13539  15015  14394   -425    606   -481       O  
ATOM   3179  N   GLY B 615       0.377  10.504  19.667  1.00116.94           N  
ANISOU 3179  N   GLY B 615    13633  16241  14557     94    411  -1528       N  
ATOM   3180  CA  GLY B 615       1.607  10.149  18.984  1.00114.26           C  
ANISOU 3180  CA  GLY B 615    13347  15913  14153    240    400  -1387       C  
ATOM   3181  C   GLY B 615       1.817  10.993  17.743  1.00102.83           C  
ANISOU 3181  C   GLY B 615    11862  14385  12825    230    378  -1343       C  
ATOM   3182  O   GLY B 615       2.949  11.296  17.369  1.00102.45           O  
ANISOU 3182  O   GLY B 615    11784  14364  12777    324    353  -1286       O  
ATOM   3183  N   SER B 616       0.713  11.381  17.112  1.00 72.19           N  
ANISOU 3183  N   SER B 616     7982  10407   9041    116    392  -1367       N  
ATOM   3184  CA  SER B 616       0.747  12.178  15.892  1.00 66.44           C  
ANISOU 3184  CA  SER B 616     7233   9583   8428    105    384  -1318       C  
ATOM   3185  C   SER B 616       1.245  13.595  16.156  1.00 57.51           C  
ANISOU 3185  C   SER B 616     5978   8427   7446     97    356  -1426       C  
ATOM   3186  O   SER B 616       1.493  14.360  15.225  1.00 62.26           O  
ANISOU 3186  O   SER B 616     6552   8946   8160    106    355  -1376       O  
ATOM   3187  CB  SER B 616      -0.649  12.239  15.270  1.00 83.11           C  
ANISOU 3187  CB  SER B 616     9379  11602  10597     -7    410  -1332       C  
ATOM   3188  OG  SER B 616      -1.246  10.956  15.228  1.00 85.63           O  
ANISOU 3188  OG  SER B 616     9805  11939  10792    -25    445  -1262       O  
ATOM   3189  N   ILE B 617       1.384  13.938  17.432  1.00 56.61           N  
ANISOU 3189  N   ILE B 617     5788   8382   7339     83    339  -1571       N  
ATOM   3190  CA  ILE B 617       1.742  15.294  17.837  1.00 60.73           C  
ANISOU 3190  CA  ILE B 617     6188   8871   8015     67    321  -1700       C  
ATOM   3191  C   ILE B 617       2.991  15.837  17.137  1.00 45.47           C  
ANISOU 3191  C   ILE B 617     4213   6922   6139    148    306  -1609       C  
ATOM   3192  O   ILE B 617       3.038  17.009  16.760  1.00 37.01           O  
ANISOU 3192  O   ILE B 617     3066   5753   5244    122    306  -1646       O  
ATOM   3193  CB  ILE B 617       1.917  15.395  19.371  1.00 71.85           C  
ANISOU 3193  CB  ILE B 617     7523  10388   9389     59    303  -1860       C  
ATOM   3194  CG1 ILE B 617       2.475  16.766  19.761  1.00 76.73           C  
ANISOU 3194  CG1 ILE B 617     8012  10974  10166     58    286  -1986       C  
ATOM   3195  CG2 ILE B 617       2.818  14.281  19.884  1.00 66.78           C  
ANISOU 3195  CG2 ILE B 617     6924   9891   8559    159    292  -1779       C  
ATOM   3196  CD1 ILE B 617       1.569  17.925  19.398  1.00 79.74           C  
ANISOU 3196  CD1 ILE B 617     8345  11203  10749    -18    304  -2076       C  
ATOM   3197  N   LEU B 618       3.996  14.986  16.960  1.00 28.74           N  
ANISOU 3197  N   LEU B 618     2142   4902   3875    250    297  -1485       N  
ATOM   3198  CA  LEU B 618       5.256  15.417  16.363  1.00 38.10           C  
ANISOU 3198  CA  LEU B 618     3282   6104   5091    328    283  -1399       C  
ATOM   3199  C   LEU B 618       5.086  15.917  14.931  1.00 47.92           C  
ANISOU 3199  C   LEU B 618     4538   7222   6449    306    298  -1285       C  
ATOM   3200  O   LEU B 618       5.824  16.790  14.476  1.00 34.16           O  
ANISOU 3200  O   LEU B 618     2716   5446   4817    322    289  -1258       O  
ATOM   3201  CB  LEU B 618       6.284  14.287  16.406  1.00 43.39           C  
ANISOU 3201  CB  LEU B 618     4014   6912   5560    458    275  -1283       C  
ATOM   3202  CG  LEU B 618       6.776  13.876  17.792  1.00 43.55           C  
ANISOU 3202  CG  LEU B 618     4007   7076   5465    514    256  -1373       C  
ATOM   3203  CD1 LEU B 618       7.772  12.734  17.685  1.00 40.49           C  
ANISOU 3203  CD1 LEU B 618     3696   6808   4879    669    254  -1237       C  
ATOM   3204  CD2 LEU B 618       7.399  15.064  18.507  1.00 42.87           C  
ANISOU 3204  CD2 LEU B 618     3775   7021   5493    493    233  -1512       C  
ATOM   3205  N   TRP B 619       4.111  15.361  14.221  1.00 55.21           N  
ANISOU 3205  N   TRP B 619     5554   8080   7344    267    321  -1217       N  
ATOM   3206  CA  TRP B 619       3.896  15.712  12.823  1.00 40.84           C  
ANISOU 3206  CA  TRP B 619     3752   6153   5612    252    336  -1098       C  
ATOM   3207  C   TRP B 619       2.812  16.767  12.659  1.00 52.08           C  
ANISOU 3207  C   TRP B 619     5127   7438   7225    157    348  -1185       C  
ATOM   3208  O   TRP B 619       2.316  16.990  11.554  1.00 55.27           O  
ANISOU 3208  O   TRP B 619     5554   7748   7696    136    364  -1095       O  
ATOM   3209  CB  TRP B 619       3.541  14.467  12.012  1.00 39.16           C  
ANISOU 3209  CB  TRP B 619     3668   5957   5253    279    355   -960       C  
ATOM   3210  CG  TRP B 619       4.655  13.472  11.937  1.00 37.13           C  
ANISOU 3210  CG  TRP B 619     3465   5820   4825    400    348   -848       C  
ATOM   3211  CD1 TRP B 619       5.607  13.382  10.966  1.00 35.27           C  
ANISOU 3211  CD1 TRP B 619     3235   5610   4555    480    346   -707       C  
ATOM   3212  CD2 TRP B 619       4.936  12.427  12.875  1.00 46.92           C  
ANISOU 3212  CD2 TRP B 619     4759   7169   5900    467    344   -866       C  
ATOM   3213  NE1 TRP B 619       6.462  12.345  11.238  1.00 37.32           N  
ANISOU 3213  NE1 TRP B 619     3554   5992   4635    601    341   -642       N  
ATOM   3214  CE2 TRP B 619       6.073  11.742  12.405  1.00 42.65           C  
ANISOU 3214  CE2 TRP B 619     4263   6712   5231    602    340   -733       C  
ATOM   3215  CE3 TRP B 619       4.337  12.004  14.064  1.00 55.64           C  
ANISOU 3215  CE3 TRP B 619     5878   8310   6952    433    346   -977       C  
ATOM   3216  CZ2 TRP B 619       6.624  10.655  13.084  1.00 43.75           C  
ANISOU 3216  CZ2 TRP B 619     4470   6956   5196    718    339   -706       C  
ATOM   3217  CZ3 TRP B 619       4.884  10.927  14.736  1.00 55.53           C  
ANISOU 3217  CZ3 TRP B 619     5929   8399   6771    538    347   -942       C  
ATOM   3218  CH2 TRP B 619       6.016  10.264  14.244  1.00 49.43           C  
ANISOU 3218  CH2 TRP B 619     5210   7694   5876    687    345   -807       C  
ATOM   3219  N   MET B 620       2.450  17.416  13.761  1.00 54.81           N  
ANISOU 3219  N   MET B 620     5401   7774   7652    110    341  -1360       N  
ATOM   3220  CA  MET B 620       1.396  18.422  13.734  1.00 48.64           C  
ANISOU 3220  CA  MET B 620     4568   6866   7047     36    355  -1459       C  
ATOM   3221  C   MET B 620       1.952  19.804  13.432  1.00 53.37           C  
ANISOU 3221  C   MET B 620     5051   7370   7859     45    345  -1467       C  
ATOM   3222  O   MET B 620       2.973  20.209  13.986  1.00 57.25           O  
ANISOU 3222  O   MET B 620     5464   7910   8377     78    324  -1509       O  
ATOM   3223  CB  MET B 620       0.633  18.447  15.059  1.00 43.35           C  
ANISOU 3223  CB  MET B 620     3875   6233   6364    -19    357  -1651       C  
ATOM   3224  CG  MET B 620      -0.042  17.134  15.399  1.00 42.61           C  
ANISOU 3224  CG  MET B 620     3885   6226   6079    -46    367  -1646       C  
ATOM   3225  SD  MET B 620      -1.636  17.370  16.203  1.00 89.41           S  
ANISOU 3225  SD  MET B 620     9800  12130  12042   -149    387  -1831       S  
ATOM   3226  CE  MET B 620      -2.145  15.667  16.432  1.00 81.78           C  
ANISOU 3226  CE  MET B 620     8953  11277  10843   -181    396  -1771       C  
ATOM   3227  N   ALA B 621       1.273  20.518  12.542  1.00 69.63           N  
ANISOU 3227  N   ALA B 621     7092   9297  10068     17    359  -1422       N  
ATOM   3228  CA  ALA B 621       1.636  21.890  12.226  1.00 69.70           C  
ANISOU 3228  CA  ALA B 621     6984   9195  10306     18    350  -1425       C  
ATOM   3229  C   ALA B 621       1.194  22.801  13.357  1.00 73.08           C  
ANISOU 3229  C   ALA B 621     7316   9580  10873    -18    347  -1631       C  
ATOM   3230  O   ALA B 621       0.243  22.488  14.074  1.00 84.69           O  
ANISOU 3230  O   ALA B 621     8817  11075  12287    -56    359  -1754       O  
ATOM   3231  CB  ALA B 621       0.995  22.321  10.923  1.00 39.18           C  
ANISOU 3231  CB  ALA B 621     3127   5207   6553      7    365  -1303       C  
ATOM   3232  N   PRO B 622       1.884  23.936  13.520  1.00 60.26           N  
ANISOU 3232  N   PRO B 622     5569   7897   9431    -10    330  -1673       N  
ATOM   3233  CA  PRO B 622       1.504  24.904  14.551  1.00 64.77           C  
ANISOU 3233  CA  PRO B 622     6034   8418  10157    -40    326  -1873       C  
ATOM   3234  C   PRO B 622       0.015  25.218  14.472  1.00 70.77           C  
ANISOU 3234  C   PRO B 622     6805   9085  11001    -80    349  -1943       C  
ATOM   3235  O   PRO B 622      -0.644  25.341  15.502  1.00 81.57           O  
ANISOU 3235  O   PRO B 622     8146  10475  12371   -109    356  -2121       O  
ATOM   3236  CB  PRO B 622       2.328  26.139  14.182  1.00 48.41           C  
ANISOU 3236  CB  PRO B 622     3836   6252   8306    -27    309  -1842       C  
ATOM   3237  CG  PRO B 622       3.529  25.588  13.491  1.00 42.65           C  
ANISOU 3237  CG  PRO B 622     3140   5601   7464     16    296  -1671       C  
ATOM   3238  CD  PRO B 622       3.053  24.379  12.741  1.00 38.36           C  
ANISOU 3238  CD  PRO B 622     2742   5105   6730     26    313  -1537       C  
ATOM   3239  N   GLU B 623      -0.501  25.331  13.252  1.00 61.42           N  
ANISOU 3239  N   GLU B 623     5653   7809   9875    -80    361  -1801       N  
ATOM   3240  CA  GLU B 623      -1.912  25.612  13.021  1.00 52.43           C  
ANISOU 3240  CA  GLU B 623     4521   6591   8808   -110    382  -1844       C  
ATOM   3241  C   GLU B 623      -2.794  24.477  13.527  1.00 50.88           C  
ANISOU 3241  C   GLU B 623     4432   6502   8398   -139    403  -1910       C  
ATOM   3242  O   GLU B 623      -3.875  24.709  14.068  1.00 54.01           O  
ANISOU 3242  O   GLU B 623     4809   6886   8826   -172    419  -2045       O  
ATOM   3243  CB  GLU B 623      -2.155  25.823  11.530  1.00 60.91           C  
ANISOU 3243  CB  GLU B 623     5614   7572   9956    -97    389  -1654       C  
ATOM   3244  CG  GLU B 623      -0.905  25.646  10.689  1.00 68.07           C  
ANISOU 3244  CG  GLU B 623     6533   8495  10837    -61    373  -1473       C  
ATOM   3245  CD  GLU B 623      -1.201  25.044   9.334  1.00 85.89           C  
ANISOU 3245  CD  GLU B 623     8877  10746  13010    -50    386  -1279       C  
ATOM   3246  OE1 GLU B 623      -0.469  25.351   8.376  1.00 89.97           O  
ANISOU 3246  OE1 GLU B 623     9367  11225  13591    -25    376  -1122       O  
ATOM   3247  OE2 GLU B 623      -2.168  24.262   9.225  1.00 95.74           O  
ANISOU 3247  OE2 GLU B 623    10216  12034  14126    -69    408  -1285       O  
ATOM   3248  N   VAL B 624      -2.331  23.247  13.338  1.00 76.52           N  
ANISOU 3248  N   VAL B 624     7788   9858  11429   -127    403  -1811       N  
ATOM   3249  CA  VAL B 624      -3.064  22.076  13.804  1.00 88.76           C  
ANISOU 3249  CA  VAL B 624     9440  11514  12770   -160    419  -1857       C  
ATOM   3250  C   VAL B 624      -3.086  22.042  15.326  1.00 96.69           C  
ANISOU 3250  C   VAL B 624    10406  12603  13729   -184    413  -2054       C  
ATOM   3251  O   VAL B 624      -4.089  21.675  15.939  1.00108.10           O  
ANISOU 3251  O   VAL B 624    11879  14097  15098   -230    431  -2166       O  
ATOM   3252  CB  VAL B 624      -2.435  20.771  13.283  1.00 70.31           C  
ANISOU 3252  CB  VAL B 624     7218   9271  10225   -135    416  -1702       C  
ATOM   3253  CG1 VAL B 624      -3.113  19.567  13.912  1.00 70.67           C  
ANISOU 3253  CG1 VAL B 624     7356   9428  10067   -175    428  -1758       C  
ATOM   3254  CG2 VAL B 624      -2.525  20.706  11.767  1.00 65.69           C  
ANISOU 3254  CG2 VAL B 624     6678   8619   9664   -115    425  -1513       C  
ATOM   3255  N   ILE B 625      -1.969  22.433  15.928  1.00 80.01           N  
ANISOU 3255  N   ILE B 625     8222  10519  11659   -154    389  -2098       N  
ATOM   3256  CA  ILE B 625      -1.823  22.426  17.377  1.00 69.03           C  
ANISOU 3256  CA  ILE B 625     6783   9223  10223   -170    379  -2280       C  
ATOM   3257  C   ILE B 625      -2.602  23.565  18.038  1.00 65.12           C  
ANISOU 3257  C   ILE B 625     6180   8653   9909   -200    389  -2469       C  
ATOM   3258  O   ILE B 625      -3.230  23.378  19.081  1.00 66.43           O  
ANISOU 3258  O   ILE B 625     6337   8894  10011   -237    397  -2629       O  
ATOM   3259  CB  ILE B 625      -0.335  22.491  17.775  1.00 54.33           C  
ANISOU 3259  CB  ILE B 625     4870   7428   8343   -123    350  -2264       C  
ATOM   3260  CG1 ILE B 625       0.309  21.110  17.621  1.00 29.60           C  
ANISOU 3260  CG1 ILE B 625     1845   4427   4977    -90    341  -2133       C  
ATOM   3261  CG2 ILE B 625      -0.180  23.000  19.198  1.00 69.29           C  
ANISOU 3261  CG2 ILE B 625     6668   9384  10277   -137    340  -2474       C  
ATOM   3262  CD1 ILE B 625       1.815  21.115  17.751  1.00 35.94           C  
ANISOU 3262  CD1 ILE B 625     2603   5304   5747    -28    314  -2079       C  
ATOM   3263  N   ARG B 626      -2.562  24.741  17.420  1.00 61.13           N  
ANISOU 3263  N   ARG B 626     5589   8005   9633   -184    386  -2446       N  
ATOM   3264  CA  ARG B 626      -3.277  25.906  17.928  1.00 61.39           C  
ANISOU 3264  CA  ARG B 626     5509   7951   9866   -203    392  -2613       C  
ATOM   3265  C   ARG B 626      -4.785  25.759  17.736  1.00 64.94           C  
ANISOU 3265  C   ARG B 626     5998   8380  10297   -237    421  -2651       C  
ATOM   3266  O   ARG B 626      -5.576  26.344  18.479  1.00 71.36           O  
ANISOU 3266  O   ARG B 626     6738   9182  11192   -259    431  -2827       O  
ATOM   3267  CB  ARG B 626      -2.796  27.179  17.230  1.00 60.31           C  
ANISOU 3267  CB  ARG B 626     5266   7659   9989   -177    378  -2556       C  
ATOM   3268  CG  ARG B 626      -1.387  27.612  17.591  1.00 68.69           C  
ANISOU 3268  CG  ARG B 626     6250   8738  11112   -151    351  -2566       C  
ATOM   3269  CD  ARG B 626      -1.109  29.017  17.068  1.00 84.72           C  
ANISOU 3269  CD  ARG B 626     8154  10607  13430   -140    339  -2547       C  
ATOM   3270  NE  ARG B 626      -0.531  29.025  15.725  1.00 93.32           N  
ANISOU 3270  NE  ARG B 626     9271  11631  14555   -117    331  -2321       N  
ATOM   3271  CZ  ARG B 626      -1.235  28.970  14.598  1.00 84.37           C  
ANISOU 3271  CZ  ARG B 626     8188  10417  13450   -116    343  -2181       C  
ATOM   3272  NH1 ARG B 626      -2.558  28.888  14.638  1.00 75.45           N  
ANISOU 3272  NH1 ARG B 626     7088   9265  12315   -137    364  -2242       N  
ATOM   3273  NH2 ARG B 626      -0.612  28.990  13.427  1.00 84.28           N  
ANISOU 3273  NH2 ARG B 626     8194  10362  13466    -94    335  -1979       N  
ATOM   3274  N   ASN B 631     -11.322  25.041  10.819  1.00 84.23           N  
ANISOU 3274  N   ASN B 631     8698  10596  12710   -285    551  -1982       N  
ATOM   3275  CA  ASN B 631     -10.651  23.761  10.622  1.00 80.91           C  
ANISOU 3275  CA  ASN B 631     8407  10261  12074   -292    553  -1884       C  
ATOM   3276  C   ASN B 631      -9.178  23.970  10.280  1.00 71.34           C  
ANISOU 3276  C   ASN B 631     7186   8985  10933   -247    524  -1765       C  
ATOM   3277  O   ASN B 631      -8.855  24.649   9.305  1.00 66.19           O  
ANISOU 3277  O   ASN B 631     6488   8236  10427   -213    512  -1632       O  
ATOM   3278  CB  ASN B 631     -11.351  22.952   9.524  1.00 82.79           C  
ANISOU 3278  CB  ASN B 631     8736  10548  12173   -306    573  -1752       C  
ATOM   3279  CG  ASN B 631     -11.027  21.467   9.590  1.00 83.92           C  
ANISOU 3279  CG  ASN B 631     9016  10804  12066   -332    581  -1707       C  
ATOM   3280  OD1 ASN B 631     -10.655  20.945  10.641  1.00 89.72           O  
ANISOU 3280  OD1 ASN B 631     9780  11606  12702   -354    577  -1807       O  
ATOM   3281  ND2 ASN B 631     -11.180  20.778   8.464  1.00 73.74           N  
ANISOU 3281  ND2 ASN B 631     7805   9537  10675   -330    588  -1555       N  
ATOM   3282  N   PRO B 632      -8.280  23.395  11.093  1.00 72.62           N  
ANISOU 3282  N   PRO B 632     7388   9216  10991   -248    513  -1812       N  
ATOM   3283  CA  PRO B 632      -6.830  23.568  10.934  1.00 76.46           C  
ANISOU 3283  CA  PRO B 632     7856   9670  11526   -207    486  -1722       C  
ATOM   3284  C   PRO B 632      -6.251  22.806   9.744  1.00 81.21           C  
ANISOU 3284  C   PRO B 632     8547  10290  12021   -181    484  -1510       C  
ATOM   3285  O   PRO B 632      -5.331  23.296   9.089  1.00 76.54           O  
ANISOU 3285  O   PRO B 632     7914   9636  11530   -144    466  -1390       O  
ATOM   3286  CB  PRO B 632      -6.269  22.991  12.236  1.00 58.14           C  
ANISOU 3286  CB  PRO B 632     5557   7452   9082   -220    478  -1848       C  
ATOM   3287  CG  PRO B 632      -7.294  22.006  12.682  1.00 52.03           C  
ANISOU 3287  CG  PRO B 632     4867   6782   8119   -271    502  -1924       C  
ATOM   3288  CD  PRO B 632      -8.615  22.593  12.282  1.00 52.06           C  
ANISOU 3288  CD  PRO B 632     4832   6733   8216   -291    524  -1963       C  
ATOM   3289  N   TYR B 633      -6.789  21.620   9.476  1.00 79.86           N  
ANISOU 3289  N   TYR B 633     8488  10207  11647   -204    502  -1469       N  
ATOM   3290  CA  TYR B 633      -6.245  20.736   8.449  1.00 63.90           C  
ANISOU 3290  CA  TYR B 633     6559   8222   9500   -180    500  -1285       C  
ATOM   3291  C   TYR B 633      -6.418  21.254   7.024  1.00 60.21           C  
ANISOU 3291  C   TYR B 633     6067   7673   9136   -155    502  -1125       C  
ATOM   3292  O   TYR B 633      -7.485  21.735   6.646  1.00 56.22           O  
ANISOU 3292  O   TYR B 633     5530   7126   8707   -172    517  -1141       O  
ATOM   3293  CB  TYR B 633      -6.862  19.344   8.573  1.00 50.74           C  
ANISOU 3293  CB  TYR B 633     5012   6665   7602   -218    518  -1297       C  
ATOM   3294  CG  TYR B 633      -6.518  18.648   9.868  1.00 56.92           C  
ANISOU 3294  CG  TYR B 633     5827   7542   8260   -241    512  -1414       C  
ATOM   3295  CD1 TYR B 633      -7.281  18.849  11.011  1.00 64.06           C  
ANISOU 3295  CD1 TYR B 633     6696   8476   9167   -291    522  -1600       C  
ATOM   3296  CD2 TYR B 633      -5.430  17.790   9.948  1.00 52.55           C  
ANISOU 3296  CD2 TYR B 633     5330   7055   7583   -210    495  -1335       C  
ATOM   3297  CE1 TYR B 633      -6.970  18.215  12.198  1.00 67.90           C  
ANISOU 3297  CE1 TYR B 633     7205   9057   9537   -316    513  -1699       C  
ATOM   3298  CE2 TYR B 633      -5.111  17.150  11.129  1.00 55.10           C  
ANISOU 3298  CE2 TYR B 633     5673   7470   7793   -228    485  -1429       C  
ATOM   3299  CZ  TYR B 633      -5.884  17.366  12.251  1.00 62.71           C  
ANISOU 3299  CZ  TYR B 633     6601   8462   8763   -284    493  -1609       C  
ATOM   3300  OH  TYR B 633      -5.573  16.733  13.432  1.00 55.90           O  
ANISOU 3300  OH  TYR B 633     5750   7700   7788   -306    481  -1695       O  
ATOM   3301  N   SER B 634      -5.351  21.138   6.241  1.00 68.78           N  
ANISOU 3301  N   SER B 634     7164   8751  10218   -113    487   -969       N  
ATOM   3302  CA  SER B 634      -5.358  21.510   4.833  1.00 68.14           C  
ANISOU 3302  CA  SER B 634     7066   8612  10213    -88    487   -795       C  
ATOM   3303  C   SER B 634      -4.245  20.750   4.133  1.00 51.52           C  
ANISOU 3303  C   SER B 634     5021   6564   7989    -50    478   -639       C  
ATOM   3304  O   SER B 634      -3.523  19.978   4.764  1.00 48.36           O  
ANISOU 3304  O   SER B 634     4673   6243   7458    -39    471   -670       O  
ATOM   3305  CB  SER B 634      -5.137  23.015   4.673  1.00 67.89           C  
ANISOU 3305  CB  SER B 634     6899   8455  10441    -75    472   -786       C  
ATOM   3306  OG  SER B 634      -3.885  23.406   5.214  1.00 66.80           O  
ANISOU 3306  OG  SER B 634     6708   8304  10368    -55    450   -804       O  
ATOM   3307  N   PHE B 635      -4.104  20.964   2.830  1.00 45.71           N  
ANISOU 3307  N   PHE B 635     4274   5796   7297    -26    476   -471       N  
ATOM   3308  CA  PHE B 635      -2.973  20.407   2.106  1.00 45.52           C  
ANISOU 3308  CA  PHE B 635     4288   5825   7182     16    467   -319       C  
ATOM   3309  C   PHE B 635      -1.696  20.944   2.737  1.00 50.94           C  
ANISOU 3309  C   PHE B 635     4906   6504   7947     38    446   -344       C  
ATOM   3310  O   PHE B 635      -0.660  20.281   2.739  1.00 53.39           O  
ANISOU 3310  O   PHE B 635     5253   6895   8137     72    439   -288       O  
ATOM   3311  CB  PHE B 635      -3.029  20.790   0.628  1.00 50.52           C  
ANISOU 3311  CB  PHE B 635     4893   6420   7883     34    468   -139       C  
ATOM   3312  CG  PHE B 635      -4.265  20.312  -0.078  1.00 56.77           C  
ANISOU 3312  CG  PHE B 635     5740   7231   8599     16    485   -109       C  
ATOM   3313  CD1 PHE B 635      -5.189  21.216  -0.576  1.00 64.18           C  
ANISOU 3313  CD1 PHE B 635     6608   8093   9684      0    490    -92       C  
ATOM   3314  CD2 PHE B 635      -4.505  18.957  -0.243  1.00 52.75           C  
ANISOU 3314  CD2 PHE B 635     5348   6821   7875     15    496   -100       C  
ATOM   3315  CE1 PHE B 635      -6.326  20.778  -1.228  1.00 61.36           C  
ANISOU 3315  CE1 PHE B 635     6294   7773   9248    -16    506    -67       C  
ATOM   3316  CE2 PHE B 635      -5.641  18.513  -0.893  1.00 50.09           C  
ANISOU 3316  CE2 PHE B 635     5055   6512   7466     -7    510    -81       C  
ATOM   3317  CZ  PHE B 635      -6.552  19.425  -1.386  1.00 53.47           C  
ANISOU 3317  CZ  PHE B 635     5410   6878   8028    -22    515    -66       C  
ATOM   3318  N   GLN B 636      -1.791  22.153   3.282  1.00 57.78           N  
ANISOU 3318  N   GLN B 636     5664   7275   9014     22    437   -433       N  
ATOM   3319  CA  GLN B 636      -0.662  22.810   3.927  1.00 60.28           C  
ANISOU 3319  CA  GLN B 636     5897   7578   9429     36    415   -475       C  
ATOM   3320  C   GLN B 636      -0.176  22.026   5.142  1.00 54.33           C  
ANISOU 3320  C   GLN B 636     5192   6927   8524     41    411   -598       C  
ATOM   3321  O   GLN B 636       1.024  21.942   5.396  1.00 59.87           O  
ANISOU 3321  O   GLN B 636     5871   7687   9190     71    395   -576       O  
ATOM   3322  CB  GLN B 636      -1.050  24.228   4.347  1.00 75.80           C  
ANISOU 3322  CB  GLN B 636     7739   9416  11646     13    406   -571       C  
ATOM   3323  CG  GLN B 636      -1.811  25.000   3.281  1.00 79.93           C  
ANISOU 3323  CG  GLN B 636     8211   9835  12323      7    412   -469       C  
ATOM   3324  CD  GLN B 636      -0.998  25.225   2.021  1.00 80.13           C  
ANISOU 3324  CD  GLN B 636     8208   9848  12390     33    402   -261       C  
ATOM   3325  OE1 GLN B 636       0.224  25.068   2.017  1.00 74.55           O  
ANISOU 3325  OE1 GLN B 636     7492   9194  11639     55    388   -207       O  
ATOM   3326  NE2 GLN B 636      -1.675  25.601   0.943  1.00 87.26           N  
ANISOU 3326  NE2 GLN B 636     9091  10693  13371     32    408   -143       N  
ATOM   3327  N   SER B 637      -1.116  21.460   5.894  1.00 39.43           N  
ANISOU 3327  N   SER B 637     3364   5072   6544     10    424   -726       N  
ATOM   3328  CA  SER B 637      -0.784  20.652   7.059  1.00 35.35           C  
ANISOU 3328  CA  SER B 637     2895   4660   5876     10    420   -838       C  
ATOM   3329  C   SER B 637      -0.036  19.410   6.602  1.00 39.48           C  
ANISOU 3329  C   SER B 637     3513   5294   6193     52    420   -715       C  
ATOM   3330  O   SER B 637       0.982  19.032   7.186  1.00 43.52           O  
ANISOU 3330  O   SER B 637     4024   5891   6621     88    405   -727       O  
ATOM   3331  CB  SER B 637      -2.054  20.248   7.804  1.00 44.16           C  
ANISOU 3331  CB  SER B 637     4058   5793   6929    -40    438   -981       C  
ATOM   3332  OG  SER B 637      -3.064  21.229   7.656  1.00 53.97           O  
ANISOU 3332  OG  SER B 637     5236   6932   8340    -70    448  -1037       O  
ATOM   3333  N   ASP B 638      -0.554  18.781   5.552  1.00 41.67           N  
ANISOU 3333  N   ASP B 638     3867   5576   6391     53    435   -597       N  
ATOM   3334  CA  ASP B 638       0.078  17.610   4.955  1.00 36.77           C  
ANISOU 3334  CA  ASP B 638     3334   5051   5587    100    437   -470       C  
ATOM   3335  C   ASP B 638       1.504  17.921   4.515  1.00 32.59           C  
ANISOU 3335  C   ASP B 638     2751   4550   5081    157    421   -360       C  
ATOM   3336  O   ASP B 638       2.404  17.091   4.656  1.00 41.61           O  
ANISOU 3336  O   ASP B 638     3936   5798   6076    211    415   -316       O  
ATOM   3337  CB  ASP B 638      -0.739  17.109   3.762  1.00 37.48           C  
ANISOU 3337  CB  ASP B 638     3492   5125   5623     90    455   -362       C  
ATOM   3338  CG  ASP B 638      -1.957  16.311   4.182  1.00 44.20           C  
ANISOU 3338  CG  ASP B 638     4425   6001   6371     41    471   -455       C  
ATOM   3339  OD1 ASP B 638      -2.203  16.189   5.401  1.00 43.82           O  
ANISOU 3339  OD1 ASP B 638     4376   5976   6296     11    470   -600       O  
ATOM   3340  OD2 ASP B 638      -2.665  15.800   3.289  1.00 49.21           O  
ANISOU 3340  OD2 ASP B 638     5117   6637   6945     30    484   -383       O  
ATOM   3341  N   VAL B 639       1.701  19.122   3.980  1.00 17.19           N  
ANISOU 3341  N   VAL B 639      703   2510   3319    149    414   -313       N  
ATOM   3342  CA  VAL B 639       3.027  19.567   3.566  1.00 32.50           C  
ANISOU 3342  CA  VAL B 639     2572   4474   5301    192    399   -215       C  
ATOM   3343  C   VAL B 639       3.988  19.602   4.753  1.00 39.92           C  
ANISOU 3343  C   VAL B 639     3470   5486   6213    216    381   -319       C  
ATOM   3344  O   VAL B 639       5.140  19.182   4.639  1.00 51.17           O  
ANISOU 3344  O   VAL B 639     4893   7013   7535    273    372   -248       O  
ATOM   3345  CB  VAL B 639       2.975  20.953   2.887  1.00 44.93           C  
ANISOU 3345  CB  VAL B 639     4035   5926   7110    169    392   -157       C  
ATOM   3346  CG1 VAL B 639       4.380  21.492   2.656  1.00 37.14           C  
ANISOU 3346  CG1 VAL B 639     2960   4972   6180    202    374    -78       C  
ATOM   3347  CG2 VAL B 639       2.206  20.872   1.575  1.00 43.97           C  
ANISOU 3347  CG2 VAL B 639     3949   5759   6998    160    408    -23       C  
ATOM   3348  N   TYR B 640       3.505  20.096   5.892  1.00 39.85           N  
ANISOU 3348  N   TYR B 640     3419   5434   6286    177    375   -489       N  
ATOM   3349  CA  TYR B 640       4.317  20.167   7.106  1.00 30.23           C  
ANISOU 3349  CA  TYR B 640     2153   4289   5042    196    356   -606       C  
ATOM   3350  C   TYR B 640       4.694  18.776   7.599  1.00 33.17           C  
ANISOU 3350  C   TYR B 640     2623   4810   5172    244    357   -607       C  
ATOM   3351  O   TYR B 640       5.859  18.503   7.879  1.00 40.64           O  
ANISOU 3351  O   TYR B 640     3548   5862   6030    304    343   -583       O  
ATOM   3352  CB  TYR B 640       3.584  20.932   8.213  1.00 34.99           C  
ANISOU 3352  CB  TYR B 640     2697   4821   5778    142    353   -797       C  
ATOM   3353  CG  TYR B 640       4.357  21.010   9.516  1.00 29.01           C  
ANISOU 3353  CG  TYR B 640     1884   4148   4991    159    333   -930       C  
ATOM   3354  CD1 TYR B 640       5.216  22.071   9.775  1.00 28.10           C  
ANISOU 3354  CD1 TYR B 640     1643   4009   5026    164    313   -966       C  
ATOM   3355  CD2 TYR B 640       4.229  20.022  10.483  1.00 23.20           C  
ANISOU 3355  CD2 TYR B 640     1217   3522   4078    168    333  -1018       C  
ATOM   3356  CE1 TYR B 640       5.924  22.145  10.961  1.00 35.11           C  
ANISOU 3356  CE1 TYR B 640     2474   4986   5881    179    295  -1093       C  
ATOM   3357  CE2 TYR B 640       4.932  20.088  11.672  1.00 26.96           C  
ANISOU 3357  CE2 TYR B 640     1637   4087   4519    188    314  -1136       C  
ATOM   3358  CZ  TYR B 640       5.779  21.152  11.905  1.00 38.83           C  
ANISOU 3358  CZ  TYR B 640     3015   5572   6168    194    296  -1177       C  
ATOM   3359  OH  TYR B 640       6.483  21.224  13.085  1.00 51.19           O  
ANISOU 3359  OH  TYR B 640     4518   7238   7693    214    276  -1300       O  
ATOM   3360  N   ALA B 641       3.697  17.904   7.706  1.00 34.99           N  
ANISOU 3360  N   ALA B 641     2954   5047   5293    221    373   -632       N  
ATOM   3361  CA  ALA B 641       3.921  16.529   8.138  1.00 30.36           C  
ANISOU 3361  CA  ALA B 641     2465   4585   4486    267    375   -623       C  
ATOM   3362  C   ALA B 641       4.958  15.851   7.250  1.00 42.30           C  
ANISOU 3362  C   ALA B 641     4016   6181   5874    354    375   -456       C  
ATOM   3363  O   ALA B 641       5.800  15.092   7.730  1.00 48.22           O  
ANISOU 3363  O   ALA B 641     4794   7052   6476    430    366   -445       O  
ATOM   3364  CB  ALA B 641       2.619  15.751   8.130  1.00 26.22           C  
ANISOU 3364  CB  ALA B 641     2037   4038   3885    219    394   -650       C  
ATOM   3365  N   PHE B 642       4.883  16.128   5.953  1.00 33.03           N  
ANISOU 3365  N   PHE B 642     2841   4950   4759    349    386   -327       N  
ATOM   3366  CA  PHE B 642       5.849  15.605   4.998  1.00 22.55           C  
ANISOU 3366  CA  PHE B 642     1538   3702   3328    427    388   -168       C  
ATOM   3367  C   PHE B 642       7.240  16.139   5.314  1.00 29.48           C  
ANISOU 3367  C   PHE B 642     2320   4653   4226    479    369   -163       C  
ATOM   3368  O   PHE B 642       8.234  15.418   5.206  1.00 24.34           O  
ANISOU 3368  O   PHE B 642     1696   4127   3424    571    367    -92       O  
ATOM   3369  CB  PHE B 642       5.453  15.988   3.572  1.00 39.77           C  
ANISOU 3369  CB  PHE B 642     3714   5804   5592    400    402    -39       C  
ATOM   3370  CG  PHE B 642       6.381  15.451   2.524  1.00 39.12           C  
ANISOU 3370  CG  PHE B 642     3655   5810   5401    476    408    123       C  
ATOM   3371  CD1 PHE B 642       6.287  14.132   2.109  1.00 35.13           C  
ANISOU 3371  CD1 PHE B 642     3263   5375   4710    532    422    192       C  
ATOM   3372  CD2 PHE B 642       7.350  16.262   1.954  1.00 38.82           C  
ANISOU 3372  CD2 PHE B 642     3518   5784   5447    493    399    207       C  
ATOM   3373  CE1 PHE B 642       7.142  13.629   1.146  1.00 41.15           C  
ANISOU 3373  CE1 PHE B 642     4044   6225   5367    611    429    334       C  
ATOM   3374  CE2 PHE B 642       8.209  15.766   0.990  1.00 43.05           C  
ANISOU 3374  CE2 PHE B 642     4069   6416   5874    563    407    352       C  
ATOM   3375  CZ  PHE B 642       8.104  14.446   0.584  1.00 45.77           C  
ANISOU 3375  CZ  PHE B 642     4529   6835   6027    625    423    413       C  
ATOM   3376  N   GLY B 643       7.303  17.408   5.703  1.00 33.52           N  
ANISOU 3376  N   GLY B 643     2719   5089   4928    426    355   -241       N  
ATOM   3377  CA  GLY B 643       8.559  18.024   6.085  1.00 31.16           C  
ANISOU 3377  CA  GLY B 643     2314   4856   4670    462    334   -256       C  
ATOM   3378  C   GLY B 643       9.195  17.292   7.250  1.00 44.99           C  
ANISOU 3378  C   GLY B 643     4086   6746   6261    527    321   -342       C  
ATOM   3379  O   GLY B 643      10.413  17.116   7.296  1.00 51.05           O  
ANISOU 3379  O   GLY B 643     4818   7639   6941    605    310   -297       O  
ATOM   3380  N   ILE B 644       8.365  16.860   8.194  1.00 51.63           N  
ANISOU 3380  N   ILE B 644     4982   7576   7059    499    323   -462       N  
ATOM   3381  CA  ILE B 644       8.847  16.128   9.360  1.00 42.75           C  
ANISOU 3381  CA  ILE B 644     3880   6582   5781    562    310   -543       C  
ATOM   3382  C   ILE B 644       9.360  14.745   8.965  1.00 35.20           C  
ANISOU 3382  C   ILE B 644     3032   5746   4598    674    318   -423       C  
ATOM   3383  O   ILE B 644      10.376  14.281   9.482  1.00 30.80           O  
ANISOU 3383  O   ILE B 644     2468   5326   3910    774    305   -419       O  
ATOM   3384  CB  ILE B 644       7.753  15.987  10.440  1.00 52.51           C  
ANISOU 3384  CB  ILE B 644     5146   7778   7027    498    311   -695       C  
ATOM   3385  CG1 ILE B 644       7.322  17.364  10.953  1.00 45.72           C  
ANISOU 3385  CG1 ILE B 644     4175   6810   6387    407    303   -833       C  
ATOM   3386  CG2 ILE B 644       8.253  15.132  11.592  1.00 56.38           C  
ANISOU 3386  CG2 ILE B 644     5665   8411   7345    573    297   -758       C  
ATOM   3387  CD1 ILE B 644       8.398  18.096  11.734  1.00 46.07           C  
ANISOU 3387  CD1 ILE B 644     4098   6922   6485    433    278   -914       C  
ATOM   3388  N   VAL B 645       8.653  14.093   8.047  1.00 41.84           N  
ANISOU 3388  N   VAL B 645     3972   6534   5392    666    340   -326       N  
ATOM   3389  CA  VAL B 645       9.078  12.792   7.541  1.00 38.44           C  
ANISOU 3389  CA  VAL B 645     3648   6195   4761    778    352   -206       C  
ATOM   3390  C   VAL B 645      10.449  12.908   6.877  1.00 46.84           C  
ANISOU 3390  C   VAL B 645     4663   7360   5774    870    347    -97       C  
ATOM   3391  O   VAL B 645      11.319  12.060   7.079  1.00 57.49           O  
ANISOU 3391  O   VAL B 645     6056   8839   6949   1001    344    -54       O  
ATOM   3392  CB  VAL B 645       8.057  12.201   6.548  1.00 30.66           C  
ANISOU 3392  CB  VAL B 645     2763   5127   3761    742    377   -123       C  
ATOM   3393  CG1 VAL B 645       8.579  10.904   5.955  1.00 31.76           C  
ANISOU 3393  CG1 VAL B 645     3009   5352   3707    871    389      3       C  
ATOM   3394  CG2 VAL B 645       6.719  11.972   7.234  1.00 16.74           C  
ANISOU 3394  CG2 VAL B 645     1048   3286   2026    655    383   -231       C  
ATOM   3395  N   LEU B 646      10.635  13.962   6.087  1.00 38.58           N  
ANISOU 3395  N   LEU B 646     3524   6254   4879    809    348    -51       N  
ATOM   3396  CA  LEU B 646      11.940  14.259   5.504  1.00 34.29           C  
ANISOU 3396  CA  LEU B 646     2908   5809   4313    877    342     42       C  
ATOM   3397  C   LEU B 646      12.993  14.340   6.603  1.00 39.23           C  
ANISOU 3397  C   LEU B 646     3465   6565   4874    948    318    -40       C  
ATOM   3398  O   LEU B 646      14.059  13.731   6.505  1.00 39.11           O  
ANISOU 3398  O   LEU B 646     3460   6700   4700   1071    317     24       O  
ATOM   3399  CB  LEU B 646      11.903  15.578   4.728  1.00 30.41           C  
ANISOU 3399  CB  LEU B 646     2306   5215   4034    784    341     81       C  
ATOM   3400  CG  LEU B 646      11.132  15.611   3.407  1.00 32.55           C  
ANISOU 3400  CG  LEU B 646     2620   5385   4363    733    363    196       C  
ATOM   3401  CD1 LEU B 646      11.158  17.006   2.798  1.00 34.77           C  
ANISOU 3401  CD1 LEU B 646     2781   5563   4868    653    355    233       C  
ATOM   3402  CD2 LEU B 646      11.696  14.591   2.432  1.00 21.30           C  
ANISOU 3402  CD2 LEU B 646     1268   4070   2757    830    381    341       C  
ATOM   3403  N   TYR B 647      12.679  15.098   7.649  1.00 47.89           N  
ANISOU 3403  N   TYR B 647     4492   7611   6093    874    301   -186       N  
ATOM   3404  CA  TYR B 647      13.568  15.261   8.792  1.00 38.90           C  
ANISOU 3404  CA  TYR B 647     3278   6594   4909    928    276   -285       C  
ATOM   3405  C   TYR B 647      13.960  13.914   9.396  1.00 45.64           C  
ANISOU 3405  C   TYR B 647     4230   7591   5520   1065    274   -277       C  
ATOM   3406  O   TYR B 647      15.086  13.738   9.862  1.00 49.35           O  
ANISOU 3406  O   TYR B 647     4655   8216   5879   1169    259   -281       O  
ATOM   3407  CB  TYR B 647      12.906  16.142   9.855  1.00 38.47           C  
ANISOU 3407  CB  TYR B 647     3154   6448   5015    822    262   -456       C  
ATOM   3408  CG  TYR B 647      13.766  16.385  11.074  1.00 52.04           C  
ANISOU 3408  CG  TYR B 647     4783   8293   6697    866    236   -572       C  
ATOM   3409  CD1 TYR B 647      14.635  17.466  11.129  1.00 60.99           C  
ANISOU 3409  CD1 TYR B 647     5770   9454   7949    845    218   -601       C  
ATOM   3410  CD2 TYR B 647      13.709  15.532  12.169  1.00 46.94           C  
ANISOU 3410  CD2 TYR B 647     4194   7743   5896    930    228   -649       C  
ATOM   3411  CE1 TYR B 647      15.426  17.691  12.240  1.00 62.52           C  
ANISOU 3411  CE1 TYR B 647     5875   9776   8106    882    195   -711       C  
ATOM   3412  CE2 TYR B 647      14.496  15.749  13.284  1.00 57.00           C  
ANISOU 3412  CE2 TYR B 647     5382   9146   7129    974    204   -754       C  
ATOM   3413  CZ  TYR B 647      15.352  16.830  13.314  1.00 59.76           C  
ANISOU 3413  CZ  TYR B 647     5583   9528   7595    948    188   -789       C  
ATOM   3414  OH  TYR B 647      16.136  17.051  14.422  1.00 63.57           O  
ANISOU 3414  OH  TYR B 647     5971  10150   8032    989    164   -899       O  
ATOM   3415  N   GLU B 648      13.026  12.968   9.387  1.00 40.26           N  
ANISOU 3415  N   GLU B 648     3682   6857   4758   1071    290   -262       N  
ATOM   3416  CA  GLU B 648      13.279  11.638   9.930  1.00 40.15           C  
ANISOU 3416  CA  GLU B 648     3780   6950   4527   1210    290   -241       C  
ATOM   3417  C   GLU B 648      14.263  10.859   9.066  1.00 45.48           C  
ANISOU 3417  C   GLU B 648     4508   7735   5037   1361    300    -94       C  
ATOM   3418  O   GLU B 648      15.015  10.025   9.568  1.00 45.88           O  
ANISOU 3418  O   GLU B 648     4608   7915   4909   1516    292    -76       O  
ATOM   3419  CB  GLU B 648      11.977  10.844  10.042  1.00 45.26           C  
ANISOU 3419  CB  GLU B 648     4554   7493   5150   1170    307   -252       C  
ATOM   3420  CG  GLU B 648      10.950  11.432  10.987  1.00 54.82           C  
ANISOU 3420  CG  GLU B 648     5723   8615   6490   1035    300   -404       C  
ATOM   3421  CD  GLU B 648       9.744  10.528  11.157  1.00 56.34           C  
ANISOU 3421  CD  GLU B 648     6040   8732   6635   1006    320   -410       C  
ATOM   3422  OE1 GLU B 648       9.913   9.394  11.653  1.00 60.27           O  
ANISOU 3422  OE1 GLU B 648     6636   9289   6973   1120    325   -382       O  
ATOM   3423  OE2 GLU B 648       8.629  10.952  10.792  1.00 47.99           O  
ANISOU 3423  OE2 GLU B 648     4982   7550   5703    875    333   -441       O  
ATOM   3424  N   LEU B 649      14.243  11.128   7.765  1.00 49.75           N  
ANISOU 3424  N   LEU B 649     5042   8227   5636   1323    318     12       N  
ATOM   3425  CA  LEU B 649      15.082  10.410   6.814  1.00 50.01           C  
ANISOU 3425  CA  LEU B 649     5124   8360   5517   1457    332    152       C  
ATOM   3426  C   LEU B 649      16.499  10.970   6.782  1.00 50.55           C  
ANISOU 3426  C   LEU B 649     5068   8578   5559   1521    319    170       C  
ATOM   3427  O   LEU B 649      17.476  10.220   6.778  1.00 53.22           O  
ANISOU 3427  O   LEU B 649     5440   9068   5711   1686    319    225       O  
ATOM   3428  CB  LEU B 649      14.470  10.472   5.413  1.00 43.23           C  
ANISOU 3428  CB  LEU B 649     4299   7399   4726   1386    358    258       C  
ATOM   3429  CG  LEU B 649      13.095   9.834   5.217  1.00 28.73           C  
ANISOU 3429  CG  LEU B 649     2586   5429   2903   1329    374    259       C  
ATOM   3430  CD1 LEU B 649      12.499  10.243   3.881  1.00 25.07           C  
ANISOU 3430  CD1 LEU B 649     2112   4869   2546   1232    394    345       C  
ATOM   3431  CD2 LEU B 649      13.179   8.322   5.329  1.00 23.16           C  
ANISOU 3431  CD2 LEU B 649     2034   4772   1993   1487    381    311       C  
ATOM   3432  N   MET B 650      16.603  12.295   6.761  1.00 46.60           N  
ANISOU 3432  N   MET B 650     4424   8032   5250   1398    307    124       N  
ATOM   3433  CA  MET B 650      17.892  12.962   6.620  1.00 52.04           C  
ANISOU 3433  CA  MET B 650     4976   8850   5945   1434    293    147       C  
ATOM   3434  C   MET B 650      18.684  13.013   7.929  1.00 65.79           C  
ANISOU 3434  C   MET B 650     6651  10730   7615   1506    265     38       C  
ATOM   3435  O   MET B 650      19.883  13.290   7.920  1.00 64.73           O  
ANISOU 3435  O   MET B 650     6416  10748   7428   1574    253     58       O  
ATOM   3436  CB  MET B 650      17.704  14.377   6.067  1.00 40.15           C  
ANISOU 3436  CB  MET B 650     3344   7228   4684   1280    288    149       C  
ATOM   3437  CG  MET B 650      16.887  14.454   4.782  1.00 38.19           C  
ANISOU 3437  CG  MET B 650     3146   6843   4522   1203    314    255       C  
ATOM   3438  SD  MET B 650      17.670  13.693   3.342  1.00 63.82           S  
ANISOU 3438  SD  MET B 650     6433  10212   7603   1316    340    441       S  
ATOM   3439  CE  MET B 650      16.828  12.113   3.279  1.00 64.14           C  
ANISOU 3439  CE  MET B 650     6680  10229   7461   1400    365    465       C  
ATOM   3440  N   THR B 651      18.014  12.752   9.048  1.00 80.29           N  
ANISOU 3440  N   THR B 651     8536  12523   9446   1490    254    -76       N  
ATOM   3441  CA  THR B 651      18.685  12.727  10.346  1.00 73.98           C  
ANISOU 3441  CA  THR B 651     7680  11861   8568   1561    228   -182       C  
ATOM   3442  C   THR B 651      18.612  11.345  10.984  1.00 71.25           C  
ANISOU 3442  C   THR B 651     7477  11588   8005   1713    229   -175       C  
ATOM   3443  O   THR B 651      19.555  10.902  11.639  1.00 71.48           O  
ANISOU 3443  O   THR B 651     7491  11789   7877   1857    213   -188       O  
ATOM   3444  CB  THR B 651      18.086  13.758  11.329  1.00 53.37           C  
ANISOU 3444  CB  THR B 651     4976   9158   6146   1415    209   -344       C  
ATOM   3445  OG1 THR B 651      16.790  13.323  11.760  1.00 39.53           O  
ANISOU 3445  OG1 THR B 651     3329   7277   4415   1357    218   -400       O  
ATOM   3446  CG2 THR B 651      17.972  15.123  10.673  1.00 56.00           C  
ANISOU 3446  CG2 THR B 651     5188   9372   6716   1269    209   -346       C  
ATOM   3447  N   GLY B 652      17.486  10.668  10.787  1.00 64.65           N  
ANISOU 3447  N   GLY B 652     6780  10620   7165   1684    247   -151       N  
ATOM   3448  CA  GLY B 652      17.268   9.368  11.391  1.00 60.71           C  
ANISOU 3448  CA  GLY B 652     6427  10151   6490   1818    248   -139       C  
ATOM   3449  C   GLY B 652      16.580   9.492  12.736  1.00 67.08           C  
ANISOU 3449  C   GLY B 652     7223  10919   7345   1753    233   -280       C  
ATOM   3450  O   GLY B 652      16.112   8.503  13.299  1.00 69.24           O  
ANISOU 3450  O   GLY B 652     7620  11173   7516   1827    237   -279       O  
ATOM   3451  N   GLN B 653      16.514  10.716  13.250  1.00 72.43           N  
ANISOU 3451  N   GLN B 653     7753  11579   8186   1615    217   -401       N  
ATOM   3452  CA  GLN B 653      15.922  10.968  14.560  1.00 72.92           C  
ANISOU 3452  CA  GLN B 653     7782  11622   8301   1545    203   -552       C  
ATOM   3453  C   GLN B 653      14.552  11.632  14.460  1.00 72.73           C  
ANISOU 3453  C   GLN B 653     7750  11408   8474   1351    214   -625       C  
ATOM   3454  O   GLN B 653      14.222  12.257  13.451  1.00 76.28           O  
ANISOU 3454  O   GLN B 653     8176  11748   9060   1255    227   -579       O  
ATOM   3455  CB  GLN B 653      16.849  11.840  15.412  1.00 65.73           C  
ANISOU 3455  CB  GLN B 653     6708  10842   7423   1545    175   -662       C  
ATOM   3456  CG  GLN B 653      18.192  11.206  15.739  1.00 67.01           C  
ANISOU 3456  CG  GLN B 653     6863  11219   7377   1742    160   -614       C  
ATOM   3457  CD  GLN B 653      18.989  12.021  16.740  1.00 81.60           C  
ANISOU 3457  CD  GLN B 653     8547  13206   9253   1732    133   -741       C  
ATOM   3458  OE1 GLN B 653      19.994  11.556  17.278  1.00 93.73           O  
ANISOU 3458  OE1 GLN B 653    10061  14933  10619   1886    118   -733       O  
ATOM   3459  NE2 GLN B 653      18.538  13.243  17.000  1.00 85.51           N  
ANISOU 3459  NE2 GLN B 653     8924  13606   9961   1557    126   -862       N  
ATOM   3460  N   LEU B 654      13.762  11.486  15.519  1.00 61.56           N  
ANISOU 3460  N   LEU B 654     6354   9964   7070   1301    210   -738       N  
ATOM   3461  CA  LEU B 654      12.486  12.178  15.635  1.00 52.83           C  
ANISOU 3461  CA  LEU B 654     5224   8704   6144   1123    219   -836       C  
ATOM   3462  C   LEU B 654      12.727  13.607  16.102  1.00 57.13           C  
ANISOU 3462  C   LEU B 654     5604   9238   6864   1022    200   -971       C  
ATOM   3463  O   LEU B 654      13.728  13.887  16.765  1.00 58.82           O  
ANISOU 3463  O   LEU B 654     5726   9585   7036   1083    179  -1024       O  
ATOM   3464  CB  LEU B 654      11.566  11.450  16.618  1.00 45.10           C  
ANISOU 3464  CB  LEU B 654     4323   7712   5102   1108    226   -908       C  
ATOM   3465  CG  LEU B 654      10.957  10.131  16.140  1.00 46.44           C  
ANISOU 3465  CG  LEU B 654     4665   7827   5152   1169    254   -788       C  
ATOM   3466  CD1 LEU B 654      10.328   9.365  17.297  1.00 51.23           C  
ANISOU 3466  CD1 LEU B 654     5340   8448   5677   1180    266   -854       C  
ATOM   3467  CD2 LEU B 654       9.936  10.377  15.040  1.00 32.10           C  
ANISOU 3467  CD2 LEU B 654     2885   5853   3458   1046    277   -742       C  
ATOM   3468  N   PRO B 655      11.810  14.521  15.755  1.00 48.76           N  
ANISOU 3468  N   PRO B 655     4506   8017   6004    874    210  -1027       N  
ATOM   3469  CA  PRO B 655      11.967  15.929  16.128  1.00 51.55           C  
ANISOU 3469  CA  PRO B 655     4711   8326   6550    783    197  -1153       C  
ATOM   3470  C   PRO B 655      11.941  16.101  17.639  1.00 71.33           C  
ANISOU 3470  C   PRO B 655     7151  10913   9040    770    179  -1328       C  
ATOM   3471  O   PRO B 655      11.331  15.292  18.338  1.00 74.08           O  
ANISOU 3471  O   PRO B 655     7573  11294   9279    782    182  -1366       O  
ATOM   3472  CB  PRO B 655      10.731  16.596  15.512  1.00 28.68           C  
ANISOU 3472  CB  PRO B 655     1827   5229   3843    651    216  -1171       C  
ATOM   3473  CG  PRO B 655      10.248  15.643  14.468  1.00 33.02           C  
ANISOU 3473  CG  PRO B 655     2512   5735   4299    678    238  -1017       C  
ATOM   3474  CD  PRO B 655      10.569  14.285  15.001  1.00 28.43           C  
ANISOU 3474  CD  PRO B 655     2024   5291   3486    793    235   -978       C  
ATOM   3475  N   TYR B 656      12.603  17.141  18.133  1.00 75.93           N  
ANISOU 3475  N   TYR B 656     7591  11530   9730    745    162  -1431       N  
ATOM   3476  CA  TYR B 656      12.528  17.495  19.544  1.00 60.10           C  
ANISOU 3476  CA  TYR B 656     5504   9592   7738    714    147  -1617       C  
ATOM   3477  C   TYR B 656      12.971  16.350  20.454  1.00 62.57           C  
ANISOU 3477  C   TYR B 656     5866  10094   7814    830    135  -1616       C  
ATOM   3478  O   TYR B 656      12.177  15.823  21.233  1.00 64.27           O  
ANISOU 3478  O   TYR B 656     6134  10318   7970    809    139  -1685       O  
ATOM   3479  CB  TYR B 656      11.102  17.930  19.893  1.00 42.74           C  
ANISOU 3479  CB  TYR B 656     3318   7245   5677    588    161  -1739       C  
ATOM   3480  CG  TYR B 656      10.407  18.677  18.774  1.00 44.06           C  
ANISOU 3480  CG  TYR B 656     3493   7210   6037    502    180  -1688       C  
ATOM   3481  CD1 TYR B 656      10.969  19.821  18.224  1.00 43.29           C  
ANISOU 3481  CD1 TYR B 656     3291   7042   6117    475    176  -1680       C  
ATOM   3482  CD2 TYR B 656       9.189  18.238  18.268  1.00 47.28           C  
ANISOU 3482  CD2 TYR B 656     4009   7503   6451    450    202  -1645       C  
ATOM   3483  CE1 TYR B 656      10.340  20.506  17.201  1.00 44.64           C  
ANISOU 3483  CE1 TYR B 656     3466   7029   6466    408    192  -1622       C  
ATOM   3484  CE2 TYR B 656       8.552  18.916  17.246  1.00 37.14           C  
ANISOU 3484  CE2 TYR B 656     2729   6046   5337    383    219  -1596       C  
ATOM   3485  CZ  TYR B 656       9.132  20.050  16.716  1.00 40.16           C  
ANISOU 3485  CZ  TYR B 656     3009   6357   5895    367    213  -1581       C  
ATOM   3486  OH  TYR B 656       8.507  20.732  15.699  1.00 38.35           O  
ANISOU 3486  OH  TYR B 656     2778   5956   5836    310    229  -1520       O  
ATOM   3487  N   SER B 657      14.241  15.969  20.351  1.00 58.23           N  
ANISOU 3487  N   SER B 657     5296   9700   7129    958    122  -1533       N  
ATOM   3488  CA  SER B 657      14.802  14.930  21.210  1.00 55.21           C  
ANISOU 3488  CA  SER B 657     4952   9506   6520   1095    110  -1524       C  
ATOM   3489  C   SER B 657      15.026  15.438  22.632  1.00 73.80           C  
ANISOU 3489  C   SER B 657     7184  11974   8882   1071     90  -1708       C  
ATOM   3490  O   SER B 657      14.947  14.671  23.592  1.00 77.75           O  
ANISOU 3490  O   SER B 657     7722  12586   9236   1137     85  -1744       O  
ATOM   3491  CB  SER B 657      16.115  14.393  20.633  1.00 49.68           C  
ANISOU 3491  CB  SER B 657     4264   8947   5666   1253    103  -1380       C  
ATOM   3492  OG  SER B 657      15.889  13.270  19.797  1.00 49.35           O  
ANISOU 3492  OG  SER B 657     4382   8866   5503   1341    121  -1215       O  
ATOM   3493  N   ASN B 658      15.305  16.732  22.757  1.00106.41           N  
ANISOU 3493  N   ASN B 658    11168  16075  13189    979     82  -1821       N  
ATOM   3494  CA  ASN B 658      15.553  17.350  24.058  1.00108.51           C  
ANISOU 3494  CA  ASN B 658    11301  16445  13481    946     66  -2010       C  
ATOM   3495  C   ASN B 658      14.278  17.624  24.854  1.00115.43           C  
ANISOU 3495  C   ASN B 658    12181  17226  14452    828     74  -2165       C  
ATOM   3496  O   ASN B 658      14.336  18.117  25.982  1.00128.47           O  
ANISOU 3496  O   ASN B 658    13727  18959  16127    792     64  -2336       O  
ATOM   3497  CB  ASN B 658      16.349  18.649  23.897  1.00 81.46           C  
ANISOU 3497  CB  ASN B 658     7713  13019  10217    893     57  -2076       C  
ATOM   3498  CG  ASN B 658      17.815  18.404  23.587  1.00 90.59           C  
ANISOU 3498  CG  ASN B 658     8820  14357  11242   1018     42  -1973       C  
ATOM   3499  OD1 ASN B 658      18.231  17.274  23.333  1.00 94.57           O  
ANISOU 3499  OD1 ASN B 658     9422  14968  11541   1154     41  -1838       O  
ATOM   3500  ND2 ASN B 658      18.607  19.470  23.610  1.00100.35           N  
ANISOU 3500  ND2 ASN B 658     9901  15632  12597    975     32  -2039       N  
ATOM   3501  N   ILE B 659      13.129  17.308  24.266  1.00 64.68           N  
ANISOU 3501  N   ILE B 659     5868  10635   8072    767     94  -2111       N  
ATOM   3502  CA  ILE B 659      11.847  17.537  24.924  1.00 57.70           C  
ANISOU 3502  CA  ILE B 659     4991   9662   7272    654    104  -2250       C  
ATOM   3503  C   ILE B 659      11.098  16.223  25.128  1.00 67.11           C  
ANISOU 3503  C   ILE B 659     6322  10878   8299    689    114  -2178       C  
ATOM   3504  O   ILE B 659      10.866  15.476  24.177  1.00 68.93           O  
ANISOU 3504  O   ILE B 659     6676  11042   8473    726    128  -2015       O  
ATOM   3505  CB  ILE B 659      10.972  18.529  24.131  1.00 72.40           C  
ANISOU 3505  CB  ILE B 659     6842  11296   9371    530    123  -2279       C  
ATOM   3506  CG1 ILE B 659      11.656  19.899  24.054  1.00 79.94           C  
ANISOU 3506  CG1 ILE B 659     7649  12211  10513    492    116  -2361       C  
ATOM   3507  CG2 ILE B 659       9.599  18.660  24.769  1.00 77.39           C  
ANISOU 3507  CG2 ILE B 659     7491  11848  10068    425    136  -2416       C  
ATOM   3508  CD1 ILE B 659      10.841  20.961  23.339  1.00 89.16           C  
ANISOU 3508  CD1 ILE B 659     8795  13151  11930    388    135  -2391       C  
ATOM   3509  N   ASN B 660      10.729  15.947  26.376  1.00 91.34           N  
ANISOU 3509  N   ASN B 660     9365  14044  11294    675    108  -2299       N  
ATOM   3510  CA  ASN B 660      10.065  14.698  26.733  1.00 92.61           C  
ANISOU 3510  CA  ASN B 660     9646  14241  11302    709    122  -2233       C  
ATOM   3511  C   ASN B 660       8.664  14.946  27.275  1.00 80.19           C  
ANISOU 3511  C   ASN B 660     8066  12586   9817    566    135  -2365       C  
ATOM   3512  O   ASN B 660       8.005  14.031  27.773  1.00 73.95           O  
ANISOU 3512  O   ASN B 660     7350  11830   8918    568    151  -2340       O  
ATOM   3513  CB  ASN B 660      10.894  13.932  27.765  1.00110.90           C  
ANISOU 3513  CB  ASN B 660    11952  16767  13418    842    109  -2230       C  
ATOM   3514  CG  ASN B 660      12.323  13.706  27.312  1.00115.63           C  
ANISOU 3514  CG  ASN B 660    12546  17472  13915    994     94  -2114       C  
ATOM   3515  OD1 ASN B 660      12.989  14.623  26.831  1.00117.38           O  
ANISOU 3515  OD1 ASN B 660    12673  17681  14243    973     81  -2137       O  
ATOM   3516  ND2 ASN B 660      12.804  12.478  27.466  1.00113.48           N  
ANISOU 3516  ND2 ASN B 660    12377  17302  13437   1154    101  -1986       N  
ATOM   3517  N   ASN B 661       8.219  16.195  27.177  1.00 70.72           N  
ANISOU 3517  N   ASN B 661     6777  11275   8817    449    135  -2501       N  
ATOM   3518  CA  ASN B 661       6.893  16.584  27.636  1.00 81.43           C  
ANISOU 3518  CA  ASN B 661     8115  12551  10271    317    148  -2642       C  
ATOM   3519  C   ASN B 661       6.000  17.034  26.484  1.00 87.26           C  
ANISOU 3519  C   ASN B 661     8909  13083  11163    235    169  -2599       C  
ATOM   3520  O   ASN B 661       6.361  17.927  25.716  1.00 90.17           O  
ANISOU 3520  O   ASN B 661     9238  13343  11679    229    172  -2586       O  
ATOM   3521  CB  ASN B 661       6.994  17.691  28.684  1.00 93.22           C  
ANISOU 3521  CB  ASN B 661     9458  14092  11870    260    137  -2872       C  
ATOM   3522  CG  ASN B 661       5.640  18.118  29.210  1.00 98.65           C  
ANISOU 3522  CG  ASN B 661    10122  14710  12650    135    152  -3032       C  
ATOM   3523  OD1 ASN B 661       5.091  17.498  30.120  1.00 99.01           O  
ANISOU 3523  OD1 ASN B 661    10172  14861  12587    108    150  -3087       O  
ATOM   3524  ND2 ASN B 661       5.094  19.185  28.639  1.00104.41           N  
ANISOU 3524  ND2 ASN B 661    10823  15264  13584     65    169  -3103       N  
ATOM   3525  N   ARG B 662       4.834  16.404  26.379  1.00 91.61           N  
ANISOU 3525  N   ARG B 662     9544  13586  11679    172    188  -2570       N  
ATOM   3526  CA  ARG B 662       3.863  16.701  25.332  1.00 91.94           C  
ANISOU 3526  CA  ARG B 662     9643  13449  11839     97    211  -2528       C  
ATOM   3527  C   ARG B 662       3.451  18.169  25.317  1.00 81.79           C  
ANISOU 3527  C   ARG B 662     8263  12039  10775     23    219  -2687       C  
ATOM   3528  O   ARG B 662       3.369  18.793  24.257  1.00 82.51           O  
ANISOU 3528  O   ARG B 662     8365  11981  11004     15    232  -2626       O  
ATOM   3529  CB  ARG B 662       2.615  15.842  25.529  1.00110.12           C  
ANISOU 3529  CB  ARG B 662    12022  15755  14063     26    231  -2514       C  
ATOM   3530  CG  ARG B 662       2.848  14.347  25.438  1.00122.89           C  
ANISOU 3530  CG  ARG B 662    13750  17454  15487    103    244  -2336       C  
ATOM   3531  CD  ARG B 662       1.556  13.605  25.718  1.00139.52           C  
ANISOU 3531  CD  ARG B 662    15914  19555  17542     15    278  -2333       C  
ATOM   3532  NE  ARG B 662       1.710  12.156  25.669  1.00156.45           N  
ANISOU 3532  NE  ARG B 662    18190  21743  19512     96    314  -2163       N  
ATOM   3533  CZ  ARG B 662       0.737  11.301  25.965  1.00168.94           C  
ANISOU 3533  CZ  ARG B 662    19849  23320  21019     38    364  -2132       C  
ATOM   3534  NH1 ARG B 662      -0.452  11.758  26.332  1.00170.13           N  
ANISOU 3534  NH1 ARG B 662    19932  23457  21253   -106    374  -2259       N  
ATOM   3535  NH2 ARG B 662       0.949   9.994  25.898  1.00175.19           N  
ANISOU 3535  NH2 ARG B 662    20801  24114  21649    126    411  -1980       N  
ATOM   3536  N   ASP B 663       3.185  18.710  26.501  1.00 77.60           N  
ANISOU 3536  N   ASP B 663     7637  11568  10280    -23    214  -2888       N  
ATOM   3537  CA  ASP B 663       2.637  20.058  26.635  1.00 79.33           C  
ANISOU 3537  CA  ASP B 663     7765  11666  10710    -85    229  -3059       C  
ATOM   3538  C   ASP B 663       3.616  21.161  26.229  1.00 66.45           C  
ANISOU 3538  C   ASP B 663     6043   9959   9245    -43    224  -3066       C  
ATOM   3539  O   ASP B 663       3.198  22.237  25.799  1.00 57.56           O  
ANISOU 3539  O   ASP B 663     4866   8678   8327    -76    241  -3124       O  
ATOM   3540  CB  ASP B 663       2.131  20.290  28.062  1.00 96.65           C  
ANISOU 3540  CB  ASP B 663     9877  13960  12885   -138    228  -3278       C  
ATOM   3541  CG  ASP B 663       0.932  19.423  28.402  1.00102.11           C  
ANISOU 3541  CG  ASP B 663    10637  14700  13460   -209    237  -3287       C  
ATOM   3542  OD1 ASP B 663      -0.135  19.612  27.779  1.00 98.38           O  
ANISOU 3542  OD1 ASP B 663    10212  14103  13064   -265    263  -3284       O  
ATOM   3543  OD2 ASP B 663       1.055  18.557  29.294  1.00104.75           O  
ANISOU 3543  OD2 ASP B 663    10969  15204  13629   -208    219  -3290       O  
ATOM   3544  N   GLN B 664       4.912  20.901  26.376  1.00 68.40           N  
ANISOU 3544  N   GLN B 664     6261  10324   9404     32    200  -3003       N  
ATOM   3545  CA  GLN B 664       5.920  21.837  25.893  1.00 75.66           C  
ANISOU 3545  CA  GLN B 664     7094  11187  10465     67    193  -2982       C  
ATOM   3546  C   GLN B 664       5.736  21.999  24.392  1.00 74.00           C  
ANISOU 3546  C   GLN B 664     6951  10809  10356     68    206  -2812       C  
ATOM   3547  O   GLN B 664       5.328  23.054  23.912  1.00 68.20           O  
ANISOU 3547  O   GLN B 664     6165   9912   9837     28    220  -2851       O  
ATOM   3548  CB  GLN B 664       7.334  21.323  26.173  1.00 96.31           C  
ANISOU 3548  CB  GLN B 664     9684  13980  12929    156    166  -2913       C  
ATOM   3549  CG  GLN B 664       7.668  21.082  27.636  1.00110.06           C  
ANISOU 3549  CG  GLN B 664    11355  15915  14547    171    150  -3060       C  
ATOM   3550  CD  GLN B 664       9.140  20.761  27.842  1.00120.59           C  
ANISOU 3550  CD  GLN B 664    12644  17422  15754    270    126  -2996       C  
ATOM   3551  OE1 GLN B 664      10.015  21.438  27.299  1.00121.15           O  
ANISOU 3551  OE1 GLN B 664    12647  17462  15922    293    120  -2957       O  
ATOM   3552  NE2 GLN B 664       9.419  19.726  28.627  1.00125.09           N  
ANISOU 3552  NE2 GLN B 664    13244  18179  16104    332    111  -2980       N  
ATOM   3553  N   ILE B 665       6.039  20.929  23.664  1.00 93.59           N  
ANISOU 3553  N   ILE B 665     9544  13335  12681    121    202  -2620       N  
ATOM   3554  CA  ILE B 665       5.890  20.886  22.215  1.00 91.25           C  
ANISOU 3554  CA  ILE B 665     9322  12906  12442    127    215  -2443       C  
ATOM   3555  C   ILE B 665       4.617  21.583  21.748  1.00 92.13           C  
ANISOU 3555  C   ILE B 665     9441  12836  12729     50    240  -2491       C  
ATOM   3556  O   ILE B 665       4.663  22.475  20.906  1.00 99.63           O  
ANISOU 3556  O   ILE B 665    10349  13646  13861     41    247  -2445       O  
ATOM   3557  CB  ILE B 665       5.879  19.432  21.709  1.00 67.47           C  
ANISOU 3557  CB  ILE B 665     6452   9968   9215    177    217  -2269       C  
ATOM   3558  CG1 ILE B 665       7.182  18.728  22.096  1.00 47.57           C  
ANISOU 3558  CG1 ILE B 665     3926   7629   6520    280    193  -2205       C  
ATOM   3559  CG2 ILE B 665       5.670  19.389  20.204  1.00 78.02           C  
ANISOU 3559  CG2 ILE B 665     7862  11174  10607    178    233  -2095       C  
ATOM   3560  CD1 ILE B 665       7.227  17.270  21.699  1.00 47.21           C  
ANISOU 3560  CD1 ILE B 665     4016   7658   6265    350    196  -2039       C  
ATOM   3561  N   ILE B 666       3.480  21.169  22.299  1.00 74.49           N  
ANISOU 3561  N   ILE B 666     7253  10613  10438     -3    254  -2580       N  
ATOM   3562  CA  ILE B 666       2.200  21.780  21.959  1.00 66.71           C  
ANISOU 3562  CA  ILE B 666     6271   9479   9598    -69    280  -2640       C  
ATOM   3563  C   ILE B 666       2.239  23.293  22.156  1.00 64.53           C  
ANISOU 3563  C   ILE B 666     5859   9090   9570    -86    282  -2773       C  
ATOM   3564  O   ILE B 666       1.863  24.057  21.266  1.00 60.59           O  
ANISOU 3564  O   ILE B 666     5341   8433   9248    -96    294  -2724       O  
ATOM   3565  CB  ILE B 666       1.050  21.180  22.792  1.00 51.03           C  
ANISOU 3565  CB  ILE B 666     4328   7557   7504   -128    293  -2754       C  
ATOM   3566  CG1 ILE B 666       0.853  19.702  22.439  1.00 40.16           C  
ANISOU 3566  CG1 ILE B 666     3086   6262   5912   -122    293  -2604       C  
ATOM   3567  CG2 ILE B 666      -0.236  21.967  22.580  1.00 30.70           C  
ANISOU 3567  CG2 ILE B 666     1731   4845   5088   -185    321  -2848       C  
ATOM   3568  CD1 ILE B 666      -0.331  19.059  23.123  1.00 42.77           C  
ANISOU 3568  CD1 ILE B 666     3458   6653   6139   -195    305  -2690       C  
ATOM   3569  N   GLU B 667       2.697  23.720  23.328  1.00 70.54           N  
ANISOU 3569  N   GLU B 667     6518   9938  10347    -86    269  -2940       N  
ATOM   3570  CA  GLU B 667       2.814  25.140  23.634  1.00 77.62           C  
ANISOU 3570  CA  GLU B 667     7273  10740  11481   -100    270  -3081       C  
ATOM   3571  C   GLU B 667       3.863  25.789  22.745  1.00 66.76           C  
ANISOU 3571  C   GLU B 667     5844   9287  10236    -65    256  -2958       C  
ATOM   3572  O   GLU B 667       3.647  26.865  22.194  1.00 58.06           O  
ANISOU 3572  O   GLU B 667     4673   8025   9363    -80    261  -2963       O  
ATOM   3573  CB  GLU B 667       3.197  25.340  25.101  1.00107.44           C  
ANISOU 3573  CB  GLU B 667    10951  14652  15218   -106    259  -3282       C  
ATOM   3574  CG  GLU B 667       3.220  26.794  25.544  1.00120.97           C  
ANISOU 3574  CG  GLU B 667    12510  16274  17180   -127    262  -3455       C  
ATOM   3575  CD  GLU B 667       1.831  27.400  25.613  1.00132.31           C  
ANISOU 3575  CD  GLU B 667    13928  17585  18758   -170    287  -3573       C  
ATOM   3576  OE1 GLU B 667       1.727  28.642  25.698  1.00135.20           O  
ANISOU 3576  OE1 GLU B 667    14173  17834  19361   -181    290  -3684       O  
ATOM   3577  OE2 GLU B 667       0.844  26.635  25.584  1.00135.89           O  
ANISOU 3577  OE2 GLU B 667    14482  18063  19087   -193    303  -3556       O  
ATOM   3578  N   MET B 668       4.998  25.114  22.607  1.00 75.40           N  
ANISOU 3578  N   MET B 668     6965  10503  11179    -15    237  -2843       N  
ATOM   3579  CA  MET B 668       6.146  25.659  21.894  1.00 82.40           C  
ANISOU 3579  CA  MET B 668     7789  11360  12159     19    222  -2734       C  
ATOM   3580  C   MET B 668       5.959  25.695  20.378  1.00 83.29           C  
ANISOU 3580  C   MET B 668     7968  11335  12344     25    230  -2534       C  
ATOM   3581  O   MET B 668       6.145  26.738  19.754  1.00 90.53           O  
ANISOU 3581  O   MET B 668     8804  12121  13473     13    229  -2504       O  
ATOM   3582  CB  MET B 668       7.418  24.886  22.259  1.00 88.44           C  
ANISOU 3582  CB  MET B 668     8558  12324  12722     80    200  -2679       C  
ATOM   3583  CG  MET B 668       7.713  24.865  23.752  1.00 90.44           C  
ANISOU 3583  CG  MET B 668     8734  12732  12896     79    188  -2869       C  
ATOM   3584  SD  MET B 668       9.467  24.709  24.145  1.00202.48           S  
ANISOU 3584  SD  MET B 668    22841  27125  26968    150    160  -2841       S  
ATOM   3585  CE  MET B 668      10.070  26.332  23.683  1.00102.01           C  
ANISOU 3585  CE  MET B 668     9958  14265  14535    115    156  -2876       C  
ATOM   3586  N   VAL B 669       5.594  24.560  19.788  1.00 74.02           N  
ANISOU 3586  N   VAL B 669     6933  10194  10996     43    239  -2396       N  
ATOM   3587  CA  VAL B 669       5.406  24.480  18.341  1.00 71.76           C  
ANISOU 3587  CA  VAL B 669     6714   9798  10752     50    249  -2202       C  
ATOM   3588  C   VAL B 669       4.249  25.359  17.872  1.00 73.98           C  
ANISOU 3588  C   VAL B 669     6973   9893  11244      1    268  -2237       C  
ATOM   3589  O   VAL B 669       4.362  26.062  16.867  1.00 75.32           O  
ANISOU 3589  O   VAL B 669     7107   9938  11572      1    268  -2131       O  
ATOM   3590  CB  VAL B 669       5.193  23.029  17.869  1.00 63.51           C  
ANISOU 3590  CB  VAL B 669     5822   8835   9472     78    257  -2062       C  
ATOM   3591  CG1 VAL B 669       4.890  22.990  16.378  1.00 53.40           C  
ANISOU 3591  CG1 VAL B 669     4607   7443   8242     80    271  -1877       C  
ATOM   3592  CG2 VAL B 669       6.421  22.198  18.181  1.00 60.44           C  
ANISOU 3592  CG2 VAL B 669     5450   8627   8889    148    237  -2002       C  
ATOM   3593  N   GLY B 670       3.141  25.317  18.605  1.00 66.67           N  
ANISOU 3593  N   GLY B 670     6062   8957  10315    -39    283  -2383       N  
ATOM   3594  CA  GLY B 670       2.005  26.173  18.314  1.00 60.93           C  
ANISOU 3594  CA  GLY B 670     5299   8070   9780    -77    300  -2441       C  
ATOM   3595  C   GLY B 670       2.336  27.638  18.531  1.00 67.37           C  
ANISOU 3595  C   GLY B 670     5959   8779  10859    -84    289  -2539       C  
ATOM   3596  O   GLY B 670       1.829  28.510  17.826  1.00 59.61           O  
ANISOU 3596  O   GLY B 670     4931   7640  10081    -94    295  -2505       O  
ATOM   3597  N   ARG B 671       3.194  27.907  19.511  1.00100.73           N  
ANISOU 3597  N   ARG B 671    10097  13094  15082    -77    273  -2661       N  
ATOM   3598  CA  ARG B 671       3.610  29.270  19.823  1.00100.34           C  
ANISOU 3598  CA  ARG B 671     9889  12957  15277    -88    262  -2769       C  
ATOM   3599  C   ARG B 671       4.496  29.843  18.722  1.00110.70           C  
ANISOU 3599  C   ARG B 671    11155  14186  16719    -70    248  -2600       C  
ATOM   3600  O   ARG B 671       4.448  31.039  18.431  1.00111.50           O  
ANISOU 3600  O   ARG B 671    11147  14143  17074    -86    243  -2623       O  
ATOM   3601  CB  ARG B 671       4.355  29.303  21.160  1.00 61.64           C  
ANISOU 3601  CB  ARG B 671     4909   8201  10311    -87    249  -2940       C  
ATOM   3602  CG  ARG B 671       4.757  30.689  21.625  1.00 74.90           C  
ANISOU 3602  CG  ARG B 671     6417   9805  12239   -105    240  -3081       C  
ATOM   3603  CD  ARG B 671       5.261  30.667  23.063  1.00 90.54           C  
ANISOU 3603  CD  ARG B 671     8321  11942  14139   -110    233  -3280       C  
ATOM   3604  NE  ARG B 671       6.712  30.515  23.154  1.00104.23           N  
ANISOU 3604  NE  ARG B 671    10009  13803  15789    -85    211  -3225       N  
ATOM   3605  CZ  ARG B 671       7.570  31.530  23.109  1.00108.46           C  
ANISOU 3605  CZ  ARG B 671    10407  14300  16503    -95    198  -3253       C  
ATOM   3606  NH1 ARG B 671       7.125  32.772  22.965  1.00113.51           N  
ANISOU 3606  NH1 ARG B 671    10943  14763  17423   -128    202  -3330       N  
ATOM   3607  NH2 ARG B 671       8.874  31.306  23.204  1.00103.43           N  
ANISOU 3607  NH2 ARG B 671     9730  13805  15763    -72    179  -3202       N  
ATOM   3608  N   GLY B 672       5.301  28.980  18.109  1.00103.28           N  
ANISOU 3608  N   GLY B 672    10294  13343  15606    -37    240  -2429       N  
ATOM   3609  CA  GLY B 672       6.258  29.404  17.105  1.00 97.60           C  
ANISOU 3609  CA  GLY B 672     9530  12581  14973    -19    226  -2264       C  
ATOM   3610  C   GLY B 672       7.646  29.517  17.702  1.00 96.67           C  
ANISOU 3610  C   GLY B 672     9324  12597  14809     -1    204  -2305       C  
ATOM   3611  O   GLY B 672       8.560  30.072  17.089  1.00 98.49           O  
ANISOU 3611  O   GLY B 672     9479  12807  15135      4    190  -2208       O  
ATOM   3612  N   SER B 673       7.796  28.983  18.910  1.00 89.70           N  
ANISOU 3612  N   SER B 673     8445  11864  13772      6    202  -2449       N  
ATOM   3613  CA  SER B 673       9.063  29.028  19.627  1.00 90.93           C  
ANISOU 3613  CA  SER B 673     8513  12176  13860     26    182  -2510       C  
ATOM   3614  C   SER B 673       9.969  27.868  19.241  1.00 90.67           C  
ANISOU 3614  C   SER B 673     8564  12310  13575     87    172  -2351       C  
ATOM   3615  O   SER B 673      11.189  27.962  19.358  1.00 96.36           O  
ANISOU 3615  O   SER B 673     9209  13149  14253    114    155  -2329       O  
ATOM   3616  CB  SER B 673       8.815  28.994  21.141  1.00 85.10           C  
ANISOU 3616  CB  SER B 673     7731  11537  13067     11    183  -2741       C  
ATOM   3617  OG  SER B 673       8.256  27.742  21.528  1.00 79.88           O  
ANISOU 3617  OG  SER B 673     7201  10980  12169     31    191  -2738       O  
ATOM   3618  N   LEU B 674       9.371  26.777  18.775  1.00 81.37           N  
ANISOU 3618  N   LEU B 674     7537  11147  12232    110    185  -2242       N  
ATOM   3619  CA  LEU B 674      10.126  25.554  18.533  1.00 76.48           C  
ANISOU 3619  CA  LEU B 674     7005  10695  11358    178    177  -2108       C  
ATOM   3620  C   LEU B 674      10.011  25.032  17.104  1.00 76.80           C  
ANISOU 3620  C   LEU B 674     7149  10675  11355    202    187  -1886       C  
ATOM   3621  O   LEU B 674       8.925  25.002  16.523  1.00 83.96           O  
ANISOU 3621  O   LEU B 674     8129  11449  12323    168    206  -1846       O  
ATOM   3622  CB  LEU B 674       9.687  24.464  19.513  1.00 68.34           C  
ANISOU 3622  CB  LEU B 674     6060   9794  10113    198    179  -2190       C  
ATOM   3623  CG  LEU B 674      10.404  23.116  19.435  1.00 68.81           C  
ANISOU 3623  CG  LEU B 674     6210  10034   9899    283    171  -2067       C  
ATOM   3624  CD1 LEU B 674      11.864  23.275  19.817  1.00 59.72           C  
ANISOU 3624  CD1 LEU B 674     4957   9044   8690    339    148  -2073       C  
ATOM   3625  CD2 LEU B 674       9.721  22.093  20.329  1.00 76.92           C  
ANISOU 3625  CD2 LEU B 674     7327  11153  10747    290    174  -2139       C  
ATOM   3626  N   SER B 675      11.148  24.616  16.552  1.00 63.34           N  
ANISOU 3626  N   SER B 675     5446   9083   9539    261    176  -1747       N  
ATOM   3627  CA  SER B 675      11.196  23.992  15.234  1.00 63.00           C  
ANISOU 3627  CA  SER B 675     5499   9020   9419    295    186  -1536       C  
ATOM   3628  C   SER B 675      12.306  22.941  15.197  1.00 49.92           C  
ANISOU 3628  C   SER B 675     3883   7567   7518    389    175  -1438       C  
ATOM   3629  O   SER B 675      13.294  23.054  15.923  1.00 51.91           O  
ANISOU 3629  O   SER B 675     4048   7960   7714    425    157  -1504       O  
ATOM   3630  CB  SER B 675      11.418  25.047  14.149  1.00117.63           C  
ANISOU 3630  CB  SER B 675    12340  15804  16550    262    185  -1435       C  
ATOM   3631  OG  SER B 675      12.644  25.729  14.340  1.00128.40           O  
ANISOU 3631  OG  SER B 675    13569  17244  17973    272    164  -1451       O  
ATOM   3632  N   PRO B 676      12.144  21.910  14.352  1.00 46.03           N  
ANISOU 3632  N   PRO B 676     3517   7097   6875    436    189  -1282       N  
ATOM   3633  CA  PRO B 676      13.121  20.816  14.296  1.00 47.01           C  
ANISOU 3633  CA  PRO B 676     3692   7414   6757    543    182  -1185       C  
ATOM   3634  C   PRO B 676      14.546  21.315  14.061  1.00 47.93           C  
ANISOU 3634  C   PRO B 676     3691   7638   6883    586    164  -1135       C  
ATOM   3635  O   PRO B 676      14.749  22.285  13.330  1.00 45.34           O  
ANISOU 3635  O   PRO B 676     3281   7214   6733    537    163  -1084       O  
ATOM   3636  CB  PRO B 676      12.646  19.984  13.102  1.00 48.43           C  
ANISOU 3636  CB  PRO B 676     4004   7545   6851    567    203  -1014       C  
ATOM   3637  CG  PRO B 676      11.191  20.267  13.003  1.00 50.65           C  
ANISOU 3637  CG  PRO B 676     4334   7649   7260    475    220  -1067       C  
ATOM   3638  CD  PRO B 676      11.033  21.706  13.407  1.00 47.26           C  
ANISOU 3638  CD  PRO B 676     3774   7107   7076    396    212  -1192       C  
ATOM   3639  N   ASP B 677      15.517  20.650  14.679  1.00 60.40           N  
ANISOU 3639  N   ASP B 677     5258   9422   8270    681    150  -1145       N  
ATOM   3640  CA  ASP B 677      16.920  21.024  14.538  1.00 57.08           C  
ANISOU 3640  CA  ASP B 677     4720   9141   7826    731    133  -1104       C  
ATOM   3641  C   ASP B 677      17.458  20.604  13.176  1.00 58.15           C  
ANISOU 3641  C   ASP B 677     4900   9308   7888    788    143   -900       C  
ATOM   3642  O   ASP B 677      17.757  19.430  12.953  1.00 56.40           O  
ANISOU 3642  O   ASP B 677     4778   9205   7448    895    149   -808       O  
ATOM   3643  CB  ASP B 677      17.755  20.380  15.645  1.00 40.04           C  
ANISOU 3643  CB  ASP B 677     2538   7210   5467    828    115  -1178       C  
ATOM   3644  CG  ASP B 677      19.192  20.849  15.638  1.00 38.53           C  
ANISOU 3644  CG  ASP B 677     2205   7180   5253    872     97  -1161       C  
ATOM   3645  OD1 ASP B 677      19.490  21.844  14.944  1.00 36.61           O  
ANISOU 3645  OD1 ASP B 677     1866   6860   5185    804     94  -1120       O  
ATOM   3646  OD2 ASP B 677      20.023  20.226  16.331  1.00 53.79           O  
ANISOU 3646  OD2 ASP B 677     4120   9325   6993    977     83  -1185       O  
ATOM   3647  N   LEU B 678      17.585  21.567  12.270  1.00 45.02           N  
ANISOU 3647  N   LEU B 678     3159   7538   6407    721    144   -830       N  
ATOM   3648  CA  LEU B 678      18.037  21.278  10.914  1.00 45.96           C  
ANISOU 3648  CA  LEU B 678     3309   7680   6475    761    154   -637       C  
ATOM   3649  C   LEU B 678      19.529  20.965  10.844  1.00 43.77           C  
ANISOU 3649  C   LEU B 678     2961   7633   6035    863    141   -574       C  
ATOM   3650  O   LEU B 678      19.994  20.356   9.882  1.00 44.52           O  
ANISOU 3650  O   LEU B 678     3103   7804   6008    934    152   -421       O  
ATOM   3651  CB  LEU B 678      17.690  22.429   9.968  1.00 60.51           C  
ANISOU 3651  CB  LEU B 678     5084   9340   8567    659    157   -574       C  
ATOM   3652  CG  LEU B 678      16.219  22.536   9.568  1.00 61.71           C  
ANISOU 3652  CG  LEU B 678     5328   9275   8843    585    177   -571       C  
ATOM   3653  CD1 LEU B 678      16.018  23.651   8.557  1.00 64.34           C  
ANISOU 3653  CD1 LEU B 678     5588   9449   9410    508    177   -485       C  
ATOM   3654  CD2 LEU B 678      15.726  21.212   9.007  1.00 56.20           C  
ANISOU 3654  CD2 LEU B 678     4795   8605   7951    646    200   -469       C  
ATOM   3655  N   SER B 679      20.276  21.378  11.863  1.00 60.60           N  
ANISOU 3655  N   SER B 679     4976   9887   8161    873    119   -695       N  
ATOM   3656  CA  SER B 679      21.711  21.115  11.892  1.00 62.53           C  
ANISOU 3656  CA  SER B 679     5140  10373   8245    973    104   -649       C  
ATOM   3657  C   SER B 679      21.994  19.644  12.192  1.00 60.78           C  
ANISOU 3657  C   SER B 679     5037  10324   7733   1127    110   -612       C  
ATOM   3658  O   SER B 679      23.151  19.227  12.255  1.00 59.50           O  
ANISOU 3658  O   SER B 679     4827  10381   7399   1240    101   -571       O  
ATOM   3659  CB  SER B 679      22.415  22.018  12.911  1.00 45.07           C  
ANISOU 3659  CB  SER B 679     2759   8252   6113    934     79   -796       C  
ATOM   3660  OG  SER B 679      22.123  21.627  14.241  1.00 40.49           O  
ANISOU 3660  OG  SER B 679     2205   7729   5451    960     72   -950       O  
ATOM   3661  N   LYS B 680      20.933  18.862  12.370  1.00 50.58           N  
ANISOU 3661  N   LYS B 680     3897   8934   6387   1136    126   -624       N  
ATOM   3662  CA  LYS B 680      21.071  17.436  12.656  1.00 48.99           C  
ANISOU 3662  CA  LYS B 680     3823   8867   5925   1285    132   -585       C  
ATOM   3663  C   LYS B 680      21.024  16.566  11.400  1.00 54.09           C  
ANISOU 3663  C   LYS B 680     4590   9505   6457   1358    157   -408       C  
ATOM   3664  O   LYS B 680      21.187  15.348  11.477  1.00 50.99           O  
ANISOU 3664  O   LYS B 680     4311   9214   5847   1497    165   -355       O  
ATOM   3665  CB  LYS B 680      20.010  16.972  13.658  1.00 50.21           C  
ANISOU 3665  CB  LYS B 680     4072   8946   6062   1264    134   -700       C  
ATOM   3666  CG  LYS B 680      20.347  17.283  15.108  1.00 52.34           C  
ANISOU 3666  CG  LYS B 680     4246   9324   6317   1267    110   -867       C  
ATOM   3667  CD  LYS B 680      19.645  16.320  16.056  1.00 52.25           C  
ANISOU 3667  CD  LYS B 680     4351   9327   6175   1318    110   -933       C  
ATOM   3668  CE  LYS B 680      18.476  16.981  16.770  1.00 62.88           C  
ANISOU 3668  CE  LYS B 680     5681  10512   7698   1172    111  -1084       C  
ATOM   3669  NZ  LYS B 680      17.752  16.017  17.649  1.00 70.60           N  
ANISOU 3669  NZ  LYS B 680     6770  11509   8547   1214    112  -1138       N  
ATOM   3670  N   VAL B 681      20.798  17.190  10.247  1.00 60.87           N  
ANISOU 3670  N   VAL B 681     5424  10240   7463   1271    170   -316       N  
ATOM   3671  CA  VAL B 681      20.795  16.460   8.985  1.00 64.67           C  
ANISOU 3671  CA  VAL B 681     6003  10721   7846   1331    195   -149       C  
ATOM   3672  C   VAL B 681      22.152  15.800   8.770  1.00 67.96           C  
ANISOU 3672  C   VAL B 681     6398  11379   8044   1494    193    -68       C  
ATOM   3673  O   VAL B 681      23.153  16.221   9.350  1.00 67.52           O  
ANISOU 3673  O   VAL B 681     6215  11477   7962   1529    170   -122       O  
ATOM   3674  CB  VAL B 681      20.467  17.379   7.791  1.00 52.18           C  
ANISOU 3674  CB  VAL B 681     4371   8990   6466   1211    205    -61       C  
ATOM   3675  CG1 VAL B 681      19.040  17.893   7.891  1.00 52.53           C  
ANISOU 3675  CG1 VAL B 681     4458   8796   6705   1074    212   -127       C  
ATOM   3676  CG2 VAL B 681      21.452  18.535   7.724  1.00 45.80           C  
ANISOU 3676  CG2 VAL B 681     3378   8245   5777   1166    183    -67       C  
ATOM   3677  N   ARG B 682      22.183  14.761   7.942  1.00 62.63           N  
ANISOU 3677  N   ARG B 682     5843  10745   7209   1599    218     56       N  
ATOM   3678  CA  ARG B 682      23.422  14.040   7.673  1.00 72.46           C  
ANISOU 3678  CA  ARG B 682     7082  12219   8231   1774    221    137       C  
ATOM   3679  C   ARG B 682      24.409  14.883   6.873  1.00 80.44           C  
ANISOU 3679  C   ARG B 682     7936  13322   9304   1744    215    210       C  
ATOM   3680  O   ARG B 682      24.022  15.815   6.167  1.00 69.24           O  
ANISOU 3680  O   ARG B 682     6456  11764   8087   1601    217    246       O  
ATOM   3681  CB  ARG B 682      23.140  12.736   6.925  1.00 69.30           C  
ANISOU 3681  CB  ARG B 682     6855  11820   7654   1893    252    248       C  
ATOM   3682  CG  ARG B 682      22.440  11.666   7.744  1.00 71.73           C  
ANISOU 3682  CG  ARG B 682     7323  12089   7843   1972    255    196       C  
ATOM   3683  CD  ARG B 682      22.375  10.362   6.966  1.00 82.10           C  
ANISOU 3683  CD  ARG B 682     8801  13423   8969   2115    284    313       C  
ATOM   3684  NE  ARG B 682      21.663   9.311   7.685  1.00 92.72           N  
ANISOU 3684  NE  ARG B 682    10309  14711  10210   2193    285    279       N  
ATOM   3685  CZ  ARG B 682      21.561   8.057   7.258  1.00 98.11           C  
ANISOU 3685  CZ  ARG B 682    11158  15398  10722   2339    304    364       C  
ATOM   3686  NH1 ARG B 682      22.132   7.697   6.116  1.00 96.44           N  
ANISOU 3686  NH1 ARG B 682    10966  15258  10416   2423    329    480       N  
ATOM   3687  NH2 ARG B 682      20.893   7.161   7.972  1.00100.02           N  
ANISOU 3687  NH2 ARG B 682    11543  15570  10891   2404    298    335       N  
ATOM   3688  N   SER B 683      25.689  14.545   6.991  1.00105.07           N  
ANISOU 3688  N   SER B 683    10993  16683  12247   1886    207    236       N  
ATOM   3689  CA  SER B 683      26.734  15.189   6.208  1.00102.83           C  
ANISOU 3689  CA  SER B 683    10561  16526  11982   1878    202    316       C  
ATOM   3690  C   SER B 683      26.509  14.923   4.727  1.00105.75           C  
ANISOU 3690  C   SER B 683    10992  16838  12349   1873    234    469       C  
ATOM   3691  O   SER B 683      26.919  15.707   3.871  1.00107.13           O  
ANISOU 3691  O   SER B 683    11053  17024  12628   1797    231    547       O  
ATOM   3692  CB  SER B 683      28.106  14.659   6.622  1.00 78.30           C  
ANISOU 3692  CB  SER B 683     7392  13713   8644   2059    192    316       C  
ATOM   3693  OG  SER B 683      29.117  15.132   5.751  1.00 76.33           O  
ANISOU 3693  OG  SER B 683     7009  13607   8385   2065    190    409       O  
ATOM   3694  N   ASN B 684      25.852  13.806   4.433  1.00 96.24           N  
ANISOU 3694  N   ASN B 684     9966  15576  11024   1952    262    512       N  
ATOM   3695  CA  ASN B 684      25.598  13.405   3.057  1.00 89.86           C  
ANISOU 3695  CA  ASN B 684     9229  14724  10189   1960    296    649       C  
ATOM   3696  C   ASN B 684      24.398  14.123   2.445  1.00 90.82           C  
ANISOU 3696  C   ASN B 684     9366  14595  10546   1771    304    672       C  
ATOM   3697  O   ASN B 684      24.314  14.273   1.226  1.00 94.05           O  
ANISOU 3697  O   ASN B 684     9767  14971  10997   1731    323    789       O  
ATOM   3698  CB  ASN B 684      25.422  11.884   2.953  1.00 87.19           C  
ANISOU 3698  CB  ASN B 684     9077  14431   9619   2132    326    686       C  
ATOM   3699  CG  ASN B 684      25.331  11.203   4.311  1.00 85.29           C  
ANISOU 3699  CG  ASN B 684     8919  14224   9263   2233    310    578       C  
ATOM   3700  OD1 ASN B 684      24.340  10.542   4.620  1.00 88.13           O  
ANISOU 3700  OD1 ASN B 684     9428  14449   9608   2234    319    550       O  
ATOM   3701  ND2 ASN B 684      26.372  11.353   5.124  1.00 81.04           N  
ANISOU 3701  ND2 ASN B 684     8280  13874   8639   2321    285    520       N  
ATOM   3702  N   CYS B 685      23.477  14.570   3.294  1.00 90.65           N  
ANISOU 3702  N   CYS B 685     9363  14408  10674   1662    288    560       N  
ATOM   3703  CA  CYS B 685      22.256  15.223   2.829  1.00 87.42           C  
ANISOU 3703  CA  CYS B 685     8975  13758  10481   1497    295    568       C  
ATOM   3704  C   CYS B 685      22.546  16.415   1.927  1.00 79.32           C  
ANISOU 3704  C   CYS B 685     7810  12689   9638   1387    287    649       C  
ATOM   3705  O   CYS B 685      23.278  17.327   2.311  1.00 84.18           O  
ANISOU 3705  O   CYS B 685     8278  13364  10345   1348    259    609       O  
ATOM   3706  CB  CYS B 685      21.394  15.668   4.013  1.00 89.26           C  
ANISOU 3706  CB  CYS B 685     9217  13848  10850   1403    275    416       C  
ATOM   3707  SG  CYS B 685      19.807  16.400   3.536  1.00 74.50           S  
ANISOU 3707  SG  CYS B 685     7384  11689   9232   1221    285    413       S  
ATOM   3708  N   PRO B 686      21.968  16.405   0.717  1.00 61.83           N  
ANISOU 3708  N   PRO B 686     5640  10376   7477   1336    310    765       N  
ATOM   3709  CA  PRO B 686      22.106  17.510  -0.237  1.00 57.71           C  
ANISOU 3709  CA  PRO B 686     4998   9793   7135   1232    303    861       C  
ATOM   3710  C   PRO B 686      21.458  18.778   0.303  1.00 52.12           C  
ANISOU 3710  C   PRO B 686     4214   8893   6695   1085    278    774       C  
ATOM   3711  O   PRO B 686      20.390  18.704   0.909  1.00 55.05           O  
ANISOU 3711  O   PRO B 686     4669   9115   7135   1036    280    680       O  
ATOM   3712  CB  PRO B 686      21.335  17.013  -1.465  1.00 60.04           C  
ANISOU 3712  CB  PRO B 686     5396  10006   7411   1218    336    982       C  
ATOM   3713  CG  PRO B 686      21.266  15.525  -1.308  1.00 58.97           C  
ANISOU 3713  CG  PRO B 686     5412   9963   7031   1353    363    972       C  
ATOM   3714  CD  PRO B 686      21.185  15.288   0.164  1.00 56.34           C  
ANISOU 3714  CD  PRO B 686     5111   9633   6661   1386    345    819       C  
ATOM   3715  N   LYS B 687      22.099  19.924   0.087  1.00 53.01           N  
ANISOU 3715  N   LYS B 687     4169   9016   6959   1019    254    804       N  
ATOM   3716  CA  LYS B 687      21.559  21.199   0.546  1.00 50.79           C  
ANISOU 3716  CA  LYS B 687     3804   8550   6945    889    230    726       C  
ATOM   3717  C   LYS B 687      20.212  21.482  -0.107  1.00 48.72           C  
ANISOU 3717  C   LYS B 687     3616   8059   6839    801    245    771       C  
ATOM   3718  O   LYS B 687      19.472  22.356   0.337  1.00 57.88           O  
ANISOU 3718  O   LYS B 687     4744   9039   8208    708    232    690       O  
ATOM   3719  CB  LYS B 687      22.530  22.347   0.253  1.00 69.69           C  
ANISOU 3719  CB  LYS B 687     6013  10998   9469    837    202    775       C  
ATOM   3720  CG  LYS B 687      23.897  22.221   0.917  1.00 85.54           C  
ANISOU 3720  CG  LYS B 687     7921  13245  11338    913    184    724       C  
ATOM   3721  CD  LYS B 687      24.775  23.423   0.580  1.00 97.92           C  
ANISOU 3721  CD  LYS B 687     9297  14856  13053    842    155    776       C  
ATOM   3722  CE  LYS B 687      26.253  23.160   0.859  1.00101.57           C  
ANISOU 3722  CE  LYS B 687     9655  15604  13333    931    141    774       C  
ATOM   3723  NZ  LYS B 687      26.585  23.121   2.311  1.00 99.13           N  
ANISOU 3723  NZ  LYS B 687     9313  15375  12976    960    124    598       N  
ATOM   3724  N   ARG B 688      19.900  20.743  -1.167  1.00 53.03           N  
ANISOU 3724  N   ARG B 688     4253   8618   7277    836    273    897       N  
ATOM   3725  CA  ARG B 688      18.618  20.893  -1.844  1.00 67.06           C  
ANISOU 3725  CA  ARG B 688     6103  10202   9173    763    289    946       C  
ATOM   3726  C   ARG B 688      17.485  20.288  -1.022  1.00 58.68           C  
ANISOU 3726  C   ARG B 688     5175   9037   8083    757    301    820       C  
ATOM   3727  O   ARG B 688      16.379  20.827  -0.984  1.00 54.79           O  
ANISOU 3727  O   ARG B 688     4703   8359   7757    673    301    783       O  
ATOM   3728  CB  ARG B 688      18.658  20.257  -3.233  1.00122.92           C  
ANISOU 3728  CB  ARG B 688    13230  17342  16131    803    316   1115       C  
ATOM   3729  CG  ARG B 688      19.566  20.973  -4.213  1.00145.75           C  
ANISOU 3729  CG  ARG B 688    15987  20311  19081    787    304   1258       C  
ATOM   3730  CD  ARG B 688      19.397  20.415  -5.609  1.00162.94           C  
ANISOU 3730  CD  ARG B 688    18216  22529  21164    812    332   1419       C  
ATOM   3731  NE  ARG B 688      19.735  18.998  -5.662  1.00183.59           N  
ANISOU 3731  NE  ARG B 688    20940  25308  23508    932    362   1421       N  
ATOM   3732  CZ  ARG B 688      20.965  18.534  -5.843  1.00198.77           C  
ANISOU 3732  CZ  ARG B 688    22816  27449  25257   1030    366   1466       C  
ATOM   3733  NH1 ARG B 688      21.976  19.379  -5.988  1.00202.54           N  
ANISOU 3733  NH1 ARG B 688    23137  28016  25801   1011    340   1512       N  
ATOM   3734  NH2 ARG B 688      21.185  17.226  -5.880  1.00203.78           N  
ANISOU 3734  NH2 ARG B 688    23558  28216  25652   1151    395   1463       N  
ATOM   3735  N   MET B 689      17.764  19.166  -0.365  1.00 47.22           N  
ANISOU 3735  N   MET B 689     3810   7714   6417    852    310    757       N  
ATOM   3736  CA  MET B 689      16.768  18.513   0.475  1.00 45.53           C  
ANISOU 3736  CA  MET B 689     3719   7425   6157    850    319    639       C  
ATOM   3737  C   MET B 689      16.572  19.290   1.771  1.00 43.81           C  
ANISOU 3737  C   MET B 689     3437   7131   6079    792    293    474       C  
ATOM   3738  O   MET B 689      15.446  19.493   2.223  1.00 50.91           O  
ANISOU 3738  O   MET B 689     4382   7879   7082    724    295    386       O  
ATOM   3739  CB  MET B 689      17.178  17.074   0.783  1.00 52.86           C  
ANISOU 3739  CB  MET B 689     4756   8514   6814    980    334    633       C  
ATOM   3740  CG  MET B 689      16.106  16.277   1.506  1.00 57.06           C  
ANISOU 3740  CG  MET B 689     5424   8972   7285    981    344    537       C  
ATOM   3741  SD  MET B 689      14.636  16.017   0.493  1.00 69.13           S  
ANISOU 3741  SD  MET B 689     7060  10337   8871    906    371    609       S  
ATOM   3742  CE  MET B 689      15.279  14.906  -0.756  1.00 46.91           C  
ANISOU 3742  CE  MET B 689     4314   7671   5840   1021    400    773       C  
ATOM   3743  N   LYS B 690      17.680  19.716   2.368  1.00 45.85           N  
ANISOU 3743  N   LYS B 690     3583   7505   6332    821    270    427       N  
ATOM   3744  CA  LYS B 690      17.641  20.562   3.554  1.00 43.29           C  
ANISOU 3744  CA  LYS B 690     3174   7125   6150    765    245    270       C  
ATOM   3745  C   LYS B 690      16.946  21.872   3.202  1.00 44.00           C  
ANISOU 3745  C   LYS B 690     3188   7009   6520    645    237    270       C  
ATOM   3746  O   LYS B 690      16.219  22.443   4.013  1.00 40.34           O  
ANISOU 3746  O   LYS B 690     2710   6417   6199    581    229    136       O  
ATOM   3747  CB  LYS B 690      19.061  20.822   4.055  1.00 42.86           C  
ANISOU 3747  CB  LYS B 690     2996   7252   6037    818    222    242       C  
ATOM   3748  CG  LYS B 690      19.153  21.546   5.387  1.00 59.16           C  
ANISOU 3748  CG  LYS B 690     4971   9298   8208    775    196     66       C  
ATOM   3749  CD  LYS B 690      20.556  21.398   5.961  1.00 75.22           C  
ANISOU 3749  CD  LYS B 690     6913  11563  10104    857    177     36       C  
ATOM   3750  CE  LYS B 690      21.219  22.743   6.209  1.00 80.34           C  
ANISOU 3750  CE  LYS B 690     7379  12206  10942    781    150    -12       C  
ATOM   3751  NZ  LYS B 690      22.707  22.640   6.128  1.00 75.56           N  
ANISOU 3751  NZ  LYS B 690     6669  11841  10199    857    136     37       N  
ATOM   3752  N   ARG B 691      17.177  22.336   1.980  1.00 50.50           N  
ANISOU 3752  N   ARG B 691     3961   7806   7421    621    240    423       N  
ATOM   3753  CA  ARG B 691      16.488  23.504   1.451  1.00 52.30           C  
ANISOU 3753  CA  ARG B 691     4126   7838   7908    524    233    457       C  
ATOM   3754  C   ARG B 691      14.988  23.273   1.476  1.00 47.56           C  
ANISOU 3754  C   ARG B 691     3639   7074   7357    484    252    413       C  
ATOM   3755  O   ARG B 691      14.233  24.038   2.075  1.00 47.71           O  
ANISOU 3755  O   ARG B 691     3628   6943   7556    420    244    303       O  
ATOM   3756  CB  ARG B 691      16.921  23.752   0.008  1.00 79.85           C  
ANISOU 3756  CB  ARG B 691     7568  11351  11420    521    237    654       C  
ATOM   3757  CG  ARG B 691      17.576  25.095  -0.225  1.00 93.93           C  
ANISOU 3757  CG  ARG B 691     9181  13097  13410    463    208    695       C  
ATOM   3758  CD  ARG B 691      18.056  25.219  -1.660  1.00100.32           C  
ANISOU 3758  CD  ARG B 691     9946  13958  14213    467    211    900       C  
ATOM   3759  NE  ARG B 691      19.507  25.358  -1.730  1.00110.20           N  
ANISOU 3759  NE  ARG B 691    11082  15399  15390    500    194    947       N  
ATOM   3760  CZ  ARG B 691      20.279  24.713  -2.598  1.00118.46           C  
ANISOU 3760  CZ  ARG B 691    12131  16618  16258    562    205   1082       C  
ATOM   3761  NH1 ARG B 691      19.741  23.878  -3.477  1.00123.77           N  
ANISOU 3761  NH1 ARG B 691    12920  17293  16812    597    235   1182       N  
ATOM   3762  NH2 ARG B 691      21.591  24.903  -2.589  1.00117.06           N  
ANISOU 3762  NH2 ARG B 691    11837  16623  16018    590    187   1112       N  
ATOM   3763  N   LEU B 692      14.571  22.207   0.802  1.00 58.30           N  
ANISOU 3763  N   LEU B 692     5125   8473   8552    525    278    498       N  
ATOM   3764  CA  LEU B 692      13.166  21.849   0.678  1.00 50.44           C  
ANISOU 3764  CA  LEU B 692     4242   7350   7572    491    298    475       C  
ATOM   3765  C   LEU B 692      12.524  21.643   2.043  1.00 48.31           C  
ANISOU 3765  C   LEU B 692     4020   7041   7295    477    295    287       C  
ATOM   3766  O   LEU B 692      11.481  22.223   2.345  1.00 43.44           O  
ANISOU 3766  O   LEU B 692     3403   6272   6832    412    295    207       O  
ATOM   3767  CB  LEU B 692      13.038  20.575  -0.156  1.00 33.70           C  
ANISOU 3767  CB  LEU B 692     2246   5320   5239    550    325    586       C  
ATOM   3768  CG  LEU B 692      11.644  19.992  -0.353  1.00 29.72           C  
ANISOU 3768  CG  LEU B 692     1866   4718   4708    522    347    572       C  
ATOM   3769  CD1 LEU B 692      10.744  20.988  -1.068  1.00 36.53           C  
ANISOU 3769  CD1 LEU B 692     2684   5411   5786    444    346    623       C  
ATOM   3770  CD2 LEU B 692      11.738  18.695  -1.133  1.00 18.71           C  
ANISOU 3770  CD2 LEU B 692      581   3436   3090    590    371    677       C  
ATOM   3771  N   MET B 693      13.158  20.809   2.860  1.00 45.97           N  
ANISOU 3771  N   MET B 693     3760   6892   6813    544    292    218       N  
ATOM   3772  CA  MET B 693      12.680  20.510   4.202  1.00 29.88           C  
ANISOU 3772  CA  MET B 693     1765   4850   4740    540    287     45       C  
ATOM   3773  C   MET B 693      12.209  21.771   4.916  1.00 32.32           C  
ANISOU 3773  C   MET B 693     1976   5018   5286    457    271    -86       C  
ATOM   3774  O   MET B 693      11.084  21.833   5.406  1.00 39.72           O  
ANISOU 3774  O   MET B 693     2959   5848   6286    409    278   -187       O  
ATOM   3775  CB  MET B 693      13.796  19.848   5.009  1.00 36.08           C  
ANISOU 3775  CB  MET B 693     2541   5826   5340    628    276     -2       C  
ATOM   3776  CG  MET B 693      13.332  18.754   5.947  1.00 33.37           C  
ANISOU 3776  CG  MET B 693     2312   5539   4828    671    282    -98       C  
ATOM   3777  SD  MET B 693      14.695  18.107   6.929  1.00 65.37           S  
ANISOU 3777  SD  MET B 693     6338   9821   8679    790    264   -149       S  
ATOM   3778  CE  MET B 693      15.943  17.845   5.667  1.00 17.86           C  
ANISOU 3778  CE  MET B 693      291   3940   2554    876    270     39       C  
ATOM   3779  N   ALA B 694      13.076  22.777   4.966  1.00 42.07           N  
ANISOU 3779  N   ALA B 694     3073   6260   6654    442    250    -87       N  
ATOM   3780  CA  ALA B 694      12.774  24.024   5.663  1.00 46.39           C  
ANISOU 3780  CA  ALA B 694     3513   6680   7435    372    234   -216       C  
ATOM   3781  C   ALA B 694      11.498  24.681   5.145  1.00 46.93           C  
ANISOU 3781  C   ALA B 694     3593   6544   7694    305    244   -204       C  
ATOM   3782  O   ALA B 694      10.710  25.220   5.922  1.00 51.61           O  
ANISOU 3782  O   ALA B 694     4165   7028   8415    260    243   -347       O  
ATOM   3783  CB  ALA B 694      13.943  24.986   5.558  1.00 50.96           C  
ANISOU 3783  CB  ALA B 694     3937   7297   8129    364    210   -187       C  
ATOM   3784  N   GLU B 695      11.305  24.639   3.831  1.00 48.97           N  
ANISOU 3784  N   GLU B 695     3879   6762   7967    304    256    -32       N  
ATOM   3785  CA  GLU B 695      10.124  25.229   3.210  1.00 54.96           C  
ANISOU 3785  CA  GLU B 695     4644   7343   8893    252    266      3       C  
ATOM   3786  C   GLU B 695       8.843  24.510   3.631  1.00 45.01           C  
ANISOU 3786  C   GLU B 695     3507   6043   7552    241    286    -87       C  
ATOM   3787  O   GLU B 695       7.791  25.134   3.772  1.00 38.66           O  
ANISOU 3787  O   GLU B 695     2689   5098   6902    196    291   -154       O  
ATOM   3788  CB  GLU B 695      10.259  25.219   1.685  1.00 63.75           C  
ANISOU 3788  CB  GLU B 695     5762   8452  10008    261    273    215       C  
ATOM   3789  CG  GLU B 695      11.455  25.997   1.160  1.00 65.20           C  
ANISOU 3789  CG  GLU B 695     5814   8673  10284    262    252    319       C  
ATOM   3790  CD  GLU B 695      11.419  27.460   1.558  1.00 70.14           C  
ANISOU 3790  CD  GLU B 695     6300   9159  11190    207    229    248       C  
ATOM   3791  OE1 GLU B 695      12.412  27.939   2.145  1.00 65.27           O  
ANISOU 3791  OE1 GLU B 695     5581   8604  10615    206    208    190       O  
ATOM   3792  OE2 GLU B 695      10.398  28.128   1.289  1.00 77.83           O  
ANISOU 3792  OE2 GLU B 695     7261   9969  12342    168    232    247       O  
ATOM   3793  N   CYS B 696       8.939  23.199   3.829  1.00 41.41           N  
ANISOU 3793  N   CYS B 696     3165   5715   6852    286    299    -87       N  
ATOM   3794  CA  CYS B 696       7.789  22.395   4.233  1.00 34.41           C  
ANISOU 3794  CA  CYS B 696     2397   4811   5867    274    318   -165       C  
ATOM   3795  C   CYS B 696       7.465  22.575   5.714  1.00 35.40           C  
ANISOU 3795  C   CYS B 696     2503   4926   6021    251    309   -372       C  
ATOM   3796  O   CYS B 696       6.335  22.347   6.140  1.00 31.01           O  
ANISOU 3796  O   CYS B 696     2006   4315   5460    219    322   -464       O  
ATOM   3797  CB  CYS B 696       8.035  20.914   3.932  1.00 35.08           C  
ANISOU 3797  CB  CYS B 696     2606   5036   5688    333    332    -89       C  
ATOM   3798  SG  CYS B 696       8.296  20.525   2.184  1.00 50.67           S  
ANISOU 3798  SG  CYS B 696     4617   7039   7597    364    348    143       S  
ATOM   3799  N   LEU B 697       8.460  22.981   6.495  1.00 52.53           N  
ANISOU 3799  N   LEU B 697     4584   7160   8214    268    288   -447       N  
ATOM   3800  CA  LEU B 697       8.285  23.152   7.935  1.00 48.63           C  
ANISOU 3800  CA  LEU B 697     4061   6678   7738    250    279   -646       C  
ATOM   3801  C   LEU B 697       8.032  24.612   8.303  1.00 44.90           C  
ANISOU 3801  C   LEU B 697     3460   6067   7533    195    267   -748       C  
ATOM   3802  O   LEU B 697       7.988  24.969   9.481  1.00 46.60           O  
ANISOU 3802  O   LEU B 697     3623   6287   7795    178    258   -921       O  
ATOM   3803  CB  LEU B 697       9.509  22.625   8.686  1.00 36.53           C  
ANISOU 3803  CB  LEU B 697     2509   5322   6048    309    263   -682       C  
ATOM   3804  CG  LEU B 697       9.848  21.152   8.454  1.00 32.49           C  
ANISOU 3804  CG  LEU B 697     2118   4959   5268    381    272   -592       C  
ATOM   3805  CD1 LEU B 697      11.208  20.806   9.040  1.00 28.91           C  
ANISOU 3805  CD1 LEU B 697     1621   4684   4681    456    254   -605       C  
ATOM   3806  CD2 LEU B 697       8.764  20.253   9.028  1.00 30.94           C  
ANISOU 3806  CD2 LEU B 697     2038   4760   4957    369    287   -670       C  
ATOM   3807  N   LYS B 698       7.864  25.449   7.285  1.00 39.32           N  
ANISOU 3807  N   LYS B 698     2699   5238   7003    172    268   -639       N  
ATOM   3808  CA  LYS B 698       7.645  26.877   7.482  1.00 39.96           C  
ANISOU 3808  CA  LYS B 698     2651   5174   7358    128    256   -713       C  
ATOM   3809  C   LYS B 698       6.575  27.128   8.538  1.00 59.86           C  
ANISOU 3809  C   LYS B 698     5173   7623   9947     93    263   -909       C  
ATOM   3810  O   LYS B 698       5.541  26.466   8.551  1.00 71.15           O  
ANISOU 3810  O   LYS B 698     6705   9044  11285     86    282   -931       O  
ATOM   3811  CB  LYS B 698       7.230  27.522   6.162  1.00 31.35           C  
ANISOU 3811  CB  LYS B 698     1533   3953   6424    111    260   -555       C  
ATOM   3812  CG  LYS B 698       7.843  28.884   5.908  1.00 33.90           C  
ANISOU 3812  CG  LYS B 698     1701   4185   6994     89    237   -525       C  
ATOM   3813  CD  LYS B 698       9.360  28.825   5.933  1.00 34.71           C  
ANISOU 3813  CD  LYS B 698     1743   4422   7026    113    219   -475       C  
ATOM   3814  CE  LYS B 698       9.955  29.923   5.063  1.00 50.52           C  
ANISOU 3814  CE  LYS B 698     3616   6347   9231     93    200   -347       C  
ATOM   3815  NZ  LYS B 698      11.353  30.259   5.461  1.00 54.89           N  
ANISOU 3815  NZ  LYS B 698     4063   7009   9785     97    177   -367       N  
ATOM   3816  N   LYS B 699       6.829  28.087   9.423  1.00 53.85           N  
ANISOU 3816  N   LYS B 699     4294   6820   9348     72    247  -1056       N  
ATOM   3817  CA  LYS B 699       5.881  28.419  10.480  1.00 49.03           C  
ANISOU 3817  CA  LYS B 699     3667   6150   8814     41    254  -1256       C  
ATOM   3818  C   LYS B 699       4.535  28.843   9.890  1.00 51.97           C  
ANISOU 3818  C   LYS B 699     4056   6369   9320     16    270  -1235       C  
ATOM   3819  O   LYS B 699       3.487  28.327  10.280  1.00 54.88           O  
ANISOU 3819  O   LYS B 699     4502   6743   9607      3    288  -1318       O  
ATOM   3820  CB  LYS B 699       6.444  29.528  11.372  1.00 58.70           C  
ANISOU 3820  CB  LYS B 699     4740   7342  10220     22    234  -1405       C  
ATOM   3821  CG  LYS B 699       6.383  29.235  12.868  1.00 58.29           C  
ANISOU 3821  CG  LYS B 699     4685   7385  10077     17    234  -1620       C  
ATOM   3822  CD  LYS B 699       7.684  28.624  13.375  1.00 57.02           C  
ANISOU 3822  CD  LYS B 699     4519   7409   9737     51    219  -1621       C  
ATOM   3823  CE  LYS B 699       7.581  27.117  13.527  1.00 59.43           C  
ANISOU 3823  CE  LYS B 699     4971   7860   9750     86    229  -1582       C  
ATOM   3824  NZ  LYS B 699       6.729  26.733  14.688  1.00 62.36           N  
ANISOU 3824  NZ  LYS B 699     5381   8265  10048     67    239  -1762       N  
ATOM   3825  N   LYS B 700       4.572  29.780   8.946  1.00 66.98           N  
ANISOU 3825  N   LYS B 700     5880   8146  11424      8    263  -1121       N  
ATOM   3826  CA  LYS B 700       3.361  30.253   8.279  1.00 77.54           C  
ANISOU 3826  CA  LYS B 700     7219   9344  12899     -8    275  -1080       C  
ATOM   3827  C   LYS B 700       2.894  29.261   7.214  1.00 82.14           C  
ANISOU 3827  C   LYS B 700     7931   9969  13308      7    294   -913       C  
ATOM   3828  O   LYS B 700       3.654  28.899   6.316  1.00 94.58           O  
ANISOU 3828  O   LYS B 700     9533  11597  14807     28    290   -742       O  
ATOM   3829  CB  LYS B 700       3.591  31.634   7.660  1.00 82.61           C  
ANISOU 3829  CB  LYS B 700     7722   9839  13829    -20    258  -1010       C  
ATOM   3830  CG  LYS B 700       4.146  32.663   8.637  1.00 94.81           C  
ANISOU 3830  CG  LYS B 700     9125  11339  15559    -37    238  -1168       C  
ATOM   3831  CD  LYS B 700       4.119  34.067   8.050  1.00 97.83           C  
ANISOU 3831  CD  LYS B 700     9368  11552  16252    -53    221  -1110       C  
ATOM   3832  CE  LYS B 700       4.827  35.064   8.956  1.00 92.33           C  
ANISOU 3832  CE  LYS B 700     8523  10820  15737    -73    200  -1257       C  
ATOM   3833  NZ  LYS B 700       6.295  34.821   9.016  1.00 84.11           N  
ANISOU 3833  NZ  LYS B 700     7456   9907  14596    -69    184  -1206       N  
ATOM   3834  N   ARG B 701       1.639  28.832   7.318  1.00 61.00           N  
ANISOU 3834  N   ARG B 701     5329   7277  10570     -6    316   -969       N  
ATOM   3835  CA  ARG B 701       1.096  27.784   6.453  1.00 50.79           C  
ANISOU 3835  CA  ARG B 701     4165   6040   9093      4    336   -841       C  
ATOM   3836  C   ARG B 701       1.188  28.076   4.956  1.00 49.53           C  
ANISOU 3836  C   ARG B 701     3992   5823   9005     15    336   -624       C  
ATOM   3837  O   ARG B 701       1.466  27.179   4.161  1.00 55.10           O  
ANISOU 3837  O   ARG B 701     4785   6611   9539     35    344   -483       O  
ATOM   3838  CB  ARG B 701      -0.356  27.473   6.830  1.00 59.08           C  
ANISOU 3838  CB  ARG B 701     5272   7075  10099    -19    358   -950       C  
ATOM   3839  CG  ARG B 701      -1.260  28.686   6.947  1.00 67.58           C  
ANISOU 3839  CG  ARG B 701     6245   8011  11421    -38    358  -1031       C  
ATOM   3840  CD  ARG B 701      -2.621  28.299   7.500  1.00 59.82           C  
ANISOU 3840  CD  ARG B 701     5315   7049  10365    -60    380  -1164       C  
ATOM   3841  NE  ARG B 701      -3.383  27.482   6.561  1.00 68.81           N  
ANISOU 3841  NE  ARG B 701     6557   8228  11360    -60    401  -1043       N  
ATOM   3842  CZ  ARG B 701      -4.566  26.942   6.832  1.00 83.16           C  
ANISOU 3842  CZ  ARG B 701     8437  10090  13073    -82    424  -1126       C  
ATOM   3843  NH1 ARG B 701      -5.122  27.127   8.022  1.00 91.76           N  
ANISOU 3843  NH1 ARG B 701     9496  11190  14180   -104    428  -1327       N  
ATOM   3844  NH2 ARG B 701      -5.192  26.215   5.917  1.00 78.97           N  
ANISOU 3844  NH2 ARG B 701     7992   9600  12413    -82    442  -1010       N  
ATOM   3845  N   ASP B 702       0.947  29.323   4.570  1.00 50.87           N  
ANISOU 3845  N   ASP B 702     4046   5854   9428      5    325   -596       N  
ATOM   3846  CA  ASP B 702       0.903  29.667   3.153  1.00 49.59           C  
ANISOU 3846  CA  ASP B 702     3861   5634   9346     13    324   -389       C  
ATOM   3847  C   ASP B 702       2.270  30.023   2.575  1.00 50.96           C  
ANISOU 3847  C   ASP B 702     3969   5825   9571     25    303   -252       C  
ATOM   3848  O   ASP B 702       2.369  30.503   1.446  1.00 51.96           O  
ANISOU 3848  O   ASP B 702     4048   5897   9797     29    297    -80       O  
ATOM   3849  CB  ASP B 702      -0.112  30.784   2.897  1.00 74.93           C  
ANISOU 3849  CB  ASP B 702     6979   8692  12798     -3    323   -403       C  
ATOM   3850  CG  ASP B 702      -1.546  30.314   3.064  1.00 84.80           C  
ANISOU 3850  CG  ASP B 702     8302   9950  13967    -12    347   -483       C  
ATOM   3851  OD1 ASP B 702      -1.785  29.090   2.976  1.00 76.63           O  
ANISOU 3851  OD1 ASP B 702     7396   9030  12688     -8    366   -467       O  
ATOM   3852  OD2 ASP B 702      -2.434  31.165   3.281  1.00 88.39           O  
ANISOU 3852  OD2 ASP B 702     8680  10301  14602    -23    347   -562       O  
ATOM   3853  N   GLU B 703       3.322  29.785   3.353  1.00 53.72           N  
ANISOU 3853  N   GLU B 703     4308   6259   9845     33    291   -326       N  
ATOM   3854  CA  GLU B 703       4.684  29.915   2.846  1.00 56.68           C  
ANISOU 3854  CA  GLU B 703     4631   6692  10215     47    273   -200       C  
ATOM   3855  C   GLU B 703       5.223  28.538   2.489  1.00 54.04           C  
ANISOU 3855  C   GLU B 703     4418   6523   9593     79    285   -112       C  
ATOM   3856  O   GLU B 703       6.332  28.405   1.965  1.00 53.66           O  
ANISOU 3856  O   GLU B 703     4345   6556   9487     99    275      7       O  
ATOM   3857  CB  GLU B 703       5.597  30.582   3.874  1.00 70.49           C  
ANISOU 3857  CB  GLU B 703     6272   8446  12065     38    250   -331       C  
ATOM   3858  CG  GLU B 703       5.325  32.057   4.095  1.00 80.26           C  
ANISOU 3858  CG  GLU B 703     7365   9518  13613      8    234   -395       C  
ATOM   3859  CD  GLU B 703       6.409  32.727   4.917  1.00 86.63           C  
ANISOU 3859  CD  GLU B 703     8054  10343  14519     -4    210   -496       C  
ATOM   3860  OE1 GLU B 703       6.067  33.444   5.879  1.00 86.94           O  
ANISOU 3860  OE1 GLU B 703     8019  10304  14711    -24    204   -674       O  
ATOM   3861  OE2 GLU B 703       7.603  32.531   4.605  1.00 85.52           O  
ANISOU 3861  OE2 GLU B 703     7890  10306  14299      7    197   -401       O  
ATOM   3862  N   ARG B 704       4.427  27.515   2.782  1.00 49.91           N  
ANISOU 3862  N   ARG B 704     4019   6053   8890     85    307   -173       N  
ATOM   3863  CA  ARG B 704       4.796  26.139   2.481  1.00 52.54           C  
ANISOU 3863  CA  ARG B 704     4475   6535   8953    118    320   -100       C  
ATOM   3864  C   ARG B 704       4.495  25.810   1.028  1.00 51.50           C  
ANISOU 3864  C   ARG B 704     4391   6403   8774    128    333     95       C  
ATOM   3865  O   ARG B 704       3.470  26.231   0.491  1.00 53.60           O  
ANISOU 3865  O   ARG B 704     4650   6570   9146    107    342    128       O  
ATOM   3866  CB  ARG B 704       4.048  25.172   3.397  1.00 55.56           C  
ANISOU 3866  CB  ARG B 704     4966   6973   9170    114    336   -243       C  
ATOM   3867  CG  ARG B 704       4.161  25.513   4.868  1.00 52.04           C  
ANISOU 3867  CG  ARG B 704     4472   6528   8773    100    325   -447       C  
ATOM   3868  CD  ARG B 704       4.223  24.255   5.704  1.00 55.45           C  
ANISOU 3868  CD  ARG B 704     5009   7095   8963    118    333   -534       C  
ATOM   3869  NE  ARG B 704       2.963  23.952   6.375  1.00 65.03           N  
ANISOU 3869  NE  ARG B 704     6281   8281  10146     86    348   -668       N  
ATOM   3870  CZ  ARG B 704       2.705  24.257   7.642  1.00 70.62           C  
ANISOU 3870  CZ  ARG B 704     6951   8984  10898     64    343   -857       C  
ATOM   3871  NH1 ARG B 704       3.618  24.877   8.374  1.00 74.77           N  
ANISOU 3871  NH1 ARG B 704     7380   9525  11503     71    323   -936       N  
ATOM   3872  NH2 ARG B 704       1.539  23.940   8.180  1.00 75.54           N  
ANISOU 3872  NH2 ARG B 704     7626   9596  11480     34    359   -970       N  
ATOM   3873  N   PRO B 705       5.393  25.050   0.388  1.00 53.50           N  
ANISOU 3873  N   PRO B 705     4686   6779   8862    164    335    222       N  
ATOM   3874  CA  PRO B 705       5.251  24.666  -1.019  1.00 49.78           C  
ANISOU 3874  CA  PRO B 705     4257   6332   8325    179    347    410       C  
ATOM   3875  C   PRO B 705       4.079  23.713  -1.220  1.00 47.41           C  
ANISOU 3875  C   PRO B 705     4082   6046   7884    176    372    395       C  
ATOM   3876  O   PRO B 705       3.435  23.311  -0.251  1.00 52.42           O  
ANISOU 3876  O   PRO B 705     4774   6680   8465    163    379    243       O  
ATOM   3877  CB  PRO B 705       6.565  23.933  -1.317  1.00 43.15           C  
ANISOU 3877  CB  PRO B 705     3437   5648   7311    225    345    500       C  
ATOM   3878  CG  PRO B 705       7.504  24.339  -0.227  1.00 44.39           C  
ANISOU 3878  CG  PRO B 705     3520   5837   7510    230    325    386       C  
ATOM   3879  CD  PRO B 705       6.643  24.540   0.973  1.00 46.03           C  
ANISOU 3879  CD  PRO B 705     3740   5968   7782    199    325    192       C  
ATOM   3880  N   SER B 706       3.807  23.363  -2.472  1.00 37.15           N  
ANISOU 3880  N   SER B 706     2820   4768   6526    187    383    551       N  
ATOM   3881  CA  SER B 706       2.803  22.357  -2.784  1.00 36.83           C  
ANISOU 3881  CA  SER B 706     2899   4763   6332    188    405    550       C  
ATOM   3882  C   SER B 706       3.494  21.135  -3.370  1.00 31.22           C  
ANISOU 3882  C   SER B 706     2273   4195   5393    234    414    649       C  
ATOM   3883  O   SER B 706       4.610  21.233  -3.876  1.00 31.29           O  
ANISOU 3883  O   SER B 706     2237   4267   5387    263    407    757       O  
ATOM   3884  CB  SER B 706       1.764  22.911  -3.758  1.00 59.07           C  
ANISOU 3884  CB  SER B 706     5689   7495   9262    166    411    638       C  
ATOM   3885  OG  SER B 706       1.024  23.964  -3.166  1.00 58.81           O  
ANISOU 3885  OG  SER B 706     5581   7334   9431    132    405    535       O  
ATOM   3886  N   PHE B 707       2.830  19.986  -3.306  1.00 29.58           N  
ANISOU 3886  N   PHE B 707     2185   4045   5011    241    430    611       N  
ATOM   3887  CA  PHE B 707       3.455  18.723  -3.700  1.00 26.85           C  
ANISOU 3887  CA  PHE B 707     1925   3832   4443    293    439    680       C  
ATOM   3888  C   PHE B 707       3.882  18.610  -5.166  1.00 32.30           C  
ANISOU 3888  C   PHE B 707     2602   4576   5094    322    444    871       C  
ATOM   3889  O   PHE B 707       4.770  17.822  -5.488  1.00 52.69           O  
ANISOU 3889  O   PHE B 707     5220   7275   7523    375    449    938       O  
ATOM   3890  CB  PHE B 707       2.595  17.529  -3.280  1.00 18.37           C  
ANISOU 3890  CB  PHE B 707      976   2796   3208    292    452    593       C  
ATOM   3891  CG  PHE B 707       2.881  17.049  -1.886  1.00 23.48           C  
ANISOU 3891  CG  PHE B 707     1659   3482   3780    299    448    447       C  
ATOM   3892  CD1 PHE B 707       3.925  16.173  -1.645  1.00 18.63           C  
ANISOU 3892  CD1 PHE B 707     1087   2985   3005    363    447    468       C  
ATOM   3893  CD2 PHE B 707       2.123  17.490  -0.815  1.00 39.21           C  
ANISOU 3893  CD2 PHE B 707     3636   5402   5859    250    445    289       C  
ATOM   3894  CE1 PHE B 707       4.199  15.737  -0.361  1.00 16.36           C  
ANISOU 3894  CE1 PHE B 707      828   2743   2647    378    442    342       C  
ATOM   3895  CE2 PHE B 707       2.394  17.056   0.470  1.00 31.24           C  
ANISOU 3895  CE2 PHE B 707     2654   4439   4778    256    440    158       C  
ATOM   3896  CZ  PHE B 707       3.433  16.179   0.696  1.00 19.27           C  
ANISOU 3896  CZ  PHE B 707     1180   3040   3103    321    437    189       C  
ATOM   3897  N   PRO B 708       3.250  19.381  -6.062  1.00 25.42           N  
ANISOU 3897  N   PRO B 708     1676   3627   4354    293    442    959       N  
ATOM   3898  CA  PRO B 708       3.798  19.417  -7.420  1.00 24.28           C  
ANISOU 3898  CA  PRO B 708     1498   3541   4187    318    443   1145       C  
ATOM   3899  C   PRO B 708       5.214  19.983  -7.418  1.00 26.36           C  
ANISOU 3899  C   PRO B 708     1669   3845   4503    338    432   1207       C  
ATOM   3900  O   PRO B 708       6.108  19.427  -8.058  1.00 33.80           O  
ANISOU 3900  O   PRO B 708     2620   4907   5317    383    438   1310       O  
ATOM   3901  CB  PRO B 708       2.859  20.378  -8.146  1.00 24.54           C  
ANISOU 3901  CB  PRO B 708     1465   3469   4391    279    439   1212       C  
ATOM   3902  CG  PRO B 708       1.576  20.274  -7.410  1.00 21.15           C  
ANISOU 3902  CG  PRO B 708     1087   2969   3981    247    444   1066       C  
ATOM   3903  CD  PRO B 708       1.943  20.053  -5.975  1.00 20.56           C  
ANISOU 3903  CD  PRO B 708     1039   2894   3879    244    442    902       C  
ATOM   3904  N   ARG B 709       5.404  21.084  -6.699  1.00 30.48           N  
ANISOU 3904  N   ARG B 709     2097   4273   5212    307    415   1140       N  
ATOM   3905  CA  ARG B 709       6.709  21.726  -6.583  1.00 41.04           C  
ANISOU 3905  CA  ARG B 709     3332   5644   6617    319    399   1180       C  
ATOM   3906  C   ARG B 709       7.645  20.864  -5.737  1.00 42.73           C  
ANISOU 3906  C   ARG B 709     3594   5982   6659    365    401   1098       C  
ATOM   3907  O   ARG B 709       8.833  20.735  -6.037  1.00 42.25           O  
ANISOU 3907  O   ARG B 709     3492   6033   6526    405    398   1175       O  
ATOM   3908  CB  ARG B 709       6.550  23.124  -5.971  1.00 61.36           C  
ANISOU 3908  CB  ARG B 709     5792   8074   9447    272    377   1112       C  
ATOM   3909  CG  ARG B 709       7.804  23.997  -5.987  1.00 81.21           C  
ANISOU 3909  CG  ARG B 709     8178  10604  12074    273    355   1167       C  
ATOM   3910  CD  ARG B 709       8.740  23.669  -4.829  1.00 97.36           C  
ANISOU 3910  CD  ARG B 709    10224  12734  14035    298    347   1042       C  
ATOM   3911  NE  ARG B 709       9.847  24.617  -4.714  1.00101.59           N  
ANISOU 3911  NE  ARG B 709    10622  13278  14698    290    321   1070       N  
ATOM   3912  CZ  ARG B 709       9.938  25.556  -3.776  1.00100.91           C  
ANISOU 3912  CZ  ARG B 709    10450  13102  14788    258    300    951       C  
ATOM   3913  NH1 ARG B 709       8.988  25.678  -2.859  1.00 90.79           N  
ANISOU 3913  NH1 ARG B 709     9204  11718  13573    233    303    794       N  
ATOM   3914  NH2 ARG B 709      10.983  26.372  -3.751  1.00109.55           N  
ANISOU 3914  NH2 ARG B 709    11416  14216  15990    250    276    985       N  
ATOM   3915  N   ILE B 710       7.098  20.272  -4.681  1.00 42.93           N  
ANISOU 3915  N   ILE B 710     3702   5998   6613    364    407    944       N  
ATOM   3916  CA  ILE B 710       7.866  19.397  -3.803  1.00 38.79           C  
ANISOU 3916  CA  ILE B 710     3228   5591   5919    414    408    862       C  
ATOM   3917  C   ILE B 710       8.408  18.186  -4.555  1.00 40.62           C  
ANISOU 3917  C   ILE B 710     3538   5970   5927    484    426    966       C  
ATOM   3918  O   ILE B 710       9.596  17.878  -4.475  1.00 45.81           O  
ANISOU 3918  O   ILE B 710     4171   6751   6482    543    425    996       O  
ATOM   3919  CB  ILE B 710       7.020  18.918  -2.605  1.00 34.21           C  
ANISOU 3919  CB  ILE B 710     2727   4972   5298    396    411    689       C  
ATOM   3920  CG1 ILE B 710       6.720  20.084  -1.662  1.00 25.39           C  
ANISOU 3920  CG1 ILE B 710     1523   3736   4387    342    394    561       C  
ATOM   3921  CG2 ILE B 710       7.731  17.799  -1.859  1.00 25.23           C  
ANISOU 3921  CG2 ILE B 710     1660   3972   3956    462    414    631       C  
ATOM   3922  CD1 ILE B 710       5.850  19.702  -0.484  1.00 19.76           C  
ANISOU 3922  CD1 ILE B 710      876   2991   3642    318    397    387       C  
ATOM   3923  N   LEU B 711       7.533  17.499  -5.284  1.00 49.41           N  
ANISOU 3923  N   LEU B 711     4738   7075   6961    482    443   1017       N  
ATOM   3924  CA  LEU B 711       7.940  16.334  -6.063  1.00 52.89           C  
ANISOU 3924  CA  LEU B 711     5254   7646   7197    551    460   1112       C  
ATOM   3925  C   LEU B 711       8.931  16.715  -7.159  1.00 54.96           C  
ANISOU 3925  C   LEU B 711     5432   7985   7464    578    461   1271       C  
ATOM   3926  O   LEU B 711       9.840  15.953  -7.478  1.00 63.21           O  
ANISOU 3926  O   LEU B 711     6499   9173   8345    653    473   1329       O  
ATOM   3927  CB  LEU B 711       6.723  15.637  -6.675  1.00 41.64           C  
ANISOU 3927  CB  LEU B 711     3924   6186   5711    535    471   1130       C  
ATOM   3928  CG  LEU B 711       7.020  14.476  -7.627  1.00 38.95           C  
ANISOU 3928  CG  LEU B 711     3656   5965   5177    605    486   1233       C  
ATOM   3929  CD1 LEU B 711       7.930  13.457  -6.963  1.00 31.44           C  
ANISOU 3929  CD1 LEU B 711     2765   5133   4047    695    493   1189       C  
ATOM   3930  CD2 LEU B 711       5.734  13.819  -8.106  1.00 44.71           C  
ANISOU 3930  CD2 LEU B 711     4473   6653   5862    584    488   1226       C  
ATOM   3931  N   ALA B 712       8.747  17.900  -7.731  1.00 48.93           N  
ANISOU 3931  N   ALA B 712     4568   7133   6889    521    450   1343       N  
ATOM   3932  CA  ALA B 712       9.619  18.383  -8.796  1.00 52.14           C  
ANISOU 3932  CA  ALA B 712     4881   7607   7322    534    447   1502       C  
ATOM   3933  C   ALA B 712      11.048  18.589  -8.298  1.00 58.61           C  
ANISOU 3933  C   ALA B 712     5625   8529   8115    574    438   1492       C  
ATOM   3934  O   ALA B 712      12.012  18.220  -8.972  1.00 55.92           O  
ANISOU 3934  O   ALA B 712     5259   8332   7657    629    447   1594       O  
ATOM   3935  CB  ALA B 712       9.070  19.667  -9.378  1.00 70.02           C  
ANISOU 3935  CB  ALA B 712     7051   9741   9814    466    432   1575       C  
ATOM   3936  N   GLU B 713      11.172  19.192  -7.119  1.00 54.93           N  
ANISOU 3936  N   GLU B 713     5115   7999   7756    548    419   1365       N  
ATOM   3937  CA  GLU B 713      12.471  19.397  -6.484  1.00 48.88           C  
ANISOU 3937  CA  GLU B 713     4274   7333   6966    586    404   1331       C  
ATOM   3938  C   GLU B 713      13.142  18.071  -6.139  1.00 57.48           C  
ANISOU 3938  C   GLU B 713     5449   8591   7801    683    422   1298       C  
ATOM   3939  O   GLU B 713      14.272  17.811  -6.552  1.00 69.05           O  
ANISOU 3939  O   GLU B 713     6871  10209   9154    748    426   1375       O  
ATOM   3940  CB  GLU B 713      12.321  20.249  -5.221  1.00 32.85           C  
ANISOU 3940  CB  GLU B 713     2188   5196   5099    538    380   1181       C  
ATOM   3941  CG  GLU B 713      12.608  21.731  -5.421  1.00 52.43           C  
ANISOU 3941  CG  GLU B 713     4518   7584   7819    478    354   1225       C  
ATOM   3942  CD  GLU B 713      14.086  22.018  -5.614  1.00 68.35           C  
ANISOU 3942  CD  GLU B 713     6425   9740   9805    512    339   1295       C  
ATOM   3943  OE1 GLU B 713      14.481  23.201  -5.536  1.00 78.00           O  
ANISOU 3943  OE1 GLU B 713     7517  10902  11218    466    312   1307       O  
ATOM   3944  OE2 GLU B 713      14.856  21.060  -5.838  1.00 70.03           O  
ANISOU 3944  OE2 GLU B 713     6678  10126   9803    588    354   1336       O  
ATOM   3945  N   ILE B 714      12.439  17.238  -5.378  1.00 49.43           N  
ANISOU 3945  N   ILE B 714     4545   7546   6689    699    431   1186       N  
ATOM   3946  CA  ILE B 714      12.950  15.928  -4.983  1.00 46.06           C  
ANISOU 3946  CA  ILE B 714     4211   7262   6026    802    446   1152       C  
ATOM   3947  C   ILE B 714      13.356  15.080  -6.190  1.00 68.14           C  
ANISOU 3947  C   ILE B 714     7051  10183   8657    874    472   1289       C  
ATOM   3948  O   ILE B 714      14.423  14.465  -6.196  1.00 77.79           O  
ANISOU 3948  O   ILE B 714     8273  11566   9718    976    481   1315       O  
ATOM   3949  CB  ILE B 714      11.917  15.150  -4.138  1.00 34.63           C  
ANISOU 3949  CB  ILE B 714     2890   5749   4520    797    451   1030       C  
ATOM   3950  CG1 ILE B 714      11.725  15.813  -2.771  1.00 42.37           C  
ANISOU 3950  CG1 ILE B 714     3828   6651   5620    748    428    876       C  
ATOM   3951  CG2 ILE B 714      12.354  13.709  -3.958  1.00 35.18           C  
ANISOU 3951  CG2 ILE B 714     3067   5954   4345    915    467   1027       C  
ATOM   3952  CD1 ILE B 714      10.666  15.152  -1.908  1.00 30.61           C  
ANISOU 3952  CD1 ILE B 714     2447   5097   4086    730    431    755       C  
ATOM   3953  N   GLU B 715      12.500  15.049  -7.208  1.00 80.06           N  
ANISOU 3953  N   GLU B 715     8593  11623  10202    830    483   1372       N  
ATOM   3954  CA  GLU B 715      12.759  14.260  -8.409  1.00 73.41           C  
ANISOU 3954  CA  GLU B 715     7790  10892   9210    892    508   1497       C  
ATOM   3955  C   GLU B 715      14.003  14.760  -9.135  1.00 75.14           C  
ANISOU 3955  C   GLU B 715     7891  11235   9424    923    508   1613       C  
ATOM   3956  O   GLU B 715      14.834  13.969  -9.583  1.00 80.25           O  
ANISOU 3956  O   GLU B 715     8557  12044   9891   1022    528   1669       O  
ATOM   3957  CB  GLU B 715      11.559  14.316  -9.356  1.00 54.81           C  
ANISOU 3957  CB  GLU B 715     5471   8435   6919    827    512   1562       C  
ATOM   3958  CG  GLU B 715      11.577  13.261 -10.449  1.00 62.36           C  
ANISOU 3958  CG  GLU B 715     6497   9495   7701    895    535   1658       C  
ATOM   3959  CD  GLU B 715      10.817  12.007 -10.059  1.00 68.55           C  
ANISOU 3959  CD  GLU B 715     7428  10263   8354    938    541   1578       C  
ATOM   3960  OE1 GLU B 715       9.627  12.120  -9.696  1.00 62.29           O  
ANISOU 3960  OE1 GLU B 715     6679   9339   7649    868    529   1506       O  
ATOM   3961  OE2 GLU B 715      11.407  10.909 -10.124  1.00 77.22           O  
ANISOU 3961  OE2 GLU B 715     8596  11480   9264   1049    556   1587       O  
ATOM   3962  N   GLU B 716      14.119  16.078  -9.250  1.00 58.99           N  
ANISOU 3962  N   GLU B 716     5722   9115   7578    842    485   1649       N  
ATOM   3963  CA  GLU B 716      15.244  16.690  -9.942  1.00 68.86           C  
ANISOU 3963  CA  GLU B 716     6843  10472   8848    855    479   1765       C  
ATOM   3964  C   GLU B 716      16.565  16.319  -9.274  1.00 69.13           C  
ANISOU 3964  C   GLU B 716     6844  10674   8748    948    477   1717       C  
ATOM   3965  O   GLU B 716      17.494  15.859  -9.935  1.00 66.94           O  
ANISOU 3965  O   GLU B 716     6541  10570   8325   1027    493   1802       O  
ATOM   3966  CB  GLU B 716      15.077  18.213  -9.991  1.00113.00           C  
ANISOU 3966  CB  GLU B 716    12308  15929  14699    752    447   1796       C  
ATOM   3967  CG  GLU B 716      15.915  18.913 -11.056  1.00133.80           C  
ANISOU 3967  CG  GLU B 716    14810  18646  17383    742    439   1956       C  
ATOM   3968  CD  GLU B 716      17.359  19.125 -10.637  1.00152.19           C  
ANISOU 3968  CD  GLU B 716    17039  21125  19663    789    425   1947       C  
ATOM   3969  OE1 GLU B 716      18.141  19.658 -11.452  1.00159.22           O  
ANISOU 3969  OE1 GLU B 716    17813  22104  20578    783    415   2075       O  
ATOM   3970  OE2 GLU B 716      17.714  18.767  -9.495  1.00157.78           O  
ANISOU 3970  OE2 GLU B 716    17776  21870  20303    833    420   1815       O  
ATOM   3971  N   LEU B 717      16.640  16.512  -7.960  1.00 93.24           N  
ANISOU 3971  N   LEU B 717     9897  13687  11843    944    458   1579       N  
ATOM   3972  CA  LEU B 717      17.887  16.300  -7.227  1.00 90.51           C  
ANISOU 3972  CA  LEU B 717     9504  13500  11385   1031    450   1526       C  
ATOM   3973  C   LEU B 717      18.344  14.842  -7.231  1.00 97.93           C  
ANISOU 3973  C   LEU B 717    10551  14603  12056   1173    479   1521       C  
ATOM   3974  O   LEU B 717      19.541  14.560  -7.243  1.00107.62           O  
ANISOU 3974  O   LEU B 717    11728  16013  13149   1272    482   1545       O  
ATOM   3975  CB  LEU B 717      17.780  16.834  -5.793  1.00 58.29           C  
ANISOU 3975  CB  LEU B 717     5399   9337   7412    993    421   1372       C  
ATOM   3976  CG  LEU B 717      16.898  16.133  -4.762  1.00 55.48           C  
ANISOU 3976  CG  LEU B 717     5171   8901   7007   1002    426   1235       C  
ATOM   3977  CD1 LEU B 717      17.597  14.910  -4.194  1.00 54.42           C  
ANISOU 3977  CD1 LEU B 717     5115   8934   6629   1144    438   1189       C  
ATOM   3978  CD2 LEU B 717      16.552  17.098  -3.642  1.00 48.95           C  
ANISOU 3978  CD2 LEU B 717     4286   7947   6367    919    395   1106       C  
ATOM   3979  N   ALA B 718      17.388  13.919  -7.219  1.00 88.55           N  
ANISOU 3979  N   ALA B 718     9508  13348  10789   1191    500   1489       N  
ATOM   3980  CA  ALA B 718      17.707  12.496  -7.251  1.00 88.51           C  
ANISOU 3980  CA  ALA B 718     9619  13473  10538   1333    528   1486       C  
ATOM   3981  C   ALA B 718      18.510  12.148  -8.502  1.00101.20           C  
ANISOU 3981  C   ALA B 718    11190  15240  12020   1409    554   1619       C  
ATOM   3982  O   ALA B 718      19.447  11.349  -8.449  1.00 96.19           O  
ANISOU 3982  O   ALA B 718    10579  14778  11192   1553    570   1623       O  
ATOM   3983  CB  ALA B 718      16.440  11.665  -7.181  1.00 58.01           C  
ANISOU 3983  CB  ALA B 718     5908   9493   6641   1321    541   1445       C  
ATOM   3984  N   ARG B 719      18.130  12.748  -9.627  1.00123.94           N  
ANISOU 3984  N   ARG B 719    14014  18068  15009   1320    557   1729       N  
ATOM   3985  CA  ARG B 719      18.857  12.573 -10.879  1.00118.75           C  
ANISOU 3985  CA  ARG B 719    13303  17563  14255   1374    579   1862       C  
ATOM   3986  C   ARG B 719      20.140  13.395 -10.875  1.00114.53           C  
ANISOU 3986  C   ARG B 719    12607  17158  13753   1383    560   1904       C  
ATOM   3987  O   ARG B 719      21.201  12.910 -11.270  1.00111.50           O  
ANISOU 3987  O   ARG B 719    12188  16973  13203   1496    577   1952       O  
ATOM   3988  CB  ARG B 719      17.992  12.992 -12.071  1.00 88.38           C  
ANISOU 3988  CB  ARG B 719     9442  13620  10519   1272    583   1971       C  
ATOM   3989  CG  ARG B 719      16.921  11.993 -12.475  1.00 76.66           C  
ANISOU 3989  CG  ARG B 719     8103  12073   8950   1288    606   1965       C  
ATOM   3990  CD  ARG B 719      16.062  12.571 -13.587  1.00 79.23           C  
ANISOU 3990  CD  ARG B 719     8396  12305   9402   1182    601   2069       C  
ATOM   3991  NE  ARG B 719      15.391  13.792 -13.150  1.00 82.85           N  
ANISOU 3991  NE  ARG B 719     8794  12585  10099   1053    569   2043       N  
ATOM   3992  CZ  ARG B 719      14.957  14.747 -13.967  1.00 81.55           C  
ANISOU 3992  CZ  ARG B 719     8549  12342  10093    961    554   2145       C  
ATOM   3993  NH1 ARG B 719      15.128  14.633 -15.277  1.00 76.90           N  
ANISOU 3993  NH1 ARG B 719     7926  11846   9447    974    568   2283       N  
ATOM   3994  NH2 ARG B 719      14.358  15.821 -13.470  1.00 78.27           N  
ANISOU 3994  NH2 ARG B 719     8086  11760   9893    863    527   2108       N  
ATOM   3995  N   GLU B 720      20.029  14.644 -10.431  1.00 99.89           N  
ANISOU 3995  N   GLU B 720    10652  15190  12112   1268    523   1884       N  
ATOM   3996  CA  GLU B 720      21.161  15.565 -10.395  1.00108.70           C  
ANISOU 3996  CA  GLU B 720    11603  16406  13290   1256    496   1923       C  
ATOM   3997  C   GLU B 720      22.374  14.937  -9.715  1.00114.81           C  
ANISOU 3997  C   GLU B 720    12363  17386  13874   1395    499   1862       C  
ATOM   3998  O   GLU B 720      23.442  14.823 -10.315  1.00123.59           O  
ANISOU 3998  O   GLU B 720    13394  18694  14871   1469    506   1941       O  
ATOM   3999  CB  GLU B 720      20.774  16.868  -9.686  1.00120.72           C  
ANISOU 3999  CB  GLU B 720    13045  17754  15067   1128    455   1867       C  
ATOM   4000  CG  GLU B 720      21.895  17.900  -9.629  1.00130.23           C  
ANISOU 4000  CG  GLU B 720    14072  19049  16360   1102    422   1904       C  
ATOM   4001  CD  GLU B 720      21.468  19.208  -8.983  1.00140.10           C  
ANISOU 4001  CD  GLU B 720    15244  20113  17876    977    383   1848       C  
ATOM   4002  OE1 GLU B 720      20.284  19.337  -8.606  1.00144.19           O  
ANISOU 4002  OE1 GLU B 720    15842  20435  18510    914    383   1781       O  
ATOM   4003  OE2 GLU B 720      22.321  20.111  -8.852  1.00144.28           O  
ANISOU 4003  OE2 GLU B 720    15625  20697  18496    946    352   1867       O  
TER    4004      GLU B 720                                                      
HETATM 4005  C10 032 A   1       9.454  -4.176 -21.735  1.00 58.37           C  
ANISOU 4005  C10 032 A   1     7138   7748   7295    865    706    658       C  
HETATM 4006  C15 032 A   1       1.934  -1.231 -18.357  1.00 37.50           C  
ANISOU 4006  C15 032 A   1     4454   5094   4699    815    677    559       C  
HETATM 4007  C17 032 A   1       1.516  -2.316 -20.597  1.00 34.06           C  
ANISOU 4007  C17 032 A   1     4037   4645   4259    832    670    564       C  
HETATM 4008  C20 032 A   1      -0.845  -3.053 -20.418  1.00 26.22           C  
ANISOU 4008  C20 032 A   1     3040   3640   3283    825    667    533       C  
HETATM 4009  C21 032 A   1      -2.207  -2.778 -20.374  1.00 27.30           C  
ANISOU 4009  C21 032 A   1     3169   3768   3436    820    661    513       C  
HETATM 4010  C22 032 A   1      -2.658  -1.461 -20.469  1.00 29.56           C  
ANISOU 4010  C22 032 A   1     3444   4049   3738    818    650    505       C  
HETATM 4011  C24 032 A   1      -0.387  -0.720 -20.649  1.00 34.82           C  
ANISOU 4011  C24 032 A   1     4117   4729   4385    825    652    536       C  
HETATM 4012  C01 032 A   1       6.130  -2.562 -19.577  1.00 50.16           C  
ANISOU 4012  C01 032 A   1     6081   6709   6270    839    690    620       C  
HETATM 4013  C02 032 A   1       6.309  -1.953 -18.333  1.00 46.22           C  
ANISOU 4013  C02 032 A   1     5572   6217   5773    830    690    618       C  
HETATM 4014  N03 032 A   1       5.354  -1.393 -17.558  1.00 44.65           N  
ANISOU 4014  N03 032 A   1     5364   6020   5580    820    688    602       N  
HETATM 4015  C04 032 A   1       4.825  -2.607 -20.089  1.00 44.14           C  
ANISOU 4015  C04 032 A   1     5319   5939   5512    839    685    605       C  
HETATM 4016  N14 032 A   1       2.999  -0.988 -17.535  1.00 34.94           N  
ANISOU 4016  N14 032 A   1     4127   4781   4368    811    682    569       N  
HETATM 4017  C16 032 A   1       2.365  -1.886 -19.491  1.00 37.77           C  
ANISOU 4017  C16 032 A   1     4501   5125   4726    826    676    571       C  
HETATM 4018  C05 032 A   1       3.781  -2.044 -19.335  1.00 42.71           C  
ANISOU 4018  C05 032 A   1     5130   5758   5341    829    681    589       C  
HETATM 4019  C06 032 A   1       4.133  -1.474 -18.114  1.00 40.72           C  
ANISOU 4019  C06 032 A   1     4868   5514   5090    820    684    588       C  
HETATM 4020  C07 032 A   1       7.269  -3.124 -20.317  1.00 54.29           C  
ANISOU 4020  C07 032 A   1     6611   7232   6787    848    694    635       C  
HETATM 4021  C18 032 A   1       0.073  -2.029 -20.549  1.00 35.44           C  
ANISOU 4021  C18 032 A   1     4206   4813   4449    827    663    544       C  
HETATM 4022  C23 032 A   1      -1.742  -0.420 -20.608  1.00 24.63           C  
ANISOU 4022  C23 032 A   1     2818   3429   3112    821    646    517       C  
HETATM 4023  F25 032 A   1       0.477   0.287 -20.782  1.00 32.98           F  
ANISOU 4023  F25 032 A   1     3880   4499   4152    828    649    548       F  
HETATM 4024  F26 032 A   1      -0.426  -4.317 -20.325  1.00 41.15           F  
ANISOU 4024  F26 032 A   1     4939   5534   5164    827    676    541       F  
HETATM 4025  N27 032 A   1      -3.116  -3.877 -20.230  1.00 36.57           N  
ANISOU 4025  N27 032 A   1     4345   4937   4614    817    666    502       N  
HETATM 4026  S28 032 A   1      -4.803  -3.571 -20.163  1.00 52.02           S  
ANISOU 4026  S28 032 A   1     6290   6882   6594    811    660    476       S  
HETATM 4027  O29 032 A   1      -5.510  -4.828 -20.031  1.00 58.84           O  
ANISOU 4027  O29 032 A   1     7157   7741   7459    809    667    468       O  
HETATM 4028  O30 032 A   1      -5.206  -2.598 -21.157  1.00 46.68           O  
ANISOU 4028  O30 032 A   1     5610   6196   5928    818    642    472       O  
HETATM 4029  C31 032 A   1      -4.997  -2.774 -18.571  1.00 50.34           C  
ANISOU 4029  C31 032 A   1     6061   6676   6388    796    669    464       C  
HETATM 4030  C32 032 A   1      -5.016  -3.720 -17.378  1.00 45.84           C  
ANISOU 4030  C32 032 A   1     5493   6116   5810    784    686    463       C  
HETATM 4031  C33 032 A   1      -4.277  -3.096 -16.205  1.00 36.76           C  
ANISOU 4031  C33 032 A   1     4336   4981   4651    774    694    467       C  
HETATM 4032  C08 032 A   1       7.146  -4.319 -21.047  1.00 58.69           C  
ANISOU 4032  C08 032 A   1     7177   7784   7340    854    699    634       C  
HETATM 4033  C09 032 A   1       8.232  -4.846 -21.751  1.00 62.06           C  
ANISOU 4033  C09 032 A   1     7608   8210   7763    863    704    646       C  
HETATM 4034  C11 032 A   1       9.603  -2.986 -21.024  1.00 48.54           C  
ANISOU 4034  C11 032 A   1     5884   6507   6053    859    701    660       C  
HETATM 4035  C12 032 A   1       8.514  -2.465 -20.323  1.00 48.21           C  
ANISOU 4035  C12 032 A   1     5838   6466   6016    851    695    648       C  
HETATM 4036 CL13 032 A   1      10.795  -4.820 -22.601  1.00 67.34          CL  
ANISOU 4036 CL13 032 A   1     8277   8881   8427    874    716    670      CL  
HETATM 4037  O19 032 A   1       1.942  -2.898 -21.592  1.00 44.03           O  
ANISOU 4037  O19 032 A   1     5310   5906   5513    841    669    573       O  
HETATM 4038  O   HOH A   2       0.360  16.940 -13.833  1.00 40.98           O  
HETATM 4039  O   HOH A   3       2.005  15.274 -12.586  1.00 30.57           O  
HETATM 4040  O   HOH A   4     -13.511 -22.832 -23.981  1.00 39.87           O  
HETATM 4041  O   HOH A   6       0.867 -11.911  -3.812  1.00 44.63           O  
HETATM 4042  O   HOH A   8      -5.183 -34.159 -22.465  1.00 38.38           O  
HETATM 4043  O   HOH A   9       3.930  14.572 -24.093  1.00 40.22           O  
HETATM 4044  O   HOH A  10       1.828  -2.294  -7.449  1.00 37.13           O  
HETATM 4045  O   HOH A  11      -4.005  14.772 -11.681  1.00 32.36           O  
HETATM 4046  O   HOH A  12       6.390 -29.427 -26.758  1.00 41.79           O  
HETATM 4047  O   HOH A  14      -6.101  -2.762 -12.175  1.00 39.53           O  
HETATM 4048  O   HOH A  16      -1.879  -3.895  -8.749  1.00 30.41           O  
HETATM 4049  O   HOH A  18      -8.548  -2.696 -26.046  1.00 47.49           O  
HETATM 4050  O   HOH A  20      -3.785  -9.253 -25.705  1.00 46.01           O  
HETATM 4051  O   HOH A  21      16.340 -31.115 -12.651  1.00 41.06           O  
HETATM 4052  O   HOH A  22      -5.509  11.875 -32.293  1.00 46.72           O  
HETATM 4053  O   HOH A  24       5.197   6.147  -9.813  1.00 29.78           O  
HETATM 4054  O   HOH A  27      -7.854 -34.790 -22.552  1.00 42.30           O  
HETATM 4055  O   HOH A  30      -5.696 -16.885 -22.039  1.00 48.97           O  
HETATM 4056  O   HOH A  31       7.673 -36.608 -19.395  1.00 50.79           O  
HETATM 4057  O   HOH A  33       5.170  15.557 -14.306  1.00 47.62           O  
HETATM 4058  O   HOH A  34       4.998 -31.492 -28.256  1.00 42.34           O  
HETATM 4059  O   HOH A  35      15.920 -32.753 -24.273  1.00 40.77           O  
HETATM 4060  O   HOH A  36       9.546 -24.321 -40.057  1.00 46.22           O  
HETATM 4061  O   HOH A  37      -2.526  17.771 -25.929  1.00 54.56           O  
HETATM 4062  O   HOH A  38      -9.772  -5.366 -25.824  1.00 45.12           O  
HETATM 4063  O   HOH A  39       5.492  13.472 -12.162  1.00 42.35           O  
HETATM 4064  O   HOH A  41     -14.092  -6.655  -4.439  1.00 53.07           O  
HETATM 4065  O   HOH A  42     -12.352 -27.678 -10.451  1.00 49.39           O  
HETATM 4066  O   HOH A  43      -4.036  13.051 -21.132  1.00 52.40           O  
HETATM 4067  O   HOH A  44      -0.199  -4.656 -23.816  1.00 50.79           O  
HETATM 4068  O   HOH A  45       5.160  -4.881  -5.594  1.00 47.83           O  
HETATM 4069  O   HOH A  48      -0.633 -25.278 -27.127  1.00 39.34           O  
HETATM 4070  O   HOH A  50     -11.830 -28.620 -25.249  1.00 52.78           O  
HETATM 4071  O   HOH A  51      -7.910 -17.735 -23.546  1.00 45.58           O  
HETATM 4072  O   HOH A  52     -10.338  -6.242  -5.139  1.00 50.32           O  
HETATM 4073  O   HOH A  54      -0.578 -12.778 -35.991  1.00 50.01           O  
HETATM 4074  O   HOH A  55      16.952 -16.829  -9.137  1.00 53.43           O  
HETATM 4075  O   HOH A  60     -15.980   7.136 -10.552  1.00 47.31           O  
HETATM 4076  O   HOH A  62      -2.852 -33.094 -23.100  1.00 48.62           O  
HETATM 4077  O   HOH A  63       2.512   7.223 -10.680  1.00 46.70           O  
HETATM 4078  O   HOH A  65      11.955 -25.800  -0.711  1.00 54.40           O  
HETATM 4079  O   HOH B   1      14.536  18.696  16.878  1.00 23.21           O  
HETATM 4080  O   HOH B   5      -0.877  14.664   7.294  1.00 44.41           O  
HETATM 4081  O   HOH B   7      -5.962   2.219  -3.236  1.00 30.07           O  
HETATM 4082  O   HOH B  13       6.789   4.962  -7.425  1.00 46.59           O  
HETATM 4083  O   HOH B  15       1.834   4.767  -9.677  1.00 42.68           O  
HETATM 4084  O   HOH B  17      -0.216  20.113  -2.800  1.00 45.19           O  
HETATM 4085  O   HOH B  19       8.272  -6.177  -5.901  1.00 42.15           O  
HETATM 4086  O   HOH B  23      22.940  -0.393  13.996  1.00 47.25           O  
HETATM 4087  O   HOH B  25       0.950  28.083  10.877  1.00 49.80           O  
HETATM 4088  O   HOH B  26      -1.376  -9.028  -1.082  1.00 36.26           O  
HETATM 4089  O   HOH B  28      -4.064  24.988  -0.861  1.00 48.71           O  
HETATM 4090  O   HOH B  29      -8.586  -1.448  19.578  1.00 44.20           O  
HETATM 4091  O   HOH B  32      13.291  24.361  11.853  1.00 39.32           O  
HETATM 4092  O   HOH B  40      -5.555 -16.168   6.791  1.00 33.45           O  
HETATM 4093  O   HOH B  46       7.558  15.859 -11.119  1.00 42.89           O  
HETATM 4094  O   HOH B  47       7.719  23.926  13.673  1.00 53.06           O  
HETATM 4095  O   HOH B  49      -2.476  17.278   7.928  1.00 52.96           O  
HETATM 4096  O   HOH B  53     -25.538   3.505   5.568  1.00 48.24           O  
HETATM 4097  O   HOH B  56       5.525  17.424 -10.280  1.00 48.83           O  
HETATM 4098  O   HOH B  57      -5.917   0.403   6.784  1.00 30.36           O  
HETATM 4099  O   HOH B  58      -6.808   3.070   5.455  1.00 29.95           O  
HETATM 4100  O   HOH B  59       6.684  19.126  14.868  1.00 50.57           O  
HETATM 4101  O   HOH B  61      -3.939  -1.249   7.650  1.00 55.05           O  
HETATM 4102  O   HOH B  64      -3.259   2.234  -4.675  1.00 50.29           O  
CONECT 4005 4033 4034 4036                                                      
CONECT 4006 4016 4017                                                           
CONECT 4007 4017 4021 4037                                                      
CONECT 4008 4009 4021 4024                                                      
CONECT 4009 4008 4010 4025                                                      
CONECT 4010 4009 4022                                                           
CONECT 4011 4021 4022 4023                                                      
CONECT 4012 4013 4015 4020                                                      
CONECT 4013 4012 4014                                                           
CONECT 4014 4013 4019                                                           
CONECT 4015 4012 4018                                                           
CONECT 4016 4006 4019                                                           
CONECT 4017 4006 4007 4018                                                      
CONECT 4018 4015 4017 4019                                                      
CONECT 4019 4014 4016 4018                                                      
CONECT 4020 4012 4032 4035                                                      
CONECT 4021 4007 4008 4011                                                      
CONECT 4022 4010 4011                                                           
CONECT 4023 4011                                                                
CONECT 4024 4008                                                                
CONECT 4025 4009 4026                                                           
CONECT 4026 4025 4027 4028 4029                                                 
CONECT 4027 4026                                                                
CONECT 4028 4026                                                                
CONECT 4029 4026 4030                                                           
CONECT 4030 4029 4031                                                           
CONECT 4031 4030                                                                
CONECT 4032 4020 4033                                                           
CONECT 4033 4005 4032                                                           
CONECT 4034 4005 4035                                                           
CONECT 4035 4020 4034                                                           
CONECT 4036 4005                                                                
CONECT 4037 4007                                                                
MASTER      381    0    1   21   15    0    4    6 4100    2   33   46          
END