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Browse entries in the PDBbind-CN Database

HEADER    APOPTOSIS                               13-JAN-11   3QBR              
TITLE     BAKBH3 IN COMPLEX WITH SJA                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SJCHGC06286 PROTEIN;                                       
COMPND   3 CHAIN: A, X;                                                         
COMPND   4 FRAGMENT: C-TERMINAL TRUNCATION (RESIDUES 21-189);                   
COMPND   5 SYNONYM: SJA;                                                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: BCL-2 HOMOLOGOUS ANTAGONIST/KILLER;                        
COMPND   9 CHAIN: B, Y;                                                         
COMPND  10 FRAGMENT: BH3 (UNP RESIDUES 63-96);                                  
COMPND  11 SYNONYM: APOPTOSIS REGULATOR BAK, BCL-2-LIKE PROTEIN 7, BCL2-L-7;    
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SCHISTOSOMA JAPONICUM;                          
SOURCE   3 ORGANISM_COMMON: BLOOD FLUKE;                                        
SOURCE   4 ORGANISM_TAXID: 6182;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PDUET;                                    
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 SYNTHETIC: YES;                                                      
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 OTHER_DETAILS: SYNTHETIC PEPTIDE                                     
KEYWDS    HELICAL BUNDLE, BCL-2-LIKE FOLD, APOPTOSIS                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.F.LEE,O.B.CLARKE,W.D.FAIRLIE,P.M.COLMAN,M.EVANGELISTA,Z.FENG,       
AUTHOR   2 T.P.SPEED,E.TCHOUBRIEVA,A.STRASSER,B.KALINNA                         
REVDAT   3   08-NOV-17 3QBR    1       REMARK                                   
REVDAT   2   26-JUN-13 3QBR    1       JRNL   VERSN                             
REVDAT   1   13-APR-11 3QBR    0                                                
JRNL        AUTH   E.F.LEE,O.B.CLARKE,M.EVANGELISTA,Z.FENG,T.P.SPEED,           
JRNL        AUTH 2 E.B.TCHOUBRIEVA,A.STRASSER,B.H.KALINNA,P.M.COLMAN,           
JRNL        AUTH 3 W.D.FAIRLIE                                                  
JRNL        TITL   DISCOVERY AND MOLECULAR CHARACTERIZATION OF A                
JRNL        TITL 2 BCL-2-REGULATED CELL DEATH PATHWAY IN SCHISTOSOMES.          
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 108  6999 2011              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   21444803                                                     
JRNL        DOI    10.1073/PNAS.1100652108                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX                                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.15                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.030                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 16303                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.178                           
REMARK   3   R VALUE            (WORKING SET) : 0.171                           
REMARK   3   FREE R VALUE                     : 0.234                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.050                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 1639                            
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 29.1496 -  5.9404    1.00     1315   151  0.1567 0.1973        
REMARK   3     2  5.9404 -  4.7216    1.00     1299   145  0.1579 0.2240        
REMARK   3     3  4.7216 -  4.1266    1.00     1253   142  0.1363 0.2069        
REMARK   3     4  4.1266 -  3.7502    0.99     1266   140  0.1618 0.1977        
REMARK   3     5  3.7502 -  3.4818    0.99     1243   141  0.1703 0.2358        
REMARK   3     6  3.4818 -  3.2769    0.98     1245   141  0.1816 0.2724        
REMARK   3     7  3.2769 -  3.1129    0.97     1221   138  0.2000 0.2891        
REMARK   3     8  3.1129 -  2.9776    0.95     1205   132  0.2053 0.2788        
REMARK   3     9  2.9776 -  2.8630    0.95     1178   134  0.1990 0.2843        
REMARK   3    10  2.8630 -  2.7643    0.93     1171   128  0.2088 0.2937        
REMARK   3    11  2.7643 -  2.6780    0.93     1173   125  0.2026 0.2742        
REMARK   3    12  2.6780 -  2.6015    0.88     1095   122  0.2160 0.3072        
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              : 0.35                                          
REMARK   3   B_SOL              : 79.28                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 2.360            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL             
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.00000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.009           3015                                  
REMARK   3   ANGLE     :  1.127           4084                                  
REMARK   3   CHIRALITY :  0.072            468                                  
REMARK   3   PLANARITY :  0.004            519                                  
REMARK   3   DIHEDRAL  : 17.048           1073                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  52.2147  10.6809  54.3188              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2610 T22:   0.4287                                     
REMARK   3      T33:   0.2595 T12:   0.0072                                     
REMARK   3      T13:   0.0715 T23:   0.0332                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3310 L22:   2.1498                                     
REMARK   3      L33:   2.8793 L12:   0.5020                                     
REMARK   3      L13:   0.9433 L23:  -0.0159                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0535 S12:   0.0415 S13:   0.0054                       
REMARK   3      S21:  -0.1613 S22:  -0.0799 S23:  -0.0474                       
REMARK   3      S31:  -0.0233 S32:   0.2536 S33:   0.0000                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN B                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  58.0987   4.5354  41.3171              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6353 T22:   0.8789                                     
REMARK   3      T33:   0.4363 T12:   0.1334                                     
REMARK   3      T13:   0.1638 T23:   0.0918                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1444 L22:   0.0573                                     
REMARK   3      L33:   0.2877 L12:  -0.1232                                     
REMARK   3      L13:   0.1745 L23:  -0.0062                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1244 S12:   0.4225 S13:  -0.0972                       
REMARK   3      S21:  -0.6020 S22:   0.1516 S23:  -0.0010                       
REMARK   3      S31:   0.2312 S32:   0.4550 S33:   0.0000                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN X                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  15.1302  17.2239  50.0572              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3839 T22:   0.3630                                     
REMARK   3      T33:   0.4557 T12:   0.0262                                     
REMARK   3      T13:   0.0301 T23:  -0.1058                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8826 L22:   2.7314                                     
REMARK   3      L33:   1.7446 L12:  -0.7737                                     
REMARK   3      L13:  -0.2182 L23:  -0.0405                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0901 S12:   0.1564 S13:  -0.1166                       
REMARK   3      S21:  -0.3978 S22:  -0.1939 S23:  -0.0919                       
REMARK   3      S31:   0.1378 S32:  -0.0067 S33:   0.0000                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN Y                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   1.7874  20.1529  57.4195              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4655 T22:   0.4896                                     
REMARK   3      T33:   0.5857 T12:  -0.0419                                     
REMARK   3      T13:   0.0466 T23:  -0.1263                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1818 L22:   0.1310                                     
REMARK   3      L33:   0.3080 L12:  -0.1513                                     
REMARK   3      L13:  -0.1227 L23:   0.3404                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3618 S12:  -0.0257 S13:   0.2243                       
REMARK   3      S21:  -0.0303 S22:   0.1363 S23:   0.9375                       
REMARK   3      S31:   0.1542 S32:  -0.1205 S33:  -0.0000                       
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 3QBR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-JAN-11.                  
REMARK 100 THE DEPOSITION ID IS D_1000063444.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-AUG-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 9.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : AUSTRALIAN SYNCHROTRON             
REMARK 200  BEAMLINE                       : MX2                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.991874, 1.009234                 
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS, SCALA                         
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 16915                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 14.60                              
REMARK 200  R MERGE                    (I) : 0.06900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 33.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.74                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 14.40                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.94600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SHELXCD                                               
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.27                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.81                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1M TRI-SODIUM CITRATE, 0.1M CHES, PH     
REMARK 280  9.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 3                            
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   Z,X,Y                                                   
REMARK 290       6555   Z,-X,-Y                                                 
REMARK 290       7555   -Z,-X,Y                                                 
REMARK 290       8555   -Z,X,-Y                                                 
REMARK 290       9555   Y,Z,X                                                   
REMARK 290      10555   -Y,Z,-X                                                 
REMARK 290      11555   Y,-Z,-X                                                 
REMARK 290      12555   -Y,-Z,X                                                 
REMARK 290      13555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290      14555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290      15555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290      16555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290      17555   Z+1/2,X+1/2,Y+1/2                                       
REMARK 290      18555   Z+1/2,-X+1/2,-Y+1/2                                     
REMARK 290      19555   -Z+1/2,-X+1/2,Y+1/2                                     
REMARK 290      20555   -Z+1/2,X+1/2,-Y+1/2                                     
REMARK 290      21555   Y+1/2,Z+1/2,X+1/2                                       
REMARK 290      22555   -Y+1/2,Z+1/2,-X+1/2                                     
REMARK 290      23555   Y+1/2,-Z+1/2,-X+1/2                                     
REMARK 290      24555   -Y+1/2,-Z+1/2,X+1/2                                     
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY2   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   6  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY2   6 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY2   7 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY2   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   9  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   9  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY3   9  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  10  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  10  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY3  10 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY3  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  12  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY3  12  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  13  1.000000  0.000000  0.000000       74.31250            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       74.31250            
REMARK 290   SMTRY3  13  0.000000  0.000000  1.000000       74.31250            
REMARK 290   SMTRY1  14 -1.000000  0.000000  0.000000       74.31250            
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000       74.31250            
REMARK 290   SMTRY3  14  0.000000  0.000000  1.000000       74.31250            
REMARK 290   SMTRY1  15 -1.000000  0.000000  0.000000       74.31250            
REMARK 290   SMTRY2  15  0.000000  1.000000  0.000000       74.31250            
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000       74.31250            
REMARK 290   SMTRY1  16  1.000000  0.000000  0.000000       74.31250            
REMARK 290   SMTRY2  16  0.000000 -1.000000  0.000000       74.31250            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000       74.31250            
REMARK 290   SMTRY1  17  0.000000  0.000000  1.000000       74.31250            
REMARK 290   SMTRY2  17  1.000000  0.000000  0.000000       74.31250            
REMARK 290   SMTRY3  17  0.000000  1.000000  0.000000       74.31250            
REMARK 290   SMTRY1  18  0.000000  0.000000  1.000000       74.31250            
REMARK 290   SMTRY2  18 -1.000000  0.000000  0.000000       74.31250            
REMARK 290   SMTRY3  18  0.000000 -1.000000  0.000000       74.31250            
REMARK 290   SMTRY1  19  0.000000  0.000000 -1.000000       74.31250            
REMARK 290   SMTRY2  19 -1.000000  0.000000  0.000000       74.31250            
REMARK 290   SMTRY3  19  0.000000  1.000000  0.000000       74.31250            
REMARK 290   SMTRY1  20  0.000000  0.000000 -1.000000       74.31250            
REMARK 290   SMTRY2  20  1.000000  0.000000  0.000000       74.31250            
REMARK 290   SMTRY3  20  0.000000 -1.000000  0.000000       74.31250            
REMARK 290   SMTRY1  21  0.000000  1.000000  0.000000       74.31250            
REMARK 290   SMTRY2  21  0.000000  0.000000  1.000000       74.31250            
REMARK 290   SMTRY3  21  1.000000  0.000000  0.000000       74.31250            
REMARK 290   SMTRY1  22  0.000000 -1.000000  0.000000       74.31250            
REMARK 290   SMTRY2  22  0.000000  0.000000  1.000000       74.31250            
REMARK 290   SMTRY3  22 -1.000000  0.000000  0.000000       74.31250            
REMARK 290   SMTRY1  23  0.000000  1.000000  0.000000       74.31250            
REMARK 290   SMTRY2  23  0.000000  0.000000 -1.000000       74.31250            
REMARK 290   SMTRY3  23 -1.000000  0.000000  0.000000       74.31250            
REMARK 290   SMTRY1  24  0.000000 -1.000000  0.000000       74.31250            
REMARK 290   SMTRY2  24  0.000000  0.000000 -1.000000       74.31250            
REMARK 290   SMTRY3  24  1.000000  0.000000  0.000000       74.31250            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1870 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 9340 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1720 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 9520 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: X, Y                                  
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     HIS A    -9                                                      
REMARK 465     HIS A    -8                                                      
REMARK 465     HIS A    -7                                                      
REMARK 465     HIS A    -6                                                      
REMARK 465     HIS A    -5                                                      
REMARK 465     HIS A    -4                                                      
REMARK 465     SER A    -3                                                      
REMARK 465     GLN A    -2                                                      
REMARK 465     ASP A    -1                                                      
REMARK 465     PRO A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     ASN A     3                                                      
REMARK 465     THR A     4                                                      
REMARK 465     ALA A     5                                                      
REMARK 465     ARG A   169                                                      
REMARK 465     LEU B    -3                                                      
REMARK 465     PRO B    -2                                                      
REMARK 465     LEU B    -1                                                      
REMARK 465     GLN B     0                                                      
REMARK 465     PRO B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     PHE B    27                                                      
REMARK 465     GLN B    28                                                      
REMARK 465     THR B    29                                                      
REMARK 465     MET B    30                                                      
REMARK 465     HIS X    -9                                                      
REMARK 465     HIS X    -8                                                      
REMARK 465     HIS X    -7                                                      
REMARK 465     HIS X    -6                                                      
REMARK 465     HIS X    -5                                                      
REMARK 465     HIS X    -4                                                      
REMARK 465     SER X    -3                                                      
REMARK 465     GLN X    -2                                                      
REMARK 465     ASP X    -1                                                      
REMARK 465     PRO X     0                                                      
REMARK 465     MET X     1                                                      
REMARK 465     SER X     2                                                      
REMARK 465     LYS X    25                                                      
REMARK 465     GLN X    26                                                      
REMARK 465     ASP X    27                                                      
REMARK 465     ASP X    36                                                      
REMARK 465     ASN X    37                                                      
REMARK 465     ARG X   169                                                      
REMARK 465     LEU Y    -3                                                      
REMARK 465     PRO Y    -2                                                      
REMARK 465     LEU Y    -1                                                      
REMARK 465     GLN Y     0                                                      
REMARK 465     PRO Y     1                                                      
REMARK 465     SER Y     2                                                      
REMARK 465     SER Y     3                                                      
REMARK 465     PHE Y    27                                                      
REMARK 465     GLN Y    28                                                      
REMARK 465     THR Y    29                                                      
REMARK 465     MET Y    30                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OE1  GLN X    10     O    HOH X   219              2.08            
REMARK 500   N    ASN X    47     O    HOH X   204              2.12            
REMARK 500   OE2  GLU X    98     O    HOH X   215              2.13            
REMARK 500   OD1  ASP X    82     CG   ARG X   125              2.16            
REMARK 500   O    HOH X   218     O    HOH Y    31              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PRO A  86      127.37    -39.84                                   
REMARK 500    PRO X  46      -72.36    -32.79                                   
REMARK 500    ASN X  47       46.53   -102.51                                   
REMARK 500    GLN X  68      -19.29    -46.54                                   
REMARK 500    SER X  78       -9.32    -51.17                                   
REMARK 500    PRO X  86      154.65    -32.23                                   
REMARK 500    LYS X 128        8.99    -61.89                                   
REMARK 500    ASP X 158       17.84     82.07                                   
REMARK 500    SER Y  25       62.31   -157.91                                   
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 NHE X 170                 
DBREF  3QBR A    1   169  UNP    Q5BWX6   Q5BWX6_SCHJA    21    189             
DBREF  3QBR B   -3    30  UNP    Q16611   BAK_HUMAN       63     96             
DBREF  3QBR X    1   169  UNP    Q5BWX6   Q5BWX6_SCHJA    21    189             
DBREF  3QBR Y   -3    30  UNP    Q16611   BAK_HUMAN       63     96             
SEQADV 3QBR HIS A   -9  UNP  Q5BWX6              EXPRESSION TAG                 
SEQADV 3QBR HIS A   -8  UNP  Q5BWX6              EXPRESSION TAG                 
SEQADV 3QBR HIS A   -7  UNP  Q5BWX6              EXPRESSION TAG                 
SEQADV 3QBR HIS A   -6  UNP  Q5BWX6              EXPRESSION TAG                 
SEQADV 3QBR HIS A   -5  UNP  Q5BWX6              EXPRESSION TAG                 
SEQADV 3QBR HIS A   -4  UNP  Q5BWX6              EXPRESSION TAG                 
SEQADV 3QBR SER A   -3  UNP  Q5BWX6              EXPRESSION TAG                 
SEQADV 3QBR GLN A   -2  UNP  Q5BWX6              EXPRESSION TAG                 
SEQADV 3QBR ASP A   -1  UNP  Q5BWX6              EXPRESSION TAG                 
SEQADV 3QBR PRO A    0  UNP  Q5BWX6              EXPRESSION TAG                 
SEQADV 3QBR HIS X   -9  UNP  Q5BWX6              EXPRESSION TAG                 
SEQADV 3QBR HIS X   -8  UNP  Q5BWX6              EXPRESSION TAG                 
SEQADV 3QBR HIS X   -7  UNP  Q5BWX6              EXPRESSION TAG                 
SEQADV 3QBR HIS X   -6  UNP  Q5BWX6              EXPRESSION TAG                 
SEQADV 3QBR HIS X   -5  UNP  Q5BWX6              EXPRESSION TAG                 
SEQADV 3QBR HIS X   -4  UNP  Q5BWX6              EXPRESSION TAG                 
SEQADV 3QBR SER X   -3  UNP  Q5BWX6              EXPRESSION TAG                 
SEQADV 3QBR GLN X   -2  UNP  Q5BWX6              EXPRESSION TAG                 
SEQADV 3QBR ASP X   -1  UNP  Q5BWX6              EXPRESSION TAG                 
SEQADV 3QBR PRO X    0  UNP  Q5BWX6              EXPRESSION TAG                 
SEQRES   1 A  179  HIS HIS HIS HIS HIS HIS SER GLN ASP PRO MET SER ASN          
SEQRES   2 A  179  THR ALA ASP PHE ARG LEU GLN THR SER THR LEU CYS HIS          
SEQRES   3 A  179  SER PHE LEU LEU ALA SER ALA ASN LYS GLN ASP THR ASP          
SEQRES   4 A  179  TYR LEU THR ASP LEU LEU ASP ASN THR ASN ILE ASP LEU          
SEQRES   5 A  179  THR CYS VAL PRO ASN GLY GLN GLU ILE ILE HIS SER LEU          
SEQRES   6 A  179  LEU GLN LEU VAL GLY ASP PHE ASN GLN ARG PHE SER GLN          
SEQRES   7 A  179  THR HIS GLU ILE GLU PRO VAL ALA GLN SER LEU GLY ILE          
SEQRES   8 A  179  ASP SER ASP LYS PRO VAL ASP LYS THR ALA LEU GLU ILE          
SEQRES   9 A  179  PHE TYR LEU GLU ILE LEU ASN GLY LEU PHE GLU LYS LEU          
SEQRES  10 A  179  ASN TRP GLY ARG ILE VAL ALA MET PHE ALA PHE LEU ARG          
SEQRES  11 A  179  ILE LEU VAL LEU ARG LEU SER LYS HIS GLY HIS SER ASP          
SEQRES  12 A  179  ALA ILE GLN MET LEU ILE LYS THR THR SER GLN TYR SER          
SEQRES  13 A  179  ASP GLU LYS LEU LYS ASN TRP ILE ASN LEU HIS ASP GLY          
SEQRES  14 A  179  TRP SER GLY LEU ILE GLU PHE SER GLY ARG                      
SEQRES   1 B   34  LEU PRO LEU GLN PRO SER SER THR MET GLY GLN VAL GLY          
SEQRES   2 B   34  ARG GLN LEU ALA ILE ILE GLY ASP ASP ILE ASN ARG ARG          
SEQRES   3 B   34  TYR ASP SER GLU PHE GLN THR MET                              
SEQRES   1 X  179  HIS HIS HIS HIS HIS HIS SER GLN ASP PRO MET SER ASN          
SEQRES   2 X  179  THR ALA ASP PHE ARG LEU GLN THR SER THR LEU CYS HIS          
SEQRES   3 X  179  SER PHE LEU LEU ALA SER ALA ASN LYS GLN ASP THR ASP          
SEQRES   4 X  179  TYR LEU THR ASP LEU LEU ASP ASN THR ASN ILE ASP LEU          
SEQRES   5 X  179  THR CYS VAL PRO ASN GLY GLN GLU ILE ILE HIS SER LEU          
SEQRES   6 X  179  LEU GLN LEU VAL GLY ASP PHE ASN GLN ARG PHE SER GLN          
SEQRES   7 X  179  THR HIS GLU ILE GLU PRO VAL ALA GLN SER LEU GLY ILE          
SEQRES   8 X  179  ASP SER ASP LYS PRO VAL ASP LYS THR ALA LEU GLU ILE          
SEQRES   9 X  179  PHE TYR LEU GLU ILE LEU ASN GLY LEU PHE GLU LYS LEU          
SEQRES  10 X  179  ASN TRP GLY ARG ILE VAL ALA MET PHE ALA PHE LEU ARG          
SEQRES  11 X  179  ILE LEU VAL LEU ARG LEU SER LYS HIS GLY HIS SER ASP          
SEQRES  12 X  179  ALA ILE GLN MET LEU ILE LYS THR THR SER GLN TYR SER          
SEQRES  13 X  179  ASP GLU LYS LEU LYS ASN TRP ILE ASN LEU HIS ASP GLY          
SEQRES  14 X  179  TRP SER GLY LEU ILE GLU PHE SER GLY ARG                      
SEQRES   1 Y   34  LEU PRO LEU GLN PRO SER SER THR MET GLY GLN VAL GLY          
SEQRES   2 Y   34  ARG GLN LEU ALA ILE ILE GLY ASP ASP ILE ASN ARG ARG          
SEQRES   3 Y   34  TYR ASP SER GLU PHE GLN THR MET                              
HET    NHE  X 170      23                                                       
HETNAM     NHE 2-[N-CYCLOHEXYLAMINO]ETHANE SULFONIC ACID                        
HETSYN     NHE N-CYCLOHEXYLTAURINE; CHES                                        
FORMUL   5  NHE    C8 H17 N O3 S                                                
FORMUL   6  HOH   *146(H2 O)                                                    
HELIX    1   1 ASP A    6  SER A   22  1                                  17    
HELIX    2   2 ASN A   24  ASN A   39  1                                  16    
HELIX    3   3 ASN A   47  HIS A   70  1                                  24    
HELIX    4   4 ILE A   72  GLY A   80  1                                   9    
HELIX    5   5 ASP A   88  PHE A  104  1                                  17    
HELIX    6   6 ASN A  108  LYS A  128  1                                  21    
HELIX    7   7 HIS A  131  LEU A  150  1                                  20    
HELIX    8   8 LEU A  150  LEU A  156  1                                   7    
HELIX    9   9 HIS A  157  TRP A  160  5                                   4    
HELIX   10  10 SER A  161  SER A  167  1                                   7    
HELIX   11  11 SER B    3  TYR B   23  1                                  21    
HELIX   12  12 ASP X    6  SER X   22  1                                  17    
HELIX   13  13 THR X   28  ASP X   33  1                                   6    
HELIX   14  14 ASP X   41  VAL X   45  5                                   5    
HELIX   15  15 ASN X   47  GLN X   68  1                                  22    
HELIX   16  16 GLU X   71  SER X   78  1                                   8    
HELIX   17  17 ASP X   88  PHE X  104  1                                  17    
HELIX   18  18 ASN X  108  LEU X  126  1                                  19    
HELIX   19  19 HIS X  131  LEU X  150  1                                  20    
HELIX   20  20 LEU X  150  HIS X  157  1                                   8    
HELIX   21  21 ASP X  158  TRP X  160  5                                   3    
HELIX   22  22 SER X  161  GLY X  168  1                                   8    
HELIX   23  23 THR Y    4  TYR Y   23  1                                  20    
SSBOND   1 CYS A   44    CYS X   44                          1555   1555  2.04  
SITE     1 AC1  7 HIS X  70  PRO X  74  SER X  78  HOH X 180                    
SITE     2 AC1  7 HOH X 201  HOH Y  38  HOH Y 152                               
CRYST1  148.625  148.625  148.625  90.00  90.00  90.00 I 2 3        48          
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      0.006728  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006728  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006728        0.00000                         
ATOM      1  N   ASP A   6      35.110  18.425  51.444  1.00 59.23           N  
ANISOU    1  N   ASP A   6     6436   8154   7914    949   -228   -128       N  
ATOM      2  CA  ASP A   6      36.273  19.201  51.044  1.00 69.88           C  
ANISOU    2  CA  ASP A   6     8024   9351   9177    928   -253    -84       C  
ATOM      3  C   ASP A   6      37.501  18.305  50.924  1.00 72.13           C  
ANISOU    3  C   ASP A   6     8415   9661   9331    763   -163    -14       C  
ATOM      4  O   ASP A   6      37.797  17.537  51.839  1.00 72.33           O  
ANISOU    4  O   ASP A   6     8360   9793   9328    692    -28    -34       O  
ATOM      5  CB  ASP A   6      36.562  20.283  52.063  1.00 78.95           C  
ANISOU    5  CB  ASP A   6     9205  10450  10342   1010   -184   -165       C  
ATOM      6  CG  ASP A   6      37.921  20.882  51.871  1.00 86.33           C  
ANISOU    6  CG  ASP A   6    10369  11260  11172    932   -178   -112       C  
ATOM      7  OD1 ASP A   6      38.095  21.640  50.896  1.00 98.47           O  
ANISOU    7  OD1 ASP A   6    12066  12652  12695    953   -314    -57       O  
ATOM      8  OD2 ASP A   6      38.818  20.585  52.680  1.00 85.71           O  
ANISOU    8  OD2 ASP A   6    10310  11234  11021    838    -46   -117       O  
ATOM      9  N   PHE A   7      38.228  18.420  49.814  1.00 66.71           N  
ANISOU    9  N   PHE A   7     7910   8878   8561    707   -238     68       N  
ATOM     10  CA  PHE A   7      39.264  17.441  49.483  1.00 55.52           C  
ANISOU   10  CA  PHE A   7     6570   7499   7027    573   -165    130       C  
ATOM     11  C   PHE A   7      40.475  17.567  50.402  1.00 52.94           C  
ANISOU   11  C   PHE A   7     6283   7193   6638    512    -25    121       C  
ATOM     12  O   PHE A   7      40.988  16.571  50.897  1.00 50.26           O  
ANISOU   12  O   PHE A   7     5898   6943   6257    439     76    126       O  
ATOM     13  CB  PHE A   7      39.664  17.526  47.995  1.00 48.90           C  
ANISOU   13  CB  PHE A   7     5907   6571   6101    532   -270    212       C  
ATOM     14  CG  PHE A   7      40.714  16.519  47.577  1.00 42.44           C  
ANISOU   14  CG  PHE A   7     5165   5801   5161    420   -188    258       C  
ATOM     15  CD1 PHE A   7      40.349  15.250  47.145  1.00 41.43           C  
ANISOU   15  CD1 PHE A   7     5001   5728   5013    384   -203    265       C  
ATOM     16  CD2 PHE A   7      42.064  16.856  47.592  1.00 41.89           C  
ANISOU   16  CD2 PHE A   7     5203   5717   4997    355   -103    292       C  
ATOM     17  CE1 PHE A   7      41.326  14.310  46.751  1.00 41.83           C  
ANISOU   17  CE1 PHE A   7     5132   5809   4951    308   -129    292       C  
ATOM     18  CE2 PHE A   7      43.051  15.937  47.200  1.00 44.63           C  
ANISOU   18  CE2 PHE A   7     5599   6121   5237    277    -21    323       C  
ATOM     19  CZ  PHE A   7      42.684  14.662  46.784  1.00 42.79           C  
ANISOU   19  CZ  PHE A   7     5341   5932   4986    266    -32    317       C  
ATOM     20  N   ARG A   8      40.917  18.788  50.656  1.00 56.56           N  
ANISOU   20  N   ARG A   8     6832   7564   7094    540    -35    111       N  
ATOM     21  CA  ARG A   8      42.062  18.963  51.533  1.00 55.84           C  
ANISOU   21  CA  ARG A   8     6777   7494   6945    470     78    106       C  
ATOM     22  C   ARG A   8      41.812  18.397  52.911  1.00 51.60           C  
ANISOU   22  C   ARG A   8     6096   7069   6442    475    190     37       C  
ATOM     23  O   ARG A   8      42.737  17.933  53.562  1.00 47.19           O  
ANISOU   23  O   ARG A   8     5537   6569   5825    393    285     49       O  
ATOM     24  CB  ARG A   8      42.448  20.425  51.690  1.00 53.70           C  
ANISOU   24  CB  ARG A   8     6633   7097   6672    491     32     98       C  
ATOM     25  CG  ARG A   8      43.747  20.583  52.463  1.00 57.98           C  
ANISOU   25  CG  ARG A   8     7222   7663   7143    388    130    109       C  
ATOM     26  CD  ARG A   8      44.150  22.032  52.655  1.00 76.67           C  
ANISOU   26  CD  ARG A   8     9735   9893   9503    385     73    103       C  
ATOM     27  NE  ARG A   8      43.008  22.826  53.087  1.00 98.16           N  
ANISOU   27  NE  ARG A   8    12441  12534  12321    536      8     11       N  
ATOM     28  CZ  ARG A   8      42.349  23.667  52.296  1.00108.63           C  
ANISOU   28  CZ  ARG A   8    13858  13723  13694    626   -134     18       C  
ATOM     29  NH1 ARG A   8      42.745  23.835  51.039  1.00108.78           N  
ANISOU   29  NH1 ARG A   8    14008  13670  13655    555   -223    123       N  
ATOM     30  NH2 ARG A   8      41.301  24.341  52.762  1.00110.74           N  
ANISOU   30  NH2 ARG A   8    14087  13928  14061    790   -188    -81       N  
ATOM     31  N   LEU A   9      40.570  18.456  53.374  1.00 52.75           N  
ANISOU   31  N   LEU A   9     6113   7251   6678    568    179    -34       N  
ATOM     32  CA  LEU A   9      40.252  18.030  54.737  1.00 52.54           C  
ANISOU   32  CA  LEU A   9     5954   7339   6669    566    296   -103       C  
ATOM     33  C   LEU A   9      40.115  16.515  54.791  1.00 61.47           C  
ANISOU   33  C   LEU A   9     6991   8586   7778    479    345    -67       C  
ATOM     34  O   LEU A   9      40.548  15.848  55.732  1.00 56.56           O  
ANISOU   34  O   LEU A   9     6335   8045   7110    405    445    -70       O  
ATOM     35  CB  LEU A   9      38.945  18.666  55.167  1.00 49.50           C  
ANISOU   35  CB  LEU A   9     5452   6971   6386    701    278   -198       C  
ATOM     36  CG  LEU A   9      38.530  18.335  56.595  1.00 56.84           C  
ANISOU   36  CG  LEU A   9     6244   8035   7318    698    414   -279       C  
ATOM     37  CD1 LEU A   9      39.660  18.635  57.586  1.00 54.40           C  
ANISOU   37  CD1 LEU A   9     6040   7711   6919    631    503   -294       C  
ATOM     38  CD2 LEU A   9      37.280  19.115  56.933  1.00 52.94           C  
ANISOU   38  CD2 LEU A   9     5629   7561   6924    858    404   -387       C  
ATOM     39  N   GLN A  10      39.483  15.984  53.758  1.00 71.44           N  
ANISOU   39  N   GLN A  10     8228   9845   9071    485    257    -29       N  
ATOM     40  CA  GLN A  10      39.431  14.558  53.546  1.00 64.22           C  
ANISOU   40  CA  GLN A  10     7274   8999   8127    395    270     16       C  
ATOM     41  C   GLN A  10      40.859  13.984  53.505  1.00 60.09           C  
ANISOU   41  C   GLN A  10     6868   8460   7503    311    323     69       C  
ATOM     42  O   GLN A  10      41.170  13.052  54.245  1.00 62.39           O  
ANISOU   42  O   GLN A  10     7126   8818   7761    243    395     76       O  
ATOM     43  CB  GLN A  10      38.670  14.277  52.251  1.00 69.07           C  
ANISOU   43  CB  GLN A  10     7891   9578   8775    414    138     50       C  
ATOM     44  CG  GLN A  10      38.201  12.853  52.050  1.00 76.75           C  
ANISOU   44  CG  GLN A  10     8805  10614   9740    329    122     80       C  
ATOM     45  CD  GLN A  10      37.427  12.684  50.744  1.00 83.07           C  
ANISOU   45  CD  GLN A  10     9621  11371  10569    344    -30    110       C  
ATOM     46  OE1 GLN A  10      36.498  13.444  50.461  1.00 80.20           O  
ANISOU   46  OE1 GLN A  10     9182  10999  10290    428   -116     87       O  
ATOM     47  NE2 GLN A  10      37.806  11.683  49.947  1.00 84.25           N  
ANISOU   47  NE2 GLN A  10     9876  11489  10645    270    -71    158       N  
ATOM     48  N   THR A  11      41.745  14.548  52.683  1.00 55.39           N  
ANISOU   48  N   THR A  11     6407   7783   6857    314    289    108       N  
ATOM     49  CA  THR A  11      43.055  13.920  52.504  1.00 50.19           C  
ANISOU   49  CA  THR A  11     5829   7133   6109    246    341    155       C  
ATOM     50  C   THR A  11      43.876  13.980  53.786  1.00 49.95           C  
ANISOU   50  C   THR A  11     5773   7151   6056    208    438    139       C  
ATOM     51  O   THR A  11      44.611  13.053  54.132  1.00 57.18           O  
ANISOU   51  O   THR A  11     6686   8112   6927    159    488    163       O  
ATOM     52  CB  THR A  11      43.872  14.495  51.313  1.00 55.24           C  
ANISOU   52  CB  THR A  11     6604   7702   6684    238    301    204       C  
ATOM     53  OG1 THR A  11      44.708  15.548  51.771  1.00 64.89           O  
ANISOU   53  OG1 THR A  11     7871   8899   7886    220    337    207       O  
ATOM     54  CG2 THR A  11      42.971  15.015  50.221  1.00 51.75           C  
ANISOU   54  CG2 THR A  11     6208   7186   6267    286    182    214       C  
ATOM     55  N   SER A  12      43.743  15.079  54.494  1.00 45.12           N  
ANISOU   55  N   SER A  12     5153   6519   5472    237    453     97       N  
ATOM     56  CA  SER A  12      44.339  15.213  55.817  1.00 54.98           C  
ANISOU   56  CA  SER A  12     6382   7812   6696    198    533     72       C  
ATOM     57  C   SER A  12      43.928  14.064  56.767  1.00 52.11           C  
ANISOU   57  C   SER A  12     5925   7545   6331    161    591     58       C  
ATOM     58  O   SER A  12      44.777  13.403  57.377  1.00 52.36           O  
ANISOU   58  O   SER A  12     5966   7617   6310     99    634     86       O  
ATOM     59  CB  SER A  12      43.962  16.587  56.402  1.00 49.47           C  
ANISOU   59  CB  SER A  12     5701   7065   6031    253    527      6       C  
ATOM     60  OG  SER A  12      44.480  16.744  57.700  1.00 52.06           O  
ANISOU   60  OG  SER A  12     6027   7433   6321    210    597    -26       O  
ATOM     61  N   THR A  13      42.625  13.820  56.866  1.00 44.23           N  
ANISOU   61  N   THR A  13     4833   6585   5388    191    584     22       N  
ATOM     62  CA  THR A  13      42.093  12.774  57.738  1.00 43.69           C  
ANISOU   62  CA  THR A  13     4676   6612   5311    131    638     18       C  
ATOM     63  C   THR A  13      42.652  11.394  57.377  1.00 46.06           C  
ANISOU   63  C   THR A  13     5018   6912   5568     61    618     88       C  
ATOM     64  O   THR A  13      42.861  10.545  58.252  1.00 42.95           O  
ANISOU   64  O   THR A  13     4615   6569   5135    -10    658    107       O  
ATOM     65  CB  THR A  13      40.532  12.735  57.705  1.00 47.17           C  
ANISOU   65  CB  THR A  13     4986   7111   5826    165    627    -25       C  
ATOM     66  OG1 THR A  13      39.985  13.986  58.145  1.00 53.66           O  
ANISOU   66  OG1 THR A  13     5761   7935   6693    257    651   -107       O  
ATOM     67  CG2 THR A  13      40.013  11.622  58.573  1.00 41.97           C  
ANISOU   67  CG2 THR A  13     4242   6559   5146     68    685    -13       C  
ATOM     68  N   LEU A  14      42.893  11.166  56.086  1.00 41.88           N  
ANISOU   68  N   LEU A  14     4552   6320   5041     86    549    123       N  
ATOM     69  CA  LEU A  14      43.444   9.878  55.654  1.00 41.56           C  
ANISOU   69  CA  LEU A  14     4569   6264   4957     45    526    172       C  
ATOM     70  C   LEU A  14      44.868   9.697  56.139  1.00 45.47           C  
ANISOU   70  C   LEU A  14     5118   6762   5395     30    570    197       C  
ATOM     71  O   LEU A  14      45.259   8.597  56.536  1.00 50.15           O  
ANISOU   71  O   LEU A  14     5731   7364   5959     -6    572    224       O  
ATOM     72  CB  LEU A  14      43.424   9.752  54.149  1.00 45.14           C  
ANISOU   72  CB  LEU A  14     5092   6653   5405     82    452    191       C  
ATOM     73  CG  LEU A  14      42.348   8.860  53.564  1.00 52.55           C  
ANISOU   73  CG  LEU A  14     6015   7582   6369     55    378    198       C  
ATOM     74  CD1 LEU A  14      42.499   8.884  52.035  1.00 54.91           C  
ANISOU   74  CD1 LEU A  14     6415   7810   6637     94    303    212       C  
ATOM     75  CD2 LEU A  14      42.467   7.439  54.137  1.00 46.63           C  
ANISOU   75  CD2 LEU A  14     5282   6845   5592    -16    384    223       C  
ATOM     76  N   CYS A  15      45.641  10.782  56.105  1.00 36.82           N  
ANISOU   76  N   CYS A  15     4047   5654   4288     55    593    190       N  
ATOM     77  CA  CYS A  15      47.014  10.713  56.578  1.00 45.39           C  
ANISOU   77  CA  CYS A  15     5158   6760   5328     34    627    216       C  
ATOM     78  C   CYS A  15      47.077  10.343  58.032  1.00 52.12           C  
ANISOU   78  C   CYS A  15     5977   7663   6165    -18    661    213       C  
ATOM     79  O   CYS A  15      47.780   9.390  58.376  1.00 45.76           O  
ANISOU   79  O   CYS A  15     5186   6871   5330    -37    655    247       O  
ATOM     80  CB  CYS A  15      47.756  12.023  56.367  1.00 54.57           C  
ANISOU   80  CB  CYS A  15     6349   7906   6479     37    638    215       C  
ATOM     81  SG  CYS A  15      48.021  12.315  54.655  1.00 56.30           S  
ANISOU   81  SG  CYS A  15     6633   8077   6680     71    605    242       S  
ATOM     82  N   HIS A  16      46.369  11.105  58.879  1.00 44.33           N  
ANISOU   82  N   HIS A  16     4954   6699   5190    -32    692    168       N  
ATOM     83  CA  HIS A  16      46.236  10.746  60.305  1.00 40.27           C  
ANISOU   83  CA  HIS A  16     4417   6244   4641    -94    732    160       C  
ATOM     84  C   HIS A  16      45.860   9.261  60.529  1.00 41.33           C  
ANISOU   84  C   HIS A  16     4545   6399   4759   -145    717    201       C  
ATOM     85  O   HIS A  16      46.613   8.510  61.149  1.00 48.54           O  
ANISOU   85  O   HIS A  16     5496   7319   5629   -187    704    244       O  
ATOM     86  CB  HIS A  16      45.274  11.693  61.030  1.00 39.05           C  
ANISOU   86  CB  HIS A  16     4219   6122   4497    -86    782     87       C  
ATOM     87  CG  HIS A  16      45.760  13.105  61.098  1.00 55.78           C  
ANISOU   87  CG  HIS A  16     6381   8199   6616    -51    784     47       C  
ATOM     88  ND1 HIS A  16      46.895  13.469  61.791  1.00 69.30           N  
ANISOU   88  ND1 HIS A  16     8148   9910   8274    -97    787     60       N  
ATOM     89  CD2 HIS A  16      45.274  14.245  60.558  1.00 58.57           C  
ANISOU   89  CD2 HIS A  16     6741   8496   7015     21    767     -2       C  
ATOM     90  CE1 HIS A  16      47.087  14.771  61.675  1.00 61.20           C  
ANISOU   90  CE1 HIS A  16     7168   8828   7257    -70    775     21       C  
ATOM     91  NE2 HIS A  16      46.114  15.266  60.934  1.00 57.66           N  
ANISOU   91  NE2 HIS A  16     6700   8338   6869      7    762    -18       N  
ATOM     92  N   SER A  17      44.731   8.819  59.993  1.00 43.82           N  
ANISOU   92  N   SER A  17     4822   6714   5112   -147    700    195       N  
ATOM     93  CA  SER A  17      44.316   7.436  60.200  1.00 47.44           C  
ANISOU   93  CA  SER A  17     5292   7179   5554   -219    672    239       C  
ATOM     94  C   SER A  17      45.388   6.487  59.754  1.00 41.77           C  
ANISOU   94  C   SER A  17     4664   6394   4812   -201    614    290       C  
ATOM     95  O   SER A  17      45.732   5.557  60.475  1.00 52.66           O  
ANISOU   95  O   SER A  17     6090   7767   6151   -256    593    333       O  
ATOM     96  CB  SER A  17      43.046   7.106  59.424  1.00 47.29           C  
ANISOU   96  CB  SER A  17     5221   7160   5586   -229    638    231       C  
ATOM     97  OG  SER A  17      42.074   8.101  59.638  1.00 55.38           O  
ANISOU   97  OG  SER A  17     6141   8248   6652   -206    685    173       O  
ATOM     98  N   PHE A  18      45.888   6.693  58.542  1.00 34.38           N  
ANISOU   98  N   PHE A  18     3759   5407   3897   -120    585    283       N  
ATOM     99  CA  PHE A  18      46.868   5.777  57.974  1.00 40.02           C  
ANISOU   99  CA  PHE A  18     4550   6066   4591    -75    541    313       C  
ATOM    100  C   PHE A  18      48.102   5.691  58.867  1.00 40.97           C  
ANISOU  100  C   PHE A  18     4678   6209   4680    -72    553    338       C  
ATOM    101  O   PHE A  18      48.572   4.611  59.161  1.00 43.20           O  
ANISOU  101  O   PHE A  18     5013   6458   4944    -71    507    372       O  
ATOM    102  CB  PHE A  18      47.243   6.158  56.535  1.00 37.87           C  
ANISOU  102  CB  PHE A  18     4305   5760   4326      8    532    294       C  
ATOM    103  CG  PHE A  18      48.574   5.604  56.101  1.00 44.16           C  
ANISOU  103  CG  PHE A  18     5147   6538   5093     77    527    306       C  
ATOM    104  CD1 PHE A  18      48.715   4.255  55.820  1.00 38.46           C  
ANISOU  104  CD1 PHE A  18     4502   5755   4357    108    474    315       C  
ATOM    105  CD2 PHE A  18      49.691   6.428  56.006  1.00 43.94           C  
ANISOU  105  CD2 PHE A  18     5084   6557   5054    112    574    306       C  
ATOM    106  CE1 PHE A  18      49.946   3.740  55.431  1.00 41.29           C  
ANISOU  106  CE1 PHE A  18     4890   6103   4694    200    475    311       C  
ATOM    107  CE2 PHE A  18      50.911   5.916  55.625  1.00 45.29           C  
ANISOU  107  CE2 PHE A  18     5263   6739   5204    183    581    312       C  
ATOM    108  CZ  PHE A  18      51.037   4.566  55.336  1.00 40.58           C  
ANISOU  108  CZ  PHE A  18     4733   6086   4598    241    535    309       C  
ATOM    109  N   LEU A  19      48.611   6.827  59.315  1.00 39.44           N  
ANISOU  109  N   LEU A  19     4440   6065   4482    -74    599    323       N  
ATOM    110  CA  LEU A  19      49.680   6.805  60.302  1.00 40.69           C  
ANISOU  110  CA  LEU A  19     4597   6255   4610    -92    596    350       C  
ATOM    111  C   LEU A  19      49.297   6.105  61.638  1.00 48.14           C  
ANISOU  111  C   LEU A  19     5567   7212   5513   -178    578    379       C  
ATOM    112  O   LEU A  19      50.106   5.384  62.232  1.00 46.22           O  
ANISOU  112  O   LEU A  19     5359   6959   5244   -183    529    423       O  
ATOM    113  CB  LEU A  19      50.212   8.215  60.554  1.00 36.62           C  
ANISOU  113  CB  LEU A  19     4043   5781   4090   -102    636    328       C  
ATOM    114  CG  LEU A  19      50.770   8.978  59.351  1.00 47.30           C  
ANISOU  114  CG  LEU A  19     5381   7126   5463    -49    651    319       C  
ATOM    115  CD1 LEU A  19      50.949  10.477  59.705  1.00 38.60           C  
ANISOU  115  CD1 LEU A  19     4269   6041   4357    -89    677    296       C  
ATOM    116  CD2 LEU A  19      52.082   8.338  58.795  1.00 39.42           C  
ANISOU  116  CD2 LEU A  19     4370   6147   4462      9    635    350       C  
ATOM    117  N   LEU A  20      48.076   6.302  62.122  1.00 42.96           N  
ANISOU  117  N   LEU A  20     4892   6583   4846   -248    616    358       N  
ATOM    118  CA  LEU A  20      47.701   5.618  63.364  1.00 47.56           C  
ANISOU  118  CA  LEU A  20     5508   7193   5371   -351    612    393       C  
ATOM    119  C   LEU A  20      47.590   4.104  63.187  1.00 51.62           C  
ANISOU  119  C   LEU A  20     6095   7640   5878   -377    534    452       C  
ATOM    120  O   LEU A  20      47.758   3.349  64.144  1.00 61.12           O  
ANISOU  120  O   LEU A  20     7363   8836   7025   -453    494    506       O  
ATOM    121  CB  LEU A  20      46.399   6.164  63.940  1.00 44.95           C  
ANISOU  121  CB  LEU A  20     5122   6935   5024   -423    690    350       C  
ATOM    122  CG  LEU A  20      46.428   7.612  64.427  1.00 47.83           C  
ANISOU  122  CG  LEU A  20     5445   7352   5377   -402    762    281       C  
ATOM    123  CD1 LEU A  20      45.193   7.908  65.270  1.00 44.19           C  
ANISOU  123  CD1 LEU A  20     4932   6978   4879   -469    848    235       C  
ATOM    124  CD2 LEU A  20      47.692   7.917  65.212  1.00 48.35           C  
ANISOU  124  CD2 LEU A  20     5563   7420   5390   -416    739    301       C  
ATOM    125  N   ALA A  21      47.318   3.660  61.966  1.00 42.28           N  
ANISOU  125  N   ALA A  21     4923   6396   4743   -319    500    443       N  
ATOM    126  CA  ALA A  21      47.100   2.233  61.723  1.00 42.38           C  
ANISOU  126  CA  ALA A  21     5030   6322   4750   -346    415    490       C  
ATOM    127  C   ALA A  21      48.336   1.502  61.233  1.00 45.52           C  
ANISOU  127  C   ALA A  21     5503   6634   5156   -233    340    506       C  
ATOM    128  O   ALA A  21      48.288   0.309  60.989  1.00 48.40           O  
ANISOU  128  O   ALA A  21     5971   6902   5516   -231    255    535       O  
ATOM    129  CB  ALA A  21      45.946   2.005  60.756  1.00 40.77           C  
ANISOU  129  CB  ALA A  21     4814   6094   4582   -367    404    469       C  
ATOM    130  N   SER A  22      49.455   2.197  61.118  1.00 38.83           N  
ANISOU  130  N   SER A  22     4606   5825   4323   -140    368    485       N  
ATOM    131  CA  SER A  22      50.642   1.556  60.566  1.00 42.57           C  
ANISOU  131  CA  SER A  22     5116   6245   4813    -12    313    488       C  
ATOM    132  C   SER A  22      51.869   1.720  61.478  1.00 55.30           C  
ANISOU  132  C   SER A  22     6694   7902   6416     14    291    519       C  
ATOM    133  O   SER A  22      52.979   1.447  61.060  1.00 59.12           O  
ANISOU  133  O   SER A  22     7158   8379   6925    134    263    513       O  
ATOM    134  CB  SER A  22      50.923   2.095  59.160  1.00 41.37           C  
ANISOU  134  CB  SER A  22     4922   6106   4692     92    363    432       C  
ATOM    135  OG  SER A  22      51.235   3.485  59.193  1.00 49.67           O  
ANISOU  135  OG  SER A  22     5873   7251   5750     82    442    412       O  
ATOM    136  N   ALA A  23      51.664   2.161  62.720  1.00 55.99           N  
ANISOU  136  N   ALA A  23     6770   8042   6463    -99    302    548       N  
ATOM    137  CA  ALA A  23      52.766   2.396  63.654  1.00 51.98           C  
ANISOU  137  CA  ALA A  23     6235   7579   5936    -97    265    581       C  
ATOM    138  C   ALA A  23      52.801   1.284  64.676  1.00 51.72           C  
ANISOU  138  C   ALA A  23     6310   7484   5856   -151    159    653       C  
ATOM    139  O   ALA A  23      51.806   0.605  64.880  1.00 53.88           O  
ANISOU  139  O   ALA A  23     6672   7704   6097   -239    142    678       O  
ATOM    140  CB  ALA A  23      52.591   3.743  64.364  1.00 44.92           C  
ANISOU  140  CB  ALA A  23     5281   6779   5009   -188    340    560       C  
ATOM    141  N   ASN A  24      53.933   1.091  65.338  1.00 54.56           N  
ANISOU  141  N   ASN A  24     6666   7851   6211   -113     78    694       N  
ATOM    142  CA  ASN A  24      53.931   0.157  66.464  1.00 61.76           C  
ANISOU  142  CA  ASN A  24     7701   8702   7062   -187    -36    774       C  
ATOM    143  C   ASN A  24      53.165   0.722  67.662  1.00 60.70           C  
ANISOU  143  C   ASN A  24     7601   8634   6829   -374     14    796       C  
ATOM    144  O   ASN A  24      52.706   1.867  67.644  1.00 55.06           O  
ANISOU  144  O   ASN A  24     6808   8008   6104   -422    131    738       O  
ATOM    145  CB  ASN A  24      55.348  -0.264  66.877  1.00 54.43           C  
ANISOU  145  CB  ASN A  24     6763   7760   6160    -86   -163    818       C  
ATOM    146  CG  ASN A  24      56.131   0.861  67.520  1.00 56.87           C  
ANISOU  146  CG  ASN A  24     6965   8189   6454   -121   -142    816       C  
ATOM    147  OD1 ASN A  24      55.556   1.759  68.140  1.00 60.31           O  
ANISOU  147  OD1 ASN A  24     7400   8692   6824   -256    -66    801       O  
ATOM    148  ND2 ASN A  24      57.461   0.813  67.384  1.00 52.78           N  
ANISOU  148  ND2 ASN A  24     6355   7702   5998      2   -215    825       N  
ATOM    149  N   LYS A  25      53.044  -0.103  68.695  1.00 51.34           N  
ANISOU  149  N   LYS A  25     6543   7399   5564   -473    -80    877       N  
ATOM    150  CA  LYS A  25      52.367   0.262  69.930  1.00 57.29           C  
ANISOU  150  CA  LYS A  25     7351   8220   6195   -657    -35    903       C  
ATOM    151  C   LYS A  25      52.832   1.600  70.488  1.00 51.59           C  
ANISOU  151  C   LYS A  25     6548   7613   5443   -678     29    857       C  
ATOM    152  O   LYS A  25      52.027   2.505  70.706  1.00 65.04           O  
ANISOU  152  O   LYS A  25     8212   9398   7102   -756    159    796       O  
ATOM    153  CB  LYS A  25      52.570  -0.831  70.981  1.00 20.00           C  
ATOM    154  CG  LYS A  25      51.904  -2.154  70.638  0.01 20.00           C  
ATOM    155  CD  LYS A  25      52.166  -3.199  71.709  0.01 20.00           C  
ATOM    156  CE  LYS A  25      51.480  -4.514  71.378  0.01 20.00           C  
ATOM    157  NZ  LYS A  25      51.749  -5.555  72.408  0.01 20.00           N  
ATOM    158  N   GLN A  26      54.125   1.733  70.724  1.00 41.77           N  
ANISOU  158  N   GLN A  26     5276   6372   4222   -607    -68    881       N  
ATOM    159  CA  GLN A  26      54.663   2.983  71.288  1.00 51.17           C  
ANISOU  159  CA  GLN A  26     6405   7659   5379   -645    -34    845       C  
ATOM    160  C   GLN A  26      54.361   4.226  70.443  1.00 47.79           C  
ANISOU  160  C   GLN A  26     5859   7289   5011   -603    107    745       C  
ATOM    161  O   GLN A  26      53.906   5.256  70.964  1.00 48.95           O  
ANISOU  161  O   GLN A  26     6008   7497   5094   -686    193    691       O  
ATOM    162  CB  GLN A  26      56.175   2.856  71.533  1.00 50.94           C  
ANISOU  162  CB  GLN A  26     6337   7630   5386   -570   -180    894       C  
ATOM    163  CG  GLN A  26      56.828   4.139  72.005  1.00 64.29           C  
ANISOU  163  CG  GLN A  26     7962   9412   7052   -619   -165    861       C  
ATOM    164  CD  GLN A  26      58.257   3.928  72.449  1.00 81.09           C  
ANISOU  164  CD  GLN A  26    10049  11556   9205   -578   -330    926       C  
ATOM    165  OE1 GLN A  26      59.015   3.191  71.814  1.00 88.74           O  
ANISOU  165  OE1 GLN A  26    10945  12495  10276   -435   -412    956       O  
ATOM    166  NE2 GLN A  26      58.637   4.579  73.541  1.00 87.05           N  
ANISOU  166  NE2 GLN A  26    10848  12362   9865   -696   -385    942       N  
ATOM    167  N   ASP A  27      54.597   4.118  69.136  1.00 42.52           N  
ANISOU  167  N   ASP A  27     5104   6595   4457   -472    126    718       N  
ATOM    168  CA  ASP A  27      54.383   5.241  68.217  1.00 44.32           C  
ANISOU  168  CA  ASP A  27     5236   6863   4742   -430    238    638       C  
ATOM    169  C   ASP A  27      52.912   5.512  68.004  1.00 43.25           C  
ANISOU  169  C   ASP A  27     5119   6726   4587   -479    350    585       C  
ATOM    170  O   ASP A  27      52.507   6.664  67.851  1.00 46.60           O  
ANISOU  170  O   ASP A  27     5503   7189   5014   -493    437    518       O  
ATOM    171  CB  ASP A  27      55.072   4.983  66.872  1.00 48.23           C  
ANISOU  171  CB  ASP A  27     5643   7338   5343   -285    228    630       C  
ATOM    172  CG  ASP A  27      56.590   5.116  66.951  1.00 62.33           C  
ANISOU  172  CG  ASP A  27     7347   9172   7166   -229    150    661       C  
ATOM    173  OD1 ASP A  27      57.088   6.237  67.260  1.00 56.93           O  
ANISOU  173  OD1 ASP A  27     6608   8554   6468   -287    167    646       O  
ATOM    174  OD2 ASP A  27      57.276   4.091  66.697  1.00 70.54           O  
ANISOU  174  OD2 ASP A  27     8374  10179   8250   -124     66    698       O  
ATOM    175  N   THR A  28      52.105   4.455  68.002  1.00 43.57           N  
ANISOU  175  N   THR A  28     5222   6721   4612   -508    337    617       N  
ATOM    176  CA  THR A  28      50.668   4.649  67.878  1.00 51.14           C  
ANISOU  176  CA  THR A  28     6175   7702   5555   -567    438    573       C  
ATOM    177  C   THR A  28      50.146   5.557  68.987  1.00 53.44           C  
ANISOU  177  C   THR A  28     6476   8076   5754   -671    519    531       C  
ATOM    178  O   THR A  28      49.416   6.529  68.732  1.00 48.64           O  
ANISOU  178  O   THR A  28     5808   7510   5164   -658    620    451       O  
ATOM    179  CB  THR A  28      49.889   3.362  67.958  1.00 48.45           C  
ANISOU  179  CB  THR A  28     5907   7313   5189   -631    402    628       C  
ATOM    180  OG1 THR A  28      50.317   2.466  66.925  1.00 56.45           O  
ANISOU  180  OG1 THR A  28     6938   8231   6279   -526    322    653       O  
ATOM    181  CG2 THR A  28      48.428   3.684  67.763  1.00 35.46           C  
ANISOU  181  CG2 THR A  28     4212   5719   3542   -693    512    578       C  
ATOM    182  N   ASP A  29      50.533   5.225  70.219  1.00 45.66           N  
ANISOU  182  N   ASP A  29     5576   7108   4666   -765    467    583       N  
ATOM    183  CA  ASP A  29      50.174   6.021  71.389  1.00 49.80           C  
ANISOU  183  CA  ASP A  29     6137   7712   5074   -867    538    541       C  
ATOM    184  C   ASP A  29      50.731   7.434  71.350  1.00 54.32           C  
ANISOU  184  C   ASP A  29     6669   8307   5665   -818    567    464       C  
ATOM    185  O   ASP A  29      50.013   8.395  71.636  1.00 46.14           O  
ANISOU  185  O   ASP A  29     5622   7318   4592   -836    673    375       O  
ATOM    186  CB  ASP A  29      50.656   5.340  72.671  1.00 52.38           C  
ANISOU  186  CB  ASP A  29     6587   8041   5272   -981    449    624       C  
ATOM    187  CG  ASP A  29      49.762   4.166  73.098  1.00 70.14           C  
ANISOU  187  CG  ASP A  29     8913  10288   7449  -1096    452    693       C  
ATOM    188  OD1 ASP A  29      48.875   3.723  72.316  1.00 76.15           O  
ANISOU  188  OD1 ASP A  29     9624  11036   8275  -1082    501    685       O  
ATOM    189  OD2 ASP A  29      49.954   3.688  74.237  1.00 72.52           O  
ANISOU  189  OD2 ASP A  29     9336  10600   7618  -1217    394    762       O  
ATOM    190  N   TYR A  30      52.014   7.575  71.029  1.00 46.20           N  
ANISOU  190  N   TYR A  30     5619   7245   4690   -760    471    497       N  
ATOM    191  CA  TYR A  30      52.573   8.919  70.958  1.00 44.99           C  
ANISOU  191  CA  TYR A  30     5436   7106   4553   -741    486    436       C  
ATOM    192  C   TYR A  30      51.822   9.742  69.906  1.00 46.04           C  
ANISOU  192  C   TYR A  30     5500   7225   4768   -664    586    354       C  
ATOM    193  O   TYR A  30      51.440  10.896  70.147  1.00 48.02           O  
ANISOU  193  O   TYR A  30     5768   7486   4993   -674    649    271       O  
ATOM    194  CB  TYR A  30      54.087   8.891  70.705  1.00 40.52           C  
ANISOU  194  CB  TYR A  30     4828   6529   4040   -705    369    494       C  
ATOM    195  CG  TYR A  30      54.637  10.232  70.263  1.00 46.82           C  
ANISOU  195  CG  TYR A  30     5577   7332   4879   -691    385    444       C  
ATOM    196  CD1 TYR A  30      54.936  11.234  71.193  1.00 51.90           C  
ANISOU  196  CD1 TYR A  30     6287   7992   5440   -781    367    407       C  
ATOM    197  CD2 TYR A  30      54.858  10.504  68.910  1.00 41.59           C  
ANISOU  197  CD2 TYR A  30     4823   6653   4327   -601    411    434       C  
ATOM    198  CE1 TYR A  30      55.430  12.487  70.780  1.00 51.97           C  
ANISOU  198  CE1 TYR A  30     6274   7987   5484   -787    367    367       C  
ATOM    199  CE2 TYR A  30      55.342  11.746  68.486  1.00 48.36           C  
ANISOU  199  CE2 TYR A  30     5653   7508   5213   -613    420    401       C  
ATOM    200  CZ  TYR A  30      55.632  12.728  69.413  1.00 55.93           C  
ANISOU  200  CZ  TYR A  30     6681   8472   6099   -708    393    370       C  
ATOM    201  OH  TYR A  30      56.116  13.943  68.969  1.00 58.23           O  
ANISOU  201  OH  TYR A  30     6964   8743   6418   -735    387    345       O  
ATOM    202  N   LEU A  31      51.562   9.142  68.751  1.00 43.33           N  
ANISOU  202  N   LEU A  31     5095   6849   4518   -584    591    373       N  
ATOM    203  CA  LEU A  31      50.878   9.884  67.691  1.00 43.60           C  
ANISOU  203  CA  LEU A  31     5073   6864   4629   -511    662    308       C  
ATOM    204  C   LEU A  31      49.411  10.159  68.019  1.00 39.41           C  
ANISOU  204  C   LEU A  31     4540   6365   4070   -531    760    238       C  
ATOM    205  O   LEU A  31      48.860  11.197  67.672  1.00 44.12           O  
ANISOU  205  O   LEU A  31     5112   6954   4699   -484    816    160       O  
ATOM    206  CB  LEU A  31      50.965   9.125  66.372  1.00 52.84           C  
ANISOU  206  CB  LEU A  31     6193   7994   5889   -427    636    345       C  
ATOM    207  CG  LEU A  31      52.357   9.024  65.744  1.00 58.10           C  
ANISOU  207  CG  LEU A  31     6825   8648   6601   -373    569    390       C  
ATOM    208  CD1 LEU A  31      52.312   8.137  64.504  1.00 57.94           C  
ANISOU  208  CD1 LEU A  31     6778   8591   6647   -284    557    411       C  
ATOM    209  CD2 LEU A  31      52.901  10.416  65.409  1.00 57.12           C  
ANISOU  209  CD2 LEU A  31     6676   8532   6496   -373    587    355       C  
ATOM    210  N   THR A  32      48.776   9.208  68.676  1.00 40.72           N  
ANISOU  210  N   THR A  32     4727   6568   4177   -601    777    269       N  
ATOM    211  CA  THR A  32      47.375   9.340  68.957  1.00 46.48           C  
ANISOU  211  CA  THR A  32     5421   7356   4882   -627    880    209       C  
ATOM    212  C   THR A  32      47.160  10.498  69.911  1.00 53.43           C  
ANISOU  212  C   THR A  32     6331   8284   5684   -647    954    117       C  
ATOM    213  O   THR A  32      46.218  11.275  69.752  1.00 53.53           O  
ANISOU  213  O   THR A  32     6290   8325   5725   -591   1041     23       O  
ATOM    214  CB  THR A  32      46.807   8.081  69.596  1.00 54.53           C  
ANISOU  214  CB  THR A  32     6468   8419   5832   -737    884    275       C  
ATOM    215  OG1 THR A  32      46.915   6.974  68.683  1.00 42.82           O  
ANISOU  215  OG1 THR A  32     4979   6870   4421   -714    806    350       O  
ATOM    216  CG2 THR A  32      45.348   8.325  69.979  1.00 30.52           C  
ANISOU  216  CG2 THR A  32     3361   5478   2759   -778   1012    206       C  
ATOM    217  N   ASP A  33      48.046  10.625  70.893  1.00 57.87           N  
ANISOU  217  N   ASP A  33     6987   8852   6150   -716    911    138       N  
ATOM    218  CA  ASP A  33      47.930  11.716  71.862  1.00 55.00           C  
ANISOU  218  CA  ASP A  33     6685   8521   5692   -741    971     43       C  
ATOM    219  C   ASP A  33      48.282  13.057  71.244  1.00 54.96           C  
ANISOU  219  C   ASP A  33     6679   8445   5760   -649    957    -31       C  
ATOM    220  O   ASP A  33      47.612  14.054  71.516  1.00 57.72           O  
ANISOU  220  O   ASP A  33     7043   8801   6089   -605   1034   -145       O  
ATOM    221  CB  ASP A  33      48.760  11.449  73.127  1.00 57.48           C  
ANISOU  221  CB  ASP A  33     7118   8857   5865   -859    912     90       C  
ATOM    222  CG  ASP A  33      48.355  10.134  73.838  1.00 80.44           C  
ANISOU  222  CG  ASP A  33    10059  11826   8678   -971    918    173       C  
ATOM    223  OD1 ASP A  33      47.331   9.504  73.458  1.00 87.46           O  
ANISOU  223  OD1 ASP A  33    10876  12753   9601   -972    987    181       O  
ATOM    224  OD2 ASP A  33      49.071   9.727  74.778  1.00 83.32           O  
ANISOU  224  OD2 ASP A  33    10530  12197   8932  -1069    841    237       O  
ATOM    225  N   LEU A  34      49.311  13.077  70.395  1.00 46.57           N  
ANISOU  225  N   LEU A  34     5600   7315   4779   -618    860     33       N  
ATOM    226  CA  LEU A  34      49.684  14.300  69.708  1.00 45.72           C  
ANISOU  226  CA  LEU A  34     5500   7135   4738   -556    837    -15       C  
ATOM    227  C   LEU A  34      48.513  14.828  68.934  1.00 49.94           C  
ANISOU  227  C   LEU A  34     5979   7646   5350   -452    908    -93       C  
ATOM    228  O   LEU A  34      48.229  16.023  68.962  1.00 55.05           O  
ANISOU  228  O   LEU A  34     6670   8244   6002   -403    928   -184       O  
ATOM    229  CB  LEU A  34      50.839  14.063  68.747  1.00 49.25           C  
ANISOU  229  CB  LEU A  34     5906   7542   5264   -544    745     76       C  
ATOM    230  CG  LEU A  34      51.155  15.218  67.794  1.00 45.04           C  
ANISOU  230  CG  LEU A  34     5375   6936   4802   -497    723     49       C  
ATOM    231  CD1 LEU A  34      51.220  16.527  68.564  1.00 45.97           C  
ANISOU  231  CD1 LEU A  34     5598   7010   4857   -534    719    -34       C  
ATOM    232  CD2 LEU A  34      52.473  14.938  67.107  1.00 44.86           C  
ANISOU  232  CD2 LEU A  34     5307   6915   4824   -519    646    143       C  
ATOM    233  N   LEU A  35      47.829  13.941  68.229  1.00 52.45           N  
ANISOU  233  N   LEU A  35     6208   7990   5731   -416    931    -56       N  
ATOM    234  CA  LEU A  35      46.667  14.366  67.460  1.00 62.44           C  
ANISOU  234  CA  LEU A  35     7403   9242   7078   -317    981   -122       C  
ATOM    235  C   LEU A  35      45.540  14.896  68.362  1.00 63.97           C  
ANISOU  235  C   LEU A  35     7586   9500   7221   -295   1085   -237       C  
ATOM    236  O   LEU A  35      44.937  15.936  68.071  1.00 64.40           O  
ANISOU  236  O   LEU A  35     7630   9513   7324   -192   1110   -332       O  
ATOM    237  CB  LEU A  35      46.161  13.231  66.571  1.00 62.99           C  
ANISOU  237  CB  LEU A  35     7387   9332   7216   -302    971    -56       C  
ATOM    238  CG  LEU A  35      44.931  13.636  65.765  1.00 69.84           C  
ANISOU  238  CG  LEU A  35     8171  10194   8172   -206   1003   -117       C  
ATOM    239  CD1 LEU A  35      45.217  14.934  65.014  1.00 70.84           C  
ANISOU  239  CD1 LEU A  35     8339  10220   8357   -116    959   -159       C  
ATOM    240  CD2 LEU A  35      44.514  12.520  64.821  1.00 76.05           C  
ANISOU  240  CD2 LEU A  35     8889  10986   9018   -208    970    -48       C  
ATOM    241  N   ASP A  36      45.272  14.181  69.459  1.00 61.35           N  
ANISOU  241  N   ASP A  36     7258   9267   6784   -387   1146   -229       N  
ATOM    242  CA  ASP A  36      44.274  14.602  70.449  1.00 61.58           C  
ANISOU  242  CA  ASP A  36     7274   9388   6736   -382   1269   -341       C  
ATOM    243  C   ASP A  36      44.541  16.018  70.941  1.00 71.86           C  
ANISOU  243  C   ASP A  36     8678  10629   7997   -322   1278   -457       C  
ATOM    244  O   ASP A  36      43.644  16.865  70.938  1.00 74.64           O  
ANISOU  244  O   ASP A  36     8996  10986   8380   -209   1348   -581       O  
ATOM    245  CB  ASP A  36      44.257  13.659  71.648  1.00 69.17           C  
ANISOU  245  CB  ASP A  36     8270  10458   7554   -527   1319   -296       C  
ATOM    246  CG  ASP A  36      43.509  12.353  71.373  1.00 92.64           C  
ANISOU  246  CG  ASP A  36    11140  13510  10550   -592   1345   -215       C  
ATOM    247  OD1 ASP A  36      42.626  12.331  70.483  1.00103.19           O  
ANISOU  247  OD1 ASP A  36    12349  14858  11999   -515   1368   -236       O  
ATOM    248  OD2 ASP A  36      43.800  11.343  72.060  1.00 98.70           O  
ANISOU  248  OD2 ASP A  36    11962  14319  11219   -728   1329   -125       O  
ATOM    249  N   ASN A  37      45.779  16.263  71.367  1.00 69.87           N  
ANISOU  249  N   ASN A  37     8555  10315   7679   -396   1195   -418       N  
ATOM    250  CA  ASN A  37      46.182  17.576  71.854  1.00 65.20           C  
ANISOU  250  CA  ASN A  37     8092   9642   7037   -370   1176   -517       C  
ATOM    251  C   ASN A  37      46.247  18.616  70.753  1.00 66.90           C  
ANISOU  251  C   ASN A  37     8316   9724   7378   -256   1112   -550       C  
ATOM    252  O   ASN A  37      46.087  19.815  71.014  1.00 63.32           O  
ANISOU  252  O   ASN A  37     7959   9192   6908   -188   1114   -665       O  
ATOM    253  CB  ASN A  37      47.544  17.506  72.528  1.00 59.15           C  
ANISOU  253  CB  ASN A  37     7449   8850   6176   -501   1080   -447       C  
ATOM    254  CG  ASN A  37      47.498  16.811  73.878  1.00 64.11           C  
ANISOU  254  CG  ASN A  37     8131   9587   6641   -618   1130   -439       C  
ATOM    255  OD1 ASN A  37      46.555  17.006  74.655  1.00 56.66           O  
ANISOU  255  OD1 ASN A  37     7200   8721   5606   -602   1255   -545       O  
ATOM    256  ND2 ASN A  37      48.527  15.994  74.170  1.00 60.05           N  
ANISOU  256  ND2 ASN A  37     7649   9084   6082   -735   1033   -312       N  
ATOM    257  N   THR A  38      46.500  18.155  69.528  1.00 64.32           N  
ANISOU  257  N   THR A  38     7911   9364   7165   -238   1048   -449       N  
ATOM    258  CA  THR A  38      46.643  19.051  68.384  1.00 61.33           C  
ANISOU  258  CA  THR A  38     7552   8858   6892   -155    976   -454       C  
ATOM    259  C   THR A  38      45.315  19.738  68.118  1.00 66.08           C  
ANISOU  259  C   THR A  38     8111   9437   7558     -1   1031   -573       C  
ATOM    260  O   THR A  38      45.276  20.805  67.508  1.00 63.67           O  
ANISOU  260  O   THR A  38     7872   9005   7315     83    971   -617       O  
ATOM    261  CB  THR A  38      47.145  18.292  67.127  1.00 73.56           C  
ANISOU  261  CB  THR A  38     9024  10397   8528   -172    912   -323       C  
ATOM    262  OG1 THR A  38      48.576  18.293  67.115  1.00 71.90           O  
ANISOU  262  OG1 THR A  38     8873  10158   8287   -273    831   -238       O  
ATOM    263  CG2 THR A  38      46.679  18.955  65.865  1.00 79.89           C  
ANISOU  263  CG2 THR A  38     9811  11106   9438    -65    873   -337       C  
ATOM    264  N   ASN A  39      44.239  19.119  68.608  1.00 69.46           N  
ANISOU  264  N   ASN A  39     8428   9994   7970     28   1142   -622       N  
ATOM    265  CA  ASN A  39      42.867  19.633  68.471  1.00 79.41           C  
ANISOU  265  CA  ASN A  39     9598  11277   9295    182   1211   -742       C  
ATOM    266  C   ASN A  39      42.559  20.177  67.087  1.00 84.53           C  
ANISOU  266  C   ASN A  39    10218  11813  10089    303   1121   -730       C  
ATOM    267  O   ASN A  39      42.221  21.353  66.924  1.00 86.05           O  
ANISOU  267  O   ASN A  39    10473  11896  10325    432   1088   -828       O  
ATOM    268  CB  ASN A  39      42.552  20.704  69.528  1.00 84.16           C  
ANISOU  268  CB  ASN A  39    10296  11862   9819    254   1276   -906       C  
ATOM    269  CG  ASN A  39      41.052  20.881  69.756  1.00 84.31           C  
ANISOU  269  CG  ASN A  39    10173  11984   9876    402   1397  -1039       C  
ATOM    270  OD1 ASN A  39      40.297  19.913  69.717  1.00 87.50           O  
ANISOU  270  OD1 ASN A  39    10405  12542  10300    373   1475  -1003       O  
ATOM    271  ND2 ASN A  39      40.622  22.119  70.001  1.00 84.45           N  
ANISOU  271  ND2 ASN A  39    10261  11919   9906    559   1408  -1195       N  
ATOM    272  N   ILE A  40      42.674  19.314  66.089  1.00 83.59           N  
ANISOU  272  N   ILE A  40    10019  11707  10034    263   1070   -610       N  
ATOM    273  CA  ILE A  40      42.414  19.724  64.726  1.00 80.43           C  
ANISOU  273  CA  ILE A  40     9603  11205   9751    356    977   -582       C  
ATOM    274  C   ILE A  40      41.218  18.979  64.163  1.00 81.37           C  
ANISOU  274  C   ILE A  40     9544  11420   9953    412   1004   -575       C  
ATOM    275  O   ILE A  40      40.762  17.971  64.724  1.00 68.79           O  
ANISOU  275  O   ILE A  40     7842   9972   8325    344   1089   -561       O  
ATOM    276  CB  ILE A  40      43.649  19.538  63.814  1.00 77.60           C  
ANISOU  276  CB  ILE A  40     9328  10761   9394    267    877   -452       C  
ATOM    277  CG1 ILE A  40      44.150  18.092  63.868  1.00 75.60           C  
ANISOU  277  CG1 ILE A  40     9013  10611   9101    146    902   -347       C  
ATOM    278  CG2 ILE A  40      44.732  20.532  64.182  1.00 72.68           C  
ANISOU  278  CG2 ILE A  40     8872  10030   8715    217    826   -461       C  
ATOM    279  CD1 ILE A  40      43.282  17.140  63.087  1.00 70.92           C  
ANISOU  279  CD1 ILE A  40     8292  10078   8576    173    904   -307       C  
ATOM    280  N   ASP A  41      40.732  19.495  63.040  1.00 91.26           N  
ANISOU  280  N   ASP A  41    10779  12585  11311    523    916   -575       N  
ATOM    281  CA  ASP A  41      39.491  19.049  62.429  1.00 90.65           C  
ANISOU  281  CA  ASP A  41    10532  12581  11329    598    913   -583       C  
ATOM    282  C   ASP A  41      39.657  17.741  61.638  1.00 85.90           C  
ANISOU  282  C   ASP A  41     9877  12025  10735    489    876   -454       C  
ATOM    283  O   ASP A  41      40.686  17.496  61.004  1.00 86.12           O  
ANISOU  283  O   ASP A  41    10011  11976  10734    417    812   -361       O  
ATOM    284  CB  ASP A  41      38.910  20.167  61.543  1.00 84.26           C  
ANISOU  284  CB  ASP A  41     9742  11645  10627    767    807   -632       C  
ATOM    285  CG  ASP A  41      37.394  20.083  61.406  1.00 86.75           C  
ANISOU  285  CG  ASP A  41     9854  12061  11046    893    826   -702       C  
ATOM    286  OD1 ASP A  41      36.760  19.263  62.110  1.00 94.97           O  
ANISOU  286  OD1 ASP A  41    10735  13282  12068    842    942   -725       O  
ATOM    287  OD2 ASP A  41      36.830  20.840  60.592  1.00 81.44           O  
ANISOU  287  OD2 ASP A  41     9178  11293  10475   1037    718   -730       O  
ATOM    288  N   LEU A  42      38.630  16.904  61.707  1.00 78.02           N  
ANISOU  288  N   LEU A  42     8712  11159   9772    475    921   -456       N  
ATOM    289  CA  LEU A  42      38.555  15.677  60.932  1.00 70.63           C  
ANISOU  289  CA  LEU A  42     7728  10256   8851    384    873   -351       C  
ATOM    290  C   LEU A  42      37.117  15.474  60.425  1.00 79.17           C  
ANISOU  290  C   LEU A  42     8628  11416  10036    445    848   -376       C  
ATOM    291  O   LEU A  42      36.138  15.672  61.169  1.00 89.03           O  
ANISOU  291  O   LEU A  42     9729  12789  11312    493    935   -462       O  
ATOM    292  CB  LEU A  42      38.994  14.481  61.779  1.00 51.67           C  
ANISOU  292  CB  LEU A  42     5330   7948   6355    226    949   -295       C  
ATOM    293  CG  LEU A  42      40.336  14.645  62.509  1.00 57.16           C  
ANISOU  293  CG  LEU A  42     6173   8597   6950    163    975   -277       C  
ATOM    294  CD1 LEU A  42      40.409  13.727  63.738  1.00 53.06           C  
ANISOU  294  CD1 LEU A  42     5636   8192   6332     34   1066   -257       C  
ATOM    295  CD2 LEU A  42      41.540  14.427  61.549  1.00 38.89           C  
ANISOU  295  CD2 LEU A  42     3980   6170   4629    134    881   -183       C  
ATOM    296  N   THR A  43      36.988  15.107  59.154  1.00 69.13           N  
ANISOU  296  N   THR A  43     7364  10083   8819    446    729   -305       N  
ATOM    297  CA  THR A  43      35.709  14.645  58.656  1.00 76.63           C  
ANISOU  297  CA  THR A  43     8141  11119   9857    461    686   -304       C  
ATOM    298  C   THR A  43      35.691  13.137  58.632  1.00 71.47           C  
ANISOU  298  C   THR A  43     7459  10537   9159    292    693   -217       C  
ATOM    299  O   THR A  43      36.575  12.468  59.157  1.00 75.06           O  
ANISOU  299  O   THR A  43     8013  10986   9519    182    744   -169       O  
ATOM    300  CB  THR A  43      35.429  15.135  57.240  1.00 79.79           C  
ANISOU  300  CB  THR A  43     8573  11406  10340    558    527   -279       C  
ATOM    301  OG1 THR A  43      36.396  14.570  56.352  1.00 77.90           O  
ANISOU  301  OG1 THR A  43     8497  11062  10038    475    453   -182       O  
ATOM    302  CG2 THR A  43      35.512  16.642  57.192  1.00 88.79           C  
ANISOU  302  CG2 THR A  43     9779  12437  11520    722    492   -353       C  
ATOM    303  N   CYS A  44      34.656  12.613  58.013  1.00 66.77           N  
ANISOU  303  N   CYS A  44     6731  10001   8637    272    626   -194       N  
ATOM    304  CA  CYS A  44      34.523  11.195  57.813  1.00 62.83           C  
ANISOU  304  CA  CYS A  44     6224   9544   8106    109    598   -109       C  
ATOM    305  C   CYS A  44      34.799  10.971  56.332  1.00 56.66           C  
ANISOU  305  C   CYS A  44     5559   8626   7342    125    440    -47       C  
ATOM    306  O   CYS A  44      34.203  11.622  55.472  1.00 56.96           O  
ANISOU  306  O   CYS A  44     5552   8628   7462    228    339    -66       O  
ATOM    307  CB  CYS A  44      33.107  10.749  58.218  1.00 61.89           C  
ANISOU  307  CB  CYS A  44     5864   9604   8048     49    634   -127       C  
ATOM    308  SG  CYS A  44      32.455   9.263  57.410  1.00 83.69           S  
ANISOU  308  SG  CYS A  44     8586  12388  10826   -127    513    -25       S  
ATOM    309  N   VAL A  45      35.715  10.058  56.040  1.00 57.80           N  
ANISOU  309  N   VAL A  45     5861   8694   7404     30    416     23       N  
ATOM    310  CA  VAL A  45      36.081   9.745  54.659  1.00 57.57           C  
ANISOU  310  CA  VAL A  45     5967   8544   7364     38    286     74       C  
ATOM    311  C   VAL A  45      35.247   8.578  54.154  1.00 58.14           C  
ANISOU  311  C   VAL A  45     5990   8645   7454    -74    197    121       C  
ATOM    312  O   VAL A  45      35.121   7.562  54.839  1.00 61.81           O  
ANISOU  312  O   VAL A  45     6431   9170   7885   -205    240    152       O  
ATOM    313  CB  VAL A  45      37.588   9.396  54.540  1.00 55.14           C  
ANISOU  313  CB  VAL A  45     5856   8138   6955     18    310    111       C  
ATOM    314  CG1 VAL A  45      37.942   8.979  53.108  1.00 52.67           C  
ANISOU  314  CG1 VAL A  45     5683   7718   6611     23    196    153       C  
ATOM    315  CG2 VAL A  45      38.446  10.582  55.012  1.00 51.36           C  
ANISOU  315  CG2 VAL A  45     5426   7630   6457    104    383     73       C  
ATOM    316  N   PRO A  46      34.648   8.728  52.963  1.00 55.45           N  
ANISOU  316  N   PRO A  46     5647   8259   7163    -36     58    132       N  
ATOM    317  CA  PRO A  46      33.826   7.630  52.440  1.00 60.90           C  
ANISOU  317  CA  PRO A  46     6299   8970   7868   -157    -48    177       C  
ATOM    318  C   PRO A  46      34.681   6.430  52.044  1.00 60.01           C  
ANISOU  318  C   PRO A  46     6395   8754   7654   -251    -82    228       C  
ATOM    319  O   PRO A  46      35.629   6.581  51.277  1.00 60.53           O  
ANISOU  319  O   PRO A  46     6639   8704   7656   -185   -109    232       O  
ATOM    320  CB  PRO A  46      33.143   8.243  51.214  1.00 53.39           C  
ANISOU  320  CB  PRO A  46     5325   7977   6983    -74   -203    174       C  
ATOM    321  CG  PRO A  46      33.269   9.724  51.395  1.00 47.41           C  
ANISOU  321  CG  PRO A  46     4526   7212   6274     93   -161    119       C  
ATOM    322  CD  PRO A  46      34.499   9.975  52.190  1.00 44.89           C  
ANISOU  322  CD  PRO A  46     4316   6861   5877    111    -16    102       C  
ATOM    323  N   ASN A  47      34.348   5.252  52.562  1.00 53.34           N  
ANISOU  323  N   ASN A  47     5530   7948   6788   -404    -79    266       N  
ATOM    324  CA  ASN A  47      35.129   4.055  52.284  1.00 49.44           C  
ANISOU  324  CA  ASN A  47     5242   7339   6202   -480   -119    306       C  
ATOM    325  C   ASN A  47      36.441   4.073  53.021  1.00 50.53           C  
ANISOU  325  C   ASN A  47     5485   7442   6271   -434     -1    300       C  
ATOM    326  O   ASN A  47      37.291   3.217  52.802  1.00 56.83           O  
ANISOU  326  O   ASN A  47     6458   8139   6997   -451    -24    321       O  
ATOM    327  CB  ASN A  47      35.376   3.932  50.798  1.00 51.10           C  
ANISOU  327  CB  ASN A  47     5615   7423   6377   -429   -250    308       C  
ATOM    328  CG  ASN A  47      34.094   3.897  50.021  1.00 61.85           C  
ANISOU  328  CG  ASN A  47     6884   8813   7804   -480   -395    320       C  
ATOM    329  OD1 ASN A  47      33.047   3.549  50.569  1.00 59.36           O  
ANISOU  329  OD1 ASN A  47     6397   8604   7552   -594   -410    340       O  
ATOM    330  ND2 ASN A  47      34.153   4.264  48.739  1.00 66.63           N  
ANISOU  330  ND2 ASN A  47     7596   9333   8389   -407   -507    313       N  
ATOM    331  N   GLY A  48      36.588   5.063  53.900  1.00 49.14           N  
ANISOU  331  N   GLY A  48     5202   7350   6120   -370    118    266       N  
ATOM    332  CA  GLY A  48      37.790   5.247  54.687  1.00 43.19           C  
ANISOU  332  CA  GLY A  48     4523   6579   5308   -330    223    259       C  
ATOM    333  C   GLY A  48      38.489   3.960  55.089  1.00 40.80           C  
ANISOU  333  C   GLY A  48     4353   6217   4931   -417    218    306       C  
ATOM    334  O   GLY A  48      39.704   3.838  54.945  1.00 40.03           O  
ANISOU  334  O   GLY A  48     4385   6043   4781   -352    231    308       O  
ATOM    335  N   GLN A  49      37.735   2.993  55.596  1.00 40.07           N  
ANISOU  335  N   GLN A  49     4227   6162   4837   -565    191    347       N  
ATOM    336  CA  GLN A  49      38.366   1.777  56.096  1.00 50.78           C  
ANISOU  336  CA  GLN A  49     5725   7445   6123   -650    172    398       C  
ATOM    337  C   GLN A  49      38.952   0.960  54.959  1.00 48.75           C  
ANISOU  337  C   GLN A  49     5659   7030   5832   -608     59    406       C  
ATOM    338  O   GLN A  49      40.093   0.496  55.039  1.00 50.76           O  
ANISOU  338  O   GLN A  49     6053   7198   6034   -549     62    410       O  
ATOM    339  CB  GLN A  49      37.392   0.935  56.924  1.00 53.59           C  
ANISOU  339  CB  GLN A  49     6018   7872   6472   -845    164    453       C  
ATOM    340  CG  GLN A  49      37.310   1.357  58.380  1.00 71.96           C  
ANISOU  340  CG  GLN A  49     8234  10333   8775   -899    300    455       C  
ATOM    341  CD  GLN A  49      36.611   0.322  59.252  1.00 93.23           C  
ANISOU  341  CD  GLN A  49    10916  13083  11425  -1119    296    528       C  
ATOM    342  OE1 GLN A  49      35.864  -0.529  58.754  1.00 95.01           O  
ANISOU  342  OE1 GLN A  49    11157  13278  11665  -1246    194    573       O  
ATOM    343  NE2 GLN A  49      36.851   0.389  60.563  1.00101.13           N  
ANISOU  343  NE2 GLN A  49    11900  14163  12360  -1182    400    546       N  
ATOM    344  N   GLU A  50      38.159   0.774  53.910  1.00 44.74           N  
ANISOU  344  N   GLU A  50     5156   6490   5351   -633    -44    401       N  
ATOM    345  CA  GLU A  50      38.632   0.128  52.693  1.00 49.49           C  
ANISOU  345  CA  GLU A  50     5949   6947   5909   -581   -149    390       C  
ATOM    346  C   GLU A  50      39.904   0.799  52.118  1.00 47.36           C  
ANISOU  346  C   GLU A  50     5757   6635   5602   -402    -91    344       C  
ATOM    347  O   GLU A  50      40.856   0.122  51.728  1.00 49.04           O  
ANISOU  347  O   GLU A  50     6132   6746   5755   -339   -110    332       O  
ATOM    348  CB  GLU A  50      37.512   0.088  51.654  1.00 57.38           C  
ANISOU  348  CB  GLU A  50     6922   7938   6941   -635   -270    388       C  
ATOM    349  CG  GLU A  50      36.619  -1.092  51.820  1.00 67.73           C  
ANISOU  349  CG  GLU A  50     8260   9222   8254   -823   -376    439       C  
ATOM    350  CD  GLU A  50      37.419  -2.345  52.140  1.00 92.40           C  
ANISOU  350  CD  GLU A  50    11594  12208  11304   -858   -410    463       C  
ATOM    351  OE1 GLU A  50      38.319  -2.703  51.342  1.00 98.15           O  
ANISOU  351  OE1 GLU A  50    12513  12803  11974   -742   -448    425       O  
ATOM    352  OE2 GLU A  50      37.160  -2.969  53.197  1.00100.19           O  
ANISOU  352  OE2 GLU A  50    12560  13220  12286   -998   -397    519       O  
ATOM    353  N   ILE A  51      39.921   2.125  52.115  1.00 43.89           N  
ANISOU  353  N   ILE A  51     5199   6279   5199   -325    -17    318       N  
ATOM    354  CA  ILE A  51      41.041   2.872  51.584  1.00 45.17           C  
ANISOU  354  CA  ILE A  51     5418   6419   5326   -190     39    287       C  
ATOM    355  C   ILE A  51      42.310   2.671  52.413  1.00 44.12           C  
ANISOU  355  C   ILE A  51     5322   6286   5158   -147    126    291       C  
ATOM    356  O   ILE A  51      43.389   2.515  51.855  1.00 51.45           O  
ANISOU  356  O   ILE A  51     6349   7164   6034    -58    142    273       O  
ATOM    357  CB  ILE A  51      40.703   4.373  51.474  1.00 40.94           C  
ANISOU  357  CB  ILE A  51     4762   5955   4839   -135     80    267       C  
ATOM    358  CG1 ILE A  51      39.588   4.602  50.445  1.00 42.23           C  
ANISOU  358  CG1 ILE A  51     4905   6105   5036   -148    -31    264       C  
ATOM    359  CG2 ILE A  51      41.952   5.168  51.134  1.00 32.20           C  
ANISOU  359  CG2 ILE A  51     3713   4835   3688    -31    149    251       C  
ATOM    360  CD1 ILE A  51      39.153   6.083  50.348  1.00 44.59           C  
ANISOU  360  CD1 ILE A  51     5091   6455   5394    -80    -17    246       C  
ATOM    361  N   ILE A  52      42.171   2.688  53.740  1.00 48.61           N  
ANISOU  361  N   ILE A  52     5802   6920   5749   -211    181    313       N  
ATOM    362  CA  ILE A  52      43.289   2.500  54.664  1.00 48.58           C  
ANISOU  362  CA  ILE A  52     5824   6921   5715   -186    242    327       C  
ATOM    363  C   ILE A  52      43.837   1.075  54.554  1.00 49.87           C  
ANISOU  363  C   ILE A  52     6136   6977   5834   -187    172    347       C  
ATOM    364  O   ILE A  52      45.038   0.884  54.563  1.00 49.68           O  
ANISOU  364  O   ILE A  52     6171   6922   5782    -94    193    339       O  
ATOM    365  CB  ILE A  52      42.867   2.749  56.140  1.00 49.49           C  
ANISOU  365  CB  ILE A  52     5833   7128   5844   -277    304    349       C  
ATOM    366  CG1 ILE A  52      42.664   4.239  56.421  1.00 56.67           C  
ANISOU  366  CG1 ILE A  52     6615   8129   6787   -237    387    311       C  
ATOM    367  CG2 ILE A  52      43.888   2.132  57.125  1.00 40.33           C  
ANISOU  367  CG2 ILE A  52     4738   5948   4639   -285    320    382       C  
ATOM    368  CD1 ILE A  52      43.918   5.104  56.358  1.00 52.76           C  
ANISOU  368  CD1 ILE A  52     6140   7632   6274   -139    440    292       C  
ATOM    369  N   HIS A  53      42.957   0.080  54.463  1.00 42.04           N  
ANISOU  369  N   HIS A  53     5204   5927   4841   -290     82    373       N  
ATOM    370  CA  HIS A  53      43.380  -1.301  54.215  1.00 45.73           C  
ANISOU  370  CA  HIS A  53     5849   6257   5268   -284    -11    385       C  
ATOM    371  C   HIS A  53      44.234  -1.442  52.937  1.00 52.09           C  
ANISOU  371  C   HIS A  53     6771   6982   6037   -131    -29    327       C  
ATOM    372  O   HIS A  53      45.324  -2.036  52.956  1.00 51.38           O  
ANISOU  372  O   HIS A  53     6777   6828   5917    -27    -32    311       O  
ATOM    373  CB  HIS A  53      42.179  -2.252  54.150  1.00 41.69           C  
ANISOU  373  CB  HIS A  53     5395   5688   4759   -443   -122    423       C  
ATOM    374  CG  HIS A  53      41.522  -2.493  55.473  1.00 75.48           C  
ANISOU  374  CG  HIS A  53     9598  10033   9046   -609   -106    490       C  
ATOM    375  ND1 HIS A  53      42.216  -2.503  56.668  1.00 84.30           N  
ANISOU  375  ND1 HIS A  53    10708  11182  10142   -611    -48    521       N  
ATOM    376  CD2 HIS A  53      40.227  -2.751  55.797  1.00 91.03           C  
ANISOU  376  CD2 HIS A  53    11495  12058  11035   -791   -139    533       C  
ATOM    377  CE1 HIS A  53      41.381  -2.739  57.665  1.00 88.22           C  
ANISOU  377  CE1 HIS A  53    11145  11747  10629   -787    -37    580       C  
ATOM    378  NE2 HIS A  53      40.168  -2.897  57.161  1.00 95.32           N  
ANISOU  378  NE2 HIS A  53    11994  12669  11556   -900    -84    588       N  
ATOM    379  N   SER A  54      43.733  -0.890  51.835  1.00 45.21           N  
ANISOU  379  N   SER A  54     5890   6124   5164   -112    -41    294       N  
ATOM    380  CA  SER A  54      44.470  -0.880  50.588  1.00 45.90           C  
ANISOU  380  CA  SER A  54     6084   6162   5196     18    -38    237       C  
ATOM    381  C   SER A  54      45.827  -0.271  50.810  1.00 49.73           C  
ANISOU  381  C   SER A  54     6515   6712   5669    141     76    218       C  
ATOM    382  O   SER A  54      46.831  -0.821  50.371  1.00 58.50           O  
ANISOU  382  O   SER A  54     7718   7776   6734    257     89    180       O  
ATOM    383  CB  SER A  54      43.730  -0.089  49.509  1.00 48.75           C  
ANISOU  383  CB  SER A  54     6421   6550   5551      5    -61    219       C  
ATOM    384  OG  SER A  54      42.625  -0.826  49.034  1.00 51.99           O  
ANISOU  384  OG  SER A  54     6908   6887   5961    -95   -190    228       O  
ATOM    385  N   LEU A  55      45.866   0.869  51.484  1.00 48.37           N  
ANISOU  385  N   LEU A  55     6191   6650   5537    119    158    241       N  
ATOM    386  CA  LEU A  55      47.138   1.565  51.662  1.00 50.56           C  
ANISOU  386  CA  LEU A  55     6409   6999   5804    210    259    230       C  
ATOM    387  C   LEU A  55      48.138   0.749  52.473  1.00 46.21           C  
ANISOU  387  C   LEU A  55     5879   6426   5251    263    262    240       C  
ATOM    388  O   LEU A  55      49.344   0.846  52.256  1.00 55.69           O  
ANISOU  388  O   LEU A  55     7067   7660   6431    371    318    217       O  
ATOM    389  CB  LEU A  55      46.926   2.909  52.331  1.00 39.25           C  
ANISOU  389  CB  LEU A  55     4833   5666   4413    161    325    252       C  
ATOM    390  CG  LEU A  55      46.633   4.046  51.393  1.00 38.08           C  
ANISOU  390  CG  LEU A  55     4663   5548   4258    174    345    237       C  
ATOM    391  CD1 LEU A  55      46.341   5.245  52.253  1.00 43.35           C  
ANISOU  391  CD1 LEU A  55     5210   6287   4976    130    392    252       C  
ATOM    392  CD2 LEU A  55      47.854   4.282  50.481  1.00 37.91           C  
ANISOU  392  CD2 LEU A  55     4689   5543   4173    265    403    215       C  
ATOM    393  N   LEU A  56      47.634  -0.032  53.425  1.00 42.03           N  
ANISOU  393  N   LEU A  56     5377   5849   4743    181    198    279       N  
ATOM    394  CA  LEU A  56      48.506  -0.848  54.259  1.00 48.42           C  
ANISOU  394  CA  LEU A  56     6227   6620   5552    226    172    300       C  
ATOM    395  C   LEU A  56      49.090  -1.937  53.383  1.00 51.12           C  
ANISOU  395  C   LEU A  56     6715   6847   5860    352    115    253       C  
ATOM    396  O   LEU A  56      50.290  -2.209  53.420  1.00 53.06           O  
ANISOU  396  O   LEU A  56     6961   7097   6103    486    135    230       O  
ATOM    397  CB  LEU A  56      47.780  -1.447  55.485  1.00 33.31           C  
ANISOU  397  CB  LEU A  56     4332   4674   3649     85    110    365       C  
ATOM    398  CG  LEU A  56      47.434  -0.483  56.636  1.00 44.31           C  
ANISOU  398  CG  LEU A  56     5588   6189   5060    -19    181    402       C  
ATOM    399  CD1 LEU A  56      46.398  -1.090  57.547  1.00 51.41           C  
ANISOU  399  CD1 LEU A  56     6512   7072   5951   -183    132    459       C  
ATOM    400  CD2 LEU A  56      48.626  -0.070  57.443  1.00 40.66           C  
ANISOU  400  CD2 LEU A  56     5067   5787   4597     40    225    415       C  
ATOM    401  N   GLN A  57      48.243  -2.554  52.577  1.00 45.19           N  
ANISOU  401  N   GLN A  57     6086   5999   5085    315     39    232       N  
ATOM    402  CA  GLN A  57      48.756  -3.554  51.666  1.00 44.98           C  
ANISOU  402  CA  GLN A  57     6224   5853   5014    443    -15    170       C  
ATOM    403  C   GLN A  57      49.819  -2.956  50.728  1.00 42.62           C  
ANISOU  403  C   GLN A  57     5878   5637   4679    603     95    100       C  
ATOM    404  O   GLN A  57      50.903  -3.507  50.592  1.00 47.19           O  
ANISOU  404  O   GLN A  57     6492   6194   5244    759    111     55       O  
ATOM    405  CB  GLN A  57      47.622  -4.186  50.890  1.00 37.77           C  
ANISOU  405  CB  GLN A  57     5456   4825   4070    357   -120    156       C  
ATOM    406  CG  GLN A  57      48.093  -5.210  49.865  1.00 44.66           C  
ANISOU  406  CG  GLN A  57     6530   5558   4879    493   -180     74       C  
ATOM    407  CD  GLN A  57      47.026  -5.461  48.828  1.00 52.94           C  
ANISOU  407  CD  GLN A  57     7705   6528   5882    408   -266     50       C  
ATOM    408  OE1 GLN A  57      45.993  -6.051  49.133  1.00 53.48           O  
ANISOU  408  OE1 GLN A  57     7843   6511   5968    252   -384     98       O  
ATOM    409  NE2 GLN A  57      47.247  -4.969  47.602  1.00 55.38           N  
ANISOU  409  NE2 GLN A  57     8040   6877   6126    491   -209    -18       N  
ATOM    410  N   LEU A  58      49.514  -1.801  50.144  1.00 46.11           N  
ANISOU  410  N   LEU A  58     6232   6181   5106    559    171     98       N  
ATOM    411  CA  LEU A  58      50.337  -1.173  49.115  1.00 49.76           C  
ANISOU  411  CA  LEU A  58     6667   6726   5512    666    275     45       C  
ATOM    412  C   LEU A  58      51.601  -0.500  49.655  1.00 54.67           C  
ANISOU  412  C   LEU A  58     7132   7482   6159    734    385     56       C  
ATOM    413  O   LEU A  58      52.614  -0.462  48.967  1.00 58.10           O  
ANISOU  413  O   LEU A  58     7551   7978   6547    855    466      5       O  
ATOM    414  CB  LEU A  58      49.505  -0.151  48.322  1.00 46.18           C  
ANISOU  414  CB  LEU A  58     6197   6317   5031    575    291     55       C  
ATOM    415  CG  LEU A  58      48.365  -0.659  47.428  1.00 50.56           C  
ANISOU  415  CG  LEU A  58     6901   6765   5544    518    184     34       C  
ATOM    416  CD1 LEU A  58      47.483   0.501  46.965  1.00 45.44           C  
ANISOU  416  CD1 LEU A  58     6193   6172   4899    421    181     66       C  
ATOM    417  CD2 LEU A  58      48.879  -1.422  46.228  1.00 48.00           C  
ANISOU  417  CD2 LEU A  58     6747   6374   5118    635    181    -50       C  
ATOM    418  N   VAL A  59      51.535   0.071  50.854  1.00 51.79           N  
ANISOU  418  N   VAL A  59     6646   7173   5859    649    391    121       N  
ATOM    419  CA  VAL A  59      52.717   0.612  51.518  1.00 46.39           C  
ANISOU  419  CA  VAL A  59     5819   6604   5203    694    466    140       C  
ATOM    420  C   VAL A  59      53.566  -0.579  51.995  1.00 50.57           C  
ANISOU  420  C   VAL A  59     6383   7080   5752    819    416    123       C  
ATOM    421  O   VAL A  59      54.788  -0.489  52.160  1.00 40.11           O  
ANISOU  421  O   VAL A  59     4956   5843   4442    921    469    112       O  
ATOM    422  CB  VAL A  59      52.318   1.517  52.680  1.00 47.36           C  
ANISOU  422  CB  VAL A  59     5835   6783   5375    563    471    205       C  
ATOM    423  CG1 VAL A  59      53.525   1.832  53.580  1.00 46.76           C  
ANISOU  423  CG1 VAL A  59     5635   6801   5329    595    508    231       C  
ATOM    424  CG2 VAL A  59      51.716   2.807  52.140  1.00 50.46           C  
ANISOU  424  CG2 VAL A  59     6187   7231   5755    481    522    211       C  
ATOM    425  N   GLY A  60      52.907  -1.718  52.184  1.00 46.52           N  
ANISOU  425  N   GLY A  60     6016   6416   5242    812    302    122       N  
ATOM    426  CA  GLY A  60      53.621  -2.939  52.495  1.00 52.20           C  
ANISOU  426  CA  GLY A  60     6813   7043   5977    946    228    101       C  
ATOM    427  C   GLY A  60      54.458  -3.352  51.293  1.00 58.02           C  
ANISOU  427  C   GLY A  60     7593   7785   6669   1139    282      2       C  
ATOM    428  O   GLY A  60      55.642  -3.682  51.437  1.00 50.61           O  
ANISOU  428  O   GLY A  60     6588   6890   5753   1299    305    -30       O  
ATOM    429  N   ASP A  61      53.833  -3.335  50.110  1.00 48.29           N  
ANISOU  429  N   ASP A  61     6467   6514   5368   1125    300    -51       N  
ATOM    430  CA  ASP A  61      54.531  -3.606  48.861  1.00 50.11           C  
ANISOU  430  CA  ASP A  61     6748   6766   5525   1291    375   -154       C  
ATOM    431  C   ASP A  61      55.723  -2.687  48.784  1.00 56.26           C  
ANISOU  431  C   ASP A  61     7319   7752   6307   1356    525   -159       C  
ATOM    432  O   ASP A  61      56.836  -3.129  48.494  1.00 59.91           O  
ANISOU  432  O   ASP A  61     7735   8266   6761   1540    582   -227       O  
ATOM    433  CB  ASP A  61      53.629  -3.361  47.651  1.00 61.57           C  
ANISOU  433  CB  ASP A  61     8323   8183   6888   1219    383   -189       C  
ATOM    434  CG  ASP A  61      52.540  -4.425  47.488  1.00 74.66           C  
ANISOU  434  CG  ASP A  61    10205   9634   8530   1167    226   -201       C  
ATOM    435  OD1 ASP A  61      52.727  -5.579  47.943  1.00 76.36           O  
ANISOU  435  OD1 ASP A  61    10532   9710   8772   1247    126   -220       O  
ATOM    436  OD2 ASP A  61      51.494  -4.098  46.881  1.00 79.06           O  
ANISOU  436  OD2 ASP A  61    10830  10162   9045   1040    191   -189       O  
ATOM    437  N   PHE A  62      55.493  -1.407  49.063  1.00 50.65           N  
ANISOU  437  N   PHE A  62     6476   7158   5610   1205    586    -88       N  
ATOM    438  CA  PHE A  62      56.553  -0.410  48.968  1.00 53.05           C  
ANISOU  438  CA  PHE A  62     6589   7659   5911   1220    720    -77       C  
ATOM    439  C   PHE A  62      57.694  -0.681  49.940  1.00 53.34           C  
ANISOU  439  C   PHE A  62     6477   7765   6025   1315    717    -61       C  
ATOM    440  O   PHE A  62      58.855  -0.600  49.563  1.00 53.18           O  
ANISOU  440  O   PHE A  62     6331   7879   5994   1433    815   -101       O  
ATOM    441  CB  PHE A  62      55.997   1.009  49.177  1.00 53.53           C  
ANISOU  441  CB  PHE A  62     6571   7793   5977   1029    755      1       C  
ATOM    442  CG  PHE A  62      57.041   2.084  49.173  1.00 47.39           C  
ANISOU  442  CG  PHE A  62     5612   7199   5194   1004    873     28       C  
ATOM    443  CD1 PHE A  62      57.156   2.945  48.100  1.00 52.97           C  
ANISOU  443  CD1 PHE A  62     6314   7996   5816    955    974     22       C  
ATOM    444  CD2 PHE A  62      57.882   2.256  50.251  1.00 54.90           C  
ANISOU  444  CD2 PHE A  62     6408   8232   6221   1010    870     70       C  
ATOM    445  CE1 PHE A  62      58.109   3.954  48.082  1.00 54.91           C  
ANISOU  445  CE1 PHE A  62     6401   8412   6051    902   1077     60       C  
ATOM    446  CE2 PHE A  62      58.850   3.279  50.252  1.00 54.71           C  
ANISOU  446  CE2 PHE A  62     6212   8382   6193    961    968    103       C  
ATOM    447  CZ  PHE A  62      58.955   4.128  49.167  1.00 56.15           C  
ANISOU  447  CZ  PHE A  62     6390   8654   6291    900   1074     99       C  
ATOM    448  N   ASN A  63      57.373  -0.986  51.197  1.00 48.65           N  
ANISOU  448  N   ASN A  63     5889   7091   5505   1258    604      2       N  
ATOM    449  CA  ASN A  63      58.415  -1.122  52.212  1.00 48.20           C  
ANISOU  449  CA  ASN A  63     5691   7102   5521   1325    578     34       C  
ATOM    450  C   ASN A  63      59.318  -2.284  51.868  1.00 46.91           C  
ANISOU  450  C   ASN A  63     5547   6906   5370   1565    558    -46       C  
ATOM    451  O   ASN A  63      60.536  -2.164  51.815  1.00 57.02           O  
ANISOU  451  O   ASN A  63     6657   8331   6677   1686    626    -71       O  
ATOM    452  CB  ASN A  63      57.807  -1.328  53.607  1.00 49.11           C  
ANISOU  452  CB  ASN A  63     5851   7120   5689   1210    449    117       C  
ATOM    453  CG  ASN A  63      57.340  -0.026  54.242  1.00 54.93           C  
ANISOU  453  CG  ASN A  63     6500   7941   6431   1010    486    189       C  
ATOM    454  OD1 ASN A  63      57.744   1.061  53.841  1.00 54.68           O  
ANISOU  454  OD1 ASN A  63     6349   8044   6383    966    590    191       O  
ATOM    455  ND2 ASN A  63      56.471  -0.138  55.235  1.00 62.46           N  
ANISOU  455  ND2 ASN A  63     7521   8810   7399    886    401    246       N  
ATOM    456  N   GLN A  64      58.689  -3.413  51.623  1.00 49.79           N  
ANISOU  456  N   GLN A  64     6123   7079   5717   1631    459    -89       N  
ATOM    457  CA  GLN A  64      59.390  -4.634  51.272  1.00 56.57           C  
ANISOU  457  CA  GLN A  64     7054   7855   6584   1876    416   -179       C  
ATOM    458  C   GLN A  64      60.413  -4.431  50.112  1.00 57.78           C  
ANISOU  458  C   GLN A  64     7090   8174   6689   2049    582   -285       C  
ATOM    459  O   GLN A  64      61.520  -4.968  50.160  1.00 59.34           O  
ANISOU  459  O   GLN A  64     7189   8428   6930   2263    594   -342       O  
ATOM    460  CB  GLN A  64      58.357  -5.749  51.036  1.00 54.10           C  
ANISOU  460  CB  GLN A  64     7026   7290   6238   1875    281   -208       C  
ATOM    461  CG  GLN A  64      58.851  -6.948  50.317  1.00 65.63           C  
ANISOU  461  CG  GLN A  64     8627   8633   7675   2124    246   -330       C  
ATOM    462  CD  GLN A  64      58.923  -6.718  48.825  1.00 73.33           C  
ANISOU  462  CD  GLN A  64     9633   9682   8546   2197    390   -442       C  
ATOM    463  OE1 GLN A  64      57.966  -6.230  48.201  1.00 66.84           O  
ANISOU  463  OE1 GLN A  64     8899   8847   7651   2034    419   -430       O  
ATOM    464  NE2 GLN A  64      60.065  -7.073  48.236  1.00 76.59           N  
ANISOU  464  NE2 GLN A  64     9973  10182   8947   2446    481   -554       N  
ATOM    465  N   ARG A  65      60.074  -3.609  49.120  1.00 53.39           N  
ANISOU  465  N   ARG A  65     6531   7713   6043   1953    711   -305       N  
ATOM    466  CA  ARG A  65      61.014  -3.263  48.037  1.00 63.32           C  
ANISOU  466  CA  ARG A  65     7668   9159   7231   2070    892   -389       C  
ATOM    467  C   ARG A  65      62.099  -2.248  48.422  1.00 70.61           C  
ANISOU  467  C   ARG A  65     8294  10336   8199   2031   1005   -334       C  
ATOM    468  O   ARG A  65      63.208  -2.312  47.914  1.00 81.58           O  
ANISOU  468  O   ARG A  65     9531  11892   9574   2184   1126   -402       O  
ATOM    469  CB  ARG A  65      60.270  -2.758  46.781  1.00 55.43           C  
ANISOU  469  CB  ARG A  65     6798   8165   6099   1966    979   -421       C  
ATOM    470  CG  ARG A  65      59.359  -3.801  46.171  1.00 66.87           C  
ANISOU  470  CG  ARG A  65     8535   9387   7486   2021    879   -495       C  
ATOM    471  CD  ARG A  65      58.339  -3.227  45.180  1.00 85.09           C  
ANISOU  471  CD  ARG A  65    10985  11668   9678   1863    906   -491       C  
ATOM    472  NE  ARG A  65      57.166  -4.104  45.069  1.00 95.50           N  
ANISOU  472  NE  ARG A  65    12562  12745  10981   1828    745   -509       N  
ATOM    473  CZ  ARG A  65      56.407  -4.241  43.983  1.00 92.14           C  
ANISOU  473  CZ  ARG A  65    12332  12238  10440   1787    731   -560       C  
ATOM    474  NH1 ARG A  65      56.695  -3.575  42.877  1.00 92.53           N  
ANISOU  474  NH1 ARG A  65    12367  12424  10367   1782    873   -600       N  
ATOM    475  NH2 ARG A  65      55.365  -5.065  43.999  1.00 87.28           N  
ANISOU  475  NH2 ARG A  65    11934  11405   9823   1737    566   -565       N  
ATOM    476  N   PHE A  66      61.778  -1.308  49.300  1.00 66.51           N  
ANISOU  476  N   PHE A  66     7692   9852   7729   1823    968   -215       N  
ATOM    477  CA  PHE A  66      62.662  -0.181  49.572  1.00 72.14           C  
ANISOU  477  CA  PHE A  66     8153  10791   8465   1732   1067   -154       C  
ATOM    478  C   PHE A  66      63.766  -0.559  50.553  1.00 76.38           C  
ANISOU  478  C   PHE A  66     8500  11406   9113   1851   1011   -137       C  
ATOM    479  O   PHE A  66      64.839   0.049  50.569  1.00 75.34           O  
ANISOU  479  O   PHE A  66     8129  11493   9004   1851   1104   -120       O  
ATOM    480  CB  PHE A  66      61.831   0.992  50.095  1.00 73.90           C  
ANISOU  480  CB  PHE A  66     8394  10997   8688   1469   1038    -47       C  
ATOM    481  CG  PHE A  66      62.629   2.077  50.771  1.00 70.50           C  
ANISOU  481  CG  PHE A  66     7742  10742   8303   1349   1077     33       C  
ATOM    482  CD1 PHE A  66      62.701   3.349  50.218  1.00 67.89           C  
ANISOU  482  CD1 PHE A  66     7349  10537   7911   1186   1186     74       C  
ATOM    483  CD2 PHE A  66      63.278   1.841  51.972  1.00 64.39           C  
ANISOU  483  CD2 PHE A  66     6844   9995   7629   1383    986     76       C  
ATOM    484  CE1 PHE A  66      63.416   4.365  50.845  1.00 56.77           C  
ANISOU  484  CE1 PHE A  66     5757   9273   6540   1054   1206    151       C  
ATOM    485  CE2 PHE A  66      64.000   2.849  52.601  1.00 65.45           C  
ANISOU  485  CE2 PHE A  66     6785  10284   7799   1255   1005    151       C  
ATOM    486  CZ  PHE A  66      64.061   4.109  52.042  1.00 62.15           C  
ANISOU  486  CZ  PHE A  66     6309   9985   7321   1087   1115    187       C  
ATOM    487  N   SER A  67      63.505  -1.566  51.377  1.00 74.39           N  
ANISOU  487  N   SER A  67     8357  10978   8930   1941    847   -133       N  
ATOM    488  CA  SER A  67      64.556  -2.128  52.208  1.00 78.26           C  
ANISOU  488  CA  SER A  67     8697  11515   9523   2096    767   -126       C  
ATOM    489  C   SER A  67      65.522  -2.965  51.355  1.00 78.44           C  
ANISOU  489  C   SER A  67     8647  11610   9546   2388    843   -255       C  
ATOM    490  O   SER A  67      66.652  -3.225  51.753  1.00 87.50           O  
ANISOU  490  O   SER A  67     9592  12877  10778   2543    828   -267       O  
ATOM    491  CB  SER A  67      63.950  -2.982  53.305  1.00 88.69           C  
ANISOU  491  CB  SER A  67    10189  12609  10901   2098    559    -77       C  
ATOM    492  OG  SER A  67      63.270  -4.084  52.734  1.00102.60           O  
ANISOU  492  OG  SER A  67    12199  14160  12623   2213    501   -153       O  
ATOM    493  N   GLN A  68      65.078  -3.378  50.175  1.00 78.57           N  
ANISOU  493  N   GLN A  68     8827  11559   9466   2468    924   -357       N  
ATOM    494  CA  GLN A  68      65.954  -4.078  49.238  1.00 91.71           C  
ANISOU  494  CA  GLN A  68    10433  13309  11105   2745   1030   -500       C  
ATOM    495  C   GLN A  68      66.980  -3.173  48.564  1.00 93.26           C  
ANISOU  495  C   GLN A  68    10346  13828  11261   2736   1249   -520       C  
ATOM    496  O   GLN A  68      68.129  -3.564  48.380  1.00 91.42           O  
ANISOU  496  O   GLN A  68     9912  13754  11071   2958   1321   -597       O  
ATOM    497  CB  GLN A  68      65.140  -4.743  48.136  1.00 94.38           C  
ANISOU  497  CB  GLN A  68    11056  13478  11326   2814   1052   -608       C  
ATOM    498  CG  GLN A  68      64.627  -6.117  48.460  1.00 97.46           C  
ANISOU  498  CG  GLN A  68    11706  13572  11753   2964    859   -656       C  
ATOM    499  CD  GLN A  68      63.744  -6.640  47.351  1.00103.38           C  
ANISOU  499  CD  GLN A  68    12747  14158  12376   2982    873   -753       C  
ATOM    500  OE1 GLN A  68      62.905  -7.508  47.570  1.00107.14           O  
ANISOU  500  OE1 GLN A  68    13487  14366  12856   2983    705   -757       O  
ATOM    501  NE2 GLN A  68      63.916  -6.094  46.149  1.00105.50           N  
ANISOU  501  NE2 GLN A  68    12977  14587  12520   2975   1069   -824       N  
ATOM    502  N   THR A  69      66.557  -1.974  48.183  1.00 97.64           N  
ANISOU  502  N   THR A  69    10884  14481  11733   2478   1353   -449       N  
ATOM    503  CA  THR A  69      67.335  -1.168  47.252  1.00102.52           C  
ANISOU  503  CA  THR A  69    11307  15378  12266   2440   1576   -474       C  
ATOM    504  C   THR A  69      67.646   0.237  47.743  1.00101.48           C  
ANISOU  504  C   THR A  69    10973  15427  12157   2174   1618   -337       C  
ATOM    505  O   THR A  69      68.052   1.085  46.958  1.00111.06           O  
ANISOU  505  O   THR A  69    12075  16844  13279   2062   1790   -326       O  
ATOM    506  CB  THR A  69      66.624  -1.059  45.883  1.00106.50           C  
ANISOU  506  CB  THR A  69    12025  15844  12598   2395   1694   -542       C  
ATOM    507  OG1 THR A  69      65.275  -0.603  46.071  1.00101.61           O  
ANISOU  507  OG1 THR A  69    11629  15028  11949   2171   1586   -457       O  
ATOM    508  CG2 THR A  69      66.601  -2.412  45.184  1.00108.73           C  
ANISOU  508  CG2 THR A  69    12478  16000  12834   2680   1693   -705       C  
ATOM    509  N   HIS A  70      67.458   0.486  49.031  1.00 88.96           N  
ANISOU  509  N   HIS A  70     9359  13762  10681   2063   1459   -231       N  
ATOM    510  CA  HIS A  70      67.744   1.798  49.597  1.00 89.72           C  
ANISOU  510  CA  HIS A  70     9289  14000  10800   1812   1473   -107       C  
ATOM    511  C   HIS A  70      67.840   1.704  51.101  1.00 92.95           C  
ANISOU  511  C   HIS A  70     9643  14336  11338   1780   1288    -26       C  
ATOM    512  O   HIS A  70      67.294   0.790  51.718  1.00 95.77           O  
ANISOU  512  O   HIS A  70    10159  14485  11746   1882   1136    -40       O  
ATOM    513  CB  HIS A  70      66.636   2.802  49.289  1.00 91.08           C  
ANISOU  513  CB  HIS A  70     9645  14081  10881   1554   1488    -41       C  
ATOM    514  CG  HIS A  70      66.385   3.022  47.828  1.00 95.09           C  
ANISOU  514  CG  HIS A  70    10250  14637  11241   1539   1646    -99       C  
ATOM    515  ND1 HIS A  70      67.185   3.822  47.055  1.00 99.62           N  
ANISOU  515  ND1 HIS A  70    10660  15455  11736   1452   1822    -86       N  
ATOM    516  CD2 HIS A  70      65.394   2.568  47.025  1.00 95.80           C  
ANISOU  516  CD2 HIS A  70    10597  14561  11240   1578   1644   -161       C  
ATOM    517  CE1 HIS A  70      66.707   3.844  45.815  1.00105.10           C  
ANISOU  517  CE1 HIS A  70    11517  16131  12285   1445   1927   -140       C  
ATOM    518  NE2 HIS A  70      65.625   3.096  45.775  1.00101.85           N  
ANISOU  518  NE2 HIS A  70    11360  15471  11866   1524   1816   -188       N  
ATOM    519  N   GLU A  71      68.524   2.671  51.691  1.00 95.88           N  
ANISOU  519  N   GLU A  71     9803  14876  11752   1619   1293     65       N  
ATOM    520  CA  GLU A  71      68.570   2.780  53.134  1.00105.69           C  
ANISOU  520  CA  GLU A  71    11011  16055  13091   1542   1116    153       C  
ATOM    521  C   GLU A  71      67.998   4.128  53.532  1.00103.87           C  
ANISOU  521  C   GLU A  71    10837  15808  12820   1238   1105    253       C  
ATOM    522  O   GLU A  71      67.764   4.998  52.681  1.00 97.38           O  
ANISOU  522  O   GLU A  71    10041  15048  11910   1097   1232    262       O  
ATOM    523  CB  GLU A  71      70.000   2.609  53.661  1.00118.88           C  
ANISOU  523  CB  GLU A  71    12373  17931  14865   1646   1087    167       C  
ATOM    524  CG  GLU A  71      70.429   1.150  53.861  1.00129.25           C  
ANISOU  524  CG  GLU A  71    13670  19177  16263   1965    995     88       C  
ATOM    525  CD  GLU A  71      70.549   0.381  52.552  1.00137.74           C  
ANISOU  525  CD  GLU A  71    14773  20277  17283   2200   1141    -51       C  
ATOM    526  OE1 GLU A  71      70.984   0.982  51.544  1.00141.09           O  
ANISOU  526  OE1 GLU A  71    15066  20909  17633   2154   1341    -82       O  
ATOM    527  OE2 GLU A  71      70.213  -0.826  52.529  1.00138.59           O  
ANISOU  527  OE2 GLU A  71    15051  20194  17412   2422   1054   -128       O  
ATOM    528  N   ILE A  72      67.771   4.297  54.829  1.00104.06           N  
ANISOU  528  N   ILE A  72    10895  15741  12901   1140    949    325       N  
ATOM    529  CA  ILE A  72      67.128   5.502  55.327  1.00104.57           C  
ANISOU  529  CA  ILE A  72    11048  15756  12929    877    922    403       C  
ATOM    530  C   ILE A  72      68.167   6.516  55.766  1.00104.24           C  
ANISOU  530  C   ILE A  72    10783  15909  12914    719    925    477       C  
ATOM    531  O   ILE A  72      68.216   7.629  55.237  1.00100.75           O  
ANISOU  531  O   ILE A  72    10317  15551  12414    539   1018    512       O  
ATOM    532  CB  ILE A  72      66.165   5.187  56.508  1.00 92.97           C  
ANISOU  532  CB  ILE A  72     9771  14074  11480    836    762    433       C  
ATOM    533  CG1 ILE A  72      65.082   4.191  56.070  1.00 99.44           C  
ANISOU  533  CG1 ILE A  72    10812  14700  12271    960    750    370       C  
ATOM    534  CG2 ILE A  72      65.527   6.445  57.038  1.00 85.64           C  
ANISOU  534  CG2 ILE A  72     8926  13101  10512    590    744    494       C  
ATOM    535  CD1 ILE A  72      63.870   4.143  56.995  1.00 99.09           C  
ANISOU  535  CD1 ILE A  72    10970  14464  12215    857    640    404       C  
ATOM    536  N   GLU A  73      69.018   6.084  56.698  1.00107.17           N  
ANISOU  536  N   GLU A  73    10999  16348  13374    787    811    505       N  
ATOM    537  CA  GLU A  73      69.894   6.955  57.494  1.00103.39           C  
ANISOU  537  CA  GLU A  73    10336  16014  12934    617    746    590       C  
ATOM    538  C   GLU A  73      70.449   8.206  56.818  1.00 90.74           C  
ANISOU  538  C   GLU A  73     8596  14597  11285    415    872    631       C  
ATOM    539  O   GLU A  73      70.510   9.277  57.440  1.00 84.41           O  
ANISOU  539  O   GLU A  73     7799  13804  10469    182    812    706       O  
ATOM    540  CB  GLU A  73      71.033   6.142  58.093  1.00114.38           C  
ANISOU  540  CB  GLU A  73    11504  17524  14432    783    645    594       C  
ATOM    541  CG  GLU A  73      70.560   5.075  59.049  1.00125.65           C  
ANISOU  541  CG  GLU A  73    13086  18754  15901    923    471    588       C  
ATOM    542  CD  GLU A  73      71.538   4.855  60.181  1.00138.93           C  
ANISOU  542  CD  GLU A  73    14595  20519  17674    946    297    649       C  
ATOM    543  OE1 GLU A  73      72.749   4.689  59.902  1.00142.92           O  
ANISOU  543  OE1 GLU A  73    14811  21237  18255   1053    319    642       O  
ATOM    544  OE2 GLU A  73      71.094   4.857  61.351  1.00141.05           O  
ANISOU  544  OE2 GLU A  73    15012  20647  17932    854    136    704       O  
ATOM    545  N   PRO A  74      70.859   8.072  55.550  1.00 89.42           N  
ANISOU  545  N   PRO A  74     8320  14573  11082    497   1045    583       N  
ATOM    546  CA  PRO A  74      71.390   9.185  54.758  1.00 90.70           C  
ANISOU  546  CA  PRO A  74     8360  14921  11180    299   1183    627       C  
ATOM    547  C   PRO A  74      70.454  10.380  54.769  1.00 90.15           C  
ANISOU  547  C   PRO A  74     8522  14703  11029     48   1169    681       C  
ATOM    548  O   PRO A  74      70.808  11.465  55.225  1.00 98.90           O  
ANISOU  548  O   PRO A  74     9583  15864  12132   -187   1123    763       O  
ATOM    549  CB  PRO A  74      71.437   8.612  53.341  1.00 97.23           C  
ANISOU  549  CB  PRO A  74     9168  15831  11944    462   1370    541       C  
ATOM    550  CG  PRO A  74      71.539   7.135  53.521  1.00 99.33           C  
ANISOU  550  CG  PRO A  74     9412  16046  12285    778   1321    452       C  
ATOM    551  CD  PRO A  74      70.842   6.800  54.801  1.00 94.13           C  
ANISOU  551  CD  PRO A  74     8922  15158  11687    784   1115    479       C  
ATOM    552  N   VAL A  75      69.245  10.153  54.274  1.00 86.02           N  
ANISOU  552  N   VAL A  75     8253  13985  10445    106   1197    631       N  
ATOM    553  CA  VAL A  75      68.283  11.218  54.010  1.00 83.53           C  
ANISOU  553  CA  VAL A  75     8158  13529  10050    -86   1203    664       C  
ATOM    554  C   VAL A  75      67.735  11.897  55.265  1.00 77.60           C  
ANISOU  554  C   VAL A  75     7532  12625   9326   -231   1050    711       C  
ATOM    555  O   VAL A  75      67.441  13.092  55.249  1.00 79.38           O  
ANISOU  555  O   VAL A  75     7858  12800   9504   -436   1039    760       O  
ATOM    556  CB  VAL A  75      67.105  10.679  53.175  1.00 85.99           C  
ANISOU  556  CB  VAL A  75     8692  13678  10302     37   1255    594       C  
ATOM    557  CG1 VAL A  75      66.440  11.808  52.412  1.00 81.50           C  
ANISOU  557  CG1 VAL A  75     8285  13043   9637   -143   1306    629       C  
ATOM    558  CG2 VAL A  75      67.588   9.585  52.226  1.00 89.37           C  
ANISOU  558  CG2 VAL A  75     9023  14218  10716    256   1371    516       C  
ATOM    559  N   ALA A  76      67.579  11.142  56.348  1.00 69.97           N  
ANISOU  559  N   ALA A  76     6581  11577   8427   -126    929    694       N  
ATOM    560  CA  ALA A  76      67.083  11.741  57.570  1.00 72.09           C  
ANISOU  560  CA  ALA A  76     6971  11716   8703   -258    796    728       C  
ATOM    561  C   ALA A  76      68.096  12.780  57.974  1.00 78.46           C  
ANISOU  561  C   ALA A  76     7636  12660   9517   -464    759    804       C  
ATOM    562  O   ALA A  76      67.754  13.939  58.225  1.00 76.88           O  
ANISOU  562  O   ALA A  76     7556  12382   9273   -660    724    838       O  
ATOM    563  CB  ALA A  76      66.898  10.708  58.662  1.00 70.75           C  
ANISOU  563  CB  ALA A  76     6830  11465   8589   -125    675    709       C  
ATOM    564  N   GLN A  77      69.355  12.361  58.004  1.00 82.70           N  
ANISOU  564  N   GLN A  77     7912  13400  10110   -417    761    827       N  
ATOM    565  CA  GLN A  77      70.436  13.271  58.324  1.00 86.30           C  
ANISOU  565  CA  GLN A  77     8191  14020  10579   -622    723    906       C  
ATOM    566  C   GLN A  77      70.414  14.460  57.386  1.00 82.58           C  
ANISOU  566  C   GLN A  77     7765  13584  10028   -828    827    946       C  
ATOM    567  O   GLN A  77      70.396  15.613  57.824  1.00 77.83           O  
ANISOU  567  O   GLN A  77     7249  12928   9394  -1061    756   1003       O  
ATOM    568  CB  GLN A  77      71.762  12.550  58.207  1.00 96.17           C  
ANISOU  568  CB  GLN A  77     9117  15517  11907   -507    743    915       C  
ATOM    569  CG  GLN A  77      71.880  11.400  59.161  1.00108.21           C  
ANISOU  569  CG  GLN A  77    10603  16998  13514   -307    611    888       C  
ATOM    570  CD  GLN A  77      73.308  10.975  59.352  1.00122.01           C  
ANISOU  570  CD  GLN A  77    12012  18992  15355   -238    575    916       C  
ATOM    571  OE1 GLN A  77      74.224  11.802  59.314  1.00127.57           O  
ANISOU  571  OE1 GLN A  77    12518  19885  16068   -427    582    983       O  
ATOM    572  NE2 GLN A  77      73.515   9.677  59.558  1.00127.10           N  
ANISOU  572  NE2 GLN A  77    12584  19634  16074     33    526    867       N  
ATOM    573  N   SER A  78      70.409  14.173  56.091  1.00 79.05           N  
ANISOU  573  N   SER A  78     7281  13216   9539   -744    989    916       N  
ATOM    574  CA  SER A  78      70.439  15.230  55.104  1.00 84.43           C  
ANISOU  574  CA  SER A  78     8008  13941  10130   -940   1091    964       C  
ATOM    575  C   SER A  78      69.237  16.149  55.302  1.00 85.29           C  
ANISOU  575  C   SER A  78     8431  13791  10183  -1066   1020    972       C  
ATOM    576  O   SER A  78      69.255  17.308  54.885  1.00 93.11           O  
ANISOU  576  O   SER A  78     9505  14765  11109  -1285   1032   1034       O  
ATOM    577  CB  SER A  78      70.465  14.654  53.689  1.00 95.76           C  
ANISOU  577  CB  SER A  78     9398  15480  11507   -807   1275    917       C  
ATOM    578  OG  SER A  78      69.159  14.349  53.222  1.00107.93           O  
ANISOU  578  OG  SER A  78    11201  16806  13000   -692   1292    854       O  
ATOM    579  N   LEU A  79      68.194  15.623  55.942  1.00 81.78           N  
ANISOU  579  N   LEU A  79     8160  13147   9766   -925    943    909       N  
ATOM    580  CA  LEU A  79      66.999  16.407  56.267  1.00 78.55           C  
ANISOU  580  CA  LEU A  79     8026  12500   9321  -1005    872    898       C  
ATOM    581  C   LEU A  79      67.106  17.049  57.640  1.00 75.47           C  
ANISOU  581  C   LEU A  79     7681  12038   8956  -1138    724    924       C  
ATOM    582  O   LEU A  79      66.516  18.100  57.895  1.00 74.67           O  
ANISOU  582  O   LEU A  79     7771  11785   8816  -1274    665    933       O  
ATOM    583  CB  LEU A  79      65.746  15.540  56.174  1.00 68.43           C  
ANISOU  583  CB  LEU A  79     6900  11057   8045   -799    882    816       C  
ATOM    584  CG  LEU A  79      65.195  15.465  54.751  1.00 72.99           C  
ANISOU  584  CG  LEU A  79     7562  11610   8560   -742    997    794       C  
ATOM    585  CD1 LEU A  79      64.369  14.201  54.528  1.00 67.12           C  
ANISOU  585  CD1 LEU A  79     6881  10786   7834   -512   1019    714       C  
ATOM    586  CD2 LEU A  79      64.404  16.732  54.443  1.00 74.97           C  
ANISOU  586  CD2 LEU A  79     8023  11708   8753   -893    968    820       C  
ATOM    587  N   GLY A  80      67.878  16.418  58.517  1.00 72.87           N  
ANISOU  587  N   GLY A  80     7185  11815   8688  -1093    655    933       N  
ATOM    588  CA  GLY A  80      68.139  16.973  59.826  1.00 79.86           C  
ANISOU  588  CA  GLY A  80     8100  12658   9584  -1230    507    962       C  
ATOM    589  C   GLY A  80      67.001  16.586  60.724  1.00 83.21           C  
ANISOU  589  C   GLY A  80     8723  12889  10004  -1123    439    896       C  
ATOM    590  O   GLY A  80      66.354  17.434  61.337  1.00 87.82           O  
ANISOU  590  O   GLY A  80     9499  13321  10546  -1229    374    880       O  
ATOM    591  N   ILE A  81      66.777  15.281  60.794  1.00 81.07           N  
ANISOU  591  N   ILE A  81     8404  12628   9772   -912    457    855       N  
ATOM    592  CA  ILE A  81      65.603  14.727  61.436  1.00 80.18           C  
ANISOU  592  CA  ILE A  81     8469  12347   9647   -802    422    796       C  
ATOM    593  C   ILE A  81      65.966  13.682  62.472  1.00 81.48           C  
ANISOU  593  C   ILE A  81     8566  12543   9850   -705    324    801       C  
ATOM    594  O   ILE A  81      65.155  13.351  63.323  1.00 81.35           O  
ANISOU  594  O   ILE A  81     8696  12404   9809   -672    269    771       O  
ATOM    595  CB  ILE A  81      64.667  14.113  60.387  1.00 85.40           C  
ANISOU  595  CB  ILE A  81     9206  12939  10303   -647    532    743       C  
ATOM    596  CG1 ILE A  81      63.685  15.174  59.898  1.00 79.46           C  
ANISOU  596  CG1 ILE A  81     8637  12055   9500   -734    572    723       C  
ATOM    597  CG2 ILE A  81      63.932  12.904  60.945  1.00 97.30           C  
ANISOU  597  CG2 ILE A  81    10783  14359  11827   -486    499    700       C  
ATOM    598  CD1 ILE A  81      62.750  14.656  58.859  1.00 84.11           C  
ANISOU  598  CD1 ILE A  81     9303  12576  10080   -602    660    677       C  
ATOM    599  N   ASP A  82      67.185  13.165  62.410  1.00 86.82           N  
ANISOU  599  N   ASP A  82     9017  13387  10583   -662    299    841       N  
ATOM    600  CA  ASP A  82      67.626  12.190  63.399  1.00 89.23           C  
ANISOU  600  CA  ASP A  82     9257  13716  10930   -567    178    857       C  
ATOM    601  C   ASP A  82      68.257  12.844  64.622  1.00 91.40           C  
ANISOU  601  C   ASP A  82     9515  14024  11191   -740     28    910       C  
ATOM    602  O   ASP A  82      68.679  12.161  65.561  1.00 83.67           O  
ANISOU  602  O   ASP A  82     8493  13062  10234   -691   -102    936       O  
ATOM    603  CB  ASP A  82      68.587  11.196  62.769  1.00 96.32           C  
ANISOU  603  CB  ASP A  82     9919  14769  11907   -392    208    863       C  
ATOM    604  CG  ASP A  82      67.878  10.197  61.903  1.00103.12           C  
ANISOU  604  CG  ASP A  82    10849  15557  12775   -185    307    798       C  
ATOM    605  OD1 ASP A  82      66.688   9.916  62.176  1.00100.93           O  
ANISOU  605  OD1 ASP A  82    10786  15104  12457   -156    299    764       O  
ATOM    606  OD2 ASP A  82      68.502   9.700  60.948  1.00110.00           O  
ANISOU  606  OD2 ASP A  82    11559  16551  13687    -56    395    779       O  
ATOM    607  N   SER A  83      68.304  14.172  64.609  1.00 97.39           N  
ANISOU  607  N   SER A  83    10326  14773  11904   -947     32    927       N  
ATOM    608  CA  SER A  83      68.901  14.931  65.696  1.00 98.73           C  
ANISOU  608  CA  SER A  83    10504  14963  12047  -1139   -114    973       C  
ATOM    609  C   SER A  83      67.963  15.046  66.893  1.00 98.45           C  
ANISOU  609  C   SER A  83    10722  14753  11931  -1175   -196    934       C  
ATOM    610  O   SER A  83      66.732  15.047  66.750  1.00 90.79           O  
ANISOU  610  O   SER A  83     9940  13639  10917  -1115   -115    869       O  
ATOM    611  CB  SER A  83      69.263  16.336  65.207  1.00100.42           C  
ANISOU  611  CB  SER A  83    10714  15209  12233  -1360    -87   1004       C  
ATOM    612  OG  SER A  83      68.148  16.955  64.577  1.00 99.71           O  
ANISOU  612  OG  SER A  83    10828  14966  12090  -1370     18    952       O  
ATOM    613  N   ASP A  84      68.562  15.135  68.075  1.00 97.55           N  
ANISOU  613  N   ASP A  84    10604  14666  11794  -1275   -357    972       N  
ATOM    614  CA  ASP A  84      67.860  15.579  69.267  1.00 92.29           C  
ANISOU  614  CA  ASP A  84    10185  13859  11024  -1371   -437    936       C  
ATOM    615  C   ASP A  84      67.642  17.081  69.101  1.00 86.48           C  
ANISOU  615  C   ASP A  84     9578  13049  10233  -1558   -414    911       C  
ATOM    616  O   ASP A  84      66.995  17.739  69.913  1.00 78.38           O  
ANISOU  616  O   ASP A  84     8776  11892   9112  -1646   -454    859       O  
ATOM    617  CB  ASP A  84      68.726  15.302  70.495  1.00 96.98           C  
ANISOU  617  CB  ASP A  84    10731  14516  11601  -1444   -632    994       C  
ATOM    618  CG  ASP A  84      68.042  15.670  71.791  1.00108.34           C  
ANISOU  618  CG  ASP A  84    12435  15822  12908  -1543   -714    954       C  
ATOM    619  OD1 ASP A  84      67.083  16.470  71.769  1.00118.61           O  
ANISOU  619  OD1 ASP A  84    13936  16996  14135  -1594   -629    879       O  
ATOM    620  OD2 ASP A  84      68.468  15.158  72.845  1.00106.08           O  
ANISOU  620  OD2 ASP A  84    12161  15560  12586  -1563   -866    995       O  
ATOM    621  N   LYS A  85      68.197  17.616  68.023  1.00 90.15           N  
ANISOU  621  N   LYS A  85     9906  13596  10751  -1616   -348    946       N  
ATOM    622  CA  LYS A  85      68.188  19.048  67.794  1.00 98.33           C  
ANISOU  622  CA  LYS A  85    11056  14564  11743  -1814   -352    945       C  
ATOM    623  C   LYS A  85      66.887  19.492  67.166  1.00 98.51           C  
ANISOU  623  C   LYS A  85    11279  14420  11730  -1747   -227    867       C  
ATOM    624  O   LYS A  85      66.512  18.979  66.113  1.00103.79           O  
ANISOU  624  O   LYS A  85    11880  15111  12444  -1608    -99    858       O  
ATOM    625  CB  LYS A  85      69.346  19.438  66.877  1.00108.67           C  
ANISOU  625  CB  LYS A  85    12134  16042  13112  -1929   -334   1030       C  
ATOM    626  CG  LYS A  85      70.618  19.815  67.616  1.00116.02           C  
ANISOU  626  CG  LYS A  85    12932  17098  14052  -2125   -499   1108       C  
ATOM    627  CD  LYS A  85      71.542  20.641  66.731  1.00122.88           C  
ANISOU  627  CD  LYS A  85    13642  18098  14951  -2317   -473   1188       C  
ATOM    628  CE  LYS A  85      72.614  21.366  67.547  1.00130.60           C  
ANISOU  628  CE  LYS A  85    14556  19151  15916  -2578   -659   1261       C  
ATOM    629  NZ  LYS A  85      72.047  22.441  68.415  1.00132.07           N  
ANISOU  629  NZ  LYS A  85    15071  19115  15996  -2744   -774   1216       N  
ATOM    630  N   PRO A  86      66.199  20.453  67.808  1.00 91.13           N  
ANISOU  630  N   PRO A  86    10592  13318  10714  -1839   -272    806       N  
ATOM    631  CA  PRO A  86      64.979  21.034  67.242  1.00 85.22           C  
ANISOU  631  CA  PRO A  86    10033  12406   9942  -1777   -174    729       C  
ATOM    632  C   PRO A  86      65.138  21.230  65.738  1.00 84.41           C  
ANISOU  632  C   PRO A  86     9832  12348   9893  -1770    -75    774       C  
ATOM    633  O   PRO A  86      66.125  21.828  65.294  1.00 87.28           O  
ANISOU  633  O   PRO A  86    10101  12794  10269  -1934   -109    853       O  
ATOM    634  CB  PRO A  86      64.868  22.370  67.967  1.00 81.55           C  
ANISOU  634  CB  PRO A  86     9792  11797   9397  -1947   -273    689       C  
ATOM    635  CG  PRO A  86      65.430  22.074  69.311  1.00 84.68           C  
ANISOU  635  CG  PRO A  86    10186  12243   9744  -2018   -400    697       C  
ATOM    636  CD  PRO A  86      66.541  21.063  69.103  1.00 87.04           C  
ANISOU  636  CD  PRO A  86    10198  12753  10121  -1998   -424    798       C  
ATOM    637  N   VAL A  87      64.182  20.706  64.970  1.00 73.31           N  
ANISOU  637  N   VAL A  87     8448  10896   8511  -1594     45    730       N  
ATOM    638  CA  VAL A  87      64.309  20.652  63.528  1.00 73.28           C  
ANISOU  638  CA  VAL A  87     8349  10950   8546  -1562    146    771       C  
ATOM    639  C   VAL A  87      63.924  21.989  62.904  1.00 78.76           C  
ANISOU  639  C   VAL A  87     9215  11505   9204  -1676    143    770       C  
ATOM    640  O   VAL A  87      63.112  22.742  63.456  1.00 73.35           O  
ANISOU  640  O   VAL A  87     8745  10645   8481  -1688     95    702       O  
ATOM    641  CB  VAL A  87      63.488  19.483  62.928  1.00 73.49           C  
ANISOU  641  CB  VAL A  87     8335  10982   8606  -1335    255    729       C  
ATOM    642  CG1 VAL A  87      63.815  18.181  63.661  1.00 63.99           C  
ANISOU  642  CG1 VAL A  87     7005   9877   7431  -1225    231    731       C  
ATOM    643  CG2 VAL A  87      61.993  19.781  62.998  1.00 79.31           C  
ANISOU  643  CG2 VAL A  87     9278  11537   9318  -1246    284    641       C  
ATOM    644  N   ASP A  88      64.545  22.284  61.764  1.00 81.21           N  
ANISOU  644  N   ASP A  88     9436  11898   9522  -1761    192    846       N  
ATOM    645  CA  ASP A  88      64.278  23.500  61.005  1.00 89.33           C  
ANISOU  645  CA  ASP A  88    10628  12799  10513  -1883    183    869       C  
ATOM    646  C   ASP A  88      62.934  23.388  60.263  1.00 90.58           C  
ANISOU  646  C   ASP A  88    10921  12821  10673  -1707    255    805       C  
ATOM    647  O   ASP A  88      62.867  22.856  59.152  1.00 82.32           O  
ANISOU  647  O   ASP A  88     9791  11849   9637  -1629    353    831       O  
ATOM    648  CB  ASP A  88      65.426  23.730  60.013  1.00 93.10           C  
ANISOU  648  CB  ASP A  88    10948  13442  10983  -2044    225    984       C  
ATOM    649  CG  ASP A  88      65.419  25.126  59.393  1.00 89.39           C  
ANISOU  649  CG  ASP A  88    10662  12844  10459  -2244    177   1039       C  
ATOM    650  OD1 ASP A  88      66.523  25.639  59.115  1.00 90.76           O  
ANISOU  650  OD1 ASP A  88    10739  13135  10610  -2470    156   1140       O  
ATOM    651  OD2 ASP A  88      64.332  25.702  59.168  1.00 89.46           O  
ANISOU  651  OD2 ASP A  88    10904  12638  10447  -2181    156    986       O  
ATOM    652  N   LYS A  89      61.872  23.888  60.890  1.00103.82           N  
ANISOU  652  N   LYS A  89    12801  14307  12339  -1643    204    717       N  
ATOM    653  CA  LYS A  89      60.524  23.846  60.319  1.00112.80           C  
ANISOU  653  CA  LYS A  89    14056  15313  13490  -1474    252    649       C  
ATOM    654  C   LYS A  89      60.516  24.067  58.806  1.00110.32           C  
ANISOU  654  C   LYS A  89    13748  15000  13167  -1493    302    715       C  
ATOM    655  O   LYS A  89      60.136  23.186  58.029  1.00105.00           O  
ANISOU  655  O   LYS A  89    12991  14393  12513  -1358    391    710       O  
ATOM    656  CB  LYS A  89      59.638  24.916  60.978  1.00123.84           C  
ANISOU  656  CB  LYS A  89    15694  16491  14869  -1468    170    564       C  
ATOM    657  CG  LYS A  89      60.094  26.354  60.700  1.00131.17           C  
ANISOU  657  CG  LYS A  89    16789  17292  15759  -1663     70    615       C  
ATOM    658  CD  LYS A  89      59.163  27.399  61.300  1.00131.61           C  
ANISOU  658  CD  LYS A  89    17100  17107  15800  -1619    -16    512       C  
ATOM    659  CE  LYS A  89      59.899  28.718  61.525  1.00132.08           C  
ANISOU  659  CE  LYS A  89    17330  17045  15810  -1850   -149    557       C  
ATOM    660  NZ  LYS A  89      60.637  29.175  60.313  1.00133.51           N  
ANISOU  660  NZ  LYS A  89    17500  17254  15975  -2025   -162    695       N  
ATOM    661  N   THR A  90      60.953  25.254  58.401  1.00107.70           N  
ANISOU  661  N   THR A  90    13534  14590  12796  -1677    237    779       N  
ATOM    662  CA  THR A  90      60.729  25.739  57.050  1.00 99.86           C  
ANISOU  662  CA  THR A  90    12629  13541  11774  -1712    256    837       C  
ATOM    663  C   THR A  90      61.753  25.210  56.031  1.00 81.98           C  
ANISOU  663  C   THR A  90    10176  11493   9479  -1799    356    939       C  
ATOM    664  O   THR A  90      61.435  25.062  54.846  1.00 68.88           O  
ANISOU  664  O   THR A  90     8540   9840   7790  -1756    417    968       O  
ATOM    665  CB  THR A  90      60.614  27.282  57.044  1.00100.40           C  
ANISOU  665  CB  THR A  90    12948  13394  11804  -1866    128    861       C  
ATOM    666  OG1 THR A  90      60.572  27.764  55.697  1.00106.32           O  
ANISOU  666  OG1 THR A  90    13787  14101  12510  -1938    134    945       O  
ATOM    667  CG2 THR A  90      61.773  27.907  57.790  1.00 91.00           C  
ANISOU  667  CG2 THR A  90    11745  12245  10586  -2103     50    917       C  
ATOM    668  N   ALA A  91      62.963  24.900  56.493  1.00 70.22           N  
ANISOU  668  N   ALA A  91     8496  10190   7994  -1912    372    987       N  
ATOM    669  CA  ALA A  91      63.941  24.228  55.634  1.00 67.62           C  
ANISOU  669  CA  ALA A  91     7943  10103   7646  -1952    489   1061       C  
ATOM    670  C   ALA A  91      63.417  22.871  55.231  1.00 69.26           C  
ANISOU  670  C   ALA A  91     8045  10387   7886  -1702    597    996       C  
ATOM    671  O   ALA A  91      63.588  22.450  54.086  1.00 75.38           O  
ANISOU  671  O   ALA A  91     8753  11266   8623  -1672    701   1026       O  
ATOM    672  CB  ALA A  91      65.285  24.066  56.333  1.00 61.55           C  
ANISOU  672  CB  ALA A  91     6958   9529   6898  -2085    475   1111       C  
ATOM    673  N   LEU A  92      62.790  22.188  56.187  1.00 63.57           N  
ANISOU  673  N   LEU A  92     7319   9612   7223  -1536    569    908       N  
ATOM    674  CA  LEU A  92      62.223  20.858  55.965  1.00 65.09           C  
ANISOU  674  CA  LEU A  92     7434   9849   7449  -1308    646    844       C  
ATOM    675  C   LEU A  92      61.012  20.877  55.021  1.00 68.60           C  
ANISOU  675  C   LEU A  92     8030  10161   7874  -1199    672    810       C  
ATOM    676  O   LEU A  92      60.816  19.949  54.237  1.00 71.47           O  
ANISOU  676  O   LEU A  92     8333  10591   8233  -1073    754    793       O  
ATOM    677  CB  LEU A  92      61.850  20.212  57.296  1.00 57.03           C  
ANISOU  677  CB  LEU A  92     6391   8795   6481  -1197    596    774       C  
ATOM    678  CG  LEU A  92      61.265  18.802  57.227  1.00 63.41           C  
ANISOU  678  CG  LEU A  92     7135   9633   7325   -983    655    715       C  
ATOM    679  CD1 LEU A  92      62.221  17.834  56.528  1.00 67.78           C  
ANISOU  679  CD1 LEU A  92     7493  10378   7884   -928    741    747       C  
ATOM    680  CD2 LEU A  92      60.916  18.306  58.623  1.00 62.87           C  
ANISOU  680  CD2 LEU A  92     7072   9526   7289   -919    595    663       C  
ATOM    681  N   GLU A  93      60.206  21.928  55.083  1.00 60.15           N  
ANISOU  681  N   GLU A  93     7162   8899   6794  -1241    592    797       N  
ATOM    682  CA  GLU A  93      59.110  22.040  54.138  1.00 64.48           C  
ANISOU  682  CA  GLU A  93     7846   9325   7327  -1148    595    776       C  
ATOM    683  C   GLU A  93      59.711  22.069  52.734  1.00 67.51           C  
ANISOU  683  C   GLU A  93     8208   9808   7636  -1230    666    858       C  
ATOM    684  O   GLU A  93      59.389  21.233  51.885  1.00 66.20           O  
ANISOU  684  O   GLU A  93     8007   9694   7452  -1114    738    841       O  
ATOM    685  CB  GLU A  93      58.279  23.291  54.409  1.00 72.51           C  
ANISOU  685  CB  GLU A  93     9081  10120   8349  -1180    482    753       C  
ATOM    686  CG  GLU A  93      56.867  23.231  53.843  1.00 79.17           C  
ANISOU  686  CG  GLU A  93    10040  10827   9215  -1021    459    699       C  
ATOM    687  CD  GLU A  93      55.992  24.404  54.291  1.00 89.23           C  
ANISOU  687  CD  GLU A  93    11509  11880  10515  -1006    343    652       C  
ATOM    688  OE1 GLU A  93      55.103  24.824  53.514  1.00 91.98           O  
ANISOU  688  OE1 GLU A  93    11984  12099  10866   -939    291    649       O  
ATOM    689  OE2 GLU A  93      56.192  24.908  55.420  1.00 92.12           O  
ANISOU  689  OE2 GLU A  93    11906  12198  10896  -1053    296    614       O  
ATOM    690  N   ILE A  94      60.609  23.027  52.514  1.00 67.00           N  
ANISOU  690  N   ILE A  94     8167   9773   7518  -1444    646    947       N  
ATOM    691  CA  ILE A  94      61.362  23.142  51.267  1.00 70.38           C  
ANISOU  691  CA  ILE A  94     8559  10329   7855  -1568    729   1038       C  
ATOM    692  C   ILE A  94      61.829  21.800  50.682  1.00 66.40           C  
ANISOU  692  C   ILE A  94     7855  10038   7337  -1447    875   1016       C  
ATOM    693  O   ILE A  94      61.515  21.452  49.534  1.00 55.05           O  
ANISOU  693  O   ILE A  94     6463   8620   5833  -1391    941   1020       O  
ATOM    694  CB  ILE A  94      62.617  24.018  51.457  1.00 78.48           C  
ANISOU  694  CB  ILE A  94     9533  11446   8841  -1832    713   1137       C  
ATOM    695  CG1 ILE A  94      62.242  25.424  51.944  1.00 74.78           C  
ANISOU  695  CG1 ILE A  94     9298  10745   8370  -1971    557   1162       C  
ATOM    696  CG2 ILE A  94      63.428  24.051  50.173  1.00 74.39           C  
ANISOU  696  CG2 ILE A  94     8948  11100   8216  -1967    827   1231       C  
ATOM    697  CD1 ILE A  94      60.832  25.811  51.634  1.00 77.06           C  
ANISOU  697  CD1 ILE A  94     9822  10788   8668  -1840    476   1111       C  
ATOM    698  N   PHE A  95      62.603  21.054  51.455  1.00 66.29           N  
ANISOU  698  N   PHE A  95     7631  10179   7380  -1404    915    992       N  
ATOM    699  CA  PHE A  95      63.106  19.801  50.937  1.00 66.82           C  
ANISOU  699  CA  PHE A  95     7514  10436   7440  -1273   1043    963       C  
ATOM    700  C   PHE A  95      61.983  18.844  50.668  1.00 64.03           C  
ANISOU  700  C   PHE A  95     7236   9985   7108  -1048   1051    876       C  
ATOM    701  O   PHE A  95      61.969  18.190  49.623  1.00 63.79           O  
ANISOU  701  O   PHE A  95     7192  10026   7018   -966   1144    860       O  
ATOM    702  CB  PHE A  95      64.104  19.178  51.883  1.00 74.88           C  
ANISOU  702  CB  PHE A  95     8300  11618   8531  -1249   1055    953       C  
ATOM    703  CG  PHE A  95      65.259  20.062  52.172  1.00 88.38           C  
ANISOU  703  CG  PHE A  95     9909  13446  10226  -1483   1038   1042       C  
ATOM    704  CD1 PHE A  95      65.670  20.991  51.228  1.00 95.59           C  
ANISOU  704  CD1 PHE A  95    10874  14402  11043  -1688   1079   1132       C  
ATOM    705  CD2 PHE A  95      65.945  19.970  53.373  1.00 93.69           C  
ANISOU  705  CD2 PHE A  95    10440  14186  10973  -1518    970   1046       C  
ATOM    706  CE1 PHE A  95      66.739  21.827  51.476  1.00100.56           C  
ANISOU  706  CE1 PHE A  95    11410  15143  11655  -1936   1057   1225       C  
ATOM    707  CE2 PHE A  95      67.021  20.796  53.627  1.00102.16           C  
ANISOU  707  CE2 PHE A  95    11413  15372  12032  -1754    940   1134       C  
ATOM    708  CZ  PHE A  95      67.419  21.730  52.677  1.00101.34           C  
ANISOU  708  CZ  PHE A  95    11355  15314  11838  -1969    985   1225       C  
ATOM    709  N   TYR A  96      61.043  18.760  51.611  1.00 65.42           N  
ANISOU  709  N   TYR A  96     7493  10004   7359   -957    956    817       N  
ATOM    710  CA  TYR A  96      59.858  17.923  51.427  1.00 64.51           C  
ANISOU  710  CA  TYR A  96     7454   9788   7270   -770    947    742       C  
ATOM    711  C   TYR A  96      59.190  18.292  50.118  1.00 64.15           C  
ANISOU  711  C   TYR A  96     7562   9665   7149   -779    956    760       C  
ATOM    712  O   TYR A  96      58.892  17.425  49.294  1.00 61.48           O  
ANISOU  712  O   TYR A  96     7227   9355   6775   -666   1011    727       O  
ATOM    713  CB  TYR A  96      58.840  18.063  52.584  1.00 60.90           C  
ANISOU  713  CB  TYR A  96     7077   9174   6889   -711    847    687       C  
ATOM    714  CG  TYR A  96      57.792  16.974  52.546  1.00 54.02           C  
ANISOU  714  CG  TYR A  96     6226   8246   6054   -532    848    615       C  
ATOM    715  CD1 TYR A  96      58.171  15.641  52.574  1.00 62.19           C  
ANISOU  715  CD1 TYR A  96     7144   9382   7105   -419    903    586       C  
ATOM    716  CD2 TYR A  96      56.446  17.268  52.447  1.00 54.04           C  
ANISOU  716  CD2 TYR A  96     6361   8095   6075   -478    788    579       C  
ATOM    717  CE1 TYR A  96      57.249  14.628  52.513  1.00 59.63           C  
ANISOU  717  CE1 TYR A  96     6853   8998   6806   -280    893    529       C  
ATOM    718  CE2 TYR A  96      55.491  16.247  52.404  1.00 52.23           C  
ANISOU  718  CE2 TYR A  96     6137   7828   5879   -339    784    521       C  
ATOM    719  CZ  TYR A  96      55.911  14.932  52.431  1.00 55.59           C  
ANISOU  719  CZ  TYR A  96     6463   8347   6310   -253    835    501       C  
ATOM    720  OH  TYR A  96      55.020  13.889  52.372  1.00 54.60           O  
ANISOU  720  OH  TYR A  96     6357   8176   6210   -139    821    452       O  
ATOM    721  N   LEU A  97      58.955  19.587  49.936  1.00 53.80           N  
ANISOU  721  N   LEU A  97     6394   8240   5806   -914    886    813       N  
ATOM    722  CA  LEU A  97      58.309  20.064  48.726  1.00 54.13           C  
ANISOU  722  CA  LEU A  97     6606   8189   5772   -936    864    845       C  
ATOM    723  C   LEU A  97      59.087  19.696  47.451  1.00 60.61           C  
ANISOU  723  C   LEU A  97     7385   9170   6474   -986    985    890       C  
ATOM    724  O   LEU A  97      58.486  19.316  46.437  1.00 64.00           O  
ANISOU  724  O   LEU A  97     7909   9567   6840   -915   1000    876       O  
ATOM    725  CB  LEU A  97      58.024  21.560  48.826  1.00 53.67           C  
ANISOU  725  CB  LEU A  97     6723   7967   5704  -1076    750    900       C  
ATOM    726  CG  LEU A  97      56.770  21.792  49.667  1.00 58.36           C  
ANISOU  726  CG  LEU A  97     7405   8372   6396   -955    637    825       C  
ATOM    727  CD1 LEU A  97      56.325  23.237  49.634  1.00 57.59           C  
ANISOU  727  CD1 LEU A  97     7510   8079   6292  -1046    509    862       C  
ATOM    728  CD2 LEU A  97      55.638  20.873  49.182  1.00 49.88           C  
ANISOU  728  CD2 LEU A  97     6346   7259   5346   -769    637    760       C  
ATOM    729  N   GLU A  98      60.414  19.783  47.517  1.00 52.99           N  
ANISOU  729  N   GLU A  98     6271   8389   5476  -1106   1074    940       N  
ATOM    730  CA  GLU A  98      61.250  19.412  46.391  1.00 60.37           C  
ANISOU  730  CA  GLU A  98     7131   9514   6293  -1150   1216    972       C  
ATOM    731  C   GLU A  98      61.169  17.906  46.120  1.00 65.39           C  
ANISOU  731  C   GLU A  98     7667  10240   6940   -930   1306    876       C  
ATOM    732  O   GLU A  98      61.214  17.466  44.968  1.00 72.88           O  
ANISOU  732  O   GLU A  98     8654  11259   7779   -895   1396    865       O  
ATOM    733  CB  GLU A  98      62.709  19.812  46.648  1.00 74.29           C  
ANISOU  733  CB  GLU A  98     8712  11479   8037  -1324   1293   1041       C  
ATOM    734  CG  GLU A  98      63.003  21.313  46.541  1.00 88.13           C  
ANISOU  734  CG  GLU A  98    10582  13171   9731  -1594   1226   1158       C  
ATOM    735  CD  GLU A  98      64.481  21.656  46.798  1.00 95.73           C  
ANISOU  735  CD  GLU A  98    11339  14358  10678  -1789   1299   1234       C  
ATOM    736  OE1 GLU A  98      65.324  20.733  46.915  1.00 98.93           O  
ANISOU  736  OE1 GLU A  98    11493  14988  11109  -1703   1418   1195       O  
ATOM    737  OE2 GLU A  98      64.798  22.860  46.886  1.00 97.14           O  
ANISOU  737  OE2 GLU A  98    11606  14483  10820  -2029   1228   1332       O  
ATOM    738  N   ILE A  99      61.078  17.113  47.182  1.00 57.47           N  
ANISOU  738  N   ILE A  99     6551   9229   6057   -789   1276    806       N  
ATOM    739  CA  ILE A  99      60.976  15.666  47.028  1.00 60.73           C  
ANISOU  739  CA  ILE A  99     6893   9693   6488   -580   1334    716       C  
ATOM    740  C   ILE A  99      59.640  15.246  46.404  1.00 65.59           C  
ANISOU  740  C   ILE A  99     7695  10146   7081   -470   1279    667       C  
ATOM    741  O   ILE A  99      59.586  14.324  45.589  1.00 64.82           O  
ANISOU  741  O   ILE A  99     7615  10092   6923   -356   1345    613       O  
ATOM    742  CB  ILE A  99      61.118  14.949  48.367  1.00 56.81           C  
ANISOU  742  CB  ILE A  99     6265   9200   6122   -472   1289    668       C  
ATOM    743  CG1 ILE A  99      62.458  15.291  49.010  1.00 58.41           C  
ANISOU  743  CG1 ILE A  99     6268   9570   6354   -575   1324    717       C  
ATOM    744  CG2 ILE A  99      60.958  13.443  48.179  1.00 50.87           C  
ANISOU  744  CG2 ILE A  99     5476   8467   5388   -259   1327    579       C  
ATOM    745  CD1 ILE A  99      62.838  14.360  50.119  1.00 50.24           C  
ANISOU  745  CD1 ILE A  99     5083   8580   5426   -448   1294    672       C  
ATOM    746  N   LEU A 100      58.569  15.920  46.774  1.00 59.17           N  
ANISOU  746  N   LEU A 100     7017   9148   6317   -500   1152    679       N  
ATOM    747  CA  LEU A 100      57.265  15.654  46.220  1.00 54.69           C  
ANISOU  747  CA  LEU A 100     6606   8433   5741   -411   1080    642       C  
ATOM    748  C   LEU A 100      57.235  16.050  44.778  1.00 55.90           C  
ANISOU  748  C   LEU A 100     6900   8588   5750   -483   1107    685       C  
ATOM    749  O   LEU A 100      56.841  15.294  43.935  1.00 58.28           O  
ANISOU  749  O   LEU A 100     7277   8877   5989   -393   1121    643       O  
ATOM    750  CB  LEU A 100      56.219  16.447  46.969  1.00 20.00           C  
ATOM    751  CG  LEU A 100      55.923  16.010  48.385  1.00 20.00           C  
ATOM    752  CD1 LEU A 100      54.726  16.692  48.896  1.00 20.00           C  
ATOM    753  CD2 LEU A 100      55.712  14.558  48.431  1.00 20.00           C  
ATOM    754  N   ASN A 101      57.657  17.264  44.496  1.00 60.35           N  
ANISOU  754  N   ASN A 101     7516   9163   6251   -658   1105    774       N  
ATOM    755  CA  ASN A 101      57.813  17.709  43.115  1.00 58.78           C  
ANISOU  755  CA  ASN A 101     7450   8993   5890   -761   1145    835       C  
ATOM    756  C   ASN A 101      58.629  16.728  42.259  1.00 68.60           C  
ANISOU  756  C   ASN A 101     8612  10432   7020   -709   1312    797       C  
ATOM    757  O   ASN A 101      58.281  16.433  41.112  1.00 74.77           O  
ANISOU  757  O   ASN A 101     9527  11207   7676   -687   1334    786       O  
ATOM    758  CB  ASN A 101      58.438  19.087  43.116  1.00 66.53           C  
ANISOU  758  CB  ASN A 101     8473   9980   6825   -983   1129    946       C  
ATOM    759  CG  ASN A 101      57.438  20.148  43.470  1.00 79.58           C  
ANISOU  759  CG  ASN A 101    10296  11400   8541  -1022    950    981       C  
ATOM    760  OD1 ASN A 101      56.247  19.988  43.198  1.00 75.74           O  
ANISOU  760  OD1 ASN A 101     9931  10766   8082   -911    849    944       O  
ATOM    761  ND2 ASN A 101      57.900  21.237  44.080  1.00 87.67           N  
ANISOU  761  ND2 ASN A 101    11330  12386   9593  -1174    902   1046       N  
ATOM    762  N   GLY A 102      59.710  16.213  42.824  1.00 64.28           N  
ANISOU  762  N   GLY A 102     7850  10060   6514   -680   1424    770       N  
ATOM    763  CA  GLY A 102      60.445  15.151  42.171  1.00 65.90           C  
ANISOU  763  CA  GLY A 102     7954  10445   6638   -576   1580    704       C  
ATOM    764  C   GLY A 102      59.651  13.869  42.023  1.00 67.86           C  
ANISOU  764  C   GLY A 102     8263  10606   6914   -360   1549    594       C  
ATOM    765  O   GLY A 102      59.665  13.250  40.963  1.00 69.45           O  
ANISOU  765  O   GLY A 102     8540  10857   6990   -296   1626    546       O  
ATOM    766  N   LEU A 103      58.964  13.458  43.087  1.00 60.96           N  
ANISOU  766  N   LEU A 103     7365   9603   6193   -260   1436    554       N  
ATOM    767  CA  LEU A 103      58.161  12.236  43.051  1.00 59.73           C  
ANISOU  767  CA  LEU A 103     7271   9349   6072    -81   1387    461       C  
ATOM    768  C   LEU A 103      57.051  12.316  42.006  1.00 59.21           C  
ANISOU  768  C   LEU A 103     7428   9152   5915    -90   1312    459       C  
ATOM    769  O   LEU A 103      56.656  11.306  41.409  1.00 54.53           O  
ANISOU  769  O   LEU A 103     6918   8528   5274     27   1311    385       O  
ATOM    770  CB  LEU A 103      57.544  11.944  44.432  1.00 50.03           C  
ANISOU  770  CB  LEU A 103     5988   8008   5015    -17   1274    440       C  
ATOM    771  CG  LEU A 103      56.536  10.780  44.496  1.00 54.66           C  
ANISOU  771  CG  LEU A 103     6654   8469   5646    127   1195    363       C  
ATOM    772  CD1 LEU A 103      57.117   9.441  44.023  1.00 54.03           C  
ANISOU  772  CD1 LEU A 103     6550   8462   5518    277   1278    278       C  
ATOM    773  CD2 LEU A 103      55.953  10.628  45.892  1.00 54.19           C  
ANISOU  773  CD2 LEU A 103     6536   8318   5735    151   1096    359       C  
ATOM    774  N   PHE A 104      56.547  13.523  41.790  1.00 59.71           N  
ANISOU  774  N   PHE A 104     7600   9131   5956   -227   1231    542       N  
ATOM    775  CA  PHE A 104      55.279  13.677  41.079  1.00 63.37           C  
ANISOU  775  CA  PHE A 104     8262   9436   6381   -225   1103    548       C  
ATOM    776  C   PHE A 104      55.370  14.237  39.648  1.00 62.47           C  
ANISOU  776  C   PHE A 104     8319   9344   6075   -332   1128    603       C  
ATOM    777  O   PHE A 104      54.347  14.632  39.069  1.00 65.66           O  
ANISOU  777  O   PHE A 104     8896   9607   6446   -358    995    633       O  
ATOM    778  CB  PHE A 104      54.235  14.428  41.945  1.00 50.72           C  
ANISOU  778  CB  PHE A 104     6683   7669   4920   -247    944    580       C  
ATOM    779  CG  PHE A 104      53.571  13.548  42.987  1.00 46.73           C  
ANISOU  779  CG  PHE A 104     6088   7103   4563   -120    887    508       C  
ATOM    780  CD1 PHE A 104      52.905  12.386  42.612  1.00 49.99           C  
ANISOU  780  CD1 PHE A 104     6552   7472   4969    -11    853    440       C  
ATOM    781  CD2 PHE A 104      53.629  13.872  44.336  1.00 40.52           C  
ANISOU  781  CD2 PHE A 104     5182   6305   3910   -125    867    511       C  
ATOM    782  CE1 PHE A 104      52.316  11.548  43.569  1.00 46.71           C  
ANISOU  782  CE1 PHE A 104     6063   7005   4679     79    801    386       C  
ATOM    783  CE2 PHE A 104      53.034  13.055  45.296  1.00 39.47           C  
ANISOU  783  CE2 PHE A 104     4977   6128   3894    -29    823    454       C  
ATOM    784  CZ  PHE A 104      52.375  11.892  44.915  1.00 46.45           C  
ANISOU  784  CZ  PHE A 104     5906   6971   4772     67    791    397       C  
ATOM    785  N   GLU A 105      56.578  14.218  39.072  1.00 66.96           N  
ANISOU  785  N   GLU A 105     8834  10095   6512   -390   1297    615       N  
ATOM    786  CA  GLU A 105      56.773  14.572  37.659  1.00 72.49           C  
ANISOU  786  CA  GLU A 105     9698  10850   6995   -493   1353    659       C  
ATOM    787  C   GLU A 105      55.728  13.889  36.776  1.00 74.20           C  
ANISOU  787  C   GLU A 105    10110  10949   7134   -404   1261    603       C  
ATOM    788  O   GLU A 105      55.330  14.417  35.751  1.00 78.48           O  
ANISOU  788  O   GLU A 105    10851  11438   7529   -500   1206    661       O  
ATOM    789  CB  GLU A 105      58.171  14.196  37.188  1.00 75.56           C  
ANISOU  789  CB  GLU A 105     9966  11488   7257   -509   1580    634       C  
ATOM    790  CG  GLU A 105      59.251  15.174  37.595  1.00 82.13           C  
ANISOU  790  CG  GLU A 105    10653  12460   8092   -681   1668    728       C  
ATOM    791  CD  GLU A 105      60.625  14.530  37.645  1.00 90.68           C  
ANISOU  791  CD  GLU A 105    11504  13806   9145   -631   1884    673       C  
ATOM    792  OE1 GLU A 105      60.702  13.286  37.723  1.00 96.27           O  
ANISOU  792  OE1 GLU A 105    12139  14551   9886   -424   1939    551       O  
ATOM    793  OE2 GLU A 105      61.633  15.266  37.621  1.00 95.45           O  
ANISOU  793  OE2 GLU A 105    11993  14577   9696   -798   1990    754       O  
ATOM    794  N   LYS A 106      55.292  12.707  37.181  1.00 74.98           N  
ANISOU  794  N   LYS A 106    10164  11001   7326   -232   1233    498       N  
ATOM    795  CA  LYS A 106      54.147  12.064  36.559  1.00 73.72           C  
ANISOU  795  CA  LYS A 106    10178  10701   7131   -158   1104    449       C  
ATOM    796  C   LYS A 106      53.184  11.648  37.673  1.00 67.90           C  
ANISOU  796  C   LYS A 106     9364   9826   6608    -65    963    416       C  
ATOM    797  O   LYS A 106      53.594  11.510  38.832  1.00 69.36           O  
ANISOU  797  O   LYS A 106     9369  10050   6936    -22   1004    401       O  
ATOM    798  CB  LYS A 106      54.565  10.836  35.731  1.00 75.94           C  
ANISOU  798  CB  LYS A 106    10520  11064   7269    -49   1217    340       C  
ATOM    799  CG  LYS A 106      53.399  10.248  34.904  1.00 90.05           C  
ANISOU  799  CG  LYS A 106    12528  12704   8983     -8   1070    298       C  
ATOM    800  CD  LYS A 106      53.412   8.716  34.831  1.00 93.84           C  
ANISOU  800  CD  LYS A 106    13027  13173   9455    159   1101    160       C  
ATOM    801  CE  LYS A 106      52.196   8.171  34.074  1.00 88.46           C  
ANISOU  801  CE  LYS A 106    12567  12332   8710    173    927    127       C  
ATOM    802  NZ  LYS A 106      51.953   6.724  34.358  1.00 79.71           N  
ANISOU  802  NZ  LYS A 106    11472  11155   7660    321    895      8       N  
ATOM    803  N   LEU A 107      51.915  11.441  37.322  1.00 58.44           N  
ANISOU  803  N   LEU A 107     8300   8480   5426    -42    796    407       N  
ATOM    804  CA  LEU A 107      50.921  11.006  38.286  1.00 56.32           C  
ANISOU  804  CA  LEU A 107     7956   8099   5344     31    668    377       C  
ATOM    805  C   LEU A 107      50.434   9.609  37.978  1.00 55.11           C  
ANISOU  805  C   LEU A 107     7870   7898   5172    131    628    285       C  
ATOM    806  O   LEU A 107      50.105   9.287  36.841  1.00 48.64           O  
ANISOU  806  O   LEU A 107     7227   7043   4210    125    583    265       O  
ATOM    807  CB  LEU A 107      49.706  11.935  38.276  1.00 54.39           C  
ANISOU  807  CB  LEU A 107     7776   7720   5169    -25    484    444       C  
ATOM    808  CG  LEU A 107      49.999  13.417  38.412  1.00 52.85           C  
ANISOU  808  CG  LEU A 107     7580   7522   4979   -130    478    538       C  
ATOM    809  CD1 LEU A 107      48.730  14.190  38.618  1.00 53.10           C  
ANISOU  809  CD1 LEU A 107     7649   7407   5121   -134    286    580       C  
ATOM    810  CD2 LEU A 107      50.957  13.618  39.542  1.00 48.82           C  
ANISOU  810  CD2 LEU A 107     6888   7103   4558   -136    603    537       C  
ATOM    811  N   ASN A 108      50.362   8.792  39.018  1.00 56.11           N  
ANISOU  811  N   ASN A 108     7873   8010   5437    212    628    234       N  
ATOM    812  CA  ASN A 108      49.605   7.543  38.994  1.00 53.16           C  
ANISOU  812  CA  ASN A 108     7562   7546   5091    284    536    165       C  
ATOM    813  C   ASN A 108      49.489   7.064  40.447  1.00 53.91           C  
ANISOU  813  C   ASN A 108     7493   7626   5366    328    527    151       C  
ATOM    814  O   ASN A 108      50.159   7.611  41.329  1.00 45.60           O  
ANISOU  814  O   ASN A 108     6293   6646   4387    319    609    181       O  
ATOM    815  CB  ASN A 108      50.297   6.493  38.116  1.00 47.29           C  
ANISOU  815  CB  ASN A 108     6936   6838   4194    364    625     76       C  
ATOM    816  CG  ASN A 108      51.762   6.290  38.493  1.00 63.39           C  
ANISOU  816  CG  ASN A 108     8847   9018   6219    436    816     41       C  
ATOM    817  OD1 ASN A 108      52.072   5.718  39.539  1.00 64.43           O  
ANISOU  817  OD1 ASN A 108     8850   9156   6476    507    837     15       O  
ATOM    818  ND2 ASN A 108      52.667   6.757  37.637  1.00 69.00           N  
ANISOU  818  ND2 ASN A 108     9591   9852   6774    411    952     45       N  
ATOM    819  N   TRP A 109      48.651   6.057  40.685  1.00 50.24           N  
ANISOU  819  N   TRP A 109     7063   7067   4959    359    421    111       N  
ATOM    820  CA  TRP A 109      48.473   5.495  42.020  1.00 55.16           C  
ANISOU  820  CA  TRP A 109     7558   7671   5730    383    405    104       C  
ATOM    821  C   TRP A 109      49.773   5.092  42.721  1.00 59.46           C  
ANISOU  821  C   TRP A 109     8003   8298   6293    459    539     77       C  
ATOM    822  O   TRP A 109      49.993   5.473  43.878  1.00 54.53           O  
ANISOU  822  O   TRP A 109     7231   7712   5774    442    567    111       O  
ATOM    823  CB  TRP A 109      47.490   4.324  41.994  1.00 50.89           C  
ANISOU  823  CB  TRP A 109     7102   7017   5216    386    275     68       C  
ATOM    824  CG  TRP A 109      46.089   4.785  41.805  1.00 50.35           C  
ANISOU  824  CG  TRP A 109     7044   6889   5199    301    127    111       C  
ATOM    825  CD1 TRP A 109      45.209   4.378  40.846  1.00 51.58           C  
ANISOU  825  CD1 TRP A 109     7341   6964   5293    268     -5     98       C  
ATOM    826  CD2 TRP A 109      45.405   5.769  42.583  1.00 47.49           C  
ANISOU  826  CD2 TRP A 109     6538   6548   4960    248     91    167       C  
ATOM    827  NE1 TRP A 109      44.008   5.035  40.991  1.00 55.81           N  
ANISOU  827  NE1 TRP A 109     7807   7478   5920    199   -128    149       N  
ATOM    828  CE2 TRP A 109      44.104   5.904  42.056  1.00 53.77           C  
ANISOU  828  CE2 TRP A 109     7372   7281   5776    196    -64    187       C  
ATOM    829  CE3 TRP A 109      45.763   6.549  43.681  1.00 44.52           C  
ANISOU  829  CE3 TRP A 109     6005   6234   4676    245    169    197       C  
ATOM    830  CZ2 TRP A 109      43.151   6.775  42.584  1.00 51.63           C  
ANISOU  830  CZ2 TRP A 109     6974   7017   5624    160   -134    229       C  
ATOM    831  CZ3 TRP A 109      44.817   7.427  44.210  1.00 55.18           C  
ANISOU  831  CZ3 TRP A 109     7255   7580   6132    205    104    233       C  
ATOM    832  CH2 TRP A 109      43.524   7.529  43.659  1.00 49.83           C  
ANISOU  832  CH2 TRP A 109     6604   6847   5481    173    -42    245       C  
ATOM    833  N   GLY A 110      50.631   4.338  42.033  1.00 58.18           N  
ANISOU  833  N   GLY A 110     7917   8165   6024    549    618     11       N  
ATOM    834  CA  GLY A 110      51.864   3.866  42.636  1.00 54.56           C  
ANISOU  834  CA  GLY A 110     7352   7787   5590    646    731    -23       C  
ATOM    835  C   GLY A 110      52.724   4.967  43.250  1.00 49.66           C  
ANISOU  835  C   GLY A 110     6557   7300   5012    601    834     37       C  
ATOM    836  O   GLY A 110      53.359   4.777  44.286  1.00 51.20           O  
ANISOU  836  O   GLY A 110     6618   7540   5294    638    868     42       O  
ATOM    837  N   ARG A 111      52.757   6.120  42.599  1.00 43.39           N  
ANISOU  837  N   ARG A 111     5779   6560   4148    510    869     86       N  
ATOM    838  CA  ARG A 111      53.534   7.246  43.080  1.00 50.82           C  
ANISOU  838  CA  ARG A 111     6581   7611   5116    439    951    150       C  
ATOM    839  C   ARG A 111      52.862   7.904  44.285  1.00 56.26           C  
ANISOU  839  C   ARG A 111     7187   8243   5945    368    866    205       C  
ATOM    840  O   ARG A 111      53.540   8.493  45.145  1.00 55.86           O  
ANISOU  840  O   ARG A 111     7005   8265   5954    332    914    241       O  
ATOM    841  CB  ARG A 111      53.719   8.285  41.961  1.00 51.59           C  
ANISOU  841  CB  ARG A 111     6757   7762   5082    344    999    195       C  
ATOM    842  CG  ARG A 111      54.829   7.951  40.979  1.00 56.66           C  
ANISOU  842  CG  ARG A 111     7418   8538   5574    390   1149    152       C  
ATOM    843  CD  ARG A 111      54.693   8.726  39.644  1.00 59.97           C  
ANISOU  843  CD  ARG A 111     7988   8976   5824    287   1168    192       C  
ATOM    844  NE  ARG A 111      55.645   8.202  38.674  1.00 61.26           N  
ANISOU  844  NE  ARG A 111     8180   9270   5824    346   1323    129       N  
ATOM    845  CZ  ARG A 111      56.734   8.838  38.259  1.00 62.60           C  
ANISOU  845  CZ  ARG A 111     8276   9616   5894    276   1477    163       C  
ATOM    846  NH1 ARG A 111      57.006  10.068  38.682  1.00 63.36           N  
ANISOU  846  NH1 ARG A 111     8286   9756   6030    127   1480    270       N  
ATOM    847  NH2 ARG A 111      57.550   8.232  37.405  1.00 56.54           N  
ANISOU  847  NH2 ARG A 111     7521   8981   4978    353   1631     87       N  
ATOM    848  N   ILE A 112      51.532   7.824  44.336  1.00 43.27           N  
ANISOU  848  N   ILE A 112     5615   6479   4347    346    740    208       N  
ATOM    849  CA  ILE A 112      50.805   8.383  45.468  1.00 45.09           C  
ANISOU  849  CA  ILE A 112     5762   6665   4703    295    672    243       C  
ATOM    850  C   ILE A 112      51.092   7.534  46.723  1.00 45.57           C  
ANISOU  850  C   ILE A 112     5724   6738   4853    342    683    221       C  
ATOM    851  O   ILE A 112      51.507   8.057  47.766  1.00 41.58           O  
ANISOU  851  O   ILE A 112     5108   6278   4411    311    713    248       O  
ATOM    852  CB  ILE A 112      49.299   8.559  45.131  1.00 46.72           C  
ANISOU  852  CB  ILE A 112     6046   6766   4939    263    540    251       C  
ATOM    853  CG1 ILE A 112      49.124   9.779  44.222  1.00 54.71           C  
ANISOU  853  CG1 ILE A 112     7135   7766   5888    204    514    296       C  
ATOM    854  CG2 ILE A 112      48.466   8.725  46.380  1.00 40.14           C  
ANISOU  854  CG2 ILE A 112     5113   5902   4238    241    483    260       C  
ATOM    855  CD1 ILE A 112      47.806   9.804  43.442  1.00 58.30           C  
ANISOU  855  CD1 ILE A 112     7693   8124   6335    192    375    300       C  
ATOM    856  N   VAL A 113      50.917   6.225  46.586  1.00 45.71           N  
ANISOU  856  N   VAL A 113     5800   6706   4861    411    651    175       N  
ATOM    857  CA  VAL A 113      51.358   5.255  47.582  1.00 50.83           C  
ANISOU  857  CA  VAL A 113     6392   7354   5568    467    654    157       C  
ATOM    858  C   VAL A 113      52.732   5.581  48.137  1.00 51.51           C  
ANISOU  858  C   VAL A 113     6354   7553   5665    495    751    170       C  
ATOM    859  O   VAL A 113      52.954   5.601  49.354  1.00 47.28           O  
ANISOU  859  O   VAL A 113     5725   7036   5204    477    741    195       O  
ATOM    860  CB  VAL A 113      51.438   3.849  46.980  1.00 45.91           C  
ANISOU  860  CB  VAL A 113     5883   6664   4895    563    626     95       C  
ATOM    861  CG1 VAL A 113      52.291   2.979  47.854  1.00 48.61           C  
ANISOU  861  CG1 VAL A 113     6169   7019   5283    647    643     79       C  
ATOM    862  CG2 VAL A 113      50.050   3.257  46.811  1.00 38.66           C  
ANISOU  862  CG2 VAL A 113     5072   5622   3993    516    501     90       C  
ATOM    863  N   ALA A 114      53.665   5.832  47.233  1.00 48.61           N  
ANISOU  863  N   ALA A 114     5981   7272   5214    530    844    155       N  
ATOM    864  CA  ALA A 114      55.017   6.163  47.640  1.00 50.66           C  
ANISOU  864  CA  ALA A 114     6100   7666   5483    546    938    170       C  
ATOM    865  C   ALA A 114      55.050   7.406  48.533  1.00 43.95           C  
ANISOU  865  C   ALA A 114     5156   6853   4692    426    933    238       C  
ATOM    866  O   ALA A 114      55.897   7.518  49.399  1.00 54.02           O  
ANISOU  866  O   ALA A 114     6308   8204   6014    422    958    258       O  
ATOM    867  CB  ALA A 114      55.905   6.341  46.409  1.00 55.56           C  
ANISOU  867  CB  ALA A 114     6725   8396   5989    578   1054    147       C  
ATOM    868  N   MET A 115      54.137   8.344  48.324  1.00 44.42           N  
ANISOU  868  N   MET A 115     5278   6852   4747    332    889    269       N  
ATOM    869  CA  MET A 115      54.058   9.537  49.182  1.00 46.26           C  
ANISOU  869  CA  MET A 115     5451   7091   5033    230    871    318       C  
ATOM    870  C   MET A 115      53.615   9.196  50.624  1.00 50.15           C  
ANISOU  870  C   MET A 115     5892   7543   5620    231    814    314       C  
ATOM    871  O   MET A 115      54.158   9.731  51.590  1.00 54.36           O  
ANISOU  871  O   MET A 115     6342   8122   6189    182    824    340       O  
ATOM    872  CB  MET A 115      53.108  10.567  48.565  1.00 41.76           C  
ANISOU  872  CB  MET A 115     4977   6447   4442    160    822    342       C  
ATOM    873  CG  MET A 115      52.843  11.787  49.422  1.00 38.53           C  
ANISOU  873  CG  MET A 115     4539   6009   4090     76    787    375       C  
ATOM    874  SD  MET A 115      51.567  12.895  48.776  1.00 48.39           S  
ANISOU  874  SD  MET A 115     5907   7141   5339     36    697    392       S  
ATOM    875  CE  MET A 115      50.232  11.756  48.473  1.00 50.98           C  
ANISOU  875  CE  MET A 115     6276   7397   5696    116    624    345       C  
ATOM    876  N   PHE A 116      52.638   8.302  50.768  1.00 43.18           N  
ANISOU  876  N   PHE A 116     5064   6577   4765    272    751    286       N  
ATOM    877  CA  PHE A 116      52.253   7.848  52.097  1.00 47.60           C  
ANISOU  877  CA  PHE A 116     5583   7111   5391    260    708    288       C  
ATOM    878  C   PHE A 116      53.335   7.014  52.771  1.00 49.97           C  
ANISOU  878  C   PHE A 116     5823   7460   5704    315    723    290       C  
ATOM    879  O   PHE A 116      53.545   7.138  53.981  1.00 49.24           O  
ANISOU  879  O   PHE A 116     5673   7389   5649    276    707    312       O  
ATOM    880  CB  PHE A 116      50.947   7.046  52.074  1.00 42.59           C  
ANISOU  880  CB  PHE A 116     5017   6386   4778    265    636    268       C  
ATOM    881  CG  PHE A 116      49.721   7.878  51.769  1.00 48.40           C  
ANISOU  881  CG  PHE A 116     5777   7081   5533    215    599    269       C  
ATOM    882  CD1 PHE A 116      48.972   8.446  52.800  1.00 61.44           C  
ANISOU  882  CD1 PHE A 116     7373   8731   7241    162    584    272       C  
ATOM    883  CD2 PHE A 116      49.311   8.091  50.453  1.00 45.59           C  
ANISOU  883  CD2 PHE A 116     5498   6689   5135    228    575    261       C  
ATOM    884  CE1 PHE A 116      47.819   9.223  52.530  1.00 60.16           C  
ANISOU  884  CE1 PHE A 116     7214   8536   7110    142    545    262       C  
ATOM    885  CE2 PHE A 116      48.169   8.863  50.170  1.00 54.78           C  
ANISOU  885  CE2 PHE A 116     6676   7811   6328    196    518    264       C  
ATOM    886  CZ  PHE A 116      47.414   9.431  51.217  1.00 49.08           C  
ANISOU  886  CZ  PHE A 116     5879   7090   5680    162    503    262       C  
ATOM    887  N   ALA A 117      54.007   6.148  52.015  1.00 49.60           N  
ANISOU  887  N   ALA A 117     5796   7429   5622    412    747    262       N  
ATOM    888  CA  ALA A 117      54.976   5.255  52.646  1.00 49.24           C  
ANISOU  888  CA  ALA A 117     5693   7416   5601    493    741    259       C  
ATOM    889  C   ALA A 117      56.165   6.067  53.157  1.00 52.97           C  
ANISOU  889  C   ALA A 117     6025   8013   6087    461    792    292       C  
ATOM    890  O   ALA A 117      56.709   5.808  54.254  1.00 47.19           O  
ANISOU  890  O   ALA A 117     5225   7307   5399    464    754    316       O  
ATOM    891  CB  ALA A 117      55.415   4.164  51.703  1.00 47.76           C  
ANISOU  891  CB  ALA A 117     5560   7211   5376    630    756    205       C  
ATOM    892  N   PHE A 118      56.524   7.084  52.376  1.00 48.03           N  
ANISOU  892  N   PHE A 118     5368   7461   5420    410    864    303       N  
ATOM    893  CA  PHE A 118      57.624   7.961  52.729  1.00 56.34           C  
ANISOU  893  CA  PHE A 118     6292   8637   6478    345    910    342       C  
ATOM    894  C   PHE A 118      57.294   8.893  53.876  1.00 51.57           C  
ANISOU  894  C   PHE A 118     5676   8008   5911    222    860    382       C  
ATOM    895  O   PHE A 118      58.107   9.079  54.783  1.00 54.21           O  
ANISOU  895  O   PHE A 118     5913   8409   6274    188    843    411       O  
ATOM    896  CB  PHE A 118      58.026   8.808  51.533  1.00 54.89           C  
ANISOU  896  CB  PHE A 118     6101   8529   6224    295    997    353       C  
ATOM    897  CG  PHE A 118      59.286   9.606  51.740  1.00 44.72           C  
ANISOU  897  CG  PHE A 118     4669   7389   4934    216   1051    399       C  
ATOM    898  CD1 PHE A 118      60.485   8.977  52.022  1.00 46.81           C  
ANISOU  898  CD1 PHE A 118     4782   7778   5227    295   1081    393       C  
ATOM    899  CD2 PHE A 118      59.280  10.976  51.586  1.00 49.78           C  
ANISOU  899  CD2 PHE A 118     5327   8042   5544     63   1063    450       C  
ATOM    900  CE1 PHE A 118      61.657   9.722  52.181  1.00 44.94           C  
ANISOU  900  CE1 PHE A 118     4388   7697   4992    205   1127    441       C  
ATOM    901  CE2 PHE A 118      60.450  11.724  51.727  1.00 53.47           C  
ANISOU  901  CE2 PHE A 118     5666   8646   6004    -40   1105    501       C  
ATOM    902  CZ  PHE A 118      61.631  11.095  52.032  1.00 46.95           C  
ANISOU  902  CZ  PHE A 118     4666   7964   5209     25   1140    498       C  
ATOM    903  N   LEU A 119      56.127   9.524  53.806  1.00 45.47           N  
ANISOU  903  N   LEU A 119     4999   7143   5133    160    834    379       N  
ATOM    904  CA  LEU A 119      55.642  10.378  54.903  1.00 49.84           C  
ANISOU  904  CA  LEU A 119     5562   7659   5716     66    791    394       C  
ATOM    905  C   LEU A 119      55.634   9.600  56.234  1.00 47.71           C  
ANISOU  905  C   LEU A 119     5267   7380   5481     82    741    394       C  
ATOM    906  O   LEU A 119      56.071  10.109  57.262  1.00 49.71           O  
ANISOU  906  O   LEU A 119     5479   7666   5743     14    719    415       O  
ATOM    907  CB  LEU A 119      54.252  10.915  54.573  1.00 45.93           C  
ANISOU  907  CB  LEU A 119     5165   7063   5221     43    768    373       C  
ATOM    908  CG  LEU A 119      53.452  11.681  55.627  1.00 47.73           C  
ANISOU  908  CG  LEU A 119     5417   7240   5480    -18    732    361       C  
ATOM    909  CD1 LEU A 119      54.013  13.098  55.909  1.00 35.37           C  
ANISOU  909  CD1 LEU A 119     3850   5687   3903   -110    734    382       C  
ATOM    910  CD2 LEU A 119      51.989  11.736  55.162  1.00 45.21           C  
ANISOU  910  CD2 LEU A 119     5163   6836   5176     10    706    330       C  
ATOM    911  N   ARG A 120      55.187   8.348  56.188  1.00 42.79           N  
ANISOU  911  N   ARG A 120     4683   6709   4868    162    714    375       N  
ATOM    912  CA  ARG A 120      55.242   7.450  57.349  1.00 44.65           C  
ANISOU  912  CA  ARG A 120     4916   6927   5123    175    655    388       C  
ATOM    913  C   ARG A 120      56.647   7.324  57.919  1.00 43.63           C  
ANISOU  913  C   ARG A 120     4687   6884   5006    194    639    418       C  
ATOM    914  O   ARG A 120      56.859   7.388  59.134  1.00 43.09           O  
ANISOU  914  O   ARG A 120     4603   6828   4943    139    589    445       O  
ATOM    915  CB  ARG A 120      54.768   6.055  56.957  1.00 39.28           C  
ANISOU  915  CB  ARG A 120     4307   6172   4445    262    619    369       C  
ATOM    916  CG  ARG A 120      54.544   5.162  58.127  1.00 39.83           C  
ANISOU  916  CG  ARG A 120     4414   6196   4525    248    546    393       C  
ATOM    917  CD  ARG A 120      54.087   3.769  57.702  1.00 40.61           C  
ANISOU  917  CD  ARG A 120     4609   6198   4623    320    493    381       C  
ATOM    918  NE  ARG A 120      55.279   2.955  57.549  1.00 60.01           N  
ANISOU  918  NE  ARG A 120     7041   8665   7094    446    465    378       N  
ATOM    919  CZ  ARG A 120      55.663   2.021  58.406  1.00 58.88           C  
ANISOU  919  CZ  ARG A 120     6928   8478   6964    480    377    409       C  
ATOM    920  NH1 ARG A 120      54.916   1.736  59.463  1.00 50.75           N  
ANISOU  920  NH1 ARG A 120     5969   7393   5920    376    316    451       N  
ATOM    921  NH2 ARG A 120      56.785   1.354  58.188  1.00 66.04           N  
ANISOU  921  NH2 ARG A 120     7797   9400   7896    622    349    397       N  
ATOM    922  N   ILE A 121      57.600   7.130  57.016  1.00 47.16           N  
ANISOU  922  N   ILE A 121     5064   7402   5454    273    682    411       N  
ATOM    923  CA  ILE A 121      58.983   6.874  57.370  1.00 48.79           C  
ANISOU  923  CA  ILE A 121     5143   7711   5686    319    669    434       C  
ATOM    924  C   ILE A 121      59.566   8.106  58.044  1.00 47.87           C  
ANISOU  924  C   ILE A 121     4946   7674   5569    185    667    475       C  
ATOM    925  O   ILE A 121      60.217   8.005  59.077  1.00 54.59           O  
ANISOU  925  O   ILE A 121     5736   8566   6441    162    600    508       O  
ATOM    926  CB  ILE A 121      59.781   6.446  56.109  1.00 57.30           C  
ANISOU  926  CB  ILE A 121     6150   8865   6755    441    743    402       C  
ATOM    927  CG1 ILE A 121      59.631   4.941  55.902  1.00 55.04           C  
ANISOU  927  CG1 ILE A 121     5931   8498   6483    602    700    361       C  
ATOM    928  CG2 ILE A 121      61.244   6.857  56.202  1.00 47.68           C  
ANISOU  928  CG2 ILE A 121     4746   7813   5559    436    773    430       C  
ATOM    929  CD1 ILE A 121      59.778   4.503  54.458  1.00 54.01           C  
ANISOU  929  CD1 ILE A 121     5821   8384   6315    719    782    301       C  
ATOM    930  N   LEU A 122      59.292   9.270  57.474  1.00 49.48           N  
ANISOU  930  N   LEU A 122     5171   7887   5744     91    723    476       N  
ATOM    931  CA  LEU A 122      59.707  10.532  58.069  1.00 47.06           C  
ANISOU  931  CA  LEU A 122     4829   7623   5429    -54    709    511       C  
ATOM    932  C   LEU A 122      59.101  10.731  59.443  1.00 52.83           C  
ANISOU  932  C   LEU A 122     5634   8281   6158   -122    636    511       C  
ATOM    933  O   LEU A 122      59.810  11.085  60.390  1.00 53.00           O  
ANISOU  933  O   LEU A 122     5605   8352   6181   -197    582    542       O  
ATOM    934  CB  LEU A 122      59.300  11.705  57.174  1.00 48.39           C  
ANISOU  934  CB  LEU A 122     5058   7767   5562   -137    764    510       C  
ATOM    935  CG  LEU A 122      59.986  11.755  55.800  1.00 57.35           C  
ANISOU  935  CG  LEU A 122     6128   8994   6668   -114    850    520       C  
ATOM    936  CD1 LEU A 122      59.723  13.050  55.063  1.00 61.48           C  
ANISOU  936  CD1 LEU A 122     6724   9489   7145   -233    880    543       C  
ATOM    937  CD2 LEU A 122      61.477  11.582  55.978  1.00 52.91           C  
ANISOU  937  CD2 LEU A 122     5385   8594   6125   -118    865    554       C  
ATOM    938  N   VAL A 123      57.782  10.524  59.535  1.00 52.61           N  
ANISOU  938  N   VAL A 123     5722   8148   6121   -103    636    476       N  
ATOM    939  CA  VAL A 123      57.026  10.745  60.767  1.00 50.12           C  
ANISOU  939  CA  VAL A 123     5481   7774   5787   -167    595    463       C  
ATOM    940  C   VAL A 123      57.540   9.831  61.891  1.00 55.27           C  
ANISOU  940  C   VAL A 123     6112   8451   6437   -157    522    493       C  
ATOM    941  O   VAL A 123      57.821  10.282  63.005  1.00 52.62           O  
ANISOU  941  O   VAL A 123     5786   8132   6073   -244    474    508       O  
ATOM    942  CB  VAL A 123      55.488  10.576  60.542  1.00 40.50           C  
ANISOU  942  CB  VAL A 123     4357   6465   4565   -141    621    419       C  
ATOM    943  CG1 VAL A 123      54.731  10.253  61.895  1.00 27.79           C  
ANISOU  943  CG1 VAL A 123     2805   4826   2929   -184    591    408       C  
ATOM    944  CG2 VAL A 123      54.917  11.814  59.821  1.00 30.38           C  
ANISOU  944  CG2 VAL A 123     3117   5145   3283   -173    659    391       C  
ATOM    945  N   LEU A 124      57.689   8.554  61.583  1.00 53.72           N  
ANISOU  945  N   LEU A 124     5900   8246   6264    -50    502    502       N  
ATOM    946  CA  LEU A 124      58.246   7.613  62.545  1.00 50.19           C  
ANISOU  946  CA  LEU A 124     5443   7807   5819    -24    412    540       C  
ATOM    947  C   LEU A 124      59.677   7.939  62.988  1.00 56.20           C  
ANISOU  947  C   LEU A 124     6084   8671   6599    -46    360    581       C  
ATOM    948  O   LEU A 124      60.064   7.627  64.115  1.00 62.40           O  
ANISOU  948  O   LEU A 124     6877   9463   7370    -79    265    619       O  
ATOM    949  CB  LEU A 124      58.185   6.210  61.976  1.00 44.37           C  
ANISOU  949  CB  LEU A 124     4728   7021   5110    111    391    537       C  
ATOM    950  CG  LEU A 124      56.751   5.722  61.833  1.00 50.93           C  
ANISOU  950  CG  LEU A 124     5683   7747   5919    100    407    512       C  
ATOM    951  CD1 LEU A 124      56.704   4.327  61.181  1.00 50.52           C  
ANISOU  951  CD1 LEU A 124     5680   7625   5890    227    371    505       C  
ATOM    952  CD2 LEU A 124      56.068   5.744  63.200  1.00 45.51           C  
ANISOU  952  CD2 LEU A 124     5076   7032   5184    -13    366    535       C  
ATOM    953  N   ARG A 125      60.472   8.562  62.124  1.00 56.05           N  
ANISOU  953  N   ARG A 125     5951   8740   6606    -40    413    581       N  
ATOM    954  CA  ARG A 125      61.830   8.923  62.530  1.00 59.81           C  
ANISOU  954  CA  ARG A 125     6286   9334   7105    -81    362    625       C  
ATOM    955  C   ARG A 125      61.824  10.212  63.320  1.00 58.64           C  
ANISOU  955  C   ARG A 125     6174   9190   6915   -257    335    639       C  
ATOM    956  O   ARG A 125      62.605  10.381  64.241  1.00 60.26           O  
ANISOU  956  O   ARG A 125     6329   9450   7118   -325    244    679       O  
ATOM    957  CB  ARG A 125      62.774   9.039  61.332  1.00 70.45           C  
ANISOU  957  CB  ARG A 125     7476  10801   8490    -22    437    625       C  
ATOM    958  CG  ARG A 125      63.044   7.711  60.659  1.00 86.51           C  
ANISOU  958  CG  ARG A 125     9462  12844  10565    175    451    600       C  
ATOM    959  CD  ARG A 125      64.391   7.702  59.944  1.00101.25           C  
ANISOU  959  CD  ARG A 125    11117  14882  12473    242    499    606       C  
ATOM    960  NE  ARG A 125      65.521   7.630  60.872  1.00111.35           N  
ANISOU  960  NE  ARG A 125    12245  16263  13798    229    394    657       N  
ATOM    961  CZ  ARG A 125      66.628   6.925  60.647  1.00116.86           C  
ANISOU  961  CZ  ARG A 125    12758  17082  14560    373    379    656       C  
ATOM    962  NH1 ARG A 125      66.752   6.217  59.533  1.00121.06           N  
ANISOU  962  NH1 ARG A 125    13247  17642  15107    546    474    598       N  
ATOM    963  NH2 ARG A 125      67.607   6.911  61.541  1.00116.12           N  
ANISOU  963  NH2 ARG A 125    12523  17082  14516    354    263    708       N  
ATOM    964  N   LEU A 126      60.951  11.129  62.938  1.00 62.34           N  
ANISOU  964  N   LEU A 126     6740   9595   7351   -325    404    603       N  
ATOM    965  CA  LEU A 126      60.766  12.371  63.674  1.00 57.41           C  
ANISOU  965  CA  LEU A 126     6192   8939   6681   -475    378    597       C  
ATOM    966  C   LEU A 126      60.293  12.118  65.105  1.00 55.19           C  
ANISOU  966  C   LEU A 126     6013   8606   6349   -515    306    589       C  
ATOM    967  O   LEU A 126      60.597  12.875  66.024  1.00 58.41           O  
ANISOU  967  O   LEU A 126     6462   9018   6712   -634    246    594       O  
ATOM    968  CB  LEU A 126      59.742  13.244  62.949  1.00 51.71           C  
ANISOU  968  CB  LEU A 126     5572   8132   5942   -496    456    550       C  
ATOM    969  CG  LEU A 126      60.283  14.125  61.826  1.00 53.50           C  
ANISOU  969  CG  LEU A 126     5747   8399   6180   -547    504    570       C  
ATOM    970  CD1 LEU A 126      59.147  14.576  60.914  1.00 45.50           C  
ANISOU  970  CD1 LEU A 126     4840   7289   5160   -514    569    528       C  
ATOM    971  CD2 LEU A 126      61.029  15.328  62.415  1.00 41.34           C  
ANISOU  971  CD2 LEU A 126     4209   6881   4615   -713    444    599       C  
ATOM    972  N   SER A 127      59.538  11.048  65.291  1.00 54.27           N  
ANISOU  972  N   SER A 127     5953   8440   6228   -430    311    577       N  
ATOM    973  CA  SER A 127      58.882  10.822  66.565  1.00 53.40           C  
ANISOU  973  CA  SER A 127     5959   8282   6048   -483    270    568       C  
ATOM    974  C   SER A 127      59.778  10.112  67.588  1.00 55.12           C  
ANISOU  974  C   SER A 127     6153   8542   6247   -501    146    630       C  
ATOM    975  O   SER A 127      59.502  10.162  68.796  1.00 49.25           O  
ANISOU  975  O   SER A 127     5512   7778   5422   -586     95    633       O  
ATOM    976  CB  SER A 127      57.536  10.113  66.363  1.00 55.08           C  
ANISOU  976  CB  SER A 127     6252   8424   6251   -423    331    533       C  
ATOM    977  OG  SER A 127      57.720   8.775  65.979  1.00 61.13           O  
ANISOU  977  OG  SER A 127     6988   9183   7057   -320    300    569       O  
ATOM    978  N   LYS A 128      60.853   9.479  67.113  1.00 58.60           N  
ANISOU  978  N   LYS A 128     6460   9046   6759   -417     96    676       N  
ATOM    979  CA  LYS A 128      61.905   8.996  68.016  1.00 67.21           C  
ANISOU  979  CA  LYS A 128     7498  10189   7850   -428    -45    741       C  
ATOM    980  C   LYS A 128      62.332  10.073  69.029  1.00 64.74           C  
ANISOU  980  C   LYS A 128     7217   9909   7472   -595   -114    752       C  
ATOM    981  O   LYS A 128      62.588   9.760  70.180  1.00 68.44           O  
ANISOU  981  O   LYS A 128     7745  10375   7884   -650   -230    791       O  
ATOM    982  CB  LYS A 128      63.134   8.468  67.253  1.00 71.47           C  
ANISOU  982  CB  LYS A 128     7843  10821   8489   -309    -77    775       C  
ATOM    983  CG  LYS A 128      62.923   7.152  66.490  1.00 78.56           C  
ANISOU  983  CG  LYS A 128     8732  11675   9442   -124    -54    764       C  
ATOM    984  CD  LYS A 128      62.492   5.999  67.410  1.00 86.87           C  
ANISOU  984  CD  LYS A 128     9919  12630  10459    -90   -162    797       C  
ATOM    985  CE  LYS A 128      62.268   4.697  66.632  1.00 84.21           C  
ANISOU  985  CE  LYS A 128     9601  12221  10174     87   -156    783       C  
ATOM    986  NZ  LYS A 128      61.769   3.568  67.488  1.00 86.34           N  
ANISOU  986  NZ  LYS A 128    10032  12372  10401     97   -268    826       N  
ATOM    987  N   HIS A 129      62.404  11.331  68.604  1.00 58.59           N  
ANISOU  987  N   HIS A 129     6419   9150   6693   -681    -54    721       N  
ATOM    988  CA  HIS A 129      62.775  12.420  69.497  1.00 56.98           C  
ANISOU  988  CA  HIS A 129     6271   8956   6423   -847   -124    722       C  
ATOM    989  C   HIS A 129      61.628  13.392  69.729  1.00 64.11           C  
ANISOU  989  C   HIS A 129     7349   9763   7248   -919    -43    642       C  
ATOM    990  O   HIS A 129      61.853  14.547  70.093  1.00 70.86           O  
ANISOU  990  O   HIS A 129     8262  10603   8058  -1045    -73    621       O  
ATOM    991  CB  HIS A 129      63.941  13.220  68.923  1.00 65.92           C  
ANISOU  991  CB  HIS A 129     7250  10184   7614   -917   -149    758       C  
ATOM    992  CG  HIS A 129      65.138  12.394  68.594  1.00 80.69           C  
ANISOU  992  CG  HIS A 129     8906  12178   9573   -833   -212    825       C  
ATOM    993  ND1 HIS A 129      65.731  11.546  69.504  1.00 87.49           N  
ANISOU  993  ND1 HIS A 129     9733  13073  10436   -802   -353    878       N  
ATOM    994  CD2 HIS A 129      65.867  12.297  67.459  1.00 85.06           C  
ANISOU  994  CD2 HIS A 129     9267  12836  10215   -766   -153    845       C  
ATOM    995  CE1 HIS A 129      66.765  10.952  68.941  1.00 82.98           C  
ANISOU  995  CE1 HIS A 129     8945  12618   9965   -700   -383    921       C  
ATOM    996  NE2 HIS A 129      66.872  11.393  67.701  1.00 89.98           N  
ANISOU  996  NE2 HIS A 129     9727  13560  10902   -678   -252    898       N  
ATOM    997  N   GLY A 130      60.402  12.946  69.507  1.00 52.51           N  
ANISOU  997  N   GLY A 130     5959   8226   5764   -838     53    593       N  
ATOM    998  CA  GLY A 130      59.270  13.800  69.782  1.00 46.99           C  
ANISOU  998  CA  GLY A 130     5405   7450   5000   -880    131    508       C  
ATOM    999  C   GLY A 130      59.244  15.117  69.044  1.00 50.20           C  
ANISOU  999  C   GLY A 130     5822   7819   5433   -918    176    466       C  
ATOM   1000  O   GLY A 130      58.990  16.150  69.639  1.00 55.90           O  
ANISOU 1000  O   GLY A 130     6663   8485   6089  -1003    165    410       O  
ATOM   1001  N   HIS A 131      59.467  15.082  67.736  1.00 49.76           N  
ANISOU 1001  N   HIS A 131     5661   7781   5464   -855    225    489       N  
ATOM   1002  CA  HIS A 131      59.437  16.307  66.955  1.00 47.47           C  
ANISOU 1002  CA  HIS A 131     5398   7446   5194   -901    258    465       C  
ATOM   1003  C   HIS A 131      58.020  16.581  66.489  1.00 53.63           C  
ANISOU 1003  C   HIS A 131     6272   8131   5976   -820    351    388       C  
ATOM   1004  O   HIS A 131      57.704  16.538  65.291  1.00 58.75           O  
ANISOU 1004  O   HIS A 131     6879   8763   6678   -749    410    391       O  
ATOM   1005  CB  HIS A 131      60.428  16.246  65.789  1.00 54.71           C  
ANISOU 1005  CB  HIS A 131     6161   8443   6181   -898    267    534       C  
ATOM   1006  CG  HIS A 131      61.863  16.274  66.216  1.00 60.09           C  
ANISOU 1006  CG  HIS A 131     6728   9233   6871   -996    172    605       C  
ATOM   1007  ND1 HIS A 131      62.416  17.343  66.897  1.00 64.56           N  
ANISOU 1007  ND1 HIS A 131     7352   9786   7392  -1161     87    614       N  
ATOM   1008  CD2 HIS A 131      62.861  15.364  66.080  1.00 56.93           C  
ANISOU 1008  CD2 HIS A 131     6152   8956   6521   -949    138    669       C  
ATOM   1009  CE1 HIS A 131      63.683  17.092  67.156  1.00 65.51           C  
ANISOU 1009  CE1 HIS A 131     7324  10028   7537  -1225      2    688       C  
ATOM   1010  NE2 HIS A 131      63.982  15.896  66.671  1.00 64.41           N  
ANISOU 1010  NE2 HIS A 131     7033   9979   7460  -1088     34    720       N  
ATOM   1011  N   SER A 132      57.170  16.882  67.462  1.00 52.91           N  
ANISOU 1011  N   SER A 132     6303   7982   5817   -831    361    315       N  
ATOM   1012  CA  SER A 132      55.749  16.976  67.211  1.00 54.36           C  
ANISOU 1012  CA  SER A 132     6546   8101   6006   -740    448    236       C  
ATOM   1013  C   SER A 132      55.393  18.017  66.153  1.00 54.38           C  
ANISOU 1013  C   SER A 132     6585   8020   6058   -712    472    206       C  
ATOM   1014  O   SER A 132      54.630  17.720  65.239  1.00 59.19           O  
ANISOU 1014  O   SER A 132     7161   8610   6720   -616    527    195       O  
ATOM   1015  CB  SER A 132      54.973  17.195  68.510  1.00 53.29           C  
ANISOU 1015  CB  SER A 132     6525   7944   5780   -760    468    154       C  
ATOM   1016  OG  SER A 132      55.149  18.502  68.998  1.00 60.80           O  
ANISOU 1016  OG  SER A 132     7596   8825   6682   -831    430     96       O  
ATOM   1017  N   ASP A 133      55.942  19.223  66.244  1.00 56.44           N  
ANISOU 1017  N   ASP A 133     6925   8222   6297   -805    415    199       N  
ATOM   1018  CA  ASP A 133      55.570  20.264  65.275  1.00 54.11           C  
ANISOU 1018  CA  ASP A 133     6696   7822   6039   -787    418    177       C  
ATOM   1019  C   ASP A 133      56.059  19.952  63.856  1.00 54.85           C  
ANISOU 1019  C   ASP A 133     6689   7958   6194   -775    434    262       C  
ATOM   1020  O   ASP A 133      55.335  20.208  62.897  1.00 59.39           O  
ANISOU 1020  O   ASP A 133     7292   8469   6806   -702    464    246       O  
ATOM   1021  CB  ASP A 133      56.085  21.621  65.704  1.00 60.36           C  
ANISOU 1021  CB  ASP A 133     7623   8522   6788   -907    337    157       C  
ATOM   1022  CG  ASP A 133      57.589  21.662  65.750  1.00 91.56           C  
ANISOU 1022  CG  ASP A 133    11508  12552  10728  -1062    264    256       C  
ATOM   1023  OD1 ASP A 133      58.181  20.724  66.341  1.00 96.98           O  
ANISOU 1023  OD1 ASP A 133    12089  13357  11402  -1080    253    298       O  
ATOM   1024  OD2 ASP A 133      58.174  22.620  65.189  1.00100.81           O  
ANISOU 1024  OD2 ASP A 133    12728  13670  11904  -1169    210    298       O  
ATOM   1025  N   ALA A 134      57.262  19.388  63.706  1.00 49.96           N  
ANISOU 1025  N   ALA A 134     5949   7452   5581   -840    415    348       N  
ATOM   1026  CA  ALA A 134      57.690  18.992  62.359  1.00 61.89           C  
ANISOU 1026  CA  ALA A 134     7358   9024   7135   -813    455    415       C  
ATOM   1027  C   ALA A 134      56.715  17.955  61.779  1.00 58.96           C  
ANISOU 1027  C   ALA A 134     6951   8655   6798   -660    524    387       C  
ATOM   1028  O   ALA A 134      56.335  18.023  60.598  1.00 52.89           O  
ANISOU 1028  O   ALA A 134     6188   7856   6050   -610    558    396       O  
ATOM   1029  CB  ALA A 134      59.165  18.471  62.316  1.00 32.40           C  
ANISOU 1029  CB  ALA A 134     3468   5436   3408   -884    435    500       C  
ATOM   1030  N   ILE A 135      56.313  17.006  62.622  1.00 46.93           N  
ANISOU 1030  N   ILE A 135     5402   7160   5268   -602    533    360       N  
ATOM   1031  CA  ILE A 135      55.389  15.957  62.223  1.00 47.16           C  
ANISOU 1031  CA  ILE A 135     5405   7190   5324   -482    582    339       C  
ATOM   1032  C   ILE A 135      54.092  16.585  61.689  1.00 55.44           C  
ANISOU 1032  C   ILE A 135     6533   8141   6391   -425    610    279       C  
ATOM   1033  O   ILE A 135      53.689  16.338  60.546  1.00 55.44           O  
ANISOU 1033  O   ILE A 135     6518   8124   6422   -361    633    289       O  
ATOM   1034  CB  ILE A 135      55.092  15.003  63.410  1.00 49.36           C  
ANISOU 1034  CB  ILE A 135     5677   7501   5577   -467    576    325       C  
ATOM   1035  CG1 ILE A 135      56.358  14.259  63.812  1.00 38.42           C  
ANISOU 1035  CG1 ILE A 135     4209   6204   4187   -496    527    391       C  
ATOM   1036  CG2 ILE A 135      53.983  14.028  63.054  1.00 49.17           C  
ANISOU 1036  CG2 ILE A 135     5644   7462   5576   -372    619    303       C  
ATOM   1037  CD1 ILE A 135      56.181  13.181  64.902  1.00 31.68           C  
ANISOU 1037  CD1 ILE A 135     3364   5373   3301   -486    498    400       C  
ATOM   1038  N   GLN A 136      53.461  17.424  62.505  1.00 53.15           N  
ANISOU 1038  N   GLN A 136     6330   7787   6079   -440    601    212       N  
ATOM   1039  CA  GLN A 136      52.224  18.074  62.099  1.00 51.75           C  
ANISOU 1039  CA  GLN A 136     6214   7519   5930   -364    616    145       C  
ATOM   1040  C   GLN A 136      52.455  18.913  60.872  1.00 49.36           C  
ANISOU 1040  C   GLN A 136     5957   7147   5652   -374    584    179       C  
ATOM   1041  O   GLN A 136      51.541  19.154  60.084  1.00 51.99           O  
ANISOU 1041  O   GLN A 136     6318   7415   6022   -295    582    155       O  
ATOM   1042  CB  GLN A 136      51.652  18.947  63.221  1.00 59.85           C  
ANISOU 1042  CB  GLN A 136     7330   8488   6922   -368    614     53       C  
ATOM   1043  CG  GLN A 136      50.933  18.162  64.327  1.00 72.40           C  
ANISOU 1043  CG  GLN A 136     8886  10146   8479   -340    670      2       C  
ATOM   1044  CD  GLN A 136      50.008  17.051  63.795  1.00 86.71           C  
ANISOU 1044  CD  GLN A 136    10603  12006  10335   -261    718     11       C  
ATOM   1045  OE1 GLN A 136      49.200  17.275  62.876  1.00 91.75           O  
ANISOU 1045  OE1 GLN A 136    11227  12599  11033   -181    722     -9       O  
ATOM   1046  NE2 GLN A 136      50.118  15.848  64.390  1.00 77.71           N  
ANISOU 1046  NE2 GLN A 136     9412  10950   9164   -292    739     47       N  
ATOM   1047  N   MET A 137      53.681  19.383  60.706  1.00 54.93           N  
ANISOU 1047  N   MET A 137     6672   7868   6332   -483    550    242       N  
ATOM   1048  CA  MET A 137      53.988  20.203  59.541  1.00 47.72           C  
ANISOU 1048  CA  MET A 137     5815   6895   5421   -526    521    290       C  
ATOM   1049  C   MET A 137      53.972  19.331  58.274  1.00 50.15           C  
ANISOU 1049  C   MET A 137     6047   7262   5744   -469    564    339       C  
ATOM   1050  O   MET A 137      53.292  19.650  57.297  1.00 53.04           O  
ANISOU 1050  O   MET A 137     6472   7557   6124   -420    551    338       O  
ATOM   1051  CB  MET A 137      55.327  20.893  59.737  1.00 52.54           C  
ANISOU 1051  CB  MET A 137     6440   7529   5993   -684    479    352       C  
ATOM   1052  CG  MET A 137      55.637  21.943  58.677  1.00 63.62           C  
ANISOU 1052  CG  MET A 137     7934   8856   7382   -769    439    408       C  
ATOM   1053  SD  MET A 137      56.601  21.230  57.343  1.00 69.19           S  
ANISOU 1053  SD  MET A 137     8512   9708   8070   -812    503    512       S  
ATOM   1054  CE  MET A 137      58.090  20.840  58.279  1.00 86.61           C  
ANISOU 1054  CE  MET A 137    10572  12072  10264   -927    505    556       C  
ATOM   1055  N   LEU A 138      54.690  18.211  58.312  1.00 43.48           N  
ANISOU 1055  N   LEU A 138     5083   6541   4895   -466    604    375       N  
ATOM   1056  CA  LEU A 138      54.711  17.292  57.183  1.00 44.49           C  
ANISOU 1056  CA  LEU A 138     5153   6724   5028   -401    648    405       C  
ATOM   1057  C   LEU A 138      53.296  16.897  56.758  1.00 48.81           C  
ANISOU 1057  C   LEU A 138     5739   7202   5604   -289    649    356       C  
ATOM   1058  O   LEU A 138      52.949  16.940  55.570  1.00 44.94           O  
ANISOU 1058  O   LEU A 138     5286   6680   5108   -257    648    372       O  
ATOM   1059  CB  LEU A 138      55.519  16.036  57.517  1.00 32.82           C  
ANISOU 1059  CB  LEU A 138     3552   5367   3551   -375    680    427       C  
ATOM   1060  CG  LEU A 138      57.028  16.213  57.579  1.00 39.16           C  
ANISOU 1060  CG  LEU A 138     4267   6277   4335   -467    685    487       C  
ATOM   1061  CD1 LEU A 138      57.703  14.906  57.988  1.00 43.90           C  
ANISOU 1061  CD1 LEU A 138     4745   6983   4953   -403    698    497       C  
ATOM   1062  CD2 LEU A 138      57.510  16.659  56.177  1.00 43.74           C  
ANISOU 1062  CD2 LEU A 138     4849   6889   4883   -509    725    534       C  
ATOM   1063  N   ILE A 139      52.477  16.516  57.738  1.00 42.74           N  
ANISOU 1063  N   ILE A 139     4959   6420   4861   -241    648    300       N  
ATOM   1064  CA  ILE A 139      51.109  16.107  57.448  1.00 46.19           C  
ANISOU 1064  CA  ILE A 139     5403   6814   5333   -150    648    256       C  
ATOM   1065  C   ILE A 139      50.293  17.235  56.817  1.00 49.60           C  
ANISOU 1065  C   ILE A 139     5918   7141   5788   -120    605    231       C  
ATOM   1066  O   ILE A 139      49.504  16.996  55.912  1.00 51.65           O  
ANISOU 1066  O   ILE A 139     6185   7369   6070    -58    585    229       O  
ATOM   1067  CB  ILE A 139      50.408  15.594  58.696  1.00 39.89           C  
ANISOU 1067  CB  ILE A 139     4569   6041   4547   -129    667    205       C  
ATOM   1068  CG1 ILE A 139      51.046  14.283  59.143  1.00 44.34           C  
ANISOU 1068  CG1 ILE A 139     5070   6686   5091   -143    686    240       C  
ATOM   1069  CG2 ILE A 139      48.952  15.374  58.403  1.00 36.49           C  
ANISOU 1069  CG2 ILE A 139     4126   5580   4159    -53    665    160       C  
ATOM   1070  CD1 ILE A 139      50.580  13.848  60.522  1.00 44.14           C  
ANISOU 1070  CD1 ILE A 139     5031   6692   5050   -162    700    209       C  
ATOM   1071  N   LYS A 140      50.497  18.467  57.267  1.00 53.76           N  
ANISOU 1071  N   LYS A 140     6519   7602   6307   -164    574    214       N  
ATOM   1072  CA  LYS A 140      49.753  19.594  56.700  1.00 56.75           C  
ANISOU 1072  CA  LYS A 140     6996   7855   6711   -123    512    191       C  
ATOM   1073  C   LYS A 140      50.203  19.907  55.279  1.00 59.41           C  
ANISOU 1073  C   LYS A 140     7397   8157   7019   -164    476    268       C  
ATOM   1074  O   LYS A 140      49.374  20.216  54.413  1.00 58.75           O  
ANISOU 1074  O   LYS A 140     7368   7994   6959   -100    422    266       O  
ATOM   1075  CB  LYS A 140      49.892  20.839  57.572  1.00 54.12           C  
ANISOU 1075  CB  LYS A 140     6756   7436   6370   -158    475    146       C  
ATOM   1076  CG  LYS A 140      49.087  22.005  57.088  1.00 60.20           C  
ANISOU 1076  CG  LYS A 140     7643   8054   7175    -91    395    111       C  
ATOM   1077  CD  LYS A 140      49.445  23.253  57.894  1.00 71.66           C  
ANISOU 1077  CD  LYS A 140     9221   9400   8605   -141    348     71       C  
ATOM   1078  CE  LYS A 140      48.512  24.429  57.621  1.00 68.39           C  
ANISOU 1078  CE  LYS A 140     8936   8812   8237    -37    257     11       C  
ATOM   1079  NZ  LYS A 140      48.979  25.650  58.345  1.00 74.15           N  
ANISOU 1079  NZ  LYS A 140     9824   9415   8936    -97    197    -27       N  
ATOM   1080  N   THR A 141      51.516  19.819  55.049  1.00 51.94           N  
ANISOU 1080  N   THR A 141     6437   7280   6019   -272    506    338       N  
ATOM   1081  CA  THR A 141      52.096  20.091  53.743  1.00 49.52           C  
ANISOU 1081  CA  THR A 141     6184   6972   5660   -337    498    417       C  
ATOM   1082  C   THR A 141      51.662  19.031  52.735  1.00 49.75           C  
ANISOU 1082  C   THR A 141     6174   7048   5680   -260    526    425       C  
ATOM   1083  O   THR A 141      51.215  19.365  51.633  1.00 52.76           O  
ANISOU 1083  O   THR A 141     6643   7364   6038   -248    480    452       O  
ATOM   1084  CB  THR A 141      53.626  20.188  53.821  1.00 52.82           C  
ANISOU 1084  CB  THR A 141     6558   7490   6023   -475    541    484       C  
ATOM   1085  OG1 THR A 141      53.972  21.329  54.610  1.00 59.46           O  
ANISOU 1085  OG1 THR A 141     7471   8258   6862   -569    487    483       O  
ATOM   1086  CG2 THR A 141      54.219  20.345  52.454  1.00 51.45           C  
ANISOU 1086  CG2 THR A 141     6421   7349   5779   -547    560    564       C  
ATOM   1087  N   THR A 142      51.773  17.757  53.102  1.00 46.74           N  
ANISOU 1087  N   THR A 142     5681   6767   5312   -211    585    403       N  
ATOM   1088  CA  THR A 142      51.173  16.709  52.275  1.00 43.96           C  
ANISOU 1088  CA  THR A 142     5313   6432   4957   -130    594    393       C  
ATOM   1089  C   THR A 142      49.712  17.043  51.869  1.00 56.18           C  
ANISOU 1089  C   THR A 142     6922   7874   6549    -57    515    361       C  
ATOM   1090  O   THR A 142      49.314  16.848  50.719  1.00 49.58           O  
ANISOU 1090  O   THR A 142     6141   7010   5685    -33    481    381       O  
ATOM   1091  CB  THR A 142      51.215  15.377  52.992  1.00 43.63           C  
ANISOU 1091  CB  THR A 142     5170   6468   4940    -80    639    362       C  
ATOM   1092  OG1 THR A 142      52.532  15.171  53.489  1.00 52.53           O  
ANISOU 1092  OG1 THR A 142     6229   7687   6041   -133    690    390       O  
ATOM   1093  CG2 THR A 142      50.823  14.231  52.064  1.00 42.17           C  
ANISOU 1093  CG2 THR A 142     4989   6296   4738    -15    642    357       C  
ATOM   1094  N   SER A 143      48.924  17.567  52.807  1.00 54.21           N  
ANISOU 1094  N   SER A 143     6660   7572   6365    -19    484    307       N  
ATOM   1095  CA  SER A 143      47.524  17.912  52.537  1.00 52.38           C  
ANISOU 1095  CA  SER A 143     6450   7257   6193     68    409    267       C  
ATOM   1096  C   SER A 143      47.340  19.033  51.530  1.00 53.71           C  
ANISOU 1096  C   SER A 143     6749   7311   6346     65    317    304       C  
ATOM   1097  O   SER A 143      46.533  18.885  50.609  1.00 49.49           O  
ANISOU 1097  O   SER A 143     6243   6735   5823    118    249    312       O  
ATOM   1098  CB  SER A 143      46.777  18.279  53.826  1.00 59.93           C  
ANISOU 1098  CB  SER A 143     7352   8202   7218    120    415    188       C  
ATOM   1099  OG  SER A 143      46.581  17.131  54.637  1.00 64.84           O  
ANISOU 1099  OG  SER A 143     7861   8923   7852    127    481    160       O  
ATOM   1100  N   GLN A 144      48.048  20.153  51.718  1.00 44.30           N  
ANISOU 1100  N   GLN A 144     5647   6057   5127     -5    299    329       N  
ATOM   1101  CA  GLN A 144      47.990  21.258  50.750  1.00 52.05           C  
ANISOU 1101  CA  GLN A 144     6785   6913   6079    -33    200    382       C  
ATOM   1102  C   GLN A 144      48.446  20.813  49.359  1.00 54.53           C  
ANISOU 1102  C   GLN A 144     7152   7265   6301    -94    205    463       C  
ATOM   1103  O   GLN A 144      47.771  21.062  48.372  1.00 62.43           O  
ANISOU 1103  O   GLN A 144     8243   8187   7291    -59    113    489       O  
ATOM   1104  CB  GLN A 144      48.853  22.443  51.184  1.00 62.79           C  
ANISOU 1104  CB  GLN A 144     8247   8203   7408   -137    181    410       C  
ATOM   1105  CG  GLN A 144      48.349  23.200  52.377  1.00 84.98           C  
ANISOU 1105  CG  GLN A 144    11071  10928  10288    -73    147    324       C  
ATOM   1106  CD  GLN A 144      49.489  23.829  53.161  1.00102.59           C  
ANISOU 1106  CD  GLN A 144    13348  13157  12476   -203    171    341       C  
ATOM   1107  OE1 GLN A 144      50.630  23.883  52.690  1.00109.53           O  
ANISOU 1107  OE1 GLN A 144    14252  14086  13279   -350    196    431       O  
ATOM   1108  NE2 GLN A 144      49.189  24.299  54.367  1.00107.13           N  
ANISOU 1108  NE2 GLN A 144    13929  13683  13092   -156    165    253       N  
ATOM   1109  N   TYR A 145      49.597  20.149  49.303  1.00 56.91           N  
ANISOU 1109  N   TYR A 145     7396   7694   6534   -178    312    498       N  
ATOM   1110  CA  TYR A 145      50.214  19.750  48.047  1.00 61.12           C  
ANISOU 1110  CA  TYR A 145     7975   8288   6959   -240    349    564       C  
ATOM   1111  C   TYR A 145      49.260  18.867  47.293  1.00 57.97           C  
ANISOU 1111  C   TYR A 145     7578   7884   6564   -144    313    539       C  
ATOM   1112  O   TYR A 145      49.091  19.015  46.076  1.00 62.25           O  
ANISOU 1112  O   TYR A 145     8235   8389   7030   -166    262    585       O  
ATOM   1113  CB  TYR A 145      51.539  19.009  48.281  1.00 60.87           C  
ANISOU 1113  CB  TYR A 145     7835   8418   6876   -304    482    579       C  
ATOM   1114  CG  TYR A 145      52.273  18.688  46.997  1.00 61.77           C  
ANISOU 1114  CG  TYR A 145     7991   8613   6865   -367    544    636       C  
ATOM   1115  CD1 TYR A 145      52.046  17.495  46.316  1.00 58.58           C  
ANISOU 1115  CD1 TYR A 145     7565   8267   6425   -287    583    605       C  
ATOM   1116  CD2 TYR A 145      53.176  19.600  46.446  1.00 63.41           C  
ANISOU 1116  CD2 TYR A 145     8274   8839   6981   -515    562    719       C  
ATOM   1117  CE1 TYR A 145      52.709  17.208  45.120  1.00 58.48           C  
ANISOU 1117  CE1 TYR A 145     7603   8335   6280   -335    651    643       C  
ATOM   1118  CE2 TYR A 145      53.856  19.326  45.270  1.00 60.28           C  
ANISOU 1118  CE2 TYR A 145     7911   8541   6453   -580    639    769       C  
ATOM   1119  CZ  TYR A 145      53.620  18.129  44.601  1.00 68.11           C  
ANISOU 1119  CZ  TYR A 145     8880   9595   7402   -481    689    724       C  
ATOM   1120  OH  TYR A 145      54.306  17.864  43.423  1.00 68.77           O  
ANISOU 1120  OH  TYR A 145     9008   9784   7339   -538    778    759       O  
ATOM   1121  N   SER A 146      48.635  17.951  48.020  1.00 49.84           N  
ANISOU 1121  N   SER A 146     6430   6892   5615    -54    332    470       N  
ATOM   1122  CA  SER A 146      47.613  17.086  47.432  1.00 56.26           C  
ANISOU 1122  CA  SER A 146     7236   7695   6446     25    281    443       C  
ATOM   1123  C   SER A 146      46.470  17.861  46.782  1.00 57.92           C  
ANISOU 1123  C   SER A 146     7535   7782   6688     70    137    453       C  
ATOM   1124  O   SER A 146      45.942  17.463  45.742  1.00 57.22           O  
ANISOU 1124  O   SER A 146     7509   7671   6560     88     70    470       O  
ATOM   1125  CB  SER A 146      47.027  16.155  48.494  1.00 49.53           C  
ANISOU 1125  CB  SER A 146     6245   6892   5684     91    311    376       C  
ATOM   1126  OG  SER A 146      47.736  14.930  48.530  1.00 44.72           O  
ANISOU 1126  OG  SER A 146     5585   6376   5030     81    398    370       O  
ATOM   1127  N   ASP A 147      46.088  18.960  47.419  1.00 54.03           N  
ANISOU 1127  N   ASP A 147     7054   7204   6269     97     80    437       N  
ATOM   1128  CA  ASP A 147      44.907  19.707  47.016  1.00 54.86           C  
ANISOU 1128  CA  ASP A 147     7217   7189   6438    177    -69    430       C  
ATOM   1129  C   ASP A 147      45.280  20.585  45.832  1.00 56.97           C  
ANISOU 1129  C   ASP A 147     7679   7358   6608    107   -156    518       C  
ATOM   1130  O   ASP A 147      44.443  20.974  45.025  1.00 67.28           O  
ANISOU 1130  O   ASP A 147     9071   8567   7924    156   -298    542       O  
ATOM   1131  CB  ASP A 147      44.419  20.555  48.194  1.00 60.66           C  
ANISOU 1131  CB  ASP A 147     7899   7865   7282    251    -89    364       C  
ATOM   1132  CG  ASP A 147      43.028  21.138  47.977  1.00 69.10           C  
ANISOU 1132  CG  ASP A 147     8968   8834   8452    382   -234    329       C  
ATOM   1133  OD1 ASP A 147      42.116  20.392  47.545  1.00 77.70           O  
ANISOU 1133  OD1 ASP A 147     9977   9963   9581    439   -282    315       O  
ATOM   1134  OD2 ASP A 147      42.846  22.344  48.262  1.00 68.56           O  
ANISOU 1134  OD2 ASP A 147     8978   8643   8428    432   -309    311       O  
ATOM   1135  N   GLU A 148      46.567  20.866  45.725  1.00 57.71           N  
ANISOU 1135  N   GLU A 148     7837   7487   6601    -18    -72    574       N  
ATOM   1136  CA  GLU A 148      47.084  21.727  44.683  1.00 67.39           C  
ANISOU 1136  CA  GLU A 148     9254   8639   7715   -125   -132    671       C  
ATOM   1137  C   GLU A 148      47.461  20.992  43.397  1.00 63.30           C  
ANISOU 1137  C   GLU A 148     8801   8197   7054   -189    -95    725       C  
ATOM   1138  O   GLU A 148      47.474  21.594  42.327  1.00 61.51           O  
ANISOU 1138  O   GLU A 148     8749   7896   6727   -257   -180    804       O  
ATOM   1139  CB  GLU A 148      48.319  22.446  45.205  1.00 73.17           C  
ANISOU 1139  CB  GLU A 148    10013   9386   8400   -255    -56    711       C  
ATOM   1140  CG  GLU A 148      48.031  23.475  46.265  1.00 85.60           C  
ANISOU 1140  CG  GLU A 148    11605  10843  10078   -217   -122    671       C  
ATOM   1141  CD  GLU A 148      49.229  24.370  46.509  1.00101.65           C  
ANISOU 1141  CD  GLU A 148    13723  12857  12044   -383    -93    735       C  
ATOM   1142  OE1 GLU A 148      50.120  24.407  45.630  1.00105.78           O  
ANISOU 1142  OE1 GLU A 148    14317  13438  12438   -531    -49    829       O  
ATOM   1143  OE2 GLU A 148      49.286  25.027  47.571  1.00104.58           O  
ANISOU 1143  OE2 GLU A 148    14091  13162  12483   -374   -111    690       O  
ATOM   1144  N   LYS A 149      47.765  19.700  43.500  1.00 56.97           N  
ANISOU 1144  N   LYS A 149     7877   7535   6234   -167     25    679       N  
ATOM   1145  CA  LYS A 149      48.431  19.025  42.409  1.00 58.59           C  
ANISOU 1145  CA  LYS A 149     8143   7831   6286   -232    101    715       C  
ATOM   1146  C   LYS A 149      47.945  17.623  42.082  1.00 67.56           C  
ANISOU 1146  C   LYS A 149     9225   9027   7417   -149    120    654       C  
ATOM   1147  O   LYS A 149      48.327  17.066  41.057  1.00 73.48           O  
ANISOU 1147  O   LYS A 149    10058   9832   8031   -183    162    670       O  
ATOM   1148  CB  LYS A 149      49.926  19.010  42.679  1.00 56.80           C  
ANISOU 1148  CB  LYS A 149     7859   7735   5986   -336    265    740       C  
ATOM   1149  CG  LYS A 149      50.430  20.398  42.969  1.00 61.24           C  
ANISOU 1149  CG  LYS A 149     8493   8231   6544   -449    233    808       C  
ATOM   1150  CD  LYS A 149      51.871  20.573  42.572  1.00 70.64           C  
ANISOU 1150  CD  LYS A 149     9689   9550   7602   -606    364    876       C  
ATOM   1151  CE  LYS A 149      52.238  22.049  42.603  1.00 81.29           C  
ANISOU 1151  CE  LYS A 149    11164  10799   8922   -753    293    966       C  
ATOM   1152  NZ  LYS A 149      53.683  22.281  42.307  1.00 84.63           N  
ANISOU 1152  NZ  LYS A 149    11566  11369   9222   -937    425   1041       N  
ATOM   1153  N   LEU A 150      47.090  17.055  42.921  1.00 60.42           N  
ANISOU 1153  N   LEU A 150     8195   8111   6650    -48     86    585       N  
ATOM   1154  CA  LEU A 150      46.723  15.658  42.752  1.00 46.70           C  
ANISOU 1154  CA  LEU A 150     6406   6426   4911     10    106    530       C  
ATOM   1155  C   LEU A 150      45.238  15.514  42.580  1.00 54.84           C  
ANISOU 1155  C   LEU A 150     7433   7376   6027     78    -50    509       C  
ATOM   1156  O   LEU A 150      44.753  14.528  42.018  1.00 61.27           O  
ANISOU 1156  O   LEU A 150     8270   8199   6811     99    -90    485       O  
ATOM   1157  CB  LEU A 150      47.171  14.873  43.978  1.00 52.40           C  
ANISOU 1157  CB  LEU A 150     6965   7235   5710     43    221    474       C  
ATOM   1158  CG  LEU A 150      48.697  14.863  44.094  1.00 59.93           C  
ANISOU 1158  CG  LEU A 150     7896   8292   6584    -16    370    493       C  
ATOM   1159  CD1 LEU A 150      49.143  14.328  45.443  1.00 54.71           C  
ANISOU 1159  CD1 LEU A 150     7079   7699   6011     13    453    451       C  
ATOM   1160  CD2 LEU A 150      49.320  14.065  42.912  1.00 45.05           C  
ANISOU 1160  CD2 LEU A 150     6094   6472   4550    -26    436    492       C  
ATOM   1161  N   LYS A 151      44.511  16.507  43.072  1.00 53.64           N  
ANISOU 1161  N   LYS A 151     7253   7146   5984    115   -144    513       N  
ATOM   1162  CA  LYS A 151      43.093  16.324  43.307  1.00 56.86           C  
ANISOU 1162  CA  LYS A 151     7573   7513   6516    198   -266    475       C  
ATOM   1163  C   LYS A 151      42.347  16.086  42.025  1.00 53.50           C  
ANISOU 1163  C   LYS A 151     7259   7034   6034    199   -413    506       C  
ATOM   1164  O   LYS A 151      41.419  15.271  41.987  1.00 44.83           O  
ANISOU 1164  O   LYS A 151     6086   5953   4995    233   -482    472       O  
ATOM   1165  CB  LYS A 151      42.493  17.505  44.066  1.00 66.97           C  
ANISOU 1165  CB  LYS A 151     8799   8723   7924    264   -332    460       C  
ATOM   1166  CG  LYS A 151      42.835  18.835  43.494  1.00 79.19           C  
ANISOU 1166  CG  LYS A 151    10511  10160   9418    234   -408    524       C  
ATOM   1167  CD  LYS A 151      41.998  19.883  44.174  1.00 78.97           C  
ANISOU 1167  CD  LYS A 151    10437  10039   9531    337   -506    490       C  
ATOM   1168  CE  LYS A 151      40.652  19.303  44.537  1.00 70.26           C  
ANISOU 1168  CE  LYS A 151     9160   8975   8561    446   -567    424       C  
ATOM   1169  NZ  LYS A 151      39.794  20.411  45.024  1.00 76.21           N  
ANISOU 1169  NZ  LYS A 151     9874   9636   9446    571   -672    384       N  
ATOM   1170  N   ASN A 152      42.742  16.814  40.986  1.00 56.01           N  
ANISOU 1170  N   ASN A 152     7761   7287   6232    146   -470    575       N  
ATOM   1171  CA  ASN A 152      42.138  16.654  39.671  1.00 53.34           C  
ANISOU 1171  CA  ASN A 152     7567   6894   5808    131   -619    614       C  
ATOM   1172  C   ASN A 152      42.434  15.282  39.102  1.00 57.44           C  
ANISOU 1172  C   ASN A 152     8123   7488   6216     95   -553    584       C  
ATOM   1173  O   ASN A 152      41.528  14.587  38.635  1.00 56.25           O  
ANISOU 1173  O   ASN A 152     7978   7318   6077    114   -671    567       O  
ATOM   1174  CB  ASN A 152      42.635  17.743  38.736  1.00 56.48           C  
ANISOU 1174  CB  ASN A 152     8176   7210   6074     60   -678    704       C  
ATOM   1175  CG  ASN A 152      42.190  19.120  39.180  1.00 68.09           C  
ANISOU 1175  CG  ASN A 152     9650   8564   7657    109   -792    733       C  
ATOM   1176  OD1 ASN A 152      41.016  19.333  39.477  1.00 63.09           O  
ANISOU 1176  OD1 ASN A 152     8927   7873   7172    216   -932    703       O  
ATOM   1177  ND2 ASN A 152      43.128  20.060  39.242  1.00 79.65           N  
ANISOU 1177  ND2 ASN A 152    11216   9994   9055     32   -734    787       N  
ATOM   1178  N   TRP A 153      43.703  14.886  39.147  1.00 54.84           N  
ANISOU 1178  N   TRP A 153     7816   7241   5779     46   -372    575       N  
ATOM   1179  CA  TRP A 153      44.048  13.526  38.761  1.00 54.57           C  
ANISOU 1179  CA  TRP A 153     7808   7273   5653     42   -295    525       C  
ATOM   1180  C   TRP A 153      43.216  12.516  39.568  1.00 59.99           C  
ANISOU 1180  C   TRP A 153     8343   7970   6480     99   -327    461       C  
ATOM   1181  O   TRP A 153      42.618  11.582  38.998  1.00 55.73           O  
ANISOU 1181  O   TRP A 153     7858   7409   5906     98   -410    435       O  
ATOM   1182  CB  TRP A 153      45.553  13.242  38.923  1.00 49.29           C  
ANISOU 1182  CB  TRP A 153     7132   6709   4887     13    -83    511       C  
ATOM   1183  CG  TRP A 153      45.937  11.936  38.272  1.00 60.37           C  
ANISOU 1183  CG  TRP A 153     8608   8160   6168     28    -18    454       C  
ATOM   1184  CD1 TRP A 153      46.418  11.773  37.010  1.00 61.54           C  
ANISOU 1184  CD1 TRP A 153     8936   8330   6118    -12     11    462       C  
ATOM   1185  CD2 TRP A 153      45.823  10.607  38.830  1.00 65.21           C  
ANISOU 1185  CD2 TRP A 153     9140   8795   6843     89     16    377       C  
ATOM   1186  NE1 TRP A 153      46.624  10.437  36.743  1.00 66.70           N  
ANISOU 1186  NE1 TRP A 153     9624   9012   6706     38     64    381       N  
ATOM   1187  CE2 TRP A 153      46.276   9.703  37.838  1.00 67.58           C  
ANISOU 1187  CE2 TRP A 153     9585   9115   6979     98     60    332       C  
ATOM   1188  CE3 TRP A 153      45.395  10.101  40.064  1.00 68.50           C  
ANISOU 1188  CE3 TRP A 153     9391   9211   7424    131     13    343       C  
ATOM   1189  CZ2 TRP A 153      46.311   8.317  38.045  1.00 67.55           C  
ANISOU 1189  CZ2 TRP A 153     9576   9109   6983    158     85    253       C  
ATOM   1190  CZ3 TRP A 153      45.429   8.721  40.269  1.00 73.03           C  
ANISOU 1190  CZ3 TRP A 153     9958   9790   8000    170     37    279       C  
ATOM   1191  CH2 TRP A 153      45.883   7.846  39.258  1.00 74.25           C  
ANISOU 1191  CH2 TRP A 153    10269   9942   8000    188     65    234       C  
ATOM   1192  N   ILE A 154      43.170  12.714  40.893  1.00 53.30           N  
ANISOU 1192  N   ILE A 154     7318   7153   5779    133   -267    439       N  
ATOM   1193  CA  ILE A 154      42.511  11.757  41.788  1.00 53.24           C  
ANISOU 1193  CA  ILE A 154     7163   7175   5892    163   -269    386       C  
ATOM   1194  C   ILE A 154      41.015  11.658  41.509  1.00 55.26           C  
ANISOU 1194  C   ILE A 154     7382   7383   6231    175   -451    388       C  
ATOM   1195  O   ILE A 154      40.446  10.564  41.449  1.00 62.62           O  
ANISOU 1195  O   ILE A 154     8294   8323   7178    156   -500    361       O  
ATOM   1196  CB  ILE A 154      42.756  12.076  43.287  1.00 48.59           C  
ANISOU 1196  CB  ILE A 154     6403   6636   5423    186   -165    365       C  
ATOM   1197  CG1 ILE A 154      44.236  11.910  43.623  1.00 53.68           C  
ANISOU 1197  CG1 ILE A 154     7060   7344   5995    168      2    361       C  
ATOM   1198  CG2 ILE A 154      41.934  11.153  44.163  1.00 47.53           C  
ANISOU 1198  CG2 ILE A 154     6127   6534   5398    195   -180    324       C  
ATOM   1199  CD1 ILE A 154      44.641  12.471  44.978  1.00 48.17           C  
ANISOU 1199  CD1 ILE A 154     6232   6685   5387    175     90    353       C  
ATOM   1200  N   ASN A 155      40.377  12.806  41.340  1.00 53.97           N  
ANISOU 1200  N   ASN A 155     7210   7168   6128    205   -561    421       N  
ATOM   1201  CA  ASN A 155      38.934  12.837  41.114  1.00 52.21           C  
ANISOU 1201  CA  ASN A 155     6916   6914   6006    232   -744    423       C  
ATOM   1202  C   ASN A 155      38.523  12.266  39.769  1.00 55.36           C  
ANISOU 1202  C   ASN A 155     7470   7265   6298    187   -889    447       C  
ATOM   1203  O   ASN A 155      37.381  11.848  39.593  1.00 64.89           O  
ANISOU 1203  O   ASN A 155     8607   8469   7580    184  -1035    443       O  
ATOM   1204  CB  ASN A 155      38.386  14.245  41.338  1.00 54.09           C  
ANISOU 1204  CB  ASN A 155     7101   7101   6349    306   -831    443       C  
ATOM   1205  CG  ASN A 155      38.300  14.583  42.806  1.00 57.87           C  
ANISOU 1205  CG  ASN A 155     7386   7636   6967    361   -722    393       C  
ATOM   1206  OD1 ASN A 155      37.864  13.749  43.616  1.00 65.51           O  
ANISOU 1206  OD1 ASN A 155     8194   8686   8011    353   -667    349       O  
ATOM   1207  ND2 ASN A 155      38.742  15.788  43.173  1.00 53.22           N  
ANISOU 1207  ND2 ASN A 155     6826   6999   6397    403   -690    401       N  
ATOM   1208  N   LEU A 156      39.476  12.218  38.839  1.00 53.48           N  
ANISOU 1208  N   LEU A 156     7440   7003   5877    144   -842    470       N  
ATOM   1209  CA  LEU A 156      39.276  11.543  37.562  1.00 53.55           C  
ANISOU 1209  CA  LEU A 156     7631   6972   5743     93   -950    480       C  
ATOM   1210  C   LEU A 156      39.283  10.030  37.725  1.00 62.43           C  
ANISOU 1210  C   LEU A 156     8743   8129   6848     66   -905    419       C  
ATOM   1211  O   LEU A 156      38.822   9.295  36.834  1.00 62.09           O  
ANISOU 1211  O   LEU A 156     8827   8045   6720     23  -1027    411       O  
ATOM   1212  CB  LEU A 156      40.330  11.963  36.542  1.00 60.63           C  
ANISOU 1212  CB  LEU A 156     8755   7850   6431     52   -889    516       C  
ATOM   1213  CG  LEU A 156      40.343  13.443  36.134  1.00 74.74           C  
ANISOU 1213  CG  LEU A 156    10624   9576   8199     49   -967    595       C  
ATOM   1214  CD1 LEU A 156      41.064  13.614  34.806  1.00 74.18           C  
ANISOU 1214  CD1 LEU A 156    10815   9486   7885    -28   -959    641       C  
ATOM   1215  CD2 LEU A 156      38.933  14.052  36.047  1.00 78.12           C  
ANISOU 1215  CD2 LEU A 156    10990   9926   8764     96  -1206    627       C  
ATOM   1216  N   HIS A 157      39.796   9.572  38.870  1.00 61.34           N  
ANISOU 1216  N   HIS A 157     8470   8053   6784     86   -747    379       N  
ATOM   1217  CA  HIS A 157      39.900   8.139  39.152  1.00 64.71           C  
ANISOU 1217  CA  HIS A 157     8897   8493   7197     63   -703    325       C  
ATOM   1218  C   HIS A 157      39.073   7.672  40.352  1.00 65.20           C  
ANISOU 1218  C   HIS A 157     8748   8592   7434     51   -719    311       C  
ATOM   1219  O   HIS A 157      39.487   6.778  41.088  1.00 62.90           O  
ANISOU 1219  O   HIS A 157     8417   8324   7157     41   -622    278       O  
ATOM   1220  CB  HIS A 157      41.357   7.740  39.352  1.00 65.13           C  
ANISOU 1220  CB  HIS A 157     9009   8585   7153     91   -504    290       C  
ATOM   1221  CG  HIS A 157      42.225   8.013  38.165  1.00 61.41           C  
ANISOU 1221  CG  HIS A 157     8737   8106   6490     90   -458    295       C  
ATOM   1222  ND1 HIS A 157      42.702   7.014  37.352  1.00 67.46           N  
ANISOU 1222  ND1 HIS A 157     9675   8854   7102     93   -432    244       N  
ATOM   1223  CD2 HIS A 157      42.709   9.173  37.667  1.00 65.79           C  
ANISOU 1223  CD2 HIS A 157     9353   8674   6972     80   -428    346       C  
ATOM   1224  CE1 HIS A 157      43.448   7.544  36.396  1.00 64.73           C  
ANISOU 1224  CE1 HIS A 157     9475   8531   6590     85   -371    258       C  
ATOM   1225  NE2 HIS A 157      43.462   8.850  36.562  1.00 67.74           N  
ANISOU 1225  NE2 HIS A 157     9794   8928   7015     65   -372    328       N  
ATOM   1226  N   ASP A 158      37.905   8.277  40.527  1.00 66.28           N  
ANISOU 1226  N   ASP A 158     8750   8737   7697     51   -845    338       N  
ATOM   1227  CA  ASP A 158      36.948   7.871  41.549  1.00 59.93           C  
ANISOU 1227  CA  ASP A 158     7731   7990   7049     24   -869    327       C  
ATOM   1228  C   ASP A 158      37.349   8.401  42.908  1.00 58.97           C  
ANISOU 1228  C   ASP A 158     7446   7939   7021     69   -708    312       C  
ATOM   1229  O   ASP A 158      36.873   7.902  43.931  1.00 56.86           O  
ANISOU 1229  O   ASP A 158     7020   7736   6849     36   -668    297       O  
ATOM   1230  CB  ASP A 158      36.810   6.357  41.624  1.00 63.62           C  
ANISOU 1230  CB  ASP A 158     8242   8446   7486    -61   -888    306       C  
ATOM   1231  CG  ASP A 158      36.598   5.731  40.284  1.00 89.42           C  
ANISOU 1231  CG  ASP A 158    11714  11629  10631   -109  -1035    306       C  
ATOM   1232  OD1 ASP A 158      37.122   4.610  40.079  1.00 97.30           O  
ANISOU 1232  OD1 ASP A 158    12859  12580  11533   -142  -1006    273       O  
ATOM   1233  OD2 ASP A 158      35.918   6.358  39.437  1.00103.19           O  
ANISOU 1233  OD2 ASP A 158    13487  13348  12371   -107  -1188    337       O  
ATOM   1234  N   GLY A 159      38.222   9.405  42.920  1.00 56.18           N  
ANISOU 1234  N   GLY A 159     7141   7574   6629    130   -619    319       N  
ATOM   1235  CA  GLY A 159      38.680   9.967  44.173  1.00 50.15           C  
ANISOU 1235  CA  GLY A 159     6250   6866   5937    167   -476    302       C  
ATOM   1236  C   GLY A 159      39.613   9.023  44.919  1.00 52.35           C  
ANISOU 1236  C   GLY A 159     6534   7182   6175    136   -331    280       C  
ATOM   1237  O   GLY A 159      40.192   8.087  44.355  1.00 55.49           O  
ANISOU 1237  O   GLY A 159     7063   7550   6471    111   -319    274       O  
ATOM   1238  N   TRP A 160      39.756   9.269  46.213  1.00 49.46           N  
ANISOU 1238  N   TRP A 160     6032   6877   5885    147   -226    264       N  
ATOM   1239  CA  TRP A 160      40.668   8.492  47.047  1.00 38.30           C  
ANISOU 1239  CA  TRP A 160     4617   5497   4441    124   -101    251       C  
ATOM   1240  C   TRP A 160      40.332   7.019  47.026  1.00 44.68           C  
ANISOU 1240  C   TRP A 160     5453   6291   5232     62   -144    247       C  
ATOM   1241  O   TRP A 160      41.190   6.194  47.285  1.00 44.20           O  
ANISOU 1241  O   TRP A 160     5459   6220   5116     57    -78    240       O  
ATOM   1242  CB  TRP A 160      40.640   9.017  48.475  1.00 31.20           C  
ANISOU 1242  CB  TRP A 160     3568   4665   3623    132     -7    236       C  
ATOM   1243  CG  TRP A 160      41.525  10.192  48.675  1.00 41.32           C  
ANISOU 1243  CG  TRP A 160     4871   5943   4886    179     67    237       C  
ATOM   1244  CD1 TRP A 160      41.168  11.430  49.148  1.00 44.09           C  
ANISOU 1244  CD1 TRP A 160     5151   6298   5304    222     69    222       C  
ATOM   1245  CD2 TRP A 160      42.940  10.248  48.423  1.00 35.23           C  
ANISOU 1245  CD2 TRP A 160     4199   5164   4024    183    146    251       C  
ATOM   1246  NE1 TRP A 160      42.278  12.243  49.220  1.00 46.70           N  
ANISOU 1246  NE1 TRP A 160     5549   6610   5586    233    135    233       N  
ATOM   1247  CE2 TRP A 160      43.376  11.545  48.771  1.00 46.22           C  
ANISOU 1247  CE2 TRP A 160     5578   6554   5430    203    186    255       C  
ATOM   1248  CE3 TRP A 160      43.880   9.315  47.958  1.00 34.59           C  
ANISOU 1248  CE3 TRP A 160     4209   5080   3852    175    187    255       C  
ATOM   1249  CZ2 TRP A 160      44.721  11.947  48.646  1.00 46.76           C  
ANISOU 1249  CZ2 TRP A 160     5711   6631   5424    190    263    277       C  
ATOM   1250  CZ3 TRP A 160      45.201   9.698  47.848  1.00 39.63           C  
ANISOU 1250  CZ3 TRP A 160     4892   5742   4424    186    276    266       C  
ATOM   1251  CH2 TRP A 160      45.614  11.013  48.181  1.00 43.84           C  
ANISOU 1251  CH2 TRP A 160     5398   6286   4972    181    313    283       C  
ATOM   1252  N   SER A 161      39.081   6.693  46.713  1.00 53.52           N  
ANISOU 1252  N   SER A 161     6526   7407   6404     14   -267    255       N  
ATOM   1253  CA  SER A 161      38.656   5.293  46.649  1.00 50.11           C  
ANISOU 1253  CA  SER A 161     6138   6947   5955    -73   -334    258       C  
ATOM   1254  C   SER A 161      39.265   4.551  45.480  1.00 50.74           C  
ANISOU 1254  C   SER A 161     6437   6931   5910    -64   -384    247       C  
ATOM   1255  O   SER A 161      39.161   3.340  45.417  1.00 54.31           O  
ANISOU 1255  O   SER A 161     6973   7332   6330   -122   -434    241       O  
ATOM   1256  CB  SER A 161      37.136   5.181  46.556  1.00 45.31           C  
ANISOU 1256  CB  SER A 161     5408   6372   5435   -145   -463    274       C  
ATOM   1257  OG  SER A 161      36.523   5.752  47.685  1.00 53.30           O  
ANISOU 1257  OG  SER A 161     6204   7490   6557   -148   -400    272       O  
ATOM   1258  N   GLY A 162      39.872   5.280  44.546  1.00 54.91           N  
ANISOU 1258  N   GLY A 162     7070   7434   6360      4   -373    242       N  
ATOM   1259  CA  GLY A 162      40.619   4.669  43.460  1.00 54.72           C  
ANISOU 1259  CA  GLY A 162     7256   7340   6194     28   -382    218       C  
ATOM   1260  C   GLY A 162      41.540   3.591  43.998  1.00 56.20           C  
ANISOU 1260  C   GLY A 162     7499   7510   6344     48   -291    187       C  
ATOM   1261  O   GLY A 162      41.672   2.497  43.423  1.00 59.38           O  
ANISOU 1261  O   GLY A 162     8058   7836   6669     43   -343    154       O  
ATOM   1262  N   LEU A 163      42.156   3.901  45.133  1.00 42.66           N  
ANISOU 1262  N   LEU A 163     5664   5859   4687     74   -170    194       N  
ATOM   1263  CA  LEU A 163      43.107   2.999  45.770  1.00 51.70           C  
ANISOU 1263  CA  LEU A 163     6842   6992   5810    108    -89    173       C  
ATOM   1264  C   LEU A 163      42.526   1.585  45.988  1.00 51.12           C  
ANISOU 1264  C   LEU A 163     6840   6838   5746     43   -187    168       C  
ATOM   1265  O   LEU A 163      43.220   0.572  45.839  1.00 48.12           O  
ANISOU 1265  O   LEU A 163     6592   6388   5305     89   -182    134       O  
ATOM   1266  CB  LEU A 163      43.600   3.619  47.089  1.00 41.96           C  
ANISOU 1266  CB  LEU A 163     5451   5841   4649    118     23    194       C  
ATOM   1267  CG  LEU A 163      44.470   4.865  46.927  1.00 49.38           C  
ANISOU 1267  CG  LEU A 163     6354   6844   5565    175    122    198       C  
ATOM   1268  CD1 LEU A 163      44.470   5.677  48.205  1.00 49.38           C  
ANISOU 1268  CD1 LEU A 163     6198   6913   5651    156    187    220       C  
ATOM   1269  CD2 LEU A 163      45.909   4.502  46.477  1.00 46.96           C  
ANISOU 1269  CD2 LEU A 163     6133   6546   5165    255    212    170       C  
ATOM   1270  N   ILE A 164      41.252   1.525  46.346  1.00 44.70           N  
ANISOU 1270  N   ILE A 164     5938   6036   5011    -65   -277    201       N  
ATOM   1271  CA  ILE A 164      40.636   0.250  46.654  1.00 53.01           C  
ANISOU 1271  CA  ILE A 164     7046   7020   6077   -164   -374    213       C  
ATOM   1272  C   ILE A 164      40.775  -0.676  45.446  1.00 61.43           C  
ANISOU 1272  C   ILE A 164     8344   7957   7038   -147   -475    172       C  
ATOM   1273  O   ILE A 164      41.402  -1.736  45.520  1.00 64.02           O  
ANISOU 1273  O   ILE A 164     8817   8193   7316   -116   -481    143       O  
ATOM   1274  CB  ILE A 164      39.172   0.432  47.051  1.00 50.82           C  
ANISOU 1274  CB  ILE A 164     6613   6802   5894   -296   -456    257       C  
ATOM   1275  CG1 ILE A 164      39.091   1.270  48.334  1.00 47.92           C  
ANISOU 1275  CG1 ILE A 164     6032   6562   5615   -299   -338    280       C  
ATOM   1276  CG2 ILE A 164      38.512  -0.922  47.228  1.00 39.91           C  
ANISOU 1276  CG2 ILE A 164     5308   5344   4511   -433   -572    281       C  
ATOM   1277  CD1 ILE A 164      37.692   1.652  48.733  1.00 54.87           C  
ANISOU 1277  CD1 ILE A 164     6719   7536   6593   -396   -385    308       C  
ATOM   1278  N   GLU A 165      40.228  -0.247  44.317  1.00 61.18           N  
ANISOU 1278  N   GLU A 165     8364   7915   6968   -156   -559    163       N  
ATOM   1279  CA  GLU A 165      40.346  -1.008  43.083  1.00 67.61           C  
ANISOU 1279  CA  GLU A 165     9416   8611   7660   -140   -653    114       C  
ATOM   1280  C   GLU A 165      41.796  -1.128  42.602  1.00 59.22           C  
ANISOU 1280  C   GLU A 165     8493   7525   6484     12   -532     48       C  
ATOM   1281  O   GLU A 165      42.224  -2.203  42.215  1.00 62.40           O  
ANISOU 1281  O   GLU A 165     9084   7820   6806     54   -564     -9       O  
ATOM   1282  CB  GLU A 165      39.484  -0.373  42.001  1.00 81.22           C  
ANISOU 1282  CB  GLU A 165    11159  10341   9358   -183   -770    127       C  
ATOM   1283  CG  GLU A 165      39.093  -1.312  40.880  1.00100.15           C  
ANISOU 1283  CG  GLU A 165    13792  12612  11648   -233   -929     90       C  
ATOM   1284  CD  GLU A 165      38.046  -0.686  39.960  1.00117.42           C  
ANISOU 1284  CD  GLU A 165    15971  14814  13831   -302  -1081    122       C  
ATOM   1285  OE1 GLU A 165      37.668  -1.319  38.947  1.00121.06           O  
ANISOU 1285  OE1 GLU A 165    16630  15175  14192   -353  -1229     95       O  
ATOM   1286  OE2 GLU A 165      37.599   0.449  40.253  1.00124.37           O  
ANISOU 1286  OE2 GLU A 165    16652  15797  14806   -299  -1063    170       O  
ATOM   1287  N   PHE A 166      42.550  -0.034  42.620  1.00 52.01           N  
ANISOU 1287  N   PHE A 166     7484   6713   5563     95   -395     52       N  
ATOM   1288  CA  PHE A 166      43.950  -0.096  42.200  1.00 50.90           C  
ANISOU 1288  CA  PHE A 166     7434   6586   5320    229   -263     -6       C  
ATOM   1289  C   PHE A 166      44.639  -1.321  42.783  1.00 56.54           C  
ANISOU 1289  C   PHE A 166     8216   7230   6035    295   -239    -49       C  
ATOM   1290  O   PHE A 166      45.505  -1.934  42.152  1.00 63.88           O  
ANISOU 1290  O   PHE A 166     9294   8117   6863    409   -194   -125       O  
ATOM   1291  CB  PHE A 166      44.706   1.160  42.629  1.00 47.85           C  
ANISOU 1291  CB  PHE A 166     6886   6330   4966    276   -113     25       C  
ATOM   1292  CG  PHE A 166      46.176   1.130  42.295  1.00 54.57           C  
ANISOU 1292  CG  PHE A 166     7781   7229   5724    399     34    -26       C  
ATOM   1293  CD1 PHE A 166      46.605   1.091  40.974  1.00 50.12           C  
ANISOU 1293  CD1 PHE A 166     7376   6659   5006    450     61    -78       C  
ATOM   1294  CD2 PHE A 166      47.135   1.137  43.303  1.00 56.16           C  
ANISOU 1294  CD2 PHE A 166     7858   7495   5985    460    148    -22       C  
ATOM   1295  CE1 PHE A 166      47.972   1.058  40.664  1.00 56.55           C  
ANISOU 1295  CE1 PHE A 166     8204   7548   5733    565    216   -130       C  
ATOM   1296  CE2 PHE A 166      48.505   1.116  43.000  1.00 53.41           C  
ANISOU 1296  CE2 PHE A 166     7515   7215   5562    576    285    -68       C  
ATOM   1297  CZ  PHE A 166      48.922   1.068  41.678  1.00 56.65           C  
ANISOU 1297  CZ  PHE A 166     8065   7636   5825    630    327   -125       C  
ATOM   1298  N   SER A 167      44.225  -1.682  43.988  1.00 52.30           N  
ANISOU 1298  N   SER A 167     7577   6682   5610    226   -272     -1       N  
ATOM   1299  CA  SER A 167      44.901  -2.698  44.776  1.00 56.38           C  
ANISOU 1299  CA  SER A 167     8138   7136   6147    282   -256    -19       C  
ATOM   1300  C   SER A 167      44.303  -4.100  44.662  1.00 56.65           C  
ANISOU 1300  C   SER A 167     8361   7001   6161    221   -413    -36       C  
ATOM   1301  O   SER A 167      44.870  -5.029  45.212  1.00 60.55           O  
ANISOU 1301  O   SER A 167     8934   7411   6663    278   -425    -54       O  
ATOM   1302  CB  SER A 167      44.896  -2.278  46.246  1.00 52.11           C  
ANISOU 1302  CB  SER A 167     7398   6680   5721    230   -200     51       C  
ATOM   1303  OG  SER A 167      43.564  -2.178  46.717  1.00 46.25           O  
ANISOU 1303  OG  SER A 167     6575   5948   5052     67   -288    112       O  
ATOM   1304  N   GLY A 168      43.156  -4.241  43.992  1.00 53.71           N  
ANISOU 1304  N   GLY A 168     8062   6575   5770     99   -548    -24       N  
ATOM   1305  CA  GLY A 168      42.471  -5.522  43.868  1.00 53.81           C  
ANISOU 1305  CA  GLY A 168     8258   6423   5764      2   -719    -30       C  
ATOM   1306  C   GLY A 168      41.577  -5.906  45.038  1.00 67.95           C  
ANISOU 1306  C   GLY A 168     9946   8211   7662   -176   -796     62       C  
ATOM   1307  O   GLY A 168      40.846  -5.085  45.616  1.00 76.71           O  
ANISOU 1307  O   GLY A 168    10835   9453   8858   -280   -769    131       O  
TER    1308      GLY A 168                                                      
ATOM   1309  N   SER B   3      67.460  18.914  41.370  1.00114.71           N  
ANISOU 1309  N   SER B   3    13294  18276  12017    455   2264   1760       N  
ATOM   1310  CA  SER B   3      68.189  19.328  42.569  1.00113.89           C  
ANISOU 1310  CA  SER B   3    13026  18220  12028    506   2318   1784       C  
ATOM   1311  C   SER B   3      68.460  18.144  43.483  1.00109.12           C  
ANISOU 1311  C   SER B   3    12364  17588  11511    669   2379   1691       C  
ATOM   1312  O   SER B   3      68.127  17.007  43.149  1.00106.62           O  
ANISOU 1312  O   SER B   3    12135  17218  11159    740   2382   1608       O  
ATOM   1313  CB  SER B   3      67.434  20.420  43.341  1.00113.51           C  
ANISOU 1313  CB  SER B   3    12923  18086  12119    435   2196   1892       C  
ATOM   1314  OG  SER B   3      66.282  19.912  44.000  1.00109.49           O  
ANISOU 1314  OG  SER B   3    12444  17418  11741    486   2088   1884       O  
ATOM   1315  N   THR B   4      69.058  18.422  44.638  1.00109.15           N  
ANISOU 1315  N   THR B   4    12220  17625  11629    728   2424   1706       N  
ATOM   1316  CA  THR B   4      69.420  17.378  45.600  1.00115.63           C  
ANISOU 1316  CA  THR B   4    12968  18427  12538    885   2489   1622       C  
ATOM   1317  C   THR B   4      68.206  16.570  46.112  1.00116.50           C  
ANISOU 1317  C   THR B   4    13138  18366  12762    949   2385   1595       C  
ATOM   1318  O   THR B   4      68.182  15.334  46.053  1.00116.43           O  
ANISOU 1318  O   THR B   4    13179  18325  12736   1050   2421   1500       O  
ATOM   1319  CB  THR B   4      70.206  17.973  46.799  1.00140.49           C  
ANISOU 1319  CB  THR B   4    15944  21636  15800    926   2542   1656       C  
ATOM   1320  OG1 THR B   4      69.565  19.178  47.239  1.00143.58           O  
ANISOU 1320  OG1 THR B   4    16298  21969  16287    830   2431   1769       O  
ATOM   1321  CG2 THR B   4      71.639  18.294  46.403  1.00135.11           C  
ANISOU 1321  CG2 THR B   4    15195  21137  15005    915   2683   1643       C  
ATOM   1322  N   MET B   5      67.199  17.275  46.616  1.00106.95           N  
ANISOU 1322  N   MET B   5    11922  17048  11668    888   2254   1679       N  
ATOM   1323  CA  MET B   5      66.007  16.619  47.133  1.00100.68           C  
ANISOU 1323  CA  MET B   5    11176  16092  10987    939   2148   1665       C  
ATOM   1324  C   MET B   5      65.089  16.101  46.018  1.00 93.16           C  
ANISOU 1324  C   MET B   5    10394  15063   9941    889   2076   1640       C  
ATOM   1325  O   MET B   5      64.449  15.061  46.167  1.00 91.25           O  
ANISOU 1325  O   MET B   5    10212  14720   9739    965   2041   1581       O  
ATOM   1326  CB  MET B   5      65.267  17.561  48.081  1.00100.63           C  
ANISOU 1326  CB  MET B   5    11099  16002  11136    896   2035   1764       C  
ATOM   1327  CG  MET B   5      65.986  17.746  49.414  1.00 97.38           C  
ANISOU 1327  CG  MET B   5    10520  15630  10850    982   2095   1769       C  
ATOM   1328  SD  MET B   5      66.350  16.154  50.197  1.00 92.58           S  
ANISOU 1328  SD  MET B   5     9875  14996  10305   1171   2181   1648       S  
ATOM   1329  CE  MET B   5      67.282  16.677  51.637  1.00 90.70           C  
ANISOU 1329  CE  MET B   5     9437  14826  10198   1244   2250   1672       C  
ATOM   1330  N   GLY B   6      65.037  16.832  44.907  1.00 85.06           N  
ANISOU 1330  N   GLY B   6     9445  14085   8789    763   2054   1687       N  
ATOM   1331  CA  GLY B   6      64.359  16.375  43.712  1.00 75.31           C  
ANISOU 1331  CA  GLY B   6     8371  12803   7440    713   2005   1659       C  
ATOM   1332  C   GLY B   6      64.791  14.972  43.347  1.00 75.30           C  
ANISOU 1332  C   GLY B   6     8424  12822   7363    824   2094   1537       C  
ATOM   1333  O   GLY B   6      63.972  14.136  42.977  1.00 72.16           O  
ANISOU 1333  O   GLY B   6     8138  12325   6955    848   2034   1491       O  
ATOM   1334  N   GLN B   7      66.088  14.706  43.464  1.00 85.77           N  
ANISOU 1334  N   GLN B   7     9672  14280   8638    894   2236   1484       N  
ATOM   1335  CA  GLN B   7      66.632  13.390  43.127  1.00 93.07           C  
ANISOU 1335  CA  GLN B   7    10641  15239   9483   1005   2332   1364       C  
ATOM   1336  C   GLN B   7      65.914  12.320  43.913  1.00 86.03           C  
ANISOU 1336  C   GLN B   7     9763  14211   8713   1116   2282   1310       C  
ATOM   1337  O   GLN B   7      65.366  11.384  43.344  1.00 84.71           O  
ANISOU 1337  O   GLN B   7     9713  13974   8497   1146   2251   1247       O  
ATOM   1338  CB  GLN B   7      68.124  13.325  43.437  1.00111.87           C  
ANISOU 1338  CB  GLN B   7    12906  17775  11825   1076   2488   1322       C  
ATOM   1339  CG  GLN B   7      68.951  14.414  42.779  1.00131.13           C  
ANISOU 1339  CG  GLN B   7    15311  20360  14151    972   2548   1380       C  
ATOM   1340  CD  GLN B   7      70.245  14.686  43.528  1.00144.41           C  
ANISOU 1340  CD  GLN B   7    16837  22171  15863   1029   2671   1374       C  
ATOM   1341  OE1 GLN B   7      70.699  13.863  44.330  1.00149.63           O  
ANISOU 1341  OE1 GLN B   7    17430  22833  16590   1161   2737   1303       O  
ATOM   1342  NE2 GLN B   7      70.845  15.848  43.273  1.00146.00           N  
ANISOU 1342  NE2 GLN B   7    16980  22480  16014    930   2701   1449       N  
ATOM   1343  N   VAL B   8      65.937  12.477  45.232  1.00 79.55           N  
ANISOU 1343  N   VAL B   8     8819  13355   8052   1175   2274   1335       N  
ATOM   1344  CA  VAL B   8      65.188  11.635  46.157  1.00 74.34           C  
ANISOU 1344  CA  VAL B   8     8153  12560   7534   1271   2214   1302       C  
ATOM   1345  C   VAL B   8      63.785  11.262  45.646  1.00 74.36           C  
ANISOU 1345  C   VAL B   8     8295  12415   7542   1226   2080   1309       C  
ATOM   1346  O   VAL B   8      63.417  10.080  45.628  1.00 71.06           O  
ANISOU 1346  O   VAL B   8     7945  11921   7132   1309   2072   1231       O  
ATOM   1347  CB  VAL B   8      65.035  12.350  47.504  1.00 78.61           C  
ANISOU 1347  CB  VAL B   8     8557  13064   8249   1283   2173   1375       C  
ATOM   1348  CG1 VAL B   8      64.730  11.353  48.593  1.00 75.17           C  
ANISOU 1348  CG1 VAL B   8     8079  12533   7949   1416   2165   1322       C  
ATOM   1349  CG2 VAL B   8      66.290  13.146  47.832  1.00 77.79           C  
ANISOU 1349  CG2 VAL B   8     8320  13107   8128   1277   2280   1402       C  
ATOM   1350  N   GLY B   9      63.014  12.271  45.234  1.00 68.12           N  
ANISOU 1350  N   GLY B   9     7548  11586   6748   1095   1975   1402       N  
ATOM   1351  CA  GLY B   9      61.668  12.054  44.728  1.00 73.77           C  
ANISOU 1351  CA  GLY B   9     8394  12168   7468   1039   1842   1418       C  
ATOM   1352  C   GLY B   9      61.556  11.058  43.577  1.00 76.59           C  
ANISOU 1352  C   GLY B   9     8897  12516   7687   1054   1860   1333       C  
ATOM   1353  O   GLY B   9      60.535  10.363  43.419  1.00 70.78           O  
ANISOU 1353  O   GLY B   9     8259  11654   6979   1066   1770   1308       O  
ATOM   1354  N   ARG B  10      62.598  10.982  42.754  1.00 69.16           N  
ANISOU 1354  N   ARG B  10     7974  11710   6596   1053   1973   1287       N  
ATOM   1355  CA  ARG B  10      62.554  10.084  41.605  1.00 66.72           C  
ANISOU 1355  CA  ARG B  10     7804  11402   6144   1066   1994   1206       C  
ATOM   1356  C   ARG B  10      63.000   8.668  41.974  1.00 72.41           C  
ANISOU 1356  C   ARG B  10     8522  12114   6877   1219   2071   1090       C  
ATOM   1357  O   ARG B  10      62.535   7.692  41.364  1.00 74.21           O  
ANISOU 1357  O   ARG B  10     8870  12277   7049   1252   2044   1021       O  
ATOM   1358  CB  ARG B  10      63.359  10.657  40.452  1.00 62.40           C  
ANISOU 1358  CB  ARG B  10     7291  10999   5420    987   2069   1213       C  
ATOM   1359  CG  ARG B  10      63.327  12.176  40.414  1.00 85.42           C  
ANISOU 1359  CG  ARG B  10    10154  13959   8343    856   2029   1330       C  
ATOM   1360  CD  ARG B  10      64.192  12.745  39.279  1.00104.31           C  
ANISOU 1360  CD  ARG B  10    12575  16502  10557    779   2110   1338       C  
ATOM   1361  NE  ARG B  10      64.478  14.169  39.464  1.00113.70           N  
ANISOU 1361  NE  ARG B  10    13679  17758  11765    675   2103   1444       N  
ATOM   1362  CZ  ARG B  10      65.349  14.865  38.739  1.00120.72           C  
ANISOU 1362  CZ  ARG B  10    14553  18788  12526    605   2180   1470       C  
ATOM   1363  NH1 ARG B  10      66.033  14.275  37.766  1.00122.31           N  
ANISOU 1363  NH1 ARG B  10    14819  19085  12568    629   2273   1397       N  
ATOM   1364  NH2 ARG B  10      65.538  16.154  38.993  1.00124.51           N  
ANISOU 1364  NH2 ARG B  10    14954  19315  13038    512   2162   1569       N  
ATOM   1365  N   GLN B  11      63.882   8.551  42.977  1.00 66.00           N  
ANISOU 1365  N   GLN B  11     7575  11363   6139   1312   2164   1069       N  
ATOM   1366  CA  GLN B  11      64.193   7.233  43.552  1.00 74.60           C  
ANISOU 1366  CA  GLN B  11     8649  12424   7272   1463   2223    967       C  
ATOM   1367  C   GLN B  11      62.916   6.621  44.110  1.00 79.66           C  
ANISOU 1367  C   GLN B  11     9338  12886   8042   1494   2101    967       C  
ATOM   1368  O   GLN B  11      62.621   5.444  43.890  1.00 84.91           O  
ANISOU 1368  O   GLN B  11    10089  13485   8689   1568   2093    885       O  
ATOM   1369  CB  GLN B  11      65.235   7.313  44.668  1.00 84.06           C  
ANISOU 1369  CB  GLN B  11     9685  13703   8549   1554   2327    956       C  
ATOM   1370  CG  GLN B  11      66.687   7.218  44.215  1.00 98.05           C  
ANISOU 1370  CG  GLN B  11    11417  15649  10190   1593   2482    898       C  
ATOM   1371  CD  GLN B  11      67.393   8.571  44.210  1.00107.74           C  
ANISOU 1371  CD  GLN B  11    12545  16999  11390   1504   2527    981       C  
ATOM   1372  OE1 GLN B  11      66.763   9.620  44.388  1.00114.62           O  
ANISOU 1372  OE1 GLN B  11    13396  17828  12325   1400   2436   1083       O  
ATOM   1373  NE2 GLN B  11      68.711   8.549  44.011  1.00103.51           N  
ANISOU 1373  NE2 GLN B  11    11949  16619  10760   1544   2666    938       N  
ATOM   1374  N   LEU B  12      62.168   7.444  44.842  1.00 77.42           N  
ANISOU 1374  N   LEU B  12     8997  12529   7890   1436   2004   1062       N  
ATOM   1375  CA  LEU B  12      60.860   7.076  45.351  1.00 71.03           C  
ANISOU 1375  CA  LEU B  12     8228  11553   7206   1443   1874   1083       C  
ATOM   1376  C   LEU B  12      59.941   6.779  44.172  1.00 70.01           C  
ANISOU 1376  C   LEU B  12     8267  11350   6982   1370   1786   1072       C  
ATOM   1377  O   LEU B  12      59.172   5.817  44.196  1.00 73.16           O  
ANISOU 1377  O   LEU B  12     8745  11634   7419   1418   1725   1026       O  
ATOM   1378  CB  LEU B  12      60.297   8.217  46.205  1.00 67.95           C  
ANISOU 1378  CB  LEU B  12     7746  11121   6952   1377   1789   1197       C  
ATOM   1379  CG  LEU B  12      61.045   8.603  47.488  1.00 63.52           C  
ANISOU 1379  CG  LEU B  12     7013  10615   6507   1444   1855   1220       C  
ATOM   1380  CD1 LEU B  12      60.578   9.939  48.015  1.00 57.44           C  
ANISOU 1380  CD1 LEU B  12     6169   9827   5829   1351   1773   1338       C  
ATOM   1381  CD2 LEU B  12      60.906   7.531  48.550  1.00 61.00           C  
ANISOU 1381  CD2 LEU B  12     6648  10216   6313   1581   1864   1162       C  
ATOM   1382  N   ALA B  13      60.046   7.594  43.126  1.00 65.85           N  
ANISOU 1382  N   ALA B  13     7796  10894   6331   1255   1782   1113       N  
ATOM   1383  CA  ALA B  13      59.211   7.407  41.941  1.00 66.09           C  
ANISOU 1383  CA  ALA B  13     7986  10863   6261   1179   1700   1107       C  
ATOM   1384  C   ALA B  13      59.408   6.069  41.256  1.00 66.27           C  
ANISOU 1384  C   ALA B  13     8115  10878   6185   1260   1748    991       C  
ATOM   1385  O   ALA B  13      58.450   5.519  40.724  1.00 72.12           O  
ANISOU 1385  O   ALA B  13     8980  11513   6911   1241   1658    970       O  
ATOM   1386  CB  ALA B  13      59.387   8.528  40.957  1.00 57.16           C  
ANISOU 1386  CB  ALA B  13     6890   9819   5009   1046   1697   1170       C  
ATOM   1387  N   ILE B  14      60.617   5.519  41.256  1.00 58.86           N  
ANISOU 1387  N   ILE B  14     7134  10050   5180   1352   1885    913       N  
ATOM   1388  CA  ILE B  14      60.762   4.245  40.540  1.00 67.76           C  
ANISOU 1388  CA  ILE B  14     8373  11168   6207   1428   1923    801       C  
ATOM   1389  C   ILE B  14      60.003   3.131  41.240  1.00 66.14           C  
ANISOU 1389  C   ILE B  14     8195  10816   6121   1521   1860    753       C  
ATOM   1390  O   ILE B  14      59.288   2.360  40.591  1.00 74.52           O  
ANISOU 1390  O   ILE B  14     9386  11788   7138   1523   1797    707       O  
ATOM   1391  CB  ILE B  14      62.236   3.807  40.187  1.00 72.62           C  
ANISOU 1391  CB  ILE B  14     8956  11940   6696   1508   2085    716       C  
ATOM   1392  CG1 ILE B  14      62.916   3.133  41.369  1.00 78.60           C  
ANISOU 1392  CG1 ILE B  14     9600  12709   7555   1648   2167    662       C  
ATOM   1393  CG2 ILE B  14      63.068   4.965  39.626  1.00 62.26           C  
ANISOU 1393  CG2 ILE B  14     7597  10782   5278   1418   2154    771       C  
ATOM   1394  CD1 ILE B  14      64.130   2.327  40.978  1.00 82.30           C  
ANISOU 1394  CD1 ILE B  14    10072  13296   7904   1748   2307    556       C  
ATOM   1395  N   ILE B  15      60.141   3.061  42.562  1.00 62.10           N  
ANISOU 1395  N   ILE B  15     7559  10278   5759   1595   1876    765       N  
ATOM   1396  CA  ILE B  15      59.383   2.089  43.351  1.00 64.75           C  
ANISOU 1396  CA  ILE B  15     7907  10472   6225   1679   1812    732       C  
ATOM   1397  C   ILE B  15      57.891   2.259  43.085  1.00 62.98           C  
ANISOU 1397  C   ILE B  15     7777  10104   6049   1590   1653    789       C  
ATOM   1398  O   ILE B  15      57.158   1.273  42.952  1.00 64.69           O  
ANISOU 1398  O   ILE B  15     8087  10207   6285   1629   1590    739       O  
ATOM   1399  CB  ILE B  15      59.655   2.237  44.869  1.00 65.77           C  
ANISOU 1399  CB  ILE B  15     7877  10592   6520   1754   1839    760       C  
ATOM   1400  CG1 ILE B  15      61.140   2.035  45.161  1.00 67.50           C  
ANISOU 1400  CG1 ILE B  15     8001  10953   6693   1847   1997    700       C  
ATOM   1401  CG2 ILE B  15      58.817   1.247  45.666  1.00 48.59           C  
ANISOU 1401  CG2 ILE B  15     5717   8267   4478   1835   1767    731       C  
ATOM   1402  CD1 ILE B  15      61.492   2.054  46.631  1.00 68.60           C  
ANISOU 1402  CD1 ILE B  15     7987  11089   6988   1934   2034    714       C  
ATOM   1403  N   GLY B  16      57.457   3.521  42.997  1.00 61.47           N  
ANISOU 1403  N   GLY B  16     7561   9920   5876   1469   1587    894       N  
ATOM   1404  CA  GLY B  16      56.070   3.853  42.706  1.00 59.62           C  
ANISOU 1404  CA  GLY B  16     7410   9562   5680   1372   1436    957       C  
ATOM   1405  C   GLY B  16      55.601   3.273  41.385  1.00 65.15           C  
ANISOU 1405  C   GLY B  16     8280  10226   6247   1334   1396    906       C  
ATOM   1406  O   GLY B  16      54.521   2.675  41.285  1.00 61.29           O  
ANISOU 1406  O   GLY B  16     7881   9604   5801   1330   1291    896       O  
ATOM   1407  N   ASP B  17      56.440   3.432  40.366  1.00 69.53           N  
ANISOU 1407  N   ASP B  17     8879  10902   6637   1308   1481    873       N  
ATOM   1408  CA  ASP B  17      56.122   2.936  39.040  1.00 68.49           C  
ANISOU 1408  CA  ASP B  17     8906  10754   6363   1272   1454    822       C  
ATOM   1409  C   ASP B  17      56.143   1.407  38.964  1.00 72.06           C  
ANISOU 1409  C   ASP B  17     9432  11148   6800   1390   1477    707       C  
ATOM   1410  O   ASP B  17      55.365   0.817  38.209  1.00 72.47           O  
ANISOU 1410  O   ASP B  17     9620  11114   6802   1370   1401    674       O  
ATOM   1411  CB  ASP B  17      57.039   3.578  38.005  1.00 66.57           C  
ANISOU 1411  CB  ASP B  17     8682  10664   5949   1212   1541    822       C  
ATOM   1412  CG  ASP B  17      56.745   5.061  37.808  1.00 81.60           C  
ANISOU 1412  CG  ASP B  17    10555  12598   7849   1072   1487    938       C  
ATOM   1413  OD1 ASP B  17      57.702   5.842  37.589  1.00 87.92           O  
ANISOU 1413  OD1 ASP B  17    11292  13538   8576   1037   1575    965       O  
ATOM   1414  OD2 ASP B  17      55.553   5.449  37.875  1.00 79.10           O  
ANISOU 1414  OD2 ASP B  17    10280  12169   7605    997   1354   1004       O  
ATOM   1415  N   ASP B  18      57.010   0.766  39.754  1.00 58.50           N  
ANISOU 1415  N   ASP B  18     7626   9474   5127   1514   1577    647       N  
ATOM   1416  CA  ASP B  18      56.988  -0.698  39.856  1.00 57.89           C  
ANISOU 1416  CA  ASP B  18     7608   9329   5057   1634   1592    541       C  
ATOM   1417  C   ASP B  18      55.666  -1.182  40.449  1.00 62.30           C  
ANISOU 1417  C   ASP B  18     8203   9711   5759   1638   1459    562       C  
ATOM   1418  O   ASP B  18      55.061  -2.146  39.962  1.00 65.42           O  
ANISOU 1418  O   ASP B  18     8718  10012   6126   1664   1404    503       O  
ATOM   1419  CB  ASP B  18      58.162  -1.233  40.685  1.00 68.65           C  
ANISOU 1419  CB  ASP B  18     8860  10771   6452   1766   1723    478       C  
ATOM   1420  CG  ASP B  18      59.496  -1.136  39.958  1.00 93.37           C  
ANISOU 1420  CG  ASP B  18    11982  14073   9421   1787   1861    427       C  
ATOM   1421  OD1 ASP B  18      60.535  -0.989  40.640  1.00103.36           O  
ANISOU 1421  OD1 ASP B  18    13124  15438  10711   1852   1970    415       O  
ATOM   1422  OD2 ASP B  18      59.512  -1.204  38.707  1.00 98.65           O  
ANISOU 1422  OD2 ASP B  18    12767  14778   9938   1738   1862    397       O  
ATOM   1423  N   ILE B  19      55.217  -0.501  41.504  1.00 59.66           N  
ANISOU 1423  N   ILE B  19     7762   9331   5576   1613   1407    648       N  
ATOM   1424  CA  ILE B  19      53.949  -0.828  42.137  1.00 62.65           C  
ANISOU 1424  CA  ILE B  19     8159   9548   6096   1610   1279    682       C  
ATOM   1425  C   ILE B  19      52.844  -0.613  41.112  1.00 63.03           C  
ANISOU 1425  C   ILE B  19     8347   9519   6084   1497   1158    713       C  
ATOM   1426  O   ILE B  19      51.988  -1.472  40.883  1.00 66.94           O  
ANISOU 1426  O   ILE B  19     8943   9894   6596   1512   1076    677       O  
ATOM   1427  CB  ILE B  19      53.731   0.033  43.409  1.00 62.55           C  
ANISOU 1427  CB  ILE B  19     8000   9520   6246   1595   1249    776       C  
ATOM   1428  CG1 ILE B  19      54.549  -0.539  44.570  1.00 64.13           C  
ANISOU 1428  CG1 ILE B  19     8080   9750   6538   1730   1344    731       C  
ATOM   1429  CG2 ILE B  19      52.247   0.095  43.794  1.00 52.02           C  
ANISOU 1429  CG2 ILE B  19     6698   8032   5035   1543   1093    840       C  
ATOM   1430  CD1 ILE B  19      54.947   0.484  45.587  1.00 65.55           C  
ANISOU 1430  CD1 ILE B  19     8100   9990   6818   1721   1374    810       C  
ATOM   1431  N   ASN B  20      52.903   0.535  40.463  1.00 59.51           N  
ANISOU 1431  N   ASN B  20     7905   9145   5560   1384   1149    779       N  
ATOM   1432  CA  ASN B  20      51.891   0.903  39.493  1.00 63.82           C  
ANISOU 1432  CA  ASN B  20     8575   9628   6046   1269   1035    819       C  
ATOM   1433  C   ASN B  20      51.744  -0.123  38.363  1.00 64.23           C  
ANISOU 1433  C   ASN B  20     8785   9649   5972   1289   1029    726       C  
ATOM   1434  O   ASN B  20      50.635  -0.535  38.018  1.00 60.63           O  
ANISOU 1434  O   ASN B  20     8433   9070   5534   1256    915    726       O  
ATOM   1435  CB  ASN B  20      52.203   2.287  38.951  1.00 55.72           C  
ANISOU 1435  CB  ASN B  20     7524   8706   4941   1153   1049    896       C  
ATOM   1436  CG  ASN B  20      51.148   2.783  38.013  1.00 59.16           C  
ANISOU 1436  CG  ASN B  20     8078   9079   5323   1029    929    946       C  
ATOM   1437  OD1 ASN B  20      51.463   3.243  36.923  1.00 65.50           O  
ANISOU 1437  OD1 ASN B  20     8947   9961   5981    959    955    947       O  
ATOM   1438  ND2 ASN B  20      49.884   2.697  38.424  1.00 58.59           N  
ANISOU 1438  ND2 ASN B  20     8031   8865   5364   1001    798    988       N  
ATOM   1439  N   ARG B  21      52.873  -0.548  37.805  1.00 65.33           N  
ANISOU 1439  N   ARG B  21     8940   9900   5983   1348   1151    647       N  
ATOM   1440  CA  ARG B  21      52.884  -1.573  36.764  1.00 70.17           C  
ANISOU 1440  CA  ARG B  21     9697  10496   6469   1383   1159    550       C  
ATOM   1441  C   ARG B  21      52.245  -2.885  37.225  1.00 69.25           C  
ANISOU 1441  C   ARG B  21     9630  10241   6441   1473   1104    486       C  
ATOM   1442  O   ARG B  21      51.423  -3.469  36.519  1.00 72.76           O  
ANISOU 1442  O   ARG B  21    10208  10590   6847   1450   1018    455       O  
ATOM   1443  CB  ARG B  21      54.319  -1.832  36.284  1.00 75.97           C  
ANISOU 1443  CB  ARG B  21    10415  11384   7065   1449   1312    473       C  
ATOM   1444  CG  ARG B  21      54.875  -0.775  35.349  1.00 90.48           C  
ANISOU 1444  CG  ARG B  21    12262  13355   8762   1353   1359    514       C  
ATOM   1445  CD  ARG B  21      56.385  -0.592  35.522  1.00107.32           C  
ANISOU 1445  CD  ARG B  21    14291  15654  10831   1413   1519    483       C  
ATOM   1446  NE  ARG B  21      56.842   0.728  35.060  1.00120.60           N  
ANISOU 1446  NE  ARG B  21    15930  17456  12436   1307   1553    560       N  
ATOM   1447  CZ  ARG B  21      58.051   1.242  35.296  1.00121.64           C  
ANISOU 1447  CZ  ARG B  21    15952  17736  12531   1327   1676    566       C  
ATOM   1448  NH1 ARG B  21      58.953   0.560  35.999  1.00122.02           N  
ANISOU 1448  NH1 ARG B  21    15918  17834  12610   1453   1780    499       N  
ATOM   1449  NH2 ARG B  21      58.361   2.444  34.827  1.00115.26           N  
ANISOU 1449  NH2 ARG B  21    15115  17025  11653   1221   1695    640       N  
ATOM   1450  N   ARG B  22      52.627  -3.347  38.406  1.00 60.62           N  
ANISOU 1450  N   ARG B  22     8432   9136   5467   1576   1152    466       N  
ATOM   1451  CA  ARG B  22      52.164  -4.631  38.886  1.00 66.60           C  
ANISOU 1451  CA  ARG B  22     9228   9772   6305   1671   1113    401       C  
ATOM   1452  C   ARG B  22      50.652  -4.648  39.039  1.00 70.72           C  
ANISOU 1452  C   ARG B  22     9808  10134   6929   1605    954    457       C  
ATOM   1453  O   ARG B  22      49.997  -5.660  38.795  1.00 77.79           O  
ANISOU 1453  O   ARG B  22    10806  10920   7832   1638    890    403       O  
ATOM   1454  CB  ARG B  22      52.835  -4.945  40.215  1.00 77.37           C  
ANISOU 1454  CB  ARG B  22    10453  11158   7788   1783   1192    385       C  
ATOM   1455  CG  ARG B  22      52.134  -6.000  41.061  1.00 91.10           C  
ANISOU 1455  CG  ARG B  22    12198  12752   9664   1864   1128    356       C  
ATOM   1456  CD  ARG B  22      53.074  -6.440  42.186  1.00110.41           C  
ANISOU 1456  CD  ARG B  22    14518  15246  12188   1991   1235    316       C  
ATOM   1457  NE  ARG B  22      52.418  -7.119  43.307  1.00116.85           N  
ANISOU 1457  NE  ARG B  22    15294  15935  13171   2057   1175    320       N  
ATOM   1458  CZ  ARG B  22      53.073  -7.613  44.357  1.00112.10           C  
ANISOU 1458  CZ  ARG B  22    14590  15350  12653   2173   1252    286       C  
ATOM   1459  NH1 ARG B  22      54.396  -7.504  44.425  1.00105.10           N  
ANISOU 1459  NH1 ARG B  22    13631  14603  11701   2235   1390    244       N  
ATOM   1460  NH2 ARG B  22      52.410  -8.216  45.334  1.00112.64           N  
ANISOU 1460  NH2 ARG B  22    14627  15299  12871   2226   1191    294       N  
ATOM   1461  N   TYR B  23      50.096  -3.510  39.433  1.00 67.59           N  
ANISOU 1461  N   TYR B  23     9345   9726   6610   1512    890    566       N  
ATOM   1462  CA  TYR B  23      48.689  -3.462  39.785  1.00 62.40           C  
ANISOU 1462  CA  TYR B  23     8716   8923   6070   1456    742    627       C  
ATOM   1463  C   TYR B  23      47.794  -3.117  38.609  1.00 70.00           C  
ANISOU 1463  C   TYR B  23     9814   9839   6943   1339    640    654       C  
ATOM   1464  O   TYR B  23      46.570  -3.061  38.743  1.00 71.43           O  
ANISOU 1464  O   TYR B  23    10035   9901   7206   1283    511    703       O  
ATOM   1465  CB  TYR B  23      48.456  -2.544  40.999  1.00 59.41           C  
ANISOU 1465  CB  TYR B  23     8191   8538   5845   1433    715    728       C  
ATOM   1466  CG  TYR B  23      48.817  -3.247  42.279  1.00 60.90           C  
ANISOU 1466  CG  TYR B  23     8276   8702   6163   1557    765    697       C  
ATOM   1467  CD1 TYR B  23      47.972  -4.213  42.814  1.00 62.65           C  
ANISOU 1467  CD1 TYR B  23     8529   8784   6492   1608    687    675       C  
ATOM   1468  CD2 TYR B  23      50.029  -2.996  42.926  1.00 62.40           C  
ANISOU 1468  CD2 TYR B  23     8338   9008   6363   1625    893    686       C  
ATOM   1469  CE1 TYR B  23      48.300  -4.889  43.975  1.00 64.57           C  
ANISOU 1469  CE1 TYR B  23     8681   9003   6851   1724    732    646       C  
ATOM   1470  CE2 TYR B  23      50.371  -3.669  44.100  1.00 65.12           C  
ANISOU 1470  CE2 TYR B  23     8589   9328   6825   1743    940    655       C  
ATOM   1471  CZ  TYR B  23      49.500  -4.617  44.614  1.00 70.26           C  
ANISOU 1471  CZ  TYR B  23     9276   9839   7581   1792    859    635       C  
ATOM   1472  OH  TYR B  23      49.809  -5.297  45.769  1.00 76.08           O  
ANISOU 1472  OH  TYR B  23     9924  10550   8435   1908    903    605       O  
ATOM   1473  N   ASP B  24      48.403  -2.905  37.451  1.00 81.58           N  
ANISOU 1473  N   ASP B  24    11353  11403   8241   1304    698    620       N  
ATOM   1474  CA  ASP B  24      47.633  -2.707  36.232  1.00 92.52           C  
ANISOU 1474  CA  ASP B  24    12880  12749   9526   1203    609    631       C  
ATOM   1475  C   ASP B  24      46.877  -3.993  35.862  1.00104.51           C  
ANISOU 1475  C   ASP B  24    14528  14139  11043   1246    536    557       C  
ATOM   1476  O   ASP B  24      47.469  -5.077  35.836  1.00104.06           O  
ANISOU 1476  O   ASP B  24    14498  14089  10951   1353    604    460       O  
ATOM   1477  CB  ASP B  24      48.551  -2.274  35.098  1.00 92.19           C  
ANISOU 1477  CB  ASP B  24    12882  12847   9299   1168    699    604       C  
ATOM   1478  CG  ASP B  24      47.858  -1.377  34.105  1.00100.43           C  
ANISOU 1478  CG  ASP B  24    14010  13885  10262   1030    615    667       C  
ATOM   1479  OD1 ASP B  24      48.122  -0.156  34.142  1.00106.09           O  
ANISOU 1479  OD1 ASP B  24    14657  14684  10969    953    632    747       O  
ATOM   1480  OD2 ASP B  24      47.045  -1.885  33.301  1.00101.54           O  
ANISOU 1480  OD2 ASP B  24    14288  13940  10353    999    528    638       O  
ATOM   1481  N   SER B  25      45.572  -3.860  35.595  1.00111.36           N  
ANISOU 1481  N   SER B  25    15472  14889  11950   1163    395    604       N  
ATOM   1482  CA  SER B  25      44.689  -4.994  35.277  1.00110.44           C  
ANISOU 1482  CA  SER B  25    15479  14636  11847   1189    305    547       C  
ATOM   1483  C   SER B  25      45.227  -5.897  34.173  1.00114.12           C  
ANISOU 1483  C   SER B  25    16070  15135  12156   1238    359    437       C  
ATOM   1484  O   SER B  25      44.755  -7.027  34.006  1.00108.59           O  
ANISOU 1484  O   SER B  25    15461  14332  11465   1289    310    370       O  
ATOM   1485  CB  SER B  25      43.290  -4.511  34.884  1.00104.58           C  
ANISOU 1485  CB  SER B  25    14812  13790  11135   1072    152    618       C  
ATOM   1486  OG  SER B  25      42.429  -4.467  36.008  1.00101.76           O  
ANISOU 1486  OG  SER B  25    14381  13330  10954   1071     67    681       O  
ATOM   1487  N   GLU B  26      46.206  -5.379  33.428  1.00118.94           N  
ANISOU 1487  N   GLU B  26    16682  15886  12622   1221    457    420       N  
ATOM   1488  CA  GLU B  26      46.871  -6.091  32.336  1.00120.03           C  
ANISOU 1488  CA  GLU B  26    16928  16083  12594   1266    524    319       C  
ATOM   1489  C   GLU B  26      46.140  -7.361  31.921  1.00129.70           C  
ANISOU 1489  C   GLU B  26    18289  17178  13814   1309    445    242       C  
ATOM   1490  O   GLU B  26      46.728  -8.442  31.896  1.00134.93           O  
ANISOU 1490  O   GLU B  26    18983  17845  14441   1418    508    143       O  
ATOM   1491  CB  GLU B  26      48.315  -6.423  32.717  1.00111.29           C  
ANISOU 1491  CB  GLU B  26    15736  15100  11450   1377    681    255       C  
ATOM   1492  CG  GLU B  26      48.454  -6.949  34.127  1.00103.51           C  
ANISOU 1492  CG  GLU B  26    14637  14066  10624   1475    705    249       C  
ATOM   1493  CD  GLU B  26      49.690  -7.800  34.314  1.00 99.49           C  
ANISOU 1493  CD  GLU B  26    14097  13639  10067   1609    839    149       C  
ATOM   1494  OE1 GLU B  26      50.373  -7.624  35.354  1.00 98.85           O  
ANISOU 1494  OE1 GLU B  26    13877  13611  10070   1669    918    163       O  
ATOM   1495  OE2 GLU B  26      49.970  -8.643  33.425  1.00 88.86           O  
ANISOU 1495  OE2 GLU B  26    12865  12301   8598   1655    864     55       O  
TER    1496      GLU B  26                                                      
ATOM   1497  N   ASN X   3      36.529  11.159  63.638  1.00102.79           N  
ANISOU 1497  N   ASN X   3    10674  12873  15507   1240   -601   -156       N  
ATOM   1498  CA  ASN X   3      36.191  11.166  62.213  1.00105.96           C  
ANISOU 1498  CA  ASN X   3    11093  13256  15912   1203   -334   -148       C  
ATOM   1499  C   ASN X   3      34.694  11.359  61.965  1.00107.86           C  
ANISOU 1499  C   ASN X   3    11596  13442  15943   1097   -255   -197       C  
ATOM   1500  O   ASN X   3      34.075  10.654  61.156  1.00108.85           O  
ANISOU 1500  O   ASN X   3    11872  13519  15969   1134    -80   -200       O  
ATOM   1501  CB  ASN X   3      36.669   9.883  61.530  1.00103.61           C  
ANISOU 1501  CB  ASN X   3    10793  12934  15640   1379   -173    -99       C  
ATOM   1502  CG  ASN X   3      38.168   9.692  61.624  1.00105.82           C  
ANISOU 1502  CG  ASN X   3    10784  13274  16149   1496   -220    -44       C  
ATOM   1503  OD1 ASN X   3      38.825  10.216  62.529  1.00100.00           O  
ANISOU 1503  OD1 ASN X   3     9880  12590  15526   1476   -437    -46       O  
ATOM   1504  ND2 ASN X   3      38.720   8.930  60.684  1.00114.57           N  
ANISOU 1504  ND2 ASN X   3    11831  14373  17329   1626    -20      2       N  
ATOM   1505  N   THR X   4      34.121  12.325  62.671  1.00106.91           N  
ANISOU 1505  N   THR X   4    11529  13329  15762    969   -392   -241       N  
ATOM   1506  CA  THR X   4      32.702  12.626  62.563  1.00101.17           C  
ANISOU 1506  CA  THR X   4    11024  12560  14854    869   -338   -288       C  
ATOM   1507  C   THR X   4      32.477  13.670  61.475  1.00 85.16           C  
ANISOU 1507  C   THR X   4     8935  10547  12874    747   -206   -301       C  
ATOM   1508  O   THR X   4      33.287  14.590  61.313  1.00 85.77           O  
ANISOU 1508  O   THR X   4     8814  10664  13110    685   -233   -287       O  
ATOM   1509  CB  THR X   4      32.166  13.171  63.897  1.00106.57           C  
ANISOU 1509  CB  THR X   4    11814  13240  15437    808   -539   -325       C  
ATOM   1510  OG1 THR X   4      32.937  14.316  64.282  1.00111.45           O  
ANISOU 1510  OG1 THR X   4    12250  13905  16191    730   -682   -335       O  
ATOM   1511  CG2 THR X   4      32.263  12.110  64.988  1.00106.61           C  
ANISOU 1511  CG2 THR X   4    11931  13218  15359    938   -658   -307       C  
ATOM   1512  N   ALA X   5      31.389  13.518  60.723  1.00 68.52           N  
ANISOU 1512  N   ALA X   5     6998   8403  10634    713    -66   -327       N  
ATOM   1513  CA  ALA X   5      31.026  14.493  59.700  1.00 64.69           C  
ANISOU 1513  CA  ALA X   5     6499   7923  10157    612     53   -341       C  
ATOM   1514  C   ALA X   5      30.157  15.617  60.300  1.00 67.18           C  
ANISOU 1514  C   ALA X   5     6894   8239  10393    481    -54   -387       C  
ATOM   1515  O   ALA X   5      29.360  15.383  61.207  1.00 60.88           O  
ANISOU 1515  O   ALA X   5     6240   7422   9472    476   -152   -419       O  
ATOM   1516  CB  ALA X   5      30.307  13.811  58.553  1.00 59.35           C  
ANISOU 1516  CB  ALA X   5     5967   7208   9375    651    236   -353       C  
ATOM   1517  N   ASP X   6      30.328  16.835  59.791  1.00 65.92           N  
ANISOU 1517  N   ASP X   6     6647   8094  10307    384    -21   -387       N  
ATOM   1518  CA  ASP X   6      29.548  17.997  60.234  1.00 67.86           C  
ANISOU 1518  CA  ASP X   6     6968   8331  10484    267   -104   -430       C  
ATOM   1519  C   ASP X   6      28.068  17.931  59.773  1.00 64.55           C  
ANISOU 1519  C   ASP X   6     6753   7887   9888    246    -22   -469       C  
ATOM   1520  O   ASP X   6      27.710  17.137  58.884  1.00 59.24           O  
ANISOU 1520  O   ASP X   6     6149   7200   9159    303    111   -467       O  
ATOM   1521  CB  ASP X   6      30.218  19.305  59.754  1.00 68.61           C  
ANISOU 1521  CB  ASP X   6     6915   8434  10722    170    -78   -412       C  
ATOM   1522  CG  ASP X   6      30.050  19.545  58.246  1.00 71.98           C  
ANISOU 1522  CG  ASP X   6     7356   8848  11146    164    137   -388       C  
ATOM   1523  OD1 ASP X   6      29.203  18.890  57.607  1.00 80.53           O  
ANISOU 1523  OD1 ASP X   6     8588   9917  12092    217    238   -403       O  
ATOM   1524  OD2 ASP X   6      30.748  20.409  57.690  1.00 73.97           O  
ANISOU 1524  OD2 ASP X   6     7480   9097  11529    105    206   -354       O  
ATOM   1525  N   PHE X   7      27.218  18.772  60.365  1.00 53.31           N  
ANISOU 1525  N   PHE X   7     5422   6454   8380    169   -104   -509       N  
ATOM   1526  CA  PHE X   7      25.785  18.746  60.057  1.00 49.38           C  
ANISOU 1526  CA  PHE X   7     5092   5939   7731    151    -47   -548       C  
ATOM   1527  C   PHE X   7      25.470  18.853  58.553  1.00 52.73           C  
ANISOU 1527  C   PHE X   7     5537   6359   8137    152    114   -546       C  
ATOM   1528  O   PHE X   7      24.611  18.133  58.017  1.00 51.82           O  
ANISOU 1528  O   PHE X   7     5533   6231   7925    186    183   -571       O  
ATOM   1529  CB  PHE X   7      25.048  19.847  60.829  1.00 47.68           C  
ANISOU 1529  CB  PHE X   7     4948   5717   7450     73   -144   -585       C  
ATOM   1530  CG  PHE X   7      23.573  19.677  60.820  1.00 46.51           C  
ANISOU 1530  CG  PHE X   7     4954   5558   7160     69   -109   -624       C  
ATOM   1531  CD1 PHE X   7      22.972  18.831  61.710  1.00 45.63           C  
ANISOU 1531  CD1 PHE X   7     4937   5433   6966    104   -150   -636       C  
ATOM   1532  CD2 PHE X   7      22.793  20.310  59.872  1.00 45.67           C  
ANISOU 1532  CD2 PHE X   7     4892   5451   7007     36    -26   -643       C  
ATOM   1533  CE1 PHE X   7      21.635  18.641  61.678  1.00 50.37           C  
ANISOU 1533  CE1 PHE X   7     5651   6024   7465     93   -105   -668       C  
ATOM   1534  CE2 PHE X   7      21.456  20.113  59.849  1.00 35.15           C  
ANISOU 1534  CE2 PHE X   7     3673   4116   5567     35     -3   -681       C  
ATOM   1535  CZ  PHE X   7      20.879  19.278  60.749  1.00 39.15           C  
ANISOU 1535  CZ  PHE X   7     4249   4611   6014     57    -39   -694       C  
ATOM   1536  N   ARG X   8      26.162  19.758  57.873  1.00 49.49           N  
ANISOU 1536  N   ARG X   8     5030   5954   7820    115    172   -517       N  
ATOM   1537  CA  ARG X   8      25.832  20.046  56.489  1.00 54.87           C  
ANISOU 1537  CA  ARG X   8     5761   6625   8462    120    320   -511       C  
ATOM   1538  C   ARG X   8      26.138  18.862  55.593  1.00 56.00           C  
ANISOU 1538  C   ARG X   8     5917   6763   8598    217    443   -494       C  
ATOM   1539  O   ARG X   8      25.407  18.568  54.647  1.00 57.43           O  
ANISOU 1539  O   ARG X   8     6217   6929   8674    250    530   -518       O  
ATOM   1540  CB  ARG X   8      26.577  21.288  55.992  1.00 55.28           C  
ANISOU 1540  CB  ARG X   8     5715   6668   8621     59    373   -471       C  
ATOM   1541  CG  ARG X   8      26.262  21.599  54.543  1.00 57.32           C  
ANISOU 1541  CG  ARG X   8     6051   6909   8820     82    536   -457       C  
ATOM   1542  CD  ARG X   8      26.294  23.058  54.307  1.00 70.53           C  
ANISOU 1542  CD  ARG X   8     7717   8557  10525      1    555   -439       C  
ATOM   1543  NE  ARG X   8      27.579  23.513  53.807  1.00 91.38           N  
ANISOU 1543  NE  ARG X   8    10211  11181  13327    -21    662   -370       N  
ATOM   1544  CZ  ARG X   8      28.078  24.723  54.049  1.00108.66           C  
ANISOU 1544  CZ  ARG X   8    12319  13339  15627   -120    642   -346       C  
ATOM   1545  NH1 ARG X   8      27.403  25.588  54.807  1.00106.94           N  
ANISOU 1545  NH1 ARG X   8    12171  13104  15359   -194    511   -389       N  
ATOM   1546  NH2 ARG X   8      29.261  25.063  53.550  1.00114.81           N  
ANISOU 1546  NH2 ARG X   8    12947  14100  16575   -146    759   -278       N  
ATOM   1547  N   LEU X   9      27.247  18.200  55.894  1.00 52.56           N  
ANISOU 1547  N   LEU X   9     5360   6337   8274    270    443   -455       N  
ATOM   1548  CA  LEU X   9      27.704  17.050  55.132  1.00 50.12           C  
ANISOU 1548  CA  LEU X   9     5056   6016   7971    378    564   -433       C  
ATOM   1549  C   LEU X   9      26.736  15.874  55.319  1.00 50.30           C  
ANISOU 1549  C   LEU X   9     5238   6012   7862    425    537   -483       C  
ATOM   1550  O   LEU X   9      26.366  15.204  54.355  1.00 48.53           O  
ANISOU 1550  O   LEU X   9     5119   5759   7560    481    641   -502       O  
ATOM   1551  CB  LEU X   9      29.134  16.684  55.555  1.00 47.61           C  
ANISOU 1551  CB  LEU X   9     4549   5718   7821    430    553   -378       C  
ATOM   1552  CG  LEU X   9      29.743  15.465  54.874  1.00 62.30           C  
ANISOU 1552  CG  LEU X   9     6403   7564   9702    561    682   -349       C  
ATOM   1553  CD1 LEU X   9      29.965  15.786  53.418  1.00 59.95           C  
ANISOU 1553  CD1 LEU X   9     6121   7253   9403    588    881   -321       C  
ATOM   1554  CD2 LEU X   9      31.031  15.038  55.567  1.00 68.87           C  
ANISOU 1554  CD2 LEU X   9     7045   8424  10700    622    628   -299       C  
ATOM   1555  N   GLN X  10      26.326  15.652  56.562  1.00 42.79           N  
ANISOU 1555  N   GLN X  10     4312   5063   6885    398    399   -504       N  
ATOM   1556  CA  GLN X  10      25.325  14.669  56.879  1.00 47.89           C  
ANISOU 1556  CA  GLN X  10     5104   5675   7419    417    375   -546       C  
ATOM   1557  C   GLN X  10      24.070  14.983  56.096  1.00 48.87           C  
ANISOU 1557  C   GLN X  10     5348   5787   7432    370    418   -600       C  
ATOM   1558  O   GLN X  10      23.526  14.121  55.396  1.00 50.27           O  
ANISOU 1558  O   GLN X  10     5631   5929   7542    407    481   -633       O  
ATOM   1559  CB  GLN X  10      25.036  14.676  58.371  1.00 41.63           C  
ANISOU 1559  CB  GLN X  10     4326   4883   6607    386    233   -552       C  
ATOM   1560  CG  GLN X  10      26.263  14.452  59.187  1.00 49.23           C  
ANISOU 1560  CG  GLN X  10     5172   5862   7672    439    157   -505       C  
ATOM   1561  CD  GLN X  10      25.981  14.350  60.670  1.00 55.42           C  
ANISOU 1561  CD  GLN X  10     6010   6639   8410    431     14   -511       C  
ATOM   1562  OE1 GLN X  10      25.073  13.662  61.104  1.00 43.55           O  
ANISOU 1562  OE1 GLN X  10     4645   5098   6806    438     14   -531       O  
ATOM   1563  NE2 GLN X  10      26.782  15.032  61.456  1.00 67.39           N  
ANISOU 1563  NE2 GLN X  10     7419   8185   9999    417   -108   -493       N  
ATOM   1564  N   THR X  11      23.621  16.231  56.172  1.00 49.24           N  
ANISOU 1564  N   THR X  11     5384   5860   7464    293    378   -611       N  
ATOM   1565  CA  THR X  11      22.422  16.622  55.433  1.00 47.32           C  
ANISOU 1565  CA  THR X  11     5245   5613   7120    259    404   -661       C  
ATOM   1566  C   THR X  11      22.628  16.299  53.981  1.00 42.39           C  
ANISOU 1566  C   THR X  11     4666   4972   6468    319    526   -662       C  
ATOM   1567  O   THR X  11      21.773  15.711  53.328  1.00 51.62           O  
ANISOU 1567  O   THR X  11     5948   6118   7548    337    547   -714       O  
ATOM   1568  CB  THR X  11      22.107  18.120  55.575  1.00 47.46           C  
ANISOU 1568  CB  THR X  11     5242   5657   7134    188    362   -661       C  
ATOM   1569  OG1 THR X  11      22.061  18.469  56.966  1.00 48.35           O  
ANISOU 1569  OG1 THR X  11     5323   5779   7268    143    249   -659       O  
ATOM   1570  CG2 THR X  11      20.770  18.449  54.918  1.00 39.99           C  
ANISOU 1570  CG2 THR X  11     4402   4711   6080    170    369   -714       C  
ATOM   1571  N   SER X  12      23.784  16.673  53.474  1.00 45.21           N  
ANISOU 1571  N   SER X  12     4935   5337   6904    351    607   -606       N  
ATOM   1572  CA  SER X  12      24.127  16.387  52.080  1.00 51.71           C  
ANISOU 1572  CA  SER X  12     5812   6140   7696    426    749   -596       C  
ATOM   1573  C   SER X  12      24.049  14.899  51.674  1.00 55.16           C  
ANISOU 1573  C   SER X  12     6341   6534   8081    511    794   -626       C  
ATOM   1574  O   SER X  12      23.443  14.562  50.644  1.00 58.76           O  
ANISOU 1574  O   SER X  12     6934   6961   8430    549    845   -671       O  
ATOM   1575  CB  SER X  12      25.509  16.940  51.771  1.00 51.40           C  
ANISOU 1575  CB  SER X  12     5636   6112   7781    447    848   -517       C  
ATOM   1576  OG  SER X  12      25.659  17.007  50.372  1.00 69.72           O  
ANISOU 1576  OG  SER X  12     8036   8410  10044    511   1000   -503       O  
ATOM   1577  N   THR X  13      24.676  14.029  52.474  1.00 41.63           N  
ANISOU 1577  N   THR X  13     4564   4812   6441    546    769   -602       N  
ATOM   1578  CA  THR X  13      24.659  12.585  52.242  1.00 41.92           C  
ANISOU 1578  CA  THR X  13     4694   4794   6440    628    809   -626       C  
ATOM   1579  C   THR X  13      23.228  12.067  52.300  1.00 50.60           C  
ANISOU 1579  C   THR X  13     5939   5857   7430    579    738   -708       C  
ATOM   1580  O   THR X  13      22.811  11.266  51.463  1.00 51.05           O  
ANISOU 1580  O   THR X  13     6126   5861   7409    622    785   -758       O  
ATOM   1581  CB  THR X  13      25.476  11.817  53.338  1.00 45.13           C  
ANISOU 1581  CB  THR X  13     5010   5195   6941    672    765   -583       C  
ATOM   1582  OG1 THR X  13      26.782  12.366  53.454  1.00 47.89           O  
ANISOU 1582  OG1 THR X  13     5185   5589   7422    702    799   -511       O  
ATOM   1583  CG2 THR X  13      25.619  10.340  53.012  1.00 51.37           C  
ANISOU 1583  CG2 THR X  13     5902   5916   7699    774    828   -598       C  
ATOM   1584  N   LEU X  14      22.470  12.515  53.303  1.00 49.38           N  
ANISOU 1584  N   LEU X  14     5761   5726   7273    488    626   -725       N  
ATOM   1585  CA  LEU X  14      21.089  12.059  53.440  1.00 49.32           C  
ANISOU 1585  CA  LEU X  14     5861   5688   7191    431    567   -796       C  
ATOM   1586  C   LEU X  14      20.303  12.421  52.192  1.00 52.79           C  
ANISOU 1586  C   LEU X  14     6388   6127   7543    423    588   -856       C  
ATOM   1587  O   LEU X  14      19.541  11.622  51.692  1.00 54.81           O  
ANISOU 1587  O   LEU X  14     6751   6333   7739    423    580   -922       O  
ATOM   1588  CB  LEU X  14      20.415  12.620  54.697  1.00 41.92           C  
ANISOU 1588  CB  LEU X  14     4881   4781   6267    345    468   -796       C  
ATOM   1589  CG  LEU X  14      20.974  12.142  56.035  1.00 53.04           C  
ANISOU 1589  CG  LEU X  14     6246   6179   7730    358    424   -748       C  
ATOM   1590  CD1 LEU X  14      20.324  12.901  57.229  1.00 39.12           C  
ANISOU 1590  CD1 LEU X  14     4460   4446   5957    283    335   -747       C  
ATOM   1591  CD2 LEU X  14      20.831  10.648  56.182  1.00 54.93           C  
ANISOU 1591  CD2 LEU X  14     6576   6341   7956    398    452   -762       C  
ATOM   1592  N   CYS X  15      20.494  13.627  51.678  1.00 59.10           N  
ANISOU 1592  N   CYS X  15     7150   6974   8333    418    608   -833       N  
ATOM   1593  CA  CYS X  15      19.765  14.024  50.479  1.00 54.15           C  
ANISOU 1593  CA  CYS X  15     6624   6346   7606    429    619   -885       C  
ATOM   1594  C   CYS X  15      20.048  13.067  49.347  1.00 54.09           C  
ANISOU 1594  C   CYS X  15     6734   6282   7535    519    699   -914       C  
ATOM   1595  O   CYS X  15      19.124  12.532  48.744  1.00 61.72           O  
ANISOU 1595  O   CYS X  15     7819   7213   8419    518    656   -995       O  
ATOM   1596  CB  CYS X  15      20.102  15.457  50.049  1.00 50.12           C  
ANISOU 1596  CB  CYS X  15     6073   5880   7092    427    654   -839       C  
ATOM   1597  SG  CYS X  15      19.335  16.708  51.074  1.00 56.93           S  
ANISOU 1597  SG  CYS X  15     6860   6794   7978    326    544   -838       S  
ATOM   1598  N   HIS X  16      21.329  12.869  49.054  1.00 48.70           N  
ANISOU 1598  N   HIS X  16     6019   5589   6897    600    815   -850       N  
ATOM   1599  CA  HIS X  16      21.732  11.970  47.971  1.00 56.70           C  
ANISOU 1599  CA  HIS X  16     7156   6542   7845    707    916   -870       C  
ATOM   1600  C   HIS X  16      21.116  10.586  48.118  1.00 56.90           C  
ANISOU 1600  C   HIS X  16     7286   6496   7839    707    864   -944       C  
ATOM   1601  O   HIS X  16      20.375  10.123  47.240  1.00 60.43           O  
ANISOU 1601  O   HIS X  16     7887   6895   8179    725    841  -1028       O  
ATOM   1602  CB  HIS X  16      23.251  11.847  47.916  1.00 59.85           C  
ANISOU 1602  CB  HIS X  16     7465   6942   8332    795   1054   -779       C  
ATOM   1603  CG  HIS X  16      23.929  13.030  47.300  1.00 67.88           C  
ANISOU 1603  CG  HIS X  16     8424   8000   9368    815   1157   -711       C  
ATOM   1604  ND1 HIS X  16      24.435  13.010  46.021  1.00 70.03           N  
ANISOU 1604  ND1 HIS X  16     8796   8242   9570    921   1310   -692       N  
ATOM   1605  CD2 HIS X  16      24.181  14.269  47.786  1.00 71.23           C  
ANISOU 1605  CD2 HIS X  16     8713   8480   9872    741   1137   -656       C  
ATOM   1606  CE1 HIS X  16      24.973  14.186  45.743  1.00 72.90           C  
ANISOU 1606  CE1 HIS X  16     9082   8641   9977    908   1393   -621       C  
ATOM   1607  NE2 HIS X  16      24.832  14.968  46.797  1.00 68.46           N  
ANISOU 1607  NE2 HIS X  16     8374   8128   9511    795   1284   -601       N  
ATOM   1608  N   SER X  17      21.420   9.935  49.235  1.00 49.66           N  
ANISOU 1608  N   SER X  17     6293   5565   7011    688    838   -916       N  
ATOM   1609  CA  SER X  17      20.921   8.589  49.486  1.00 52.84           C  
ANISOU 1609  CA  SER X  17     6794   5882   7398    683    804   -973       C  
ATOM   1610  C   SER X  17      19.416   8.494  49.274  1.00 56.44           C  
ANISOU 1610  C   SER X  17     7338   6316   7790    590    699  -1073       C  
ATOM   1611  O   SER X  17      18.933   7.595  48.582  1.00 65.11           O  
ANISOU 1611  O   SER X  17     8579   7334   8825    606    691  -1152       O  
ATOM   1612  CB  SER X  17      21.252   8.140  50.904  1.00 54.88           C  
ANISOU 1612  CB  SER X  17     6961   6137   7755    658    771   -921       C  
ATOM   1613  OG  SER X  17      22.617   8.367  51.194  1.00 60.74           O  
ANISOU 1613  OG  SER X  17     7586   6916   8576    737    837   -830       O  
ATOM   1614  N   PHE X  18      18.687   9.424  49.886  1.00 46.50           N  
ANISOU 1614  N   PHE X  18     5990   5125   6554    494    615  -1072       N  
ATOM   1615  CA  PHE X  18      17.233   9.440  49.853  1.00 52.39           C  
ANISOU 1615  CA  PHE X  18     6770   5865   7270    400    511  -1157       C  
ATOM   1616  C   PHE X  18      16.712   9.602  48.435  1.00 61.39           C  
ANISOU 1616  C   PHE X  18     8029   6995   8302    434    487  -1236       C  
ATOM   1617  O   PHE X  18      15.841   8.851  48.003  1.00 74.14           O  
ANISOU 1617  O   PHE X  18     9737   8550   9883    402    422  -1330       O  
ATOM   1618  CB  PHE X  18      16.691  10.546  50.776  1.00 52.62           C  
ANISOU 1618  CB  PHE X  18     6675   5976   7344    316    446  -1127       C  
ATOM   1619  CG  PHE X  18      15.302  11.004  50.433  1.00 48.87           C  
ANISOU 1619  CG  PHE X  18     6210   5527   6832    248    352  -1205       C  
ATOM   1620  CD1 PHE X  18      14.199  10.222  50.754  1.00 51.82           C  
ANISOU 1620  CD1 PHE X  18     6598   5855   7238    167    290  -1273       C  
ATOM   1621  CD2 PHE X  18      15.100  12.203  49.780  1.00 50.81           C  
ANISOU 1621  CD2 PHE X  18     6447   5838   7022    268    328  -1206       C  
ATOM   1622  CE1 PHE X  18      12.920  10.630  50.445  1.00 45.91           C  
ANISOU 1622  CE1 PHE X  18     5830   5135   6477    107    197  -1345       C  
ATOM   1623  CE2 PHE X  18      13.824  12.617  49.468  1.00 58.47           C  
ANISOU 1623  CE2 PHE X  18     7418   6835   7962    222    231  -1277       C  
ATOM   1624  CZ  PHE X  18      12.729  11.829  49.810  1.00 50.94           C  
ANISOU 1624  CZ  PHE X  18     6455   5846   7053    141    160  -1348       C  
ATOM   1625  N   LEU X  19      17.243  10.576  47.711  1.00 56.29           N  
ANISOU 1625  N   LEU X  19     7386   6401   7602    499    536  -1198       N  
ATOM   1626  CA  LEU X  19      16.794  10.809  46.351  1.00 56.21           C  
ANISOU 1626  CA  LEU X  19     7511   6382   7465    552    515  -1264       C  
ATOM   1627  C   LEU X  19      17.021   9.581  45.478  1.00 67.55           C  
ANISOU 1627  C   LEU X  19     9118   7721   8829    630    554  -1325       C  
ATOM   1628  O   LEU X  19      16.173   9.216  44.668  1.00 73.29           O  
ANISOU 1628  O   LEU X  19     9974   8406   9467    630    467  -1429       O  
ATOM   1629  CB  LEU X  19      17.507  12.011  45.752  1.00 56.86           C  
ANISOU 1629  CB  LEU X  19     7585   6519   7501    623    599  -1192       C  
ATOM   1630  CG  LEU X  19      17.018  13.346  46.296  1.00 57.64           C  
ANISOU 1630  CG  LEU X  19     7570   6699   7632    553    537  -1160       C  
ATOM   1631  CD1 LEU X  19      17.837  14.477  45.686  1.00 55.34           C  
ANISOU 1631  CD1 LEU X  19     7283   6439   7304    619    641  -1080       C  
ATOM   1632  CD2 LEU X  19      15.558  13.495  45.959  1.00 55.28           C  
ANISOU 1632  CD2 LEU X  19     7322   6413   7271    509    393  -1257       C  
ATOM   1633  N   LEU X  20      18.172   8.942  45.634  1.00 67.22           N  
ANISOU 1633  N   LEU X  20     9079   7638   8825    702    677  -1265       N  
ATOM   1634  CA  LEU X  20      18.466   7.787  44.811  1.00 70.35           C  
ANISOU 1634  CA  LEU X  20     9651   7933   9146    793    731  -1319       C  
ATOM   1635  C   LEU X  20      17.530   6.668  45.200  1.00 74.66           C  
ANISOU 1635  C   LEU X  20    10251   8396   9720    706    624  -1413       C  
ATOM   1636  O   LEU X  20      17.016   5.946  44.355  1.00 84.99           O  
ANISOU 1636  O   LEU X  20    11729   9622  10941    725    575  -1517       O  
ATOM   1637  CB  LEU X  20      19.927   7.358  44.956  1.00 73.99           C  
ANISOU 1637  CB  LEU X  20    10083   8371   9657    901    895  -1225       C  
ATOM   1638  CG  LEU X  20      20.928   8.128  44.082  1.00 81.89           C  
ANISOU 1638  CG  LEU X  20    11097   9411  10607   1020   1042  -1152       C  
ATOM   1639  CD1 LEU X  20      22.354   7.873  44.534  1.00 83.99           C  
ANISOU 1639  CD1 LEU X  20    11249   9682  10982   1100   1190  -1044       C  
ATOM   1640  CD2 LEU X  20      20.771   7.785  42.602  1.00 84.39           C  
ANISOU 1640  CD2 LEU X  20    11656   9660  10749   1129   1084  -1225       C  
ATOM   1641  N   ALA X  21      17.284   6.541  46.489  1.00 73.78           N  
ANISOU 1641  N   ALA X  21    10003   8300   9730    606    586  -1379       N  
ATOM   1642  CA  ALA X  21      16.506   5.420  46.971  1.00 71.59           C  
ANISOU 1642  CA  ALA X  21     9770   7931   9501    520    518  -1449       C  
ATOM   1643  C   ALA X  21      15.023   5.570  46.658  1.00 79.08           C  
ANISOU 1643  C   ALA X  21    10734   8881  10433    409    369  -1559       C  
ATOM   1644  O   ALA X  21      14.280   4.593  46.690  1.00 84.36           O  
ANISOU 1644  O   ALA X  21    11468   9454  11130    335    307  -1644       O  
ATOM   1645  CB  ALA X  21      16.741   5.212  48.455  1.00 65.46           C  
ANISOU 1645  CB  ALA X  21     8863   7162   8847    463    541  -1367       C  
ATOM   1646  N   SER X  22      14.587   6.784  46.342  1.00 79.76           N  
ANISOU 1646  N   SER X  22    10755   9069  10481    397    311  -1560       N  
ATOM   1647  CA  SER X  22      13.167   7.000  46.071  1.00 88.77           C  
ANISOU 1647  CA  SER X  22    11883  10227  11619    303    159  -1661       C  
ATOM   1648  C   SER X  22      12.815   6.936  44.580  1.00 99.81           C  
ANISOU 1648  C   SER X  22    13454  11594  12876    371     82  -1767       C  
ATOM   1649  O   SER X  22      11.745   7.383  44.164  1.00106.43           O  
ANISOU 1649  O   SER X  22    14278  12469  13691    325    -59  -1846       O  
ATOM   1650  CB  SER X  22      12.652   8.303  46.718  1.00 87.91           C  
ANISOU 1650  CB  SER X  22    11604  10240  11559    246    115  -1612       C  
ATOM   1651  OG  SER X  22      13.195   9.477  46.135  1.00 83.54           O  
ANISOU 1651  OG  SER X  22    11057   9766  10920    336    151  -1559       O  
ATOM   1652  N   ALA X  23      13.699   6.362  43.775  1.00105.34           N  
ANISOU 1652  N   ALA X  23    14324  12223  13479    490    169  -1772       N  
ATOM   1653  CA  ALA X  23      13.426   6.252  42.346  1.00110.71           C  
ANISOU 1653  CA  ALA X  23    15207  12861  13999    574    101  -1874       C  
ATOM   1654  C   ALA X  23      12.628   4.995  41.982  1.00116.22           C  
ANISOU 1654  C   ALA X  23    16031  13433  14694    511    -19  -2019       C  
ATOM   1655  O   ALA X  23      12.857   3.908  42.529  1.00112.74           O  
ANISOU 1655  O   ALA X  23    15609  12894  14334    469     31  -2022       O  
ATOM   1656  CB  ALA X  23      14.711   6.325  41.552  1.00109.68           C  
ANISOU 1656  CB  ALA X  23    15217  12712  13746    745    264  -1811       C  
ATOM   1657  N   ASN X  24      11.691   5.169  41.051  1.00127.03           N  
ANISOU 1657  N   ASN X  24    17493  14801  15971    507   -187  -2140       N  
ATOM   1658  CA  ASN X  24      10.846   4.081  40.564  1.00141.15           C  
ANISOU 1658  CA  ASN X  24    19406  16470  17755    440   -338  -2299       C  
ATOM   1659  C   ASN X  24      11.626   2.825  40.164  1.00145.01           C  
ANISOU 1659  C   ASN X  24    20111  16806  18182    515   -242  -2331       C  
ATOM   1660  O   ASN X  24      11.256   2.116  39.221  1.00145.41           O  
ANISOU 1660  O   ASN X  24    20369  16750  18130    540   -349  -2468       O  
ATOM   1661  CB  ASN X  24       9.976   4.567  39.396  1.00149.14           C  
ANISOU 1661  CB  ASN X  24    20525  17510  18633    477   -533  -2421       C  
ATOM   1662  CG  ASN X  24      10.796   5.118  38.229  1.00153.43           C  
ANISOU 1662  CG  ASN X  24    21281  18069  18948    679   -455  -2393       C  
ATOM   1663  OD1 ASN X  24      11.853   4.583  37.878  1.00154.18           O  
ANISOU 1663  OD1 ASN X  24    21536  18087  18957    794   -295  -2355       O  
ATOM   1664  ND2 ASN X  24      10.294   6.182  37.608  1.00154.81           N  
ANISOU 1664  ND2 ASN X  24    21465  18336  19020    733   -559  -2408       N  
ATOM   1665  N   THR X  28      16.086   5.961  37.951  1.00 97.41           N  
ANISOU 1665  N   THR X  28    14325  11008  11680   1185    449  -1894       N  
ATOM   1666  CA  THR X  28      17.302   5.897  38.763  1.00112.36           C  
ANISOU 1666  CA  THR X  28    16071  12921  13700   1210    651  -1753       C  
ATOM   1667  C   THR X  28      18.563   5.901  37.914  1.00123.96           C  
ANISOU 1667  C   THR X  28    17683  14359  15058   1401    874  -1680       C  
ATOM   1668  O   THR X  28      19.617   6.371  38.356  1.00126.38           O  
ANISOU 1668  O   THR X  28    17840  14721  15456   1441   1048  -1542       O  
ATOM   1669  CB  THR X  28      17.365   4.626  39.638  1.00119.20           C  
ANISOU 1669  CB  THR X  28    16891  13701  14698   1139    647  -1777       C  
ATOM   1670  OG1 THR X  28      16.308   4.636  40.604  1.00122.89           O  
ANISOU 1670  OG1 THR X  28    17195  14199  15298    956    484  -1817       O  
ATOM   1671  CG2 THR X  28      18.705   4.549  40.365  1.00118.14           C  
ANISOU 1671  CG2 THR X  28    16624  13588  14676   1199    846  -1632       C  
ATOM   1672  N   ASP X  29      18.461   5.339  36.712  1.00126.83           N  
ANISOU 1672  N   ASP X  29    18333  14627  15231   1520    869  -1775       N  
ATOM   1673  CA  ASP X  29      19.603   5.235  35.812  1.00122.94           C  
ANISOU 1673  CA  ASP X  29    18012  14088  14612   1719   1098  -1714       C  
ATOM   1674  C   ASP X  29      20.276   6.576  35.694  1.00113.93           C  
ANISOU 1674  C   ASP X  29    16757  13054  13478   1770   1250  -1571       C  
ATOM   1675  O   ASP X  29      21.445   6.740  36.049  1.00106.21           O  
ANISOU 1675  O   ASP X  29    15645  12105  12605   1824   1460  -1439       O  
ATOM   1676  CB  ASP X  29      19.151   4.799  34.423  1.00128.16           C  
ANISOU 1676  CB  ASP X  29    19025  14648  15021   1839   1034  -1845       C  
ATOM   1677  CG  ASP X  29      19.012   3.305  34.301  1.00133.87           C  
ANISOU 1677  CG  ASP X  29    19923  15224  15717   1854    984  -1965       C  
ATOM   1678  OD1 ASP X  29      19.141   2.611  35.332  1.00136.02           O  
ANISOU 1678  OD1 ASP X  29    20038  15473  16171   1758    984  -1947       O  
ATOM   1679  OD2 ASP X  29      18.778   2.830  33.169  1.00134.46           O  
ANISOU 1679  OD2 ASP X  29    20310  15198  15580   1967    943  -2077       O  
ATOM   1680  N   TYR X  30      19.512   7.534  35.184  1.00111.34           N  
ANISOU 1680  N   TYR X  30    16483  12779  13042   1753   1137  -1601       N  
ATOM   1681  CA  TYR X  30      20.002   8.883  35.032  1.00107.04           C  
ANISOU 1681  CA  TYR X  30    15854  12322  12494   1788   1265  -1473       C  
ATOM   1682  C   TYR X  30      20.602   9.367  36.340  1.00108.32           C  
ANISOU 1682  C   TYR X  30    15682  12571  12905   1674   1336  -1348       C  
ATOM   1683  O   TYR X  30      21.798   9.655  36.427  1.00112.67           O  
ANISOU 1683  O   TYR X  30    16138  13140  13532   1738   1558  -1220       O  
ATOM   1684  CB  TYR X  30      18.872   9.824  34.631  1.00105.73           C  
ANISOU 1684  CB  TYR X  30    15745  12209  12220   1747   1077  -1530       C  
ATOM   1685  CG  TYR X  30      19.284  11.275  34.755  1.00108.49           C  
ANISOU 1685  CG  TYR X  30    15964  12647  12610   1744   1190  -1392       C  
ATOM   1686  CD1 TYR X  30      20.519  11.706  34.269  1.00107.99           C  
ANISOU 1686  CD1 TYR X  30    15937  12573  12521   1866   1468  -1260       C  
ATOM   1687  CD2 TYR X  30      18.460  12.210  35.370  1.00106.71           C  
ANISOU 1687  CD2 TYR X  30    15576  12507  12459   1619   1032  -1391       C  
ATOM   1688  CE1 TYR X  30      20.918  13.028  34.388  1.00107.38           C  
ANISOU 1688  CE1 TYR X  30    15741  12561  12497   1848   1578  -1134       C  
ATOM   1689  CE2 TYR X  30      18.851  13.544  35.490  1.00105.91           C  
ANISOU 1689  CE2 TYR X  30    15373  12471  12397   1613   1137  -1267       C  
ATOM   1690  CZ  TYR X  30      20.082  13.946  34.996  1.00108.90           C  
ANISOU 1690  CZ  TYR X  30    15793  12830  12754   1721   1407  -1140       C  
ATOM   1691  OH  TYR X  30      20.484  15.266  35.107  1.00110.52           O  
ANISOU 1691  OH  TYR X  30    15900  13083  13011   1703   1518  -1017       O  
ATOM   1692  N   LEU X  31      19.751   9.453  37.358  1.00101.52           N  
ANISOU 1692  N   LEU X  31    14642  11759  12171   1506   1144  -1389       N  
ATOM   1693  CA  LEU X  31      20.140  10.027  38.633  1.00 91.51           C  
ANISOU 1693  CA  LEU X  31    13079  10575  11114   1392   1170  -1286       C  
ATOM   1694  C   LEU X  31      21.359   9.332  39.197  1.00 88.36           C  
ANISOU 1694  C   LEU X  31    12571  10152  10848   1432   1335  -1204       C  
ATOM   1695  O   LEU X  31      22.286   9.998  39.662  1.00 86.82           O  
ANISOU 1695  O   LEU X  31    12196  10015  10775   1430   1464  -1081       O  
ATOM   1696  CB  LEU X  31      18.980   9.971  39.626  1.00 90.77           C  
ANISOU 1696  CB  LEU X  31    12851  10518  11119   1223    947  -1357       C  
ATOM   1697  CG  LEU X  31      17.965  11.107  39.496  1.00 89.88           C  
ANISOU 1697  CG  LEU X  31    12717  10476  10957   1162    805  -1383       C  
ATOM   1698  CD1 LEU X  31      16.758  10.872  40.397  1.00 86.64           C  
ANISOU 1698  CD1 LEU X  31    12185  10090  10643   1009    598  -1464       C  
ATOM   1699  CD2 LEU X  31      18.635  12.435  39.815  1.00 87.36           C  
ANISOU 1699  CD2 LEU X  31    12253  10235  10704   1157    920  -1250       C  
ATOM   1700  N   THR X  32      21.355   8.000  39.156  1.00 88.32           N  
ANISOU 1700  N   THR X  32    12675  10058  10826   1468   1321  -1276       N  
ATOM   1701  CA  THR X  32      22.493   7.215  39.633  1.00 89.13           C  
ANISOU 1701  CA  THR X  32    12697  10126  11041   1532   1471  -1205       C  
ATOM   1702  C   THR X  32      23.791   7.632  38.925  1.00 90.66           C  
ANISOU 1702  C   THR X  32    12902  10330  11215   1685   1725  -1092       C  
ATOM   1703  O   THR X  32      24.849   7.743  39.550  1.00 94.25           O  
ANISOU 1703  O   THR X  32    13156  10825  11829   1702   1853   -980       O  
ATOM   1704  CB  THR X  32      22.237   5.711  39.425  1.00 20.00           C  
ATOM   1705  OG1 THR X  32      22.020   5.448  38.034  0.01 20.00           O  
ATOM   1706  CG2 THR X  32      20.922   5.299  40.069  0.01 20.00           C  
ATOM   1707  N   ASP X  33      23.690   7.882  37.622  1.00 88.53           N  
ANISOU 1707  N   ASP X  33    12865  10023  10750   1799   1797  -1121       N  
ATOM   1708  CA  ASP X  33      24.826   8.323  36.813  1.00 88.59           C  
ANISOU 1708  CA  ASP X  33    12914  10029  10717   1951   2062  -1012       C  
ATOM   1709  C   ASP X  33      25.189   9.768  37.123  1.00 90.33           C  
ANISOU 1709  C   ASP X  33    12928  10350  11045   1881   2126   -892       C  
ATOM   1710  O   ASP X  33      26.135  10.316  36.549  1.00 88.22           O  
ANISOU 1710  O   ASP X  33    12652  10088  10779   1979   2356   -785       O  
ATOM   1711  CB  ASP X  33      24.516   8.165  35.323  1.00 20.00           C  
ATOM   1712  CG  ASP X  33      24.482   6.714  34.886  0.01 20.00           C  
ATOM   1713  OD1 ASP X  33      24.968   5.851  35.646  0.01 20.00           O  
ATOM   1714  OD2 ASP X  33      23.988   6.342  33.800  0.01 20.00           O  
ATOM   1715  N   LEU X  34      24.427  10.369  38.037  1.00 91.75           N  
ANISOU 1715  N   LEU X  34    12946  10599  11316   1712   1930   -912       N  
ATOM   1716  CA  LEU X  34      24.584  11.773  38.407  1.00 86.59           C  
ANISOU 1716  CA  LEU X  34    12115  10030  10756   1626   1950   -819       C  
ATOM   1717  C   LEU X  34      25.104  11.978  39.839  1.00 89.61           C  
ANISOU 1717  C   LEU X  34    12181  10480  11388   1503   1916   -748       C  
ATOM   1718  O   LEU X  34      25.773  12.965  40.123  1.00 89.51           O  
ANISOU 1718  O   LEU X  34    11996  10518  11494   1464   2007   -644       O  
ATOM   1719  CB  LEU X  34      23.261  12.512  38.202  1.00 88.90           C  
ANISOU 1719  CB  LEU X  34    12502  10348  10928   1549   1756   -895       C  
ATOM   1720  CG  LEU X  34      23.205  13.999  38.571  1.00 90.45           C  
ANISOU 1720  CG  LEU X  34    12553  10618  11197   1458   1748   -816       C  
ATOM   1721  CD1 LEU X  34      24.355  14.780  37.942  1.00 91.21           C  
ANISOU 1721  CD1 LEU X  34    12638  10707  11309   1541   2008   -683       C  
ATOM   1722  CD2 LEU X  34      21.869  14.603  38.171  1.00 85.64           C  
ANISOU 1722  CD2 LEU X  34    12080  10022  10437   1426   1565   -899       C  
ATOM   1723  N   LEU X  35      24.820  11.042  40.737  1.00 97.93           N  
ANISOU 1723  N   LEU X  35    13167  11525  12518   1446   1786   -804       N  
ATOM   1724  CA  LEU X  35      25.230  11.186  42.137  1.00 99.21           C  
ANISOU 1724  CA  LEU X  35    13060  11746  12890   1341   1728   -746       C  
ATOM   1725  C   LEU X  35      26.310  10.176  42.569  1.00102.68           C  
ANISOU 1725  C   LEU X  35    13405  12160  13448   1420   1829   -699       C  
ATOM   1726  O   LEU X  35      27.518  10.457  42.502  1.00102.07           O  
ANISOU 1726  O   LEU X  35    13193  12106  13483   1484   1997   -595       O  
ATOM   1727  CB  LEU X  35      23.994  11.102  43.043  1.00 94.40           C  
ANISOU 1727  CB  LEU X  35    12424  11157  12287   1199   1491   -831       C  
ATOM   1728  CG  LEU X  35      22.759  11.824  42.465  1.00 87.80           C  
ANISOU 1728  CG  LEU X  35    11717  10332  11309   1150   1375   -903       C  
ATOM   1729  CD1 LEU X  35      21.502  11.541  43.264  1.00 83.02           C  
ANISOU 1729  CD1 LEU X  35    11090   9737  10716   1026   1161   -993       C  
ATOM   1730  CD2 LEU X  35      22.985  13.327  42.349  1.00 80.15           C  
ANISOU 1730  CD2 LEU X  35    10665   9425  10363   1119   1426   -823       C  
ATOM   1731  N   THR X  38      30.492   8.121  44.616  1.00 76.74           N  
ANISOU 1731  N   THR X  38     9520   8902  10736   1681   2127   -433       N  
ATOM   1732  CA  THR X  38      31.596   7.424  45.288  1.00 84.42           C  
ANISOU 1732  CA  THR X  38    10319   9884  11873   1773   2171   -367       C  
ATOM   1733  C   THR X  38      31.967   8.101  46.587  1.00 88.25           C  
ANISOU 1733  C   THR X  38    10528  10459  12545   1659   2033   -313       C  
ATOM   1734  O   THR X  38      32.367   7.443  47.549  1.00 87.54           O  
ANISOU 1734  O   THR X  38    10335  10375  12553   1689   1947   -296       O  
ATOM   1735  CB  THR X  38      32.876   7.378  44.429  1.00 89.74           C  
ANISOU 1735  CB  THR X  38    10922  10556  12620   1935   2433   -278       C  
ATOM   1736  OG1 THR X  38      32.780   6.301  43.495  1.00105.40           O  
ANISOU 1736  OG1 THR X  38    13161  12439  14447   2092   2555   -326       O  
ATOM   1737  CG2 THR X  38      34.094   7.123  45.287  1.00 80.56           C  
ANISOU 1737  CG2 THR X  38     9477   9444  11687   1993   2448   -190       C  
ATOM   1738  N   ASN X  39      31.859   9.429  46.586  1.00 87.48           N  
ANISOU 1738  N   ASN X  39    10327  10423  12489   1538   2012   -287       N  
ATOM   1739  CA  ASN X  39      32.047  10.243  47.779  1.00 87.19           C  
ANISOU 1739  CA  ASN X  39    10062  10462  12604   1408   1858   -254       C  
ATOM   1740  C   ASN X  39      30.796  10.236  48.649  1.00 83.79           C  
ANISOU 1740  C   ASN X  39     9728  10029  12081   1283   1634   -335       C  
ATOM   1741  O   ASN X  39      30.698  10.962  49.634  1.00 81.55           O  
ANISOU 1741  O   ASN X  39     9312   9798  11876   1168   1490   -326       O  
ATOM   1742  CB  ASN X  39      32.396  11.680  47.401  1.00 97.26           C  
ANISOU 1742  CB  ASN X  39    11211  11787  13959   1324   1934   -197       C  
ATOM   1743  CG  ASN X  39      33.864  11.996  47.607  1.00113.31           C  
ANISOU 1743  CG  ASN X  39    12956  13866  16230   1360   2035    -95       C  
ATOM   1744  OD1 ASN X  39      34.739  11.140  47.420  1.00121.56           O  
ANISOU 1744  OD1 ASN X  39    13936  14900  17350   1503   2151    -53       O  
ATOM   1745  ND2 ASN X  39      34.145  13.235  48.000  1.00114.59           N  
ANISOU 1745  ND2 ASN X  39    12938  14078  16523   1229   1989    -56       N  
ATOM   1746  N   ILE X  40      29.833   9.413  48.266  1.00 82.41           N  
ANISOU 1746  N   ILE X  40     9788   9785  11738   1307   1610   -416       N  
ATOM   1747  CA  ILE X  40      28.642   9.225  49.064  1.00 80.19           C  
ANISOU 1747  CA  ILE X  40     9596   9491  11382   1200   1423   -490       C  
ATOM   1748  C   ILE X  40      28.808   7.988  49.940  1.00 75.51           C  
ANISOU 1748  C   ILE X  40     9013   8856  10822   1257   1357   -494       C  
ATOM   1749  O   ILE X  40      28.856   6.861  49.446  1.00 83.71           O  
ANISOU 1749  O   ILE X  40    10192   9816  11799   1364   1432   -520       O  
ATOM   1750  CB  ILE X  40      27.393   9.093  48.161  1.00 82.99           C  
ANISOU 1750  CB  ILE X  40    10189   9793  11551   1172   1415   -583       C  
ATOM   1751  CG1 ILE X  40      26.985  10.452  47.606  1.00 78.93           C  
ANISOU 1751  CG1 ILE X  40     9669   9326  10993   1094   1422   -582       C  
ATOM   1752  CG2 ILE X  40      26.220   8.479  48.907  1.00 85.95           C  
ANISOU 1752  CG2 ILE X  40    10662  10130  11863   1089   1255   -661       C  
ATOM   1753  CD1 ILE X  40      25.885  10.327  46.557  1.00 88.99           C  
ANISOU 1753  CD1 ILE X  40    11176  10552  12082   1098   1417   -671       C  
ATOM   1754  N   ASP X  41      28.919   8.203  51.244  1.00 66.23           N  
ANISOU 1754  N   ASP X  41     7704   7723   9736   1194   1219   -467       N  
ATOM   1755  CA  ASP X  41      28.931   7.090  52.181  1.00 67.87           C  
ANISOU 1755  CA  ASP X  41     7949   7884   9953   1241   1141   -469       C  
ATOM   1756  C   ASP X  41      27.944   7.313  53.334  1.00 66.60           C  
ANISOU 1756  C   ASP X  41     7817   7731   9756   1113    970   -503       C  
ATOM   1757  O   ASP X  41      28.222   8.048  54.288  1.00 62.46           O  
ANISOU 1757  O   ASP X  41     7152   7272   9309   1056    865   -467       O  
ATOM   1758  CB  ASP X  41      30.338   6.828  52.706  1.00 71.52           C  
ANISOU 1758  CB  ASP X  41     8227   8381  10568   1354   1160   -385       C  
ATOM   1759  CG  ASP X  41      30.400   5.606  53.606  1.00 77.86           C  
ANISOU 1759  CG  ASP X  41     9095   9123  11365   1433   1090   -380       C  
ATOM   1760  OD1 ASP X  41      29.341   4.995  53.853  1.00 73.47           O  
ANISOU 1760  OD1 ASP X  41     8725   8495  10696   1383   1037   -438       O  
ATOM   1761  OD2 ASP X  41      31.506   5.257  54.074  1.00 90.04           O  
ANISOU 1761  OD2 ASP X  41    10501  10688  13022   1546   1087   -315       O  
ATOM   1762  N   LEU X  42      26.794   6.657  53.236  1.00 60.50           N  
ANISOU 1762  N   LEU X  42     7232   6885   8870   1069    945   -574       N  
ATOM   1763  CA  LEU X  42      25.730   6.812  54.212  1.00 58.31           C  
ANISOU 1763  CA  LEU X  42     6997   6605   8552    949    816   -607       C  
ATOM   1764  C   LEU X  42      26.151   6.359  55.598  1.00 56.39           C  
ANISOU 1764  C   LEU X  42     6707   6357   8363    981    730   -557       C  
ATOM   1765  O   LEU X  42      25.486   6.669  56.584  1.00 57.77           O  
ANISOU 1765  O   LEU X  42     6890   6544   8516    894    628   -564       O  
ATOM   1766  CB  LEU X  42      24.493   6.040  53.765  1.00 52.45           C  
ANISOU 1766  CB  LEU X  42     6450   5773   7704    903    823   -691       C  
ATOM   1767  CG  LEU X  42      23.179   6.225  54.514  1.00 55.78           C  
ANISOU 1767  CG  LEU X  42     6920   6188   8085    767    723   -735       C  
ATOM   1768  CD1 LEU X  42      22.742   7.716  54.480  1.00 38.84           C  
ANISOU 1768  CD1 LEU X  42     4680   4140   5937    669    669   -743       C  
ATOM   1769  CD2 LEU X  42      22.102   5.286  53.924  1.00 47.04           C  
ANISOU 1769  CD2 LEU X  42     5989   4979   6904    729    741   -821       C  
ATOM   1770  N   THR X  43      27.250   5.631  55.697  1.00 47.82           N  
ANISOU 1770  N   THR X  43     5578   5252   7340   1117    771   -504       N  
ATOM   1771  CA  THR X  43      27.728   5.249  57.028  1.00 57.18           C  
ANISOU 1771  CA  THR X  43     6719   6437   8570   1166    672   -451       C  
ATOM   1772  C   THR X  43      28.427   6.427  57.687  1.00 63.22           C  
ANISOU 1772  C   THR X  43     7281   7311   9429   1133    572   -407       C  
ATOM   1773  O   THR X  43      28.834   6.348  58.845  1.00 66.49           O  
ANISOU 1773  O   THR X  43     7646   7741   9874   1166    457   -369       O  
ATOM   1774  CB  THR X  43      28.674   4.035  56.991  1.00 61.93           C  
ANISOU 1774  CB  THR X  43     7342   6978   9210   1341    733   -407       C  
ATOM   1775  OG1 THR X  43      29.889   4.402  56.323  1.00 67.31           O  
ANISOU 1775  OG1 THR X  43     7851   7724  10000   1432    808   -363       O  
ATOM   1776  CG2 THR X  43      28.008   2.865  56.264  1.00 53.49           C  
ANISOU 1776  CG2 THR X  43     6493   5783   8048   1370    834   -460       C  
ATOM   1777  N   CYS X  44      28.566   7.520  56.939  1.00 61.46           N  
ANISOU 1777  N   CYS X  44     6952   7155   9247   1070    613   -414       N  
ATOM   1778  CA  CYS X  44      29.080   8.769  57.508  1.00 62.68           C  
ANISOU 1778  CA  CYS X  44     6925   7399   9491   1005    516   -386       C  
ATOM   1779  C   CYS X  44      28.040   9.464  58.395  1.00 64.77           C  
ANISOU 1779  C   CYS X  44     7254   7677   9680    876    391   -422       C  
ATOM   1780  O   CYS X  44      28.395  10.191  59.323  1.00 68.60           O  
ANISOU 1780  O   CYS X  44     7641   8211  10215    840    265   -403       O  
ATOM   1781  CB  CYS X  44      29.590   9.720  56.416  1.00 63.70           C  
ANISOU 1781  CB  CYS X  44     6930   7579   9695    978    619   -373       C  
ATOM   1782  SG  CYS X  44      31.257   9.293  55.762  1.00 74.06           S  
ANISOU 1782  SG  CYS X  44     8062   8912  11167   1133    746   -299       S  
ATOM   1783  N   VAL X  45      26.761   9.230  58.106  1.00 59.59           N  
ANISOU 1783  N   VAL X  45     6761   6973   8907    812    425   -477       N  
ATOM   1784  CA  VAL X  45      25.687   9.740  58.947  1.00 52.67           C  
ANISOU 1784  CA  VAL X  45     5954   6100   7957    705    332   -509       C  
ATOM   1785  C   VAL X  45      25.347   8.695  60.007  1.00 57.14           C  
ANISOU 1785  C   VAL X  45     6641   6602   8469    745    284   -498       C  
ATOM   1786  O   VAL X  45      24.990   7.574  59.663  1.00 63.86           O  
ANISOU 1786  O   VAL X  45     7611   7374   9278    785    358   -513       O  
ATOM   1787  CB  VAL X  45      24.423  10.034  58.137  1.00 42.02           C  
ANISOU 1787  CB  VAL X  45     4703   4737   6527    615    388   -573       C  
ATOM   1788  CG1 VAL X  45      23.348  10.565  59.055  1.00 38.01           C  
ANISOU 1788  CG1 VAL X  45     4248   4237   5958    518    305   -598       C  
ATOM   1789  CG2 VAL X  45      24.722  11.008  56.998  1.00 53.62           C  
ANISOU 1789  CG2 VAL X  45     6091   6256   8027    592    451   -578       C  
ATOM   1790  N   PRO X  46      25.453   9.061  61.293  1.00 56.90           N  
ANISOU 1790  N   PRO X  46     6595   6594   8431    736    162   -474       N  
ATOM   1791  CA  PRO X  46      25.309   8.139  62.415  1.00 62.27           C  
ANISOU 1791  CA  PRO X  46     7394   7212   9054    794    115   -446       C  
ATOM   1792  C   PRO X  46      24.323   6.988  62.204  1.00 80.06           C  
ANISOU 1792  C   PRO X  46     9823   9363  11234    786    214   -469       C  
ATOM   1793  O   PRO X  46      24.786   5.850  62.067  1.00103.59           O  
ANISOU 1793  O   PRO X  46    12860  12277  14224    886    262   -444       O  
ATOM   1794  CB  PRO X  46      24.885   9.061  63.549  1.00 58.93           C  
ANISOU 1794  CB  PRO X  46     6984   6825   8582    728      0   -449       C  
ATOM   1795  CG  PRO X  46      25.697  10.296  63.283  1.00 57.72           C  
ANISOU 1795  CG  PRO X  46     6652   6761   8519    698    -67   -450       C  
ATOM   1796  CD  PRO X  46      25.725  10.430  61.769  1.00 62.45           C  
ANISOU 1796  CD  PRO X  46     7185   7374   9170    672     59   -472       C  
ATOM   1797  N   ASN X  47      23.020   7.246  62.200  1.00 61.18           N  
ANISOU 1797  N   ASN X  47     7510   6954   8782    673    242   -514       N  
ATOM   1798  CA  ASN X  47      22.045   6.182  61.946  1.00 55.43           C  
ANISOU 1798  CA  ASN X  47     6927   6124   8010    642    332   -543       C  
ATOM   1799  C   ASN X  47      21.530   6.285  60.521  1.00 61.01           C  
ANISOU 1799  C   ASN X  47     7619   6833   8728    583    404   -610       C  
ATOM   1800  O   ASN X  47      20.332   6.214  60.262  1.00 59.43           O  
ANISOU 1800  O   ASN X  47     7481   6601   8499    487    435   -662       O  
ATOM   1801  CB  ASN X  47      20.903   6.232  62.969  1.00 52.39           C  
ANISOU 1801  CB  ASN X  47     6638   5705   7561    563    323   -543       C  
ATOM   1802  CG  ASN X  47      21.390   5.974  64.402  1.00 52.12           C  
ANISOU 1802  CG  ASN X  47     6668   5648   7485    644    258   -474       C  
ATOM   1803  OD1 ASN X  47      21.683   4.847  64.775  1.00 59.40           O  
ANISOU 1803  OD1 ASN X  47     7696   6483   8391    726    288   -434       O  
ATOM   1804  ND2 ASN X  47      21.493   7.022  65.193  1.00 55.63           N  
ANISOU 1804  ND2 ASN X  47     7066   6165   7904    629    164   -462       N  
ATOM   1805  N   GLY X  48      22.469   6.457  59.600  1.00 61.09           N  
ANISOU 1805  N   GLY X  48     7546   6882   8784    647    429   -606       N  
ATOM   1806  CA  GLY X  48      22.176   6.715  58.208  1.00 56.69           C  
ANISOU 1806  CA  GLY X  48     6981   6336   8221    615    491   -663       C  
ATOM   1807  C   GLY X  48      21.042   5.919  57.606  1.00 59.64           C  
ANISOU 1807  C   GLY X  48     7489   6624   8548    558    540   -733       C  
ATOM   1808  O   GLY X  48      20.064   6.505  57.161  1.00 59.47           O  
ANISOU 1808  O   GLY X  48     7467   6629   8501    462    526   -790       O  
ATOM   1809  N   GLN X  49      21.162   4.594  57.569  1.00 57.87           N  
ANISOU 1809  N   GLN X  49     7378   6292   8318    615    591   -733       N  
ATOM   1810  CA  GLN X  49      20.208   3.785  56.800  1.00 50.47           C  
ANISOU 1810  CA  GLN X  49     6568   5258   7349    560    634   -812       C  
ATOM   1811  C   GLN X  49      18.818   3.840  57.439  1.00 56.18           C  
ANISOU 1811  C   GLN X  49     7323   5957   8067    422    602   -846       C  
ATOM   1812  O   GLN X  49      17.797   3.956  56.740  1.00 60.43           O  
ANISOU 1812  O   GLN X  49     7880   6486   8594    330    592   -925       O  
ATOM   1813  CB  GLN X  49      20.710   2.329  56.623  1.00 61.41           C  
ANISOU 1813  CB  GLN X  49     8084   6515   8733    657    702   -806       C  
ATOM   1814  CG  GLN X  49      19.937   1.464  55.594  1.00 94.22           C  
ANISOU 1814  CG  GLN X  49    12383  10558  12857    614    742   -901       C  
ATOM   1815  CD  GLN X  49      19.941   2.039  54.164  1.00 95.94           C  
ANISOU 1815  CD  GLN X  49    12588  10828  13036    624    750   -967       C  
ATOM   1816  OE1 GLN X  49      20.958   2.002  53.470  1.00 95.12           O  
ANISOU 1816  OE1 GLN X  49    12483  10738  12921    746    809   -945       O  
ATOM   1817  NE2 GLN X  49      18.790   2.554  53.721  1.00 95.07           N  
ANISOU 1817  NE2 GLN X  49    12475  10743  12906    502    696  -1044       N  
ATOM   1818  N   GLU X  50      18.798   3.789  58.770  1.00 45.09           N  
ANISOU 1818  N   GLU X  50     5919   4545   6667    417    584   -783       N  
ATOM   1819  CA  GLU X  50      17.551   3.849  59.550  1.00 48.95           C  
ANISOU 1819  CA  GLU X  50     6433   5010   7156    300    579   -795       C  
ATOM   1820  C   GLU X  50      16.815   5.197  59.391  1.00 48.88           C  
ANISOU 1820  C   GLU X  50     6314   5113   7144    212    529   -830       C  
ATOM   1821  O   GLU X  50      15.601   5.232  59.167  1.00 52.70           O  
ANISOU 1821  O   GLU X  50     6800   5582   7643    106    534   -888       O  
ATOM   1822  CB  GLU X  50      17.820   3.514  61.030  1.00 60.42           C  
ANISOU 1822  CB  GLU X  50     7939   6426   8593    343    583   -709       C  
ATOM   1823  CG  GLU X  50      18.802   2.333  61.236  1.00 73.64           C  
ANISOU 1823  CG  GLU X  50     9711   8004  10263    470    617   -658       C  
ATOM   1824  CD  GLU X  50      20.293   2.749  61.312  1.00 79.87           C  
ANISOU 1824  CD  GLU X  50    10414   8877  11058    608    562   -602       C  
ATOM   1825  OE1 GLU X  50      20.732   3.120  62.424  1.00 82.43           O  
ANISOU 1825  OE1 GLU X  50    10716   9240  11363    655    502   -538       O  
ATOM   1826  OE2 GLU X  50      21.033   2.680  60.288  1.00 69.28           O  
ANISOU 1826  OE2 GLU X  50     9027   7555   9743    674    581   -621       O  
ATOM   1827  N   ILE X  51      17.564   6.297  59.473  1.00 50.17           N  
ANISOU 1827  N   ILE X  51     6378   5384   7299    257    479   -797       N  
ATOM   1828  CA  ILE X  51      17.027   7.598  59.117  1.00 45.95           C  
ANISOU 1828  CA  ILE X  51     5753   4948   6758    194    436   -832       C  
ATOM   1829  C   ILE X  51      16.456   7.514  57.724  1.00 47.20           C  
ANISOU 1829  C   ILE X  51     5924   5099   6912    158    448   -913       C  
ATOM   1830  O   ILE X  51      15.361   8.024  57.479  1.00 52.34           O  
ANISOU 1830  O   ILE X  51     6547   5779   7561     75    423   -965       O  
ATOM   1831  CB  ILE X  51      18.100   8.727  59.129  1.00 45.74           C  
ANISOU 1831  CB  ILE X  51     5626   5020   6735    250    390   -790       C  
ATOM   1832  CG1 ILE X  51      18.628   8.991  60.531  1.00 47.34           C  
ANISOU 1832  CG1 ILE X  51     5814   5240   6934    282    342   -722       C  
ATOM   1833  CG2 ILE X  51      17.542   9.995  58.574  1.00 32.42           C  
ANISOU 1833  CG2 ILE X  51     3871   3413   5036    192    360   -828       C  
ATOM   1834  CD1 ILE X  51      19.973   9.677  60.492  1.00 54.73           C  
ANISOU 1834  CD1 ILE X  51     6651   6242   7904    350    295   -680       C  
ATOM   1835  N   ILE X  52      17.185   6.888  56.798  1.00 46.02           N  
ANISOU 1835  N   ILE X  52     5819   4910   6756    230    482   -927       N  
ATOM   1836  CA  ILE X  52      16.697   6.828  55.410  1.00 52.44           C  
ANISOU 1836  CA  ILE X  52     6671   5712   7541    212    484  -1011       C  
ATOM   1837  C   ILE X  52      15.453   5.926  55.262  1.00 56.50           C  
ANISOU 1837  C   ILE X  52     7263   6135   8068    121    477  -1087       C  
ATOM   1838  O   ILE X  52      14.587   6.213  54.446  1.00 60.59           O  
ANISOU 1838  O   ILE X  52     7780   6670   8573     65    432  -1166       O  
ATOM   1839  CB  ILE X  52      17.812   6.538  54.342  1.00 55.24           C  
ANISOU 1839  CB  ILE X  52     7067   6053   7870    326    535  -1007       C  
ATOM   1840  CG1 ILE X  52      18.743   7.755  54.192  1.00 67.20           C  
ANISOU 1840  CG1 ILE X  52     8472   7673   9389    379    540   -950       C  
ATOM   1841  CG2 ILE X  52      17.191   6.240  52.957  1.00 38.42           C  
ANISOU 1841  CG2 ILE X  52     5030   3882   5685    316    532  -1105       C  
ATOM   1842  CD1 ILE X  52      18.190   8.941  53.252  1.00 38.69           C  
ANISOU 1842  CD1 ILE X  52     4834   4135   5732    343    511   -994       C  
ATOM   1843  N   HIS X  53      15.341   4.873  56.072  1.00 53.14           N  
ANISOU 1843  N   HIS X  53     6903   5612   7676    103    515  -1064       N  
ATOM   1844  CA  HIS X  53      14.110   4.079  56.074  1.00 64.77           C  
ANISOU 1844  CA  HIS X  53     8429   6991   9189     -9    515  -1129       C  
ATOM   1845  C   HIS X  53      12.928   4.941  56.526  1.00 64.47           C  
ANISOU 1845  C   HIS X  53     8286   7025   9184   -116    476  -1146       C  
ATOM   1846  O   HIS X  53      11.901   5.037  55.828  1.00 56.28           O  
ANISOU 1846  O   HIS X  53     7222   5991   8170   -197    428  -1233       O  
ATOM   1847  CB  HIS X  53      14.230   2.839  56.970  1.00 68.39           C  
ANISOU 1847  CB  HIS X  53     8986   7321   9679     -8    584  -1083       C  
ATOM   1848  CG  HIS X  53      15.103   1.771  56.400  1.00 82.71           C  
ANISOU 1848  CG  HIS X  53    10923   9033  11470     87    625  -1089       C  
ATOM   1849  ND1 HIS X  53      14.925   1.267  55.129  1.00 86.08           N  
ANISOU 1849  ND1 HIS X  53    11428   9400  11879     84    612  -1183       N  
ATOM   1850  CD2 HIS X  53      16.170   1.117  56.921  1.00 91.56           C  
ANISOU 1850  CD2 HIS X  53    12110  10100  12579    201    677  -1012       C  
ATOM   1851  CE1 HIS X  53      15.849   0.352  54.890  1.00 88.19           C  
ANISOU 1851  CE1 HIS X  53    11809   9577  12122    193    667  -1164       C  
ATOM   1852  NE2 HIS X  53      16.615   0.240  55.960  1.00 91.01           N  
ANISOU 1852  NE2 HIS X  53    12152   9939  12489    267    708  -1059       N  
ATOM   1853  N   SER X  54      13.088   5.558  57.699  1.00 60.19           N  
ANISOU 1853  N   SER X  54     7688   6538   8641   -107    492  -1066       N  
ATOM   1854  CA  SER X  54      12.099   6.480  58.255  1.00 54.65           C  
ANISOU 1854  CA  SER X  54     6893   5910   7962   -183    471  -1067       C  
ATOM   1855  C   SER X  54      11.672   7.507  57.211  1.00 53.75           C  
ANISOU 1855  C   SER X  54     6700   5892   7830   -196    397  -1133       C  
ATOM   1856  O   SER X  54      10.497   7.643  56.915  1.00 60.12           O  
ANISOU 1856  O   SER X  54     7455   6709   8678   -278    367  -1196       O  
ATOM   1857  CB  SER X  54      12.680   7.188  59.469  1.00 51.84           C  
ANISOU 1857  CB  SER X  54     6514   5611   7573   -131    482   -975       C  
ATOM   1858  OG  SER X  54      13.260   6.261  60.356  1.00 56.88           O  
ANISOU 1858  OG  SER X  54     7243   6163   8205    -88    536   -909       O  
ATOM   1859  N   LEU X  55      12.629   8.227  56.645  1.00 59.16           N  
ANISOU 1859  N   LEU X  55     7375   6645   8460   -111    371  -1116       N  
ATOM   1860  CA  LEU X  55      12.302   9.236  55.654  1.00 63.09           C  
ANISOU 1860  CA  LEU X  55     7823   7225   8924   -107    310  -1166       C  
ATOM   1861  C   LEU X  55      11.456   8.630  54.543  1.00 68.53           C  
ANISOU 1861  C   LEU X  55     8551   7868   9620   -151    267  -1269       C  
ATOM   1862  O   LEU X  55      10.532   9.261  54.038  1.00 75.58           O  
ANISOU 1862  O   LEU X  55     9391   8814  10513   -189    201  -1327       O  
ATOM   1863  CB  LEU X  55      13.573   9.856  55.073  1.00 57.50           C  
ANISOU 1863  CB  LEU X  55     7120   6564   8161     -9    316  -1128       C  
ATOM   1864  CG  LEU X  55      13.382  11.279  54.543  1.00 64.46           C  
ANISOU 1864  CG  LEU X  55     7944   7542   9005      2    272  -1136       C  
ATOM   1865  CD1 LEU X  55      12.480  12.111  55.481  1.00 59.48           C  
ANISOU 1865  CD1 LEU X  55     7236   6964   8400    -59    243  -1125       C  
ATOM   1866  CD2 LEU X  55      14.727  11.979  54.301  1.00 61.42           C  
ANISOU 1866  CD2 LEU X  55     7545   7198   8595     82    302  -1074       C  
ATOM   1867  N   LEU X  56      11.772   7.396  54.171  1.00 60.47           N  
ANISOU 1867  N   LEU X  56     7629   6745   8603   -141    295  -1297       N  
ATOM   1868  CA  LEU X  56      11.117   6.764  53.036  1.00 61.37           C  
ANISOU 1868  CA  LEU X  56     7807   6801   8711   -174    240  -1406       C  
ATOM   1869  C   LEU X  56       9.623   6.570  53.282  1.00 61.81           C  
ANISOU 1869  C   LEU X  56     7792   6839   8855   -305    189  -1471       C  
ATOM   1870  O   LEU X  56       8.821   6.860  52.391  1.00 56.44           O  
ANISOU 1870  O   LEU X  56     7088   6188   8169   -334     93  -1560       O  
ATOM   1871  CB  LEU X  56      11.801   5.439  52.675  1.00 72.70           C  
ANISOU 1871  CB  LEU X  56     9381   8111  10132   -132    288  -1421       C  
ATOM   1872  CG  LEU X  56      13.222   5.512  52.072  1.00 80.93           C  
ANISOU 1872  CG  LEU X  56    10495   9164  11092     10    340  -1378       C  
ATOM   1873  CD1 LEU X  56      13.832   4.129  51.793  1.00 79.23           C  
ANISOU 1873  CD1 LEU X  56    10422   8816  10867     62    398  -1392       C  
ATOM   1874  CD2 LEU X  56      13.256   6.372  50.820  1.00 76.95           C  
ANISOU 1874  CD2 LEU X  56    10005   8732  10501     66    291  -1424       C  
ATOM   1875  N   GLN X  57       9.252   6.085  54.473  1.00 57.03           N  
ANISOU 1875  N   GLN X  57     7152   6185   8332   -377    255  -1424       N  
ATOM   1876  CA  GLN X  57       7.839   5.993  54.854  1.00 65.10           C  
ANISOU 1876  CA  GLN X  57     8076   7197   9462   -505    236  -1467       C  
ATOM   1877  C   GLN X  57       7.174   7.366  54.835  1.00 66.64           C  
ANISOU 1877  C   GLN X  57     8138   7528   9654   -504    177  -1472       C  
ATOM   1878  O   GLN X  57       6.241   7.611  54.062  1.00 65.05           O  
ANISOU 1878  O   GLN X  57     7873   7360   9484   -548     80  -1561       O  
ATOM   1879  CB  GLN X  57       7.661   5.417  56.260  1.00 77.53           C  
ANISOU 1879  CB  GLN X  57     9645   8703  11109   -562    351  -1388       C  
ATOM   1880  CG  GLN X  57       8.701   4.412  56.687  1.00100.67           C  
ANISOU 1880  CG  GLN X  57    12715  11527  14009   -508    432  -1328       C  
ATOM   1881  CD  GLN X  57       8.717   4.236  58.193  1.00118.21           C  
ANISOU 1881  CD  GLN X  57    14943  13715  16255   -520    541  -1224       C  
ATOM   1882  OE1 GLN X  57       7.782   4.658  58.881  1.00125.75           O  
ANISOU 1882  OE1 GLN X  57    15806  14703  17270   -592    573  -1207       O  
ATOM   1883  NE2 GLN X  57       9.781   3.621  58.718  1.00120.13           N  
ANISOU 1883  NE2 GLN X  57    15301  13893  16449   -437    600  -1150       N  
ATOM   1884  N   LEU X  58       7.660   8.249  55.709  1.00 60.05           N  
ANISOU 1884  N   LEU X  58     7269   6767   8781   -450    229  -1378       N  
ATOM   1885  CA  LEU X  58       7.088   9.575  55.904  1.00 55.01           C  
ANISOU 1885  CA  LEU X  58     6521   6244   8137   -441    195  -1368       C  
ATOM   1886  C   LEU X  58       6.866  10.333  54.597  1.00 58.02           C  
ANISOU 1886  C   LEU X  58     6884   6697   8464   -398     81  -1440       C  
ATOM   1887  O   LEU X  58       5.840  10.977  54.434  1.00 58.82           O  
ANISOU 1887  O   LEU X  58     6885   6862   8603   -425     22  -1481       O  
ATOM   1888  CB  LEU X  58       7.961  10.381  56.870  1.00 55.75           C  
ANISOU 1888  CB  LEU X  58     6625   6387   8170   -370    251  -1265       C  
ATOM   1889  CG  LEU X  58       8.123   9.750  58.257  1.00 58.53           C  
ANISOU 1889  CG  LEU X  58     7012   6674   8552   -393    354  -1188       C  
ATOM   1890  CD1 LEU X  58       9.265  10.390  59.035  1.00 58.68           C  
ANISOU 1890  CD1 LEU X  58     7072   6730   8495   -308    375  -1100       C  
ATOM   1891  CD2 LEU X  58       6.835   9.806  59.061  1.00 57.19           C  
ANISOU 1891  CD2 LEU X  58     6759   6504   8466   -475    406  -1185       C  
ATOM   1892  N   VAL X  59       7.813  10.256  53.662  1.00 54.03           N  
ANISOU 1892  N   VAL X  59     6480   6180   7868   -321     56  -1453       N  
ATOM   1893  CA  VAL X  59       7.646  10.913  52.365  1.00 56.99           C  
ANISOU 1893  CA  VAL X  59     6874   6610   8169   -266    -42  -1517       C  
ATOM   1894  C   VAL X  59       6.568  10.241  51.517  1.00 58.46           C  
ANISOU 1894  C   VAL X  59     7055   6757   8398   -329   -147  -1638       C  
ATOM   1895  O   VAL X  59       5.870  10.896  50.752  1.00 64.36           O  
ANISOU 1895  O   VAL X  59     7767   7566   9119   -309   -255  -1699       O  
ATOM   1896  CB  VAL X  59       8.967  10.994  51.583  1.00 64.30           C  
ANISOU 1896  CB  VAL X  59     7921   7527   8985   -160    -15  -1491       C  
ATOM   1897  CG1 VAL X  59       8.725  11.474  50.163  1.00 53.81           C  
ANISOU 1897  CG1 VAL X  59     6651   6230   7563    -99   -107  -1562       C  
ATOM   1898  CG2 VAL X  59       9.935  11.936  52.292  1.00 62.40           C  
ANISOU 1898  CG2 VAL X  59     7651   7342   8716   -105     56  -1383       C  
ATOM   1899  N   GLY X  60       6.423   8.928  51.660  1.00 62.27           N  
ANISOU 1899  N   GLY X  60     7578   7132   8950   -404   -125  -1675       N  
ATOM   1900  CA  GLY X  60       5.310   8.228  51.038  1.00 70.00           C  
ANISOU 1900  CA  GLY X  60     8531   8061  10004   -493   -231  -1795       C  
ATOM   1901  C   GLY X  60       3.972   8.718  51.570  1.00 69.25           C  
ANISOU 1901  C   GLY X  60     8249   8029  10033   -579   -271  -1813       C  
ATOM   1902  O   GLY X  60       3.071   9.066  50.814  1.00 68.50           O  
ANISOU 1902  O   GLY X  60     8087   7982   9958   -591   -407  -1901       O  
ATOM   1903  N   ASP X  61       3.861   8.743  52.892  1.00 67.87           N  
ANISOU 1903  N   ASP X  61     7995   7854   9940   -628   -148  -1726       N  
ATOM   1904  CA  ASP X  61       2.710   9.301  53.586  1.00 60.40           C  
ANISOU 1904  CA  ASP X  61     6870   6971   9107   -690   -139  -1716       C  
ATOM   1905  C   ASP X  61       2.420  10.734  53.118  1.00 61.25           C  
ANISOU 1905  C   ASP X  61     6911   7212   9147   -601   -227  -1723       C  
ATOM   1906  O   ASP X  61       1.295  11.061  52.739  1.00 53.79           O  
ANISOU 1906  O   ASP X  61     5839   6321   8278   -631   -326  -1792       O  
ATOM   1907  CB  ASP X  61       2.970   9.267  55.088  1.00 57.95           C  
ANISOU 1907  CB  ASP X  61     6545   6641   8832   -709     28  -1599       C  
ATOM   1908  CG  ASP X  61       1.719   9.452  55.899  1.00 74.78           C  
ANISOU 1908  CG  ASP X  61     8508   8798  11106   -793     81  -1589       C  
ATOM   1909  OD1 ASP X  61       0.668   9.836  55.326  1.00 83.17           O  
ANISOU 1909  OD1 ASP X  61     9434   9921  12244   -822    -21  -1665       O  
ATOM   1910  OD2 ASP X  61       1.791   9.205  57.121  1.00 78.85           O  
ANISOU 1910  OD2 ASP X  61     9030   9272  11656   -820    227  -1501       O  
ATOM   1911  N   PHE X  62       3.437  11.587  53.138  1.00 54.26           N  
ANISOU 1911  N   PHE X  62     6110   6377   8129   -490   -193  -1652       N  
ATOM   1912  CA  PHE X  62       3.282  12.939  52.627  1.00 60.76           C  
ANISOU 1912  CA  PHE X  62     6905   7307   8875   -398   -268  -1654       C  
ATOM   1913  C   PHE X  62       2.714  12.921  51.197  1.00 68.01           C  
ANISOU 1913  C   PHE X  62     7838   8243   9760   -374   -434  -1768       C  
ATOM   1914  O   PHE X  62       1.741  13.620  50.873  1.00 66.50           O  
ANISOU 1914  O   PHE X  62     7543   8126   9598   -356   -533  -1812       O  
ATOM   1915  CB  PHE X  62       4.636  13.656  52.651  1.00 55.56           C  
ANISOU 1915  CB  PHE X  62     6361   6668   8081   -296   -209  -1570       C  
ATOM   1916  CG  PHE X  62       4.581  15.058  52.140  1.00 61.06           C  
ANISOU 1916  CG  PHE X  62     7053   7454   8692   -203   -266  -1561       C  
ATOM   1917  CD1 PHE X  62       4.408  16.118  53.009  1.00 58.88           C  
ANISOU 1917  CD1 PHE X  62     6711   7236   8424   -180   -218  -1496       C  
ATOM   1918  CD2 PHE X  62       4.684  15.321  50.785  1.00 68.48           C  
ANISOU 1918  CD2 PHE X  62     8076   8409   9534   -130   -365  -1616       C  
ATOM   1919  CE1 PHE X  62       4.347  17.420  52.541  1.00 55.71           C  
ANISOU 1919  CE1 PHE X  62     6321   6903   7945    -91   -266  -1485       C  
ATOM   1920  CE2 PHE X  62       4.624  16.626  50.311  1.00 62.66           C  
ANISOU 1920  CE2 PHE X  62     7354   7742   8712    -36   -409  -1599       C  
ATOM   1921  CZ  PHE X  62       4.446  17.673  51.199  1.00 54.01           C  
ANISOU 1921  CZ  PHE X  62     6184   6699   7637    -21   -360  -1533       C  
ATOM   1922  N   ASN X  63       3.340  12.103  50.356  1.00 67.46           N  
ANISOU 1922  N   ASN X  63     7909   8100   9624   -361   -468  -1815       N  
ATOM   1923  CA  ASN X  63       3.002  11.993  48.942  1.00 66.22           C  
ANISOU 1923  CA  ASN X  63     7823   7942   9397   -320   -627  -1926       C  
ATOM   1924  C   ASN X  63       1.539  11.663  48.669  1.00 71.17           C  
ANISOU 1924  C   ASN X  63     8311   8579  10153   -407   -771  -2037       C  
ATOM   1925  O   ASN X  63       0.909  12.292  47.817  1.00 78.21           O  
ANISOU 1925  O   ASN X  63     9181   9535  11000   -347   -923  -2104       O  
ATOM   1926  CB  ASN X  63       3.890  10.947  48.278  1.00 72.35           C  
ANISOU 1926  CB  ASN X  63     8780   8613  10095   -305   -611  -1958       C  
ATOM   1927  CG  ASN X  63       5.268  11.478  47.949  1.00 75.23           C  
ANISOU 1927  CG  ASN X  63     9289   8990  10305   -178   -523  -1878       C  
ATOM   1928  OD1 ASN X  63       5.461  12.687  47.747  1.00 68.78           O  
ANISOU 1928  OD1 ASN X  63     8470   8255   9407    -91   -525  -1830       O  
ATOM   1929  ND2 ASN X  63       6.242  10.571  47.886  1.00 75.01           N  
ANISOU 1929  ND2 ASN X  63     9385   8873  10244   -167   -438  -1860       N  
ATOM   1930  N   GLN X  64       0.999  10.673  49.372  1.00 68.44           N  
ANISOU 1930  N   GLN X  64     7871   8164   9972   -546   -728  -2057       N  
ATOM   1931  CA  GLN X  64      -0.427  10.393  49.269  1.00 70.40           C  
ANISOU 1931  CA  GLN X  64     7941   8422  10385   -649   -847  -2153       C  
ATOM   1932  C   GLN X  64      -1.260  11.640  49.664  1.00 80.05           C  
ANISOU 1932  C   GLN X  64     8980   9776  11659   -607   -867  -2119       C  
ATOM   1933  O   GLN X  64      -2.079  12.116  48.872  1.00 82.98           O  
ANISOU 1933  O   GLN X  64     9277  10215  12037   -569  -1040  -2202       O  
ATOM   1934  CB  GLN X  64      -0.788   9.179  50.125  1.00 75.99           C  
ANISOU 1934  CB  GLN X  64     8575   9023  11274   -813   -749  -2153       C  
ATOM   1935  CG  GLN X  64      -0.999   9.522  51.589  1.00 98.92           C  
ANISOU 1935  CG  GLN X  64    11347  11958  14281   -854   -568  -2036       C  
ATOM   1936  CD  GLN X  64      -0.934   8.312  52.497  1.00111.63           C  
ANISOU 1936  CD  GLN X  64    12966  13440  16010   -983   -420  -1999       C  
ATOM   1937  OE1 GLN X  64      -0.569   7.216  52.061  1.00112.43           O  
ANISOU 1937  OE1 GLN X  64    13189  13422  16107  -1035   -441  -2052       O  
ATOM   1938  NE2 GLN X  64      -1.281   8.505  53.773  1.00110.88           N  
ANISOU 1938  NE2 GLN X  64    12760  13359  16011  -1026   -261  -1904       N  
ATOM   1939  N   ARG X  65      -1.013  12.186  50.863  1.00 71.88           N  
ANISOU 1939  N   ARG X  65     7890   8774  10645   -598   -696  -1999       N  
ATOM   1940  CA  ARG X  65      -1.800  13.300  51.404  1.00 63.35           C  
ANISOU 1940  CA  ARG X  65     6646   7803   9623   -559   -683  -1959       C  
ATOM   1941  C   ARG X  65      -1.701  14.466  50.458  1.00 67.79           C  
ANISOU 1941  C   ARG X  65     7267   8453  10035   -410   -810  -1977       C  
ATOM   1942  O   ARG X  65      -2.612  15.273  50.330  1.00 66.73           O  
ANISOU 1942  O   ARG X  65     7001   8408   9945   -363   -891  -1999       O  
ATOM   1943  CB  ARG X  65      -1.361  13.665  52.833  1.00 48.63           C  
ANISOU 1943  CB  ARG X  65     4772   5940   7765   -558   -475  -1827       C  
ATOM   1944  CG  ARG X  65      -1.169  12.405  53.710  1.00 55.02           C  
ANISOU 1944  CG  ARG X  65     5595   6638   8674   -683   -335  -1794       C  
ATOM   1945  CD  ARG X  65      -0.670  12.666  55.121  1.00 60.81           C  
ANISOU 1945  CD  ARG X  65     6355   7361   9390   -671   -142  -1667       C  
ATOM   1946  NE  ARG X  65      -1.758  13.100  55.994  1.00 76.35           N  
ANISOU 1946  NE  ARG X  65     8147   9378  11486   -701    -63  -1637       N  
ATOM   1947  CZ  ARG X  65      -2.120  12.481  57.111  1.00 74.52           C  
ANISOU 1947  CZ  ARG X  65     7861   9086  11366   -788     97  -1582       C  
ATOM   1948  NH1 ARG X  65      -1.476  11.401  57.524  1.00 64.99           N  
ANISOU 1948  NH1 ARG X  65     6770   7766  10157   -852    187  -1549       N  
ATOM   1949  NH2 ARG X  65      -3.131  12.952  57.816  1.00 82.51           N  
ANISOU 1949  NH2 ARG X  65     8711  10149  12490   -800    178  -1554       N  
ATOM   1950  N   PHE X  66      -0.584  14.513  49.761  1.00 70.05           N  
ANISOU 1950  N   PHE X  66     7759   8709  10146   -331   -820  -1966       N  
ATOM   1951  CA  PHE X  66      -0.338  15.535  48.769  1.00 81.90           C  
ANISOU 1951  CA  PHE X  66     9362  10272  11485   -187   -921  -1975       C  
ATOM   1952  C   PHE X  66      -1.150  15.285  47.490  1.00 83.73           C  
ANISOU 1952  C   PHE X  66     9592  10517  11705   -165  -1145  -2110       C  
ATOM   1953  O   PHE X  66      -1.831  16.184  46.994  1.00 80.62           O  
ANISOU 1953  O   PHE X  66     9146  10206  11281    -75  -1267  -2138       O  
ATOM   1954  CB  PHE X  66       1.157  15.566  48.468  1.00 94.63           C  
ANISOU 1954  CB  PHE X  66    11189  11836  12930   -119   -832  -1913       C  
ATOM   1955  CG  PHE X  66       1.521  16.430  47.307  1.00108.73           C  
ANISOU 1955  CG  PHE X  66    13117  13657  14538     25   -916  -1921       C  
ATOM   1956  CD1 PHE X  66       1.854  17.765  47.502  1.00112.35           C  
ANISOU 1956  CD1 PHE X  66    13598  14174  14917    121   -859  -1835       C  
ATOM   1957  CD2 PHE X  66       1.530  15.911  46.017  1.00111.48           C  
ANISOU 1957  CD2 PHE X  66    13597  13969  14789     67  -1046  -2016       C  
ATOM   1958  CE1 PHE X  66       2.186  18.571  46.437  1.00117.97           C  
ANISOU 1958  CE1 PHE X  66    14454  14905  15463    253   -918  -1833       C  
ATOM   1959  CE2 PHE X  66       1.866  16.706  44.940  1.00116.69           C  
ANISOU 1959  CE2 PHE X  66    14414  14655  15269    211  -1109  -2016       C  
ATOM   1960  CZ  PHE X  66       2.194  18.043  45.146  1.00121.68           C  
ANISOU 1960  CZ  PHE X  66    15061  15342  15829    304  -1038  -1919       C  
ATOM   1961  N   SER X  67      -1.068  14.059  46.967  1.00 84.55           N  
ANISOU 1961  N   SER X  67     9766  10533  11828   -240  -1206  -2195       N  
ATOM   1962  CA  SER X  67      -1.837  13.622  45.794  1.00 85.71           C  
ANISOU 1962  CA  SER X  67     9923  10671  11972   -240  -1437  -2342       C  
ATOM   1963  C   SER X  67      -3.328  13.880  45.945  1.00 95.59           C  
ANISOU 1963  C   SER X  67    10919  11999  13401   -288  -1571  -2407       C  
ATOM   1964  O   SER X  67      -3.982  14.421  45.053  1.00 93.70           O  
ANISOU 1964  O   SER X  67    10665  11825  13113   -199  -1769  -2483       O  
ATOM   1965  CB  SER X  67      -1.666  12.119  45.594  1.00 82.23           C  
ANISOU 1965  CB  SER X  67     9553  10104  11587   -360  -1452  -2421       C  
ATOM   1966  OG  SER X  67      -0.306  11.767  45.477  1.00 84.61           O  
ANISOU 1966  OG  SER X  67    10075  10331  11742   -312  -1322  -2363       O  
ATOM   1967  N   GLN X  68      -3.852  13.453  47.087  1.00104.21           N  
ANISOU 1967  N   GLN X  68    11813  13078  14704   -425  -1455  -2374       N  
ATOM   1968  CA  GLN X  68      -5.266  13.567  47.399  1.00106.03           C  
ANISOU 1968  CA  GLN X  68    11764  13372  15148   -494  -1538  -2424       C  
ATOM   1969  C   GLN X  68      -5.869  14.934  47.102  1.00109.07           C  
ANISOU 1969  C   GLN X  68    12063  13891  15488   -346  -1639  -2414       C  
ATOM   1970  O   GLN X  68      -7.089  15.052  46.997  1.00117.57           O  
ANISOU 1970  O   GLN X  68    12916  15031  16723   -370  -1772  -2484       O  
ATOM   1971  CB  GLN X  68      -5.502  13.235  48.867  1.00109.01           C  
ANISOU 1971  CB  GLN X  68    11978  13725  15714   -620  -1318  -2336       C  
ATOM   1972  CG  GLN X  68      -6.920  13.516  49.304  1.00116.92           C  
ANISOU 1972  CG  GLN X  68    12676  14805  16944   -672  -1355  -2362       C  
ATOM   1973  CD  GLN X  68      -7.021  13.900  50.762  1.00120.58           C  
ANISOU 1973  CD  GLN X  68    13023  15291  17501   -696  -1107  -2231       C  
ATOM   1974  OE1 GLN X  68      -6.014  14.169  51.420  1.00121.51           O  
ANISOU 1974  OE1 GLN X  68    13297  15383  17488   -650   -934  -2121       O  
ATOM   1975  NE2 GLN X  68      -8.244  13.931  51.278  1.00122.25           N  
ANISOU 1975  NE2 GLN X  68    12959  15549  17940   -763  -1089  -2244       N  
ATOM   1976  N   THR X  69      -5.037  15.967  46.980  1.00104.00           N  
ANISOU 1976  N   THR X  69    11588  13287  14642   -194  -1575  -2326       N  
ATOM   1977  CA  THR X  69      -5.551  17.313  46.712  1.00105.44           C  
ANISOU 1977  CA  THR X  69    11717  13580  14764    -41  -1656  -2307       C  
ATOM   1978  C   THR X  69      -4.721  18.122  45.721  1.00108.68           C  
ANISOU 1978  C   THR X  69    12386  14000  14909    132  -1714  -2285       C  
ATOM   1979  O   THR X  69      -5.152  19.191  45.292  1.00117.00           O  
ANISOU 1979  O   THR X  69    13432  15131  15890    273  -1810  -2281       O  
ATOM   1980  CB  THR X  69      -5.716  18.152  48.006  1.00 81.84           C  
ANISOU 1980  CB  THR X  69     8596  10646  11855    -28  -1464  -2187       C  
ATOM   1981  OG1 THR X  69      -4.529  18.055  48.798  1.00 81.50           O  
ANISOU 1981  OG1 THR X  69     8693  10538  11736    -59  -1247  -2080       O  
ATOM   1982  CG2 THR X  69      -6.907  17.666  48.831  1.00 79.75           C  
ANISOU 1982  CG2 THR X  69     8037  10404  11862   -154  -1433  -2212       C  
ATOM   1983  N   HIS X  70      -3.540  17.632  45.357  1.00107.17           N  
ANISOU 1983  N   HIS X  70    12423  13725  14573    130  -1646  -2267       N  
ATOM   1984  CA  HIS X  70      -2.661  18.392  44.461  1.00106.92           C  
ANISOU 1984  CA  HIS X  70    12641  13690  14293    289  -1657  -2229       C  
ATOM   1985  C   HIS X  70      -1.980  17.526  43.399  1.00111.50           C  
ANISOU 1985  C   HIS X  70    13445  14187  14735    300  -1724  -2298       C  
ATOM   1986  O   HIS X  70      -1.922  16.298  43.528  1.00111.54           O  
ANISOU 1986  O   HIS X  70    13435  14117  14827    174  -1718  -2356       O  
ATOM   1987  CB  HIS X  70      -1.598  19.164  45.253  1.00101.96           C  
ANISOU 1987  CB  HIS X  70    12090  13054  13594    324  -1429  -2081       C  
ATOM   1988  CG  HIS X  70      -2.154  20.173  46.205  1.00104.08           C  
ANISOU 1988  CG  HIS X  70    12198  13396  13951    346  -1360  -2010       C  
ATOM   1989  ND1 HIS X  70      -2.729  21.364  45.784  1.00108.45           N  
ANISOU 1989  ND1 HIS X  70    12744  14022  14439    488  -1453  -2004       N  
ATOM   1990  CD2 HIS X  70      -2.213  20.200  47.557  1.00100.08           C  
ANISOU 1990  CD2 HIS X  70    11554  12893  13576    261  -1201  -1940       C  
ATOM   1991  CE1 HIS X  70      -3.120  22.055  46.830  1.00108.20           C  
ANISOU 1991  CE1 HIS X  70    12572  14035  14504    485  -1353  -1938       C  
ATOM   1992  NE2 HIS X  70      -2.814  21.374  47.928  1.00100.53           N  
ANISOU 1992  NE2 HIS X  70    11525  13024  13649    349  -1197  -1898       N  
ATOM   1993  N   GLU X  71      -1.461  18.183  42.360  1.00112.30           N  
ANISOU 1993  N   GLU X  71    13767  14290  14613    459  -1773  -2287       N  
ATOM   1994  CA  GLU X  71      -0.763  17.508  41.265  1.00115.28           C  
ANISOU 1994  CA  GLU X  71    14393  14586  14820    507  -1819  -2344       C  
ATOM   1995  C   GLU X  71       0.622  18.097  41.001  1.00119.88           C  
ANISOU 1995  C   GLU X  71    15203  15135  15213    613  -1636  -2227       C  
ATOM   1996  O   GLU X  71       0.858  19.288  41.209  1.00117.76           O  
ANISOU 1996  O   GLU X  71    14943  14912  14887    698  -1554  -2127       O  
ATOM   1997  CB  GLU X  71      -1.596  17.550  39.981  1.00112.54           C  
ANISOU 1997  CB  GLU X  71    14128  14263  14370    609  -2094  -2474       C  
ATOM   1998  CG  GLU X  71      -2.722  16.534  39.934  1.00114.16           C  
ANISOU 1998  CG  GLU X  71    14162  14461  14751    483  -2296  -2624       C  
ATOM   1999  CD  GLU X  71      -3.691  16.797  38.798  1.00125.17           C  
ANISOU 1999  CD  GLU X  71    15589  15903  16066    594  -2600  -2751       C  
ATOM   2000  OE1 GLU X  71      -3.801  17.963  38.359  1.00126.28           O  
ANISOU 2000  OE1 GLU X  71    15799  16111  16069    763  -2648  -2705       O  
ATOM   2001  OE2 GLU X  71      -4.351  15.835  38.347  1.00133.30           O  
ANISOU 2001  OE2 GLU X  71    16580  16896  17172    513  -2799  -2899       O  
ATOM   2002  N   ILE X  72       1.526  17.246  40.526  1.00122.92           N  
ANISOU 2002  N   ILE X  72    15766  15430  15507    607  -1569  -2241       N  
ATOM   2003  CA  ILE X  72       2.907  17.632  40.252  1.00121.84           C  
ANISOU 2003  CA  ILE X  72    15827  15251  15214    696  -1379  -2132       C  
ATOM   2004  C   ILE X  72       3.037  18.714  39.179  1.00127.89           C  
ANISOU 2004  C   ILE X  72    16789  16040  15765    882  -1421  -2104       C  
ATOM   2005  O   ILE X  72       3.898  19.590  39.280  1.00125.17           O  
ANISOU 2005  O   ILE X  72    16518  15694  15347    946  -1252  -1980       O  
ATOM   2006  CB  ILE X  72       3.749  16.405  39.827  1.00120.53           C  
ANISOU 2006  CB  ILE X  72    15820  14983  14993    672  -1313  -2167       C  
ATOM   2007  CG1 ILE X  72       3.978  15.472  41.022  1.00118.76           C  
ANISOU 2007  CG1 ILE X  72    15436  14722  14964    505  -1201  -2147       C  
ATOM   2008  CG2 ILE X  72       5.071  16.843  39.201  1.00119.18           C  
ANISOU 2008  CG2 ILE X  72    15874  14772  14637    799  -1141  -2071       C  
ATOM   2009  CD1 ILE X  72       4.727  14.204  40.685  1.00117.69           C  
ANISOU 2009  CD1 ILE X  72    15445  14479  14792    482  -1140  -2185       C  
ATOM   2010  N   GLU X  73       2.181  18.656  38.158  1.00134.94           N  
ANISOU 2010  N   GLU X  73    17768  16947  16557    967  -1649  -2218       N  
ATOM   2011  CA  GLU X  73       2.354  19.492  36.964  1.00136.64           C  
ANISOU 2011  CA  GLU X  73    18230  17160  16526   1164  -1697  -2202       C  
ATOM   2012  C   GLU X  73       2.088  20.979  37.190  1.00131.64           C  
ANISOU 2012  C   GLU X  73    17549  16598  15872   1253  -1674  -2107       C  
ATOM   2013  O   GLU X  73       2.923  21.822  36.852  1.00130.00           O  
ANISOU 2013  O   GLU X  73    17510  16364  15521   1358  -1523  -1997       O  
ATOM   2014  CB  GLU X  73       1.506  18.978  35.796  1.00142.42           C  
ANISOU 2014  CB  GLU X  73    19089  17883  17140   1242  -1973  -2360       C  
ATOM   2015  CG  GLU X  73       1.871  19.613  34.459  1.00147.01           C  
ANISOU 2015  CG  GLU X  73    19997  18436  17424   1460  -2001  -2344       C  
ATOM   2016  CD  GLU X  73       3.318  19.364  34.073  1.00150.50           C  
ANISOU 2016  CD  GLU X  73    20675  18786  17722   1509  -1752  -2258       C  
ATOM   2017  OE1 GLU X  73       3.874  18.316  34.471  1.00149.21           O  
ANISOU 2017  OE1 GLU X  73    20475  18567  17651   1393  -1651  -2274       O  
ATOM   2018  OE2 GLU X  73       3.901  20.215  33.370  1.00154.23           O  
ANISOU 2018  OE2 GLU X  73    21368  19238  17994   1668  -1650  -2169       O  
ATOM   2019  N   PRO X  74       0.917  21.308  37.747  1.00127.35           N  
ANISOU 2019  N   PRO X  74    16777  16136  15475   1213  -1818  -2150       N  
ATOM   2020  CA  PRO X  74       0.638  22.712  38.054  1.00122.65           C  
ANISOU 2020  CA  PRO X  74    16131  15600  14869   1300  -1788  -2060       C  
ATOM   2021  C   PRO X  74       1.789  23.295  38.865  1.00115.79           C  
ANISOU 2021  C   PRO X  74    15270  14700  14027   1256  -1508  -1907       C  
ATOM   2022  O   PRO X  74       2.320  24.352  38.517  1.00112.15           O  
ANISOU 2022  O   PRO X  74    14961  14220  13432   1370  -1412  -1811       O  
ATOM   2023  CB  PRO X  74      -0.632  22.632  38.899  1.00122.71           C  
ANISOU 2023  CB  PRO X  74    15832  15691  15102   1207  -1919  -2122       C  
ATOM   2024  CG  PRO X  74      -1.294  21.371  38.460  1.00125.20           C  
ANISOU 2024  CG  PRO X  74    16095  15996  15478   1134  -2115  -2276       C  
ATOM   2025  CD  PRO X  74      -0.181  20.416  38.155  1.00127.16           C  
ANISOU 2025  CD  PRO X  74    16524  16146  15645   1084  -1993  -2275       C  
ATOM   2026  N   VAL X  75       2.178  22.583  39.920  1.00113.43           N  
ANISOU 2026  N   VAL X  75    14813  14385  13899   1090  -1386  -1888       N  
ATOM   2027  CA  VAL X  75       3.298  22.972  40.778  1.00110.37           C  
ANISOU 2027  CA  VAL X  75    14411  13966  13558   1031  -1143  -1758       C  
ATOM   2028  C   VAL X  75       4.620  23.134  40.008  1.00104.44           C  
ANISOU 2028  C   VAL X  75    13901  13141  12639   1109   -990  -1682       C  
ATOM   2029  O   VAL X  75       5.425  24.010  40.326  1.00 93.23           O  
ANISOU 2029  O   VAL X  75    12517  11701  11204   1125   -825  -1565       O  
ATOM   2030  CB  VAL X  75       3.487  21.949  41.930  1.00 93.13           C  
ANISOU 2030  CB  VAL X  75    12047  11772  11567    852  -1064  -1766       C  
ATOM   2031  CG1 VAL X  75       4.366  22.519  43.026  1.00 83.49           C  
ANISOU 2031  CG1 VAL X  75    10764  10540  10419    793   -863  -1642       C  
ATOM   2032  CG2 VAL X  75       2.135  21.537  42.496  1.00 95.18           C  
ANISOU 2032  CG2 VAL X  75    12084  12090  11991    772  -1212  -1856       C  
ATOM   2033  N   ALA X  76       4.838  22.296  38.996  1.00105.41           N  
ANISOU 2033  N   ALA X  76    14190  13219  12643   1158  -1040  -1749       N  
ATOM   2034  CA  ALA X  76       6.063  22.362  38.199  1.00104.54           C  
ANISOU 2034  CA  ALA X  76    14313  13035  12371   1244   -879  -1679       C  
ATOM   2035  C   ALA X  76       6.092  23.569  37.256  1.00113.90           C  
ANISOU 2035  C   ALA X  76    15704  14213  13361   1417   -874  -1621       C  
ATOM   2036  O   ALA X  76       7.059  24.332  37.235  1.00111.78           O  
ANISOU 2036  O   ALA X  76    15522  13904  13047   1452   -677  -1497       O  
ATOM   2037  CB  ALA X  76       6.264  21.068  37.421  1.00 95.99           C  
ANISOU 2037  CB  ALA X  76    13365  11897  11211   1256   -925  -1772       C  
ATOM   2038  N   GLN X  77       5.028  23.739  36.480  1.00127.14           N  
ANISOU 2038  N   GLN X  77    17457  15923  14929   1526  -1095  -1711       N  
ATOM   2039  CA  GLN X  77       4.960  24.819  35.504  1.00141.34           C  
ANISOU 2039  CA  GLN X  77    19479  17707  16516   1713  -1113  -1663       C  
ATOM   2040  C   GLN X  77       4.805  26.192  36.145  1.00146.95           C  
ANISOU 2040  C   GLN X  77    20103  18448  17284   1727  -1051  -1562       C  
ATOM   2041  O   GLN X  77       5.245  27.195  35.580  1.00151.05           O  
ANISOU 2041  O   GLN X  77    20813  18922  17656   1850   -950  -1466       O  
ATOM   2042  CB  GLN X  77       3.811  24.585  34.535  1.00151.77           C  
ANISOU 2042  CB  GLN X  77    20898  19059  17707   1833  -1400  -1797       C  
ATOM   2043  CG  GLN X  77       3.974  23.356  33.685  1.00161.21           C  
ANISOU 2043  CG  GLN X  77    22253  20204  18794   1852  -1476  -1903       C  
ATOM   2044  CD  GLN X  77       2.833  23.204  32.716  1.00171.07           C  
ANISOU 2044  CD  GLN X  77    23607  21482  19908   1975  -1786  -2043       C  
ATOM   2045  OE1 GLN X  77       1.925  24.037  32.680  1.00173.86           O  
ANISOU 2045  OE1 GLN X  77    23903  21901  20256   2054  -1942  -2053       O  
ATOM   2046  NE2 GLN X  77       2.866  22.142  31.920  1.00174.89           N  
ANISOU 2046  NE2 GLN X  77    24253  21916  20284   2000  -1889  -2156       N  
ATOM   2047  N   SER X  78       4.162  26.242  37.310  1.00144.80           N  
ANISOU 2047  N   SER X  78    19559  18241  17219   1609  -1104  -1581       N  
ATOM   2048  CA  SER X  78       4.063  27.488  38.062  1.00139.57           C  
ANISOU 2048  CA  SER X  78    18811  17597  16624   1611  -1030  -1489       C  
ATOM   2049  C   SER X  78       5.469  28.035  38.179  1.00137.25           C  
ANISOU 2049  C   SER X  78    18626  17222  16299   1590   -767  -1351       C  
ATOM   2050  O   SER X  78       5.686  29.166  38.614  1.00136.09           O  
ANISOU 2050  O   SER X  78    18479  17057  16173   1602   -669  -1257       O  
ATOM   2051  CB  SER X  78       3.501  27.236  39.459  1.00133.50           C  
ANISOU 2051  CB  SER X  78    17741  16890  16093   1458  -1055  -1516       C  
ATOM   2052  OG  SER X  78       4.467  26.606  40.286  1.00125.35           O  
ANISOU 2052  OG  SER X  78    16622  15825  15182   1306   -885  -1474       O  
ATOM   2053  N   LEU X  79       6.418  27.199  37.774  1.00133.76           N  
ANISOU 2053  N   LEU X  79    18277  16729  15819   1559   -656  -1344       N  
ATOM   2054  CA  LEU X  79       7.833  27.511  37.835  1.00128.72           C  
ANISOU 2054  CA  LEU X  79    17715  16016  15177   1528   -401  -1221       C  
ATOM   2055  C   LEU X  79       8.513  27.252  36.488  1.00136.30           C  
ANISOU 2055  C   LEU X  79    18948  16907  15933   1653   -317  -1201       C  
ATOM   2056  O   LEU X  79       9.713  27.477  36.334  1.00138.07           O  
ANISOU 2056  O   LEU X  79    19254  17064  16143   1647    -90  -1096       O  
ATOM   2057  CB  LEU X  79       8.474  26.666  38.933  1.00114.79           C  
ANISOU 2057  CB  LEU X  79    15747  14258  13611   1351   -307  -1218       C  
ATOM   2058  CG  LEU X  79       9.971  26.784  39.201  1.00109.90           C  
ANISOU 2058  CG  LEU X  79    15137  13576  13046   1289    -61  -1103       C  
ATOM   2059  CD1 LEU X  79      10.546  28.106  38.725  1.00106.79           C  
ANISOU 2059  CD1 LEU X  79    14893  13121  12562   1370     81   -985       C  
ATOM   2060  CD2 LEU X  79      10.213  26.576  40.694  1.00113.67           C  
ANISOU 2060  CD2 LEU X  79    15366  14082  13743   1123    -26  -1089       C  
ATOM   2061  N   GLY X  80       7.742  26.790  35.508  1.00137.85           N  
ANISOU 2061  N   GLY X  80    19287  17118  15973   1771   -499  -1303       N  
ATOM   2062  CA  GLY X  80       8.305  26.443  34.216  1.00136.45           C  
ANISOU 2062  CA  GLY X  80    19395  16872  15578   1904   -432  -1298       C  
ATOM   2063  C   GLY X  80       9.567  25.626  34.413  1.00134.28           C  
ANISOU 2063  C   GLY X  80    19099  16547  15376   1815   -216  -1253       C  
ATOM   2064  O   GLY X  80      10.678  26.107  34.178  1.00130.92           O  
ANISOU 2064  O   GLY X  80    18772  16056  14916   1842     26  -1129       O  
ATOM   2065  N   ILE X  81       9.387  24.385  34.859  1.00137.81           N  
ANISOU 2065  N   ILE X  81    19407  17019  15934   1710   -302  -1352       N  
ATOM   2066  CA  ILE X  81      10.502  23.502  35.196  1.00139.90           C  
ANISOU 2066  CA  ILE X  81    19617  17243  16293   1623   -120  -1319       C  
ATOM   2067  C   ILE X  81      10.477  22.226  34.382  1.00142.92           C  
ANISOU 2067  C   ILE X  81    20153  17588  16562   1679   -186  -1425       C  
ATOM   2068  O   ILE X  81      11.522  21.699  33.993  1.00139.30           O  
ANISOU 2068  O   ILE X  81    19803  17067  16058   1712      0  -1381       O  
ATOM   2069  CB  ILE X  81      10.425  23.043  36.648  1.00138.31           C  
ANISOU 2069  CB  ILE X  81    19112  17091  16349   1434   -140  -1335       C  
ATOM   2070  CG1 ILE X  81      10.347  24.239  37.589  1.00142.95           C  
ANISOU 2070  CG1 ILE X  81    19542  17715  17058   1369   -102  -1249       C  
ATOM   2071  CG2 ILE X  81      11.607  22.143  36.976  1.00134.72           C  
ANISOU 2071  CG2 ILE X  81    18610  16593  15985   1364     40  -1296       C  
ATOM   2072  CD1 ILE X  81      10.095  23.840  39.029  1.00145.87           C  
ANISOU 2072  CD1 ILE X  81    19635  18135  17654   1201   -145  -1273       C  
ATOM   2073  N   ASP X  82       9.276  21.703  34.172  1.00151.63           N  
ANISOU 2073  N   ASP X  82    21250  18727  17635   1684   -451  -1570       N  
ATOM   2074  CA  ASP X  82       9.119  20.510  33.363  1.00163.85           C  
ANISOU 2074  CA  ASP X  82    22962  20229  19067   1735   -553  -1692       C  
ATOM   2075  C   ASP X  82       9.500  20.847  31.934  1.00173.50           C  
ANISOU 2075  C   ASP X  82    24536  21387  20000   1943   -491  -1667       C  
ATOM   2076  O   ASP X  82       9.848  19.969  31.148  1.00175.85           O  
ANISOU 2076  O   ASP X  82    25036  21617  20161   2018   -471  -1725       O  
ATOM   2077  CB  ASP X  82       7.686  19.994  33.441  1.00167.54           C  
ANISOU 2077  CB  ASP X  82    23331  20746  19581   1686   -869  -1855       C  
ATOM   2078  CG  ASP X  82       7.432  19.196  34.697  1.00169.38           C  
ANISOU 2078  CG  ASP X  82    23270  21009  20079   1483   -900  -1897       C  
ATOM   2079  OD1 ASP X  82       8.359  18.489  35.151  1.00169.77           O  
ANISOU 2079  OD1 ASP X  82    23280  21013  20213   1409   -727  -1855       O  
ATOM   2080  OD2 ASP X  82       6.306  19.272  35.230  1.00170.20           O  
ANISOU 2080  OD2 ASP X  82    23184  21179  20305   1406  -1091  -1968       O  
ATOM   2081  N   SER X  83       9.442  22.134  31.608  1.00176.66           N  
ANISOU 2081  N   SER X  83    25025  21799  20300   2043   -450  -1576       N  
ATOM   2082  CA  SER X  83       9.857  22.617  30.298  1.00177.21           C  
ANISOU 2082  CA  SER X  83    25444  21800  20088   2250   -354  -1524       C  
ATOM   2083  C   SER X  83      11.210  22.032  29.898  1.00170.75           C  
ANISOU 2083  C   SER X  83    24766  20897  19215   2285    -71  -1452       C  
ATOM   2084  O   SER X  83      12.187  22.140  30.639  1.00168.77           O  
ANISOU 2084  O   SER X  83    24349  20639  19139   2182    163  -1339       O  
ATOM   2085  CB  SER X  83       9.931  24.146  30.302  1.00181.76           C  
ANISOU 2085  CB  SER X  83    26052  22384  20627   2314   -256  -1389       C  
ATOM   2086  OG  SER X  83      10.781  24.612  31.338  1.00181.69           O  
ANISOU 2086  OG  SER X  83    25820  22378  20835   2173    -30  -1260       O  
ATOM   2087  N   ASP X  84      11.258  21.395  28.732  1.00166.12           N  
ANISOU 2087  N   ASP X  84    24484  20245  18389   2437   -100  -1522       N  
ATOM   2088  CA  ASP X  84      12.527  20.947  28.175  1.00162.97           C  
ANISOU 2088  CA  ASP X  84    24265  19758  17899   2516    190  -1445       C  
ATOM   2089  C   ASP X  84      13.445  22.154  28.124  1.00157.60           C  
ANISOU 2089  C   ASP X  84    23615  19050  17214   2560    488  -1248       C  
ATOM   2090  O   ASP X  84      14.653  22.054  28.350  1.00154.60           O  
ANISOU 2090  O   ASP X  84    23174  18632  16934   2523    781  -1134       O  
ATOM   2091  CB  ASP X  84      12.328  20.376  26.766  1.00165.11           C  
ANISOU 2091  CB  ASP X  84    24930  19954  17849   2719    110  -1541       C  
ATOM   2092  CG  ASP X  84      13.604  20.402  25.930  1.00165.91           C  
ANISOU 2092  CG  ASP X  84    25297  19958  17785   2869    456  -1419       C  
ATOM   2093  OD1 ASP X  84      14.709  20.271  26.502  1.00164.89           O  
ANISOU 2093  OD1 ASP X  84    25004  19814  17832   2784    735  -1306       O  
ATOM   2094  OD2 ASP X  84      13.500  20.552  24.693  1.00168.02           O  
ANISOU 2094  OD2 ASP X  84    25937  20161  17741   3080    449  -1435       O  
ATOM   2095  N   LYS X  85      12.845  23.300  27.826  1.00155.94           N  
ANISOU 2095  N   LYS X  85    23494  18858  16899   2638    406  -1210       N  
ATOM   2096  CA  LYS X  85      13.558  24.562  27.757  1.00156.25           C  
ANISOU 2096  CA  LYS X  85    23578  18859  16931   2676    663  -1028       C  
ATOM   2097  C   LYS X  85      14.458  24.715  28.974  1.00155.82           C  
ANISOU 2097  C   LYS X  85    23191  18825  17188   2477    866   -923       C  
ATOM   2098  O   LYS X  85      13.977  24.663  30.108  1.00157.28           O  
ANISOU 2098  O   LYS X  85    23077  19086  17594   2311    719   -970       O  
ATOM   2099  CB  LYS X  85      12.550  25.709  27.668  1.00156.29           C  
ANISOU 2099  CB  LYS X  85    23629  18899  16857   2737    478  -1026       C  
ATOM   2100  CG  LYS X  85      11.792  25.734  26.346  1.00158.11           C  
ANISOU 2100  CG  LYS X  85    24227  19099  16749   2967    297  -1106       C  
ATOM   2101  CD  LYS X  85      10.303  25.981  26.533  1.00155.77           C  
ANISOU 2101  CD  LYS X  85    23848  18890  16449   2974    -81  -1232       C  
ATOM   2102  CE  LYS X  85       9.549  25.733  25.232  1.00157.62           C  
ANISOU 2102  CE  LYS X  85    24432  19099  16356   3197   -310  -1344       C  
ATOM   2103  NZ  LYS X  85       8.069  25.710  25.401  1.00157.39           N  
ANISOU 2103  NZ  LYS X  85    24285  19164  16352   3193   -715  -1497       N  
ATOM   2104  N   PRO X  86      15.774  24.885  28.739  1.00151.87           N  
ANISOU 2104  N   PRO X  86    22742  18255  16708   2498   1206   -781       N  
ATOM   2105  CA  PRO X  86      16.794  25.041  29.782  1.00147.02           C  
ANISOU 2105  CA  PRO X  86    21827  17650  16383   2325   1416   -674       C  
ATOM   2106  C   PRO X  86      16.283  25.755  31.042  1.00140.65           C  
ANISOU 2106  C   PRO X  86    20725  16915  15801   2153   1277   -671       C  
ATOM   2107  O   PRO X  86      15.328  26.535  30.984  1.00142.86           O  
ANISOU 2107  O   PRO X  86    21059  17219  16002   2189   1105   -697       O  
ATOM   2108  CB  PRO X  86      17.869  25.868  29.074  1.00145.83           C  
ANISOU 2108  CB  PRO X  86    21844  17406  16159   2418   1759   -499       C  
ATOM   2109  CG  PRO X  86      17.809  25.377  27.661  1.00145.87           C  
ANISOU 2109  CG  PRO X  86    22232  17346  15846   2641   1797   -534       C  
ATOM   2110  CD  PRO X  86      16.367  24.974  27.391  1.00149.12           C  
ANISOU 2110  CD  PRO X  86    22756  17808  16093   2705   1417   -711       C  
ATOM   2111  N   VAL X  87      16.926  25.485  32.174  1.00129.79           N  
ANISOU 2111  N   VAL X  87    19048  15571  14695   1978   1351   -640       N  
ATOM   2112  CA  VAL X  87      16.448  25.988  33.460  1.00117.33           C  
ANISOU 2112  CA  VAL X  87    17194  14060  13325   1814   1212   -653       C  
ATOM   2113  C   VAL X  87      17.378  27.018  34.121  1.00100.12           C  
ANISOU 2113  C   VAL X  87    14860  11851  11329   1707   1416   -508       C  
ATOM   2114  O   VAL X  87      18.598  26.842  34.172  1.00 96.11           O  
ANISOU 2114  O   VAL X  87    14283  11305  10930   1670   1649   -419       O  
ATOM   2115  CB  VAL X  87      16.153  24.822  34.435  1.00117.44           C  
ANISOU 2115  CB  VAL X  87    16974  14143  13504   1685   1054   -764       C  
ATOM   2116  CG1 VAL X  87      16.355  25.261  35.875  1.00118.06           C  
ANISOU 2116  CG1 VAL X  87    16750  14266  13842   1504   1049   -723       C  
ATOM   2117  CG2 VAL X  87      14.741  24.275  34.204  1.00115.32           C  
ANISOU 2117  CG2 VAL X  87    16772  13923  13123   1727    756   -921       C  
ATOM   2118  N   ASP X  88      16.787  28.101  34.615  1.00 86.53           N  
ANISOU 2118  N   ASP X  88    13086  10144   9648   1661   1322   -489       N  
ATOM   2119  CA  ASP X  88      17.546  29.124  35.325  1.00 87.22           C  
ANISOU 2119  CA  ASP X  88    13029  10196   9916   1544   1476   -371       C  
ATOM   2120  C   ASP X  88      17.731  28.723  36.790  1.00 85.95           C  
ANISOU 2120  C   ASP X  88    12546  10099  10013   1357   1397   -407       C  
ATOM   2121  O   ASP X  88      16.779  28.752  37.571  1.00 78.69           O  
ANISOU 2121  O   ASP X  88    11516   9243   9140   1299   1184   -489       O  
ATOM   2122  CB  ASP X  88      16.841  30.479  35.226  1.00 88.30           C  
ANISOU 2122  CB  ASP X  88    13273  10305   9973   1586   1414   -336       C  
ATOM   2123  CG  ASP X  88      17.603  31.593  35.929  1.00 92.56           C  
ANISOU 2123  CG  ASP X  88    13687  10787  10694   1460   1566   -220       C  
ATOM   2124  OD1 ASP X  88      17.081  32.727  35.982  1.00 91.82           O  
ANISOU 2124  OD1 ASP X  88    13670  10659  10559   1479   1523   -188       O  
ATOM   2125  OD2 ASP X  88      18.722  31.338  36.426  1.00 99.45           O  
ANISOU 2125  OD2 ASP X  88    14386  11644  11756   1343   1722   -163       O  
ATOM   2126  N   LYS X  89      18.961  28.341  37.139  1.00 92.57           N  
ANISOU 2126  N   LYS X  89    13240  10919  11015   1276   1574   -342       N  
ATOM   2127  CA  LYS X  89      19.322  27.889  38.484  1.00 91.48           C  
ANISOU 2127  CA  LYS X  89    12813  10832  11112   1115   1516   -366       C  
ATOM   2128  C   LYS X  89      19.154  29.006  39.503  1.00 83.27           C  
ANISOU 2128  C   LYS X  89    11640   9793  10206    994   1454   -337       C  
ATOM   2129  O   LYS X  89      18.460  28.849  40.518  1.00 77.18           O  
ANISOU 2129  O   LYS X  89    10733   9084   9509    915   1268   -413       O  
ATOM   2130  CB  LYS X  89      20.790  27.433  38.526  1.00 96.04           C  
ANISOU 2130  CB  LYS X  89    13274  11380  11836   1074   1737   -284       C  
ATOM   2131  CG  LYS X  89      21.102  26.129  37.822  1.00 97.92           C  
ANISOU 2131  CG  LYS X  89    13594  11622  11991   1174   1801   -320       C  
ATOM   2132  CD  LYS X  89      22.590  25.857  37.881  1.00102.73           C  
ANISOU 2132  CD  LYS X  89    14069  12201  12762   1143   2038   -222       C  
ATOM   2133  CE  LYS X  89      23.366  26.813  36.977  1.00110.89           C  
ANISOU 2133  CE  LYS X  89    15223  13149  13762   1200   2302    -88       C  
ATOM   2134  NZ  LYS X  89      23.106  26.564  35.517  1.00112.92           N  
ANISOU 2134  NZ  LYS X  89    15798  13357  13748   1393   2399    -88       N  
ATOM   2135  N   THR X  90      19.825  30.119  39.228  1.00 69.26           N  
ANISOU 2135  N   THR X  90     9912   7939   8463    981   1624   -225       N  
ATOM   2136  CA  THR X  90      19.817  31.269  40.109  1.00 73.80           C  
ANISOU 2136  CA  THR X  90    10388   8488   9165    866   1592   -189       C  
ATOM   2137  C   THR X  90      18.396  31.748  40.474  1.00 74.07           C  
ANISOU 2137  C   THR X  90    10477   8562   9105    893   1369   -269       C  
ATOM   2138  O   THR X  90      18.143  32.138  41.605  1.00 71.90           O  
ANISOU 2138  O   THR X  90    10059   8309   8951    788   1261   -297       O  
ATOM   2139  CB  THR X  90      20.642  32.400  39.492  1.00 77.12           C  
ANISOU 2139  CB  THR X  90    10907   8795   9600    868   1821    -56       C  
ATOM   2140  OG1 THR X  90      20.542  33.573  40.304  1.00 66.86           O  
ANISOU 2140  OG1 THR X  90     9542   7453   8407    761   1775    -31       O  
ATOM   2141  CG2 THR X  90      20.154  32.698  38.090  1.00 85.22           C  
ANISOU 2141  CG2 THR X  90    12237   9772  10370   1049   1890    -27       C  
ATOM   2142  N   ALA X  91      17.468  31.700  39.528  1.00 71.51           N  
ANISOU 2142  N   ALA X  91    10357   8247   8565   1043   1296   -310       N  
ATOM   2143  CA  ALA X  91      16.072  32.012  39.824  1.00 64.41           C  
ANISOU 2143  CA  ALA X  91     9486   7400   7587   1084   1075   -394       C  
ATOM   2144  C   ALA X  91      15.326  30.828  40.464  1.00 62.22           C  
ANISOU 2144  C   ALA X  91     9064   7227   7350   1048    881   -519       C  
ATOM   2145  O   ALA X  91      14.274  30.984  41.079  1.00 69.75           O  
ANISOU 2145  O   ALA X  91     9954   8236   8313   1036    707   -588       O  
ATOM   2146  CB  ALA X  91      15.362  32.461  38.560  1.00 59.49           C  
ANISOU 2146  CB  ALA X  91     9132   6747   6725   1265   1053   -389       C  
ATOM   2147  N   LEU X  92      15.875  29.636  40.315  1.00 58.64           N  
ANISOU 2147  N   LEU X  92     8560   6795   6925   1033    925   -543       N  
ATOM   2148  CA  LEU X  92      15.300  28.463  40.942  1.00 58.70           C  
ANISOU 2148  CA  LEU X  92     8435   6881   6987    985    770   -650       C  
ATOM   2149  C   LEU X  92      15.627  28.447  42.431  1.00 59.51           C  
ANISOU 2149  C   LEU X  92     8304   7011   7297    830    747   -646       C  
ATOM   2150  O   LEU X  92      14.779  28.174  43.270  1.00 64.21           O  
ANISOU 2150  O   LEU X  92     8793   7664   7941    781    594   -719       O  
ATOM   2151  CB  LEU X  92      15.865  27.217  40.278  1.00 62.39           C  
ANISOU 2151  CB  LEU X  92     8950   7344   7413   1028    840   -671       C  
ATOM   2152  CG  LEU X  92      15.332  25.935  40.906  1.00 68.22           C  
ANISOU 2152  CG  LEU X  92     9563   8144   8214    972    694   -779       C  
ATOM   2153  CD1 LEU X  92      13.825  25.845  40.729  1.00 62.91           C  
ANISOU 2153  CD1 LEU X  92     8938   7520   7444   1020    478   -885       C  
ATOM   2154  CD2 LEU X  92      16.036  24.747  40.301  1.00 70.68           C  
ANISOU 2154  CD2 LEU X  92     9930   8432   8494   1014    785   -791       C  
ATOM   2155  N   GLU X  93      16.877  28.728  42.753  1.00 55.72           N  
ANISOU 2155  N   GLU X  93     7746   6486   6940    756    901   -559       N  
ATOM   2156  CA  GLU X  93      17.278  28.874  44.133  1.00 53.27           C  
ANISOU 2156  CA  GLU X  93     7237   6189   6813    618    872   -550       C  
ATOM   2157  C   GLU X  93      16.383  29.874  44.874  1.00 57.65           C  
ANISOU 2157  C   GLU X  93     7780   6753   7372    587    753   -572       C  
ATOM   2158  O   GLU X  93      15.916  29.593  45.978  1.00 63.12           O  
ANISOU 2158  O   GLU X  93     8349   7493   8140    519    637   -626       O  
ATOM   2159  CB  GLU X  93      18.750  29.285  44.216  1.00 60.32           C  
ANISOU 2159  CB  GLU X  93     8059   7022   7838    551   1050   -448       C  
ATOM   2160  CG  GLU X  93      19.352  29.213  45.612  1.00 66.21           C  
ANISOU 2160  CG  GLU X  93     8595   7785   8778    413   1007   -446       C  
ATOM   2161  CD  GLU X  93      20.848  29.428  45.589  1.00 77.31           C  
ANISOU 2161  CD  GLU X  93     9903   9140  10332    351   1171   -355       C  
ATOM   2162  OE1 GLU X  93      21.388  29.653  44.486  1.00 87.29           O  
ANISOU 2162  OE1 GLU X  93    11266  10353  11548    413   1341   -286       O  
ATOM   2163  OE2 GLU X  93      21.490  29.367  46.659  1.00 80.10           O  
ANISOU 2163  OE2 GLU X  93    10082   9503  10850    245   1133   -350       O  
ATOM   2164  N   ILE X  94      16.156  31.040  44.271  1.00 62.14           N  
ANISOU 2164  N   ILE X  94     8488   7268   7853    647    794   -526       N  
ATOM   2165  CA  ILE X  94      15.241  32.050  44.816  1.00 50.47           C  
ANISOU 2165  CA  ILE X  94     7031   5788   6356    650    691   -545       C  
ATOM   2166  C   ILE X  94      13.876  31.453  45.177  1.00 55.41           C  
ANISOU 2166  C   ILE X  94     7614   6504   6936    687    507   -650       C  
ATOM   2167  O   ILE X  94      13.449  31.506  46.339  1.00 49.36           O  
ANISOU 2167  O   ILE X  94     6729   5771   6255    617    421   -687       O  
ATOM   2168  CB  ILE X  94      14.993  33.174  43.796  1.00 54.78           C  
ANISOU 2168  CB  ILE X  94     7783   6266   6766    758    751   -490       C  
ATOM   2169  CG1 ILE X  94      16.306  33.623  43.144  1.00 62.88           C  
ANISOU 2169  CG1 ILE X  94     8877   7196   7820    739    965   -379       C  
ATOM   2170  CG2 ILE X  94      14.243  34.354  44.441  1.00 43.55           C  
ANISOU 2170  CG2 ILE X  94     6381   4822   5343    758    670   -494       C  
ATOM   2171  CD1 ILE X  94      17.059  34.662  43.887  1.00 45.16           C  
ANISOU 2171  CD1 ILE X  94     6567   4872   5720    619   1042   -312       C  
ATOM   2172  N   PHE X  95      13.195  30.890  44.181  1.00 56.35           N  
ANISOU 2172  N   PHE X  95     7832   6656   6921    797    450   -698       N  
ATOM   2173  CA  PHE X  95      11.895  30.276  44.410  1.00 63.19           C  
ANISOU 2173  CA  PHE X  95     8643   7605   7763    826    275   -801       C  
ATOM   2174  C   PHE X  95      11.954  29.302  45.561  1.00 58.27           C  
ANISOU 2174  C   PHE X  95     7832   7029   7279    709    234   -846       C  
ATOM   2175  O   PHE X  95      11.148  29.347  46.491  1.00 56.51           O  
ANISOU 2175  O   PHE X  95     7507   6850   7115    671    140   -890       O  
ATOM   2176  CB  PHE X  95      11.434  29.501  43.179  1.00 71.50           C  
ANISOU 2176  CB  PHE X  95     9811   8680   8677    934    218   -856       C  
ATOM   2177  CG  PHE X  95      10.848  30.361  42.111  1.00 90.24           C  
ANISOU 2177  CG  PHE X  95    12374  11032  10883   1081    184   -844       C  
ATOM   2178  CD1 PHE X  95       9.733  31.144  42.370  1.00102.62           C  
ANISOU 2178  CD1 PHE X  95    13932  12631  12427   1134     61   -872       C  
ATOM   2179  CD2 PHE X  95      11.403  30.390  40.839  1.00100.49           C  
ANISOU 2179  CD2 PHE X  95    13869  12274  12037   1182    280   -801       C  
ATOM   2180  CE1 PHE X  95       9.178  31.956  41.377  1.00105.67           C  
ANISOU 2180  CE1 PHE X  95    14504  12996  12651   1289     18   -857       C  
ATOM   2181  CE2 PHE X  95      10.855  31.192  39.840  1.00103.93           C  
ANISOU 2181  CE2 PHE X  95    14507  12684  12298   1335    244   -784       C  
ATOM   2182  CZ  PHE X  95       9.740  31.978  40.112  1.00106.10           C  
ANISOU 2182  CZ  PHE X  95    14769  12992  12551   1389    105   -813       C  
ATOM   2183  N   TYR X  96      12.914  28.398  45.474  1.00 51.66           N  
ANISOU 2183  N   TYR X  96     6961   6178   6488    663    316   -831       N  
ATOM   2184  CA  TYR X  96      12.951  27.276  46.386  1.00 55.54           C  
ANISOU 2184  CA  TYR X  96     7307   6708   7087    575    274   -876       C  
ATOM   2185  C   TYR X  96      13.189  27.761  47.810  1.00 52.01           C  
ANISOU 2185  C   TYR X  96     6736   6262   6765    475    272   -850       C  
ATOM   2186  O   TYR X  96      12.494  27.340  48.736  1.00 59.31           O  
ANISOU 2186  O   TYR X  96     7565   7228   7742    430    188   -900       O  
ATOM   2187  CB  TYR X  96      14.024  26.277  45.928  1.00 54.55           C  
ANISOU 2187  CB  TYR X  96     7188   6559   6979    569    374   -856       C  
ATOM   2188  CG  TYR X  96      14.232  25.076  46.820  1.00 56.69           C  
ANISOU 2188  CG  TYR X  96     7329   6854   7357    489    349   -890       C  
ATOM   2189  CD1 TYR X  96      13.313  24.027  46.845  1.00 58.82           C  
ANISOU 2189  CD1 TYR X  96     7580   7158   7611    489    245   -979       C  
ATOM   2190  CD2 TYR X  96      15.361  24.973  47.616  1.00 57.96           C  
ANISOU 2190  CD2 TYR X  96     7388   6996   7638    415    426   -833       C  
ATOM   2191  CE1 TYR X  96      13.515  22.912  47.646  1.00 57.49           C  
ANISOU 2191  CE1 TYR X  96     7314   6996   7535    421    236  -1002       C  
ATOM   2192  CE2 TYR X  96      15.573  23.860  48.418  1.00 62.07           C  
ANISOU 2192  CE2 TYR X  96     7808   7532   8242    360    402   -858       C  
ATOM   2193  CZ  TYR X  96      14.648  22.835  48.424  1.00 62.58           C  
ANISOU 2193  CZ  TYR X  96     7876   7622   8280    365    316   -939       C  
ATOM   2194  OH  TYR X  96      14.869  21.735  49.212  1.00 61.61           O  
ANISOU 2194  OH  TYR X  96     7674   7500   8236    314    306   -955       O  
ATOM   2195  N   LEU X  97      14.170  28.642  47.980  1.00 45.47           N  
ANISOU 2195  N   LEU X  97     5915   5378   5982    439    367   -772       N  
ATOM   2196  CA  LEU X  97      14.467  29.201  49.294  1.00 51.31           C  
ANISOU 2196  CA  LEU X  97     6562   6105   6828    348    352   -753       C  
ATOM   2197  C   LEU X  97      13.297  29.988  49.881  1.00 60.48           C  
ANISOU 2197  C   LEU X  97     7738   7285   7958    368    259   -788       C  
ATOM   2198  O   LEU X  97      13.080  29.953  51.079  1.00 65.17           O  
ANISOU 2198  O   LEU X  97     8253   7895   8615    310    209   -809       O  
ATOM   2199  CB  LEU X  97      15.721  30.072  49.252  1.00 50.91           C  
ANISOU 2199  CB  LEU X  97     6520   5981   6842    299    461   -669       C  
ATOM   2200  CG  LEU X  97      17.038  29.297  49.337  1.00 57.81           C  
ANISOU 2200  CG  LEU X  97     7299   6847   7821    243    542   -633       C  
ATOM   2201  CD1 LEU X  97      18.231  30.231  49.226  1.00 50.86           C  
ANISOU 2201  CD1 LEU X  97     6406   5892   7027    188    652   -550       C  
ATOM   2202  CD2 LEU X  97      17.120  28.488  50.615  1.00 56.51           C  
ANISOU 2202  CD2 LEU X  97     7003   6722   7747    173    460   -670       C  
ATOM   2203  N   GLU X  98      12.541  30.700  49.046  1.00 67.52           N  
ANISOU 2203  N   GLU X  98     8740   8171   8743    462    240   -791       N  
ATOM   2204  CA  GLU X  98      11.375  31.418  49.556  1.00 63.15           C  
ANISOU 2204  CA  GLU X  98     8192   7639   8162    502    155   -824       C  
ATOM   2205  C   GLU X  98      10.343  30.434  50.051  1.00 67.78           C  
ANISOU 2205  C   GLU X  98     8676   8307   8771    499     60   -902       C  
ATOM   2206  O   GLU X  98       9.811  30.577  51.158  1.00 75.19           O  
ANISOU 2206  O   GLU X  98     9544   9266   9761    467     23   -923       O  
ATOM   2207  CB  GLU X  98      10.759  32.369  48.521  1.00 65.38           C  
ANISOU 2207  CB  GLU X  98     8617   7900   8324    623    145   -810       C  
ATOM   2208  CG  GLU X  98      11.311  33.815  48.592  1.00 73.21           C  
ANISOU 2208  CG  GLU X  98     9708   8798   9311    620    221   -738       C  
ATOM   2209  CD  GLU X  98      12.235  34.085  49.807  1.00 78.82           C  
ANISOU 2209  CD  GLU X  98    10339   9462  10148    487    262   -711       C  
ATOM   2210  OE1 GLU X  98      11.758  34.173  50.967  1.00 73.86           O  
ANISOU 2210  OE1 GLU X  98     9644   8855   9566    452    198   -747       O  
ATOM   2211  OE2 GLU X  98      13.455  34.240  49.588  1.00 72.40           O  
ANISOU 2211  OE2 GLU X  98     9535   8586   9388    422    359   -652       O  
ATOM   2212  N   ILE X  99      10.065  29.424  49.238  1.00 63.45           N  
ANISOU 2212  N   ILE X  99     8126   7795   8186    531     28   -944       N  
ATOM   2213  CA  ILE X  99       9.119  28.414  49.644  1.00 62.97           C  
ANISOU 2213  CA  ILE X  99     7961   7799   8166    512    -55  -1018       C  
ATOM   2214  C   ILE X  99       9.526  27.816  50.996  1.00 65.63           C  
ANISOU 2214  C   ILE X  99     8188   8136   8612    405    -27  -1012       C  
ATOM   2215  O   ILE X  99       8.693  27.637  51.883  1.00 64.53           O  
ANISOU 2215  O   ILE X  99     7966   8031   8520    382    -67  -1045       O  
ATOM   2216  CB  ILE X  99       8.961  27.345  48.575  1.00 60.76           C  
ANISOU 2216  CB  ILE X  99     7710   7538   7838    545    -93  -1068       C  
ATOM   2217  CG1 ILE X  99       8.468  27.990  47.287  1.00 59.91           C  
ANISOU 2217  CG1 ILE X  99     7732   7431   7601    669   -141  -1077       C  
ATOM   2218  CG2 ILE X  99       7.989  26.264  49.034  1.00 57.29           C  
ANISOU 2218  CG2 ILE X  99     7152   7150   7464    503   -177  -1147       C  
ATOM   2219  CD1 ILE X  99       8.085  26.957  46.224  1.00 60.56           C  
ANISOU 2219  CD1 ILE X  99     7858   7533   7618    715   -216  -1148       C  
ATOM   2220  N   LEU X 100      10.810  27.533  51.169  1.00 64.63           N  
ANISOU 2220  N   LEU X 100     8062   7970   8525    348     47   -966       N  
ATOM   2221  CA  LEU X 100      11.273  26.990  52.440  1.00 60.08           C  
ANISOU 2221  CA  LEU X 100     7398   7390   8038    262     61   -958       C  
ATOM   2222  C   LEU X 100      11.077  27.979  53.601  1.00 57.92           C  
ANISOU 2222  C   LEU X 100     7115   7104   7788    239     48   -941       C  
ATOM   2223  O   LEU X 100      10.676  27.592  54.705  1.00 62.30           O  
ANISOU 2223  O   LEU X 100     7612   7676   8382    204     28   -960       O  
ATOM   2224  CB  LEU X 100      12.748  26.593  52.340  1.00 20.00           C  
ATOM   2225  CG  LEU X 100      13.079  25.457  51.369  1.00 20.00           C  
ATOM   2226  CD1 LEU X 100      14.584  25.267  51.259  1.00 20.00           C  
ATOM   2227  CD2 LEU X 100      12.401  24.165  51.799  1.00 20.00           C  
ATOM   2228  N   ASN X 101      11.336  29.260  53.345  1.00 52.36           N  
ANISOU 2228  N   ASN X 101     6484   6358   7050    266     68   -905       N  
ATOM   2229  CA  ASN X 101      11.145  30.282  54.365  1.00 46.97           C  
ANISOU 2229  CA  ASN X 101     5822   5649   6377    253     53   -896       C  
ATOM   2230  C   ASN X 101       9.700  30.283  54.803  1.00 52.53           C  
ANISOU 2230  C   ASN X 101     6498   6403   7057    304      7   -943       C  
ATOM   2231  O   ASN X 101       9.396  30.519  55.962  1.00 62.32           O  
ANISOU 2231  O   ASN X 101     7724   7639   8316    287     -1   -950       O  
ATOM   2232  CB  ASN X 101      11.502  31.657  53.824  1.00 47.15           C  
ANISOU 2232  CB  ASN X 101     5945   5607   6361    282     84   -854       C  
ATOM   2233  CG  ASN X 101      12.986  31.921  53.843  1.00 52.54           C  
ANISOU 2233  CG  ASN X 101     6633   6225   7106    205    140   -801       C  
ATOM   2234  OD1 ASN X 101      13.745  31.169  54.441  1.00 56.96           O  
ANISOU 2234  OD1 ASN X 101     7113   6792   7738    136    139   -797       O  
ATOM   2235  ND2 ASN X 101      13.409  33.001  53.192  1.00 63.19           N  
ANISOU 2235  ND2 ASN X 101     8071   7506   8434    219    190   -755       N  
ATOM   2236  N   GLY X 102       8.805  30.029  53.857  1.00 54.74           N  
ANISOU 2236  N   GLY X 102     6772   6729   7297    372    -26   -976       N  
ATOM   2237  CA  GLY X 102       7.398  29.901  54.170  1.00 54.43           C  
ANISOU 2237  CA  GLY X 102     6669   6747   7264    417    -72  -1023       C  
ATOM   2238  C   GLY X 102       7.131  28.654  54.984  1.00 60.52           C  
ANISOU 2238  C   GLY X 102     7336   7552   8108    350    -68  -1052       C  
ATOM   2239  O   GLY X 102       6.709  28.752  56.137  1.00 69.68           O  
ANISOU 2239  O   GLY X 102     8461   8715   9297    335    -48  -1052       O  
ATOM   2240  N   LEU X 103       7.398  27.484  54.405  1.00 48.39           N  
ANISOU 2240  N   LEU X 103     5764   6028   6592    313    -76  -1072       N  
ATOM   2241  CA  LEU X 103       7.181  26.220  55.111  1.00 49.92           C  
ANISOU 2241  CA  LEU X 103     5873   6237   6856    246    -64  -1095       C  
ATOM   2242  C   LEU X 103       7.635  26.266  56.567  1.00 56.11           C  
ANISOU 2242  C   LEU X 103     6656   6993   7670    197    -16  -1060       C  
ATOM   2243  O   LEU X 103       7.033  25.628  57.437  1.00 64.93           O  
ANISOU 2243  O   LEU X 103     7716   8123   8831    168      6  -1072       O  
ATOM   2244  CB  LEU X 103       7.894  25.072  54.392  1.00 51.83           C  
ANISOU 2244  CB  LEU X 103     6120   6465   7107    210    -61  -1105       C  
ATOM   2245  CG  LEU X 103       7.860  23.690  55.043  1.00 53.92           C  
ANISOU 2245  CG  LEU X 103     6323   6724   7441    139    -40  -1122       C  
ATOM   2246  CD1 LEU X 103       6.451  23.135  55.159  1.00 55.66           C  
ANISOU 2246  CD1 LEU X 103     6454   6980   7714    127    -71  -1178       C  
ATOM   2247  CD2 LEU X 103       8.721  22.741  54.247  1.00 53.43           C  
ANISOU 2247  CD2 LEU X 103     6295   6635   7373    124    -31  -1126       C  
ATOM   2248  N   PHE X 104       8.694  27.025  56.835  1.00 44.58           N  
ANISOU 2248  N   PHE X 104     5264   5489   6186    188      0  -1016       N  
ATOM   2249  CA  PHE X 104       9.329  26.978  58.151  1.00 44.23           C  
ANISOU 2249  CA  PHE X 104     5234   5411   6160    141     19   -989       C  
ATOM   2250  C   PHE X 104       9.031  28.178  59.045  1.00 48.80           C  
ANISOU 2250  C   PHE X 104     5870   5967   6705    170     19   -980       C  
ATOM   2251  O   PHE X 104       9.851  28.555  59.887  1.00 45.01           O  
ANISOU 2251  O   PHE X 104     5441   5442   6219    139     11   -957       O  
ATOM   2252  CB  PHE X 104      10.837  26.721  58.033  1.00 35.66           C  
ANISOU 2252  CB  PHE X 104     4163   4288   5097     95     23   -953       C  
ATOM   2253  CG  PHE X 104      11.153  25.356  57.514  1.00 48.81           C  
ANISOU 2253  CG  PHE X 104     5782   5966   6796     73     37   -961       C  
ATOM   2254  CD1 PHE X 104      10.678  24.235  58.174  1.00 44.25           C  
ANISOU 2254  CD1 PHE X 104     5166   5399   6246     49     48   -978       C  
ATOM   2255  CD2 PHE X 104      11.905  25.181  56.363  1.00 48.89           C  
ANISOU 2255  CD2 PHE X 104     5801   5968   6806     81     53   -949       C  
ATOM   2256  CE1 PHE X 104      10.957  22.953  57.706  1.00 45.35           C  
ANISOU 2256  CE1 PHE X 104     5279   5535   6416     29     61   -988       C  
ATOM   2257  CE2 PHE X 104      12.177  23.910  55.882  1.00 45.56           C  
ANISOU 2257  CE2 PHE X 104     5355   5550   6407     71     70   -961       C  
ATOM   2258  CZ  PHE X 104      11.703  22.793  56.552  1.00 47.71           C  
ANISOU 2258  CZ  PHE X 104     5592   5827   6709     44     68   -983       C  
ATOM   2259  N   GLU X 105       7.849  28.763  58.882  1.00 45.44           N  
ANISOU 2259  N   GLU X 105     5439   5569   6256    234     19  -1002       N  
ATOM   2260  CA  GLU X 105       7.365  29.697  59.891  1.00 50.57           C  
ANISOU 2260  CA  GLU X 105     6144   6198   6872    273     35   -999       C  
ATOM   2261  C   GLU X 105       7.377  29.001  61.248  1.00 53.39           C  
ANISOU 2261  C   GLU X 105     6499   6546   7240    238     69   -994       C  
ATOM   2262  O   GLU X 105       7.669  29.632  62.265  1.00 54.99           O  
ANISOU 2262  O   GLU X 105     6790   6703   7401    246     72   -983       O  
ATOM   2263  CB  GLU X 105       5.978  30.221  59.543  1.00 59.77           C  
ANISOU 2263  CB  GLU X 105     7275   7406   8026    360     41  -1024       C  
ATOM   2264  CG  GLU X 105       5.899  30.718  58.117  1.00 84.09           C  
ANISOU 2264  CG  GLU X 105    10367  10501  11084    409     -3  -1029       C  
ATOM   2265  CD  GLU X 105       5.344  32.122  58.019  1.00100.51           C  
ANISOU 2265  CD  GLU X 105    12519  12560  13109    505     -8  -1025       C  
ATOM   2266  OE1 GLU X 105       5.012  32.699  59.081  1.00108.04           O  
ANISOU 2266  OE1 GLU X 105    13514  13489  14047    532     25  -1022       O  
ATOM   2267  OE2 GLU X 105       5.252  32.647  56.884  1.00103.73           O  
ANISOU 2267  OE2 GLU X 105    12963  12969  13481    562    -42  -1023       O  
ATOM   2268  N   LYS X 106       7.059  27.704  61.267  1.00 46.86           N  
ANISOU 2268  N   LYS X 106     5590   5753   6463    204     95  -1002       N  
ATOM   2269  CA  LYS X 106       7.306  26.892  62.460  1.00 54.57           C  
ANISOU 2269  CA  LYS X 106     6585   6707   7443    167    131   -985       C  
ATOM   2270  C   LYS X 106       8.156  25.681  62.118  1.00 50.79           C  
ANISOU 2270  C   LYS X 106     6070   6222   7005    105    117   -975       C  
ATOM   2271  O   LYS X 106       8.326  25.343  60.946  1.00 52.50           O  
ANISOU 2271  O   LYS X 106     6237   6459   7252     92     93   -989       O  
ATOM   2272  CB  LYS X 106       6.014  26.406  63.114  1.00 54.65           C  
ANISOU 2272  CB  LYS X 106     6544   6744   7478    188    210   -992       C  
ATOM   2273  CG  LYS X 106       4.868  27.376  63.054  1.00 60.54           C  
ANISOU 2273  CG  LYS X 106     7270   7518   8214    264    235  -1008       C  
ATOM   2274  CD  LYS X 106       3.815  26.998  64.082  1.00 66.88           C  
ANISOU 2274  CD  LYS X 106     8042   8331   9039    286    341   -999       C  
ATOM   2275  CE  LYS X 106       2.735  28.054  64.197  1.00 72.33           C  
ANISOU 2275  CE  LYS X 106     8718   9046   9717    380    379  -1010       C  
ATOM   2276  NZ  LYS X 106       1.671  27.544  65.104  1.00 82.28           N  
ANISOU 2276  NZ  LYS X 106     9920  10320  11022    398    507   -995       N  
ATOM   2277  N   LEU X 107       8.668  25.023  63.150  1.00 50.21           N  
ANISOU 2277  N   LEU X 107     6037   6117   6922     81    133   -951       N  
ATOM   2278  CA  LEU X 107       9.519  23.863  62.975  1.00 51.89           C  
ANISOU 2278  CA  LEU X 107     6228   6316   7170     38    123   -937       C  
ATOM   2279  C   LEU X 107       8.884  22.654  63.612  1.00 48.39           C  
ANISOU 2279  C   LEU X 107     5771   5864   6751     21    191   -930       C  
ATOM   2280  O   LEU X 107       8.417  22.726  64.749  1.00 45.73           O  
ANISOU 2280  O   LEU X 107     5489   5510   6378     42    240   -913       O  
ATOM   2281  CB  LEU X 107      10.861  24.108  63.645  1.00 55.93           C  
ANISOU 2281  CB  LEU X 107     6807   6788   7655     30     67   -909       C  
ATOM   2282  CG  LEU X 107      11.663  25.231  63.010  1.00 58.35           C  
ANISOU 2282  CG  LEU X 107     7119   7087   7963     26      8   -909       C  
ATOM   2283  CD1 LEU X 107      13.065  25.274  63.583  1.00 67.46           C  
ANISOU 2283  CD1 LEU X 107     8299   8205   9126      2    -58   -886       C  
ATOM   2284  CD2 LEU X 107      11.690  25.048  61.502  1.00 51.24           C  
ANISOU 2284  CD2 LEU X 107     6151   6215   7104     18     20   -919       C  
ATOM   2285  N   ASN X 108       8.850  21.556  62.863  1.00 37.97           N  
ANISOU 2285  N   ASN X 108     4389   4548   5488    -14    203   -943       N  
ATOM   2286  CA  ASN X 108       8.481  20.249  63.398  1.00 38.57           C  
ANISOU 2286  CA  ASN X 108     4461   4593   5599    -45    269   -930       C  
ATOM   2287  C   ASN X 108       8.875  19.184  62.377  1.00 46.95           C  
ANISOU 2287  C   ASN X 108     5482   5644   6713    -80    252   -950       C  
ATOM   2288  O   ASN X 108       9.143  19.500  61.217  1.00 48.30           O  
ANISOU 2288  O   ASN X 108     5621   5841   6891    -75    202   -978       O  
ATOM   2289  CB  ASN X 108       6.988  20.171  63.754  1.00 40.49           C  
ANISOU 2289  CB  ASN X 108     4654   4851   5879    -52    350   -944       C  
ATOM   2290  CG  ASN X 108       6.083  20.191  62.528  1.00 44.26           C  
ANISOU 2290  CG  ASN X 108     5016   5375   6426    -71    326   -999       C  
ATOM   2291  OD1 ASN X 108       6.344  19.518  61.530  1.00 58.75           O  
ANISOU 2291  OD1 ASN X 108     6819   7208   8297   -103    284  -1029       O  
ATOM   2292  ND2 ASN X 108       5.004  20.947  62.608  1.00 43.06           N  
ANISOU 2292  ND2 ASN X 108     4809   5263   6289    -43    348  -1016       N  
ATOM   2293  N   TRP X 109       8.913  17.929  62.797  1.00 45.51           N  
ANISOU 2293  N   TRP X 109     5320   5414   6559   -108    302   -933       N  
ATOM   2294  CA  TRP X 109       9.454  16.888  61.937  1.00 43.49           C  
ANISOU 2294  CA  TRP X 109     5054   5130   6341   -130    287   -948       C  
ATOM   2295  C   TRP X 109       8.636  16.729  60.664  1.00 46.67           C  
ANISOU 2295  C   TRP X 109     5383   5557   6792   -160    266  -1014       C  
ATOM   2296  O   TRP X 109       9.186  16.385  59.616  1.00 49.90           O  
ANISOU 2296  O   TRP X 109     5796   5961   7201   -154    228  -1039       O  
ATOM   2297  CB  TRP X 109       9.591  15.571  62.689  1.00 44.78           C  
ANISOU 2297  CB  TRP X 109     5271   5221   6522   -149    349   -915       C  
ATOM   2298  CG  TRP X 109      10.764  15.478  63.655  1.00 46.95           C  
ANISOU 2298  CG  TRP X 109     5633   5466   6740   -100    335   -855       C  
ATOM   2299  CD1 TRP X 109      10.711  15.259  65.010  1.00 45.01           C  
ANISOU 2299  CD1 TRP X 109     5472   5181   6449    -79    379   -806       C  
ATOM   2300  CD2 TRP X 109      12.153  15.549  63.324  1.00 45.77           C  
ANISOU 2300  CD2 TRP X 109     5493   5321   6576    -61    267   -838       C  
ATOM   2301  NE1 TRP X 109      11.983  15.195  65.536  1.00 46.13           N  
ANISOU 2301  NE1 TRP X 109     5677   5306   6544    -25    320   -766       N  
ATOM   2302  CE2 TRP X 109      12.886  15.374  64.515  1.00 47.11           C  
ANISOU 2302  CE2 TRP X 109     5740   5460   6700    -18    252   -785       C  
ATOM   2303  CE3 TRP X 109      12.851  15.757  62.138  1.00 42.99           C  
ANISOU 2303  CE3 TRP X 109     5092   4997   6247    -52    224   -860       C  
ATOM   2304  CZ2 TRP X 109      14.265  15.403  64.553  1.00 48.80           C  
ANISOU 2304  CZ2 TRP X 109     5957   5676   6909     27    181   -758       C  
ATOM   2305  CZ3 TRP X 109      14.237  15.774  62.178  1.00 48.69           C  
ANISOU 2305  CZ3 TRP X 109     5817   5717   6967     -9    180   -826       C  
ATOM   2306  CH2 TRP X 109      14.924  15.596  63.375  1.00 48.17           C  
ANISOU 2306  CH2 TRP X 109     5802   5626   6875     26    152   -778       C  
ATOM   2307  N   GLY X 110       7.340  17.042  60.739  1.00 43.24           N  
ANISOU 2307  N   GLY X 110     4882   5152   6395   -182    286  -1043       N  
ATOM   2308  CA  GLY X 110       6.452  16.861  59.605  1.00 46.08           C  
ANISOU 2308  CA  GLY X 110     5163   5537   6809   -209    243  -1113       C  
ATOM   2309  C   GLY X 110       6.785  17.864  58.532  1.00 49.61           C  
ANISOU 2309  C   GLY X 110     5614   6037   7200   -155    160  -1138       C  
ATOM   2310  O   GLY X 110       6.656  17.603  57.331  1.00 52.80           O  
ANISOU 2310  O   GLY X 110     6007   6448   7607   -154    102  -1191       O  
ATOM   2311  N   ARG X 111       7.209  19.041  58.972  1.00 44.28           N  
ANISOU 2311  N   ARG X 111     4971   5389   6466   -106    157  -1099       N  
ATOM   2312  CA  ARG X 111       7.601  20.094  58.040  1.00 47.47           C  
ANISOU 2312  CA  ARG X 111     5395   5827   6813    -54     97  -1107       C  
ATOM   2313  C   ARG X 111       8.957  19.829  57.386  1.00 47.89           C  
ANISOU 2313  C   ARG X 111     5507   5854   6836    -41     86  -1088       C  
ATOM   2314  O   ARG X 111       9.163  20.113  56.205  1.00 44.42           O  
ANISOU 2314  O   ARG X 111     5087   5427   6362     -9     52  -1110       O  
ATOM   2315  CB  ARG X 111       7.599  21.450  58.747  1.00 39.38           C  
ANISOU 2315  CB  ARG X 111     4394   4822   5745    -14    102  -1074       C  
ATOM   2316  CG  ARG X 111       6.210  21.996  58.899  1.00 40.94           C  
ANISOU 2316  CG  ARG X 111     4529   5061   5965      7    105  -1101       C  
ATOM   2317  CD  ARG X 111       6.219  23.404  59.456  1.00 55.27           C  
ANISOU 2317  CD  ARG X 111     6390   6886   7724     62    108  -1074       C  
ATOM   2318  NE  ARG X 111       4.879  23.798  59.877  1.00 58.59           N  
ANISOU 2318  NE  ARG X 111     6747   7341   8173     92    138  -1090       N  
ATOM   2319  CZ  ARG X 111       4.294  24.940  59.538  1.00 59.89           C  
ANISOU 2319  CZ  ARG X 111     6907   7539   8311    161    110  -1102       C  
ATOM   2320  NH1 ARG X 111       4.942  25.830  58.792  1.00 56.63           N  
ANISOU 2320  NH1 ARG X 111     6563   7119   7833    201     56  -1096       N  
ATOM   2321  NH2 ARG X 111       3.067  25.199  59.969  1.00 50.74           N  
ANISOU 2321  NH2 ARG X 111     5673   6414   7192    195    148  -1115       N  
ATOM   2322  N   ILE X 112       9.875  19.296  58.180  1.00 47.86           N  
ANISOU 2322  N   ILE X 112     5533   5811   6839    -57    120  -1044       N  
ATOM   2323  CA  ILE X 112      11.178  18.893  57.696  1.00 42.31           C  
ANISOU 2323  CA  ILE X 112     4863   5083   6130    -42    123  -1019       C  
ATOM   2324  C   ILE X 112      11.012  17.809  56.633  1.00 47.11           C  
ANISOU 2324  C   ILE X 112     5479   5669   6750    -47    125  -1065       C  
ATOM   2325  O   ILE X 112      11.678  17.840  55.594  1.00 45.52           O  
ANISOU 2325  O   ILE X 112     5309   5466   6521    -11    122  -1069       O  
ATOM   2326  CB  ILE X 112      12.050  18.414  58.865  1.00 43.26           C  
ANISOU 2326  CB  ILE X 112     5004   5169   6265    -48    145   -967       C  
ATOM   2327  CG1 ILE X 112      12.682  19.628  59.552  1.00 43.15           C  
ANISOU 2327  CG1 ILE X 112     5000   5168   6226    -33    117   -929       C  
ATOM   2328  CG2 ILE X 112      13.108  17.428  58.384  1.00 44.33           C  
ANISOU 2328  CG2 ILE X 112     5155   5269   6420    -32    162   -952       C  
ATOM   2329  CD1 ILE X 112      13.010  19.444  61.023  1.00 44.99           C  
ANISOU 2329  CD1 ILE X 112     5267   5377   6452    -35    112   -892       C  
ATOM   2330  N   VAL X 113      10.086  16.882  56.886  1.00 52.32           N  
ANISOU 2330  N   VAL X 113     6119   6307   7453    -91    134  -1101       N  
ATOM   2331  CA  VAL X 113       9.721  15.857  55.918  1.00 55.99           C  
ANISOU 2331  CA  VAL X 113     6597   6740   7935   -109    117  -1162       C  
ATOM   2332  C   VAL X 113       9.195  16.506  54.648  1.00 57.75           C  
ANISOU 2332  C   VAL X 113     6820   7007   8117    -76     51  -1218       C  
ATOM   2333  O   VAL X 113       9.542  16.118  53.534  1.00 59.10           O  
ANISOU 2333  O   VAL X 113     7049   7159   8249    -45     30  -1252       O  
ATOM   2334  CB  VAL X 113       8.623  14.957  56.467  1.00 53.19           C  
ANISOU 2334  CB  VAL X 113     6202   6354   7655   -181    134  -1195       C  
ATOM   2335  CG1 VAL X 113       7.993  14.146  55.333  1.00 50.41           C  
ANISOU 2335  CG1 VAL X 113     5853   5974   7327   -210     83  -1282       C  
ATOM   2336  CG2 VAL X 113       9.172  14.056  57.568  1.00 43.82           C  
ANISOU 2336  CG2 VAL X 113     5054   5103   6494   -203    207  -1140       C  
ATOM   2337  N   ALA X 114       8.339  17.497  54.821  1.00 54.44           N  
ANISOU 2337  N   ALA X 114     6348   6642   7697    -70     18  -1227       N  
ATOM   2338  CA  ALA X 114       7.780  18.210  53.684  1.00 54.84           C  
ANISOU 2338  CA  ALA X 114     6403   6736   7699    -23    -55  -1275       C  
ATOM   2339  C   ALA X 114       8.904  18.663  52.781  1.00 59.28           C  
ANISOU 2339  C   ALA X 114     7058   7291   8177     44    -44  -1247       C  
ATOM   2340  O   ALA X 114       8.801  18.587  51.551  1.00 58.09           O  
ANISOU 2340  O   ALA X 114     6966   7140   7967     89    -90  -1292       O  
ATOM   2341  CB  ALA X 114       6.966  19.407  54.159  1.00 50.58           C  
ANISOU 2341  CB  ALA X 114     5804   6252   7162     -2    -74  -1265       C  
ATOM   2342  N   MET X 115       9.982  19.139  53.402  1.00 57.82           N  
ANISOU 2342  N   MET X 115     6886   7096   7987     52     17  -1172       N  
ATOM   2343  CA  MET X 115      11.151  19.651  52.671  1.00 57.24           C  
ANISOU 2343  CA  MET X 115     6877   7013   7860    104     53  -1130       C  
ATOM   2344  C   MET X 115      11.741  18.594  51.744  1.00 58.59           C  
ANISOU 2344  C   MET X 115     7111   7144   8009    129     79  -1151       C  
ATOM   2345  O   MET X 115      12.005  18.866  50.587  1.00 58.01           O  
ANISOU 2345  O   MET X 115     7112   7066   7862    190     85  -1159       O  
ATOM   2346  CB  MET X 115      12.244  20.106  53.642  1.00 50.57           C  
ANISOU 2346  CB  MET X 115     6007   6157   7050     87    104  -1054       C  
ATOM   2347  CG  MET X 115      13.425  20.773  52.955  1.00 44.17           C  
ANISOU 2347  CG  MET X 115     5233   5334   6215    127    153  -1003       C  
ATOM   2348  SD  MET X 115      14.742  21.201  54.114  1.00 57.27           S  
ANISOU 2348  SD  MET X 115     6836   6978   7946     93    185   -926       S  
ATOM   2349  CE  MET X 115      15.058  19.615  54.871  1.00 47.70           C  
ANISOU 2349  CE  MET X 115     5596   5743   6786     73    192   -929       C  
ATOM   2350  N   PHE X 116      11.953  17.393  52.276  1.00 51.92           N  
ANISOU 2350  N   PHE X 116     6251   6260   7216     91    102  -1156       N  
ATOM   2351  CA  PHE X 116      12.518  16.314  51.496  1.00 52.23           C  
ANISOU 2351  CA  PHE X 116     6360   6249   7236    121    133  -1178       C  
ATOM   2352  C   PHE X 116      11.539  15.928  50.417  1.00 51.96           C  
ANISOU 2352  C   PHE X 116     6383   6207   7150    133     61  -1270       C  
ATOM   2353  O   PHE X 116      11.891  15.901  49.241  1.00 58.02           O  
ANISOU 2353  O   PHE X 116     7248   6960   7836    201     68  -1290       O  
ATOM   2354  CB  PHE X 116      12.853  15.115  52.374  1.00 48.20           C  
ANISOU 2354  CB  PHE X 116     5832   5689   6793     81    168  -1164       C  
ATOM   2355  CG  PHE X 116      14.089  15.306  53.214  1.00 51.71           C  
ANISOU 2355  CG  PHE X 116     6239   6133   7275     96    226  -1078       C  
ATOM   2356  CD1 PHE X 116      13.989  15.666  54.554  1.00 44.85           C  
ANISOU 2356  CD1 PHE X 116     5310   5282   6450     54    214  -1039       C  
ATOM   2357  CD2 PHE X 116      15.358  15.137  52.662  1.00 54.70           C  
ANISOU 2357  CD2 PHE X 116     6644   6494   7647    158    290  -1037       C  
ATOM   2358  CE1 PHE X 116      15.137  15.853  55.349  1.00 48.50           C  
ANISOU 2358  CE1 PHE X 116     5739   5743   6945     69    237   -968       C  
ATOM   2359  CE2 PHE X 116      16.506  15.321  53.445  1.00 57.94           C  
ANISOU 2359  CE2 PHE X 116     6993   6908   8111    170    325   -961       C  
ATOM   2360  CZ  PHE X 116      16.395  15.680  54.800  1.00 50.31           C  
ANISOU 2360  CZ  PHE X 116     5968   5960   7186    123    285   -931       C  
ATOM   2361  N   ALA X 117      10.306  15.655  50.818  1.00 55.90           N  
ANISOU 2361  N   ALA X 117     6824   6717   7699     69     -9  -1327       N  
ATOM   2362  CA  ALA X 117       9.260  15.292  49.867  1.00 61.16           C  
ANISOU 2362  CA  ALA X 117     7520   7380   8339     68   -108  -1427       C  
ATOM   2363  C   ALA X 117       9.270  16.220  48.659  1.00 63.79           C  
ANISOU 2363  C   ALA X 117     7933   7748   8555    161   -153  -1441       C  
ATOM   2364  O   ALA X 117       9.120  15.789  47.519  1.00 70.83           O  
ANISOU 2364  O   ALA X 117     8928   8614   9371    207   -208  -1508       O  
ATOM   2365  CB  ALA X 117       7.917  15.336  50.534  1.00 60.96           C  
ANISOU 2365  CB  ALA X 117     7377   7385   8401     -8   -172  -1467       C  
ATOM   2366  N   PHE X 118       9.455  17.502  48.919  1.00 59.79           N  
ANISOU 2366  N   PHE X 118     7398   7291   8028    193   -129  -1378       N  
ATOM   2367  CA  PHE X 118       9.344  18.522  47.890  1.00 60.62           C  
ANISOU 2367  CA  PHE X 118     7583   7426   8024    283   -165  -1380       C  
ATOM   2368  C   PHE X 118      10.599  18.594  47.045  1.00 60.95           C  
ANISOU 2368  C   PHE X 118     7751   7431   7977    360    -71  -1332       C  
ATOM   2369  O   PHE X 118      10.537  18.679  45.827  1.00 69.14           O  
ANISOU 2369  O   PHE X 118     8915   8457   8900    443    -99  -1366       O  
ATOM   2370  CB  PHE X 118       9.094  19.866  48.573  1.00 59.80           C  
ANISOU 2370  CB  PHE X 118     7409   7372   7939    285   -160  -1326       C  
ATOM   2371  CG  PHE X 118       9.067  21.033  47.639  1.00 57.75           C  
ANISOU 2371  CG  PHE X 118     7241   7132   7569    382   -178  -1309       C  
ATOM   2372  CD1 PHE X 118       8.197  21.058  46.573  1.00 60.28           C  
ANISOU 2372  CD1 PHE X 118     7627   7469   7806    448   -291  -1382       C  
ATOM   2373  CD2 PHE X 118       9.892  22.125  47.850  1.00 60.17           C  
ANISOU 2373  CD2 PHE X 118     7572   7433   7858    405    -91  -1219       C  
ATOM   2374  CE1 PHE X 118       8.165  22.142  45.712  1.00 61.97           C  
ANISOU 2374  CE1 PHE X 118     7948   7694   7902    553   -306  -1360       C  
ATOM   2375  CE2 PHE X 118       9.860  23.214  46.998  1.00 59.77           C  
ANISOU 2375  CE2 PHE X 118     7621   7384   7704    494    -94  -1195       C  
ATOM   2376  CZ  PHE X 118       8.995  23.220  45.925  1.00 60.94           C  
ANISOU 2376  CZ  PHE X 118     7852   7550   7753    576   -198  -1262       C  
ATOM   2377  N   LEU X 119      11.745  18.601  47.712  1.00 59.53           N  
ANISOU 2377  N   LEU X 119     7535   7233   7852    338     43  -1250       N  
ATOM   2378  CA  LEU X 119      13.033  18.539  47.040  1.00 55.58           C  
ANISOU 2378  CA  LEU X 119     7119   6695   7304    401    158  -1195       C  
ATOM   2379  C   LEU X 119      13.046  17.359  46.053  1.00 63.42           C  
ANISOU 2379  C   LEU X 119     8230   7639   8228    449    152  -1262       C  
ATOM   2380  O   LEU X 119      13.506  17.476  44.917  1.00 53.52           O  
ANISOU 2380  O   LEU X 119     7110   6359   6864    542    203  -1256       O  
ATOM   2381  CB  LEU X 119      14.136  18.351  48.074  1.00 41.77           C  
ANISOU 2381  CB  LEU X 119     5275   4934   5661    354    251  -1117       C  
ATOM   2382  CG  LEU X 119      15.483  17.923  47.509  1.00 49.66           C  
ANISOU 2382  CG  LEU X 119     6324   5894   6652    413    376  -1066       C  
ATOM   2383  CD1 LEU X 119      16.050  19.045  46.681  1.00 45.21           C  
ANISOU 2383  CD1 LEU X 119     5820   5332   6025    476    457  -1007       C  
ATOM   2384  CD2 LEU X 119      16.427  17.537  48.637  1.00 56.12           C  
ANISOU 2384  CD2 LEU X 119     7027   6704   7590    367    429  -1006       C  
ATOM   2385  N   ARG X 120      12.541  16.214  46.498  1.00 68.10           N  
ANISOU 2385  N   ARG X 120     8788   8206   8880    388     96  -1325       N  
ATOM   2386  CA  ARG X 120      12.440  15.060  45.624  1.00 69.19           C  
ANISOU 2386  CA  ARG X 120     9048   8284   8958    422     71  -1404       C  
ATOM   2387  C   ARG X 120      11.614  15.391  44.385  1.00 77.41           C  
ANISOU 2387  C   ARG X 120    10211   9334   9869    489    -37  -1484       C  
ATOM   2388  O   ARG X 120      12.129  15.403  43.270  1.00 85.76           O  
ANISOU 2388  O   ARG X 120    11427  10359  10798    593      8  -1486       O  
ATOM   2389  CB  ARG X 120      11.836  13.870  46.357  1.00 64.25           C  
ANISOU 2389  CB  ARG X 120     8361   7620   8430    326     15  -1464       C  
ATOM   2390  CG  ARG X 120      11.618  12.698  45.444  1.00 75.36           C  
ANISOU 2390  CG  ARG X 120     9905   8951   9778    351    -31  -1562       C  
ATOM   2391  CD  ARG X 120      10.603  11.710  46.001  1.00 83.34           C  
ANISOU 2391  CD  ARG X 120    10854   9922  10889    237   -124  -1644       C  
ATOM   2392  NE  ARG X 120      10.202  10.767  44.963  1.00 96.45           N  
ANISOU 2392  NE  ARG X 120    12658  11506  12481    256   -207  -1760       N  
ATOM   2393  CZ  ARG X 120       9.483   9.673  45.172  1.00105.73           C  
ANISOU 2393  CZ  ARG X 120    13824  12612  13735    161   -279  -1846       C  
ATOM   2394  NH1 ARG X 120       9.075   9.367  46.396  1.00109.54           N  
ANISOU 2394  NH1 ARG X 120    14161  13093  14367     46   -259  -1819       N  
ATOM   2395  NH2 ARG X 120       9.177   8.884  44.150  1.00108.36           N  
ANISOU 2395  NH2 ARG X 120    14306  12869  13995    183   -367  -1959       N  
ATOM   2396  N   ILE X 121      10.334  15.668  44.589  1.00 78.31           N  
ANISOU 2396  N   ILE X 121    10250   9490  10013    438   -178  -1548       N  
ATOM   2397  CA  ILE X 121       9.431  15.971  43.487  1.00 75.70           C  
ANISOU 2397  CA  ILE X 121    10018   9176   9570    503   -317  -1633       C  
ATOM   2398  C   ILE X 121      10.083  16.866  42.430  1.00 71.55           C  
ANISOU 2398  C   ILE X 121     9652   8652   8881    639   -253  -1582       C  
ATOM   2399  O   ILE X 121       9.953  16.609  41.233  1.00 75.06           O  
ANISOU 2399  O   ILE X 121    10272   9063   9182    732   -309  -1645       O  
ATOM   2400  CB  ILE X 121       8.132  16.625  43.993  1.00 79.01           C  
ANISOU 2400  CB  ILE X 121    10293   9667  10059    451   -448  -1668       C  
ATOM   2401  CG1 ILE X 121       7.506  15.774  45.106  1.00 80.85           C  
ANISOU 2401  CG1 ILE X 121    10364   9893  10463    312   -477  -1703       C  
ATOM   2402  CG2 ILE X 121       7.160  16.797  42.854  1.00 80.38           C  
ANISOU 2402  CG2 ILE X 121    10557   9858  10127    522   -621  -1769       C  
ATOM   2403  CD1 ILE X 121       6.204  16.344  45.697  1.00 74.66           C  
ANISOU 2403  CD1 ILE X 121     9415   9180   9773    258   -580  -1732       C  
ATOM   2404  N   LEU X 122      10.774  17.916  42.870  1.00 60.30           N  
ANISOU 2404  N   LEU X 122     8178   7256   7477    652   -136  -1468       N  
ATOM   2405  CA  LEU X 122      11.498  18.799  41.954  1.00 58.91           C  
ANISOU 2405  CA  LEU X 122     8147   7068   7168    768    -38  -1399       C  
ATOM   2406  C   LEU X 122      12.572  18.057  41.161  1.00 68.46           C  
ANISOU 2406  C   LEU X 122     9505   8210   8298    843     93  -1381       C  
ATOM   2407  O   LEU X 122      12.640  18.163  39.939  1.00 79.11           O  
ANISOU 2407  O   LEU X 122    11052   9528   9480    962    101  -1399       O  
ATOM   2408  CB  LEU X 122      12.198  19.932  42.711  1.00 54.70           C  
ANISOU 2408  CB  LEU X 122     7515   6559   6709    739     82  -1277       C  
ATOM   2409  CG  LEU X 122      11.347  20.989  43.389  1.00 66.32           C  
ANISOU 2409  CG  LEU X 122     8881   8089   8230    700     -4  -1269       C  
ATOM   2410  CD1 LEU X 122      12.200  22.220  43.708  1.00 70.07           C  
ANISOU 2410  CD1 LEU X 122     9338   8558   8726    704    125  -1151       C  
ATOM   2411  CD2 LEU X 122      10.208  21.337  42.473  1.00 63.65           C  
ANISOU 2411  CD2 LEU X 122     8640   7773   7769    784   -153  -1344       C  
ATOM   2412  N   VAL X 123      13.428  17.339  41.885  1.00 70.00           N  
ANISOU 2412  N   VAL X 123     9610   8379   8607    784    200  -1340       N  
ATOM   2413  CA  VAL X 123      14.615  16.708  41.324  1.00 72.84           C  
ANISOU 2413  CA  VAL X 123    10073   8679   8925    857    358  -1300       C  
ATOM   2414  C   VAL X 123      14.217  15.668  40.276  1.00 80.21           C  
ANISOU 2414  C   VAL X 123    11199   9553   9725    930    289  -1410       C  
ATOM   2415  O   VAL X 123      14.928  15.462  39.299  1.00 84.38           O  
ANISOU 2415  O   VAL X 123    11900  10030  10131   1047    403  -1392       O  
ATOM   2416  CB  VAL X 123      15.490  16.085  42.443  1.00 61.95           C  
ANISOU 2416  CB  VAL X 123     8536   7290   7711    780    454  -1242       C  
ATOM   2417  CG1 VAL X 123      16.575  15.242  41.861  1.00 70.29           C  
ANISOU 2417  CG1 VAL X 123     9691   8284   8733    865    600  -1218       C  
ATOM   2418  CG2 VAL X 123      16.105  17.171  43.301  1.00 59.58           C  
ANISOU 2418  CG2 VAL X 123     8081   7036   7520    729    531  -1132       C  
ATOM   2419  N   LEU X 124      13.060  15.042  40.473  1.00 85.35           N  
ANISOU 2419  N   LEU X 124    11821  10205  10401    861    104  -1526       N  
ATOM   2420  CA  LEU X 124      12.501  14.121  39.486  1.00 90.81           C  
ANISOU 2420  CA  LEU X 124    12695  10837  10971    914     -8  -1653       C  
ATOM   2421  C   LEU X 124      11.920  14.856  38.264  1.00 98.50           C  
ANISOU 2421  C   LEU X 124    13849  11824  11752   1031   -105  -1698       C  
ATOM   2422  O   LEU X 124      12.409  14.687  37.145  1.00100.34           O  
ANISOU 2422  O   LEU X 124    14311  12002  11812   1164    -41  -1706       O  
ATOM   2423  CB  LEU X 124      11.453  13.202  40.130  1.00 85.42           C  
ANISOU 2423  CB  LEU X 124    11905  10144  10407    784   -175  -1763       C  
ATOM   2424  CG  LEU X 124      11.956  12.331  41.291  1.00 76.25           C  
ANISOU 2424  CG  LEU X 124    10607   8951   9414    681    -86  -1725       C  
ATOM   2425  CD1 LEU X 124      10.903  11.319  41.741  1.00 69.66           C  
ANISOU 2425  CD1 LEU X 124     9708   8079   8679    559   -233  -1838       C  
ATOM   2426  CD2 LEU X 124      13.251  11.626  40.921  1.00 68.41           C  
ANISOU 2426  CD2 LEU X 124     9736   7884   8373    768     86  -1679       C  
ATOM   2427  N   ARG X 125      10.910  15.675  38.451  1.00 97.40           N  
ANISOU 2427  N   ARG X 125    13619  11756  11634    996   -256  -1724       N  
ATOM   2428  CA  ARG X 125      10.379  16.409  37.335  1.00 93.10           C  
ANISOU 2428  CA  ARG X 125    13239  11230  10906   1119   -358  -1756       C  
ATOM   2429  C   ARG X 125      11.516  17.045  36.594  1.00 95.09           C  
ANISOU 2429  C   ARG X 125    13659  11455  11018   1254   -152  -1639       C  
ATOM   2430  O   ARG X 125      11.418  17.350  35.427  1.00105.44           O  
ANISOU 2430  O   ARG X 125    15182  12751  12130   1392   -187  -1652       O  
ATOM   2431  CB  ARG X 125       9.441  17.486  37.831  1.00 20.00           C  
ATOM   2432  CG  ARG X 125       8.141  17.542  37.075  0.01 20.00           C  
ATOM   2433  CD  ARG X 125       7.208  16.424  37.495  0.01 20.00           C  
ATOM   2434  NE  ARG X 125       7.709  15.118  37.081  0.01 20.00           N  
ATOM   2435  CZ  ARG X 125       6.964  14.178  36.516  0.01 20.00           C  
ATOM   2436  NH1 ARG X 125       5.676  14.394  36.297  0.01 20.00           N  
ATOM   2437  NH2 ARG X 125       7.509  13.023  36.173  0.01 20.00           N  
ATOM   2438  N   LEU X 126      12.608  17.247  37.289  1.00 85.49           N  
ANISOU 2438  N   LEU X 126    12348  10228   9908   1215     63  -1523       N  
ATOM   2439  CA  LEU X 126      13.758  17.953  36.741  1.00 81.28           C  
ANISOU 2439  CA  LEU X 126    11925   9667   9292   1317    289  -1397       C  
ATOM   2440  C   LEU X 126      14.799  17.025  36.124  1.00 83.00           C  
ANISOU 2440  C   LEU X 126    12287   9807   9443   1399    457  -1383       C  
ATOM   2441  O   LEU X 126      15.707  17.468  35.419  1.00 83.70           O  
ANISOU 2441  O   LEU X 126    12507   9859   9434   1510    654  -1290       O  
ATOM   2442  CB  LEU X 126      14.423  18.771  37.830  1.00 77.43           C  
ANISOU 2442  CB  LEU X 126    11220   9220   8982   1223    418  -1270       C  
ATOM   2443  CG  LEU X 126      15.326  19.858  37.277  1.00 81.53           C  
ANISOU 2443  CG  LEU X 126    11828   9716   9431   1308    618  -1140       C  
ATOM   2444  CD1 LEU X 126      14.476  20.859  36.529  1.00 72.35           C  
ANISOU 2444  CD1 LEU X 126    10815   8566   8107   1397    515  -1155       C  
ATOM   2445  CD2 LEU X 126      16.099  20.521  38.407  1.00 89.64           C  
ANISOU 2445  CD2 LEU X 126    12629  10771  10659   1197    738  -1027       C  
ATOM   2446  N   SER X 127      14.681  15.736  36.402  1.00 80.95           N  
ANISOU 2446  N   SER X 127    12002   9514   9241   1348    395  -1470       N  
ATOM   2447  CA  SER X 127      15.648  14.772  35.889  1.00 84.64           C  
ANISOU 2447  CA  SER X 127    12603   9901   9654   1432    553  -1462       C  
ATOM   2448  C   SER X 127      15.086  14.097  34.644  1.00 91.90           C  
ANISOU 2448  C   SER X 127    13812  10753  10352   1548    440  -1591       C  
ATOM   2449  O   SER X 127      15.828  13.531  33.837  1.00 85.82           O  
ANISOU 2449  O   SER X 127    13243   9906   9457   1674    581  -1585       O  
ATOM   2450  CB  SER X 127      16.040  13.741  36.963  1.00 77.07           C  
ANISOU 2450  CB  SER X 127    11464   8929   8890   1321    582  -1465       C  
ATOM   2451  OG  SER X 127      15.034  12.769  37.179  1.00 73.16           O  
ANISOU 2451  OG  SER X 127    10970   8409   8420   1243    379  -1604       O  
ATOM   2452  N   LYS X 128      13.766  14.171  34.495  1.00101.64           N  
ANISOU 2452  N   LYS X 128    15065  12013  11540   1512    180  -1709       N  
ATOM   2453  CA  LYS X 128      13.108  13.739  33.273  1.00108.11           C  
ANISOU 2453  CA  LYS X 128    16163  12777  12137   1625     25  -1841       C  
ATOM   2454  C   LYS X 128      13.585  14.577  32.088  1.00110.74           C  
ANISOU 2454  C   LYS X 128    16756  13090  12232   1817    149  -1772       C  
ATOM   2455  O   LYS X 128      13.030  14.474  31.003  1.00117.24           O  
ANISOU 2455  O   LYS X 128    17838  13874  12833   1938     15  -1869       O  
ATOM   2456  CB  LYS X 128      11.584  13.855  33.414  1.00109.74           C  
ANISOU 2456  CB  LYS X 128    16290  13035  12370   1543   -288  -1969       C  
ATOM   2457  CG  LYS X 128      10.908  12.645  34.045  1.00112.26           C  
ANISOU 2457  CG  LYS X 128    16484  13326  12842   1393   -448  -2095       C  
ATOM   2458  CD  LYS X 128      11.182  11.385  33.224  1.00119.04           C  
ANISOU 2458  CD  LYS X 128    17594  14064  13571   1467   -454  -2200       C  
ATOM   2459  CE  LYS X 128      10.264  10.228  33.609  1.00115.07           C  
ANISOU 2459  CE  LYS X 128    17015  13515  13191   1323   -665  -2354       C  
ATOM   2460  NZ  LYS X 128      10.760   8.917  33.088  1.00111.41           N  
ANISOU 2460  NZ  LYS X 128    16769  12917  12647   1371   -618  -2433       N  
ATOM   2461  N   HIS X 129      14.612  15.399  32.297  1.00108.25           N  
ANISOU 2461  N   HIS X 129    16374  12793  11962   1844    403  -1606       N  
ATOM   2462  CA  HIS X 129      15.077  16.335  31.272  1.00109.62           C  
ANISOU 2462  CA  HIS X 129    16774  12944  11933   2011    553  -1515       C  
ATOM   2463  C   HIS X 129      16.580  16.573  31.348  1.00 98.78           C  
ANISOU 2463  C   HIS X 129    15366  11543  10624   2049    900  -1349       C  
ATOM   2464  O   HIS X 129      17.117  17.435  30.647  1.00 90.95           O  
ANISOU 2464  O   HIS X 129    14519  10528   9508   2165   1080  -1242       O  
ATOM   2465  CB  HIS X 129      14.359  17.686  31.399  1.00122.46           C  
ANISOU 2465  CB  HIS X 129    18337  14641  13551   1995    446  -1476       C  
ATOM   2466  CG  HIS X 129      12.956  17.683  30.881  1.00132.49           C  
ANISOU 2466  CG  HIS X 129    19721  15934  14687   2034    130  -1622       C  
ATOM   2467  ND1 HIS X 129      12.656  17.604  29.534  1.00134.04           N  
ANISOU 2467  ND1 HIS X 129    20261  16074  14596   2217     53  -1691       N  
ATOM   2468  CD2 HIS X 129      11.765  17.767  31.521  1.00136.73           C  
ANISOU 2468  CD2 HIS X 129    20070  16541  15339   1919   -132  -1713       C  
ATOM   2469  CE1 HIS X 129      11.349  17.626  29.373  1.00136.03           C  
ANISOU 2469  CE1 HIS X 129    20519  16366  14800   2209   -262  -1824       C  
ATOM   2470  NE2 HIS X 129      10.780  17.724  30.566  1.00136.48           N  
ANISOU 2470  NE2 HIS X 129    20245  16502  15108   2027   -372  -1837       N  
ATOM   2471  N   GLY X 130      17.254  15.826  32.217  1.00 94.73           N  
ANISOU 2471  N   GLY X 130    14651  11030  10314   1950    996  -1324       N  
ATOM   2472  CA  GLY X 130      18.692  15.958  32.385  1.00 93.02           C  
ANISOU 2472  CA  GLY X 130    14351  10794  10196   1975   1307  -1175       C  
ATOM   2473  C   GLY X 130      19.221  17.361  32.649  1.00 96.14           C  
ANISOU 2473  C   GLY X 130    14622  11230  10676   1945   1462  -1020       C  
ATOM   2474  O   GLY X 130      20.137  17.809  31.960  1.00 93.25           O  
ANISOU 2474  O   GLY X 130    14371  10821  10240   2055   1716   -907       O  
ATOM   2475  N   HIS X 131      18.650  18.056  33.635  1.00102.59           N  
ANISOU 2475  N   HIS X 131    15213  12121  11645   1798   1320  -1014       N  
ATOM   2476  CA  HIS X 131      19.182  19.343  34.079  1.00102.01           C  
ANISOU 2476  CA  HIS X 131    14993  12078  11688   1741   1454   -875       C  
ATOM   2477  C   HIS X 131      20.071  19.042  35.258  1.00103.40           C  
ANISOU 2477  C   HIS X 131    14875  12282  12131   1612   1550   -811       C  
ATOM   2478  O   HIS X 131      19.749  19.383  36.391  1.00104.28           O  
ANISOU 2478  O   HIS X 131    14759  12451  12409   1468   1432   -813       O  
ATOM   2479  CB  HIS X 131      18.066  20.283  34.530  1.00101.03           C  
ANISOU 2479  CB  HIS X 131    14800  12011  11574   1664   1243   -908       C  
ATOM   2480  CG  HIS X 131      17.121  20.684  33.437  1.00103.55           C  
ANISOU 2480  CG  HIS X 131    15391  12314  11640   1795   1115   -970       C  
ATOM   2481  ND1 HIS X 131      17.442  21.622  32.484  1.00102.06           N  
ANISOU 2481  ND1 HIS X 131    15412  12079  11288   1924   1264   -878       N  
ATOM   2482  CD2 HIS X 131      15.853  20.288  33.170  1.00106.72           C  
ANISOU 2482  CD2 HIS X 131    15881  12738  11930   1816    844  -1114       C  
ATOM   2483  CE1 HIS X 131      16.416  21.779  31.662  1.00103.12           C  
ANISOU 2483  CE1 HIS X 131    15771  12209  11201   2035   1081   -964       C  
ATOM   2484  NE2 HIS X 131      15.441  20.985  32.058  1.00105.91           N  
ANISOU 2484  NE2 HIS X 131    16044  12607  11590   1969    817  -1111       N  
ATOM   2485  N   SER X 132      21.189  18.390  34.981  1.00103.30           N  
ANISOU 2485  N   SER X 132    14874  12226  12150   1678   1762   -756       N  
ATOM   2486  CA  SER X 132      21.992  17.776  36.027  1.00 97.04           C  
ANISOU 2486  CA  SER X 132    13824  11456  11590   1584   1820   -721       C  
ATOM   2487  C   SER X 132      22.409  18.719  37.155  1.00 94.12           C  
ANISOU 2487  C   SER X 132    13171  11141  11448   1437   1836   -629       C  
ATOM   2488  O   SER X 132      22.467  18.308  38.313  1.00 94.40           O  
ANISOU 2488  O   SER X 132    12990  11217  11659   1324   1742   -648       O  
ATOM   2489  CB  SER X 132      23.239  17.136  35.428  1.00 91.92           C  
ANISOU 2489  CB  SER X 132    13232  10752  10941   1704   2083   -652       C  
ATOM   2490  OG  SER X 132      24.280  18.089  35.315  1.00 91.50           O  
ANISOU 2490  OG  SER X 132    13087  10696  10985   1709   2322   -502       O  
ATOM   2491  N   ASP X 133      22.717  19.971  36.834  1.00 87.53           N  
ANISOU 2491  N   ASP X 133    12352  10299  10609   1441   1956   -531       N  
ATOM   2492  CA  ASP X 133      23.310  20.849  37.842  1.00 86.69           C  
ANISOU 2492  CA  ASP X 133    11985  10225  10727   1304   1997   -440       C  
ATOM   2493  C   ASP X 133      22.277  21.691  38.575  1.00 80.59           C  
ANISOU 2493  C   ASP X 133    11149   9497   9974   1194   1783   -482       C  
ATOM   2494  O   ASP X 133      22.536  22.177  39.675  1.00 75.90           O  
ANISOU 2494  O   ASP X 133    10336   8937   9567   1063   1742   -448       O  
ATOM   2495  CB  ASP X 133      24.390  21.726  37.231  1.00 96.93           C  
ANISOU 2495  CB  ASP X 133    13293  11475  12062   1345   2271   -297       C  
ATOM   2496  CG  ASP X 133      23.968  22.305  35.927  1.00106.57           C  
ANISOU 2496  CG  ASP X 133    14812  12640  13039   1476   2349   -281       C  
ATOM   2497  OD1 ASP X 133      22.755  22.237  35.620  1.00111.27           O  
ANISOU 2497  OD1 ASP X 133    15577  13247  13454   1517   2148   -383       O  
ATOM   2498  OD2 ASP X 133      24.850  22.816  35.213  1.00109.96           O  
ANISOU 2498  OD2 ASP X 133    15305  13014  13462   1542   2610   -164       O  
ATOM   2499  N   ALA X 134      21.109  21.859  37.969  1.00 85.25           N  
ANISOU 2499  N   ALA X 134    11935  10086  10370   1254   1643   -560       N  
ATOM   2500  CA  ALA X 134      19.981  22.408  38.702  1.00 87.63           C  
ANISOU 2500  CA  ALA X 134    12169  10438  10690   1164   1419   -621       C  
ATOM   2501  C   ALA X 134      19.793  21.524  39.933  1.00 87.07           C  
ANISOU 2501  C   ALA X 134    11894  10416  10773   1051   1282   -687       C  
ATOM   2502  O   ALA X 134      19.678  22.019  41.064  1.00 86.21           O  
ANISOU 2502  O   ALA X 134    11603  10344  10806    931   1204   -674       O  
ATOM   2503  CB  ALA X 134      18.726  22.422  37.839  1.00 89.94           C  
ANISOU 2503  CB  ALA X 134    12685  10729  10758   1260   1265   -715       C  
ATOM   2504  N   ILE X 135      19.787  20.211  39.696  1.00 81.26           N  
ANISOU 2504  N   ILE X 135    11211   9667   9998   1097   1262   -755       N  
ATOM   2505  CA  ILE X 135      19.704  19.209  40.755  1.00 74.17           C  
ANISOU 2505  CA  ILE X 135    10154   8796   9232   1009   1162   -809       C  
ATOM   2506  C   ILE X 135      20.820  19.348  41.809  1.00 70.18           C  
ANISOU 2506  C   ILE X 135     9417   8308   8941    924   1256   -719       C  
ATOM   2507  O   ILE X 135      20.568  19.222  43.008  1.00 66.23           O  
ANISOU 2507  O   ILE X 135     8756   7845   8562    818   1140   -740       O  
ATOM   2508  CB  ILE X 135      19.666  17.765  40.172  1.00 67.65           C  
ANISOU 2508  CB  ILE X 135     9456   7928   8321   1088   1158   -888       C  
ATOM   2509  CG1 ILE X 135      18.257  17.414  39.660  1.00 66.49           C  
ANISOU 2509  CG1 ILE X 135     9461   7778   8023   1110    959  -1019       C  
ATOM   2510  CG2 ILE X 135      20.111  16.758  41.215  1.00 58.50           C  
ANISOU 2510  CG2 ILE X 135     8132   6774   7322   1019   1147   -895       C  
ATOM   2511  CD1 ILE X 135      18.167  16.069  38.967  1.00 55.27           C  
ANISOU 2511  CD1 ILE X 135     8203   6298   6501   1188    943  -1109       C  
ATOM   2512  N   GLN X 136      22.043  19.622  41.373  1.00 72.79           N  
ANISOU 2512  N   GLN X 136     9728   8610   9318    973   1464   -618       N  
ATOM   2513  CA  GLN X 136      23.144  19.844  42.306  1.00 75.99           C  
ANISOU 2513  CA  GLN X 136     9900   9033   9938    893   1542   -533       C  
ATOM   2514  C   GLN X 136      22.847  20.950  43.317  1.00 76.84           C  
ANISOU 2514  C   GLN X 136     9870   9177  10149    764   1433   -514       C  
ATOM   2515  O   GLN X 136      23.004  20.755  44.532  1.00 75.62           O  
ANISOU 2515  O   GLN X 136     9541   9056  10136    672   1340   -521       O  
ATOM   2516  CB  GLN X 136      24.424  20.180  41.548  1.00 89.70           C  
ANISOU 2516  CB  GLN X 136    11632  10731  11717    962   1795   -421       C  
ATOM   2517  CG  GLN X 136      24.955  19.039  40.694  1.00108.13           C  
ANISOU 2517  CG  GLN X 136    14079  13028  13979   1099   1934   -426       C  
ATOM   2518  CD  GLN X 136      25.411  17.846  41.524  1.00118.35           C  
ANISOU 2518  CD  GLN X 136    15228  14340  15400   1085   1892   -451       C  
ATOM   2519  OE1 GLN X 136      25.206  17.799  42.746  1.00124.22           O  
ANISOU 2519  OE1 GLN X 136    15807  15126  16265    975   1738   -474       O  
ATOM   2520  NE2 GLN X 136      26.035  16.873  40.863  1.00114.38           N  
ANISOU 2520  NE2 GLN X 136    14803  13797  14858   1209   2033   -443       N  
ATOM   2521  N   MET X 137      22.431  22.109  42.802  1.00 73.09           N  
ANISOU 2521  N   MET X 137     9492   8687   9592    768   1448   -490       N  
ATOM   2522  CA  MET X 137      22.158  23.294  43.618  1.00 64.07           C  
ANISOU 2522  CA  MET X 137     8254   7560   8528    660   1365   -469       C  
ATOM   2523  C   MET X 137      21.036  23.027  44.615  1.00 56.36           C  
ANISOU 2523  C   MET X 137     7231   6633   7551    593   1144   -562       C  
ATOM   2524  O   MET X 137      21.154  23.345  45.797  1.00 60.94           O  
ANISOU 2524  O   MET X 137     7660   7235   8257    493   1068   -554       O  
ATOM   2525  CB  MET X 137      21.832  24.502  42.718  1.00 72.74           C  
ANISOU 2525  CB  MET X 137     9511   8619   9508    705   1430   -428       C  
ATOM   2526  CG  MET X 137      21.263  25.728  43.439  1.00 80.24           C  
ANISOU 2526  CG  MET X 137    10419   9575  10496    616   1324   -425       C  
ATOM   2527  SD  MET X 137      19.464  25.700  43.549  1.00 81.45           S  
ANISOU 2527  SD  MET X 137    10678   9773  10496    644   1093   -541       S  
ATOM   2528  CE  MET X 137      19.055  25.687  41.816  1.00 66.60           C  
ANISOU 2528  CE  MET X 137     9069   7856   8380    809   1162   -547       C  
ATOM   2529  N   LEU X 138      19.950  22.428  44.148  1.00 53.26           N  
ANISOU 2529  N   LEU X 138     6968   6252   7016    650   1042   -650       N  
ATOM   2530  CA  LEU X 138      18.902  22.034  45.077  1.00 59.74           C  
ANISOU 2530  CA  LEU X 138     7729   7116   7855    586    857   -734       C  
ATOM   2531  C   LEU X 138      19.498  21.333  46.303  1.00 62.41           C  
ANISOU 2531  C   LEU X 138     7895   7470   8347    508    836   -725       C  
ATOM   2532  O   LEU X 138      19.257  21.737  47.456  1.00 56.82           O  
ANISOU 2532  O   LEU X 138     7077   6789   7723    422    746   -727       O  
ATOM   2533  CB  LEU X 138      17.870  21.151  44.392  1.00 51.84           C  
ANISOU 2533  CB  LEU X 138     6861   6118   6720    649    763   -834       C  
ATOM   2534  CG  LEU X 138      17.051  21.898  43.339  1.00 56.19           C  
ANISOU 2534  CG  LEU X 138     7578   6663   7107    728    725   -858       C  
ATOM   2535  CD1 LEU X 138      15.917  21.026  42.884  1.00 62.19           C  
ANISOU 2535  CD1 LEU X 138     8430   7433   7765    765    582   -975       C  
ATOM   2536  CD2 LEU X 138      16.529  23.240  43.898  1.00 50.22           C  
ANISOU 2536  CD2 LEU X 138     6772   5931   6378    679    664   -832       C  
ATOM   2537  N   ILE X 139      20.309  20.311  46.053  1.00 58.10           N  
ANISOU 2537  N   ILE X 139     7339   6905   7833    552    923   -712       N  
ATOM   2538  CA  ILE X 139      20.892  19.547  47.139  1.00 54.63           C  
ANISOU 2538  CA  ILE X 139     6754   6476   7525    504    900   -702       C  
ATOM   2539  C   ILE X 139      21.835  20.383  47.983  1.00 57.79           C  
ANISOU 2539  C   ILE X 139     6993   6889   8075    434    927   -624       C  
ATOM   2540  O   ILE X 139      21.812  20.312  49.218  1.00 55.63           O  
ANISOU 2540  O   ILE X 139     6610   6638   7887    362    827   -632       O  
ATOM   2541  CB  ILE X 139      21.598  18.284  46.630  1.00 51.28           C  
ANISOU 2541  CB  ILE X 139     6363   6022   7101    585    995   -700       C  
ATOM   2542  CG1 ILE X 139      20.556  17.270  46.181  1.00 44.97           C  
ANISOU 2542  CG1 ILE X 139     5704   5201   6180    622    915   -800       C  
ATOM   2543  CG2 ILE X 139      22.484  17.694  47.716  1.00 48.22           C  
ANISOU 2543  CG2 ILE X 139     5813   5644   6866    553    993   -663       C  
ATOM   2544  CD1 ILE X 139      21.150  16.092  45.480  1.00 55.08           C  
ANISOU 2544  CD1 ILE X 139     7068   6434   7425    718   1013   -809       C  
ATOM   2545  N   LYS X 140      22.655  21.192  47.328  1.00 58.11           N  
ANISOU 2545  N   LYS X 140     7024   6908   8145    452   1060   -550       N  
ATOM   2546  CA  LYS X 140      23.583  22.021  48.071  1.00 59.88           C  
ANISOU 2546  CA  LYS X 140     7086   7135   8530    372   1080   -481       C  
ATOM   2547  C   LYS X 140      22.836  23.055  48.935  1.00 63.87           C  
ANISOU 2547  C   LYS X 140     7577   7653   9037    280    944   -506       C  
ATOM   2548  O   LYS X 140      23.079  23.182  50.143  1.00 55.84           O  
ANISOU 2548  O   LYS X 140     6440   6654   8125    204    848   -508       O  
ATOM   2549  CB  LYS X 140      24.574  22.700  47.132  1.00 63.52           C  
ANISOU 2549  CB  LYS X 140     7540   7558   9035    400   1271   -393       C  
ATOM   2550  CG  LYS X 140      25.623  23.513  47.891  1.00 82.00           C  
ANISOU 2550  CG  LYS X 140     9687   9894  11575    301   1288   -326       C  
ATOM   2551  CD  LYS X 140      26.866  23.739  47.062  1.00 97.23           C  
ANISOU 2551  CD  LYS X 140    11551  11789  13603    333   1505   -230       C  
ATOM   2552  CE  LYS X 140      27.516  22.405  46.725  1.00113.64           C  
ANISOU 2552  CE  LYS X 140    13593  13882  15704    433   1595   -221       C  
ATOM   2553  NZ  LYS X 140      26.648  21.552  45.852  1.00119.92           N  
ANISOU 2553  NZ  LYS X 140    14606  14669  16288    547   1609   -281       N  
ATOM   2554  N   THR X 141      21.909  23.780  48.317  1.00 60.70           N  
ANISOU 2554  N   THR X 141     7312   7240   8510    299    931   -528       N  
ATOM   2555  CA  THR X 141      21.196  24.803  49.064  1.00 63.04           C  
ANISOU 2555  CA  THR X 141     7607   7542   8803    230    820   -548       C  
ATOM   2556  C   THR X 141      20.269  24.185  50.118  1.00 63.07           C  
ANISOU 2556  C   THR X 141     7587   7588   8790    200    664   -622       C  
ATOM   2557  O   THR X 141      19.991  24.818  51.136  1.00 57.81           O  
ANISOU 2557  O   THR X 141     6875   6928   8162    135    573   -632       O  
ATOM   2558  CB  THR X 141      20.498  25.871  48.149  1.00 67.08           C  
ANISOU 2558  CB  THR X 141     8267   8026   9193    270    851   -541       C  
ATOM   2559  OG1 THR X 141      19.328  25.331  47.527  1.00 54.18           O  
ANISOU 2559  OG1 THR X 141     6761   6418   7409    347    789   -611       O  
ATOM   2560  CG2 THR X 141      21.466  26.350  47.069  1.00 78.27           C  
ANISOU 2560  CG2 THR X 141     9727   9392  10621    308   1036   -456       C  
ATOM   2561  N   THR X 142      19.830  22.942  49.912  1.00 58.18           N  
ANISOU 2561  N   THR X 142     7001   6986   8117    247    642   -672       N  
ATOM   2562  CA  THR X 142      19.059  22.276  50.953  1.00 50.89           C  
ANISOU 2562  CA  THR X 142     6046   6091   7199    211    521   -730       C  
ATOM   2563  C   THR X 142      19.886  21.981  52.220  1.00 52.97           C  
ANISOU 2563  C   THR X 142     6183   6358   7583    158    487   -701       C  
ATOM   2564  O   THR X 142      19.368  22.030  53.347  1.00 50.51           O  
ANISOU 2564  O   THR X 142     5847   6062   7284    112    390   -727       O  
ATOM   2565  CB  THR X 142      18.335  21.022  50.464  1.00 52.93           C  
ANISOU 2565  CB  THR X 142     6374   6352   7383    258    501   -794       C  
ATOM   2566  OG1 THR X 142      17.456  21.359  49.372  1.00 54.06           O  
ANISOU 2566  OG1 THR X 142     6636   6496   7406    309    493   -833       O  
ATOM   2567  CG2 THR X 142      17.508  20.437  51.611  1.00 42.41           C  
ANISOU 2567  CG2 THR X 142     5003   5039   6071    207    396   -842       C  
ATOM   2568  N   SER X 143      21.180  21.726  52.067  1.00 51.55           N  
ANISOU 2568  N   SER X 143     5927   6167   7495    171    565   -647       N  
ATOM   2569  CA  SER X 143      21.974  21.422  53.262  1.00 58.38           C  
ANISOU 2569  CA  SER X 143     6669   7038   8473    133    508   -624       C  
ATOM   2570  C   SER X 143      22.550  22.663  53.919  1.00 60.93           C  
ANISOU 2570  C   SER X 143     6911   7356   8885     59    467   -590       C  
ATOM   2571  O   SER X 143      22.713  22.694  55.133  1.00 61.56           O  
ANISOU 2571  O   SER X 143     6934   7443   9014     16    362   -598       O  
ATOM   2572  CB  SER X 143      23.079  20.411  52.973  1.00 57.38           C  
ANISOU 2572  CB  SER X 143     6473   6907   8420    189    587   -588       C  
ATOM   2573  OG  SER X 143      23.881  20.849  51.901  1.00 62.52           O  
ANISOU 2573  OG  SER X 143     7105   7542   9108    218    725   -535       O  
ATOM   2574  N   GLN X 144      22.873  23.673  53.114  1.00 65.95           N  
ANISOU 2574  N   GLN X 144     7555   7966   9535     45    552   -552       N  
ATOM   2575  CA  GLN X 144      23.228  24.993  53.643  1.00 66.89           C  
ANISOU 2575  CA  GLN X 144     7627   8061   9729    -38    512   -530       C  
ATOM   2576  C   GLN X 144      22.065  25.531  54.468  1.00 55.51           C  
ANISOU 2576  C   GLN X 144     6267   6623   8200    -68    389   -584       C  
ATOM   2577  O   GLN X 144      22.249  25.961  55.604  1.00 50.30           O  
ANISOU 2577  O   GLN X 144     5564   5957   7592   -126    285   -595       O  
ATOM   2578  CB  GLN X 144      23.522  25.984  52.515  1.00 89.27           C  
ANISOU 2578  CB  GLN X 144    10499  10852  12567    -41    642   -480       C  
ATOM   2579  CG  GLN X 144      24.738  25.668  51.661  1.00115.25           C  
ANISOU 2579  CG  GLN X 144    13706  14129  15956    -12    799   -411       C  
ATOM   2580  CD  GLN X 144      24.937  26.680  50.539  1.00127.40           C  
ANISOU 2580  CD  GLN X 144    15312  15614  17480    -11    949   -354       C  
ATOM   2581  OE1 GLN X 144      23.980  27.321  50.077  1.00128.56           O  
ANISOU 2581  OE1 GLN X 144    15610  15742  17495     11    945   -373       O  
ATOM   2582  NE2 GLN X 144      26.186  26.824  50.091  1.00130.50           N  
ANISOU 2582  NE2 GLN X 144    15590  15979  18014    -27   1089   -278       N  
ATOM   2583  N   TYR X 145      20.864  25.489  53.894  1.00 41.55           N  
ANISOU 2583  N   TYR X 145     4618   4866   6301    -21    399   -621       N  
ATOM   2584  CA  TYR X 145      19.682  25.955  54.599  1.00 50.23           C  
ANISOU 2584  CA  TYR X 145     5786   5975   7323    -35    303   -670       C  
ATOM   2585  C   TYR X 145      19.495  25.225  55.908  1.00 58.81           C  
ANISOU 2585  C   TYR X 145     6836   7085   8424    -53    206   -701       C  
ATOM   2586  O   TYR X 145      19.291  25.851  56.956  1.00 60.18           O  
ANISOU 2586  O   TYR X 145     7019   7248   8599    -91    124   -716       O  
ATOM   2587  CB  TYR X 145      18.441  25.763  53.756  1.00 50.99           C  
ANISOU 2587  CB  TYR X 145     5985   6092   7297     28    319   -709       C  
ATOM   2588  CG  TYR X 145      17.252  26.503  54.294  1.00 55.14           C  
ANISOU 2588  CG  TYR X 145     6569   6625   7757     25    245   -748       C  
ATOM   2589  CD1 TYR X 145      16.486  25.981  55.341  1.00 54.21           C  
ANISOU 2589  CD1 TYR X 145     6438   6534   7624     14    170   -790       C  
ATOM   2590  CD2 TYR X 145      16.887  27.737  53.753  1.00 60.73           C  
ANISOU 2590  CD2 TYR X 145     7352   7307   8417     41    264   -737       C  
ATOM   2591  CE1 TYR X 145      15.370  26.678  55.834  1.00 57.93           C  
ANISOU 2591  CE1 TYR X 145     6957   7014   8040     23    121   -822       C  
ATOM   2592  CE2 TYR X 145      15.785  28.442  54.227  1.00 60.73           C  
ANISOU 2592  CE2 TYR X 145     7405   7312   8357     55    202   -770       C  
ATOM   2593  CZ  TYR X 145      15.030  27.920  55.271  1.00 66.33           C  
ANISOU 2593  CZ  TYR X 145     8088   8056   9060     47    133   -813       C  
ATOM   2594  OH  TYR X 145      13.939  28.650  55.726  1.00 65.70           O  
ANISOU 2594  OH  TYR X 145     8054   7982   8927     72     91   -842       O  
ATOM   2595  N   SER X 146      19.554  23.898  55.849  1.00 54.16           N  
ANISOU 2595  N   SER X 146     6225   6517   7835    -17    220   -710       N  
ATOM   2596  CA  SER X 146      19.354  23.104  57.049  1.00 49.01           C  
ANISOU 2596  CA  SER X 146     5560   5877   7185    -24    145   -730       C  
ATOM   2597  C   SER X 146      20.345  23.524  58.117  1.00 49.30           C  
ANISOU 2597  C   SER X 146     5528   5899   7303    -65     71   -705       C  
ATOM   2598  O   SER X 146      19.989  23.628  59.310  1.00 46.78           O  
ANISOU 2598  O   SER X 146     5241   5579   6956    -81    -16   -726       O  
ATOM   2599  CB  SER X 146      19.508  21.615  56.744  1.00 47.72           C  
ANISOU 2599  CB  SER X 146     5386   5720   7025     21    184   -733       C  
ATOM   2600  OG  SER X 146      18.459  21.164  55.914  1.00 47.40           O  
ANISOU 2600  OG  SER X 146     5417   5686   6907     50    220   -774       O  
ATOM   2601  N   ASP X 147      21.586  23.737  57.669  1.00 49.89           N  
ANISOU 2601  N   ASP X 147     5511   5964   7480    -78    108   -662       N  
ATOM   2602  CA  ASP X 147      22.730  24.071  58.525  1.00 56.04           C  
ANISOU 2602  CA  ASP X 147     6191   6732   8371   -121     29   -639       C  
ATOM   2603  C   ASP X 147      22.513  25.383  59.275  1.00 56.87           C  
ANISOU 2603  C   ASP X 147     6334   6806   8466   -186    -61   -660       C  
ATOM   2604  O   ASP X 147      22.792  25.500  60.485  1.00 56.62           O  
ANISOU 2604  O   ASP X 147     6296   6766   8451   -209   -185   -677       O  
ATOM   2605  CB  ASP X 147      24.001  24.151  57.670  1.00 53.54           C  
ANISOU 2605  CB  ASP X 147     5750   6408   8184   -127    116   -585       C  
ATOM   2606  CG  ASP X 147      25.278  24.216  58.501  1.00 60.35           C  
ANISOU 2606  CG  ASP X 147     6469   7269   9192   -163     24   -563       C  
ATOM   2607  OD1 ASP X 147      25.399  23.488  59.517  1.00 54.20           O  
ANISOU 2607  OD1 ASP X 147     5680   6508   8406   -135    -83   -579       O  
ATOM   2608  OD2 ASP X 147      26.174  24.999  58.112  1.00 68.63           O  
ANISOU 2608  OD2 ASP X 147     7414   8295  10367   -218     61   -528       O  
ATOM   2609  N   GLU X 148      21.985  26.351  58.535  1.00 58.03           N  
ANISOU 2609  N   GLU X 148     6543   6931   8575   -204      0   -661       N  
ATOM   2610  CA  GLU X 148      21.675  27.679  59.044  1.00 59.87           C  
ANISOU 2610  CA  GLU X 148     6839   7121   8789   -257    -61   -681       C  
ATOM   2611  C   GLU X 148      20.409  27.722  59.902  1.00 56.67           C  
ANISOU 2611  C   GLU X 148     6552   6724   8255   -228   -126   -731       C  
ATOM   2612  O   GLU X 148      20.430  28.223  61.025  1.00 61.40           O  
ANISOU 2612  O   GLU X 148     7190   7298   8842   -255   -229   -756       O  
ATOM   2613  CB  GLU X 148      21.527  28.651  57.864  1.00 62.58           C  
ANISOU 2613  CB  GLU X 148     7222   7429   9127   -268     44   -656       C  
ATOM   2614  CG  GLU X 148      22.847  29.010  57.209  1.00 77.75           C  
ANISOU 2614  CG  GLU X 148     9032   9317  11191   -319    117   -600       C  
ATOM   2615  CD  GLU X 148      22.691  29.673  55.845  1.00 93.35           C  
ANISOU 2615  CD  GLU X 148    11069  11260  13141   -303    260   -560       C  
ATOM   2616  OE1 GLU X 148      23.727  29.867  55.170  1.00 98.27           O  
ANISOU 2616  OE1 GLU X 148    11607  11854  13878   -334    360   -503       O  
ATOM   2617  OE2 GLU X 148      21.548  29.996  55.444  1.00 96.94           O  
ANISOU 2617  OE2 GLU X 148    11654  11715  13463   -253    278   -582       O  
ATOM   2618  N   LYS X 149      19.308  27.216  59.354  1.00 49.77           N  
ANISOU 2618  N   LYS X 149     5736   5884   7290   -171    -63   -746       N  
ATOM   2619  CA  LYS X 149      17.995  27.396  59.959  1.00 54.54           C  
ANISOU 2619  CA  LYS X 149     6436   6498   7789   -142    -92   -786       C  
ATOM   2620  C   LYS X 149      17.464  26.212  60.759  1.00 52.71           C  
ANISOU 2620  C   LYS X 149     6215   6298   7515   -110   -114   -805       C  
ATOM   2621  O   LYS X 149      16.629  26.407  61.621  1.00 53.06           O  
ANISOU 2621  O   LYS X 149     6329   6339   7492    -95   -143   -830       O  
ATOM   2622  CB  LYS X 149      16.973  27.774  58.892  1.00 57.79           C  
ANISOU 2622  CB  LYS X 149     6899   6923   8136   -102    -22   -796       C  
ATOM   2623  CG  LYS X 149      17.469  28.843  57.938  1.00 62.49           C  
ANISOU 2623  CG  LYS X 149     7506   7477   8759   -120     26   -766       C  
ATOM   2624  CD  LYS X 149      17.424  30.205  58.579  1.00 68.33           C  
ANISOU 2624  CD  LYS X 149     8311   8160   9491   -153    -23   -774       C  
ATOM   2625  CE  LYS X 149      18.667  31.037  58.230  1.00 84.99           C  
ANISOU 2625  CE  LYS X 149    10384  10206  11702   -222     -4   -734       C  
ATOM   2626  NZ  LYS X 149      18.628  31.711  56.905  1.00 84.04           N  
ANISOU 2626  NZ  LYS X 149    10307  10055  11569   -204     99   -697       N  
ATOM   2627  N   LEU X 150      17.937  24.994  60.505  1.00 50.08           N  
ANISOU 2627  N   LEU X 150     5823   5986   7221    -95    -89   -789       N  
ATOM   2628  CA  LEU X 150      17.306  23.818  61.123  1.00 37.23           C  
ANISOU 2628  CA  LEU X 150     4221   4375   5550    -65    -87   -802       C  
ATOM   2629  C   LEU X 150      18.157  23.125  62.172  1.00 43.36           C  
ANISOU 2629  C   LEU X 150     4983   5139   6354    -60   -150   -783       C  
ATOM   2630  O   LEU X 150      17.630  22.441  63.074  1.00 42.90           O  
ANISOU 2630  O   LEU X 150     4983   5076   6242    -36   -162   -788       O  
ATOM   2631  CB  LEU X 150      16.907  22.812  60.064  1.00 40.25           C  
ANISOU 2631  CB  LEU X 150     4582   4777   5932    -41    -10   -808       C  
ATOM   2632  CG  LEU X 150      15.989  23.191  58.891  1.00 48.45           C  
ANISOU 2632  CG  LEU X 150     5642   5834   6933    -27     40   -834       C  
ATOM   2633  CD1 LEU X 150      15.811  21.964  57.972  1.00 48.24           C  
ANISOU 2633  CD1 LEU X 150     5605   5817   6908     -3     91   -848       C  
ATOM   2634  CD2 LEU X 150      14.591  23.681  59.362  1.00 44.81           C  
ANISOU 2634  CD2 LEU X 150     5229   5386   6411    -21     27   -868       C  
ATOM   2635  N   LYS X 151      19.473  23.304  62.053  1.00 41.06           N  
ANISOU 2635  N   LYS X 151     4612   4840   6149    -77   -189   -757       N  
ATOM   2636  CA  LYS X 151      20.415  22.530  62.850  1.00 42.52           C  
ANISOU 2636  CA  LYS X 151     4760   5022   6375    -55   -258   -736       C  
ATOM   2637  C   LYS X 151      20.157  22.630  64.349  1.00 47.96           C  
ANISOU 2637  C   LYS X 151     5543   5691   6990    -42   -356   -751       C  
ATOM   2638  O   LYS X 151      20.198  21.619  65.060  1.00 49.81           O  
ANISOU 2638  O   LYS X 151     5815   5920   7190      4   -377   -738       O  
ATOM   2639  CB  LYS X 151      21.853  22.917  62.525  1.00 44.52           C  
ANISOU 2639  CB  LYS X 151     4888   5273   6755    -82   -294   -708       C  
ATOM   2640  CG  LYS X 151      22.890  22.015  63.170  1.00 45.21           C  
ANISOU 2640  CG  LYS X 151     4909   5366   6902    -42   -367   -683       C  
ATOM   2641  CD  LYS X 151      24.151  22.776  63.536  1.00 54.76           C  
ANISOU 2641  CD  LYS X 151     6008   6569   8230    -85   -476   -675       C  
ATOM   2642  CE  LYS X 151      24.494  23.835  62.508  1.00 58.06           C  
ANISOU 2642  CE  LYS X 151     6346   6977   8738   -155   -408   -664       C  
ATOM   2643  NZ  LYS X 151      25.968  24.044  62.448  1.00 54.58           N  
ANISOU 2643  NZ  LYS X 151     5729   6536   8471   -187   -457   -635       N  
ATOM   2644  N   ASN X 152      19.867  23.832  64.836  1.00 47.31           N  
ANISOU 2644  N   ASN X 152     5520   5588   6868    -74   -411   -777       N  
ATOM   2645  CA  ASN X 152      19.681  24.019  66.274  1.00 43.17           C  
ANISOU 2645  CA  ASN X 152     5109   5036   6256    -51   -507   -795       C  
ATOM   2646  C   ASN X 152      18.497  23.253  66.777  1.00 48.40           C  
ANISOU 2646  C   ASN X 152     5876   5700   6812     -1   -433   -794       C  
ATOM   2647  O   ASN X 152      18.566  22.586  67.806  1.00 50.99           O  
ANISOU 2647  O   ASN X 152     6283   6012   7080     45   -473   -783       O  
ATOM   2648  CB  ASN X 152      19.587  25.501  66.641  1.00 47.79           C  
ANISOU 2648  CB  ASN X 152     5754   5586   6816    -91   -573   -829       C  
ATOM   2649  CG  ASN X 152      20.948  26.188  66.586  1.00 56.93           C  
ANISOU 2649  CG  ASN X 152     6818   6724   8090   -150   -685   -830       C  
ATOM   2650  OD1 ASN X 152      21.980  25.537  66.765  1.00 63.25           O  
ANISOU 2650  OD1 ASN X 152     7528   7538   8968   -143   -753   -811       O  
ATOM   2651  ND2 ASN X 152      20.959  27.486  66.290  1.00 51.23           N  
ANISOU 2651  ND2 ASN X 152     6105   5965   7395   -209   -697   -851       N  
ATOM   2652  N   TRP X 153      17.417  23.316  66.013  1.00 41.46           N  
ANISOU 2652  N   TRP X 153     4995   4839   5917    -10   -321   -804       N  
ATOM   2653  CA  TRP X 153      16.216  22.582  66.345  1.00 41.78           C  
ANISOU 2653  CA  TRP X 153     5102   4882   5889     21   -233   -804       C  
ATOM   2654  C   TRP X 153      16.426  21.070  66.177  1.00 47.86           C  
ANISOU 2654  C   TRP X 153     5842   5652   6690     41   -188   -777       C  
ATOM   2655  O   TRP X 153      16.027  20.287  67.042  1.00 49.46           O  
ANISOU 2655  O   TRP X 153     6126   5830   6835     74   -160   -760       O  
ATOM   2656  CB  TRP X 153      15.056  23.067  65.469  1.00 41.97           C  
ANISOU 2656  CB  TRP X 153     5104   4931   5912      6   -146   -828       C  
ATOM   2657  CG  TRP X 153      13.746  22.493  65.892  1.00 41.39           C  
ANISOU 2657  CG  TRP X 153     5078   4860   5790     27    -57   -832       C  
ATOM   2658  CD1 TRP X 153      12.859  23.054  66.752  1.00 39.25           C  
ANISOU 2658  CD1 TRP X 153     4891   4576   5445     54    -29   -840       C  
ATOM   2659  CD2 TRP X 153      13.188  21.216  65.504  1.00 41.53           C  
ANISOU 2659  CD2 TRP X 153     5057   4882   5839     21     24   -825       C  
ATOM   2660  NE1 TRP X 153      11.769  22.224  66.921  1.00 50.71           N  
ANISOU 2660  NE1 TRP X 153     6343   6032   6894     62     76   -834       N  
ATOM   2661  CE2 TRP X 153      11.933  21.107  66.164  1.00 41.32           C  
ANISOU 2661  CE2 TRP X 153     5078   4849   5772     34    104   -828       C  
ATOM   2662  CE3 TRP X 153      13.612  20.185  64.658  1.00 39.63           C  
ANISOU 2662  CE3 TRP X 153     4752   4643   5661      6     43   -820       C  
ATOM   2663  CZ2 TRP X 153      11.107  19.991  66.003  1.00 40.50           C  
ANISOU 2663  CZ2 TRP X 153     4945   4739   5704     15    195   -825       C  
ATOM   2664  CZ3 TRP X 153      12.792  19.083  64.497  1.00 42.12           C  
ANISOU 2664  CZ3 TRP X 153     5060   4947   5996     -7    123   -824       C  
ATOM   2665  CH2 TRP X 153      11.546  18.989  65.177  1.00 44.54           C  
ANISOU 2665  CH2 TRP X 153     5401   5245   6277    -10    196   -827       C  
ATOM   2666  N   ILE X 154      17.040  20.661  65.060  1.00 40.88           N  
ANISOU 2666  N   ILE X 154     4857   4787   5889     26   -169   -770       N  
ATOM   2667  CA  ILE X 154      17.312  19.241  64.846  1.00 40.95           C  
ANISOU 2667  CA  ILE X 154     4848   4783   5926     52   -127   -748       C  
ATOM   2668  C   ILE X 154      18.203  18.650  65.941  1.00 42.18           C  
ANISOU 2668  C   ILE X 154     5046   4914   6067    101   -203   -714       C  
ATOM   2669  O   ILE X 154      17.833  17.645  66.551  1.00 36.22           O  
ANISOU 2669  O   ILE X 154     4369   4126   5267    135   -165   -694       O  
ATOM   2670  CB  ILE X 154      17.888  18.960  63.462  1.00 43.37           C  
ANISOU 2670  CB  ILE X 154     5056   5109   6314     44    -88   -747       C  
ATOM   2671  CG1 ILE X 154      16.813  19.192  62.421  1.00 35.38           C  
ANISOU 2671  CG1 ILE X 154     4037   4115   5291     16    -14   -782       C  
ATOM   2672  CG2 ILE X 154      18.418  17.514  63.396  1.00 43.75           C  
ANISOU 2672  CG2 ILE X 154     5099   5132   6390     87    -60   -721       C  
ATOM   2673  CD1 ILE X 154      17.313  19.289  61.023  1.00 33.64           C  
ANISOU 2673  CD1 ILE X 154     3750   3910   5119     15     21   -785       C  
ATOM   2674  N   ASN X 155      19.341  19.285  66.231  1.00 42.25           N  
ANISOU 2674  N   ASN X 155     5007   4931   6114    104   -315   -708       N  
ATOM   2675  CA  ASN X 155      20.234  18.799  67.318  1.00 47.89           C  
ANISOU 2675  CA  ASN X 155     5759   5626   6812    162   -422   -682       C  
ATOM   2676  C   ASN X 155      19.609  18.697  68.698  1.00 57.19           C  
ANISOU 2676  C   ASN X 155     7104   6768   7859    203   -450   -679       C  
ATOM   2677  O   ASN X 155      19.998  17.847  69.491  1.00 52.64           O  
ANISOU 2677  O   ASN X 155     6597   6163   7239    271   -491   -648       O  
ATOM   2678  CB  ASN X 155      21.527  19.614  67.435  1.00 41.40           C  
ANISOU 2678  CB  ASN X 155     4841   4819   6069    147   -561   -686       C  
ATOM   2679  CG  ASN X 155      22.460  19.380  66.271  1.00 46.92           C  
ANISOU 2679  CG  ASN X 155     5374   5546   6907    135   -526   -667       C  
ATOM   2680  OD1 ASN X 155      22.488  18.298  65.711  1.00 50.96           O  
ANISOU 2680  OD1 ASN X 155     5864   6058   7441    175   -440   -643       O  
ATOM   2681  ND2 ASN X 155      23.199  20.396  65.884  1.00 41.09           N  
ANISOU 2681  ND2 ASN X 155     4526   4823   6263     81   -578   -675       N  
ATOM   2682  N   LEU X 156      18.662  19.573  69.005  1.00 58.44           N  
ANISOU 2682  N   LEU X 156     7337   6921   7946    175   -423   -706       N  
ATOM   2683  CA  LEU X 156      17.962  19.490  70.288  1.00 51.54           C  
ANISOU 2683  CA  LEU X 156     6637   6010   6938    223   -415   -699       C  
ATOM   2684  C   LEU X 156      17.192  18.194  70.411  1.00 56.42           C  
ANISOU 2684  C   LEU X 156     7315   6598   7523    251   -280   -663       C  
ATOM   2685  O   LEU X 156      17.043  17.630  71.508  1.00 55.53           O  
ANISOU 2685  O   LEU X 156     7347   6440   7311    315   -274   -632       O  
ATOM   2686  CB  LEU X 156      16.975  20.611  70.408  1.00 51.72           C  
ANISOU 2686  CB  LEU X 156     6713   6034   6906    194   -374   -733       C  
ATOM   2687  CG  LEU X 156      16.546  20.927  71.818  1.00 54.72           C  
ANISOU 2687  CG  LEU X 156     7281   6372   7139    253   -397   -733       C  
ATOM   2688  CD1 LEU X 156      17.768  21.056  72.727  1.00 50.54           C  
ANISOU 2688  CD1 LEU X 156     6818   5819   6566    299   -583   -736       C  
ATOM   2689  CD2 LEU X 156      15.785  22.235  71.722  1.00 53.74           C  
ANISOU 2689  CD2 LEU X 156     7180   6253   6985    225   -371   -774       C  
ATOM   2690  N   HIS X 157      16.714  17.731  69.259  1.00 50.82           N  
ANISOU 2690  N   HIS X 157     6504   5907   6897    204   -175   -670       N  
ATOM   2691  CA  HIS X 157      15.944  16.498  69.159  1.00 53.39           C  
ANISOU 2691  CA  HIS X 157     6864   6197   7224    205    -44   -646       C  
ATOM   2692  C   HIS X 157      16.813  15.298  68.780  1.00 56.54           C  
ANISOU 2692  C   HIS X 157     7231   6574   7679    236    -53   -617       C  
ATOM   2693  O   HIS X 157      16.346  14.358  68.136  1.00 59.28           O  
ANISOU 2693  O   HIS X 157     7558   6896   8071    213     47   -615       O  
ATOM   2694  CB  HIS X 157      14.818  16.706  68.152  1.00 55.72           C  
ANISOU 2694  CB  HIS X 157     7078   6519   7573    135     59   -682       C  
ATOM   2695  CG  HIS X 157      13.937  17.860  68.503  1.00 64.28           C  
ANISOU 2695  CG  HIS X 157     8190   7625   8609    121     76   -707       C  
ATOM   2696  ND1 HIS X 157      12.688  17.698  69.054  1.00 62.16           N  
ANISOU 2696  ND1 HIS X 157     7981   7335   8300    119    190   -699       N  
ATOM   2697  CD2 HIS X 157      14.157  19.194  68.435  1.00 65.03           C  
ANISOU 2697  CD2 HIS X 157     8266   7752   8689    115      0   -735       C  
ATOM   2698  CE1 HIS X 157      12.155  18.890  69.283  1.00 57.24           C  
ANISOU 2698  CE1 HIS X 157     7374   6738   7638    123    184   -723       C  
ATOM   2699  NE2 HIS X 157      13.027  19.808  68.923  1.00 57.25           N  
ANISOU 2699  NE2 HIS X 157     7338   6766   7647    120     66   -747       N  
ATOM   2700  N   ASP X 158      18.086  15.370  69.170  1.00 58.73           N  
ANISOU 2700  N   ASP X 158     7498   6858   7958    290   -180   -600       N  
ATOM   2701  CA  ASP X 158      19.029  14.256  69.098  1.00 56.04           C  
ANISOU 2701  CA  ASP X 158     7144   6492   7655    353   -204   -563       C  
ATOM   2702  C   ASP X 158      19.637  14.093  67.717  1.00 56.99           C  
ANISOU 2702  C   ASP X 158     7110   6646   7897    329   -186   -577       C  
ATOM   2703  O   ASP X 158      20.183  13.039  67.392  1.00 59.97           O  
ANISOU 2703  O   ASP X 158     7474   6996   8314    378   -160   -551       O  
ATOM   2704  CB  ASP X 158      18.386  12.949  69.566  1.00 56.95           C  
ANISOU 2704  CB  ASP X 158     7389   6531   7717    387    -94   -524       C  
ATOM   2705  CG  ASP X 158      17.998  12.970  71.044  1.00 69.58           C  
ANISOU 2705  CG  ASP X 158     9169   8085   9182    441   -104   -491       C  
ATOM   2706  OD1 ASP X 158      18.554  13.768  71.835  1.00 62.50           O  
ANISOU 2706  OD1 ASP X 158     8314   7210   8222    483   -236   -496       O  
ATOM   2707  OD2 ASP X 158      17.122  12.167  71.420  1.00 88.59           O  
ANISOU 2707  OD2 ASP X 158    11687  10428  11546    441     27   -461       O  
ATOM   2708  N   GLY X 159      19.538  15.143  66.911  1.00 54.25           N  
ANISOU 2708  N   GLY X 159     6663   6351   7599    263   -190   -615       N  
ATOM   2709  CA  GLY X 159      20.143  15.166  65.591  1.00 47.57           C  
ANISOU 2709  CA  GLY X 159     5684   5537   6854    246   -164   -626       C  
ATOM   2710  C   GLY X 159      19.198  14.602  64.560  1.00 46.89           C  
ANISOU 2710  C   GLY X 159     5604   5436   6776    208    -39   -651       C  
ATOM   2711  O   GLY X 159      18.019  14.370  64.847  1.00 57.85           O  
ANISOU 2711  O   GLY X 159     7070   6799   8112    177     21   -666       O  
ATOM   2712  N   TRP X 160      19.718  14.380  63.362  1.00 41.46           N  
ANISOU 2712  N   TRP X 160     4835   4762   6156    214      1   -658       N  
ATOM   2713  CA  TRP X 160      18.946  13.813  62.258  1.00 40.75           C  
ANISOU 2713  CA  TRP X 160     4759   4654   6070    187     98   -692       C  
ATOM   2714  C   TRP X 160      18.244  12.495  62.618  1.00 43.33           C  
ANISOU 2714  C   TRP X 160     5186   4911   6368    194    158   -691       C  
ATOM   2715  O   TRP X 160      17.197  12.173  62.067  1.00 48.51           O  
ANISOU 2715  O   TRP X 160     5868   5546   7017    143    218   -732       O  
ATOM   2716  CB  TRP X 160      19.854  13.598  61.059  1.00 42.23           C  
ANISOU 2716  CB  TRP X 160     4875   4853   6318    223    133   -689       C  
ATOM   2717  CG  TRP X 160      19.966  14.771  60.160  1.00 47.15           C  
ANISOU 2717  CG  TRP X 160     5426   5527   6963    189    137   -706       C  
ATOM   2718  CD1 TRP X 160      21.114  15.377  59.748  1.00 41.13           C  
ANISOU 2718  CD1 TRP X 160     4565   4794   6267    208    128   -677       C  
ATOM   2719  CD2 TRP X 160      18.879  15.480  59.526  1.00 41.41           C  
ANISOU 2719  CD2 TRP X 160     4719   4819   6195    134    160   -752       C  
ATOM   2720  NE1 TRP X 160      20.818  16.411  58.885  1.00 44.70           N  
ANISOU 2720  NE1 TRP X 160     4995   5275   6714    167    156   -697       N  
ATOM   2721  CE2 TRP X 160      19.470  16.500  58.734  1.00 41.33           C  
ANISOU 2721  CE2 TRP X 160     4643   4844   6215    129    167   -743       C  
ATOM   2722  CE3 TRP X 160      17.496  15.351  59.557  1.00 34.04           C  
ANISOU 2722  CE3 TRP X 160     3844   3876   5213     91    175   -795       C  
ATOM   2723  CZ2 TRP X 160      18.696  17.416  58.001  1.00 38.70           C  
ANISOU 2723  CZ2 TRP X 160     4325   4535   5845     95    181   -776       C  
ATOM   2724  CZ3 TRP X 160      16.731  16.243  58.804  1.00 46.97           C  
ANISOU 2724  CZ3 TRP X 160     5473   5548   6826     59    178   -832       C  
ATOM   2725  CH2 TRP X 160      17.339  17.268  58.035  1.00 41.32           C  
ANISOU 2725  CH2 TRP X 160     4714   4865   6122     67    178   -822       C  
ATOM   2726  N   SER X 161      18.794  11.742  63.558  1.00 41.52           N  
ANISOU 2726  N   SER X 161     5014   4639   6124    254    137   -645       N  
ATOM   2727  CA  SER X 161      18.156  10.479  63.939  1.00 53.37           C  
ANISOU 2727  CA  SER X 161     6625   6055   7598    259    208   -635       C  
ATOM   2728  C   SER X 161      16.886  10.631  64.782  1.00 59.62           C  
ANISOU 2728  C   SER X 161     7491   6823   8338    201    246   -639       C  
ATOM   2729  O   SER X 161      16.228   9.631  65.121  1.00 57.64           O  
ANISOU 2729  O   SER X 161     7330   6494   8078    186    325   -628       O  
ATOM   2730  CB  SER X 161      19.144   9.550  64.645  1.00 50.89           C  
ANISOU 2730  CB  SER X 161     6369   5690   7276    359    183   -577       C  
ATOM   2731  OG  SER X 161      20.075  10.292  65.401  1.00 56.25           O  
ANISOU 2731  OG  SER X 161     7006   6421   7945    411     70   -545       O  
ATOM   2732  N   GLY X 162      16.542  11.875  65.124  1.00 58.26           N  
ANISOU 2732  N   GLY X 162     7285   6713   8138    169    203   -653       N  
ATOM   2733  CA  GLY X 162      15.314  12.142  65.851  1.00 45.49           C  
ANISOU 2733  CA  GLY X 162     5725   5083   6476    124    254   -657       C  
ATOM   2734  C   GLY X 162      14.166  11.727  64.967  1.00 50.07           C  
ANISOU 2734  C   GLY X 162     6268   5646   7109     46    340   -704       C  
ATOM   2735  O   GLY X 162      13.077  11.448  65.451  1.00 53.15           O  
ANISOU 2735  O   GLY X 162     6696   6001   7496      2    418   -703       O  
ATOM   2736  N   LEU X 163      14.423  11.655  63.664  1.00 49.34           N  
ANISOU 2736  N   LEU X 163     6104   5576   7067     31    325   -746       N  
ATOM   2737  CA  LEU X 163      13.381  11.322  62.697  1.00 43.54           C  
ANISOU 2737  CA  LEU X 163     5334   4830   6378    -39    372   -807       C  
ATOM   2738  C   LEU X 163      12.879   9.889  62.871  1.00 50.88           C  
ANISOU 2738  C   LEU X 163     6334   5658   7341    -70    452   -804       C  
ATOM   2739  O   LEU X 163      11.717   9.578  62.597  1.00 53.82           O  
ANISOU 2739  O   LEU X 163     6685   6005   7760   -149    499   -846       O  
ATOM   2740  CB  LEU X 163      13.912  11.531  61.295  1.00 49.94           C  
ANISOU 2740  CB  LEU X 163     6088   5677   7210    -26    335   -848       C  
ATOM   2741  CG  LEU X 163      12.894  11.865  60.227  1.00 64.29           C  
ANISOU 2741  CG  LEU X 163     7854   7524   9048    -83    330   -921       C  
ATOM   2742  CD1 LEU X 163      12.177  13.135  60.580  1.00 61.11           C  
ANISOU 2742  CD1 LEU X 163     7399   7190   8628   -106    306   -927       C  
ATOM   2743  CD2 LEU X 163      13.614  12.026  58.920  1.00 72.63           C  
ANISOU 2743  CD2 LEU X 163     8894   8605  10098    -44    303   -948       C  
ATOM   2744  N   ILE X 164      13.765   9.022  63.353  1.00 54.29           N  
ANISOU 2744  N   ILE X 164     6847   6026   7755     -7    464   -754       N  
ATOM   2745  CA  ILE X 164      13.418   7.628  63.584  1.00 53.36           C  
ANISOU 2745  CA  ILE X 164     6821   5791   7661    -28    546   -741       C  
ATOM   2746  C   ILE X 164      12.368   7.461  64.695  1.00 50.10           C  
ANISOU 2746  C   ILE X 164     6461   5331   7243    -80    631   -708       C  
ATOM   2747  O   ILE X 164      11.331   6.838  64.480  1.00 54.25           O  
ANISOU 2747  O   ILE X 164     6984   5795   7835   -169    706   -738       O  
ATOM   2748  CB  ILE X 164      14.664   6.786  63.933  1.00 55.63           C  
ANISOU 2748  CB  ILE X 164     7196   6020   7921     76    538   -684       C  
ATOM   2749  CG1 ILE X 164      15.703   6.830  62.811  1.00 49.11           C  
ANISOU 2749  CG1 ILE X 164     6314   5232   7114    134    485   -709       C  
ATOM   2750  CG2 ILE X 164      14.263   5.362  64.229  1.00 46.37           C  
ANISOU 2750  CG2 ILE X 164     6143   4709   6768     57    632   -665       C  
ATOM   2751  CD1 ILE X 164      17.112   6.620  63.321  1.00 41.33           C  
ANISOU 2751  CD1 ILE X 164     5352   4247   6106    257    441   -644       C  
ATOM   2752  N   GLU X 165      12.628   8.006  65.881  1.00 55.14           N  
ANISOU 2752  N   GLU X 165     7151   5992   7808    -24    622   -647       N  
ATOM   2753  CA  GLU X 165      11.643   7.912  66.962  1.00 65.54           C  
ANISOU 2753  CA  GLU X 165     8534   7264   9106    -58    725   -608       C  
ATOM   2754  C   GLU X 165      10.313   8.504  66.505  1.00 67.97           C  
ANISOU 2754  C   GLU X 165     8724   7618   9483   -160    766   -665       C  
ATOM   2755  O   GLU X 165       9.256   8.032  66.878  1.00 71.75           O  
ANISOU 2755  O   GLU X 165     9211   8038  10011   -229    881   -655       O  
ATOM   2756  CB  GLU X 165      12.144   8.628  68.218  1.00 20.00           C  
ATOM   2757  CG  GLU X 165      13.340   7.960  68.878  0.01 20.00           C  
ATOM   2758  CD  GLU X 165      13.852   8.738  70.076  0.01 20.00           C  
ATOM   2759  OE1 GLU X 165      13.402   9.884  70.278  0.01 20.00           O  
ATOM   2760  OE2 GLU X 165      14.706   8.202  70.814  0.01 20.00           O  
ATOM   2761  N   PHE X 166      10.378   9.528  65.668  1.00 63.68           N  
ANISOU 2761  N   PHE X 166     8067   7178   8950   -166    674   -721       N  
ATOM   2762  CA  PHE X 166       9.183  10.230  65.223  1.00 58.71           C  
ANISOU 2762  CA  PHE X 166     7323   6608   8378   -238    689   -775       C  
ATOM   2763  C   PHE X 166       8.397   9.422  64.186  1.00 62.88           C  
ANISOU 2763  C   PHE X 166     7780   7096   9017   -333    710   -842       C  
ATOM   2764  O   PHE X 166       7.169   9.420  64.183  1.00 69.02           O  
ANISOU 2764  O   PHE X 166     8480   7871   9873   -411    768   -870       O  
ATOM   2765  CB  PHE X 166       9.587  11.604  64.672  1.00 50.81           C  
ANISOU 2765  CB  PHE X 166     6249   5719   7339   -200    580   -808       C  
ATOM   2766  CG  PHE X 166       8.549  12.255  63.802  1.00 50.72           C  
ANISOU 2766  CG  PHE X 166     6114   5770   7387   -255    561   -876       C  
ATOM   2767  CD1 PHE X 166       8.668  12.231  62.421  1.00 45.67           C  
ANISOU 2767  CD1 PHE X 166     5413   5158   6781   -272    488   -941       C  
ATOM   2768  CD2 PHE X 166       7.461  12.923  64.371  1.00 48.94           C  
ANISOU 2768  CD2 PHE X 166     5841   5578   7175   -275    616   -873       C  
ATOM   2769  CE1 PHE X 166       7.701  12.848  61.615  1.00 56.24           C  
ANISOU 2769  CE1 PHE X 166     6648   6557   8163   -308    452  -1005       C  
ATOM   2770  CE2 PHE X 166       6.504  13.550  63.586  1.00 42.58           C  
ANISOU 2770  CE2 PHE X 166     4913   4837   6428   -310    587   -935       C  
ATOM   2771  CZ  PHE X 166       6.617  13.516  62.203  1.00 49.00           C  
ANISOU 2771  CZ  PHE X 166     5668   5678   7271   -326    495  -1002       C  
ATOM   2772  N   SER X 167       9.111   8.745  63.296  1.00 68.40           N  
ANISOU 2772  N   SER X 167     8503   7760   9726   -322    660   -873       N  
ATOM   2773  CA  SER X 167       8.472   7.936  62.262  1.00 71.77           C  
ANISOU 2773  CA  SER X 167     8890   8136  10243   -406    658   -949       C  
ATOM   2774  C   SER X 167       7.781   6.745  62.907  1.00 74.07           C  
ANISOU 2774  C   SER X 167     9235   8302  10607   -483    776   -925       C  
ATOM   2775  O   SER X 167       6.853   6.173  62.339  1.00 72.49           O  
ANISOU 2775  O   SER X 167     8977   8054  10512   -586    791   -988       O  
ATOM   2776  CB  SER X 167       9.520   7.417  61.278  1.00 72.44           C  
ANISOU 2776  CB  SER X 167     9028   8196  10300   -355    595   -978       C  
ATOM   2777  OG  SER X 167      10.413   6.526  61.939  1.00 69.56           O  
ANISOU 2777  OG  SER X 167     8784   7745   9901   -297    644   -911       O  
ATOM   2778  N   GLY X 168       8.251   6.368  64.093  1.00 77.62           N  
ANISOU 2778  N   GLY X 168     9800   8692  11000   -431    855   -833       N  
ATOM   2779  CA  GLY X 168       7.753   5.188  64.774  1.00 81.32           C  
ANISOU 2779  CA  GLY X 168    10354   9022  11522   -489    987   -791       C  
ATOM   2780  C   GLY X 168       8.272   3.901  64.151  1.00 89.97           C  
ANISOU 2780  C   GLY X 168    11540   9999  12646   -498    984   -814       C  
ATOM   2781  O   GLY X 168       9.479   3.725  63.932  1.00 87.63           O  
ANISOU 2781  O   GLY X 168    11320   9703  12274   -395    924   -796       O  
TER    2782      GLY X 168                                                      
ATOM   2783  N   THR Y   4       2.075  33.247  45.614  1.00 65.11           N  
ANISOU 2783  N   THR Y   4     7408   7649   9682    443    642   -806       N  
ATOM   2784  CA  THR Y   4       2.086  31.872  45.104  1.00 79.98           C  
ANISOU 2784  CA  THR Y   4     9355   9566  11467    436    334   -786       C  
ATOM   2785  C   THR Y   4       3.278  31.005  45.552  1.00 80.29           C  
ANISOU 2785  C   THR Y   4     9558   9722  11227    395    288   -941       C  
ATOM   2786  O   THR Y   4       3.127  29.795  45.712  1.00 83.18           O  
ANISOU 2786  O   THR Y   4     9946  10111  11547    357    111   -933       O  
ATOM   2787  CB  THR Y   4       1.995  31.822  43.571  1.00 88.26           C  
ANISOU 2787  CB  THR Y   4    10438  10593  12505    520     82   -706       C  
ATOM   2788  OG1 THR Y   4       1.603  30.504  43.162  1.00 85.76           O  
ANISOU 2788  OG1 THR Y   4    10127  10281  12176    508   -209   -650       O  
ATOM   2789  CG2 THR Y   4       3.342  32.171  42.951  1.00 94.45           C  
ANISOU 2789  CG2 THR Y   4    11393  11454  13039    565     73   -826       C  
ATOM   2790  N   MET Y   5       4.459  31.591  45.728  1.00 73.53           N  
ANISOU 2790  N   MET Y   5     8817   8938  10181    405    439  -1083       N  
ATOM   2791  CA  MET Y   5       5.502  30.871  46.445  1.00 73.37           C  
ANISOU 2791  CA  MET Y   5     8929   9026   9921    358    453  -1238       C  
ATOM   2792  C   MET Y   5       5.022  30.775  47.882  1.00 74.30           C  
ANISOU 2792  C   MET Y   5     8955   9130  10146    282    654  -1249       C  
ATOM   2793  O   MET Y   5       5.227  29.772  48.569  1.00 69.27           O  
ANISOU 2793  O   MET Y   5     8366   8544   9411    229    600  -1304       O  
ATOM   2794  CB  MET Y   5       6.823  31.623  46.428  1.00 80.99           C  
ANISOU 2794  CB  MET Y   5    10023  10071  10679    381    605  -1394       C  
ATOM   2795  CG  MET Y   5       7.424  31.894  45.068  1.00 83.87           C  
ANISOU 2795  CG  MET Y   5    10488  10454  10925    455    452  -1402       C  
ATOM   2796  SD  MET Y   5       8.877  32.963  45.263  1.00 96.45           S  
ANISOU 2796  SD  MET Y   5    12207  12130  12311    471    699  -1590       S  
ATOM   2797  CE  MET Y   5       8.880  33.793  43.680  1.00145.20           C  
ANISOU 2797  CE  MET Y   5    18403  18251  18513    564    598  -1511       C  
ATOM   2798  N   GLY Y   6       4.374  31.844  48.333  1.00 77.11           N  
ANISOU 2798  N   GLY Y   6     9177   9414  10705    279    888  -1195       N  
ATOM   2799  CA  GLY Y   6       3.769  31.853  49.649  1.00 73.84           C  
ANISOU 2799  CA  GLY Y   6     8653   8973  10427    210   1084  -1186       C  
ATOM   2800  C   GLY Y   6       2.685  30.802  49.661  1.00 73.28           C  
ANISOU 2800  C   GLY Y   6     8496   8848  10498    176    893  -1062       C  
ATOM   2801  O   GLY Y   6       2.448  30.121  50.672  1.00 64.94           O  
ANISOU 2801  O   GLY Y   6     7415   7804   9456    109    938  -1080       O  
ATOM   2802  N   GLN Y   7       2.034  30.673  48.508  1.00 75.89           N  
ANISOU 2802  N   GLN Y   7     8783   9118  10933    226    676   -937       N  
ATOM   2803  CA  GLN Y   7       0.998  29.678  48.303  1.00 77.72           C  
ANISOU 2803  CA  GLN Y   7     8933   9296  11300    204    463   -815       C  
ATOM   2804  C   GLN Y   7       1.571  28.277  48.519  1.00 78.67           C  
ANISOU 2804  C   GLN Y   7     9178   9493  11221    163    283   -887       C  
ATOM   2805  O   GLN Y   7       1.074  27.508  49.365  1.00 76.51           O  
ANISOU 2805  O   GLN Y   7     8857   9208  11004     96    288   -870       O  
ATOM   2806  CB  GLN Y   7       0.401  29.824  46.896  1.00 84.53           C  
ANISOU 2806  CB  GLN Y   7     9751  10096  12270    277    251   -688       C  
ATOM   2807  CG  GLN Y   7      -0.873  29.037  46.675  1.00 95.59           C  
ANISOU 2807  CG  GLN Y   7    11029  11424  13868    259     65   -547       C  
ATOM   2808  CD  GLN Y   7      -1.812  29.115  47.873  1.00108.42           C  
ANISOU 2808  CD  GLN Y   7    12505  12992  15698    188    252   -501       C  
ATOM   2809  OE1 GLN Y   7      -1.803  30.102  48.613  1.00116.52           O  
ANISOU 2809  OE1 GLN Y   7    13475  14004  16794    174    527   -531       O  
ATOM   2810  NE2 GLN Y   7      -2.625  28.073  48.072  1.00106.75           N  
ANISOU 2810  NE2 GLN Y   7    12227  12748  15583    140    107   -429       N  
ATOM   2811  N   VAL Y   8       2.633  27.956  47.777  1.00 70.44           N  
ANISOU 2811  N   VAL Y   8     8295   8528   9939    203    132   -972       N  
ATOM   2812  CA  VAL Y   8       3.208  26.618  47.846  1.00 64.20           C  
ANISOU 2812  CA  VAL Y   8     7632   7813   8950    174    -63  -1040       C  
ATOM   2813  C   VAL Y   8       3.695  26.284  49.259  1.00 62.30           C  
ANISOU 2813  C   VAL Y   8     7436   7630   8604    104    117  -1156       C  
ATOM   2814  O   VAL Y   8       3.511  25.165  49.736  1.00 66.05           O  
ANISOU 2814  O   VAL Y   8     7932   8119   9046     54     12  -1155       O  
ATOM   2815  CB  VAL Y   8       4.332  26.416  46.823  1.00 55.73           C  
ANISOU 2815  CB  VAL Y   8     6725   6818   7629    231   -242  -1122       C  
ATOM   2816  CG1 VAL Y   8       4.992  25.083  47.049  1.00 56.44           C  
ANISOU 2816  CG1 VAL Y   8     6950   6991   7504    198   -411  -1207       C  
ATOM   2817  CG2 VAL Y   8       3.784  26.480  45.412  1.00 44.99           C  
ANISOU 2817  CG2 VAL Y   8     5326   5402   6365    298   -466   -998       C  
ATOM   2818  N   GLY Y   9       4.293  27.258  49.937  1.00 56.77           N  
ANISOU 2818  N   GLY Y   9     6749   6964   7857    101    391  -1255       N  
ATOM   2819  CA  GLY Y   9       4.782  27.044  51.291  1.00 47.71           C  
ANISOU 2819  CA  GLY Y   9     5641   5875   6610     42    579  -1371       C  
ATOM   2820  C   GLY Y   9       3.688  26.652  52.261  1.00 59.91           C  
ANISOU 2820  C   GLY Y   9     7054   7355   8354    -26    656  -1286       C  
ATOM   2821  O   GLY Y   9       3.900  25.820  53.134  1.00 68.14           O  
ANISOU 2821  O   GLY Y   9     8147   8440   9303    -78    666  -1346       O  
ATOM   2822  N   ARG Y  10       2.509  27.247  52.109  1.00 64.36           N  
ANISOU 2822  N   ARG Y  10     7449   7814   9191    -24    709  -1147       N  
ATOM   2823  CA  ARG Y  10       1.381  26.972  53.012  1.00 60.09           C  
ANISOU 2823  CA  ARG Y  10     6765   7202   8863    -89    794  -1059       C  
ATOM   2824  C   ARG Y  10       0.753  25.591  52.784  1.00 62.26           C  
ANISOU 2824  C   ARG Y  10     7037   7452   9169   -121    533   -979       C  
ATOM   2825  O   ARG Y  10       0.456  24.867  53.745  1.00 66.62           O  
ANISOU 2825  O   ARG Y  10     7572   8001   9738   -188    573   -985       O  
ATOM   2826  CB  ARG Y  10       0.321  28.086  52.926  1.00 62.02           C  
ANISOU 2826  CB  ARG Y  10     6827   7346   9392    -75    939   -942       C  
ATOM   2827  CG  ARG Y  10       0.601  29.251  53.853  1.00 71.98           C  
ANISOU 2827  CG  ARG Y  10     8046   8618  10686    -87   1275  -1014       C  
ATOM   2828  CD  ARG Y  10      -0.402  30.372  53.718  1.00 82.55           C  
ANISOU 2828  CD  ARG Y  10     9211   9858  12297    -68   1413   -901       C  
ATOM   2829  NE  ARG Y  10      -0.180  31.186  52.528  1.00 87.42           N  
ANISOU 2829  NE  ARG Y  10     9848  10458  12912     14   1355   -874       N  
ATOM   2830  CZ  ARG Y  10      -1.038  31.265  51.515  1.00 88.39           C  
ANISOU 2830  CZ  ARG Y  10     9887  10503  13196     58   1190   -737       C  
ATOM   2831  NH1 ARG Y  10      -2.174  30.578  51.567  1.00 91.05           N  
ANISOU 2831  NH1 ARG Y  10    10111  10774  13710     25   1069   -620       N  
ATOM   2832  NH2 ARG Y  10      -0.767  32.029  50.454  1.00 78.88           N  
ANISOU 2832  NH2 ARG Y  10     8711   9286  11973    136   1148   -719       N  
ATOM   2833  N   GLN Y  11       0.552  25.222  51.520  1.00 59.19           N  
ANISOU 2833  N   GLN Y  11     6663   7040   8785    -73    269   -904       N  
ATOM   2834  CA  GLN Y  11       0.091  23.869  51.218  1.00 58.38           C  
ANISOU 2834  CA  GLN Y  11     6575   6922   8683   -100      5   -842       C  
ATOM   2835  C   GLN Y  11       1.082  22.878  51.818  1.00 56.04           C  
ANISOU 2835  C   GLN Y  11     6444   6721   8128   -135    -39   -971       C  
ATOM   2836  O   GLN Y  11       0.694  21.994  52.585  1.00 53.69           O  
ANISOU 2836  O   GLN Y  11     6133   6412   7854   -199    -53   -959       O  
ATOM   2837  CB  GLN Y  11      -0.068  23.660  49.712  1.00 62.23           C  
ANISOU 2837  CB  GLN Y  11     7076   7389   9177    -34   -274   -764       C  
ATOM   2838  CG  GLN Y  11      -1.038  24.643  49.059  1.00 82.81           C  
ANISOU 2838  CG  GLN Y  11     9526   9904  12035     10   -241   -637       C  
ATOM   2839  CD  GLN Y  11      -0.747  24.898  47.564  1.00107.36           C  
ANISOU 2839  CD  GLN Y  11    12687  13019  15087     99   -440   -606       C  
ATOM   2840  OE1 GLN Y  11       0.030  24.181  46.923  1.00107.61           O  
ANISOU 2840  OE1 GLN Y  11    12859  13116  14913    123   -645   -661       O  
ATOM   2841  NE2 GLN Y  11      -1.383  25.927  47.012  1.00117.58           N  
ANISOU 2841  NE2 GLN Y  11    13866  14243  16564    150   -379   -516       N  
ATOM   2842  N   LEU Y  12       2.366  23.058  51.488  1.00 54.65           N  
ANISOU 2842  N   LEU Y  12     6422   6639   7704    -92    -51  -1098       N  
ATOM   2843  CA  LEU Y  12       3.457  22.244  52.028  1.00 48.24           C  
ANISOU 2843  CA  LEU Y  12     5779   5929   6620   -113    -79  -1240       C  
ATOM   2844  C   LEU Y  12       3.434  22.145  53.566  1.00 50.60           C  
ANISOU 2844  C   LEU Y  12     6059   6243   6924   -182    154  -1300       C  
ATOM   2845  O   LEU Y  12       3.564  21.057  54.135  1.00 53.00           O  
ANISOU 2845  O   LEU Y  12     6432   6576   7128   -225     80  -1335       O  
ATOM   2846  CB  LEU Y  12       4.803  22.798  51.541  1.00 48.30           C  
ANISOU 2846  CB  LEU Y  12     5928   6032   6392    -56    -58  -1374       C  
ATOM   2847  CG  LEU Y  12       5.233  22.531  50.093  1.00 51.45           C  
ANISOU 2847  CG  LEU Y  12     6416   6456   6679      9   -329  -1363       C  
ATOM   2848  CD1 LEU Y  12       6.602  23.158  49.759  1.00 48.21           C  
ANISOU 2848  CD1 LEU Y  12     6144   6142   6034     59   -267  -1510       C  
ATOM   2849  CD2 LEU Y  12       5.271  21.038  49.822  1.00 50.09           C  
ANISOU 2849  CD2 LEU Y  12     6328   6308   6396     -9   -608  -1353       C  
ATOM   2850  N   ALA Y  13       3.251  23.286  54.233  1.00 51.04           N  
ANISOU 2850  N   ALA Y  13     6019   6275   7098   -190    438  -1311       N  
ATOM   2851  CA  ALA Y  13       3.182  23.337  55.691  1.00 48.81           C  
ANISOU 2851  CA  ALA Y  13     5703   6003   6839   -250    681  -1364       C  
ATOM   2852  C   ALA Y  13       1.953  22.618  56.270  1.00 55.49           C  
ANISOU 2852  C   ALA Y  13     6433   6766   7885   -317    653  -1246       C  
ATOM   2853  O   ALA Y  13       2.037  22.017  57.361  1.00 53.82           O  
ANISOU 2853  O   ALA Y  13     6253   6580   7617   -372    740  -1297       O  
ATOM   2854  CB  ALA Y  13       3.237  24.778  56.167  1.00 39.59           C  
ANISOU 2854  CB  ALA Y  13     4452   4826   5763   -239    981  -1396       C  
ATOM   2855  N   ILE Y  14       0.821  22.675  55.557  1.00 52.58           N  
ANISOU 2855  N   ILE Y  14     5932   6300   7747   -312    536  -1093       N  
ATOM   2856  CA  ILE Y  14      -0.396  21.997  56.020  1.00 50.33           C  
ANISOU 2856  CA  ILE Y  14     5528   5932   7664   -376    500   -978       C  
ATOM   2857  C   ILE Y  14      -0.164  20.503  56.118  1.00 52.93           C  
ANISOU 2857  C   ILE Y  14     5973   6294   7844   -409    294  -1002       C  
ATOM   2858  O   ILE Y  14      -0.305  19.903  57.189  1.00 51.86           O  
ANISOU 2858  O   ILE Y  14     5845   6160   7698   -472    380  -1026       O  
ATOM   2859  CB  ILE Y  14      -1.614  22.234  55.101  1.00 56.84           C  
ANISOU 2859  CB  ILE Y  14     6198   6652   8747   -357    375   -815       C  
ATOM   2860  CG1 ILE Y  14      -1.988  23.710  55.066  1.00 57.02           C  
ANISOU 2860  CG1 ILE Y  14     6092   6629   8943   -326    586   -778       C  
ATOM   2861  CG2 ILE Y  14      -2.809  21.441  55.612  1.00 49.26           C  
ANISOU 2861  CG2 ILE Y  14     5125   5614   7978   -428    332   -711       C  
ATOM   2862  CD1 ILE Y  14      -2.069  24.270  56.446  1.00 57.24           C  
ANISOU 2862  CD1 ILE Y  14     6060   6658   9033   -378    895   -825       C  
ATOM   2863  N   ILE Y  15       0.206  19.896  54.994  1.00 57.59           N  
ANISOU 2863  N   ILE Y  15     6656   6910   8316   -366     21   -997       N  
ATOM   2864  CA  ILE Y  15       0.517  18.469  54.985  1.00 61.24           C  
ANISOU 2864  CA  ILE Y  15     7242   7409   8619   -391   -191  -1026       C  
ATOM   2865  C   ILE Y  15       1.569  18.143  56.041  1.00 60.97           C  
ANISOU 2865  C   ILE Y  15     7351   7468   8347   -414    -61  -1178       C  
ATOM   2866  O   ILE Y  15       1.378  17.228  56.835  1.00 62.50           O  
ANISOU 2866  O   ILE Y  15     7573   7658   8516   -470    -67  -1183       O  
ATOM   2867  CB  ILE Y  15       0.918  17.980  53.582  1.00 60.96           C  
ANISOU 2867  CB  ILE Y  15     7296   7400   8466   -332   -494  -1015       C  
ATOM   2868  CG1 ILE Y  15      -0.282  18.105  52.646  1.00 73.10           C  
ANISOU 2868  CG1 ILE Y  15     8682   8838  10255   -317   -636   -854       C  
ATOM   2869  CG2 ILE Y  15       1.381  16.527  53.610  1.00 56.47           C  
ANISOU 2869  CG2 ILE Y  15     6871   6880   7705   -355   -704  -1062       C  
ATOM   2870  CD1 ILE Y  15       0.087  18.079  51.180  1.00 80.25           C  
ANISOU 2870  CD1 ILE Y  15     9647   9765  11078   -243   -880   -838       C  
ATOM   2871  N   GLY Y  16       2.660  18.909  56.068  1.00 58.57           N  
ANISOU 2871  N   GLY Y  16     7134   7247   7873   -369     62  -1302       N  
ATOM   2872  CA  GLY Y  16       3.648  18.787  57.130  1.00 49.65           C  
ANISOU 2872  CA  GLY Y  16     6124   6210   6532   -385    222  -1454       C  
ATOM   2873  C   GLY Y  16       3.034  18.705  58.517  1.00 51.50           C  
ANISOU 2873  C   GLY Y  16     6276   6406   6884   -455    434  -1438       C  
ATOM   2874  O   GLY Y  16       3.359  17.807  59.294  1.00 52.14           O  
ANISOU 2874  O   GLY Y  16     6451   6527   6833   -490    428  -1500       O  
ATOM   2875  N   ASP Y  17       2.143  19.646  58.829  1.00 52.15           N  
ANISOU 2875  N   ASP Y  17     6186   6412   7217   -474    623  -1355       N  
ATOM   2876  CA  ASP Y  17       1.480  19.679  60.136  1.00 46.31           C  
ANISOU 2876  CA  ASP Y  17     5351   5630   6613   -542    839  -1332       C  
ATOM   2877  C   ASP Y  17       0.560  18.483  60.331  1.00 51.54           C  
ANISOU 2877  C   ASP Y  17     5978   6225   7379   -602    692  -1232       C  
ATOM   2878  O   ASP Y  17       0.437  17.956  61.444  1.00 58.41           O  
ANISOU 2878  O   ASP Y  17     6862   7098   8235   -658    799  -1257       O  
ATOM   2879  CB  ASP Y  17       0.707  20.985  60.327  1.00 46.86           C  
ANISOU 2879  CB  ASP Y  17     5238   5631   6935   -545   1061  -1262       C  
ATOM   2880  CG  ASP Y  17       1.609  22.151  60.701  1.00 55.72           C  
ANISOU 2880  CG  ASP Y  17     6391   6822   7957   -509   1300  -1384       C  
ATOM   2881  OD1 ASP Y  17       2.784  21.906  61.045  1.00 57.44           O  
ANISOU 2881  OD1 ASP Y  17     6763   7143   7917   -493   1326  -1530       O  
ATOM   2882  OD2 ASP Y  17       1.142  23.307  60.668  1.00 52.37           O  
ANISOU 2882  OD2 ASP Y  17     5837   6351   7712   -498   1465  -1337       O  
ATOM   2883  N   ASP Y  18      -0.076  18.048  59.247  1.00 45.51           N  
ANISOU 2883  N   ASP Y  18     5172   5403   6718   -590    448  -1120       N  
ATOM   2884  CA  ASP Y  18      -0.877  16.835  59.291  1.00 51.75           C  
ANISOU 2884  CA  ASP Y  18     5941   6133   7588   -644    279  -1031       C  
ATOM   2885  C   ASP Y  18       0.013  15.614  59.635  1.00 65.25           C  
ANISOU 2885  C   ASP Y  18     7845   7920   9029   -655    160  -1132       C  
ATOM   2886  O   ASP Y  18      -0.302  14.837  60.548  1.00 62.74           O  
ANISOU 2886  O   ASP Y  18     7539   7582   8717   -717    202  -1127       O  
ATOM   2887  CB  ASP Y  18      -1.608  16.639  57.961  1.00 60.50           C  
ANISOU 2887  CB  ASP Y  18     6975   7174   8836   -618     28   -907       C  
ATOM   2888  CG  ASP Y  18      -2.718  17.670  57.734  1.00 72.82           C  
ANISOU 2888  CG  ASP Y  18     8329   8643  10695   -617    136   -790       C  
ATOM   2889  OD1 ASP Y  18      -3.241  18.235  58.718  1.00 75.08           O  
ANISOU 2889  OD1 ASP Y  18     8508   8893  11127   -660    379   -774       O  
ATOM   2890  OD2 ASP Y  18      -3.084  17.904  56.562  1.00 73.54           O  
ANISOU 2890  OD2 ASP Y  18     8367   8699  10877   -570    -27   -712       O  
ATOM   2891  N   ILE Y  19       1.126  15.455  58.911  1.00 69.07           N  
ANISOU 2891  N   ILE Y  19     8481   8491   9273   -595     17  -1225       N  
ATOM   2892  CA  ILE Y  19       2.101  14.409  59.224  1.00 63.88           C  
ANISOU 2892  CA  ILE Y  19     8016   7918   8338   -595    -84  -1337       C  
ATOM   2893  C   ILE Y  19       2.512  14.501  60.686  1.00 61.72           C  
ANISOU 2893  C   ILE Y  19     7784   7690   7978   -629    172  -1436       C  
ATOM   2894  O   ILE Y  19       2.604  13.491  61.380  1.00 62.34           O  
ANISOU 2894  O   ILE Y  19     7947   7781   7960   -668    141  -1464       O  
ATOM   2895  CB  ILE Y  19       3.391  14.508  58.374  1.00 61.28           C  
ANISOU 2895  CB  ILE Y  19     7841   7692   7751   -520   -212  -1450       C  
ATOM   2896  CG1 ILE Y  19       3.079  14.548  56.879  1.00 54.03           C  
ANISOU 2896  CG1 ILE Y  19     6885   6737   6905   -476   -453  -1360       C  
ATOM   2897  CG2 ILE Y  19       4.327  13.361  58.712  1.00 53.64           C  
ANISOU 2897  CG2 ILE Y  19     7067   6808   6504   -521   -326  -1561       C  
ATOM   2898  CD1 ILE Y  19       2.791  13.212  56.309  1.00 58.31           C  
ANISOU 2898  CD1 ILE Y  19     7482   7257   7417   -492   -744  -1302       C  
ATOM   2899  N   ASN Y  20       2.765  15.721  61.152  1.00 59.03           N  
ANISOU 2899  N   ASN Y  20     7386   7373   7670   -613    426  -1490       N  
ATOM   2900  CA  ASN Y  20       3.229  15.928  62.522  1.00 57.65           C  
ANISOU 2900  CA  ASN Y  20     7248   7250   7406   -637    682  -1595       C  
ATOM   2901  C   ASN Y  20       2.179  15.585  63.586  1.00 63.00           C  
ANISOU 2901  C   ASN Y  20     7819   7847   8270   -715    810  -1512       C  
ATOM   2902  O   ASN Y  20       2.500  15.002  64.629  1.00 59.00           O  
ANISOU 2902  O   ASN Y  20     7393   7378   7646   -746    898  -1582       O  
ATOM   2903  CB  ASN Y  20       3.732  17.358  62.696  1.00 50.52           C  
ANISOU 2903  CB  ASN Y  20     6301   6390   6504   -599    920  -1671       C  
ATOM   2904  CG  ASN Y  20       4.409  17.582  64.034  1.00 55.41           C  
ANISOU 2904  CG  ASN Y  20     6978   7084   6993   -612   1173  -1804       C  
ATOM   2905  OD1 ASN Y  20       3.810  18.134  64.950  1.00 61.30           O  
ANISOU 2905  OD1 ASN Y  20     7604   7787   7899   -652   1404  -1774       O  
ATOM   2906  ND2 ASN Y  20       5.653  17.145  64.157  1.00 56.00           N  
ANISOU 2906  ND2 ASN Y  20     7233   7270   6774   -577   1128  -1953       N  
ATOM   2907  N   ARG Y  21       0.927  15.953  63.316  1.00 58.19           N  
ANISOU 2907  N   ARG Y  21     7029   7129   7951   -746    820  -1366       N  
ATOM   2908  CA  ARG Y  21      -0.181  15.596  64.195  1.00 50.12           C  
ANISOU 2908  CA  ARG Y  21     5894   6022   7129   -824    917  -1274       C  
ATOM   2909  C   ARG Y  21      -0.302  14.094  64.242  1.00 49.91           C  
ANISOU 2909  C   ARG Y  21     5965   5981   7017   -861    714  -1252       C  
ATOM   2910  O   ARG Y  21      -0.318  13.474  65.298  1.00 62.13           O  
ANISOU 2910  O   ARG Y  21     7559   7533   8514   -909    804  -1282       O  
ATOM   2911  CB  ARG Y  21      -1.478  16.165  63.636  1.00 52.66           C  
ANISOU 2911  CB  ARG Y  21     6013   6232   7765   -842    907  -1120       C  
ATOM   2912  CG  ARG Y  21      -2.657  16.061  64.577  1.00 56.64           C  
ANISOU 2912  CG  ARG Y  21     6373   6646   8500   -922   1051  -1029       C  
ATOM   2913  CD  ARG Y  21      -2.274  16.461  65.981  1.00 60.67           C  
ANISOU 2913  CD  ARG Y  21     6899   7201   8952   -948   1341  -1121       C  
ATOM   2914  NE  ARG Y  21      -3.436  16.522  66.857  1.00 60.76           N  
ANISOU 2914  NE  ARG Y  21     6756   7125   9203  -1023   1498  -1032       N  
ATOM   2915  CZ  ARG Y  21      -3.925  15.474  67.501  1.00 72.23           C  
ANISOU 2915  CZ  ARG Y  21     8228   8539  10677  -1089   1464   -995       C  
ATOM   2916  NH1 ARG Y  21      -3.342  14.283  67.374  1.00 73.54           N  
ANISOU 2916  NH1 ARG Y  21     8561   8744  10635  -1086   1278  -1041       N  
ATOM   2917  NH2 ARG Y  21      -4.989  15.619  68.273  1.00 70.94           N  
ANISOU 2917  NH2 ARG Y  21     7917   8296  10742  -1157   1617   -915       N  
ATOM   2918  N   ARG Y  22      -0.393  13.531  63.054  1.00 43.86           N  
ANISOU 2918  N   ARG Y  22     5229   5197   6237   -837    436  -1197       N  
ATOM   2919  CA  ARG Y  22      -0.541  12.108  62.841  1.00 58.10           C  
ANISOU 2919  CA  ARG Y  22     7122   6983   7972   -865    202  -1164       C  
ATOM   2920  C   ARG Y  22       0.457  11.253  63.630  1.00 65.15           C  
ANISOU 2920  C   ARG Y  22     8209   7960   8586   -868    210  -1291       C  
ATOM   2921  O   ARG Y  22       0.054  10.350  64.341  1.00 66.64           O  
ANISOU 2921  O   ARG Y  22     8420   8112   8787   -926    208  -1265       O  
ATOM   2922  CB  ARG Y  22      -0.440  11.841  61.334  1.00 67.29           C  
ANISOU 2922  CB  ARG Y  22     8314   8146   9106   -815    -89  -1123       C  
ATOM   2923  CG  ARG Y  22      -0.293  10.399  60.953  1.00 68.46           C  
ANISOU 2923  CG  ARG Y  22     8587   8299   9125   -828   -355  -1117       C  
ATOM   2924  CD  ARG Y  22      -1.371   9.634  61.609  1.00 76.12           C  
ANISOU 2924  CD  ARG Y  22     9481   9177  10264   -911   -342  -1023       C  
ATOM   2925  NE  ARG Y  22      -1.302   8.221  61.266  1.00 90.03           N  
ANISOU 2925  NE  ARG Y  22    11357  10935  11916   -928   -594  -1011       N  
ATOM   2926  CZ  ARG Y  22      -0.873   7.265  62.084  1.00 83.45           C  
ANISOU 2926  CZ  ARG Y  22    10660  10131  10916   -958   -588  -1075       C  
ATOM   2927  NH1 ARG Y  22      -0.458   7.557  63.312  1.00 68.23           N  
ANISOU 2927  NH1 ARG Y  22     8774   8244   8907   -973   -344  -1157       N  
ATOM   2928  NH2 ARG Y  22      -0.877   6.006  61.671  1.00 87.24           N  
ANISOU 2928  NH2 ARG Y  22    11235  10598  11313   -972   -829  -1054       N  
ATOM   2929  N   TYR Y  23       1.752  11.538  63.512  1.00 65.87           N  
ANISOU 2929  N   TYR Y  23     8438   8163   8425   -805    222  -1430       N  
ATOM   2930  CA  TYR Y  23       2.773  10.744  64.199  1.00 60.25           C  
ANISOU 2930  CA  TYR Y  23     7919   7542   7433   -797    219  -1561       C  
ATOM   2931  C   TYR Y  23       3.128  11.263  65.582  1.00 74.89           C  
ANISOU 2931  C   TYR Y  23     9779   9440   9236   -811    521  -1654       C  
ATOM   2932  O   TYR Y  23       4.063  10.761  66.219  1.00 82.73           O  
ANISOU 2932  O   TYR Y  23    10929  10518   9984   -795    550  -1778       O  
ATOM   2933  CB  TYR Y  23       4.056  10.677  63.369  1.00 46.12           C  
ANISOU 2933  CB  TYR Y  23     6289   5860   5376   -720     62  -1677       C  
ATOM   2934  CG  TYR Y  23       3.885   9.950  62.056  1.00 47.06           C  
ANISOU 2934  CG  TYR Y  23     6438   5951   5489   -702   -261  -1606       C  
ATOM   2935  CD1 TYR Y  23       4.162   8.596  61.951  1.00 39.01           C  
ANISOU 2935  CD1 TYR Y  23     5559   4949   4313   -711   -473  -1623       C  
ATOM   2936  CD2 TYR Y  23       3.427  10.616  60.934  1.00 47.24           C  
ANISOU 2936  CD2 TYR Y  23     6349   5930   5668   -675   -350  -1521       C  
ATOM   2937  CE1 TYR Y  23       3.991   7.933  60.767  1.00 44.68           C  
ANISOU 2937  CE1 TYR Y  23     6301   5644   5033   -696   -764  -1559       C  
ATOM   2938  CE2 TYR Y  23       3.259   9.963  59.749  1.00 53.55           C  
ANISOU 2938  CE2 TYR Y  23     7172   6707   6466   -657   -641  -1457       C  
ATOM   2939  CZ  TYR Y  23       3.534   8.619  59.668  1.00 50.03           C  
ANISOU 2939  CZ  TYR Y  23     6862   6281   5867   -669   -848  -1476       C  
ATOM   2940  OH  TYR Y  23       3.366   7.968  58.470  1.00 55.00           O  
ANISOU 2940  OH  TYR Y  23     7511   6888   6497   -650  -1141  -1414       O  
ATOM   2941  N   ASP Y  24       2.408  12.281  66.036  1.00 76.60           N  
ANISOU 2941  N   ASP Y  24     9825   9602   9676   -838    745  -1597       N  
ATOM   2942  CA  ASP Y  24       2.729  12.908  67.308  1.00 82.25           C  
ANISOU 2942  CA  ASP Y  24    10532  10362  10359   -848   1044  -1685       C  
ATOM   2943  C   ASP Y  24       1.650  12.603  68.340  1.00 98.88           C  
ANISOU 2943  C   ASP Y  24    12533  12380  12658   -928   1180  -1596       C  
ATOM   2944  O   ASP Y  24       0.485  12.369  67.998  1.00102.37           O  
ANISOU 2944  O   ASP Y  24    12850  12715  13332   -976   1099  -1452       O  
ATOM   2945  CB  ASP Y  24       2.921  14.424  67.148  1.00 75.03           C  
ANISOU 2945  CB  ASP Y  24     9517   9470   9522   -810   1231  -1717       C  
ATOM   2946  CG  ASP Y  24       3.637  15.053  68.340  1.00 86.51           C  
ANISOU 2946  CG  ASP Y  24    11005  11004  10862   -801   1515  -1851       C  
ATOM   2947  OD1 ASP Y  24       4.877  14.865  68.486  1.00 88.93           O  
ANISOU 2947  OD1 ASP Y  24    11475  11423  10891   -754   1507  -2002       O  
ATOM   2948  OD2 ASP Y  24       2.951  15.744  69.126  1.00 82.30           O  
ANISOU 2948  OD2 ASP Y  24    10331  10421  10519   -840   1746  -1808       O  
ATOM   2949  N   SER Y  25       2.058  12.596  69.604  1.00108.79           N  
ANISOU 2949  N   SER Y  25    13842  13684  13811   -942   1388  -1686       N  
ATOM   2950  CA  SER Y  25       1.148  12.363  70.721  1.00117.49           C  
ANISOU 2950  CA  SER Y  25    14856  14713  15073  -1017   1549  -1619       C  
ATOM   2951  C   SER Y  25       1.763  12.948  72.004  1.00116.88           C  
ANISOU 2951  C   SER Y  25    14806  14711  14894  -1009   1839  -1741       C  
ATOM   2952  O   SER Y  25       2.048  12.223  72.974  1.00110.33           O  
ANISOU 2952  O   SER Y  25    14077  13910  13932  -1027   1899  -1798       O  
ATOM   2953  CB  SER Y  25       0.840  10.863  70.864  1.00115.72           C  
ANISOU 2953  CB  SER Y  25    14726  14448  14796  -1061   1371  -1572       C  
ATOM   2954  OG  SER Y  25       0.234  10.345  69.681  1.00110.94           O  
ANISOU 2954  OG  SER Y  25    14084  13773  14296  -1070   1107  -1460       O  
ATOM   2955  N   GLU Y  26       1.958  14.268  71.989  1.00116.12           N  
ANISOU 2955  N   GLU Y  26    14617  14642  14862   -978   2018  -1779       N  
ATOM   2956  CA  GLU Y  26       2.733  14.958  73.016  1.00112.89           C  
ANISOU 2956  CA  GLU Y  26    14241  14323  14331   -955   2280  -1916       C  
ATOM   2957  C   GLU Y  26       2.109  16.269  73.459  1.00116.59           C  
ANISOU 2957  C   GLU Y  26    14518  14750  15031   -975   2540  -1877       C  
ATOM   2958  O   GLU Y  26       2.673  16.954  74.315  1.00121.11           O  
ANISOU 2958  O   GLU Y  26    15096  15391  15531   -958   2775  -1985       O  
ATOM   2959  CB  GLU Y  26       4.154  15.224  72.515  1.00108.85           C  
ANISOU 2959  CB  GLU Y  26    13875  13936  13547   -873   2226  -2071       C  
ATOM   2960  CG  GLU Y  26       4.971  13.963  72.341  1.00107.38           C  
ANISOU 2960  CG  GLU Y  26    13898  13815  13088   -846   2013  -2146       C  
ATOM   2961  CD  GLU Y  26       6.439  14.247  72.254  1.00103.78           C  
ANISOU 2961  CD  GLU Y  26    13589  13497  12345   -771   2029  -2328       C  
ATOM   2962  OE1 GLU Y  26       6.789  15.362  71.812  1.00104.37           O  
ANISOU 2962  OE1 GLU Y  26    13606  13605  12443   -734   2115  -2371       O  
ATOM   2963  OE2 GLU Y  26       7.236  13.362  72.632  1.00100.66           O  
ANISOU 2963  OE2 GLU Y  26    13367  13178  11702   -748   1958  -2429       O  
TER    2964      GLU Y  26                                                      
HETATM 2965  C3' NHE X 170       0.701  27.251  37.479  1.00104.47           C  
HETATM 2966  C2' NHE X 170       0.122  26.311  38.328  1.00107.33           C  
HETATM 2967  C1' NHE X 170      -0.587  26.707  39.454  1.00110.65           C  
HETATM 2968  C6' NHE X 170      -0.730  28.072  39.704  1.00113.56           C  
HETATM 2969  N   NHE X 170      -1.151  25.752  40.241  1.00113.35           N  
HETATM 2970  C1  NHE X 170      -2.003  26.056  41.386  1.00118.61           C  
HETATM 2971  C2  NHE X 170      -1.560  25.412  42.701  1.00122.24           C  
HETATM 2972  S   NHE X 170      -2.344  23.962  42.964  1.00167.60           S  
HETATM 2973  O1  NHE X 170      -1.403  22.996  43.584  1.00166.98           O  
HETATM 2974  O2  NHE X 170      -3.508  24.160  43.863  1.00164.93           O  
HETATM 2975  O3  NHE X 170      -2.848  23.436  41.675  1.00169.15           O  
HETATM 2976  C5' NHE X 170      -0.156  29.019  38.854  1.00108.20           C  
HETATM 2977  C4' NHE X 170       0.564  28.608  37.740  1.00104.36           C  
HETATM 2978 H3'2 NHE X 170       1.261  26.922  36.611  1.00125.38           H  
HETATM 2979 H2'1 NHE X 170       0.239  25.256  38.115  1.00128.82           H  
HETATM 2980 H6'2 NHE X 170      -1.290  28.401  40.571  1.00136.29           H  
HETATM 2981  HN  NHE X 170      -1.007  24.779  40.013  1.00136.04           H  
HETATM 2982 HC11 NHE X 170      -2.035  27.139  41.520  1.00142.35           H  
HETATM 2983 HC12 NHE X 170      -3.020  25.728  41.162  1.00142.35           H  
HETATM 2984 HC21 NHE X 170      -0.481  25.242  42.676  1.00146.71           H  
HETATM 2985 HC22 NHE X 170      -1.771  26.094  43.527  1.00146.71           H  
HETATM 2986 H5'2 NHE X 170      -0.268  30.075  39.067  1.00129.86           H  
HETATM 2987 H4'2 NHE X 170       1.013  29.340  37.079  1.00125.25           H  
HETATM 2988  O   HOH A 170      42.451  16.529  66.657  1.00 59.10           O  
HETATM 2989  O   HOH A 171      64.482  18.801  70.545  1.00 70.41           O  
HETATM 2990  O   HOH A 172      45.621  16.575  39.575  1.00 51.15           O  
HETATM 2991  O   HOH A 173      58.319  23.282  62.433  1.00 64.28           O  
HETATM 2992  O   HOH A 174      74.566  14.424  58.274  1.00 73.13           O  
HETATM 2993  O   HOH A 175      45.077  19.304  41.380  1.00 62.48           O  
HETATM 2994  O   HOH A 176      41.674   3.819  40.127  1.00 61.18           O  
HETATM 2995  O   HOH A 177      39.060  -5.179  56.110  1.00 87.67           O  
HETATM 2996  O   HOH A 178      35.230   1.397  54.416  1.00 60.42           O  
HETATM 2997  O   HOH A 179      36.531   8.257  47.527  1.00 78.41           O  
HETATM 2998  O   HOH A 180      65.173   3.532  67.022  1.00 68.11           O  
HETATM 2999  O   HOH A 181      62.175  19.407  69.055  1.00 75.47           O  
HETATM 3000  O   HOH A 182      37.838   1.445  43.820  1.00 64.53           O  
HETATM 3001  O   HOH A 183      49.018   1.381  64.743  1.00 52.62           O  
HETATM 3002  O   HOH A 184      56.624   2.481  64.836  1.00 54.61           O  
HETATM 3003  O   HOH A 185      56.896  18.107  39.286  1.00 77.15           O  
HETATM 3004  O   HOH A 186      61.847  19.738  66.676  1.00113.79           O  
HETATM 3005  O   HOH A 187      38.111  11.682  47.314  1.00 58.46           O  
HETATM 3006  O   HOH A 188      54.021  17.580  40.355  1.00 64.52           O  
HETATM 3007  O   HOH A 189      53.352  22.253  63.123  1.00 61.79           O  
HETATM 3008  O   HOH A 190      39.304   6.618  34.546  1.00 75.80           O  
HETATM 3009  O   HOH A 191      67.804   9.039  57.413  1.00 78.28           O  
HETATM 3010  O   HOH A 192      42.551  18.622  58.879  1.00 75.37           O  
HETATM 3011  O   HOH A 193      56.535   3.229  54.963  1.00 45.09           O  
HETATM 3012  O   HOH A 194      50.892  14.972  72.859  1.00 51.62           O  
HETATM 3013  O   HOH A 195      59.679  18.847  65.856  1.00 91.57           O  
HETATM 3014  O   HOH A 196      41.419  17.942  72.227  1.00 70.28           O  
HETATM 3015  O   HOH A 197      59.881   5.563  65.412  1.00 64.52           O  
HETATM 3016  O   HOH A 198      50.723  11.293  76.646  1.00 61.18           O  
HETATM 3017  O   HOH A 199      60.539  21.896  44.208  1.00 84.50           O  
HETATM 3018  O   HOH A 200      55.457  -0.728  70.143  1.00 55.84           O  
HETATM 3019  O   HOH A 201      64.050  12.586  65.335  1.00 70.13           O  
HETATM 3020  O   HOH A 202      52.380  10.919  74.366  1.00 54.35           O  
HETATM 3021  O   HOH A 203      39.769  -7.105  57.514  1.00 70.05           O  
HETATM 3022  O   HOH A 204      52.276  23.976  55.546  1.00 81.71           O  
HETATM 3023  O   HOH A 205      48.906  -0.494  68.097  1.00 69.65           O  
HETATM 3024  O   HOH A 206      51.949  12.752  72.346  1.00 48.76           O  
HETATM 3025  O   HOH A 207      43.441   3.988  62.073  1.00 53.77           O  
HETATM 3026  O   HOH A 208      38.928  16.944  37.012  1.00 75.49           O  
HETATM 3027  O   HOH A 209      62.865  27.559  61.055  1.00 85.08           O  
HETATM 3028  O   HOH A 210      51.488  20.060  66.091  1.00 76.95           O  
HETATM 3029  O   HOH A 211      39.702   7.113  57.681  1.00 51.74           O  
HETATM 3030  O   HOH A 212      30.090   3.973  50.156  1.00 57.34           O  
HETATM 3031  O   HOH A 213      65.597  20.396  58.379  1.00 65.65           O  
HETATM 3032  O   HOH A 214      61.562  26.453  62.866  1.00 76.44           O  
HETATM 3033  O   HOH A 215      64.847  28.352  59.303  1.00 70.85           O  
HETATM 3034  O   HOH A 216      36.010   8.608  50.034  1.00 68.04           O  
HETATM 3035  O   HOH A 217      57.480  18.722  57.215  1.00117.86           O  
HETATM 3036  O   HOH A 218      43.782  21.797  42.171  1.00 67.58           O  
HETATM 3037  O   HOH A 219      71.129   9.714  60.994  1.00 89.38           O  
HETATM 3038  O   HOH A 220      59.533  11.278  39.192  1.00 86.96           O  
HETATM 3039  O   HOH A 221      45.080  24.207  50.111  1.00 93.62           O  
HETATM 3040  O   HOH A 222      69.534  13.530  61.326  1.00101.15           O  
HETATM 3041  O   HOH A 223      48.900   1.622  55.343  1.00 98.32           O  
HETATM 3042  O   HOH A 224      48.653   8.127  34.986  1.00 64.57           O  
HETATM 3043  O   HOH A 225      62.246  -7.498  51.600  1.00 59.54           O  
HETATM 3044  O   HOH A 226      46.596  21.269  54.178  1.00 73.95           O  
HETATM 3045  O   HOH A 227      60.934  -9.234  50.017  1.00 86.07           O  
HETATM 3046  O   HOH A 228      56.094   9.220  34.641  1.00 71.11           O  
HETATM 3047  O   HOH A 229      37.386  20.577  46.555  1.00 63.22           O  
HETATM 3048  O   HOH A 230      71.014  15.219  62.659  1.00 70.53           O  
HETATM 3049  O   HOH A 231      35.862  14.441  63.760  1.00 96.77           O  
HETATM 3050  O   HOH A 232      55.837  22.357  44.795  1.00 81.57           O  
HETATM 3051  O   HOH A 233      74.377  15.254  55.773  1.00 70.93           O  
HETATM 3052  O   HOH B  31      47.381  -7.410  37.060  1.00 72.25           O  
HETATM 3053  O   HOH B  35      53.068  -7.994  36.272  1.00 69.31           O  
HETATM 3054  O   HOH B  42      47.690   4.446  38.143  1.00 47.56           O  
HETATM 3055  O   HOH B  49      46.989   5.734  35.760  1.00 70.48           O  
HETATM 3056  O   HOH B  78      60.160   6.049  37.103  1.00 71.39           O  
HETATM 3057  O   HOH B  87      49.958  -4.418  34.843  1.00105.05           O  
HETATM 3058  O   HOH B 169      49.904  -7.869  41.090  1.00 84.35           O  
HETATM 3059  O   HOH B 173      60.726   1.552  38.022  1.00 69.10           O  
HETATM 3060  O   HOH X 171      25.189   3.379  62.699  1.00 61.05           O  
HETATM 3061  O   HOH X 172      24.935   7.388  50.710  1.00101.11           O  
HETATM 3062  O   HOH X 173      20.093  26.152  63.450  1.00 46.05           O  
HETATM 3063  O   HOH X 174      16.915  25.337  64.321  1.00 38.79           O  
HETATM 3064  O   HOH X 175      23.352   6.147  66.966  1.00 85.28           O  
HETATM 3065  O   HOH X 176      32.027   8.947  62.105  1.00 86.02           O  
HETATM 3066  O   HOH X 177      15.142   2.233  47.187  1.00 79.07           O  
HETATM 3067  O   HOH X 178      20.570  29.615  42.011  1.00118.73           O  
HETATM 3068  O   HOH X 179      11.231   2.956  60.610  1.00 65.27           O  
HETATM 3069  O   HOH X 180      -1.876  20.789  41.566  1.00 81.25           O  
HETATM 3070  O   HOH X 181      27.213  22.308  63.851  1.00 64.13           O  
HETATM 3071  O   HOH X 182      23.027  22.567  67.879  1.00 50.34           O  
HETATM 3072  O   HOH X 183      -0.666  18.192  48.017  1.00 83.73           O  
HETATM 3073  O   HOH X 185      32.957  17.317  58.233  1.00 68.28           O  
HETATM 3074  O   HOH X 186      41.964   9.595  62.713  1.00 71.80           O  
HETATM 3075  O   HOH X 187      17.189  21.542  27.832  1.00104.12           O  
HETATM 3076  O   HOH X 188      19.685  32.095  60.938  1.00 89.87           O  
HETATM 3077  O   HOH X 189       6.666  29.294  34.765  1.00 95.46           O  
HETATM 3078  O   HOH X 190      22.646  14.491  63.254  1.00 52.77           O  
HETATM 3079  O   HOH X 191      30.670   4.982  48.030  1.00 65.05           O  
HETATM 3080  O   HOH X 192      17.951   2.659  51.400  1.00 63.07           O  
HETATM 3081  O   HOH X 193      25.377  18.807  45.583  1.00 63.01           O  
HETATM 3082  O   HOH X 194       9.151   7.709  48.677  1.00 71.97           O  
HETATM 3083  O   HOH X 195       7.559  13.530  46.889  1.00 66.71           O  
HETATM 3084  O   HOH X 196      16.349  33.764  52.667  1.00 67.23           O  
HETATM 3085  O   HOH X 197      23.763   2.579  60.391  1.00 64.86           O  
HETATM 3086  O   HOH X 198      11.900   3.359  65.265  1.00 73.74           O  
HETATM 3087  O   HOH X 199      21.843  11.662  63.960  1.00 59.34           O  
HETATM 3088  O   HOH X 200      24.566   3.985  58.512  1.00 70.11           O  
HETATM 3089  O   HOH X 201      -5.465  22.949  44.704  1.00 79.94           O  
HETATM 3090  O   HOH X 202      -4.203  16.926  51.159  1.00 79.62           O  
HETATM 3091  O   HOH X 203      28.699  20.785  62.555  1.00 56.93           O  
HETATM 3092  O   HOH X 204      22.518   9.287  61.917  1.00 69.90           O  
HETATM 3093  O   HOH X 205      30.160  11.105  61.252  1.00 84.40           O  
HETATM 3094  O   HOH X 206      24.186  30.464  44.871  1.00 79.99           O  
HETATM 3095  O   HOH X 207      22.651  27.887  63.323  1.00 66.01           O  
HETATM 3096  O   HOH X 208      24.060  16.646  64.845  1.00 62.01           O  
HETATM 3097  O   HOH X 209       7.967  11.769  44.153  1.00 65.82           O  
HETATM 3098  O   HOH X 210      24.207  20.467  32.690  1.00 78.71           O  
HETATM 3099  O   HOH X 211      10.772  25.660  46.629  1.00 89.48           O  
HETATM 3100  O   HOH X 212      32.893   5.693  56.108  1.00 72.68           O  
HETATM 3101  O   HOH X 213       7.784  14.482  41.281  1.00 73.07           O  
HETATM 3102  O   HOH X 214      22.925  29.650  42.124  1.00 80.87           O  
HETATM 3103  O   HOH X 215      14.277  35.483  51.116  1.00 65.40           O  
HETATM 3104  O   HOH X 216      27.753  21.526  59.905  1.00 68.25           O  
HETATM 3105  O   HOH X 217      22.902  18.885  51.120  1.00 73.76           O  
HETATM 3106  O   HOH X 218      -5.127  15.175  53.865  1.00 69.91           O  
HETATM 3107  O   HOH X 219      23.369  14.427  60.187  1.00100.35           O  
HETATM 3108  O   HOH X 220      11.895   7.064  48.813  1.00132.71           O  
HETATM 3109  O   HOH X 221      12.785  13.187  67.988  1.00 53.58           O  
HETATM 3110  O   HOH X 222      29.551  12.529  63.375  1.00 69.94           O  
HETATM 3111  O   HOH X 223      18.951  13.448  74.976  1.00 66.09           O  
HETATM 3112  O   HOH X 224      29.355  10.834  52.107  1.00 58.13           O  
HETATM 3113  O   HOH X 225       1.876  25.414  41.858  1.00 79.27           O  
HETATM 3114  O   HOH X 226      16.609  14.700  74.435  1.00 83.08           O  
HETATM 3115  O   HOH X 227      25.253  27.462  53.863  1.00 97.65           O  
HETATM 3116  O   HOH X 228      26.907   4.859  60.535  1.00 72.98           O  
HETATM 3117  O   HOH X 229       9.461  25.919  66.184  1.00 85.90           O  
HETATM 3118  O   HOH X 230      26.633  20.732  50.474  1.00 73.43           O  
HETATM 3119  O   HOH X 231      11.742  11.050  36.656  1.00101.34           O  
HETATM 3120  O   HOH X 232      21.206  32.153  58.009  1.00 68.43           O  
HETATM 3121  O   HOH Y  31      -3.101  15.563  54.598  1.00 62.42           O  
HETATM 3122  O   HOH Y  32       8.038  17.673  65.483  1.00 43.76           O  
HETATM 3123  O   HOH Y  38      -0.289  28.143  43.076  1.00 73.78           O  
HETATM 3124  O   HOH Y  44      -2.441  20.726  59.062  1.00 56.87           O  
HETATM 3125  O   HOH Y 104       1.528  33.561  51.232  1.00 72.94           O  
HETATM 3126  O   HOH Y 110       5.851  20.128  71.708  1.00 53.16           O  
HETATM 3127  O   HOH Y 125       0.727  17.237  67.578  1.00 59.26           O  
HETATM 3128  O   HOH Y 139       6.128  17.260  70.441  1.00 58.36           O  
HETATM 3129  O   HOH Y 143       0.798  19.476  64.224  1.00 58.67           O  
HETATM 3130  O   HOH Y 144       3.912  17.926  71.195  1.00131.79           O  
HETATM 3131  O   HOH Y 152      -0.022  30.050  41.435  1.00 62.72           O  
HETATM 3132  O   HOH Y 162       3.893  34.635  47.555  1.00 85.34           O  
HETATM 3133  O   HOH Y 167       5.066  18.272  68.152  1.00 65.56           O  
CONECT  308 1782                                                                
CONECT 1782  308                                                                
CONECT 2965 2966 2977 2978                                                      
CONECT 2966 2965 2967 2979                                                      
CONECT 2967 2966 2968 2969                                                      
CONECT 2968 2967 2976 2980                                                      
CONECT 2969 2967 2970 2981                                                      
CONECT 2970 2969 2971 2982 2983                                                 
CONECT 2971 2970 2972 2984 2985                                                 
CONECT 2972 2971 2973 2974 2975                                                 
CONECT 2973 2972                                                                
CONECT 2974 2972                                                                
CONECT 2975 2972                                                                
CONECT 2976 2968 2977 2986                                                      
CONECT 2977 2965 2976 2987                                                      
CONECT 2978 2965                                                                
CONECT 2979 2966                                                                
CONECT 2980 2968                                                                
CONECT 2981 2969                                                                
CONECT 2982 2970                                                                
CONECT 2983 2970                                                                
CONECT 2984 2971                                                                
CONECT 2985 2971                                                                
CONECT 2986 2976                                                                
CONECT 2987 2977                                                                
MASTER      462    0    1   23    0    0    2    6 3119    4   25   34          
END

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Related entries of code: 3qbr

Entries with 90% protein sequence similarity cutoff in PDBbind
PDB Code	Check Database	Protein Sequence Similarity
1bxl	RCSB PDB PDBbind	16aa, >1BXL_2\|Chain... at 100%
2xpx	RCSB PDB PDBbind	26aa, >2XPX_2\|Chain... at 100%
Complexes with the same small molecule ligand
PDB Code	Check Database	Ligand Name
3gj5	RCSB PDB PDBbind	34-mer
3gj6	RCSB PDB PDBbind	34-mer

Entry Information

PDB ID	3qbr
Complex Type	Protein-Protein
PDBbind Subset	general set
Protein Name	SJCHGC06286 protein
Ligand Name	34-mer
EC.Number	E.C.-.-.-.-
Resolution	2.6(Å)
Affinity (Kd/Ki/IC50)	IC50=68nM
Release Year	2011
Protein/NA Sequence	Check fasta file
Primary Reference	(2011) Proc. Natl. Acad. Sci. USA Vol. vol. 108: pp. 6999-7003

Links to External Databases

RCSB PDB	The mother database
PDBsum	Enhanced annotations on PDB entries
Pubchem	Comprehensive collection of chemical and biological data
UniProtKB AC	UniProt accession number (AC): Q5BWX6 Q16611
Entrez Gene ID	NCBI Entrez Gene ID: 578
ASD	Information of known allosteric effects of PDB entries

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