HEADER    SIGNALING PROTEIN                       23-JUL-19   6KK1              
TITLE     STRUCTURE OF THERMAL-STABILISED(M8) HUMAN GLP-1 RECEPTOR TRANSMEMBRANE
TITLE    2 DOMAIN                                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUCAGON-LIKE PEPTIDE 1 RECEPTOR,ENDOLYSIN,GLUCAGON-LIKE   
COMPND   3 PEPTIDE 1 RECEPTOR;                                                  
COMPND   4 CHAIN: A, B;                                                         
COMPND   5 SYNONYM: GLP-1R,LYSIS PROTEIN,LYSOZYME,MURAMIDASE,GLP-1R;            
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ENTEROBACTERIA PHAGE T4;          
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606, 10665;                                         
SOURCE   5 GENE: GLP1R;                                                         
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA AFF. FRUGIPERDA 1 BOLD-2017;           
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 2449148;                                    
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: IPLB-SF-21-AE;                          
SOURCE   9 EXPRESSION_SYSTEM_CELL: SF9;                                         
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PFASTBAC                                  
KEYWDS    GPCR, SEVEN-TRANSMEMBRANE, ALLOSTERIC MODULATORS, DIABETES, SIGNALING 
KEYWDS   2 PROTEIN                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.SONG                                                                
REVDAT   2   25-DEC-19 6KK1    1       AUTHOR JRNL                              
REVDAT   1   13-NOV-19 6KK1    0                                                
JRNL        AUTH   Y.XU,Y.WANG,Y.WANG,K.LIU,Y.PENG,D.YAO,H.TAO,H.LIU,G.SONG     
JRNL        TITL   MUTAGENESIS FACILITATED CRYSTALLIZATION OF GLP-1R.           
JRNL        REF    IUCRJ                         V.   6   996 2019              
JRNL        REFN                   ESSN 2052-2525                               
JRNL        PMID   31709055                                                     
JRNL        DOI    10.1107/S2052252519013496                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.14_3260: ???)                              
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.50                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.960                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 77.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 25796                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.246                           
REMARK   3   R VALUE            (WORKING SET) : 0.244                           
REMARK   3   FREE R VALUE                     : 0.290                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.400                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1136                            
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 49.5116 -  5.5977    0.85     3323   193  0.2132 0.2751        
REMARK   3     2  5.5977 -  4.4440    0.82     3271   154  0.2179 0.2475        
REMARK   3     3  4.4440 -  3.8825    0.79     3144   148  0.2337 0.3152        
REMARK   3     4  3.8825 -  3.5276    0.80     3142   157  0.2421 0.3007        
REMARK   3     5  3.5276 -  3.2748    0.77     3036   165  0.2499 0.3140        
REMARK   3     6  3.2748 -  3.0818    0.76     2995   121  0.3263 0.3389        
REMARK   3     7  3.0818 -  2.9275    0.74     2983   104  0.3710 0.3460        
REMARK   3     8  2.9275 -  2.8000    0.69     2766    94  0.3971 0.4003        
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              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.470            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 39.290           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 90.71                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.009           6856                                  
REMARK   3   ANGLE     :  1.441           9342                                  
REMARK   3   CHIRALITY :  0.097           1083                                  
REMARK   3   PLANARITY :  0.005           1138                                  
REMARK   3   DIHEDRAL  : 13.193           2337                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 10                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ( CHAIN A AND RESID 136:256 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):   6.1151  35.8768  43.3587              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3675 T22:   0.3157                                     
REMARK   3      T33:   0.2666 T12:  -0.0060                                     
REMARK   3      T13:   0.0368 T23:  -0.0216                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3054 L22:  -0.0884                                     
REMARK   3      L33:  -0.0844 L12:  -0.0685                                     
REMARK   3      L13:   0.5533 L23:  -0.1471                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0021 S12:   0.0446 S13:  -0.0697                       
REMARK   3      S21:   0.0152 S22:   0.0063 S23:  -0.0220                       
REMARK   3      S31:  -0.0282 S32:  -0.3465 S33:  -0.0000                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: ( CHAIN A AND RESID 257:422 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):   10.048   27.391   37.850              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3588 T22:   0.4502                                     
REMARK   3      T33:   0.3511 T12:   0.0733                                     
REMARK   3      T13:  -0.0484 T23:   0.0237                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0274 L22:  -0.1689                                     
REMARK   3      L33:   0.1874 L12:   0.1105                                     
REMARK   3      L13:  -0.0389 L23:  -0.1421                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1595 S12:   0.2969 S13:  -0.0364                       
REMARK   3      S21:   0.0871 S22:   0.0641 S23:   0.0746                       
REMARK   3      S31:  -0.1319 S32:  -0.0597 S33:   0.0000                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: ( CHAIN A AND RESID 1001:1060 )                        
REMARK   3    ORIGIN FOR THE GROUP (A):   -2.866    8.159   -1.073              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3447 T22:   0.4754                                     
REMARK   3      T33:   0.4362 T12:  -0.0109                                     
REMARK   3      T13:  -0.0103 T23:   0.0056                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1357 L22:   0.0806                                     
REMARK   3      L33:   0.0050 L12:   0.0386                                     
REMARK   3      L13:   0.0866 L23:  -0.0935                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0821 S12:  -0.1506 S13:   0.0436                       
REMARK   3      S21:  -0.1546 S22:   0.0411 S23:   0.0506                       
REMARK   3      S31:   0.0983 S32:   0.2743 S33:   0.0000                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: ( CHAIN A AND RESID 1061:1160 )                        
REMARK   3    ORIGIN FOR THE GROUP (A):    2.693   28.742    3.522              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3976 T22:   0.2373                                     
REMARK   3      T33:   0.4195 T12:  -0.0225                                     
REMARK   3      T13:   0.0527 T23:   0.0135                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.5563 L22:   0.1380                                     
REMARK   3      L33:  -0.0776 L12:   0.0552                                     
REMARK   3      L13:   0.2428 L23:  -0.1300                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2173 S12:   0.7666 S13:  -0.0004                       
REMARK   3      S21:  -0.1062 S22:   0.4374 S23:  -0.1447                       
REMARK   3      S31:  -0.4872 S32:   1.0101 S33:   0.0000                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: ( CHAIN B AND RESID 136:256 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):  38.6692   6.3221  39.0456              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4692 T22:   0.2154                                     
REMARK   3      T33:   0.3686 T12:  -0.0223                                     
REMARK   3      T13:  -0.0400 T23:  -0.0210                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.0232 L22:   0.0549                                     
REMARK   3      L33:  -0.0101 L12:   0.1979                                     
REMARK   3      L13:   0.1384 L23:   0.0272                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0386 S12:  -0.1567 S13:   0.0513                       
REMARK   3      S21:   0.0414 S22:   0.0699 S23:   0.1051                       
REMARK   3      S31:   0.2161 S32:  -0.3717 S33:   0.0000                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: ( CHAIN B AND RESID 257:335 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):   37.450   21.511   38.502              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5506 T22:   0.6020                                     
REMARK   3      T33:   0.6734 T12:  -0.0634                                     
REMARK   3      T13:   0.2042 T23:  -0.1148                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0022 L22:  -0.0281                                     
REMARK   3      L33:   0.0978 L12:   0.0007                                     
REMARK   3      L13:   0.1747 L23:   0.0847                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4090 S12:  -0.4967 S13:   0.0358                       
REMARK   3      S21:  -0.0095 S22:  -0.0391 S23:   0.0202                       
REMARK   3      S31:  -0.0376 S32:  -0.0125 S33:   0.0000                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: ( CHAIN B AND RESID 336:422 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):   47.681    8.300   50.173              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4347 T22:   0.6330                                     
REMARK   3      T33:   0.3963 T12:  -0.1150                                     
REMARK   3      T13:  -0.0139 T23:   0.0908                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2639 L22:   0.2637                                     
REMARK   3      L33:   0.0426 L12:   0.1543                                     
REMARK   3      L13:   0.2426 L23:   0.0457                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1406 S12:  -0.0667 S13:  -0.0918                       
REMARK   3      S21:   0.0954 S22:   0.0688 S23:   0.0704                       
REMARK   3      S31:   0.2770 S32:  -0.3228 S33:  -0.0000                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: ( CHAIN B AND RESID 1001:1027 )                        
REMARK   3    ORIGIN FOR THE GROUP (A):   27.916   29.436   79.829              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4522 T22:   0.2381                                     
REMARK   3      T33:   0.4579 T12:  -0.0116                                     
REMARK   3      T13:  -0.0174 T23:   0.0038                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0043 L22:  -0.0061                                     
REMARK   3      L33:  -0.0039 L12:  -0.0151                                     
REMARK   3      L13:  -0.0558 L23:  -0.0334                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3502 S12:   0.4364 S13:  -0.1789                       
REMARK   3      S21:   0.2294 S22:   0.3007 S23:  -0.2728                       
REMARK   3      S31:   0.1230 S32:  -0.0400 S33:   0.0000                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: ( CHAIN B AND RESID 1028:1060 )                        
REMARK   3    ORIGIN FOR THE GROUP (A):   30.852   38.410   87.343              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4466 T22:   0.3434                                     
REMARK   3      T33:   0.5064 T12:   0.0416                                     
REMARK   3      T13:  -0.0291 T23:   0.0189                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1554 L22:   0.1017                                     
REMARK   3      L33:   0.0071 L12:  -0.1578                                     
REMARK   3      L13:  -0.0555 L23:   0.0007                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3463 S12:  -0.0738 S13:   0.2901                       
REMARK   3      S21:   0.1361 S22:  -0.1923 S23:   0.3588                       
REMARK   3      S31:   0.3551 S32:   0.5621 S33:   0.0000                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: ( CHAIN B AND RESID 1061:1160 )                        
REMARK   3    ORIGIN FOR THE GROUP (A):   35.055   13.450   78.963              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4472 T22:   0.3570                                     
REMARK   3      T33:   0.4882 T12:   0.0349                                     
REMARK   3      T13:  -0.0581 T23:   0.0072                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1683 L22:   0.6173                                     
REMARK   3      L33:   0.2882 L12:  -0.3652                                     
REMARK   3      L13:  -0.0030 L23:   0.6427                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0245 S12:  -0.0896 S13:   0.0072                       
REMARK   3      S21:   0.1816 S22:  -0.0042 S23:   0.0155                       
REMARK   3      S31:   0.1948 S32:  -0.0922 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 6KK1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-JUL-19.                  
REMARK 100 THE DEPOSITION ID IS D_1300013147.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-JAN-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 80                                 
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL41XU                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX225HE                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 25859                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.500                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 77.9                               
REMARK 200  DATA REDUNDANCY                : 3.100                              
REMARK 200  R MERGE                    (I) : 0.13000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.3000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.95                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 70.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.40000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 5VEW                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 64.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.43                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.4-0.45 M AMMONIUM ACETATE, 0.1 M       
REMARK 280  SODIUM CACODYLATE, PH 6.2-6.6, 35-38% PEG400, 3% W/V                
REMARK 280  AMINOHEXANOIC ACID, LIPIDIC CUBIC PHASE, TEMPERATURE 293K           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290                                                                      
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: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     SER A   127                                                      
REMARK 465     GLU A   128                                                      
REMARK 465     SER A   129                                                      
REMARK 465     LYS A   130                                                      
REMARK 465     ARG A   131                                                      
REMARK 465     GLY A   132                                                      
REMARK 465     GLU A   133                                                      
REMARK 465     ARG A   134                                                      
REMARK 465     SER A   135                                                      
REMARK 465     MET A   211                                                      
REMARK 465     GLY A   212                                                      
REMARK 465     SER A   213                                                      
REMARK 465     GLY A   214                                                      
REMARK 465     ASP A   215                                                      
REMARK 465     GLY A   216                                                      
REMARK 465     LEU A   217                                                      
REMARK 465     GLU A   373                                                      
REMARK 465     HIS A   374                                                      
REMARK 465     ALA A   375                                                      
REMARK 465     ARG A   376                                                      
REMARK 465     GLY A   377                                                      
REMARK 465     THR A   378                                                      
REMARK 465     LEU A   379                                                      
REMARK 465     GLU A   423                                                      
REMARK 465     HIS A   424                                                      
REMARK 465     LEU A   425                                                      
REMARK 465     HIS A   426                                                      
REMARK 465     ILE A   427                                                      
REMARK 465     GLN A   428                                                      
REMARK 465     ARG A   429                                                      
REMARK 465     ASP A   430                                                      
REMARK 465     SER A   431                                                      
REMARK 465     SER B   127                                                      
REMARK 465     GLU B   128                                                      
REMARK 465     SER B   129                                                      
REMARK 465     LYS B   130                                                      
REMARK 465     ARG B   131                                                      
REMARK 465     GLY B   132                                                      
REMARK 465     GLU B   133                                                      
REMARK 465     ARG B   134                                                      
REMARK 465     SER B   135                                                      
REMARK 465     MET B   211                                                      
REMARK 465     GLY B   212                                                      
REMARK 465     SER B   213                                                      
REMARK 465     GLY B   214                                                      
REMARK 465     ASP B   215                                                      
REMARK 465     ASP B   372                                                      
REMARK 465     GLU B   373                                                      
REMARK 465     HIS B   374                                                      
REMARK 465     ALA B   375                                                      
REMARK 465     ARG B   376                                                      
REMARK 465     GLY B   377                                                      
REMARK 465     THR B   378                                                      
REMARK 465     LEU B   379                                                      
REMARK 465     GLU B   423                                                      
REMARK 465     HIS B   424                                                      
REMARK 465     LEU B   425                                                      
REMARK 465     HIS B   426                                                      
REMARK 465     ILE B   427                                                      
REMARK 465     GLN B   428                                                      
REMARK 465     ARG B   429                                                      
REMARK 465     ASP B   430                                                      
REMARK 465     SER B   431                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     SER A 136    OG                                                  
REMARK 470     GLU A 138    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 139    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 140    CG   CD   OE1  NE2                                  
REMARK 470     LEU A 141    CG   CD1  CD2                                       
REMARK 470     LEU A 142    CG   CD1  CD2                                       
REMARK 470     ARG A 170    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     TRP A 203    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP A 203    CZ3  CH2                                            
REMARK 470     GLN A 221    CG   CD   OE1  NE2                                  
REMARK 470     ARG A1007    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A1018    CG   CD   CE   NZ                                   
REMARK 470     THR A1020    OG1  CG2                                            
REMARK 470     LYS A1042    CG   CD   CE   NZ                                   
REMARK 470     GLU A1044    CG   CD   OE1  OE2                                  
REMARK 470     ASP A1046    CG   OD1  OD2                                       
REMARK 470     ARG A1051    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU A1065    CG   CD1  CD2                                       
REMARK 470     ASP A1071    CG   OD1  OD2                                       
REMARK 470     ARG A1079    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A1082    CG   CD   CE   NZ                                   
REMARK 470     GLU A1107    CG   CD   OE1  OE2                                  
REMARK 470     LYS A1146    CG   CD   CE   NZ                                   
REMARK 470     GLN A 263    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 294    CG   CD   OE1  OE2                                  
REMARK 470     THR A 298    OG1  CG2                                            
REMARK 470     ARG A 299    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN A 300    CG   OD1  ND2                                       
REMARK 470     SER A 301    OG                                                  
REMARK 470     VAL A 370    CG1  CG2                                            
REMARK 470     MET A 371    CG   SD   CE                                        
REMARK 470     ASP A 372    CG   OD1  OD2                                       
REMARK 470     ARG A 380    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PHE A 381    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS A 383    CG   CD   CE   NZ                                   
REMARK 470     PHE A 385    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     TRP A 417    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP A 417    CZ3  CH2                                            
REMARK 470     ARG A 421    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU A 422    CG   CD1  CD2                                       
REMARK 470     SER B 136    OG                                                  
REMARK 470     GLU B 138    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 139    CG   CD   OE1  OE2                                  
REMARK 470     GLN B 140    CG   CD   OE1  NE2                                  
REMARK 470     LEU B 141    CG   CD1  CD2                                       
REMARK 470     LEU B 142    CG   CD1  CD2                                       
REMARK 470     ARG B 170    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU B 192    CG   CD1  CD2                                       
REMARK 470     TRP B 203    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP B 203    CZ3  CH2                                            
REMARK 470     LEU B 217    CG   CD1  CD2                                       
REMARK 470     LEU B 218    CG   CD1  CD2                                       
REMARK 470     SER B 219    OG                                                  
REMARK 470     GLN B 221    CG   CD   OE1  NE2                                  
REMARK 470     ASP B 222    CG   OD1  OD2                                       
REMARK 470     ARG B1007    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B1018    CG   CD   CE   NZ                                   
REMARK 470     THR B1020    OG1  CG2                                            
REMARK 470     LYS B1042    CG   CD   CE   NZ                                   
REMARK 470     GLU B1044    CG   CD   OE1  OE2                                  
REMARK 470     ASP B1046    CG   OD1  OD2                                       
REMARK 470     ARG B1051    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU B1065    CG   CD1  CD2                                       
REMARK 470     ASP B1071    CG   OD1  OD2                                       
REMARK 470     ARG B1079    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B1082    CG   CD   CE   NZ                                   
REMARK 470     GLU B1107    CG   CD   OE1  OE2                                  
REMARK 470     LYS B1146    CG   CD   CE   NZ                                   
REMARK 470     GLN B 263    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 294    CG   CD   OE1  OE2                                  
REMARK 470     THR B 298    OG1  CG2                                            
REMARK 470     ASN B 300    CG   OD1  ND2                                       
REMARK 470     MET B 371    CG   SD   CE                                        
REMARK 470     ARG B 380    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PHE B 381    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     TRP B 417    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP B 417    CZ3  CH2                                            
REMARK 470     ARG B 421    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU B 422    CG   CD1  CD2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A1001     -169.08   -164.84                                   
REMARK 500    LEU A1032     -102.95    -97.23                                   
REMARK 500    ASN A1054      -35.97     73.84                                   
REMARK 500    LYS A1134       35.23    -85.14                                   
REMARK 500    GLU A 292       78.66   -152.73                                   
REMARK 500    GLU A 294      100.26   -161.17                                   
REMARK 500    CYS A 296       29.85     48.67                                   
REMARK 500    ASN A 302      -65.86   -153.81                                   
REMARK 500    MET A 303     -154.85   -145.53                                   
REMARK 500    PHE A 367       50.76    -99.32                                   
REMARK 500    CYS A 403      -65.67   -147.67                                   
REMARK 500    ASN B1001     -169.76   -164.38                                   
REMARK 500    LEU B1032     -102.26    -95.88                                   
REMARK 500    ASN B1054      -35.89     74.34                                   
REMARK 500    LYS B1134       37.56    -86.52                                   
REMARK 500    GLU B 292       81.72   -154.26                                   
REMARK 500    GLU B 294      102.43   -160.86                                   
REMARK 500    ASN B 302      -63.59   -153.40                                   
REMARK 500    MET B 303     -159.09   -144.92                                   
REMARK 500    PHE B 367       52.50   -100.11                                   
REMARK 500    CYS B 403      -66.49   -147.67                                   
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 97Y A 2001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 97Y B 2001                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5VEW   RELATED DB: PDB                                   
REMARK 900 5VEW CONTAINS THE SAME PROTEIN-LIGAND COMPLEX BUT WITH DIFFERENT     
REMARK 900 MUTATIONS                                                            
DBREF  6KK1 A  128   257  UNP    P43220   GLP1R_HUMAN    128    257             
DBREF  6KK1 A 1001  1160  UNP    P00720   ENLYS_BPT4       2    161             
DBREF  6KK1 A  261   431  UNP    P43220   GLP1R_HUMAN    261    431             
DBREF  6KK1 B  128   257  UNP    P43220   GLP1R_HUMAN    128    257             
DBREF  6KK1 B 1001  1160  UNP    P00720   ENLYS_BPT4       2    161             
DBREF  6KK1 B  261   431  UNP    P43220   GLP1R_HUMAN    261    431             
SEQADV 6KK1 SER A  127  UNP  P43220              EXPRESSION TAG                 
SEQADV 6KK1 PHE A  196  UNP  P43220    ILE   196 ENGINEERED MUTATION            
SEQADV 6KK1     A       UNP  P43220    TYR   205 DELETION                       
SEQADV 6KK1     A       UNP  P43220    SER   206 DELETION                       
SEQADV 6KK1     A       UNP  P43220    THR   207 DELETION                       
SEQADV 6KK1     A       UNP  P43220    ALA   208 DELETION                       
SEQADV 6KK1     A       UNP  P43220    ALA   209 DELETION                       
SEQADV 6KK1     A       UNP  P43220    GLN   210 DELETION                       
SEQADV 6KK1     A       UNP  P43220    GLN   211 DELETION                       
SEQADV 6KK1     A       UNP  P43220    HIS   212 DELETION                       
SEQADV 6KK1     A       UNP  P43220    GLN   213 DELETION                       
SEQADV 6KK1     A       UNP  P43220    TRP   214 DELETION                       
SEQADV 6KK1 GLY A  212  UNP  P43220              LINKER                         
SEQADV 6KK1 SER A  213  UNP  P43220              LINKER                         
SEQADV 6KK1 GLY A  214  UNP  P43220              LINKER                         
SEQADV 6KK1 ALA A  225  UNP  P43220    SER   225 ENGINEERED MUTATION            
SEQADV 6KK1 GLY A 1011  UNP  P00720    ARG    12 ENGINEERED MUTATION            
SEQADV 6KK1 THR A 1053  UNP  P00720    CYS    54 ENGINEERED MUTATION            
SEQADV 6KK1 ALA A 1096  UNP  P00720    CYS    97 ENGINEERED MUTATION            
SEQADV 6KK1 ARG A 1136  UNP  P00720    ILE   137 ENGINEERED MUTATION            
SEQADV 6KK1 ALA A  271  UNP  P43220    SER   271 ENGINEERED MUTATION            
SEQADV 6KK1 CYS A  317  UNP  P43220    ILE   317 ENGINEERED MUTATION            
SEQADV 6KK1 ILE A  318  UNP  P43220    GLY   318 ENGINEERED MUTATION            
SEQADV 6KK1 ALA A  346  UNP  P43220    LYS   346 ENGINEERED MUTATION            
SEQADV 6KK1 PHE A  347  UNP  P43220    CYS   347 ENGINEERED MUTATION            
SEQADV 6KK1 CYS A  361  UNP  P43220    GLY   361 ENGINEERED MUTATION            
SEQADV 6KK1 SER B  127  UNP  P43220              EXPRESSION TAG                 
SEQADV 6KK1 PHE B  196  UNP  P43220    ILE   196 ENGINEERED MUTATION            
SEQADV 6KK1     B       UNP  P43220    TYR   205 DELETION                       
SEQADV 6KK1     B       UNP  P43220    SER   206 DELETION                       
SEQADV 6KK1     B       UNP  P43220    THR   207 DELETION                       
SEQADV 6KK1     B       UNP  P43220    ALA   208 DELETION                       
SEQADV 6KK1     B       UNP  P43220    ALA   209 DELETION                       
SEQADV 6KK1     B       UNP  P43220    GLN   210 DELETION                       
SEQADV 6KK1     B       UNP  P43220    GLN   211 DELETION                       
SEQADV 6KK1     B       UNP  P43220    HIS   212 DELETION                       
SEQADV 6KK1     B       UNP  P43220    GLN   213 DELETION                       
SEQADV 6KK1     B       UNP  P43220    TRP   214 DELETION                       
SEQADV 6KK1 GLY B  212  UNP  P43220              LINKER                         
SEQADV 6KK1 SER B  213  UNP  P43220              LINKER                         
SEQADV 6KK1 GLY B  214  UNP  P43220              LINKER                         
SEQADV 6KK1 ALA B  225  UNP  P43220    SER   225 ENGINEERED MUTATION            
SEQADV 6KK1 GLY B 1011  UNP  P00720    ARG    12 ENGINEERED MUTATION            
SEQADV 6KK1 THR B 1053  UNP  P00720    CYS    54 ENGINEERED MUTATION            
SEQADV 6KK1 ALA B 1096  UNP  P00720    CYS    97 ENGINEERED MUTATION            
SEQADV 6KK1 ARG B 1136  UNP  P00720    ILE   137 ENGINEERED MUTATION            
SEQADV 6KK1 ALA B  271  UNP  P43220    SER   271 ENGINEERED MUTATION            
SEQADV 6KK1 CYS B  317  UNP  P43220    ILE   317 ENGINEERED MUTATION            
SEQADV 6KK1 ILE B  318  UNP  P43220    GLY   318 ENGINEERED MUTATION            
SEQADV 6KK1 ALA B  346  UNP  P43220    LYS   346 ENGINEERED MUTATION            
SEQADV 6KK1 PHE B  347  UNP  P43220    CYS   347 ENGINEERED MUTATION            
SEQADV 6KK1 CYS B  361  UNP  P43220    GLY   361 ENGINEERED MUTATION            
SEQRES   1 A  455  SER GLU SER LYS ARG GLY GLU ARG SER SER PRO GLU GLU          
SEQRES   2 A  455  GLN LEU LEU PHE LEU TYR ILE ILE TYR THR VAL GLY TYR          
SEQRES   3 A  455  ALA LEU SER PHE SER ALA LEU VAL ILE ALA SER ALA ILE          
SEQRES   4 A  455  LEU LEU GLY PHE ARG HIS LEU HIS CYS THR ARG ASN TYR          
SEQRES   5 A  455  ILE HIS LEU ASN LEU PHE ALA SER PHE ILE LEU ARG ALA          
SEQRES   6 A  455  LEU SER VAL PHE PHE LYS ASP ALA ALA LEU LYS TRP MET          
SEQRES   7 A  455  GLY SER GLY ASP GLY LEU LEU SER TYR GLN ASP SER LEU          
SEQRES   8 A  455  ALA CYS ARG LEU VAL PHE LEU LEU MET GLN TYR CYS VAL          
SEQRES   9 A  455  ALA ALA ASN TYR TYR TRP LEU LEU VAL GLU GLY VAL TYR          
SEQRES  10 A  455  LEU TYR THR LEU LEU ALA PHE ASN ILE PHE GLU MET LEU          
SEQRES  11 A  455  ARG ILE ASP GLU GLY LEU ARG LEU LYS ILE TYR LYS ASP          
SEQRES  12 A  455  THR GLU GLY TYR TYR THR ILE GLY ILE GLY HIS LEU LEU          
SEQRES  13 A  455  THR LYS SER PRO SER LEU ASN ALA ALA LYS SER GLU LEU          
SEQRES  14 A  455  ASP LYS ALA ILE GLY ARG ASN THR ASN GLY VAL ILE THR          
SEQRES  15 A  455  LYS ASP GLU ALA GLU LYS LEU PHE ASN GLN ASP VAL ASP          
SEQRES  16 A  455  ALA ALA VAL ARG GLY ILE LEU ARG ASN ALA LYS LEU LYS          
SEQRES  17 A  455  PRO VAL TYR ASP SER LEU ASP ALA VAL ARG ARG ALA ALA          
SEQRES  18 A  455  LEU ILE ASN MET VAL PHE GLN MET GLY GLU THR GLY VAL          
SEQRES  19 A  455  ALA GLY PHE THR ASN SER LEU ARG MET LEU GLN GLN LYS          
SEQRES  20 A  455  ARG TRP ASP GLU ALA ALA VAL ASN LEU ALA LYS SER ARG          
SEQRES  21 A  455  TRP TYR ASN GLN THR PRO ASN ARG ALA LYS ARG VAL ILE          
SEQRES  22 A  455  THR THR PHE ARG THR GLY THR TRP ASP ALA TYR SER GLU          
SEQRES  23 A  455  GLN TRP ILE PHE ARG LEU TYR VAL ALA ILE GLY TRP GLY          
SEQRES  24 A  455  VAL PRO LEU LEU PHE VAL VAL PRO TRP GLY ILE VAL LYS          
SEQRES  25 A  455  TYR LEU TYR GLU ASP GLU GLY CYS TRP THR ARG ASN SER          
SEQRES  26 A  455  ASN MET ASN TYR TRP LEU ILE ILE ARG LEU PRO ILE LEU          
SEQRES  27 A  455  PHE ALA CYS ILE VAL ASN PHE LEU ILE PHE VAL ARG VAL          
SEQRES  28 A  455  ILE CYS ILE VAL VAL SER LYS LEU LYS ALA ASN LEU MET          
SEQRES  29 A  455  CYS LYS THR ASP ILE ALA PHE ARG LEU ALA LYS SER THR          
SEQRES  30 A  455  LEU THR LEU ILE PRO LEU LEU CYS THR HIS GLU VAL ILE          
SEQRES  31 A  455  PHE ALA PHE VAL MET ASP GLU HIS ALA ARG GLY THR LEU          
SEQRES  32 A  455  ARG PHE ILE LYS LEU PHE THR GLU LEU SER PHE THR SER          
SEQRES  33 A  455  PHE GLN GLY LEU MET VAL ALA ILE LEU TYR CYS PHE VAL          
SEQRES  34 A  455  ASN ASN GLU VAL GLN LEU GLU PHE ARG LYS SER TRP GLU          
SEQRES  35 A  455  ARG TRP ARG LEU GLU HIS LEU HIS ILE GLN ARG ASP SER          
SEQRES   1 B  455  SER GLU SER LYS ARG GLY GLU ARG SER SER PRO GLU GLU          
SEQRES   2 B  455  GLN LEU LEU PHE LEU TYR ILE ILE TYR THR VAL GLY TYR          
SEQRES   3 B  455  ALA LEU SER PHE SER ALA LEU VAL ILE ALA SER ALA ILE          
SEQRES   4 B  455  LEU LEU GLY PHE ARG HIS LEU HIS CYS THR ARG ASN TYR          
SEQRES   5 B  455  ILE HIS LEU ASN LEU PHE ALA SER PHE ILE LEU ARG ALA          
SEQRES   6 B  455  LEU SER VAL PHE PHE LYS ASP ALA ALA LEU LYS TRP MET          
SEQRES   7 B  455  GLY SER GLY ASP GLY LEU LEU SER TYR GLN ASP SER LEU          
SEQRES   8 B  455  ALA CYS ARG LEU VAL PHE LEU LEU MET GLN TYR CYS VAL          
SEQRES   9 B  455  ALA ALA ASN TYR TYR TRP LEU LEU VAL GLU GLY VAL TYR          
SEQRES  10 B  455  LEU TYR THR LEU LEU ALA PHE ASN ILE PHE GLU MET LEU          
SEQRES  11 B  455  ARG ILE ASP GLU GLY LEU ARG LEU LYS ILE TYR LYS ASP          
SEQRES  12 B  455  THR GLU GLY TYR TYR THR ILE GLY ILE GLY HIS LEU LEU          
SEQRES  13 B  455  THR LYS SER PRO SER LEU ASN ALA ALA LYS SER GLU LEU          
SEQRES  14 B  455  ASP LYS ALA ILE GLY ARG ASN THR ASN GLY VAL ILE THR          
SEQRES  15 B  455  LYS ASP GLU ALA GLU LYS LEU PHE ASN GLN ASP VAL ASP          
SEQRES  16 B  455  ALA ALA VAL ARG GLY ILE LEU ARG ASN ALA LYS LEU LYS          
SEQRES  17 B  455  PRO VAL TYR ASP SER LEU ASP ALA VAL ARG ARG ALA ALA          
SEQRES  18 B  455  LEU ILE ASN MET VAL PHE GLN MET GLY GLU THR GLY VAL          
SEQRES  19 B  455  ALA GLY PHE THR ASN SER LEU ARG MET LEU GLN GLN LYS          
SEQRES  20 B  455  ARG TRP ASP GLU ALA ALA VAL ASN LEU ALA LYS SER ARG          
SEQRES  21 B  455  TRP TYR ASN GLN THR PRO ASN ARG ALA LYS ARG VAL ILE          
SEQRES  22 B  455  THR THR PHE ARG THR GLY THR TRP ASP ALA TYR SER GLU          
SEQRES  23 B  455  GLN TRP ILE PHE ARG LEU TYR VAL ALA ILE GLY TRP GLY          
SEQRES  24 B  455  VAL PRO LEU LEU PHE VAL VAL PRO TRP GLY ILE VAL LYS          
SEQRES  25 B  455  TYR LEU TYR GLU ASP GLU GLY CYS TRP THR ARG ASN SER          
SEQRES  26 B  455  ASN MET ASN TYR TRP LEU ILE ILE ARG LEU PRO ILE LEU          
SEQRES  27 B  455  PHE ALA CYS ILE VAL ASN PHE LEU ILE PHE VAL ARG VAL          
SEQRES  28 B  455  ILE CYS ILE VAL VAL SER LYS LEU LYS ALA ASN LEU MET          
SEQRES  29 B  455  CYS LYS THR ASP ILE ALA PHE ARG LEU ALA LYS SER THR          
SEQRES  30 B  455  LEU THR LEU ILE PRO LEU LEU CYS THR HIS GLU VAL ILE          
SEQRES  31 B  455  PHE ALA PHE VAL MET ASP GLU HIS ALA ARG GLY THR LEU          
SEQRES  32 B  455  ARG PHE ILE LYS LEU PHE THR GLU LEU SER PHE THR SER          
SEQRES  33 B  455  PHE GLN GLY LEU MET VAL ALA ILE LEU TYR CYS PHE VAL          
SEQRES  34 B  455  ASN ASN GLU VAL GLN LEU GLU PHE ARG LYS SER TRP GLU          
SEQRES  35 B  455  ARG TRP ARG LEU GLU HIS LEU HIS ILE GLN ARG ASP SER          
HET    97Y  A2001      37                                                       
HET    97Y  B2001      37                                                       
HETNAM     97Y N-{4-[(R)-(3,3-DIMETHYLCYCLOBUTYL)({6-[4-                        
HETNAM   2 97Y  (TRIFLUOROMETHYL)-1H-IMIDAZOL-1-YL]PYRIDIN-3-                   
HETNAM   3 97Y  YL}AMINO)METHYL]BENZENE-1-CARBONYL}-BETA-ALANINE                
FORMUL   3  97Y    2(C26 H28 F3 N5 O3)                                          
FORMUL   5  HOH   *7(H2 O)                                                      
HELIX    1 AA1 SER A  136  PHE A  169  1                                  34    
HELIX    2 AA2 ARG A  170  HIS A  173  5                                   4    
HELIX    3 AA3 CYS A  174  ALA A  200  1                                  27    
HELIX    4 AA4 SER A  223  PHE A  257  1                                  35    
HELIX    5 AA5 ASN A 1001  GLY A 1011  1                                  11    
HELIX    6 AA6 SER A 1037  ALA A 1048  1                                  12    
HELIX    7 AA7 THR A 1058  ARG A 1079  1                                  22    
HELIX    8 AA8 LEU A 1083  LEU A 1090  1                                   8    
HELIX    9 AA9 ASP A 1091  MET A 1105  1                                  15    
HELIX   10 AB1 GLY A 1106  ALA A 1111  1                                   6    
HELIX   11 AB2 PHE A 1113  GLN A 1122  1                                  10    
HELIX   12 AB3 ARG A 1124  LYS A 1134  1                                  11    
HELIX   13 AB4 SER A 1135  THR A 1141  1                                   7    
HELIX   14 AB5 THR A 1141  GLY A 1155  1                                  15    
HELIX   15 AB6 TRP A 1157  SER A  261  5                                   5    
HELIX   16 AB7 GLU A  262  TRP A  274  1                                  13    
HELIX   17 AB8 TRP A  274  TYR A  291  1                                  18    
HELIX   18 AB9 MET A  303  TYR A  305  5                                   3    
HELIX   19 AC1 TRP A  306  ALA A  337  1                                  32    
HELIX   20 AC2 ASP A  344  PHE A  367  1                                  24    
HELIX   21 AC3 PHE A  381  PHE A  385  1                                   5    
HELIX   22 AC4 THR A  386  TYR A  402  1                                  17    
HELIX   23 AC5 ASN A  406  LEU A  422  1                                  17    
HELIX   24 AC6 PRO B  137  PHE B  169  1                                  33    
HELIX   25 AC7 ARG B  170  HIS B  173  5                                   4    
HELIX   26 AC8 CYS B  174  ALA B  200  1                                  27    
HELIX   27 AC9 SER B  223  PHE B  257  1                                  35    
HELIX   28 AD1 ASN B 1001  GLY B 1011  1                                  11    
HELIX   29 AD2 SER B 1037  ALA B 1048  1                                  12    
HELIX   30 AD3 THR B 1058  ARG B 1079  1                                  22    
HELIX   31 AD4 LEU B 1083  LEU B 1090  1                                   8    
HELIX   32 AD5 ASP B 1091  MET B 1105  1                                  15    
HELIX   33 AD6 GLY B 1106  ALA B 1111  1                                   6    
HELIX   34 AD7 PHE B 1113  GLN B 1122  1                                  10    
HELIX   35 AD8 ARG B 1124  LYS B 1134  1                                  11    
HELIX   36 AD9 SER B 1135  THR B 1141  1                                   7    
HELIX   37 AE1 THR B 1141  GLY B 1155  1                                  15    
HELIX   38 AE2 TRP B 1157  SER B  261  5                                   5    
HELIX   39 AE3 GLU B  262  TRP B  274  1                                  13    
HELIX   40 AE4 TRP B  274  TYR B  291  1                                  18    
HELIX   41 AE5 MET B  303  TYR B  305  5                                   3    
HELIX   42 AE6 TRP B  306  ALA B  337  1                                  32    
HELIX   43 AE7 ASP B  344  PHE B  367  1                                  24    
HELIX   44 AE8 PHE B  381  TYR B  402  1                                  22    
HELIX   45 AE9 ASN B  406  LEU B  422  1                                  17    
SHEET    1 AA1 3 ARG A1013  LYS A1018  0                                        
SHEET    2 AA1 3 TYR A1024  GLY A1027 -1  O  THR A1025   N  TYR A1017           
SHEET    3 AA1 3 HIS A1030  LEU A1031 -1  O  HIS A1030   N  ILE A1026           
SHEET    1 AA2 3 ARG B1013  LYS B1018  0                                        
SHEET    2 AA2 3 TYR B1024  GLY B1027 -1  O  THR B1025   N  TYR B1017           
SHEET    3 AA2 3 HIS B1030  LEU B1031 -1  O  HIS B1030   N  ILE B1026           
SSBOND   1 CYS A  226    CYS A  296                          1555   1555  2.03  
SSBOND   2 CYS A  317    CYS A  361                          1555   1555  2.17  
SSBOND   3 CYS B  226    CYS B  296                          1555   1555  1.99  
SSBOND   4 CYS B  317    CYS B  361                          1555   1555  2.16  
SITE     1 AC1 11 VAL A 331  PHE A 347  ARG A 348  LYS A 351                    
SITE     2 AC1 11 SER A 352  LEU A 354  THR A 355  LEU A 401                    
SITE     3 AC1 11 VAL A 405  ASN A 406  ILE B 286                               
SITE     1 AC2 10 ILE A 286  VAL B 331  PHE B 347  ARG B 348                    
SITE     2 AC2 10 LYS B 351  SER B 352  THR B 355  LEU B 401                    
SITE     3 AC2 10 VAL B 405  ASN B 406                                          
CRYST1   64.930   67.350   83.680  91.07  90.10 107.96 P 1           2          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.015401  0.004992  0.000128        0.00000                         
SCALE2      0.000000  0.015608  0.000315        0.00000                         
SCALE3      0.000000  0.000000  0.011953        0.00000                         
ATOM      1  N   SER A 136      29.814  42.784  63.383  1.00107.07           N  
ANISOU    1  N   SER A 136    14484  12186  14012    182     67    152       N  
ATOM      2  CA  SER A 136      28.682  43.113  64.309  1.00125.95           C  
ANISOU    2  CA  SER A 136    16878  14579  16399    214     63    148       C  
ATOM      3  C   SER A 136      27.500  42.180  64.048  1.00143.05           C  
ANISOU    3  C   SER A 136    19036  16745  18572    186     75    132       C  
ATOM      4  O   SER A 136      27.204  41.865  62.897  1.00145.23           O  
ANISOU    4  O   SER A 136    19309  17020  18850    170     79    127       O  
ATOM      5  CB  SER A 136      28.278  44.558  64.196  1.00115.83           C  
ANISOU    5  CB  SER A 136    15606  13302  15104    285     40    163       C  
ATOM      6  N   PRO A 137      26.802  41.697  65.105  1.00152.02           N  
ANISOU    6  N   PRO A 137    20168  17881  19711    175     82    122       N  
ATOM      7  CA  PRO A 137      25.690  40.759  64.927  1.00148.25           C  
ANISOU    7  CA  PRO A 137    19683  17403  19243    142     92    106       C  
ATOM      8  C   PRO A 137      24.429  41.435  64.387  1.00145.23           C  
ANISOU    8  C   PRO A 137    19305  17024  18852    194     84    106       C  
ATOM      9  O   PRO A 137      23.784  40.932  63.471  1.00127.28           O  
ANISOU    9  O   PRO A 137    17029  14750  16584    173     89     96       O  
ATOM     10  CB  PRO A 137      25.451  40.229  66.353  1.00149.99           C  
ANISOU   10  CB  PRO A 137    19897  17624  19469    123     97    101       C  
ATOM     11  CG  PRO A 137      25.917  41.349  67.270  1.00139.27           C  
ANISOU   11  CG  PRO A 137    18549  16269  18100    179     86    114       C  
ATOM     12  CD  PRO A 137      27.055  42.017  66.524  1.00147.25           C  
ANISOU   12  CD  PRO A 137    19566  17278  19104    193     78    126       C  
ATOM     13  N   GLU A 138      24.096  42.591  64.971  1.00147.84           N  
ANISOU   13  N   GLU A 138    19644  17362  19168    266     70    116       N  
ATOM     14  CA  GLU A 138      22.905  43.340  64.614  1.00130.03           C  
ANISOU   14  CA  GLU A 138    17390  15116  16898    330     59    116       C  
ATOM     15  C   GLU A 138      23.077  43.963  63.232  1.00131.46           C  
ANISOU   15  C   GLU A 138    17575  15301  17074    352     50    124       C  
ATOM     16  O   GLU A 138      22.094  44.081  62.512  1.00135.12           O  
ANISOU   16  O   GLU A 138    18062  15765  17514    384     54    118       O  
ATOM     17  CB  GLU A 138      22.578  44.387  65.683  1.00128.80           C  
ANISOU   17  CB  GLU A 138    17240  14974  16724    404     42    122       C  
ATOM     18  N   GLU A 139      24.315  44.339  62.864  1.00122.31           N  
ANISOU   18  N   GLU A 139    16419  14137  15915    343     43    138       N  
ATOM     19  CA  GLU A 139      24.590  44.981  61.584  1.00105.43           C  
ANISOU   19  CA  GLU A 139    14283  12003  13774    363     32    150       C  
ATOM     20  C   GLU A 139      24.395  43.986  60.443  1.00109.02           C  
ANISOU   20  C   GLU A 139    14731  12451  14241    311     48    138       C  
ATOM     21  O   GLU A 139      23.954  44.358  59.351  1.00 93.05           O  
ANISOU   21  O   GLU A 139    12707  10433  12215    334     42    142       O  
ATOM     22  CB  GLU A 139      26.011  45.550  61.543  1.00 94.27           C  
ANISOU   22  CB  GLU A 139    12874  10586  12360    361     21    168       C  
ATOM     23  N   GLN A 140      24.726  42.716  60.723  1.00119.24           N  
ANISOU   23  N   GLN A 140    16020  13735  15549    241     67    124       N  
ATOM     24  CA  GLN A 140      24.648  41.648  59.738  1.00105.23           C  
ANISOU   24  CA  GLN A 140    14239  11956  13786    184     81    109       C  
ATOM     25  C   GLN A 140      23.186  41.397  59.381  1.00102.02           C  
ANISOU   25  C   GLN A 140    13853  11544  13364    194     92     94       C  
ATOM     26  O   GLN A 140      22.851  41.347  58.198  1.00106.74           O  
ANISOU   26  O   GLN A 140    14501  12128  13929    198    110     90       O  
ATOM     27  CB  GLN A 140      25.355  40.386  60.241  1.00101.29           C  
ANISOU   27  CB  GLN A 140    13733  11453  13299    111     95     97       C  
ATOM     28  N   LEU A 141      22.329  41.254  60.404  1.00 93.83           N  
ANISOU   28  N   LEU A 141    12866  10494  12291    211    112     87       N  
ATOM     29  CA  LEU A 141      20.925  40.930  60.199  1.00 91.89           C  
ANISOU   29  CA  LEU A 141    12733  10215  11964    231    159     72       C  
ATOM     30  C   LEU A 141      20.184  42.096  59.540  1.00 92.42           C  
ANISOU   30  C   LEU A 141    12863  10281  11971    334    155     80       C  
ATOM     31  O   LEU A 141      19.212  41.866  58.842  1.00101.10           O  
ANISOU   31  O   LEU A 141    14046  11359  13010    355    189     68       O  
ATOM     32  CB  LEU A 141      20.271  40.498  61.518  1.00 78.47           C  
ANISOU   32  CB  LEU A 141    11066   8505  10245    227    179     66       C  
ATOM     33  N   LEU A 142      20.649  43.337  59.727  1.00 96.69           N  
ANISOU   33  N   LEU A 142    13357  10851  12532    397    111     99       N  
ATOM     34  CA  LEU A 142      19.989  44.492  59.128  1.00 97.67           C  
ANISOU   34  CA  LEU A 142    13523  10987  12602    498     92    107       C  
ATOM     35  C   LEU A 142      20.400  44.649  57.669  1.00 90.77           C  
ANISOU   35  C   LEU A 142    12639  10111  11737    483     87    115       C  
ATOM     36  O   LEU A 142      19.586  45.056  56.838  1.00 99.51           O  
ANISOU   36  O   LEU A 142    13807  11217  12784    548     89    113       O  
ATOM     37  CB  LEU A 142      20.329  45.769  59.899  1.00107.96           C  
ANISOU   37  CB  LEU A 142    14769  12324  13926    556     44    124       C  
ATOM     38  N   PHE A 143      21.659  44.334  57.362  1.00 78.54           N  
ANISOU   38  N   PHE A 143    11011   8568  10262    407     77    124       N  
ATOM     39  CA  PHE A 143      22.140  44.521  56.005  1.00 85.84           C  
ANISOU   39  CA  PHE A 143    11924   9495  11198    397     70    134       C  
ATOM     40  C   PHE A 143      21.468  43.548  55.037  1.00 96.38           C  
ANISOU   40  C   PHE A 143    13335  10799  12485    368    114    113       C  
ATOM     41  O   PHE A 143      21.098  43.933  53.921  1.00 95.00           O  
ANISOU   41  O   PHE A 143    13202  10620  12274    406    116    117       O  
ATOM     42  CB  PHE A 143      23.659  44.387  55.942  1.00 91.46           C  
ANISOU   42  CB  PHE A 143    12528  10225  11996    334     48    147       C  
ATOM     43  CG  PHE A 143      24.205  44.810  54.607  1.00101.04           C  
ANISOU   43  CG  PHE A 143    13724  11444  13221    337     36    164       C  
ATOM     44  CD1 PHE A 143      24.320  46.155  54.280  1.00113.37           C  
ANISOU   44  CD1 PHE A 143    15266  13025  14786    394      7    192       C  
ATOM     45  CD2 PHE A 143      24.565  43.866  53.660  1.00119.04           C  
ANISOU   45  CD2 PHE A 143    16011  13713  15506    283     54    153       C  
ATOM     46  CE1 PHE A 143      24.804  46.548  53.041  1.00123.90           C  
ANISOU   46  CE1 PHE A 143    16592  14361  16122    399     -3    211       C  
ATOM     47  CE2 PHE A 143      25.058  44.260  52.422  1.00131.86           C  
ANISOU   47  CE2 PHE A 143    17625  15342  17136    290     44    170       C  
ATOM     48  CZ  PHE A 143      25.174  45.599  52.113  1.00130.64           C  
ANISOU   48  CZ  PHE A 143    17450  15203  16984    347     16    201       C  
ATOM     49  N   LEU A 144      21.321  42.289  55.474  1.00100.70           N  
ANISOU   49  N   LEU A 144    13896  11329  13038    296    148     89       N  
ATOM     50  CA  LEU A 144      20.647  41.274  54.682  1.00 94.15           C  
ANISOU   50  CA  LEU A 144    13132  10470  12172    249    196     63       C  
ATOM     51  C   LEU A 144      19.155  41.573  54.546  1.00105.66           C  
ANISOU   51  C   LEU A 144    14692  11907  13546    320    227     51       C  
ATOM     52  O   LEU A 144      18.567  41.207  53.537  1.00119.85           O  
ANISOU   52  O   LEU A 144    16453  13780  15303    289    243     31       O  
ATOM     53  CB  LEU A 144      20.890  39.892  55.289  1.00 90.94           C  
ANISOU   53  CB  LEU A 144    12696  10059  11800    147    215     42       C  
ATOM     54  CG  LEU A 144      22.357  39.475  55.369  1.00 84.80           C  
ANISOU   54  CG  LEU A 144    11809   9309  11100     93    177     49       C  
ATOM     55  CD1 LEU A 144      22.559  38.511  56.522  1.00 82.02           C  
ANISOU   55  CD1 LEU A 144    11413   8966  10783     32    173     39       C  
ATOM     56  CD2 LEU A 144      22.805  38.800  54.076  1.00 76.52           C  
ANISOU   56  CD2 LEU A 144    10751   8260  10063     43    184     37       C  
ATOM     57  N   TYR A 145      18.550  42.234  55.544  1.00108.49           N  
ANISOU   57  N   TYR A 145    15058  12289  13873    395    212     58       N  
ATOM     58  CA  TYR A 145      17.151  42.633  55.470  1.00105.94           C  
ANISOU   58  CA  TYR A 145    14663  12124  13463    439    203     40       C  
ATOM     59  C   TYR A 145      16.928  43.651  54.349  1.00107.89           C  
ANISOU   59  C   TYR A 145    14897  12419  13679    510    175     48       C  
ATOM     60  O   TYR A 145      15.845  43.690  53.766  1.00110.37           O  
ANISOU   60  O   TYR A 145    15146  12864  13925    513    178     27       O  
ATOM     61  CB  TYR A 145      16.652  43.153  56.823  1.00109.13           C  
ANISOU   61  CB  TYR A 145    15065  12557  13844    507    185     43       C  
ATOM     62  CG  TYR A 145      15.275  43.770  56.795  1.00111.23           C  
ANISOU   62  CG  TYR A 145    15262  12980  14018    571    169     27       C  
ATOM     63  CD1 TYR A 145      14.130  42.993  56.925  1.00110.50           C  
ANISOU   63  CD1 TYR A 145    15098  13022  13866    517    195      2       C  
ATOM     64  CD2 TYR A 145      15.113  45.136  56.618  1.00109.28           C  
ANISOU   64  CD2 TYR A 145    15023  12749  13749    686    121     38       C  
ATOM     65  CE1 TYR A 145      12.861  43.556  56.881  1.00114.22           C  
ANISOU   65  CE1 TYR A 145    15507  13638  14252    576    181    -12       C  
ATOM     66  CE2 TYR A 145      13.852  45.713  56.571  1.00111.99           C  
ANISOU   66  CE2 TYR A 145    15305  13237  14010    745    104     20       C  
ATOM     67  CZ  TYR A 145      12.720  44.922  56.701  1.00114.69           C  
ANISOU   67  CZ  TYR A 145    15577  13711  14290    690    136     -6       C  
ATOM     68  OH  TYR A 145      11.489  45.506  56.649  1.00114.77           O  
ANISOU   68  OH  TYR A 145    15528  13862  14218    749    119    -23       O  
ATOM     69  N   ILE A 146      17.950  44.464  54.050  1.00104.63           N  
ANISOU   69  N   ILE A 146    14543  11897  13315    564    144     81       N  
ATOM     70  CA  ILE A 146      17.856  45.464  52.993  1.00106.18           C  
ANISOU   70  CA  ILE A 146    14726  12128  13490    629    109     96       C  
ATOM     71  C   ILE A 146      17.888  44.790  51.620  1.00114.56           C  
ANISOU   71  C   ILE A 146    15756  13227  14543    555    138     82       C  
ATOM     72  O   ILE A 146      16.984  44.991  50.806  1.00 98.14           O  
ANISOU   72  O   ILE A 146    13618  11265  12404    563    137     65       O  
ATOM     73  CB  ILE A 146      18.953  46.535  53.149  1.00111.41           C  
ANISOU   73  CB  ILE A 146    15375  12744  14211    668     55    136       C  
ATOM     74  CG1 ILE A 146      18.798  47.294  54.469  1.00110.53           C  
ANISOU   74  CG1 ILE A 146    15233  12662  14102    721     20    140       C  
ATOM     75  CG2 ILE A 146      18.975  47.487  51.964  1.00108.55           C  
ANISOU   75  CG2 ILE A 146    15004  12406  13836    722     18    157       C  
ATOM     76  CD1 ILE A 146      17.432  47.915  54.662  1.00109.72           C  
ANISOU   76  CD1 ILE A 146    15178  12594  13918    845      0    126       C  
ATOM     77  N   ILE A 147      18.924  43.974  51.377  1.00118.18           N  
ANISOU   77  N   ILE A 147    16254  13588  15061    481    163     87       N  
ATOM     78  CA  ILE A 147      19.102  43.308  50.092  1.00114.73           C  
ANISOU   78  CA  ILE A 147    15793  13177  14622    414    187     73       C  
ATOM     79  C   ILE A 147      17.942  42.347  49.812  1.00107.47           C  
ANISOU   79  C   ILE A 147    14801  12385  13646    347    221     28       C  
ATOM     80  O   ILE A 147      17.669  42.030  48.664  1.00124.83           O  
ANISOU   80  O   ILE A 147    16961  14648  15819    314    233     12       O  
ATOM     81  CB  ILE A 147      20.488  42.631  49.980  1.00113.39           C  
ANISOU   81  CB  ILE A 147    15659  12897  14528    348    199     84       C  
ATOM     82  CG1 ILE A 147      20.702  41.561  51.052  1.00138.90           C  
ANISOU   82  CG1 ILE A 147    18861  16120  17793    265    217     63       C  
ATOM     83  CG2 ILE A 147      21.605  43.663  50.020  1.00114.29           C  
ANISOU   83  CG2 ILE A 147    15692  13043  14691    376    141    123       C  
ATOM     84  CD1 ILE A 147      20.228  40.180  50.666  1.00142.98           C  
ANISOU   84  CD1 ILE A 147    19403  16626  18297    175    267     21       C  
ATOM     85  N   TYR A 148      17.257  41.885  50.865  1.00 95.80           N  
ANISOU   85  N   TYR A 148    13305  10946  12149    327    234     10       N  
ATOM     86  CA  TYR A 148      16.120  40.987  50.744  1.00 88.28           C  
ANISOU   86  CA  TYR A 148    12283  10115  11144    265    260    -24       C  
ATOM     87  C   TYR A 148      14.884  41.770  50.313  1.00 94.32           C  
ANISOU   87  C   TYR A 148    12992  11015  11830    328    246    -31       C  
ATOM     88  O   TYR A 148      14.141  41.337  49.435  1.00 97.95           O  
ANISOU   88  O   TYR A 148    13398  11570  12249    292    262    -53       O  
ATOM     89  CB  TYR A 148      15.874  40.241  52.059  1.00 91.52           C  
ANISOU   89  CB  TYR A 148    12691  10520  11563    221    274    -33       C  
ATOM     90  CG  TYR A 148      14.745  39.238  52.053  1.00 96.40           C  
ANISOU   90  CG  TYR A 148    13238  11257  12134    152    295    -61       C  
ATOM     91  CD1 TYR A 148      14.976  37.910  51.712  1.00 94.49           C  
ANISOU   91  CD1 TYR A 148    12982  10998  11923     46    315    -81       C  
ATOM     92  CD2 TYR A 148      13.450  39.611  52.414  1.00 87.88           C  
ANISOU   92  CD2 TYR A 148    12104  10307  10981    194    290    -66       C  
ATOM     93  CE1 TYR A 148      13.933  36.996  51.710  1.00 93.72           C  
ANISOU   93  CE1 TYR A 148    12816  11008  11784    -16    325   -100       C  
ATOM     94  CE2 TYR A 148      12.404  38.704  52.408  1.00 78.78           C  
ANISOU   94  CE2 TYR A 148    10885   9265   9785    132    306    -84       C  
ATOM     95  CZ  TYR A 148      12.654  37.388  52.064  1.00 82.54           C  
ANISOU   95  CZ  TYR A 148    11347   9719  10295     27    322    -99       C  
ATOM     96  OH  TYR A 148      11.657  36.461  52.042  1.00 72.72           O  
ANISOU   96  OH  TYR A 148    10038   8579   9015    -36    330   -112       O  
ATOM     97  N   THR A 149      14.655  42.924  50.949  1.00 91.79           N  
ANISOU   97  N   THR A 149    12683  10702  11491    423    214    -14       N  
ATOM     98  CA  THR A 149      13.452  43.694  50.676  1.00 91.15           C  
ANISOU   98  CA  THR A 149    12549  10748  11336    485    197    -23       C  
ATOM     99  C   THR A 149      13.571  44.421  49.336  1.00 92.92           C  
ANISOU   99  C   THR A 149    12766  10989  11553    518    178    -15       C  
ATOM    100  O   THR A 149      12.585  44.529  48.605  1.00 87.40           O  
ANISOU  100  O   THR A 149    12011  10403  10796    520    182    -33       O  
ATOM    101  CB  THR A 149      13.089  44.612  51.845  1.00 86.30           C  
ANISOU  101  CB  THR A 149    11943  10147  10701    575    165    -15       C  
ATOM    102  OG1 THR A 149      14.285  45.340  52.115  1.00104.48           O  
ANISOU  102  OG1 THR A 149    14315  12316  13066    628    133     17       O  
ATOM    103  CG2 THR A 149      12.604  43.855  53.066  1.00 87.30           C  
ANISOU  103  CG2 THR A 149    12053  10306  10812    540    187    -27       C  
ATOM    104  N   VAL A 150      14.783  44.885  49.001  1.00 89.04           N  
ANISOU  104  N   VAL A 150    12328  10385  11120    540    157     14       N  
ATOM    105  CA  VAL A 150      15.010  45.505  47.701  1.00 94.18           C  
ANISOU  105  CA  VAL A 150    12968  11047  11767    564    138     28       C  
ATOM    106  C   VAL A 150      14.994  44.447  46.602  1.00 98.58           C  
ANISOU  106  C   VAL A 150    13494  11640  12320    475    179      5       C  
ATOM    107  O   VAL A 150      14.725  44.768  45.449  1.00114.12           O  
ANISOU  107  O   VAL A 150    15429  13668  14262    482    174      4       O  
ATOM    108  CB  VAL A 150      16.284  46.371  47.638  1.00 89.26           C  
ANISOU  108  CB  VAL A 150    12406  10302  11206    618     97     74       C  
ATOM    109  CG1 VAL A 150      16.325  47.397  48.758  1.00 80.73           C  
ANISOU  109  CG1 VAL A 150    11358   9181  10136    710     50     96       C  
ATOM    110  CG2 VAL A 150      17.558  45.545  47.595  1.00 89.63           C  
ANISOU  110  CG2 VAL A 150    12505  10231  11321    554    122     87       C  
ATOM    111  N   GLY A 151      15.311  43.198  46.963  1.00 97.15           N  
ANISOU  111  N   GLY A 151    13325  11420  12167    392    215    -12       N  
ATOM    112  CA  GLY A 151      15.208  42.066  46.054  1.00 85.31           C  
ANISOU  112  CA  GLY A 151    11793   9958  10662    306    249    -41       C  
ATOM    113  C   GLY A 151      13.764  41.841  45.611  1.00 80.84           C  
ANISOU  113  C   GLY A 151    11154   9536  10024    294    263    -69       C  
ATOM    114  O   GLY A 151      13.493  41.673  44.423  1.00 74.49           O  
ANISOU  114  O   GLY A 151    10316   8791   9198    274    272    -83       O  
ATOM    115  N   TYR A 152      12.840  41.861  46.579  1.00 76.46           N  
ANISOU  115  N   TYR A 152    10578   9041   9432    308    263    -77       N  
ATOM    116  CA  TYR A 152      11.427  41.698  46.269  1.00 75.09           C  
ANISOU  116  CA  TYR A 152    10338   9005   9189    301    275   -100       C  
ATOM    117  C   TYR A 152      10.810  42.989  45.728  1.00 81.11           C  
ANISOU  117  C   TYR A 152    11078   9835   9904    383    248    -93       C  
ATOM    118  O   TYR A 152       9.799  42.933  45.034  1.00 78.74           O  
ANISOU  118  O   TYR A 152    10726   9639   9552    375    258   -110       O  
ATOM    119  CB  TYR A 152      10.647  41.164  47.469  1.00 72.54           C  
ANISOU  119  CB  TYR A 152     9993   8730   8840    281    285   -108       C  
ATOM    120  CG  TYR A 152      10.797  39.680  47.697  1.00 69.76           C  
ANISOU  120  CG  TYR A 152     9633   8358   8516    180    310   -122       C  
ATOM    121  CD1 TYR A 152      10.018  38.762  47.007  1.00 68.41           C  
ANISOU  121  CD1 TYR A 152     9407   8270   8315    117    327   -144       C  
ATOM    122  CD2 TYR A 152      11.698  39.190  48.634  1.00 70.78           C  
ANISOU  122  CD2 TYR A 152     9806   8383   8703    147    312   -114       C  
ATOM    123  CE1 TYR A 152      10.164  37.395  47.227  1.00 71.70           C  
ANISOU  123  CE1 TYR A 152     9814   8667   8764     25    339   -156       C  
ATOM    124  CE2 TYR A 152      11.838  37.833  48.878  1.00 62.80           C  
ANISOU  124  CE2 TYR A 152     8784   7353   7723     51    327   -127       C  
ATOM    125  CZ  TYR A 152      11.080  36.926  48.158  1.00 66.56           C  
ANISOU  125  CZ  TYR A 152     9205   7913   8172    -10    338   -149       C  
ATOM    126  OH  TYR A 152      11.248  35.582  48.363  1.00 60.77           O  
ANISOU  126  OH  TYR A 152     8460   7158   7474   -105    343   -162       O  
ATOM    127  N   ALA A 153      11.400  44.148  46.061  1.00 89.74           N  
ANISOU  127  N   ALA A 153    12211  10867  11019    462    211    -66       N  
ATOM    128  CA  ALA A 153      10.943  45.410  45.495  1.00 83.77           C  
ANISOU  128  CA  ALA A 153    11434  10164  10229    538    175    -58       C  
ATOM    129  C   ALA A 153      11.280  45.483  44.002  1.00 85.45           C  
ANISOU  129  C   ALA A 153    11633  10383  10450    518    177    -54       C  
ATOM    130  O   ALA A 153      10.441  45.877  43.196  1.00 85.67           O  
ANISOU  130  O   ALA A 153    11615  10504  10432    532    173    -65       O  
ATOM    131  CB  ALA A 153      11.493  46.577  46.276  1.00 70.22           C  
ANISOU  131  CB  ALA A 153     9762   8379   8540    627    125    -30       C  
ATOM    132  N   LEU A 154      12.508  45.093  43.631  1.00 82.30           N  
ANISOU  132  N   LEU A 154    11272   9889  10109    485    184    -38       N  
ATOM    133  CA  LEU A 154      12.929  45.091  42.235  1.00 83.57           C  
ANISOU  133  CA  LEU A 154    11419  10057  10278    464    187    -33       C  
ATOM    134  C   LEU A 154      12.181  44.013  41.447  1.00 90.37           C  
ANISOU  134  C   LEU A 154    12230  11003  11104    391    229    -71       C  
ATOM    135  O   LEU A 154      11.933  44.188  40.256  1.00 82.00           O  
ANISOU  135  O   LEU A 154    11134  10001  10022    388    230    -76       O  
ATOM    136  CB  LEU A 154      14.442  44.857  42.142  1.00 71.61           C  
ANISOU  136  CB  LEU A 154     9958   8419   8831    446    184     -7       C  
ATOM    137  CG  LEU A 154      15.298  46.107  41.993  1.00 69.88           C  
ANISOU  137  CG  LEU A 154     9772   8134   8645    518    134     42       C  
ATOM    138  CD1 LEU A 154      14.935  47.122  43.058  1.00 74.64           C  
ANISOU  138  CD1 LEU A 154    10391   8727   9241    597     92     57       C  
ATOM    139  CD2 LEU A 154      16.784  45.771  42.042  1.00 69.02           C  
ANISOU  139  CD2 LEU A 154     9721   7900   8605    495    135     69       C  
ATOM    140  N   SER A 155      11.863  42.886  42.106  1.00 90.32           N  
ANISOU  140  N   SER A 155    12219  11002  11096    333    259    -95       N  
ATOM    141  CA  SER A 155      11.173  41.785  41.451  1.00 77.99           C  
ANISOU  141  CA  SER A 155    10611   9513   9508    263    292   -128       C  
ATOM    142  C   SER A 155       9.713  42.152  41.181  1.00 71.22           C  
ANISOU  142  C   SER A 155     9699   8781   8581    286    293   -142       C  
ATOM    143  O   SER A 155       9.218  41.947  40.077  1.00 67.62           O  
ANISOU  143  O   SER A 155     9203   8391   8098    265    305   -158       O  
ATOM    144  CB  SER A 155      11.302  40.497  42.234  1.00 76.23           C  
ANISOU  144  CB  SER A 155    10398   9256   9311    192    313   -145       C  
ATOM    145  OG  SER A 155      12.649  40.048  42.278  1.00 68.30           O  
ANISOU  145  OG  SER A 155     9442   8138   8372    161    314   -138       O  
ATOM    146  N   PHE A 156       9.036  42.709  42.190  1.00 69.30           N  
ANISOU  146  N   PHE A 156     9453   8570   8309    330    280   -137       N  
ATOM    147  CA  PHE A 156       7.623  43.040  42.081  1.00 69.96           C  
ANISOU  147  CA  PHE A 156     9486   8772   8325    352    282   -151       C  
ATOM    148  C   PHE A 156       7.422  44.029  40.945  1.00 66.53           C  
ANISOU  148  C   PHE A 156     9031   8378   7869    395    263   -147       C  
ATOM    149  O   PHE A 156       6.556  43.835  40.093  1.00 58.76           O  
ANISOU  149  O   PHE A 156     8003   7479   6846    374    279   -164       O  
ATOM    150  CB  PHE A 156       7.088  43.670  43.369  1.00 73.17           C  
ANISOU  150  CB  PHE A 156     9897   9200   8705    408    262   -144       C  
ATOM    151  CG  PHE A 156       5.630  44.062  43.350  1.00 78.76           C  
ANISOU  151  CG  PHE A 156    10554  10032   9340    436    261   -158       C  
ATOM    152  CD1 PHE A 156       4.641  43.140  43.692  1.00 88.05           C  
ANISOU  152  CD1 PHE A 156    11691  11286  10477    388    289   -172       C  
ATOM    153  CD2 PHE A 156       5.245  45.354  43.011  1.00 72.54           C  
ANISOU  153  CD2 PHE A 156     9756   9282   8524    509    228   -156       C  
ATOM    154  CE1 PHE A 156       3.300  43.507  43.693  1.00 91.74           C  
ANISOU  154  CE1 PHE A 156    12113  11867  10876    415    288   -183       C  
ATOM    155  CE2 PHE A 156       3.904  45.717  43.004  1.00 76.12           C  
ANISOU  155  CE2 PHE A 156    10164   9848   8911    533    226   -171       C  
ATOM    156  CZ  PHE A 156       2.935  44.796  43.341  1.00 86.29           C  
ANISOU  156  CZ  PHE A 156    11415  11213  10158    487    258   -184       C  
ATOM    157  N   SER A 157       8.230  45.094  40.962  1.00 70.59           N  
ANISOU  157  N   SER A 157     9578   8829   8413    454    226   -121       N  
ATOM    158  CA  SER A 157       8.133  46.139  39.959  1.00 74.76           C  
ANISOU  158  CA  SER A 157    10087   9389   8928    497    198   -111       C  
ATOM    159  C   SER A 157       8.348  45.564  38.563  1.00 71.53           C  
ANISOU  159  C   SER A 157     9654   8999   8524    444    223   -119       C  
ATOM    160  O   SER A 157       7.538  45.808  37.665  1.00 63.81           O  
ANISOU  160  O   SER A 157     8632   8105   7507    444    227   -132       O  
ATOM    161  CB  SER A 157       9.081  47.257  40.252  1.00 69.82           C  
ANISOU  161  CB  SER A 157     9502   8684   8343    564    148    -75       C  
ATOM    162  OG  SER A 157       8.698  47.870  41.462  1.00 69.95           O  
ANISOU  162  OG  SER A 157     9532   8700   8347    622    120    -73       O  
ATOM    163  N   ALA A 158       9.436  44.794  38.421  1.00 66.73           N  
ANISOU  163  N   ALA A 158     9076   8314   7964    401    239   -114       N  
ATOM    164  CA  ALA A 158       9.836  44.220  37.147  1.00 66.01           C  
ANISOU  164  CA  ALA A 158     8967   8232   7883    356    258   -122       C  
ATOM    165  C   ALA A 158       8.762  43.259  36.625  1.00 72.02           C  
ANISOU  165  C   ALA A 158     9680   9082   8603    302    295   -160       C  
ATOM    166  O   ALA A 158       8.500  43.227  35.424  1.00 74.40           O  
ANISOU  166  O   ALA A 158     9946   9438   8886    289    303   -170       O  
ATOM    167  CB  ALA A 158      11.197  43.571  37.266  1.00 57.80           C  
ANISOU  167  CB  ALA A 158     7971   7089   6902    324    265   -112       C  
ATOM    168  N   LEU A 159       8.120  42.501  37.521  1.00 64.11           N  
ANISOU  168  N   LEU A 159     8675   8097   7587    272    313   -177       N  
ATOM    169  CA  LEU A 159       7.122  41.540  37.098  1.00 64.44           C  
ANISOU  169  CA  LEU A 159     8673   8217   7594    221    341   -206       C  
ATOM    170  C   LEU A 159       5.810  42.228  36.720  1.00 67.79           C  
ANISOU  170  C   LEU A 159     9055   8744   7959    252    339   -212       C  
ATOM    171  O   LEU A 159       5.105  41.778  35.819  1.00 73.34           O  
ANISOU  171  O   LEU A 159     9719   9514   8635    222    357   -230       O  
ATOM    172  CB  LEU A 159       6.923  40.502  38.204  1.00 68.16           C  
ANISOU  172  CB  LEU A 159     9153   8672   8075    176    353   -215       C  
ATOM    173  CG  LEU A 159       8.070  39.508  38.374  1.00 65.09           C  
ANISOU  173  CG  LEU A 159     8796   8191   7745    123    359   -220       C  
ATOM    174  CD1 LEU A 159       7.994  38.820  39.728  1.00 64.04           C  
ANISOU  174  CD1 LEU A 159     8676   8028   7626     92    361   -219       C  
ATOM    175  CD2 LEU A 159       8.082  38.491  37.246  1.00 57.66           C  
ANISOU  175  CD2 LEU A 159     7826   7273   6809     67    374   -246       C  
ATOM    176  N   VAL A 160       5.475  43.325  37.399  1.00 76.91           N  
ANISOU  176  N   VAL A 160    10217   9911   9093    314    314   -197       N  
ATOM    177  CA  VAL A 160       4.243  44.032  37.066  1.00 84.27           C  
ANISOU  177  CA  VAL A 160    11110  10940   9970    345    309   -205       C  
ATOM    178  C   VAL A 160       4.436  44.771  35.737  1.00 82.82           C  
ANISOU  178  C   VAL A 160    10908  10772   9787    363    296   -200       C  
ATOM    179  O   VAL A 160       3.522  44.832  34.913  1.00 78.35           O  
ANISOU  179  O   VAL A 160    10302  10285   9183    353    308   -215       O  
ATOM    180  CB  VAL A 160       3.763  44.959  38.210  1.00 82.76           C  
ANISOU  180  CB  VAL A 160    10927  10765   9754    409    281   -197       C  
ATOM    181  CG1 VAL A 160       2.587  45.834  37.805  1.00 67.53           C  
ANISOU  181  CG1 VAL A 160     8959   8928   7770    446    268   -206       C  
ATOM    182  CG2 VAL A 160       3.430  44.192  39.487  1.00 72.62           C  
ANISOU  182  CG2 VAL A 160     9649   9483   8460    389    296   -200       C  
ATOM    183  N   ILE A 161       5.644  45.312  35.523  1.00 71.69           N  
ANISOU  183  N   ILE A 161     9528   9289   8422    386    271   -177       N  
ATOM    184  CA  ILE A 161       5.972  45.991  34.277  1.00 66.36           C  
ANISOU  184  CA  ILE A 161     8834   8627   7753    400    255   -165       C  
ATOM    185  C   ILE A 161       6.000  44.979  33.133  1.00 69.58           C  
ANISOU  185  C   ILE A 161     9215   9062   8159    340    292   -185       C  
ATOM    186  O   ILE A 161       5.442  45.226  32.060  1.00 65.24           O  
ANISOU  186  O   ILE A 161     8626   8578   7583    335    296   -194       O  
ATOM    187  CB  ILE A 161       7.301  46.757  34.416  1.00 63.00           C  
ANISOU  187  CB  ILE A 161     8447   8114   7377    439    215   -127       C  
ATOM    188  CG1 ILE A 161       7.130  48.001  35.302  1.00 62.46           C  
ANISOU  188  CG1 ILE A 161     8394   8033   7306    512    166   -108       C  
ATOM    189  CG2 ILE A 161       7.892  47.084  33.053  1.00 61.96           C  
ANISOU  189  CG2 ILE A 161     8293   7990   7259    434    206   -111       C  
ATOM    190  CD1 ILE A 161       8.413  48.720  35.640  1.00 63.11           C  
ANISOU  190  CD1 ILE A 161     8519   8019   7442    555    121    -66       C  
ATOM    191  N   ALA A 162       6.653  43.835  33.373  1.00 74.87           N  
ANISOU  191  N   ALA A 162     9908   9680   8859    294    314   -194       N  
ATOM    192  CA  ALA A 162       6.786  42.804  32.355  1.00 83.12           C  
ANISOU  192  CA  ALA A 162    10931  10744   9909    240    342   -217       C  
ATOM    193  C   ALA A 162       5.410  42.282  31.974  1.00 84.31           C  
ANISOU  193  C   ALA A 162    11037  10984  10012    213    366   -245       C  
ATOM    194  O   ALA A 162       5.129  42.099  30.793  1.00 83.71           O  
ANISOU  194  O   ALA A 162    10928  10958   9921    196    378   -259       O  
ATOM    195  CB  ALA A 162       7.686  41.683  32.815  1.00 94.23           C  
ANISOU  195  CB  ALA A 162    12369  12077  11358    197    354   -225       C  
ATOM    196  N   SER A 163       4.564  42.053  32.983  1.00 86.61           N  
ANISOU  196  N   SER A 163    11330  11297  10280    210    372   -250       N  
ATOM    197  CA  SER A 163       3.229  41.540  32.722  1.00 96.93           C  
ANISOU  197  CA  SER A 163    12597  12687  11543    185    393   -271       C  
ATOM    198  C   SER A 163       2.396  42.578  31.965  1.00 92.73           C  
ANISOU  198  C   SER A 163    12034  12227  10971    220    387   -270       C  
ATOM    199  O   SER A 163       1.544  42.205  31.157  1.00 83.92           O  
ANISOU  199  O   SER A 163    10883  11175   9827    195    406   -286       O  
ATOM    200  CB  SER A 163       2.560  41.041  33.974  1.00 87.88           C  
ANISOU  200  CB  SER A 163    11456  11554  10381    173    398   -271       C  
ATOM    201  OG  SER A 163       2.558  42.069  34.945  1.00110.46           O  
ANISOU  201  OG  SER A 163    14336  14401  13232    227    376   -253       O  
ATOM    202  N   ALA A 164       2.666  43.868  32.213  1.00 85.74           N  
ANISOU  202  N   ALA A 164    11162  11328  10087    275    357   -250       N  
ATOM    203  CA  ALA A 164       2.015  44.946  31.476  1.00 82.94           C  
ANISOU  203  CA  ALA A 164    10778  11033   9703    307    342   -248       C  
ATOM    204  C   ALA A 164       2.432  44.923  30.007  1.00 83.06           C  
ANISOU  204  C   ALA A 164    10769  11060   9729    288    348   -250       C  
ATOM    205  O   ALA A 164       1.636  45.237  29.125  1.00 82.21           O  
ANISOU  205  O   ALA A 164    10625  11019   9593    285    354   -259       O  
ATOM    206  CB  ALA A 164       2.305  46.291  32.094  1.00 69.48           C  
ANISOU  206  CB  ALA A 164     9091   9304   8004    371    296   -226       C  
ATOM    207  N   ILE A 165       3.689  44.558  29.748  1.00 77.82           N  
ANISOU  207  N   ILE A 165    10125  10334   9108    276    346   -240       N  
ATOM    208  CA  ILE A 165       4.175  44.522  28.380  1.00 78.63           C  
ANISOU  208  CA  ILE A 165    10203  10453   9221    261    350   -240       C  
ATOM    209  C   ILE A 165       3.488  43.404  27.597  1.00 80.14           C  
ANISOU  209  C   ILE A 165    10363  10696   9391    213    388   -273       C  
ATOM    210  O   ILE A 165       3.019  43.642  26.482  1.00 81.35           O  
ANISOU  210  O   ILE A 165    10478  10907   9523    209    394   -281       O  
ATOM    211  CB  ILE A 165       5.708  44.407  28.332  1.00 76.65           C  
ANISOU  211  CB  ILE A 165     9980  10125   9017    263    337   -220       C  
ATOM    212  CG1 ILE A 165       6.369  45.647  28.935  1.00 77.86           C  
ANISOU  212  CG1 ILE A 165    10160  10230   9193    316    293   -180       C  
ATOM    213  CG2 ILE A 165       6.187  44.159  26.905  1.00 70.59           C  
ANISOU  213  CG2 ILE A 165     9182   9386   8255    244    346   -224       C  
ATOM    214  CD1 ILE A 165       7.867  45.519  29.072  1.00 79.51           C  
ANISOU  214  CD1 ILE A 165    10405  10355   9451    319    280   -155       C  
ATOM    215  N   LEU A 166       3.444  42.197  28.186  1.00 83.59           N  
ANISOU  215  N   LEU A 166    10814  11108   9836    177    407   -291       N  
ATOM    216  CA  LEU A 166       2.861  41.024  27.543  1.00 90.82           C  
ANISOU  216  CA  LEU A 166    11703  12063  10740    131    433   -321       C  
ATOM    217  C   LEU A 166       1.370  41.232  27.275  1.00 93.73           C  
ANISOU  217  C   LEU A 166    12040  12511  11062    131    446   -330       C  
ATOM    218  O   LEU A 166       0.846  40.749  26.272  1.00100.98           O  
ANISOU  218  O   LEU A 166    12927  13476  11965    109    463   -349       O  
ATOM    219  CB  LEU A 166       3.096  39.773  28.404  1.00 86.50           C  
ANISOU  219  CB  LEU A 166    11179  11471  10217     93    439   -333       C  
ATOM    220  CG  LEU A 166       4.558  39.369  28.590  1.00 67.23           C  
ANISOU  220  CG  LEU A 166     8771   8948   7826     84    429   -331       C  
ATOM    221  CD1 LEU A 166       4.656  37.979  29.192  1.00 55.68           C  
ANISOU  221  CD1 LEU A 166     7319   7451   6386     35    433   -350       C  
ATOM    222  CD2 LEU A 166       5.288  39.426  27.256  1.00 67.30           C  
ANISOU  222  CD2 LEU A 166     8761   8965   7844     86    429   -337       C  
ATOM    223  N   LEU A 167       0.693  41.952  28.173  1.00 92.54           N  
ANISOU  223  N   LEU A 167    11898  12377  10887    159    437   -318       N  
ATOM    224  CA  LEU A 167      -0.726  42.213  27.979  1.00100.16           C  
ANISOU  224  CA  LEU A 167    12834  13417  11806    161    448   -325       C  
ATOM    225  C   LEU A 167      -0.953  43.405  27.045  1.00105.08           C  
ANISOU  225  C   LEU A 167    13433  14079  12413    189    437   -320       C  
ATOM    226  O   LEU A 167      -1.905  43.398  26.272  1.00 98.65           O  
ANISOU  226  O   LEU A 167    12588  13325  11570    176    453   -333       O  
ATOM    227  CB  LEU A 167      -1.398  42.455  29.333  1.00 95.56           C  
ANISOU  227  CB  LEU A 167    12264  12844  11199    180    441   -316       C  
ATOM    228  CG  LEU A 167      -1.570  41.236  30.235  1.00 93.67           C  
ANISOU  228  CG  LEU A 167    12035  12590  10964    144    453   -319       C  
ATOM    229  CD1 LEU A 167      -2.139  41.668  31.570  1.00 89.91           C  
ANISOU  229  CD1 LEU A 167    11570  12130  10462    171    443   -306       C  
ATOM    230  CD2 LEU A 167      -2.465  40.180  29.604  1.00 98.28           C  
ANISOU  230  CD2 LEU A 167    12589  13222  11531     99    475   -333       C  
ATOM    231  N   GLY A 168      -0.106  44.439  27.141  1.00109.35           N  
ANISOU  231  N   GLY A 168    13988  14586  12975    226    406   -300       N  
ATOM    232  CA  GLY A 168      -0.309  45.683  26.410  1.00100.16           C  
ANISOU  232  CA  GLY A 168    12800  13457  11799    254    384   -290       C  
ATOM    233  C   GLY A 168      -0.279  45.489  24.897  1.00103.90           C  
ANISOU  233  C   GLY A 168    13237  13967  12273    229    400   -299       C  
ATOM    234  O   GLY A 168      -1.208  45.875  24.198  1.00116.56           O  
ANISOU  234  O   GLY A 168    14809  15630  13848    224    407   -309       O  
ATOM    235  N   PHE A 169       0.803  44.888  24.399  1.00105.94           N  
ANISOU  235  N   PHE A 169    13500  14190  12562    213    406   -297       N  
ATOM    236  CA  PHE A 169       0.976  44.683  22.973  1.00 96.40           C  
ANISOU  236  CA  PHE A 169    12256  13018  11354    193    418   -306       C  
ATOM    237  C   PHE A 169       0.195  43.456  22.512  1.00 93.77           C  
ANISOU  237  C   PHE A 169    11906  12718  11002    154    456   -339       C  
ATOM    238  O   PHE A 169       0.384  42.359  23.037  1.00 79.37           O  
ANISOU  238  O   PHE A 169    10103  10862   9191    133    468   -352       O  
ATOM    239  CB  PHE A 169       2.455  44.502  22.669  1.00105.82           C  
ANISOU  239  CB  PHE A 169    13458  14164  12583    195    407   -291       C  
ATOM    240  CG  PHE A 169       3.319  45.665  23.071  1.00112.15           C  
ANISOU  240  CG  PHE A 169    14276  14927  13408    234    364   -252       C  
ATOM    241  CD1 PHE A 169       3.357  46.815  22.294  1.00118.21           C  
ANISOU  241  CD1 PHE A 169    15011  15731  14173    254    336   -228       C  
ATOM    242  CD2 PHE A 169       4.120  45.593  24.199  1.00125.68           C  
ANISOU  242  CD2 PHE A 169    16036  16566  15150    250    349   -236       C  
ATOM    243  CE1 PHE A 169       4.180  47.877  22.639  1.00133.84           C  
ANISOU  243  CE1 PHE A 169    17003  17673  16178    291    288   -186       C  
ATOM    244  CE2 PHE A 169       4.932  46.662  24.550  1.00141.71           C  
ANISOU  244  CE2 PHE A 169    18083  18556  17206    289    305   -196       C  
ATOM    245  CZ  PHE A 169       4.955  47.803  23.774  1.00137.58           C  
ANISOU  245  CZ  PHE A 169    17526  18069  16680    311    272   -170       C  
ATOM    246  N   ARG A 170      -0.650  43.658  21.493  1.00 93.36           N  
ANISOU  246  N   ARG A 170    11817  12729  10926    145    470   -350       N  
ATOM    247  CA  ARG A 170      -1.588  42.641  21.043  1.00 88.85           C  
ANISOU  247  CA  ARG A 170    11230  12193  10336    113    501   -378       C  
ATOM    248  C   ARG A 170      -0.829  41.453  20.453  1.00 88.90           C  
ANISOU  248  C   ARG A 170    11232  12181  10364     90    511   -397       C  
ATOM    249  O   ARG A 170      -1.266  40.313  20.568  1.00 80.12           O  
ANISOU  249  O   ARG A 170    10122  11067   9252     65    525   -417       O  
ATOM    250  CB  ARG A 170      -2.635  43.225  20.084  1.00 82.09           C  
ANISOU  250  CB  ARG A 170    10338  11403   9450    110    512   -384       C  
ATOM    251  N   HIS A 171       0.323  41.721  19.824  1.00 95.63           N  
ANISOU  251  N   HIS A 171    12076  13021  11238    101    499   -389       N  
ATOM    252  CA  HIS A 171       1.053  40.691  19.097  1.00 96.07           C  
ANISOU  252  CA  HIS A 171    12121  13071  11311     85    506   -411       C  
ATOM    253  C   HIS A 171       1.649  39.652  20.037  1.00 93.77           C  
ANISOU  253  C   HIS A 171    11865  12716  11046     70    501   -422       C  
ATOM    254  O   HIS A 171       2.040  38.573  19.594  1.00102.55           O  
ANISOU  254  O   HIS A 171    12970  13821  12173     52    503   -449       O  
ATOM    255  CB  HIS A 171       2.097  41.325  18.176  1.00106.95           C  
ANISOU  255  CB  HIS A 171    13476  14462  12699    102    493   -396       C  
ATOM    256  CG  HIS A 171       1.448  42.078  17.070  1.00120.56           C  
ANISOU  256  CG  HIS A 171    15155  16256  14398    106    499   -392       C  
ATOM    257  ND1 HIS A 171       0.853  43.313  17.261  1.00132.08           N  
ANISOU  257  ND1 HIS A 171    16608  17734  15843    120    487   -368       N  
ATOM    258  CD2 HIS A 171       1.237  41.750  15.784  1.00125.48           C  
ANISOU  258  CD2 HIS A 171    15736  16933  15008     97    514   -412       C  
ATOM    259  CE1 HIS A 171       0.322  43.721  16.126  1.00122.10           C  
ANISOU  259  CE1 HIS A 171    15300  16531  14560    115    495   -372       C  
ATOM    260  NE2 HIS A 171       0.546  42.783  15.211  1.00119.17           N  
ANISOU  260  NE2 HIS A 171    14907  16183  14189    101    513   -398       N  
ATOM    261  N   LEU A 172       1.698  39.984  21.330  1.00 96.77           N  
ANISOU  261  N   LEU A 172    12282  13052  11435     78    491   -402       N  
ATOM    262  CA  LEU A 172       2.318  39.114  22.316  1.00100.29           C  
ANISOU  262  CA  LEU A 172    12762  13433  11909     62    484   -408       C  
ATOM    263  C   LEU A 172       1.294  38.149  22.927  1.00 85.01           C  
ANISOU  263  C   LEU A 172    10831  11506   9965     33    493   -424       C  
ATOM    264  O   LEU A 172       1.637  37.371  23.802  1.00 88.32           O  
ANISOU  264  O   LEU A 172    11274  11876  10407     13    484   -428       O  
ATOM    265  CB  LEU A 172       2.978  39.994  23.385  1.00107.79           C  
ANISOU  265  CB  LEU A 172    13749  14330  12875     88    466   -375       C  
ATOM    266  CG  LEU A 172       4.086  40.949  22.926  1.00104.49           C  
ANISOU  266  CG  LEU A 172    13332  13896  12473    118    448   -349       C  
ATOM    267  CD1 LEU A 172       4.528  41.829  24.090  1.00119.35           C  
ANISOU  267  CD1 LEU A 172    15253  15725  14371    147    425   -316       C  
ATOM    268  CD2 LEU A 172       5.284  40.191  22.380  1.00100.38           C  
ANISOU  268  CD2 LEU A 172    12813  13346  11982    105    446   -362       C  
ATOM    269  N   HIS A 173       0.042  38.190  22.465  1.00 72.35           N  
ANISOU  269  N   HIS A 173     9201   9962   8329     28    507   -430       N  
ATOM    270  CA  HIS A 173      -1.006  37.366  23.037  1.00 69.90           C  
ANISOU  270  CA  HIS A 173     8890   9665   8006      3    512   -436       C  
ATOM    271  C   HIS A 173      -0.939  35.959  22.455  1.00 71.16           C  
ANISOU  271  C   HIS A 173     9033   9820   8184    -29    507   -465       C  
ATOM    272  O   HIS A 173      -1.669  35.633  21.525  1.00 94.71           O  
ANISOU  272  O   HIS A 173    11987  12847  11150    -36    516   -480       O  
ATOM    273  CB  HIS A 173      -2.391  37.967  22.757  1.00 73.96           C  
ANISOU  273  CB  HIS A 173     9382  10242   8477     11    527   -429       C  
ATOM    274  CG  HIS A 173      -2.707  39.177  23.562  1.00 83.99           C  
ANISOU  274  CG  HIS A 173    10667  11520   9726     40    524   -405       C  
ATOM    275  ND1 HIS A 173      -1.899  40.298  23.561  1.00 98.40           N  
ANISOU  275  ND1 HIS A 173    12502  13326  11561     72    511   -391       N  
ATOM    276  CD2 HIS A 173      -3.746  39.455  24.372  1.00 89.31           C  
ANISOU  276  CD2 HIS A 173    11343  12220  10369     45    527   -393       C  
ATOM    277  CE1 HIS A 173      -2.406  41.196  24.377  1.00 92.71           C  
ANISOU  277  CE1 HIS A 173    11791  12614  10819     96    503   -374       C  
ATOM    278  NE2 HIS A 173      -3.544  40.708  24.877  1.00 91.20           N  
ANISOU  278  NE2 HIS A 173    11596  12455  10601     81    515   -377       N  
ATOM    279  N   CYS A 174      -0.078  35.123  23.026  1.00 63.13           N  
ANISOU  279  N   CYS A 174     8036   8747   7203    -48    490   -474       N  
ATOM    280  CA  CYS A 174       0.002  33.734  22.620  1.00 60.48           C  
ANISOU  280  CA  CYS A 174     7686   8402   6891    -79    474   -503       C  
ATOM    281  C   CYS A 174       0.163  32.881  23.874  1.00 63.65           C  
ANISOU  281  C   CYS A 174     8109   8753   7319   -110    453   -498       C  
ATOM    282  O   CYS A 174       0.548  33.406  24.937  1.00 53.05           O  
ANISOU  282  O   CYS A 174     6797   7376   5983   -104    454   -476       O  
ATOM    283  CB  CYS A 174       1.155  33.511  21.644  1.00 69.84           C  
ANISOU  283  CB  CYS A 174     8864   9574   8099    -71    467   -529       C  
ATOM    284  SG  CYS A 174       2.785  34.071  22.214  1.00 83.07           S  
ANISOU  284  SG  CYS A 174    10575  11182   9805    -56    460   -517       S  
ATOM    285  N   THR A 175      -0.124  31.578  23.710  1.00 65.72           N  
ANISOU  285  N   THR A 175     8356   9014   7601   -143    431   -519       N  
ATOM    286  CA  THR A 175      -0.106  30.603  24.794  1.00 78.17           C  
ANISOU  286  CA  THR A 175     9943  10551   9207   -182    403   -514       C  
ATOM    287  C   THR A 175       1.234  30.654  25.552  1.00 82.64           C  
ANISOU  287  C   THR A 175    10545  11045   9810   -188    394   -516       C  
ATOM    288  O   THR A 175       1.256  30.548  26.782  1.00 89.05           O  
ANISOU  288  O   THR A 175    11377  11825  10634   -206    386   -495       O  
ATOM    289  CB  THR A 175      -0.522  29.205  24.296  1.00 72.11           C  
ANISOU  289  CB  THR A 175     9147   9791   8460   -214    369   -538       C  
ATOM    290  OG1 THR A 175       0.575  28.725  23.530  1.00101.84           O  
ANISOU  290  OG1 THR A 175    12911  13527  12257   -212    352   -577       O  
ATOM    291  CG2 THR A 175      -1.731  29.191  23.386  1.00 68.58           C  
ANISOU  291  CG2 THR A 175     8668   9408   7980   -204    379   -538       C  
ATOM    292  N   ARG A 176       2.357  30.830  24.832  1.00 76.18           N  
ANISOU  292  N   ARG A 176     9734  10203   9010   -171    395   -537       N  
ATOM    293  CA  ARG A 176       3.655  30.893  25.482  1.00 74.82           C  
ANISOU  293  CA  ARG A 176     9596   9958   8873   -175    387   -537       C  
ATOM    294  C   ARG A 176       3.726  32.047  26.486  1.00 82.62           C  
ANISOU  294  C   ARG A 176    10616  10927   9848   -152    406   -498       C  
ATOM    295  O   ARG A 176       4.273  31.880  27.584  1.00 91.45           O  
ANISOU  295  O   ARG A 176    11765  11986  10994   -169    396   -487       O  
ATOM    296  CB  ARG A 176       4.793  30.960  24.468  1.00 75.21           C  
ANISOU  296  CB  ARG A 176     9644   9996   8938   -157    386   -562       C  
ATOM    297  CG  ARG A 176       6.145  31.256  25.108  1.00 82.77           C  
ANISOU  297  CG  ARG A 176    10642  10878   9927   -155    383   -553       C  
ATOM    298  CD  ARG A 176       7.285  31.362  24.100  1.00 74.57           C  
ANISOU  298  CD  ARG A 176     9599   9834   8899   -135    381   -572       C  
ATOM    299  NE  ARG A 176       6.832  32.085  22.923  1.00 74.02           N  
ANISOU  299  NE  ARG A 176     9495   9839   8789    -99    400   -569       N  
ATOM    300  CZ  ARG A 176       6.885  33.405  22.800  1.00 83.09           C  
ANISOU  300  CZ  ARG A 176    10648  11007   9914    -63    420   -534       C  
ATOM    301  NH1 ARG A 176       7.415  34.138  23.777  1.00 89.95           N  
ANISOU  301  NH1 ARG A 176    11556  11823  10796    -52    421   -500       N  
ATOM    302  NH2 ARG A 176       6.433  33.976  21.692  1.00 72.65           N  
ANISOU  302  NH2 ARG A 176     9290   9755   8557    -38    433   -533       N  
ATOM    303  N   ASN A 177       3.164  33.208  26.121  1.00 78.36           N  
ANISOU  303  N   ASN A 177    10068  10436   9267   -114    430   -478       N  
ATOM    304  CA  ASN A 177       3.209  34.367  27.001  1.00 78.47           C  
ANISOU  304  CA  ASN A 177    10109  10437   9269    -84    440   -444       C  
ATOM    305  C   ASN A 177       2.161  34.272  28.109  1.00 75.13           C  
ANISOU  305  C   ASN A 177     9688  10033   8827    -96    440   -425       C  
ATOM    306  O   ASN A 177       2.344  34.851  29.181  1.00 72.02           O  
ANISOU  306  O   ASN A 177     9320   9609   8433    -81    440   -402       O  
ATOM    307  CB  ASN A 177       3.139  35.686  26.231  1.00 76.97           C  
ANISOU  307  CB  ASN A 177     9909  10286   9049    -38    454   -430       C  
ATOM    308  CG  ASN A 177       4.384  35.954  25.411  1.00 72.20           C  
ANISOU  308  CG  ASN A 177     9309   9657   8467    -22    450   -435       C  
ATOM    309  OD1 ASN A 177       5.465  35.511  25.779  1.00 75.16           O  
ANISOU  309  OD1 ASN A 177     9710   9968   8880    -35    439   -440       O  
ATOM    310  ND2 ASN A 177       4.258  36.706  24.326  1.00 74.27           N  
ANISOU  310  ND2 ASN A 177     9545   9970   8706      4    459   -432       N  
ATOM    311  N   TYR A 178       1.060  33.558  27.846  1.00 74.20           N  
ANISOU  311  N   TYR A 178     9539   9966   8690   -120    439   -432       N  
ATOM    312  CA  TYR A 178       0.029  33.393  28.863  1.00 69.97           C  
ANISOU  312  CA  TYR A 178     8997   9457   8131   -133    438   -411       C  
ATOM    313  C   TYR A 178       0.564  32.545  30.009  1.00 68.12           C  
ANISOU  313  C   TYR A 178     8782   9166   7936   -170    416   -406       C  
ATOM    314  O   TYR A 178       0.248  32.817  31.175  1.00 68.33           O  
ANISOU  314  O   TYR A 178     8819   9193   7951   -168    417   -382       O  
ATOM    315  CB  TYR A 178      -1.248  32.781  28.285  1.00 75.43           C  
ANISOU  315  CB  TYR A 178     9650  10214   8797   -151    438   -414       C  
ATOM    316  CG  TYR A 178      -2.014  33.668  27.341  1.00 84.99           C  
ANISOU  316  CG  TYR A 178    10842  11485   9964   -118    462   -414       C  
ATOM    317  CD1 TYR A 178      -2.348  34.971  27.690  1.00 87.99           C  
ANISOU  317  CD1 TYR A 178    11232  11890  10310    -79    478   -394       C  
ATOM    318  CD2 TYR A 178      -2.382  33.209  26.084  1.00 91.52           C  
ANISOU  318  CD2 TYR A 178    11642  12344  10788   -125    464   -435       C  
ATOM    319  CE1 TYR A 178      -3.037  35.796  26.816  1.00 82.81           C  
ANISOU  319  CE1 TYR A 178    10558  11288   9620    -53    496   -396       C  
ATOM    320  CE2 TYR A 178      -3.073  34.024  25.194  1.00 91.98           C  
ANISOU  320  CE2 TYR A 178    11682  12455  10810    -99    486   -435       C  
ATOM    321  CZ  TYR A 178      -3.427  35.311  25.581  1.00 87.09           C  
ANISOU  321  CZ  TYR A 178    11072  11860  10158    -65    502   -414       C  
ATOM    322  OH  TYR A 178      -4.136  36.142  24.767  1.00 87.20           O  
ANISOU  322  OH  TYR A 178    11068  11926  10139    -43    520   -414       O  
ATOM    323  N   ILE A 179       1.379  31.535  29.658  1.00 66.98           N  
ANISOU  323  N   ILE A 179     8638   8974   7836   -204    396   -432       N  
ATOM    324  CA  ILE A 179       2.013  30.693  30.665  1.00 70.10           C  
ANISOU  324  CA  ILE A 179     9051   9307   8276   -245    371   -432       C  
ATOM    325  C   ILE A 179       2.976  31.520  31.512  1.00 64.10           C  
ANISOU  325  C   ILE A 179     8336   8487   7532   -223    381   -417       C  
ATOM    326  O   ILE A 179       3.015  31.327  32.725  1.00 57.72           O  
ANISOU  326  O   ILE A 179     7542   7650   6737   -242    373   -399       O  
ATOM    327  CB  ILE A 179       2.655  29.440  30.047  1.00 68.24           C  
ANISOU  327  CB  ILE A 179     8806   9036   8088   -285    341   -468       C  
ATOM    328  CG1 ILE A 179       1.556  28.553  29.452  1.00 64.86           C  
ANISOU  328  CG1 ILE A 179     8332   8664   7646   -309    321   -477       C  
ATOM    329  CG2 ILE A 179       3.477  28.693  31.092  1.00 64.49           C  
ANISOU  329  CG2 ILE A 179     8354   8486   7664   -329    314   -470       C  
ATOM    330  CD1 ILE A 179       2.087  27.433  28.589  1.00 67.84           C  
ANISOU  330  CD1 ILE A 179     8695   9019   8064   -335    287   -518       C  
ATOM    331  N   HIS A 180       3.678  32.468  30.872  1.00 63.19           N  
ANISOU  331  N   HIS A 180     8239   8358   7414   -180    397   -420       N  
ATOM    332  CA  HIS A 180       4.563  33.395  31.561  1.00 69.35           C  
ANISOU  332  CA  HIS A 180     9061   9082   8207   -149    403   -400       C  
ATOM    333  C   HIS A 180       3.785  34.249  32.559  1.00 74.66           C  
ANISOU  333  C   HIS A 180     9739   9783   8844   -119    412   -369       C  
ATOM    334  O   HIS A 180       4.238  34.415  33.694  1.00 79.87           O  
ANISOU  334  O   HIS A 180    10430  10393   9523   -118    407   -353       O  
ATOM    335  CB  HIS A 180       5.333  34.291  30.581  1.00 74.34           C  
ANISOU  335  CB  HIS A 180     9702   9706   8839   -107    412   -401       C  
ATOM    336  CG  HIS A 180       6.335  33.560  29.754  1.00 78.50           C  
ANISOU  336  CG  HIS A 180    10228  10196   9401   -128    403   -430       C  
ATOM    337  ND1 HIS A 180       6.411  32.182  29.758  1.00 86.18           N  
ANISOU  337  ND1 HIS A 180    11191  11152  10403   -180    384   -459       N  
ATOM    338  CD2 HIS A 180       7.264  33.999  28.877  1.00 70.63           C  
ANISOU  338  CD2 HIS A 180     9238   9186   8414   -104    405   -434       C  
ATOM    339  CE1 HIS A 180       7.340  31.796  28.912  1.00 90.40           C  
ANISOU  339  CE1 HIS A 180    11724  11661  10962   -185    376   -485       C  
ATOM    340  NE2 HIS A 180       7.882  32.897  28.359  1.00 86.36           N  
ANISOU  340  NE2 HIS A 180    11223  11155  10437   -138    391   -469       N  
ATOM    341  N   LEU A 181       2.624  34.770  32.128  1.00 65.18           N  
ANISOU  341  N   LEU A 181     8509   8664   7593    -96    424   -363       N  
ATOM    342  CA  LEU A 181       1.827  35.660  32.961  1.00 63.53           C  
ANISOU  342  CA  LEU A 181     8300   8493   7344    -61    430   -338       C  
ATOM    343  C   LEU A 181       1.380  34.965  34.252  1.00 73.01           C  
ANISOU  343  C   LEU A 181     9500   9695   8546    -92    422   -325       C  
ATOM    344  O   LEU A 181       1.346  35.619  35.303  1.00 60.23           O  
ANISOU  344  O   LEU A 181     7899   8070   6916    -64    421   -305       O  
ATOM    345  CB  LEU A 181       0.623  36.173  32.177  1.00 57.73           C  
ANISOU  345  CB  LEU A 181     7532   7847   6558    -39    443   -339       C  
ATOM    346  CG  LEU A 181       0.935  37.253  31.152  1.00 59.81           C  
ANISOU  346  CG  LEU A 181     7795   8119   6812      3    450   -342       C  
ATOM    347  CD1 LEU A 181      -0.220  37.438  30.172  1.00 59.30           C  
ANISOU  347  CD1 LEU A 181     7692   8136   6704      8    463   -350       C  
ATOM    348  CD2 LEU A 181       1.292  38.560  31.838  1.00 58.43           C  
ANISOU  348  CD2 LEU A 181     7647   7923   6632     56    441   -321       C  
ATOM    349  N   ASN A 182       1.054  33.657  34.170  1.00 69.63           N  
ANISOU  349  N   ASN A 182     9048   9277   8133   -149    411   -334       N  
ATOM    350  CA  ASN A 182       0.704  32.890  35.361  1.00 69.51           C  
ANISOU  350  CA  ASN A 182     9025   9262   8125   -188    396   -318       C  
ATOM    351  C   ASN A 182       1.923  32.629  36.240  1.00 67.99           C  
ANISOU  351  C   ASN A 182     8870   8978   7984   -207    385   -317       C  
ATOM    352  O   ASN A 182       1.792  32.624  37.466  1.00 65.68           O  
ANISOU  352  O   ASN A 182     8585   8681   7691   -213    380   -296       O  
ATOM    353  CB  ASN A 182       0.029  31.561  35.050  1.00 77.32           C  
ANISOU  353  CB  ASN A 182     9975  10285   9121   -245    377   -323       C  
ATOM    354  CG  ASN A 182      -1.361  31.729  34.484  1.00 86.92           C  
ANISOU  354  CG  ASN A 182    11152  11593  10282   -231    388   -314       C  
ATOM    355  OD1 ASN A 182      -2.347  31.453  35.175  1.00 75.69           O  
ANISOU  355  OD1 ASN A 182     9704  10225   8830   -245    382   -288       O  
ATOM    356  ND2 ASN A 182      -1.432  32.190  33.240  1.00 95.97           N  
ANISOU  356  ND2 ASN A 182    12294  12757  11414   -204    403   -333       N  
ATOM    357  N   LEU A 183       3.094  32.422  35.613  1.00 59.27           N  
ANISOU  357  N   LEU A 183     7790   7803   6925   -216    380   -340       N  
ATOM    358  CA  LEU A 183       4.321  32.258  36.375  1.00 54.87           C  
ANISOU  358  CA  LEU A 183     7274   7151   6421   -232    371   -340       C  
ATOM    359  C   LEU A 183       4.690  33.580  37.061  1.00 65.17           C  
ANISOU  359  C   LEU A 183     8617   8431   7714   -172    384   -317       C  
ATOM    360  O   LEU A 183       5.129  33.569  38.210  1.00 69.38           O  
ANISOU  360  O   LEU A 183     9176   8913   8270   -179    378   -303       O  
ATOM    361  CB  LEU A 183       5.425  31.744  35.449  1.00 48.50           C  
ANISOU  361  CB  LEU A 183     6482   6286   5661   -252    363   -370       C  
ATOM    362  CG  LEU A 183       6.826  31.620  36.056  1.00 46.82           C  
ANISOU  362  CG  LEU A 183     6318   5967   5506   -267    356   -372       C  
ATOM    363  CD1 LEU A 183       6.967  30.417  36.957  1.00 42.42           C  
ANISOU  363  CD1 LEU A 183     5759   5369   4990   -335    331   -377       C  
ATOM    364  CD2 LEU A 183       7.886  31.580  34.966  1.00 49.24           C  
ANISOU  364  CD2 LEU A 183     6638   6230   5839   -261    355   -397       C  
ATOM    365  N   PHE A 184       4.481  34.719  36.377  1.00 60.79           N  
ANISOU  365  N   PHE A 184     8061   7911   7124   -113    397   -313       N  
ATOM    366  CA  PHE A 184       4.770  36.010  36.973  1.00 58.56           C  
ANISOU  366  CA  PHE A 184     7811   7608   6832    -52    399   -291       C  
ATOM    367  C   PHE A 184       3.841  36.258  38.149  1.00 58.39           C  
ANISOU  367  C   PHE A 184     7778   7633   6774    -37    398   -272       C  
ATOM    368  O   PHE A 184       4.259  36.783  39.164  1.00 65.55           O  
ANISOU  368  O   PHE A 184     8716   8499   7692     -9    392   -256       O  
ATOM    369  CB  PHE A 184       4.556  37.141  35.972  1.00 66.17           C  
ANISOU  369  CB  PHE A 184     8765   8612   7764      3    404   -289       C  
ATOM    370  CG  PHE A 184       5.464  37.093  34.771  1.00 71.84           C  
ANISOU  370  CG  PHE A 184     9489   9297   8510     -1    405   -303       C  
ATOM    371  CD1 PHE A 184       6.668  36.393  34.811  1.00 71.68           C  
ANISOU  371  CD1 PHE A 184     9497   9194   8545    -34    399   -312       C  
ATOM    372  CD2 PHE A 184       5.114  37.761  33.609  1.00 64.66           C  
ANISOU  372  CD2 PHE A 184     8555   8442   7572     28    410   -306       C  
ATOM    373  CE1 PHE A 184       7.510  36.368  33.710  1.00 68.91           C  
ANISOU  373  CE1 PHE A 184     9148   8820   8214    -34    398   -323       C  
ATOM    374  CE2 PHE A 184       5.953  37.733  32.511  1.00 64.82           C  
ANISOU  374  CE2 PHE A 184     8576   8440   7614     27    410   -316       C  
ATOM    375  CZ  PHE A 184       7.151  37.049  32.567  1.00 67.68           C  
ANISOU  375  CZ  PHE A 184     8964   8724   8026     -2    404   -324       C  
ATOM    376  N   ALA A 185       2.570  35.890  38.002  1.00 64.58           N  
ANISOU  376  N   ALA A 185     8517   8507   7513    -53    403   -273       N  
ATOM    377  CA  ALA A 185       1.595  36.134  39.058  1.00 69.81           C  
ANISOU  377  CA  ALA A 185     9161   9230   8132    -36    402   -254       C  
ATOM    378  C   ALA A 185       2.003  35.419  40.339  1.00 64.76           C  
ANISOU  378  C   ALA A 185     8535   8546   7524    -73    392   -242       C  
ATOM    379  O   ALA A 185       1.859  35.989  41.416  1.00 65.24           O  
ANISOU  379  O   ALA A 185     8606   8615   7567    -39    389   -225       O  
ATOM    380  CB  ALA A 185       0.202  35.728  38.625  1.00 71.54           C  
ANISOU  380  CB  ALA A 185     9329   9550   8302    -54    409   -254       C  
ATOM    381  N   SER A 186       2.501  34.182  40.201  1.00 65.97           N  
ANISOU  381  N   SER A 186     8687   8655   7726   -142    383   -252       N  
ATOM    382  CA  SER A 186       2.924  33.397  41.350  1.00 67.74           C  
ANISOU  382  CA  SER A 186     8920   8832   7987   -189    370   -242       C  
ATOM    383  C   SER A 186       4.121  34.061  42.048  1.00 65.08           C  
ANISOU  383  C   SER A 186     8640   8400   7688   -158    371   -238       C  
ATOM    384  O   SER A 186       4.235  33.973  43.270  1.00 56.77           O  
ANISOU  384  O   SER A 186     7598   7328   6646   -165    365   -221       O  
ATOM    385  CB  SER A 186       3.192  31.963  40.985  1.00 56.52           C  
ANISOU  385  CB  SER A 186     7481   7382   6611   -269    352   -257       C  
ATOM    386  OG  SER A 186       4.292  31.891  40.097  1.00 68.91           O  
ANISOU  386  OG  SER A 186     9081   8876   8224   -274    353   -283       O  
ATOM    387  N   PHE A 187       5.000  34.725  41.278  1.00 59.84           N  
ANISOU  387  N   PHE A 187     8012   7679   7046   -123    376   -249       N  
ATOM    388  CA  PHE A 187       6.074  35.536  41.850  1.00 66.24           C  
ANISOU  388  CA  PHE A 187     8877   8401   7888    -82    373   -238       C  
ATOM    389  C   PHE A 187       5.550  36.859  42.439  1.00 70.90           C  
ANISOU  389  C   PHE A 187     9472   9033   8432     -1    372   -219       C  
ATOM    390  O   PHE A 187       6.053  37.329  43.462  1.00 67.93           O  
ANISOU  390  O   PHE A 187     9131   8605   8074     28    365   -204       O  
ATOM    391  CB  PHE A 187       7.226  35.737  40.858  1.00 54.27           C  
ANISOU  391  CB  PHE A 187     7395   6812   6414    -75    374   -249       C  
ATOM    392  CG  PHE A 187       8.134  34.544  40.722  1.00 54.17           C  
ANISOU  392  CG  PHE A 187     7396   6725   6461   -146    368   -267       C  
ATOM    393  CD1 PHE A 187       9.131  34.294  41.655  1.00 56.95           C  
ANISOU  393  CD1 PHE A 187     7792   6978   6867   -167    362   -260       C  
ATOM    394  CD2 PHE A 187       7.963  33.635  39.689  1.00 59.38           C  
ANISOU  394  CD2 PHE A 187     8024   7413   7125   -192    366   -293       C  
ATOM    395  CE1 PHE A 187       9.982  33.200  41.550  1.00 48.27           C  
ANISOU  395  CE1 PHE A 187     6708   5808   5826   -235    353   -280       C  
ATOM    396  CE2 PHE A 187       8.791  32.526  39.586  1.00 53.83           C  
ANISOU  396  CE2 PHE A 187     7332   6643   6478   -255    354   -315       C  
ATOM    397  CZ  PHE A 187       9.791  32.310  40.520  1.00 53.42           C  
ANISOU  397  CZ  PHE A 187     7325   6493   6481   -278    347   -309       C  
ATOM    398  N   ILE A 188       4.550  37.469  41.782  1.00 67.08           N  
ANISOU  398  N   ILE A 188     8954   8640   7892     36    377   -222       N  
ATOM    399  CA  ILE A 188       3.987  38.723  42.256  1.00 69.24           C  
ANISOU  399  CA  ILE A 188     9227   8959   8120    113    369   -209       C  
ATOM    400  C   ILE A 188       3.279  38.504  43.593  1.00 71.31           C  
ANISOU  400  C   ILE A 188     9473   9269   8354    112    367   -197       C  
ATOM    401  O   ILE A 188       3.491  39.273  44.526  1.00 67.73           O  
ANISOU  401  O   ILE A 188     9042   8794   7896    166    355   -186       O  
ATOM    402  CB  ILE A 188       3.055  39.372  41.218  1.00 72.53           C  
ANISOU  402  CB  ILE A 188     9610   9463   8485    146    373   -218       C  
ATOM    403  CG1 ILE A 188       3.867  39.927  40.045  1.00 77.19           C  
ANISOU  403  CG1 ILE A 188    10220  10007   9103    165    369   -223       C  
ATOM    404  CG2 ILE A 188       2.222  40.467  41.885  1.00 67.71           C  
ANISOU  404  CG2 ILE A 188     8989   8918   7821    216    361   -210       C  
ATOM    405  CD1 ILE A 188       3.033  40.425  38.882  1.00 73.80           C  
ANISOU  405  CD1 ILE A 188     9755   9657   8630    183    374   -233       C  
ATOM    406  N   LEU A 189       2.432  37.468  43.669  1.00 71.62           N  
ANISOU  406  N   LEU A 189     9468   9374   8372     54    375   -197       N  
ATOM    407  CA  LEU A 189       1.748  37.108  44.905  1.00 71.89           C  
ANISOU  407  CA  LEU A 189     9476   9461   8377     43    372   -181       C  
ATOM    408  C   LEU A 189       2.746  36.770  46.014  1.00 72.82           C  
ANISOU  408  C   LEU A 189     9631   9490   8548     23    364   -171       C  
ATOM    409  O   LEU A 189       2.497  37.059  47.179  1.00 66.07           O  
ANISOU  409  O   LEU A 189     8773   8659   7673     50    358   -157       O  
ATOM    410  CB  LEU A 189       0.842  35.903  44.661  1.00 70.44           C  
ANISOU  410  CB  LEU A 189     9239   9349   8175    -27    375   -177       C  
ATOM    411  CG  LEU A 189      -0.645  36.206  44.526  1.00 77.18           C  
ANISOU  411  CG  LEU A 189    10043  10331   8952     -2    380   -169       C  
ATOM    412  CD1 LEU A 189      -0.919  36.933  43.210  1.00 87.71           C  
ANISOU  412  CD1 LEU A 189    11376  11686  10263     35    389   -187       C  
ATOM    413  CD2 LEU A 189      -1.457  34.911  44.615  1.00 79.74           C  
ANISOU  413  CD2 LEU A 189    10315  10717   9265    -75    376   -154       C  
ATOM    414  N   ARG A 190       3.851  36.104  45.666  1.00 73.85           N  
ANISOU  414  N   ARG A 190     9792   9520   8746    -28    364   -180       N  
ATOM    415  CA  ARG A 190       4.849  35.761  46.664  1.00 68.93           C  
ANISOU  415  CA  ARG A 190     9208   8803   8179    -53    357   -172       C  
ATOM    416  C   ARG A 190       5.406  37.052  47.252  1.00 72.85           C  
ANISOU  416  C   ARG A 190     9751   9250   8678     32    352   -163       C  
ATOM    417  O   ARG A 190       5.613  37.129  48.462  1.00 72.33           O  
ANISOU  417  O   ARG A 190     9701   9160   8622     43    346   -150       O  
ATOM    418  CB  ARG A 190       5.949  34.895  46.045  1.00 79.15           C  
ANISOU  418  CB  ARG A 190    10530   9999   9545   -118    356   -188       C  
ATOM    419  CG  ARG A 190       7.110  34.542  46.963  1.00 74.79           C  
ANISOU  419  CG  ARG A 190    10025   9333   9060   -148    351   -183       C  
ATOM    420  CD  ARG A 190       8.143  33.696  46.248  1.00 84.19           C  
ANISOU  420  CD  ARG A 190    11239  10434  10316   -211    348   -203       C  
ATOM    421  NE  ARG A 190       9.198  33.252  47.141  1.00 96.45           N  
ANISOU  421  NE  ARG A 190    12835  11878  11935   -250    342   -199       N  
ATOM    422  CZ  ARG A 190      10.142  32.360  46.841  1.00102.31           C  
ANISOU  422  CZ  ARG A 190    13598  12533  12741   -316    334   -217       C  
ATOM    423  NH1 ARG A 190      10.172  31.763  45.658  1.00 93.84           N  
ANISOU  423  NH1 ARG A 190    12506  11474  11676   -349    330   -242       N  
ATOM    424  NH2 ARG A 190      11.059  32.053  47.739  1.00111.51           N  
ANISOU  424  NH2 ARG A 190    14805  13599  13965   -348    330   -212       N  
ATOM    425  N   ALA A 191       5.663  38.050  46.391  1.00 77.61           N  
ANISOU  425  N   ALA A 191    10375   9838   9274     91    349   -169       N  
ATOM    426  CA  ALA A 191       6.201  39.332  46.839  1.00 76.74           C  
ANISOU  426  CA  ALA A 191    10308   9679   9171    176    333   -158       C  
ATOM    427  C   ALA A 191       5.183  40.042  47.724  1.00 71.79           C  
ANISOU  427  C   ALA A 191     9655   9142   8481    238    323   -151       C  
ATOM    428  O   ALA A 191       5.557  40.578  48.757  1.00 74.24           O  
ANISOU  428  O   ALA A 191     9993   9412   8802    284    308   -140       O  
ATOM    429  CB  ALA A 191       6.652  40.190  45.675  1.00 76.74           C  
ANISOU  429  CB  ALA A 191    10328   9652   9179    219    325   -161       C  
ATOM    430  N   LEU A 192       3.899  39.985  47.338  1.00 81.23           N  
ANISOU  430  N   LEU A 192    10794  10458   9611    237    330   -158       N  
ATOM    431  CA  LEU A 192       2.811  40.556  48.127  1.00 78.68           C  
ANISOU  431  CA  LEU A 192    10437  10237   9221    291    321   -154       C  
ATOM    432  C   LEU A 192       2.782  39.948  49.537  1.00 76.91           C  
ANISOU  432  C   LEU A 192    10207  10017   8999    267    322   -140       C  
ATOM    433  O   LEU A 192       2.481  40.662  50.481  1.00 77.53           O  
ANISOU  433  O   LEU A 192    10284  10130   9046    332    307   -135       O  
ATOM    434  CB  LEU A 192       1.457  40.379  47.420  1.00 72.73           C  
ANISOU  434  CB  LEU A 192     9625   9608   8403    278    333   -162       C  
ATOM    435  CG  LEU A 192       1.227  41.110  46.097  1.00 79.45           C  
ANISOU  435  CG  LEU A 192    10472  10479   9237    309    331   -176       C  
ATOM    436  CD1 LEU A 192      -0.089  40.671  45.471  1.00 72.06           C  
ANISOU  436  CD1 LEU A 192     9478   9656   8244    279    347   -181       C  
ATOM    437  CD2 LEU A 192       1.254  42.622  46.264  1.00 86.43           C  
ANISOU  437  CD2 LEU A 192    11374  11363  10101    408    302   -180       C  
ATOM    438  N   SER A 193       3.109  38.654  49.691  1.00 71.44           N  
ANISOU  438  N   SER A 193     9507   9290   8345    176    335   -135       N  
ATOM    439  CA  SER A 193       3.183  38.018  50.996  1.00 68.88           C  
ANISOU  439  CA  SER A 193     9176   8962   8033    143    333   -119       C  
ATOM    440  C   SER A 193       4.314  38.619  51.810  1.00 77.75           C  
ANISOU  440  C   SER A 193    10361   9975   9204    186    322   -114       C  
ATOM    441  O   SER A 193       4.174  38.804  53.008  1.00 83.42           O  
ANISOU  441  O   SER A 193    11075  10713   9907    214    314   -103       O  
ATOM    442  CB  SER A 193       3.438  36.555  50.897  1.00 76.20           C  
ANISOU  442  CB  SER A 193    10088   9860   9005     34    340   -115       C  
ATOM    443  OG  SER A 193       2.368  35.918  50.259  1.00 91.07           O  
ANISOU  443  OG  SER A 193    11912  11844  10845     -7    344   -114       O  
ATOM    444  N   VAL A 194       5.448  38.872  51.163  1.00 82.81           N  
ANISOU  444  N   VAL A 194    11058  10500   9905    189    320   -121       N  
ATOM    445  CA  VAL A 194       6.602  39.388  51.874  1.00 90.98           C  
ANISOU  445  CA  VAL A 194    12156  11417  10994    226    309   -112       C  
ATOM    446  C   VAL A 194       6.309  40.811  52.351  1.00 92.77           C  
ANISOU  446  C   VAL A 194    12393  11674  11181    341    285   -109       C  
ATOM    447  O   VAL A 194       6.676  41.176  53.464  1.00101.12           O  
ANISOU  447  O   VAL A 194    13477  12691  12252    382    271    -99       O  
ATOM    448  CB  VAL A 194       7.874  39.287  51.008  1.00 91.53           C  
ANISOU  448  CB  VAL A 194    12281  11361  11136    200    311   -115       C  
ATOM    449  CG1 VAL A 194       9.095  39.886  51.681  1.00 91.35           C  
ANISOU  449  CG1 VAL A 194    12328  11208  11172    242    297   -101       C  
ATOM    450  CG2 VAL A 194       8.142  37.847  50.592  1.00 93.56           C  
ANISOU  450  CG2 VAL A 194    12524  11592  11432     89    328   -124       C  
ATOM    451  N   PHE A 195       5.640  41.613  51.514  1.00105.14           N  
ANISOU  451  N   PHE A 195    13938  13311  12701    395    275   -119       N  
ATOM    452  CA  PHE A 195       5.354  42.992  51.875  1.00115.08           C  
ANISOU  452  CA  PHE A 195    15204  14598  13924    505    243   -120       C  
ATOM    453  C   PHE A 195       4.251  43.047  52.925  1.00120.05           C  
ANISOU  453  C   PHE A 195    15785  15344  14484    536    239   -122       C  
ATOM    454  O   PHE A 195       4.236  43.952  53.745  1.00121.09           O  
ANISOU  454  O   PHE A 195    15930  15479  14600    621    210   -122       O  
ATOM    455  CB  PHE A 195       4.997  43.839  50.653  1.00118.83           C  
ANISOU  455  CB  PHE A 195    15667  15110  14373    548    229   -130       C  
ATOM    456  CG  PHE A 195       6.069  43.896  49.595  1.00125.06           C  
ANISOU  456  CG  PHE A 195    16497  15795  15223    526    228   -125       C  
ATOM    457  CD1 PHE A 195       7.373  44.251  49.913  1.00117.33           C  
ANISOU  457  CD1 PHE A 195    15582  14685  14312    550    210   -108       C  
ATOM    458  CD2 PHE A 195       5.760  43.599  48.274  1.00120.92           C  
ANISOU  458  CD2 PHE A 195    15947  15310  14688    485    245   -135       C  
ATOM    459  CE1 PHE A 195       8.346  44.303  48.926  1.00116.76           C  
ANISOU  459  CE1 PHE A 195    15544  14528  14292    531    209    -99       C  
ATOM    460  CE2 PHE A 195       6.734  43.656  47.292  1.00106.34           C  
ANISOU  460  CE2 PHE A 195    14132  13379  12892    468    244   -130       C  
ATOM    461  CZ  PHE A 195       8.022  44.006  47.622  1.00101.56           C  
ANISOU  461  CZ  PHE A 195    13588  12650  12351    491    226   -111       C  
ATOM    462  N   PHE A 196       3.342  42.072  52.907  1.00109.41           N  
ANISOU  462  N   PHE A 196    14381  14092  13097    468    265   -122       N  
ATOM    463  CA  PHE A 196       2.243  42.057  53.857  1.00 98.82           C  
ANISOU  463  CA  PHE A 196    12987  12874  11684    492    262   -119       C  
ATOM    464  C   PHE A 196       2.747  41.626  55.227  1.00 98.17           C  
ANISOU  464  C   PHE A 196    12919  12752  11630    479    261   -104       C  
ATOM    465  O   PHE A 196       2.301  42.160  56.234  1.00114.19           O  
ANISOU  465  O   PHE A 196    14931  14842  13615    544    245   -103       O  
ATOM    466  CB  PHE A 196       1.126  41.138  53.369  1.00104.65           C  
ANISOU  466  CB  PHE A 196    13660  13727  12375    422    285   -116       C  
ATOM    467  CG  PHE A 196      -0.219  41.432  53.973  1.00129.44           C  
ANISOU  467  CG  PHE A 196    16739  17017  15424    466    279   -114       C  
ATOM    468  CD1 PHE A 196      -0.572  40.922  55.216  1.00131.11           C  
ANISOU  468  CD1 PHE A 196    16917  17289  15610    452    280    -96       C  
ATOM    469  CD2 PHE A 196      -1.152  42.203  53.284  1.00136.65           C  
ANISOU  469  CD2 PHE A 196    17625  18019  16276    519    272   -130       C  
ATOM    470  CE1 PHE A 196      -1.829  41.168  55.755  1.00116.82           C  
ANISOU  470  CE1 PHE A 196    15046  15627  13712    493    275    -93       C  
ATOM    471  CE2 PHE A 196      -2.402  42.465  53.831  1.00133.14           C  
ANISOU  471  CE2 PHE A 196    17124  17716  15746    560    266   -130       C  
ATOM    472  CZ  PHE A 196      -2.736  41.950  55.067  1.00126.41           C  
ANISOU  472  CZ  PHE A 196    16238  16926  14865    549    268   -110       C  
ATOM    473  N   LYS A 197       3.672  40.659  55.259  1.00 89.95           N  
ANISOU  473  N   LYS A 197    11906  11610  10660    394    278    -94       N  
ATOM    474  CA  LYS A 197       4.283  40.187  56.494  1.00 79.32           C  
ANISOU  474  CA  LYS A 197    10578  10207   9352    369    278    -79       C  
ATOM    475  C   LYS A 197       5.060  41.326  57.134  1.00 80.49           C  
ANISOU  475  C   LYS A 197    10786  10271   9526    466    253    -80       C  
ATOM    476  O   LYS A 197       4.978  41.511  58.346  1.00 87.42           O  
ANISOU  476  O   LYS A 197    11659  11169  10389    503    243    -73       O  
ATOM    477  CB  LYS A 197       5.205  38.990  56.243  1.00 70.59           C  
ANISOU  477  CB  LYS A 197     9498   8996   8327    258    295    -73       C  
ATOM    478  CG  LYS A 197       5.874  38.384  57.470  1.00 80.65           C  
ANISOU  478  CG  LYS A 197    10791  10203   9649    216    297    -58       C  
ATOM    479  CD  LYS A 197       7.178  37.640  57.154  1.00 93.13           C  
ANISOU  479  CD  LYS A 197    12427  11633  11326    136    306    -59       C  
ATOM    480  CE  LYS A 197       7.564  36.566  58.157  1.00 93.13           C  
ANISOU  480  CE  LYS A 197    12421  11593  11372     49    310    -45       C  
ATOM    481  NZ  LYS A 197       8.047  37.130  59.442  1.00104.40           N  
ANISOU  481  NZ  LYS A 197    13882  12970  12814    104    302    -34       N  
ATOM    482  N   ASP A 198       5.793  42.084  56.306  1.00 88.99           N  
ANISOU  482  N   ASP A 198    11914  11257  10640    507    239    -87       N  
ATOM    483  CA  ASP A 198       6.626  43.181  56.779  1.00103.63           C  
ANISOU  483  CA  ASP A 198    13829  13017  12530    599    208    -83       C  
ATOM    484  C   ASP A 198       5.753  44.341  57.251  1.00108.81           C  
ANISOU  484  C   ASP A 198    14457  13771  13113    713    173    -94       C  
ATOM    485  O   ASP A 198       6.074  44.991  58.240  1.00134.42           O  
ANISOU  485  O   ASP A 198    17728  16982  16365    788    146    -91       O  
ATOM    486  CB  ASP A 198       7.604  43.675  55.711  1.00115.63           C  
ANISOU  486  CB  ASP A 198    15404  14422  14106    611    197    -81       C  
ATOM    487  CG  ASP A 198       8.560  44.747  56.222  1.00127.08           C  
ANISOU  487  CG  ASP A 198    16921  15761  15603    701    158    -69       C  
ATOM    488  OD1 ASP A 198       8.879  44.730  57.441  1.00117.39           O  
ANISOU  488  OD1 ASP A 198    15715  14495  14393    722    151    -61       O  
ATOM    489  OD2 ASP A 198       8.999  45.587  55.396  1.00131.02           O1-
ANISOU  489  OD2 ASP A 198    17448  16209  16122    749    131    -65       O1-
ATOM    490  N   ALA A 199       4.648  44.585  56.540  1.00 95.34           N  
ANISOU  490  N   ALA A 199    12698  12187  11339    728    173   -109       N  
ATOM    491  CA  ALA A 199       3.749  45.684  56.846  1.00 92.09           C  
ANISOU  491  CA  ALA A 199    12256  11877  10856    833    138   -124       C  
ATOM    492  C   ALA A 199       2.973  45.407  58.130  1.00102.49           C  
ANISOU  492  C   ALA A 199    13526  13299  12115    849    142   -124       C  
ATOM    493  O   ALA A 199       2.538  46.353  58.770  1.00123.35           O  
ANISOU  493  O   ALA A 199    16158  15999  14712    950    105   -137       O  
ATOM    494  CB  ALA A 199       2.831  45.953  55.675  1.00 88.03           C  
ANISOU  494  CB  ALA A 199    11701  11455  10291    834    140   -140       C  
ATOM    495  N   ALA A 200       2.819  44.131  58.521  1.00106.38           N  
ANISOU  495  N   ALA A 200    13989  13820  12609    751    179   -108       N  
ATOM    496  CA  ALA A 200       2.107  43.766  59.744  1.00103.06           C  
ANISOU  496  CA  ALA A 200    13519  13505  12135    756    183   -101       C  
ATOM    497  C   ALA A 200       3.001  43.907  60.978  1.00106.75           C  
ANISOU  497  C   ALA A 200    14028  13885  12648    788    170    -92       C  
ATOM    498  O   ALA A 200       2.518  43.872  62.101  1.00108.43           O  
ANISOU  498  O   ALA A 200    14204  14179  12816    817    164    -87       O  
ATOM    499  CB  ALA A 200       1.524  42.375  59.647  1.00 95.01           C  
ANISOU  499  CB  ALA A 200    12443  12558  11099    639    220    -83       C  
ATOM    500  N   LEU A 201       4.306  44.090  60.781  1.00114.03           N  
ANISOU  500  N   LEU A 201    15027  14642  13658    785    164    -87       N  
ATOM    501  CA  LEU A 201       5.199  44.331  61.904  1.00117.62           C  
ANISOU  501  CA  LEU A 201    15530  15000  14160    824    148    -78       C  
ATOM    502  C   LEU A 201       4.883  45.673  62.553  1.00130.46           C  
ANISOU  502  C   LEU A 201    17157  16669  15742    967     99    -94       C  
ATOM    503  O   LEU A 201       5.076  45.808  63.756  1.00164.87           O  
ANISOU  503  O   LEU A 201    21521  21020  20100   1010     86    -90       O  
ATOM    504  CB  LEU A 201       6.653  44.309  61.437  1.00125.76           C  
ANISOU  504  CB  LEU A 201    16645  15843  15294    795    149    -68       C  
ATOM    505  CG  LEU A 201       7.143  42.995  60.832  1.00125.19           C  
ANISOU  505  CG  LEU A 201    16579  15710  15276    658    191    -57       C  
ATOM    506  CD1 LEU A 201       8.600  43.145  60.410  1.00134.86           C  
ANISOU  506  CD1 LEU A 201    17891  16752  16599    647    187    -48       C  
ATOM    507  CD2 LEU A 201       6.965  41.826  61.800  1.00104.13           C  
ANISOU  507  CD2 LEU A 201    13877  13079  12611    572    217    -44       C  
ATOM    508  N   LYS A 202       4.440  46.659  61.760  1.00126.90           N  
ANISOU  508  N   LYS A 202    16701  16257  15257   1041     68   -113       N  
ATOM    509  CA  LYS A 202       3.979  47.930  62.304  1.00143.04           C  
ANISOU  509  CA  LYS A 202    18737  18362  17252   1178     13   -133       C  
ATOM    510  C   LYS A 202       2.621  47.716  62.978  1.00143.81           C  
ANISOU  510  C   LYS A 202    18749  18645  17246   1193     22   -145       C  
ATOM    511  O   LYS A 202       1.601  47.577  62.308  1.00136.44           O  
ANISOU  511  O   LYS A 202    17762  17830  16251   1170     35   -155       O  
ATOM    512  CB  LYS A 202       4.007  49.056  61.256  1.00148.43           C  
ANISOU  512  CB  LYS A 202    19440  19017  17938   1247    -30   -148       C  
ATOM    513  CG  LYS A 202       3.659  50.447  61.793  1.00160.15           C  
ANISOU  513  CG  LYS A 202    20921  20544  19384   1394   -101   -172       C  
ATOM    514  CD  LYS A 202       4.268  51.672  61.116  1.00152.76           C  
ANISOU  514  CD  LYS A 202    20034  19514  18494   1476   -164   -176       C  
ATOM    515  CE  LYS A 202       4.135  52.918  61.978  1.00140.18           C  
ANISOU  515  CE  LYS A 202    18445  17940  16878   1622   -242   -196       C  
ATOM    516  NZ  LYS A 202       4.435  54.188  61.265  1.00107.23           N  
ANISOU  516  NZ  LYS A 202    14299  13708  12734   1706   -317   -202       N  
ATOM    517  N   TRP A 203       2.640  47.680  64.319  1.00162.18           N  
ANISOU  517  N   TRP A 203    21066  20998  19558   1232     13   -142       N  
ATOM    518  CA  TRP A 203       1.474  47.442  65.160  1.00164.56           C  
ANISOU  518  CA  TRP A 203    21286  21475  19763   1249     20   -147       C  
ATOM    519  C   TRP A 203       0.820  46.101  64.804  1.00153.52           C  
ANISOU  519  C   TRP A 203    19829  20161  18338   1118     75   -125       C  
ATOM    520  O   TRP A 203       1.371  45.069  65.230  1.00130.99           O  
ANISOU  520  O   TRP A 203    16985  17253  15534   1025    107    -99       O  
ATOM    521  CB  TRP A 203       0.475  48.608  65.077  1.00170.96           C  
ANISOU  521  CB  TRP A 203    22058  22409  20489   1370    -27   -181       C  
ATOM    522  N   LEU A 218      -0.655  41.085  72.235  1.00180.36           N  
ANISOU  522  N   LEU A 218    22886  24053  21589    836    163     50       N  
ATOM    523  CA  LEU A 218      -0.094  39.768  71.824  1.00175.98           C  
ANISOU  523  CA  LEU A 218    22342  23405  21118    676    191     82       C  
ATOM    524  C   LEU A 218       0.620  39.902  70.475  1.00174.71           C  
ANISOU  524  C   LEU A 218    22262  23087  21032    648    200     61       C  
ATOM    525  O   LEU A 218       0.140  40.556  69.548  1.00156.35           O  
ANISOU  525  O   LEU A 218    19943  20793  18670    703    193     37       O  
ATOM    526  CB  LEU A 218      -1.195  38.693  71.836  1.00160.74           C  
ANISOU  526  CB  LEU A 218    20306  21641  19127    580    202    124       C  
ATOM    527  CG  LEU A 218      -1.591  38.131  73.208  1.00138.00           C  
ANISOU  527  CG  LEU A 218    17345  18884  16204    555    198    161       C  
ATOM    528  CD1 LEU A 218      -2.480  36.908  73.059  1.00129.18           C  
ANISOU  528  CD1 LEU A 218    16132  17896  15053    435    204    212       C  
ATOM    529  CD2 LEU A 218      -0.371  37.779  74.043  1.00126.71           C  
ANISOU  529  CD2 LEU A 218    15965  17311  14868    512    202    169       C  
ATOM    530  N   SER A 219       1.798  39.268  70.405  1.00182.97           N  
ANISOU  530  N   SER A 219    23371  23964  22187    561    213     70       N  
ATOM    531  CA  SER A 219       2.793  39.404  69.353  1.00175.62           C  
ANISOU  531  CA  SER A 219    22529  22856  21343    538    220     51       C  
ATOM    532  C   SER A 219       2.249  38.944  67.998  1.00176.44           C  
ANISOU  532  C   SER A 219    22609  22995  21434    474    233     51       C  
ATOM    533  O   SER A 219       1.254  38.229  67.925  1.00180.90           O  
ANISOU  533  O   SER A 219    23093  23698  21943    416    239     72       O  
ATOM    534  CB  SER A 219       4.051  38.656  69.757  1.00163.96           C  
ANISOU  534  CB  SER A 219    21107  21215  19975    448    233     66       C  
ATOM    535  OG  SER A 219       5.071  38.784  68.781  1.00157.15           O  
ANISOU  535  OG  SER A 219    20332  20182  19197    428    239     50       O  
ATOM    536  N   TYR A 220       2.932  39.356  66.922  1.00168.64           N  
ANISOU  536  N   TYR A 220    21695  21882  20501    485    234     29       N  
ATOM    537  CA  TYR A 220       2.607  38.978  65.552  1.00141.69           C  
ANISOU  537  CA  TYR A 220    18272  18476  17088    428    247     24       C  
ATOM    538  C   TYR A 220       2.790  37.472  65.344  1.00137.47           C  
ANISOU  538  C   TYR A 220    17712  17915  16604    276    264     48       C  
ATOM    539  O   TYR A 220       2.066  36.869  64.559  1.00134.55           O  
ANISOU  539  O   TYR A 220    17295  17621  16206    217    270     56       O  
ATOM    540  CB  TYR A 220       3.396  39.807  64.525  1.00139.48           C  
ANISOU  540  CB  TYR A 220    18075  18065  16857    478    241     -3       C  
ATOM    541  CG  TYR A 220       3.117  39.456  63.081  1.00134.68           C  
ANISOU  541  CG  TYR A 220    17459  17461  16250    424    254    -10       C  
ATOM    542  CD1 TYR A 220       1.869  39.680  62.517  1.00135.48           C  
ANISOU  542  CD1 TYR A 220    17501  17708  16268    450    253    -16       C  
ATOM    543  CD2 TYR A 220       4.083  38.870  62.278  1.00121.17           C  
ANISOU  543  CD2 TYR A 220    15799  15613  14625    344    267    -12       C  
ATOM    544  CE1 TYR A 220       1.584  39.325  61.208  1.00125.94           C  
ANISOU  544  CE1 TYR A 220    16285  16506  15062    399    265    -21       C  
ATOM    545  CE2 TYR A 220       3.820  38.524  60.961  1.00123.04           C  
ANISOU  545  CE2 TYR A 220    16027  15860  14863    296    278    -20       C  
ATOM    546  CZ  TYR A 220       2.566  38.752  60.422  1.00122.86           C  
ANISOU  546  CZ  TYR A 220    15944  15980  14756    324    277    -24       C  
ATOM    547  OH  TYR A 220       2.281  38.400  59.135  1.00115.80           O  
ANISOU  547  OH  TYR A 220    15040  15096  13863    278    288    -32       O  
ATOM    548  N   GLN A 221       3.755  36.871  66.053  1.00131.54           N  
ANISOU  548  N   GLN A 221    16994  17056  15930    213    268     61       N  
ATOM    549  CA  GLN A 221       4.049  35.448  65.959  1.00115.36           C  
ANISOU  549  CA  GLN A 221    14925  14967  13941     68    275     81       C  
ATOM    550  C   GLN A 221       2.847  34.623  66.420  1.00122.72           C  
ANISOU  550  C   GLN A 221    15749  16073  14806     11    269    115       C  
ATOM    551  O   GLN A 221       2.631  33.527  65.922  1.00116.43           O  
ANISOU  551  O   GLN A 221    14915  15293  14032    -98    267    131       O  
ATOM    552  CB  GLN A 221       5.315  35.087  66.747  1.00 98.42           C  
ANISOU  552  CB  GLN A 221    12835  12670  11888     22    277     86       C  
ATOM    553  N   ASP A 222       2.068  35.153  67.372  1.00144.49           N  
ANISOU  553  N   ASP A 222    18454  18963  17480     86    261    126       N  
ATOM    554  CA  ASP A 222       0.976  34.428  68.009  1.00141.16           C  
ANISOU  554  CA  ASP A 222    17928  18713  16993     39    253    166       C  
ATOM    555  C   ASP A 222      -0.339  34.637  67.260  1.00129.45           C  
ANISOU  555  C   ASP A 222    16385  17383  15417     72    251    169       C  
ATOM    556  O   ASP A 222      -1.288  33.879  67.453  1.00117.99           O  
ANISOU  556  O   ASP A 222    14846  16069  13917     14    243    206       O  
ATOM    557  CB  ASP A 222       0.845  34.797  69.489  1.00142.54           C  
ANISOU  557  CB  ASP A 222    18073  18960  17128     97    245    180       C  
ATOM    558  CG  ASP A 222       2.119  34.558  70.279  1.00156.87           C  
ANISOU  558  CG  ASP A 222    19945  20622  19035     60    248    180       C  
ATOM    559  OD1 ASP A 222       2.920  33.703  69.860  1.00170.07           O  
ANISOU  559  OD1 ASP A 222    21653  22168  20800    -48    252    183       O  
ATOM    560  OD2 ASP A 222       2.303  35.231  71.303  1.00175.14           O1-
ANISOU  560  OD2 ASP A 222    22271  22946  21331    141    244    175       O1-
ATOM    561  N   SER A 223      -0.391  35.661  66.404  1.00129.81           N  
ANISOU  561  N   SER A 223    16478  17404  15441    162    257    132       N  
ATOM    562  CA  SER A 223      -1.624  36.011  65.714  1.00137.95           C  
ANISOU  562  CA  SER A 223    17458  18574  16383    205    256    129       C  
ATOM    563  C   SER A 223      -1.969  34.962  64.658  1.00135.56           C  
ANISOU  563  C   SER A 223    17128  18278  16102     96    260    146       C  
ATOM    564  O   SER A 223      -1.109  34.195  64.224  1.00134.84           O  
ANISOU  564  O   SER A 223    17073  18059  16099      6    263    146       O  
ATOM    565  CB  SER A 223      -1.531  37.388  65.109  1.00148.68           C  
ANISOU  565  CB  SER A 223    18875  19898  17721    326    255     85       C  
ATOM    566  OG  SER A 223      -0.581  37.417  64.052  1.00136.26           O  
ANISOU  566  OG  SER A 223    17379  18165  16230    298    263     62       O  
ATOM    567  N   LEU A 224      -3.242  34.946  64.246  1.00122.81           N  
ANISOU  567  N   LEU A 224    15447  16812  14404    108    258    161       N  
ATOM    568  CA  LEU A 224      -3.671  34.030  63.203  1.00104.60           C  
ANISOU  568  CA  LEU A 224    13113  14519  12112     17    259    177       C  
ATOM    569  C   LEU A 224      -3.430  34.633  61.821  1.00101.64           C  
ANISOU  569  C   LEU A 224    12799  14063  11756     53    271    135       C  
ATOM    570  O   LEU A 224      -3.294  33.885  60.866  1.00 92.46           O  
ANISOU  570  O   LEU A 224    11642  12849  10639    -25    273    137       O  
ATOM    571  CB  LEU A 224      -5.140  33.642  63.403  1.00 95.30           C  
ANISOU  571  CB  LEU A 224    11835  13534  10841      5    249    219       C  
ATOM    572  CG  LEU A 224      -5.668  32.613  62.408  1.00100.31           C  
ANISOU  572  CG  LEU A 224    12434  14190  11490    -91    242    243       C  
ATOM    573  CD1 LEU A 224      -6.486  31.554  63.120  1.00 87.84           C  
ANISOU  573  CD1 LEU A 224    10757  12741   9878   -168    219    308       C  
ATOM    574  CD2 LEU A 224      -6.498  33.283  61.320  1.00102.51           C  
ANISOU  574  CD2 LEU A 224    12714  14525  11709    -30    254    222       C  
ATOM    575  N   ALA A 225      -3.386  35.971  61.729  1.00110.61           N  
ANISOU  575  N   ALA A 225    13976  15192  12859    170    276     99       N  
ATOM    576  CA  ALA A 225      -3.104  36.699  60.492  1.00101.45           C  
ANISOU  576  CA  ALA A 225    12874  13956  11717    214    284     61       C  
ATOM    577  C   ALA A 225      -1.759  36.274  59.907  1.00 94.71           C  
ANISOU  577  C   ALA A 225    12091  12923  10971    152    290     46       C  
ATOM    578  O   ALA A 225      -1.607  36.156  58.691  1.00 92.95           O  
ANISOU  578  O   ALA A 225    11892  12647  10776    126    298     30       O  
ATOM    579  CB  ALA A 225      -3.113  38.189  60.740  1.00 95.86           C  
ANISOU  579  CB  ALA A 225    12198  13257  10967    347    276     28       C  
ATOM    580  N   CYS A 226      -0.787  36.049  60.794  1.00 92.70           N  
ANISOU  580  N   CYS A 226    11870  12577  10776    132    287     52       N  
ATOM    581  CA  CYS A 226       0.551  35.649  60.400  1.00 91.82           C  
ANISOU  581  CA  CYS A 226    11827  12292  10767     75    292     39       C  
ATOM    582  C   CYS A 226       0.538  34.262  59.748  1.00 98.51           C  
ANISOU  582  C   CYS A 226    12647  13125  11659    -52    292     54       C  
ATOM    583  O   CYS A 226       1.214  34.061  58.742  1.00113.48           O  
ANISOU  583  O   CYS A 226    14587  14917  13612    -85    297     33       O  
ATOM    584  CB  CYS A 226       1.483  35.672  61.601  1.00 84.31           C  
ANISOU  584  CB  CYS A 226    10912  11257   9865     78    288     45       C  
ATOM    585  SG  CYS A 226       3.125  35.018  61.218  1.00 98.28           S  
ANISOU  585  SG  CYS A 226    12762  12816  11764     -6    293     34       S  
ATOM    586  N   ARG A 227      -0.259  33.336  60.296  1.00 96.35           N  
ANISOU  586  N   ARG A 227    12296  12959  11355   -118    281     90       N  
ATOM    587  CA  ARG A 227      -0.355  31.970  59.793  1.00 93.66           C  
ANISOU  587  CA  ARG A 227    11919  12612  11054   -238    268    108       C  
ATOM    588  C   ARG A 227      -1.017  31.939  58.413  1.00 87.46           C  
ANISOU  588  C   ARG A 227    11120  11868  10242   -239    272     97       C  
ATOM    589  O   ARG A 227      -0.659  31.092  57.602  1.00 80.90           O  
ANISOU  589  O   ARG A 227    10298  10973   9469   -317    265     91       O  
ATOM    590  CB  ARG A 227      -1.072  31.063  60.800  1.00 92.50           C  
ANISOU  590  CB  ARG A 227    11687  12578  10881   -304    247    157       C  
ATOM    591  CG  ARG A 227      -0.564  31.250  62.223  1.00105.58           C  
ANISOU  591  CG  ARG A 227    13351  14217  12549   -288    246    169       C  
ATOM    592  CD  ARG A 227      -1.298  30.450  63.280  1.00110.73           C  
ANISOU  592  CD  ARG A 227    13912  14993  13167   -346    224    221       C  
ATOM    593  NE  ARG A 227      -0.926  30.894  64.615  1.00125.09           N  
ANISOU  593  NE  ARG A 227    15737  16811  14979   -304    227    228       N  
ATOM    594  CZ  ARG A 227       0.153  30.499  65.294  1.00138.50           C  
ANISOU  594  CZ  ARG A 227    17472  18393  16759   -356    224    227       C  
ATOM    595  NH1 ARG A 227       1.000  29.632  64.780  1.00144.04           N  
ANISOU  595  NH1 ARG A 227    18208  18966  17556   -454    215    218       N  
ATOM    596  NH2 ARG A 227       0.390  30.968  66.502  1.00147.08           N  
ANISOU  596  NH2 ARG A 227    18562  19490  17832   -308    227    233       N  
ATOM    597  N   LEU A 228      -1.957  32.864  58.151  1.00 83.82           N  
ANISOU  597  N   LEU A 228    10641  11511   9697   -151    282     92       N  
ATOM    598  CA  LEU A 228      -2.631  32.961  56.857  1.00 88.57           C  
ANISOU  598  CA  LEU A 228    11231  12152  10268   -143    289     80       C  
ATOM    599  C   LEU A 228      -1.681  33.511  55.789  1.00 88.17           C  
ANISOU  599  C   LEU A 228    11258  11971  10270   -116    302     37       C  
ATOM    600  O   LEU A 228      -1.624  33.007  54.664  1.00 84.03           O  
ANISOU  600  O   LEU A 228    10739  11414   9776   -162    303     26       O  
ATOM    601  CB  LEU A 228      -3.880  33.851  56.938  1.00 86.05           C  
ANISOU  601  CB  LEU A 228    10871  11978   9844    -56    295     84       C  
ATOM    602  CG  LEU A 228      -5.030  33.362  57.812  1.00 86.20           C  
ANISOU  602  CG  LEU A 228    10804  12153   9794    -75    282    131       C  
ATOM    603  CD1 LEU A 228      -6.155  34.390  57.853  1.00 81.06           C  
ANISOU  603  CD1 LEU A 228    10123  11634   9040     23    289    126       C  
ATOM    604  CD2 LEU A 228      -5.515  31.978  57.384  1.00 79.62           C  
ANISOU  604  CD2 LEU A 228     9917  11355   8980   -185    265    167       C  
ATOM    605  N   VAL A 229      -0.953  34.573  56.145  1.00 84.94           N  
ANISOU  605  N   VAL A 229    10907  11493   9872    -37    309     14       N  
ATOM    606  CA  VAL A 229      -0.006  35.180  55.226  1.00 76.74           C  
ANISOU  606  CA  VAL A 229     9940  10334   8883     -6    318    -19       C  
ATOM    607  C   VAL A 229       1.119  34.185  54.940  1.00 74.52           C  
ANISOU  607  C   VAL A 229     9693   9923   8697    -98    316    -24       C  
ATOM    608  O   VAL A 229       1.608  34.114  53.818  1.00 81.56           O  
ANISOU  608  O   VAL A 229    10618  10746   9627   -115    321    -45       O  
ATOM    609  CB  VAL A 229       0.492  36.529  55.776  1.00 72.34           C  
ANISOU  609  CB  VAL A 229     9433   9735   8318    101    316    -35       C  
ATOM    610  CG1 VAL A 229       1.647  37.085  54.984  1.00 61.51           C  
ANISOU  610  CG1 VAL A 229     8138   8226   7010    125    319    -60       C  
ATOM    611  CG2 VAL A 229      -0.631  37.559  55.831  1.00 75.34           C  
ANISOU  611  CG2 VAL A 229     9780  10241   8605    195    312    -40       C  
ATOM    612  N   PHE A 230       1.493  33.385  55.945  1.00 77.90           N  
ANISOU  612  N   PHE A 230    10111  10325   9163   -161    306     -4       N  
ATOM    613  CA  PHE A 230       2.487  32.333  55.774  1.00 82.35           C  
ANISOU  613  CA  PHE A 230    10700  10773   9816   -257    299     -8       C  
ATOM    614  C   PHE A 230       1.926  31.191  54.933  1.00 81.78           C  
ANISOU  614  C   PHE A 230    10578  10745   9750   -343    285     -3       C  
ATOM    615  O   PHE A 230       2.662  30.594  54.162  1.00 86.25           O  
ANISOU  615  O   PHE A 230    11171  11219  10380   -397    280    -23       O  
ATOM    616  CB  PHE A 230       2.967  31.802  57.127  1.00 85.74           C  
ANISOU  616  CB  PHE A 230    11126  11167  10283   -303    288     13       C  
ATOM    617  CG  PHE A 230       4.058  30.765  57.074  1.00 76.70           C  
ANISOU  617  CG  PHE A 230    10010   9895   9236   -403    277      5       C  
ATOM    618  CD1 PHE A 230       5.223  30.990  56.367  1.00 79.28           C  
ANISOU  618  CD1 PHE A 230    10412  10084   9627   -398    287    -25       C  
ATOM    619  CD2 PHE A 230       3.925  29.565  57.734  1.00 78.58           C  
ANISOU  619  CD2 PHE A 230    10201  10154   9503   -502    253     30       C  
ATOM    620  CE1 PHE A 230       6.227  30.037  56.315  1.00 78.36           C  
ANISOU  620  CE1 PHE A 230    10323   9852   9600   -488    275    -35       C  
ATOM    621  CE2 PHE A 230       4.945  28.623  57.697  1.00 87.47           C  
ANISOU  621  CE2 PHE A 230    11354  11160  10723   -595    238     19       C  
ATOM    622  CZ  PHE A 230       6.102  28.861  56.997  1.00 72.80           C  
ANISOU  622  CZ  PHE A 230     9573   9163   8926   -587    250    -16       C  
ATOM    623  N   LEU A 231       0.631  30.895  55.080  1.00 82.11           N  
ANISOU  623  N   LEU A 231    10545  10927   9724   -351    276     25       N  
ATOM    624  CA  LEU A 231       0.008  29.859  54.274  1.00 75.22           C  
ANISOU  624  CA  LEU A 231     9623  10101   8854   -425    258     35       C  
ATOM    625  C   LEU A 231      -0.134  30.306  52.814  1.00 75.56           C  
ANISOU  625  C   LEU A 231     9689  10136   8884   -387    273      4       C  
ATOM    626  O   LEU A 231       0.056  29.483  51.918  1.00 73.88           O  
ANISOU  626  O   LEU A 231     9472   9884   8714   -448    260     -7       O  
ATOM    627  CB  LEU A 231      -1.324  29.419  54.888  1.00 62.20           C  
ANISOU  627  CB  LEU A 231     7889   8606   7140   -444    242     80       C  
ATOM    628  CG  LEU A 231      -2.052  28.349  54.086  1.00 60.06           C  
ANISOU  628  CG  LEU A 231     7563   8386   6870   -517    216     98       C  
ATOM    629  CD1 LEU A 231      -1.331  27.001  54.124  1.00 63.76           C  
ANISOU  629  CD1 LEU A 231     8026   8772   7429   -629    179    101       C  
ATOM    630  CD2 LEU A 231      -3.470  28.212  54.576  1.00 62.60           C  
ANISOU  630  CD2 LEU A 231     7804   8869   7111   -512    205    146       C  
ATOM    631  N   LEU A 232      -0.427  31.597  52.576  1.00 72.38           N  
ANISOU  631  N   LEU A 232     9309   9766   8427   -288    297    -10       N  
ATOM    632  CA  LEU A 232      -0.455  32.139  51.219  1.00 73.19           C  
ANISOU  632  CA  LEU A 232     9436   9853   8521   -250    312    -39       C  
ATOM    633  C   LEU A 232       0.944  32.078  50.595  1.00 81.50           C  
ANISOU  633  C   LEU A 232    10554  10759   9654   -268    315    -70       C  
ATOM    634  O   LEU A 232       1.093  31.763  49.411  1.00 71.77           O  
ANISOU  634  O   LEU A 232     9327   9498   8443   -291    316    -90       O  
ATOM    635  CB  LEU A 232      -0.981  33.580  51.222  1.00 71.83           C  
ANISOU  635  CB  LEU A 232     9274   9740   8280   -141    328    -47       C  
ATOM    636  CG  LEU A 232      -1.084  34.238  49.840  1.00 69.34           C  
ANISOU  636  CG  LEU A 232     8978   9416   7951   -100    341    -74       C  
ATOM    637  CD1 LEU A 232      -1.989  33.448  48.897  1.00 73.77           C  
ANISOU  637  CD1 LEU A 232     9492  10047   8492   -150    339    -68       C  
ATOM    638  CD2 LEU A 232      -1.501  35.703  49.914  1.00 58.51           C  
ANISOU  638  CD2 LEU A 232     7618   8093   6520      6    349    -84       C  
ATOM    639  N   MET A 233       1.966  32.401  51.401  1.00 81.33           N  
ANISOU  639  N   MET A 233    10582  10646   9675   -253    317    -73       N  
ATOM    640  CA  MET A 233       3.337  32.360  50.935  1.00 75.40           C  
ANISOU  640  CA  MET A 233     9894   9754   9000   -269    320    -97       C  
ATOM    641  C   MET A 233       3.707  30.933  50.513  1.00 75.83           C  
ANISOU  641  C   MET A 233     9934   9763   9116   -375    301   -104       C  
ATOM    642  O   MET A 233       4.277  30.727  49.437  1.00 80.83           O  
ANISOU  642  O   MET A 233    10591  10335   9784   -391    302   -130       O  
ATOM    643  CB  MET A 233       4.282  32.911  52.003  1.00 70.69           C  
ANISOU  643  CB  MET A 233     9350   9070   8438   -237    322    -93       C  
ATOM    644  CG  MET A 233       5.757  32.663  51.712  1.00 83.33           C  
ANISOU  644  CG  MET A 233    11016  10520  10126   -270    323   -111       C  
ATOM    645  SD  MET A 233       6.737  34.179  51.899  1.00 99.70           S  
ANISOU  645  SD  MET A 233    13170  12499  12214   -165    333   -116       S  
ATOM    646  CE  MET A 233       8.162  33.815  50.874  1.00 87.08           C  
ANISOU  646  CE  MET A 233    11630  10758  10699   -206    335   -139       C  
ATOM    647  N   GLN A 234       3.342  29.944  51.337  1.00 66.83           N  
ANISOU  647  N   GLN A 234     8748   8658   7985   -446    280    -80       N  
ATOM    648  CA  GLN A 234       3.605  28.544  51.029  1.00 71.58           C  
ANISOU  648  CA  GLN A 234     9328   9224   8646   -549    250    -85       C  
ATOM    649  C   GLN A 234       2.924  28.131  49.728  1.00 69.60           C  
ANISOU  649  C   GLN A 234     9043   9029   8375   -563    242    -97       C  
ATOM    650  O   GLN A 234       3.463  27.306  48.987  1.00 67.15           O  
ANISOU  650  O   GLN A 234     8738   8657   8119   -619    222   -120       O  
ATOM    651  CB  GLN A 234       3.146  27.612  52.149  1.00 77.67           C  
ANISOU  651  CB  GLN A 234    10044  10044   9423   -621    221    -50       C  
ATOM    652  CG  GLN A 234       4.044  27.674  53.377  1.00 96.72           C  
ANISOU  652  CG  GLN A 234    12492  12377  11881   -635    222    -43       C  
ATOM    653  CD  GLN A 234       5.465  27.248  53.107  1.00 93.22           C  
ANISOU  653  CD  GLN A 234    12108  11780  11529   -682    217    -74       C  
ATOM    654  OE1 GLN A 234       5.722  26.409  52.254  1.00 83.59           O  
ANISOU  654  OE1 GLN A 234    10882  10525  10352   -741    195    -96       O  
ATOM    655  NE2 GLN A 234       6.397  27.827  53.847  1.00106.62           N  
ANISOU  655  NE2 GLN A 234    13865  13388  13259   -654    234    -78       N  
ATOM    656  N   TYR A 235       1.747  28.708  49.468  1.00 65.16           N  
ANISOU  656  N   TYR A 235     8445   8581   7733   -509    255    -82       N  
ATOM    657  CA  TYR A 235       1.024  28.422  48.241  1.00 63.24           C  
ANISOU  657  CA  TYR A 235     8170   8392   7465   -514    250    -91       C  
ATOM    658  C   TYR A 235       1.773  28.990  47.038  1.00 65.17           C  
ANISOU  658  C   TYR A 235     8466   8565   7730   -475    270   -131       C  
ATOM    659  O   TYR A 235       1.852  28.336  46.001  1.00 63.90           O  
ANISOU  659  O   TYR A 235     8296   8387   7594   -510    257   -152       O  
ATOM    660  CB  TYR A 235      -0.413  28.934  48.329  1.00 60.21           C  
ANISOU  660  CB  TYR A 235     7738   8146   6992   -468    261    -64       C  
ATOM    661  CG  TYR A 235      -1.200  28.730  47.070  1.00 55.04           C  
ANISOU  661  CG  TYR A 235     7056   7547   6311   -467    259    -71       C  
ATOM    662  CD1 TYR A 235      -1.671  27.472  46.723  1.00 59.54           C  
ANISOU  662  CD1 TYR A 235     7578   8144   6902   -542    223    -57       C  
ATOM    663  CD2 TYR A 235      -1.448  29.795  46.225  1.00 51.10           C  
ANISOU  663  CD2 TYR A 235     6577   7068   5769   -393    290    -91       C  
ATOM    664  CE1 TYR A 235      -2.387  27.278  45.549  1.00 68.22           C  
ANISOU  664  CE1 TYR A 235     8653   9288   7978   -539    220    -64       C  
ATOM    665  CE2 TYR A 235      -2.164  29.622  45.053  1.00 57.31           C  
ANISOU  665  CE2 TYR A 235     7340   7903   6533   -393    290    -98       C  
ATOM    666  CZ  TYR A 235      -2.629  28.361  44.709  1.00 66.16           C  
ANISOU  666  CZ  TYR A 235     8416   9048   7674   -464    257    -85       C  
ATOM    667  OH  TYR A 235      -3.318  28.197  43.533  1.00 68.25           O  
ANISOU  667  OH  TYR A 235     8660   9354   7918   -461    257    -93       O  
ATOM    668  N   CYS A 236       2.311  30.209  47.180  1.00 67.64           N  
ANISOU  668  N   CYS A 236     8829   8838   8031   -400    298   -141       N  
ATOM    669  CA  CYS A 236       2.996  30.858  46.071  1.00 65.23           C  
ANISOU  669  CA  CYS A 236     8568   8474   7741   -358    315   -171       C  
ATOM    670  C   CYS A 236       4.249  30.092  45.683  1.00 62.33           C  
ANISOU  670  C   CYS A 236     8235   7993   7455   -414    302   -196       C  
ATOM    671  O   CYS A 236       4.537  29.982  44.492  1.00 61.35           O  
ANISOU  671  O   CYS A 236     8118   7848   7344   -415    304   -222       O  
ATOM    672  CB  CYS A 236       3.395  32.281  46.411  1.00 67.36           C  
ANISOU  672  CB  CYS A 236     8884   8718   7991   -270    336   -170       C  
ATOM    673  SG  CYS A 236       1.920  33.317  46.519  1.00 82.86           S  
ANISOU  673  SG  CYS A 236    10809  10819   9856   -193    348   -154       S  
ATOM    674  N   VAL A 237       4.975  29.600  46.695  1.00 58.22           N  
ANISOU  674  N   VAL A 237     7735   7402   6986   -459    290   -190       N  
ATOM    675  CA  VAL A 237       6.203  28.858  46.465  1.00 55.46           C  
ANISOU  675  CA  VAL A 237     7419   6938   6715   -516    275   -214       C  
ATOM    676  C   VAL A 237       5.940  27.577  45.658  1.00 62.70           C  
ANISOU  676  C   VAL A 237     8294   7874   7656   -588    244   -232       C  
ATOM    677  O   VAL A 237       6.616  27.356  44.648  1.00 72.65           O  
ANISOU  677  O   VAL A 237     9574   9081   8949   -596    241   -265       O  
ATOM    678  CB  VAL A 237       6.986  28.619  47.764  1.00 49.13           C  
ANISOU  678  CB  VAL A 237     6648   6057   5964   -550    268   -202       C  
ATOM    679  CG1 VAL A 237       8.124  27.641  47.557  1.00 42.66           C  
ANISOU  679  CG1 VAL A 237     5854   5126   5228   -625    246   -229       C  
ATOM    680  CG2 VAL A 237       7.538  29.935  48.283  1.00 54.34           C  
ANISOU  680  CG2 VAL A 237     7363   6669   6613   -469    295   -193       C  
ATOM    681  N   ALA A 238       4.949  26.769  46.065  1.00 49.68           N  
ANISOU  681  N   ALA A 238     6583   6302   5989   -637    217   -210       N  
ATOM    682  CA  ALA A 238       4.581  25.590  45.297  1.00 48.75           C  
ANISOU  682  CA  ALA A 238     6421   6209   5893   -699    179   -223       C  
ATOM    683  C   ALA A 238       4.077  25.972  43.895  1.00 54.27           C  
ANISOU  683  C   ALA A 238     7111   6959   6551   -652    194   -242       C  
ATOM    684  O   ALA A 238       4.227  25.218  42.923  1.00 40.02           O  
ANISOU  684  O   ALA A 238     5292   5139   4774   -684    169   -270       O  
ATOM    685  CB  ALA A 238       3.523  24.833  46.036  1.00 51.97           C  
ANISOU  685  CB  ALA A 238     6764   6700   6282   -749    146   -185       C  
ATOM    686  N   ALA A 239       3.470  27.161  43.783  1.00 57.80           N  
ANISOU  686  N   ALA A 239     7563   7467   6931   -573    232   -228       N  
ATOM    687  CA  ALA A 239       2.979  27.612  42.494  1.00 57.05           C  
ANISOU  687  CA  ALA A 239     7459   7420   6796   -528    249   -245       C  
ATOM    688  C   ALA A 239       4.147  27.959  41.587  1.00 62.04           C  
ANISOU  688  C   ALA A 239     8140   7969   7464   -505    262   -282       C  
ATOM    689  O   ALA A 239       4.074  27.729  40.384  1.00 65.59           O  
ANISOU  689  O   ALA A 239     8577   8433   7912   -503    259   -306       O  
ATOM    690  CB  ALA A 239       2.040  28.777  42.649  1.00 64.58           C  
ANISOU  690  CB  ALA A 239     8405   8460   7675   -456    281   -222       C  
ATOM    691  N   ASN A 240       5.215  28.515  42.171  1.00 62.30           N  
ANISOU  691  N   ASN A 240     8226   7918   7528   -487    276   -283       N  
ATOM    692  CA  ASN A 240       6.391  28.866  41.396  1.00 55.46           C  
ANISOU  692  CA  ASN A 240     7406   6972   6696   -465    287   -311       C  
ATOM    693  C   ASN A 240       6.942  27.598  40.772  1.00 58.66           C  
ANISOU  693  C   ASN A 240     7800   7332   7156   -532    255   -344       C  
ATOM    694  O   ASN A 240       7.257  27.618  39.582  1.00 57.82           O  
ANISOU  694  O   ASN A 240     7696   7221   7051   -516    258   -372       O  
ATOM    695  CB  ASN A 240       7.456  29.554  42.246  1.00 63.05           C  
ANISOU  695  CB  ASN A 240     8426   7842   7687   -440    301   -301       C  
ATOM    696  CG  ASN A 240       7.003  30.903  42.761  1.00 66.65           C  
ANISOU  696  CG  ASN A 240     8895   8337   8091   -362    326   -274       C  
ATOM    697  OD1 ASN A 240       6.160  31.544  42.139  1.00 64.85           O  
ANISOU  697  OD1 ASN A 240     8643   8190   7807   -315    338   -270       O  
ATOM    698  ND2 ASN A 240       7.543  31.333  43.893  1.00 58.93           N  
ANISOU  698  ND2 ASN A 240     7955   7303   7134   -347    329   -256       N  
ATOM    699  N   TYR A 241       7.022  26.514  41.574  1.00 58.44           N  
ANISOU  699  N   TYR A 241     7758   7276   7172   -606    221   -342       N  
ATOM    700  CA  TYR A 241       7.671  25.268  41.166  1.00 65.39           C  
ANISOU  700  CA  TYR A 241     8630   8099   8114   -675    180   -376       C  
ATOM    701  C   TYR A 241       6.840  24.495  40.148  1.00 59.45           C  
ANISOU  701  C   TYR A 241     7824   7418   7347   -694    151   -392       C  
ATOM    702  O   TYR A 241       7.390  23.777  39.319  1.00 57.20           O  
ANISOU  702  O   TYR A 241     7535   7097   7099   -720    124   -432       O  
ATOM    703  CB  TYR A 241       8.116  24.399  42.351  1.00 69.92           C  
ANISOU  703  CB  TYR A 241     9208   8612   8748   -751    148   -369       C  
ATOM    704  CG  TYR A 241       9.290  24.989  43.084  1.00 78.02           C  
ANISOU  704  CG  TYR A 241    10299   9538   9809   -738    171   -367       C  
ATOM    705  CD1 TYR A 241      10.584  24.846  42.609  1.00 81.03           C  
ANISOU  705  CD1 TYR A 241    10724   9821  10242   -748    169   -401       C  
ATOM    706  CD2 TYR A 241       9.099  25.737  44.230  1.00 86.89           C  
ANISOU  706  CD2 TYR A 241    11439  10666  10910   -711    196   -329       C  
ATOM    707  CE1 TYR A 241      11.655  25.432  43.256  1.00 88.02           C  
ANISOU  707  CE1 TYR A 241    11672  10611  11160   -732    192   -394       C  
ATOM    708  CE2 TYR A 241      10.162  26.324  44.893  1.00 91.43           C  
ANISOU  708  CE2 TYR A 241    12076  11145  11519   -693    216   -325       C  
ATOM    709  CZ  TYR A 241      11.443  26.174  44.402  1.00 90.70           C  
ANISOU  709  CZ  TYR A 241    12030  10950  11481   -704    214   -355       C  
ATOM    710  OH  TYR A 241      12.499  26.750  45.041  1.00100.49           O  
ANISOU  710  OH  TYR A 241    13334  12091  12755   -686    233   -346       O  
ATOM    711  N   TYR A 242       5.518  24.646  40.221  1.00 61.77           N  
ANISOU  711  N   TYR A 242     8074   7811   7585   -679    155   -363       N  
ATOM    712  CA  TYR A 242       4.650  23.922  39.302  1.00 60.56           C  
ANISOU  712  CA  TYR A 242     7869   7723   7417   -695    126   -372       C  
ATOM    713  C   TYR A 242       4.413  24.689  38.008  1.00 57.97           C  
ANISOU  713  C   TYR A 242     7546   7437   7044   -629    159   -390       C  
ATOM    714  O   TYR A 242       4.329  24.053  36.964  1.00 63.61           O  
ANISOU  714  O   TYR A 242     8236   8162   7769   -640    135   -419       O  
ATOM    715  CB  TYR A 242       3.381  23.443  40.011  1.00 56.30           C  
ANISOU  715  CB  TYR A 242     7276   7265   6851   -726    101   -329       C  
ATOM    716  CG  TYR A 242       3.627  22.181  40.799  1.00 49.52           C  
ANISOU  716  CG  TYR A 242     6394   6367   6053   -814     42   -323       C  
ATOM    717  CD1 TYR A 242       3.567  20.935  40.169  1.00 45.50           C  
ANISOU  717  CD1 TYR A 242     5849   5851   5587   -867    -20   -346       C  
ATOM    718  CD2 TYR A 242       4.021  22.253  42.128  1.00 40.30           C  
ANISOU  718  CD2 TYR A 242     5242   5162   4906   -841     45   -300       C  
ATOM    719  CE1 TYR A 242       3.819  19.766  40.856  1.00 39.99           C  
ANISOU  719  CE1 TYR A 242     5127   5115   4952   -951    -83   -342       C  
ATOM    720  CE2 TYR A 242       4.304  21.094  42.820  1.00 40.87           C  
ANISOU  720  CE2 TYR A 242     5292   5195   5040   -926    -12   -296       C  
ATOM    721  CZ  TYR A 242       4.185  19.860  42.187  1.00 44.50           C  
ANISOU  721  CZ  TYR A 242     5713   5653   5543   -982    -78   -316       C  
ATOM    722  OH  TYR A 242       4.467  18.716  42.876  1.00 47.38           O  
ANISOU  722  OH  TYR A 242     6051   5977   5972  -1070   -143   -312       O  
ATOM    723  N   TRP A 243       4.308  26.029  38.073  1.00 57.40           N  
ANISOU  723  N   TRP A 243     7499   7386   6923   -561    210   -373       N  
ATOM    724  CA  TRP A 243       4.258  26.841  36.864  1.00 58.94           C  
ANISOU  724  CA  TRP A 243     7701   7610   7084   -500    240   -390       C  
ATOM    725  C   TRP A 243       5.587  26.777  36.125  1.00 64.35           C  
ANISOU  725  C   TRP A 243     8420   8218   7812   -497    239   -428       C  
ATOM    726  O   TRP A 243       5.600  26.971  34.907  1.00 59.88           O  
ANISOU  726  O   TRP A 243     7845   7678   7230   -468    248   -451       O  
ATOM    727  CB  TRP A 243       3.826  28.284  37.141  1.00 58.18           C  
ANISOU  727  CB  TRP A 243     7621   7555   6930   -432    284   -362       C  
ATOM    728  CG  TRP A 243       2.337  28.432  37.142  1.00 70.86           C  
ANISOU  728  CG  TRP A 243     9184   9263   8477   -418    290   -337       C  
ATOM    729  CD1 TRP A 243       1.553  28.599  38.244  1.00 71.27           C  
ANISOU  729  CD1 TRP A 243     9221   9361   8498   -419    291   -301       C  
ATOM    730  CD2 TRP A 243       1.435  28.334  36.020  1.00 72.93           C  
ANISOU  730  CD2 TRP A 243     9411   9595   8705   -406    292   -345       C  
ATOM    731  NE1 TRP A 243       0.234  28.655  37.891  1.00 71.55           N  
ANISOU  731  NE1 TRP A 243     9215   9491   8480   -407    295   -285       N  
ATOM    732  CE2 TRP A 243       0.126  28.492  36.532  1.00 79.42           C  
ANISOU  732  CE2 TRP A 243    10200  10500   9475   -400    296   -311       C  
ATOM    733  CE3 TRP A 243       1.587  28.137  34.639  1.00 80.64           C  
ANISOU  733  CE3 TRP A 243    10379  10575   9687   -398    291   -377       C  
ATOM    734  CZ2 TRP A 243      -1.011  28.448  35.712  1.00 83.06           C  
ANISOU  734  CZ2 TRP A 243    10625  11038   9895   -389    300   -306       C  
ATOM    735  CZ3 TRP A 243       0.466  28.110  33.829  1.00 85.24           C  
ANISOU  735  CZ3 TRP A 243    10925  11234  10228   -385    294   -374       C  
ATOM    736  CH2 TRP A 243      -0.821  28.263  34.360  1.00 77.95           C  
ANISOU  736  CH2 TRP A 243     9974  10385   9258   -382    299   -339       C  
ATOM    737  N   LEU A 244       6.678  26.514  36.877  1.00 68.72           N  
ANISOU  737  N   LEU A 244     9009   8682   8418   -527    229   -434       N  
ATOM    738  CA  LEU A 244       7.976  26.220  36.287  1.00 72.03           C  
ANISOU  738  CA  LEU A 244     9457   9024   8885   -537    220   -470       C  
ATOM    739  C   LEU A 244       7.952  24.825  35.646  1.00 73.03           C  
ANISOU  739  C   LEU A 244     9548   9151   9048   -592    170   -509       C  
ATOM    740  O   LEU A 244       8.669  24.582  34.669  1.00 70.96           O  
ANISOU  740  O   LEU A 244     9292   8866   8805   -585    162   -547       O  
ATOM    741  CB  LEU A 244       9.085  26.355  37.341  1.00 78.63           C  
ANISOU  741  CB  LEU A 244    10345   9761   9769   -555    223   -462       C  
ATOM    742  CG  LEU A 244      10.518  26.094  36.847  1.00 82.16           C  
ANISOU  742  CG  LEU A 244    10828  10120  10267   -565    215   -497       C  
ATOM    743  CD1 LEU A 244      10.953  27.104  35.806  1.00 71.03           C  
ANISOU  743  CD1 LEU A 244     9436   8723   8828   -497    247   -500       C  
ATOM    744  CD2 LEU A 244      11.517  26.070  37.987  1.00 86.32           C  
ANISOU  744  CD2 LEU A 244    11405  10545  10846   -594    214   -487       C  
ATOM    745  N   LEU A 245       7.108  23.921  36.179  1.00 60.96           N  
ANISOU  745  N   LEU A 245     7980   7656   7527   -643    133   -497       N  
ATOM    746  CA  LEU A 245       7.018  22.579  35.635  1.00 51.74           C  
ANISOU  746  CA  LEU A 245     6774   6488   6397   -695     74   -529       C  
ATOM    747  C   LEU A 245       6.318  22.624  34.289  1.00 54.82           C  
ANISOU  747  C   LEU A 245     7131   6950   6747   -656     77   -546       C  
ATOM    748  O   LEU A 245       6.783  22.009  33.332  1.00 62.96           O  
ANISOU  748  O   LEU A 245     8152   7967   7802   -661     49   -591       O  
ATOM    749  CB  LEU A 245       6.247  21.654  36.572  1.00 50.81           C  
ANISOU  749  CB  LEU A 245     6618   6390   6298   -759     28   -503       C  
ATOM    750  CG  LEU A 245       6.073  20.257  35.978  1.00 48.61           C  
ANISOU  750  CG  LEU A 245     6295   6114   6060   -810    -45   -534       C  
ATOM    751  CD1 LEU A 245       7.433  19.648  35.772  1.00 48.52           C  
ANISOU  751  CD1 LEU A 245     6309   6010   6114   -841    -75   -585       C  
ATOM    752  CD2 LEU A 245       5.224  19.371  36.864  1.00 52.60           C  
ANISOU  752  CD2 LEU A 245     6755   6648   6583   -873    -97   -498       C  
ATOM    753  N   VAL A 246       5.186  23.326  34.227  1.00 50.75           N  
ANISOU  753  N   VAL A 246     6597   6515   6170   -618    109   -512       N  
ATOM    754  CA  VAL A 246       4.467  23.411  32.969  1.00 64.81           C  
ANISOU  754  CA  VAL A 246     8348   8364   7913   -583    114   -525       C  
ATOM    755  C   VAL A 246       5.275  24.237  31.970  1.00 66.90           C  
ANISOU  755  C   VAL A 246     8640   8615   8164   -528    152   -552       C  
ATOM    756  O   VAL A 246       5.120  24.080  30.760  1.00 63.56           O  
ANISOU  756  O   VAL A 246     8194   8226   7727   -506    147   -580       O  
ATOM    757  CB  VAL A 246       3.025  23.928  33.150  1.00 63.11           C  
ANISOU  757  CB  VAL A 246     8105   8236   7637   -560    137   -481       C  
ATOM    758  CG1 VAL A 246       2.302  23.172  34.260  1.00 59.11           C  
ANISOU  758  CG1 VAL A 246     7571   7746   7142   -614    100   -446       C  
ATOM    759  CG2 VAL A 246       2.992  25.419  33.409  1.00 70.12           C  
ANISOU  759  CG2 VAL A 246     9025   9142   8477   -501    198   -457       C  
ATOM    760  N   GLU A 247       6.126  25.132  32.489  1.00 65.49           N  
ANISOU  760  N   GLU A 247     8507   8388   7988   -504    187   -541       N  
ATOM    761  CA  GLU A 247       6.977  25.944  31.637  1.00 61.55           C  
ANISOU  761  CA  GLU A 247     8034   7874   7479   -455    218   -558       C  
ATOM    762  C   GLU A 247       7.975  25.038  30.919  1.00 62.52           C  
ANISOU  762  C   GLU A 247     8156   7952   7649   -478    183   -609       C  
ATOM    763  O   GLU A 247       8.345  25.302  29.775  1.00 62.32           O  
ANISOU  763  O   GLU A 247     8124   7947   7609   -442    194   -633       O  
ATOM    764  CB  GLU A 247       7.672  26.997  32.484  1.00 62.65           C  
ANISOU  764  CB  GLU A 247     8222   7962   7619   -429    251   -529       C  
ATOM    765  CG  GLU A 247       8.409  28.008  31.642  1.00 79.86           C  
ANISOU  765  CG  GLU A 247    10423  10137   9782   -373    281   -533       C  
ATOM    766  CD  GLU A 247       7.506  28.911  30.835  1.00 89.81           C  
ANISOU  766  CD  GLU A 247    11658  11483  10982   -322    310   -518       C  
ATOM    767  OE1 GLU A 247       6.729  29.661  31.472  1.00 86.31           O  
ANISOU  767  OE1 GLU A 247    11217  11072  10505   -300    329   -484       O  
ATOM    768  OE2 GLU A 247       7.598  28.859  29.578  1.00 93.82           O1-
ANISOU  768  OE2 GLU A 247    12143  12025  11477   -303    310   -544       O1-
ATOM    769  N   GLY A 248       8.408  23.975  31.608  1.00 61.60           N  
ANISOU  769  N   GLY A 248     8042   7775   7587   -539    140   -624       N  
ATOM    770  CA  GLY A 248       9.231  22.937  31.006  1.00 54.38           C  
ANISOU  770  CA  GLY A 248     7120   6821   6720   -568     95   -677       C  
ATOM    771  C   GLY A 248       8.417  21.990  30.125  1.00 54.92           C  
ANISOU  771  C   GLY A 248     7135   6948   6786   -579     50   -706       C  
ATOM    772  O   GLY A 248       8.865  21.617  29.037  1.00 53.85           O  
ANISOU  772  O   GLY A 248     6985   6820   6656   -562     32   -751       O  
ATOM    773  N   VAL A 249       7.214  21.606  30.591  1.00 53.91           N  
ANISOU  773  N   VAL A 249     6974   6862   6645   -604     31   -677       N  
ATOM    774  CA  VAL A 249       6.367  20.689  29.832  1.00 50.25           C  
ANISOU  774  CA  VAL A 249     6461   6451   6182   -615    -17   -696       C  
ATOM    775  C   VAL A 249       5.938  21.325  28.513  1.00 53.28           C  
ANISOU  775  C   VAL A 249     6829   6902   6513   -551     18   -707       C  
ATOM    776  O   VAL A 249       5.928  20.638  27.502  1.00 57.49           O  
ANISOU  776  O   VAL A 249     7333   7453   7056   -545    -19   -748       O  
ATOM    777  CB  VAL A 249       5.135  20.202  30.599  1.00 41.93           C  
ANISOU  777  CB  VAL A 249     5375   5433   5125   -653    -46   -654       C  
ATOM    778  CG1 VAL A 249       4.282  19.366  29.676  1.00 36.42           C  
ANISOU  778  CG1 VAL A 249     4627   4786   4425   -653    -94   -671       C  
ATOM    779  CG2 VAL A 249       5.522  19.411  31.840  1.00 43.97           C  
ANISOU  779  CG2 VAL A 249     5637   5630   5440   -723    -91   -645       C  
ATOM    780  N   TYR A 250       5.609  22.628  28.536  1.00 53.42           N  
ANISOU  780  N   TYR A 250     6864   6955   6478   -505     84   -672       N  
ATOM    781  CA  TYR A 250       5.234  23.358  27.338  1.00 50.91           C  
ANISOU  781  CA  TYR A 250     6533   6700   6110   -448    120   -678       C  
ATOM    782  C   TYR A 250       6.380  23.336  26.331  1.00 58.95           C  
ANISOU  782  C   TYR A 250     7557   7698   7142   -423    119   -725       C  
ATOM    783  O   TYR A 250       6.160  23.069  25.137  1.00 52.71           O  
ANISOU  783  O   TYR A 250     6736   6953   6337   -399    108   -756       O  
ATOM    784  CB  TYR A 250       4.844  24.796  27.680  1.00 53.32           C  
ANISOU  784  CB  TYR A 250     6860   7035   6365   -408    183   -632       C  
ATOM    785  CG  TYR A 250       4.547  25.638  26.468  1.00 64.25           C  
ANISOU  785  CG  TYR A 250     8230   8480   7701   -353    220   -637       C  
ATOM    786  CD1 TYR A 250       3.374  25.443  25.751  1.00 67.77           C  
ANISOU  786  CD1 TYR A 250     8639   8994   8118   -343    217   -636       C  
ATOM    787  CD2 TYR A 250       5.439  26.600  26.012  1.00 64.88           C  
ANISOU  787  CD2 TYR A 250     8332   8549   7769   -313    255   -640       C  
ATOM    788  CE1 TYR A 250       3.078  26.181  24.619  1.00 61.74           C  
ANISOU  788  CE1 TYR A 250     7860   8285   7312   -297    250   -641       C  
ATOM    789  CE2 TYR A 250       5.148  27.356  24.887  1.00 67.88           C  
ANISOU  789  CE2 TYR A 250     8694   8989   8108   -267    284   -641       C  
ATOM    790  CZ  TYR A 250       3.970  27.134  24.184  1.00 65.89           C  
ANISOU  790  CZ  TYR A 250     8404   8803   7826   -261    283   -645       C  
ATOM    791  OH  TYR A 250       3.629  27.841  23.073  1.00 66.97           O  
ANISOU  791  OH  TYR A 250     8522   9000   7924   -220    311   -647       O  
ATOM    792  N   LEU A 251       7.600  23.618  26.837  1.00 67.71           N  
ANISOU  792  N   LEU A 251     8707   8742   8278   -428    129   -729       N  
ATOM    793  CA  LEU A 251       8.804  23.714  26.018  1.00 63.40           C  
ANISOU  793  CA  LEU A 251     8171   8175   7742   -404    132   -765       C  
ATOM    794  C   LEU A 251       9.043  22.377  25.330  1.00 55.81           C  
ANISOU  794  C   LEU A 251     7178   7210   6816   -426     70   -824       C  
ATOM    795  O   LEU A 251       9.379  22.372  24.144  1.00 46.15           O  
ANISOU  795  O   LEU A 251     5935   6022   5577   -390     69   -859       O  
ATOM    796  CB  LEU A 251       9.996  24.133  26.891  1.00 67.16           C  
ANISOU  796  CB  LEU A 251     8699   8570   8249   -414    147   -752       C  
ATOM    797  CG  LEU A 251      11.395  24.098  26.262  1.00 66.67           C  
ANISOU  797  CG  LEU A 251     8652   8471   8207   -399    143   -787       C  
ATOM    798  CD1 LEU A 251      11.522  25.093  25.100  1.00 70.55           C  
ANISOU  798  CD1 LEU A 251     9131   9026   8649   -335    182   -780       C  
ATOM    799  CD2 LEU A 251      12.466  24.403  27.313  1.00 65.27           C  
ANISOU  799  CD2 LEU A 251     8530   8203   8066   -418    153   -767       C  
ATOM    800  N   TYR A 252       8.835  21.279  26.080  1.00 49.72           N  
ANISOU  800  N   TYR A 252     6400   6401   6092   -483     15   -834       N  
ATOM    801  CA  TYR A 252       9.147  19.958  25.567  1.00 56.22           C  
ANISOU  801  CA  TYR A 252     7195   7209   6957   -509    -57   -892       C  
ATOM    802  C   TYR A 252       8.246  19.651  24.392  1.00 62.78           C  
ANISOU  802  C   TYR A 252     7978   8117   7759   -477    -74   -911       C  
ATOM    803  O   TYR A 252       8.737  19.200  23.359  1.00 76.64           O  
ANISOU  803  O   TYR A 252     9713   9888   9520   -453   -101   -964       O  
ATOM    804  CB  TYR A 252       8.969  18.869  26.611  1.00 61.32           C  
ANISOU  804  CB  TYR A 252     7835   7804   7660   -580   -120   -891       C  
ATOM    805  CG  TYR A 252       9.234  17.478  26.101  1.00 70.22           C  
ANISOU  805  CG  TYR A 252     8930   8915   8836   -607   -206   -952       C  
ATOM    806  CD1 TYR A 252      10.508  16.941  26.109  1.00 77.09           C  
ANISOU  806  CD1 TYR A 252     9817   9721   9754   -627   -240  -1001       C  
ATOM    807  CD2 TYR A 252       8.198  16.684  25.637  1.00 84.15           C  
ANISOU  807  CD2 TYR A 252    10646  10725  10603   -612   -260   -959       C  
ATOM    808  CE1 TYR A 252      10.738  15.639  25.685  1.00 98.57           C  
ANISOU  808  CE1 TYR A 252    12505  12426  12522   -652   -329  -1061       C  
ATOM    809  CE2 TYR A 252       8.412  15.393  25.186  1.00 98.51           C  
ANISOU  809  CE2 TYR A 252    12432  12527  12470   -634   -351  -1016       C  
ATOM    810  CZ  TYR A 252       9.688  14.861  25.220  1.00 99.07           C  
ANISOU  810  CZ  TYR A 252    12518  12536  12588   -654   -387  -1069       C  
ATOM    811  OH  TYR A 252       9.889  13.581  24.786  1.00100.43           O  
ANISOU  811  OH  TYR A 252    12656  12692  12810   -674   -484  -1129       O  
ATOM    812  N   THR A 253       6.949  19.939  24.548  1.00 69.62           N  
ANISOU  812  N   THR A 253     8828   9032   8592   -473    -57   -869       N  
ATOM    813  CA  THR A 253       5.986  19.673  23.492  1.00 85.99           C  
ANISOU  813  CA  THR A 253    10859  11175  10639   -444    -71   -880       C  
ATOM    814  C   THR A 253       6.223  20.610  22.299  1.00 87.82           C  
ANISOU  814  C   THR A 253    11087  11458  10820   -380    -17   -893       C  
ATOM    815  O   THR A 253       5.971  20.247  21.148  1.00 87.34           O  
ANISOU  815  O   THR A 253    10993  11443  10748   -350    -36   -928       O  
ATOM    816  CB  THR A 253       4.545  19.738  24.015  1.00 86.50           C  
ANISOU  816  CB  THR A 253    10908  11275  10681   -460    -67   -827       C  
ATOM    817  OG1 THR A 253       4.338  21.048  24.553  1.00 88.42           O  
ANISOU  817  OG1 THR A 253    11180  11534  10881   -440      8   -778       O  
ATOM    818  CG2 THR A 253       4.229  18.637  25.003  1.00 81.89           C  
ANISOU  818  CG2 THR A 253    10312  10655  10149   -524   -135   -816       C  
ATOM    819  N   LEU A 254       6.715  21.821  22.578  1.00 73.46           N  
ANISOU  819  N   LEU A 254     9303   9634   8976   -358     48   -863       N  
ATOM    820  CA  LEU A 254       6.998  22.775  21.521  1.00 69.61           C  
ANISOU  820  CA  LEU A 254     8810   9195   8443   -301     96   -867       C  
ATOM    821  C   LEU A 254       8.125  22.268  20.615  1.00 67.38           C  
ANISOU  821  C   LEU A 254     8516   8907   8177   -283     68   -925       C  
ATOM    822  O   LEU A 254       8.122  22.537  19.419  1.00 60.15           O  
ANISOU  822  O   LEU A 254     7573   8051   7230   -239     82   -946       O  
ATOM    823  CB  LEU A 254       7.348  24.111  22.185  1.00 71.47           C  
ANISOU  823  CB  LEU A 254     9086   9415   8657   -287    156   -818       C  
ATOM    824  CG  LEU A 254       7.481  25.304  21.254  1.00 68.95           C  
ANISOU  824  CG  LEU A 254     8760   9149   8288   -233    207   -805       C  
ATOM    825  CD1 LEU A 254       6.148  25.612  20.594  1.00 77.86           C  
ANISOU  825  CD1 LEU A 254     9856  10352   9374   -212    225   -791       C  
ATOM    826  CD2 LEU A 254       7.959  26.500  22.045  1.00 77.11           C  
ANISOU  826  CD2 LEU A 254     9835  10151   9313   -223    249   -757       C  
ATOM    827  N   LEU A 255       9.097  21.542  21.192  1.00 76.71           N  
ANISOU  827  N   LEU A 255     9716  10020   9409   -317     29   -953       N  
ATOM    828  CA  LEU A 255      10.215  20.977  20.446  1.00 76.66           C  
ANISOU  828  CA  LEU A 255     9699  10004   9422   -304     -4  -1012       C  
ATOM    829  C   LEU A 255       9.774  19.739  19.670  1.00 72.21           C  
ANISOU  829  C   LEU A 255     9090   9469   8876   -304    -72  -1068       C  
ATOM    830  O   LEU A 255      10.435  19.360  18.712  1.00 74.55           O  
ANISOU  830  O   LEU A 255     9365   9790   9173   -274    -96  -1121       O  
ATOM    831  CB  LEU A 255      11.390  20.658  21.387  1.00 72.66           C  
ANISOU  831  CB  LEU A 255     9233   9408   8966   -343    -23  -1022       C  
ATOM    832  CG  LEU A 255      12.057  21.851  22.088  1.00 74.78           C  
ANISOU  832  CG  LEU A 255     9551   9640   9224   -336     38   -971       C  
ATOM    833  CD1 LEU A 255      12.991  21.370  23.189  1.00 75.22           C  
ANISOU  833  CD1 LEU A 255     9647   9597   9337   -386     13   -977       C  
ATOM    834  CD2 LEU A 255      12.798  22.794  21.132  1.00 57.97           C  
ANISOU  834  CD2 LEU A 255     7420   7552   7055   -279     81   -968       C  
ATOM    835  N   ALA A 256       8.652  19.128  20.075  1.00 71.02           N  
ANISOU  835  N   ALA A 256     8923   9320   8740   -334   -107  -1054       N  
ATOM    836  CA  ALA A 256       8.180  17.877  19.484  1.00 80.64           C  
ANISOU  836  CA  ALA A 256    10100  10555   9985   -338   -185  -1101       C  
ATOM    837  C   ALA A 256       7.216  18.106  18.302  1.00 78.03           C  
ANISOU  837  C   ALA A 256     9731  10307   9608   -288   -169  -1103       C  
ATOM    838  O   ALA A 256       6.896  17.188  17.537  1.00 66.51           O  
ANISOU  838  O   ALA A 256     8236   8871   8164   -274   -230  -1147       O  
ATOM    839  CB  ALA A 256       7.568  17.016  20.564  1.00 86.20           C  
ANISOU  839  CB  ALA A 256    10803  11212  10736   -400   -241  -1081       C  
ATOM    840  N   PHE A 257       6.715  19.334  18.163  1.00 59.60           N  
ANISOU  840  N   PHE A 257     7550   7802   7293    443   -635    -88       N  
ATOM    841  CA  PHE A 257       5.831  19.660  17.065  1.00 60.61           C  
ANISOU  841  CA  PHE A 257     7637   7984   7407    491   -621    -56       C  
ATOM    842  C   PHE A 257       6.649  20.214  15.916  1.00 65.51           C  
ANISOU  842  C   PHE A 257     8246   8670   7977    500   -612    -87       C  
ATOM    843  O   PHE A 257       7.665  20.847  16.145  1.00 83.06           O  
ANISOU  843  O   PHE A 257    10519  10876  10165    475   -580   -103       O  
ATOM    844  CB  PHE A 257       4.786  20.689  17.479  1.00 66.35           C  
ANISOU  844  CB  PHE A 257     8408   8680   8123    515   -534     31       C  
ATOM    845  CG  PHE A 257       3.519  20.606  16.672  1.00 72.67           C  
ANISOU  845  CG  PHE A 257     9154   9527   8932    563   -536     77       C  
ATOM    846  CD1 PHE A 257       2.556  19.647  16.953  1.00 75.93           C  
ANISOU  846  CD1 PHE A 257     9525   9933   9392    572   -584     89       C  
ATOM    847  CD2 PHE A 257       3.311  21.462  15.604  1.00 75.35           C  
ANISOU  847  CD2 PHE A 257     9477   9923   9231    597   -491    110       C  
ATOM    848  CE1 PHE A 257       1.397  19.572  16.194  1.00 79.62           C  
ANISOU  848  CE1 PHE A 257     9941  10449   9863    614   -585    131       C  
ATOM    849  CE2 PHE A 257       2.145  21.399  14.856  1.00 77.31           C  
ANISOU  849  CE2 PHE A 257     9671  10222   9482    639   -490    156       C  
ATOM    850  CZ  PHE A 257       1.189  20.452  15.150  1.00 82.91           C  
ANISOU  850  CZ  PHE A 257    10343  10924  10234    647   -537    164       C  
ATOM    851  N   ASN A1001       6.183  19.975  14.688  1.00 76.64           N  
ANISOU  851  N   ASN A1001     9584  10157   9378    536   -641    -92       N  
ATOM    852  CA  ASN A1001       6.877  20.353  13.466  1.00 64.66           C  
ANISOU  852  CA  ASN A1001     8033   8723   7812    547   -645   -122       C  
ATOM    853  C   ASN A1001       5.894  20.269  12.289  1.00 66.57           C  
ANISOU  853  C   ASN A1001     8196   9051   8045    592   -655    -97       C  
ATOM    854  O   ASN A1001       4.678  20.113  12.478  1.00 56.65           O  
ANISOU  854  O   ASN A1001     6925   7782   6816    614   -645    -47       O  
ATOM    855  CB  ASN A1001       8.132  19.495  13.279  1.00 63.76           C  
ANISOU  855  CB  ASN A1001     7894   8630   7701    518   -720   -219       C  
ATOM    856  CG  ASN A1001       7.842  18.009  13.324  1.00 68.39           C  
ANISOU  856  CG  ASN A1001     8418   9217   8351    514   -810   -276       C  
ATOM    857  OD1 ASN A1001       6.789  17.582  12.885  1.00 84.06           O  
ANISOU  857  OD1 ASN A1001    10348  11232  10360    543   -830   -260       O  
ATOM    858  ND2 ASN A1001       8.730  17.213  13.903  1.00 79.27           N  
ANISOU  858  ND2 ASN A1001     9802  10557   9761    479   -862   -338       N  
ATOM    859  N   ILE A1002       6.442  20.367  11.067  1.00 57.80           N  
ANISOU  859  N   ILE A1002     7030   8038   6892    604   -676   -132       N  
ATOM    860  CA  ILE A1002       5.663  20.343   9.844  1.00 57.07           C  
ANISOU  860  CA  ILE A1002     6855   8051   6780    642   -684   -113       C  
ATOM    861  C   ILE A1002       5.008  18.973   9.675  1.00 62.59           C  
ANISOU  861  C   ILE A1002     7482   8771   7529    648   -763   -165       C  
ATOM    862  O   ILE A1002       3.877  18.886   9.199  1.00 74.68           O  
ANISOU  862  O   ILE A1002     8964  10347   9063    678   -758   -125       O  
ATOM    863  CB  ILE A1002       6.548  20.691   8.638  1.00 59.22           C  
ANISOU  863  CB  ILE A1002     7078   8431   6992    646   -695   -147       C  
ATOM    864  CG1 ILE A1002       5.765  20.690   7.324  1.00 59.04           C  
ANISOU  864  CG1 ILE A1002     6958   8535   6941    684   -703   -125       C  
ATOM    865  CG2 ILE A1002       7.728  19.736   8.565  1.00 60.85           C  
ANISOU  865  CG2 ILE A1002     7263   8650   7206    617   -775   -261       C  
ATOM    866  CD1 ILE A1002       4.567  21.593   7.333  1.00 60.95           C  
ANISOU  866  CD1 ILE A1002     7212   8770   7177    716   -625     -9       C  
ATOM    867  N   PHE A1003       5.716  17.903  10.058  1.00 58.16           N  
ANISOU  867  N   PHE A1003     6912   8177   7009    619   -836   -253       N  
ATOM    868  CA  PHE A1003       5.167  16.571   9.890  1.00 62.03           C  
ANISOU  868  CA  PHE A1003     7330   8680   7557    622   -914   -309       C  
ATOM    869  C   PHE A1003       3.946  16.378  10.777  1.00 70.46           C  
ANISOU  869  C   PHE A1003     8423   9675   8675    629   -898   -242       C  
ATOM    870  O   PHE A1003       3.024  15.652  10.417  1.00 80.45           O  
ANISOU  870  O   PHE A1003     9624  10970   9973    646   -936   -248       O  
ATOM    871  CB  PHE A1003       6.198  15.506  10.242  1.00 70.64           C  
ANISOU  871  CB  PHE A1003     8411   9735   8694    588   -990   -408       C  
ATOM    872  CG  PHE A1003       7.420  15.538   9.363  1.00 83.82           C  
ANISOU  872  CG  PHE A1003    10048  11480  10318    581  -1018   -485       C  
ATOM    873  CD1 PHE A1003       7.416  14.908   8.124  1.00 79.28           C  
ANISOU  873  CD1 PHE A1003     9372  11015   9736    597  -1074   -560       C  
ATOM    874  CD2 PHE A1003       8.571  16.194   9.782  1.00 82.87           C  
ANISOU  874  CD2 PHE A1003     9997  11329  10161    556   -987   -486       C  
ATOM    875  CE1 PHE A1003       8.535  14.942   7.309  1.00 75.40           C  
ANISOU  875  CE1 PHE A1003     8847  10603   9199    591  -1100   -631       C  
ATOM    876  CE2 PHE A1003       9.692  16.221   8.964  1.00 77.88           C  
ANISOU  876  CE2 PHE A1003     9334  10773   9483    550  -1014   -554       C  
ATOM    877  CZ  PHE A1003       9.672  15.592   7.739  1.00 79.19           C  
ANISOU  877  CZ  PHE A1003     9398  11049   9641    568  -1071   -626       C  
ATOM    878  N   GLU A1004       3.957  17.006  11.956  1.00 77.32           N  
ANISOU  878  N   GLU A1004     9381  10449   9547    614   -842   -181       N  
ATOM    879  CA  GLU A1004       2.840  16.879  12.879  1.00 75.31           C  
ANISOU  879  CA  GLU A1004     9152  10127   9334    619   -824   -115       C  
ATOM    880  C   GLU A1004       1.719  17.821  12.445  1.00 73.34           C  
ANISOU  880  C   GLU A1004     8904   9915   9047    659   -753    -23       C  
ATOM    881  O   GLU A1004       0.547  17.521  12.676  1.00 67.69           O  
ANISOU  881  O   GLU A1004     8170   9188   8360    677   -755     24       O  
ATOM    882  CB  GLU A1004       3.290  17.098  14.326  1.00 74.23           C  
ANISOU  882  CB  GLU A1004     9101   9888   9216    585   -797    -94       C  
ATOM    883  CG  GLU A1004       4.386  16.145  14.756  1.00 82.84           C  
ANISOU  883  CG  GLU A1004    10184  10945  10345    546   -866   -176       C  
ATOM    884  CD  GLU A1004       4.157  14.672  14.466  1.00100.22           C  
ANISOU  884  CD  GLU A1004    12303  13160  12617    545   -962   -238       C  
ATOM    885  OE1 GLU A1004       3.024  14.204  14.687  1.00117.02           O  
ANISOU  885  OE1 GLU A1004    14403  15273  14787    559   -977   -200       O  
ATOM    886  OE2 GLU A1004       5.112  13.995  14.002  1.00120.75           O1-
ANISOU  886  OE2 GLU A1004    14863  15785  15232    530  -1022   -325       O1-
ATOM    887  N   MET A1005       2.107  18.953  11.834  1.00 69.13           N  
ANISOU  887  N   MET A1005     8389   9425   8453    672   -692      6       N  
ATOM    888  CA  MET A1005       1.166  19.937  11.332  1.00 68.80           C  
ANISOU  888  CA  MET A1005     8342   9422   8375    710   -621     98       C  
ATOM    889  C   MET A1005       0.369  19.330  10.179  1.00 84.40           C  
ANISOU  889  C   MET A1005    10218  11504  10347    739   -663     89       C  
ATOM    890  O   MET A1005      -0.858  19.443  10.173  1.00 96.37           O  
ANISOU  890  O   MET A1005    11718  13028  11869    766   -637    158       O  
ATOM    891  CB  MET A1005       1.898  21.190  10.850  1.00 60.04           C  
ANISOU  891  CB  MET A1005     7262   8341   7211    714   -556    126       C  
ATOM    892  CG  MET A1005       0.989  22.300  10.349  1.00 55.20           C  
ANISOU  892  CG  MET A1005     6643   7762   6568    754   -475    230       C  
ATOM    893  SD  MET A1005       1.990  23.580   9.614  1.00 71.47           S  
ANISOU  893  SD  MET A1005     8715   9867   8572    755   -418    253       S  
ATOM    894  CE  MET A1005       0.850  24.949   9.432  1.00 82.74           C  
ANISOU  894  CE  MET A1005    10155  11294   9990    799   -310    393       C  
ATOM    895  N   LEU A1006       1.060  18.698   9.211  1.00 80.25           N  
ANISOU  895  N   LEU A1006     9620  11063   9807    732   -727      2       N  
ATOM    896  CA  LEU A1006       0.406  18.142   8.036  1.00 79.43           C  
ANISOU  896  CA  LEU A1006     9412  11075   9692    756   -767    -19       C  
ATOM    897  C   LEU A1006      -0.435  16.922   8.385  1.00 89.55           C  
ANISOU  897  C   LEU A1006    10657  12329  11038    754   -829    -47       C  
ATOM    898  O   LEU A1006      -1.451  16.700   7.726  1.00118.71           O  
ANISOU  898  O   LEU A1006    14285  16094  14726    778   -835    -23       O  
ATOM    899  CB  LEU A1006       1.425  17.764   6.963  1.00 73.44           C  
ANISOU  899  CB  LEU A1006     8585  10416   8902    747   -820   -115       C  
ATOM    900  CG  LEU A1006       2.010  18.915   6.155  1.00 77.25           C  
ANISOU  900  CG  LEU A1006     9063  10978   9310    758   -767    -79       C  
ATOM    901  CD1 LEU A1006       3.154  18.412   5.297  1.00 67.40           C  
ANISOU  901  CD1 LEU A1006     7755   9818   8036    743   -830   -187       C  
ATOM    902  CD2 LEU A1006       0.949  19.637   5.322  1.00 72.16           C  
ANISOU  902  CD2 LEU A1006     8367  10426   8623    797   -713     15       C  
ATOM    903  N   ARG A1007      -0.004  16.122   9.372  1.00 84.77           N  
ANISOU  903  N   ARG A1007    10086  11627  10494    723   -876    -97       N  
ATOM    904  CA  ARG A1007      -0.750  14.915   9.726  1.00 75.11           C  
ANISOU  904  CA  ARG A1007     8823  10373   9343    719   -940   -122       C  
ATOM    905  C   ARG A1007      -2.133  15.293  10.254  1.00 69.26           C  
ANISOU  905  C   ARG A1007     8108   9600   8607    741   -892    -15       C  
ATOM    906  O   ARG A1007      -3.051  14.494  10.155  1.00 67.96           O  
ANISOU  906  O   ARG A1007     7891   9449   8481    749   -933    -16       O  
ATOM    907  CB  ARG A1007       0.019  13.976  10.669  1.00 64.08           C  
ANISOU  907  CB  ARG A1007     7450   8882   8017    681  -1002   -189       C  
ATOM    908  N   ILE A1008      -2.266  16.510  10.800  1.00 67.66           N  
ANISOU  908  N   ILE A1008     7984   9355   8367    751   -804     74       N  
ATOM    909  CA  ILE A1008      -3.533  16.984  11.333  1.00 61.82           C  
ANISOU  909  CA  ILE A1008     7274   8584   7629    774   -750    179       C  
ATOM    910  C   ILE A1008      -4.387  17.487  10.171  1.00 59.25           C  
ANISOU  910  C   ILE A1008     6890   8367   7255    813   -715    231       C  
ATOM    911  O   ILE A1008      -5.555  17.144  10.065  1.00 73.18           O  
ANISOU  911  O   ILE A1008     8618  10156   9032    833   -723    274       O  
ATOM    912  CB  ILE A1008      -3.342  18.055  12.431  1.00 60.74           C  
ANISOU  912  CB  ILE A1008     7241   8357   7480    768   -670    245       C  
ATOM    913  CG1 ILE A1008      -2.593  17.532  13.658  1.00 61.71           C  
ANISOU  913  CG1 ILE A1008     7416   8382   7648    727   -703    201       C  
ATOM    914  CG2 ILE A1008      -4.664  18.678  12.828  1.00 57.83           C  
ANISOU  914  CG2 ILE A1008     6897   7969   7106    799   -606    353       C  
ATOM    915  CD1 ILE A1008      -3.224  16.318  14.291  1.00 76.45           C  
ANISOU  915  CD1 ILE A1008     9253  10212   9582    716   -771    191       C  
ATOM    916  N   ASP A1009      -3.799  18.284   9.286  1.00 56.22           N  
ANISOU  916  N   ASP A1009     6493   8055   6814    824   -679    232       N  
ATOM    917  CA  ASP A1009      -4.577  18.922   8.242  1.00 61.78           C  
ANISOU  917  CA  ASP A1009     7143   8864   7468    860   -634    300       C  
ATOM    918  C   ASP A1009      -4.938  17.935   7.148  1.00 64.36           C  
ANISOU  918  C   ASP A1009     7357   9307   7792    865   -704    239       C  
ATOM    919  O   ASP A1009      -6.048  17.974   6.652  1.00 85.64           O  
ANISOU  919  O   ASP A1009    10002  12067  10470    892   -688    296       O  
ATOM    920  CB  ASP A1009      -3.853  20.126   7.656  1.00 75.65           C  
ANISOU  920  CB  ASP A1009     8913  10663   9168    869   -571    332       C  
ATOM    921  CG  ASP A1009      -3.685  21.267   8.642  1.00 83.46           C  
ANISOU  921  CG  ASP A1009    10007  11544  10159    868   -487    405       C  
ATOM    922  OD1 ASP A1009      -4.489  21.354   9.639  1.00 67.00           O  
ANISOU  922  OD1 ASP A1009     7976   9374   8107    874   -457    460       O  
ATOM    923  OD2 ASP A1009      -2.752  22.078   8.395  1.00 87.48           O1-
ANISOU  923  OD2 ASP A1009    10541  12059  10638    862   -451    404       O1-
ATOM    924  N   GLU A1010      -4.010  17.053   6.776  1.00 72.12           N  
ANISOU  924  N   GLU A1010     8297  10316   8790    840   -781    120       N  
ATOM    925  CA  GLU A1010      -4.213  16.140   5.663  1.00 76.43           C  
ANISOU  925  CA  GLU A1010     8729  10980   9332    843   -848     44       C  
ATOM    926  C   GLU A1010      -4.919  14.850   6.077  1.00 79.76           C  
ANISOU  926  C   GLU A1010     9120  11360   9826    832   -918      0       C  
ATOM    927  O   GLU A1010      -5.562  14.212   5.244  1.00 95.61           O  
ANISOU  927  O   GLU A1010    11035  13462  11832    841   -956    -32       O  
ATOM    928  CB  GLU A1010      -2.889  15.838   4.982  1.00 81.88           C  
ANISOU  928  CB  GLU A1010     9380  11727  10004    823   -895    -67       C  
ATOM    929  CG  GLU A1010      -2.322  17.060   4.297  1.00104.80           C  
ANISOU  929  CG  GLU A1010    12287  14705  12829    836   -833    -21       C  
ATOM    930  CD  GLU A1010      -3.045  17.514   3.035  1.00113.13           C  
ANISOU  930  CD  GLU A1010    13250  15915  13819    865   -803     31       C  
ATOM    931  OE1 GLU A1010      -3.915  16.779   2.559  1.00127.24           O  
ANISOU  931  OE1 GLU A1010    14961  17768  15616    874   -839     11       O  
ATOM    932  OE2 GLU A1010      -2.720  18.609   2.519  1.00112.38           O1-
ANISOU  932  OE2 GLU A1010    13157  15879  13665    879   -744     93       O1-
ATOM    933  N   GLY A1011      -4.789  14.453   7.344  1.00 69.80           N  
ANISOU  933  N   GLY A1011     7928   9965   8629    812   -935     -1       N  
ATOM    934  CA  GLY A1011      -5.418  13.233   7.822  1.00 71.71           C  
ANISOU  934  CA  GLY A1011     8141  10158   8949    800  -1003    -34       C  
ATOM    935  C   GLY A1011      -4.686  11.988   7.321  1.00 75.26           C  
ANISOU  935  C   GLY A1011     8516  10633   9448    776  -1098   -174       C  
ATOM    936  O   GLY A1011      -3.623  12.104   6.706  1.00 87.67           O  
ANISOU  936  O   GLY A1011    10068  12253  10990    768  -1110   -245       O  
ATOM    937  N   LEU A1012      -5.231  10.809   7.647  1.00 79.44           N  
ANISOU  937  N   LEU A1012     9005  11121  10059    765  -1166   -211       N  
ATOM    938  CA  LEU A1012      -4.624   9.541   7.264  1.00 93.31           C  
ANISOU  938  CA  LEU A1012    10688  12884  11883    742  -1258   -344       C  
ATOM    939  C   LEU A1012      -5.638   8.661   6.546  1.00 91.16           C  
ANISOU  939  C   LEU A1012    10316  12681  11641    750  -1307   -380       C  
ATOM    940  O   LEU A1012      -6.751   8.470   7.031  1.00 99.61           O  
ANISOU  940  O   LEU A1012    11391  13716  12739    758  -1303   -309       O  
ATOM    941  CB  LEU A1012      -4.076   8.796   8.489  1.00100.01           C  
ANISOU  941  CB  LEU A1012    11580  13592  12825    712  -1305   -369       C  
ATOM    942  CG  LEU A1012      -3.382   7.460   8.175  1.00100.45           C  
ANISOU  942  CG  LEU A1012    11561  13638  12967    688  -1401   -507       C  
ATOM    943  CD1 LEU A1012      -2.189   7.662   7.246  1.00 93.35           C  
ANISOU  943  CD1 LEU A1012    10633  12819  12019    685  -1408   -602       C  
ATOM    944  CD2 LEU A1012      -2.985   6.686   9.425  1.00 91.48           C  
ANISOU  944  CD2 LEU A1012    10460  12365  11933    659  -1446   -513       C  
ATOM    945  N   ARG A1013      -5.211   8.115   5.404  1.00 88.13           N  
ANISOU  945  N   ARG A1013     9837  12397  11251    746  -1353   -496       N  
ATOM    946  CA  ARG A1013      -6.020   7.162   4.674  1.00 95.02           C  
ANISOU  946  CA  ARG A1013    10605  13339  12161    748  -1408   -557       C  
ATOM    947  C   ARG A1013      -5.290   5.830   4.599  1.00 97.04           C  
ANISOU  947  C   ARG A1013    10799  13554  12517    721  -1502   -703       C  
ATOM    948  O   ARG A1013      -4.100   5.759   4.292  1.00 99.61           O  
ANISOU  948  O   ARG A1013    11115  13893  12838    709  -1522   -791       O  
ATOM    949  CB  ARG A1013      -6.321   7.667   3.266  1.00 95.16           C  
ANISOU  949  CB  ARG A1013    10544  13533  12079    768  -1379   -569       C  
ATOM    950  CG  ARG A1013      -7.207   8.898   3.218  1.00 89.60           C  
ANISOU  950  CG  ARG A1013     9881  12878  11284    798  -1288   -421       C  
ATOM    951  CD  ARG A1013      -7.611   9.164   1.781  1.00 94.57           C  
ANISOU  951  CD  ARG A1013    10409  13693  11830    814  -1272   -437       C  
ATOM    952  NE  ARG A1013      -8.581  10.240   1.779  1.00 82.78           N  
ANISOU  952  NE  ARG A1013     8948  12239  10264    843  -1188   -288       N  
ATOM    953  CZ  ARG A1013      -9.877  10.065   1.967  1.00 93.77           C  
ANISOU  953  CZ  ARG A1013    10329  13630  11668    855  -1178   -217       C  
ATOM    954  NH1 ARG A1013     -10.372   8.848   2.126  1.00101.13           N  
ANISOU  954  NH1 ARG A1013    11214  14530  12681    839  -1250   -283       N  
ATOM    955  NH2 ARG A1013     -10.679  11.115   1.977  1.00114.84           N  
ANISOU  955  NH2 ARG A1013    13030  16332  14271    884  -1097    -78       N  
ATOM    956  N   LEU A1014      -6.063   4.782   4.868  1.00100.98           N  
ANISOU  956  N   LEU A1014    11253  14006  13110    711  -1557   -724       N  
ATOM    957  CA  LEU A1014      -5.585   3.423   4.758  1.00115.68           C  
ANISOU  957  CA  LEU A1014    13041  15826  15085    687  -1649   -860       C  
ATOM    958  C   LEU A1014      -5.813   2.885   3.343  1.00127.08           C  
ANISOU  958  C   LEU A1014    14359  17412  16512    690  -1685   -977       C  
ATOM    959  O   LEU A1014      -4.960   2.157   2.851  1.00112.90           O  
ANISOU  959  O   LEU A1014    12506  15627  14763    673  -1736  -1111       O  
ATOM    960  CB  LEU A1014      -6.276   2.571   5.824  1.00133.30           C  
ANISOU  960  CB  LEU A1014    15286  17927  17434    673  -1691   -817       C  
ATOM    961  CG  LEU A1014      -5.487   1.346   6.284  1.00160.39           C  
ANISOU  961  CG  LEU A1014    18686  21251  21004    645  -1774   -918       C  
ATOM    962  CD1 LEU A1014      -4.333   1.756   7.197  1.00147.37           C  
ANISOU  962  CD1 LEU A1014    17127  19509  19357    632  -1756   -891       C  
ATOM    963  CD2 LEU A1014      -6.397   0.359   7.001  1.00177.20           C  
ANISOU  963  CD2 LEU A1014    20789  23285  23253    633  -1826   -887       C  
ATOM    964  N   LYS A1015      -6.950   3.224   2.703  1.00136.62           N  
ANISOU  964  N   LYS A1015    15527  18729  17655    709  -1652   -925       N  
ATOM    965  CA  LYS A1015      -7.301   2.695   1.386  1.00124.60           C  
ANISOU  965  CA  LYS A1015    13885  17345  16112    705  -1677  -1026       C  
ATOM    966  C   LYS A1015      -7.327   3.812   0.342  1.00130.97           C  
ANISOU  966  C   LYS A1015    14665  18327  16770    729  -1615   -993       C  
ATOM    967  O   LYS A1015      -7.491   4.978   0.691  1.00142.72           O  
ANISOU  967  O   LYS A1015    16232  19816  18180    750  -1542   -862       O  
ATOM    968  CB  LYS A1015      -8.650   1.973   1.412  1.00112.74           C  
ANISOU  968  CB  LYS A1015    12342  15830  14663    698  -1695  -1000       C  
ATOM    969  CG  LYS A1015      -8.759   0.825   2.404  1.00121.56           C  
ANISOU  969  CG  LYS A1015    13478  16778  15930    672  -1754  -1018       C  
ATOM    970  CD  LYS A1015     -10.180   0.320   2.611  1.00135.42           C  
ANISOU  970  CD  LYS A1015    15203  18520  17729    672  -1770   -961       C  
ATOM    971  CE  LYS A1015     -10.297  -0.929   3.464  1.00123.47           C  
ANISOU  971  CE  LYS A1015    13698  16847  16368    641  -1825   -981       C  
ATOM    972  NZ  LYS A1015     -11.639  -0.985   4.109  1.00109.80           N  
ANISOU  972  NZ  LYS A1015    11967  15089  14665    655  -1838   -873       N  
ATOM    973  N   ILE A1016      -7.174   3.432  -0.937  1.00124.52           N  
ANISOU  973  N   ILE A1016    13791  17605  15917    703  -1596  -1079       N  
ATOM    974  CA  ILE A1016      -7.206   4.376  -2.045  1.00115.23           C  
ANISOU  974  CA  ILE A1016    12578  16598  14605    718  -1535  -1050       C  
ATOM    975  C   ILE A1016      -8.602   4.978  -2.122  1.00113.70           C  
ANISOU  975  C   ILE A1016    12359  16491  14351    748  -1501   -929       C  
ATOM    976  O   ILE A1016      -9.607   4.281  -1.963  1.00112.92           O  
ANISOU  976  O   ILE A1016    12235  16361  14307    739  -1523   -922       O  
ATOM    977  CB  ILE A1016      -6.797   3.728  -3.382  1.00110.72           C  
ANISOU  977  CB  ILE A1016    11949  16105  14016    683  -1525  -1171       C  
ATOM    978  CG1 ILE A1016      -5.418   3.080  -3.276  1.00124.16           C  
ANISOU  978  CG1 ILE A1016    13679  17717  15780    658  -1556  -1286       C  
ATOM    979  CG2 ILE A1016      -6.871   4.719  -4.545  1.00109.98           C  
ANISOU  979  CG2 ILE A1016    11815  16191  13782    696  -1461  -1131       C  
ATOM    980  CD1 ILE A1016      -5.083   2.184  -4.445  1.00144.31           C  
ANISOU  980  CD1 ILE A1016    16175  20318  18339    628  -1553  -1416       C  
ATOM    981  N   TYR A1017      -8.630   6.288  -2.361  1.00107.00           N  
ANISOU  981  N   TYR A1017    11517  15750  13388    783  -1444   -829       N  
ATOM    982  CA  TYR A1017      -9.884   7.014  -2.388  1.00102.36           C  
ANISOU  982  CA  TYR A1017    10927  15228  12736    812  -1388   -687       C  
ATOM    983  C   TYR A1017      -9.869   8.057  -3.498  1.00107.04           C  
ANISOU  983  C   TYR A1017    11467  16008  13196    830  -1326   -636       C  
ATOM    984  O   TYR A1017      -8.874   8.759  -3.662  1.00 99.22           O  
ANISOU  984  O   TYR A1017    10504  15037  12157    835  -1300   -634       O  
ATOM    985  CB  TYR A1017     -10.111   7.686  -1.038  1.00 88.46           C  
ANISOU  985  CB  TYR A1017     9310  13303  11000    824  -1338   -544       C  
ATOM    986  CG  TYR A1017     -11.443   8.367  -0.932  1.00 85.14           C  
ANISOU  986  CG  TYR A1017     8908  12914  10527    849  -1273   -392       C  
ATOM    987  CD1 TYR A1017     -12.609   7.644  -0.731  1.00 87.74           C  
ANISOU  987  CD1 TYR A1017     9207  13227  10904    846  -1300   -376       C  
ATOM    988  CD2 TYR A1017     -11.524   9.744  -1.016  1.00 84.48           C  
ANISOU  988  CD2 TYR A1017     8874  12873  10353    876  -1183   -261       C  
ATOM    989  CE1 TYR A1017     -13.837   8.280  -0.609  1.00 94.85           C  
ANISOU  989  CE1 TYR A1017    10128  14157  11755    871  -1239   -232       C  
ATOM    990  CE2 TYR A1017     -12.741  10.396  -0.901  1.00 88.81           C  
ANISOU  990  CE2 TYR A1017     9440  13446  10858    901  -1119   -117       C  
ATOM    991  CZ  TYR A1017     -13.902   9.662  -0.705  1.00 94.23           C  
ANISOU  991  CZ  TYR A1017    10097  14122  11585    899  -1148   -103       C  
ATOM    992  OH  TYR A1017     -15.099  10.309  -0.589  1.00102.07           O  
ANISOU  992  OH  TYR A1017    11108  15142  12533    925  -1085     41       O  
ATOM    993  N   LYS A1018     -10.991   8.152  -4.232  1.00107.22           N  
ANISOU  993  N   LYS A1018    11434  16138  13165    832  -1287   -582       N  
ATOM    994  CA  LYS A1018     -11.170   9.167  -5.263  1.00 91.80           C  
ANISOU  994  CA  LYS A1018     9441  14348  11091    844  -1212   -505       C  
ATOM    995  C   LYS A1018     -11.813  10.386  -4.616  1.00 79.87           C  
ANISOU  995  C   LYS A1018     7984  12830   9532    891  -1147   -317       C  
ATOM    996  O   LYS A1018     -12.960  10.343  -4.195  1.00 78.34           O  
ANISOU  996  O   LYS A1018     7812  12599   9353    901  -1127   -230       O  
ATOM    997  CB  LYS A1018     -11.995   8.661  -6.453  1.00 89.06           C  
ANISOU  997  CB  LYS A1018     9016  14115  10709    816  -1193   -542       C  
ATOM    998  N   ASP A1019     -11.050  11.473  -4.543  1.00 98.85           N  
ANISOU  998  N   ASP A1019    10447  15225  11888    904  -1092   -249       N  
ATOM    999  CA  ASP A1019     -11.453  12.658  -3.807  1.00127.86           C  
ANISOU  999  CA  ASP A1019    14227  18813  15540    932  -1005    -75       C  
ATOM   1000  C   ASP A1019     -12.352  13.516  -4.693  1.00128.18           C  
ANISOU 1000  C   ASP A1019    14198  19020  15484    957   -935     47       C  
ATOM   1001  O   ASP A1019     -12.517  13.197  -5.869  1.00122.82           O  
ANISOU 1001  O   ASP A1019    13389  18527  14750    951   -957     -9       O  
ATOM   1002  CB  ASP A1019     -10.229  13.379  -3.236  1.00146.96           C  
ANISOU 1002  CB  ASP A1019    16744  21129  17965    931   -980    -63       C  
ATOM   1003  CG  ASP A1019     -10.533  14.261  -2.031  1.00141.84           C  
ANISOU 1003  CG  ASP A1019    16232  20321  17340    949   -911     76       C  
ATOM   1004  OD1 ASP A1019     -11.736  14.436  -1.696  1.00133.28           O  
ANISOU 1004  OD1 ASP A1019    15165  19217  16258    968   -875    179       O  
ATOM   1005  OD2 ASP A1019      -9.563  14.828  -1.472  1.00139.73           O1-
ANISOU 1005  OD2 ASP A1019    16049  19959  17082    946   -890     84       O1-
ATOM   1006  N   THR A1020     -12.922  14.579  -4.097  1.00130.77           N  
ANISOU 1006  N   THR A1020    14610  19281  15797    986   -852    212       N  
ATOM   1007  CA  THR A1020     -13.889  15.481  -4.713  1.00104.63           C  
ANISOU 1007  CA  THR A1020    11251  16095  12409   1015   -775    358       C  
ATOM   1008  C   THR A1020     -13.352  16.028  -6.035  1.00110.88           C  
ANISOU 1008  C   THR A1020    11934  17086  13110   1017   -756    354       C  
ATOM   1009  O   THR A1020     -14.147  16.264  -6.942  1.00123.71           O  
ANISOU 1009  O   THR A1020    13458  18881  14666   1029   -726    417       O  
ATOM   1010  CB  THR A1020     -14.352  16.576  -3.736  1.00 83.72           C  
ANISOU 1010  CB  THR A1020     8724  13313   9774   1045   -689    522       C  
ATOM   1011  N   GLU A1021     -12.020  16.175  -6.159  1.00120.59           N  
ANISOU 1011  N   GLU A1021    13177  18305  14337   1004   -776    279       N  
ATOM   1012  CA  GLU A1021     -11.408  16.878  -7.285  1.00115.39           C  
ANISOU 1012  CA  GLU A1021    12430  17821  13592   1008   -751    296       C  
ATOM   1013  C   GLU A1021     -11.236  15.963  -8.498  1.00 99.39           C  
ANISOU 1013  C   GLU A1021    10295  15937  11532    968   -798    152       C  
ATOM   1014  O   GLU A1021     -10.976  16.453  -9.591  1.00 90.34           O  
ANISOU 1014  O   GLU A1021     9097  14916  10312    953   -755    167       O  
ATOM   1015  CB  GLU A1021     -10.053  17.484  -6.905  1.00119.21           C  
ANISOU 1015  CB  GLU A1021    12993  18214  14087   1004   -741    282       C  
ATOM   1016  CG  GLU A1021     -10.075  18.359  -5.667  1.00136.73           C  
ANISOU 1016  CG  GLU A1021    15365  20233  16354   1021   -676    398       C  
ATOM   1017  CD  GLU A1021     -10.074  17.627  -4.336  1.00136.58           C  
ANISOU 1017  CD  GLU A1021    15460  20005  16431   1008   -715    339       C  
ATOM   1018  OE1 GLU A1021      -9.469  16.527  -4.264  1.00118.01           O  
ANISOU 1018  OE1 GLU A1021    13093  17626  14119    979   -799    187       O  
ATOM   1019  OE2 GLU A1021     -10.701  18.157  -3.378  1.00159.67           O1-
ANISOU 1019  OE2 GLU A1021    18483  22797  19389   1025   -661    448       O1-
ATOM   1020  N   GLY A1022     -11.358  14.643  -8.290  1.00 98.59           N  
ANISOU 1020  N   GLY A1022    10194  15769  11495    938   -868     11       N  
ATOM   1021  CA  GLY A1022     -11.078  13.662  -9.327  1.00 93.44           C  
ANISOU 1021  CA  GLY A1022     9487  15179  10837    887   -900   -146       C  
ATOM   1022  C   GLY A1022      -9.740  12.947  -9.131  1.00111.99           C  
ANISOU 1022  C   GLY A1022    11865  17443  13242    860   -966   -305       C  
ATOM   1023  O   GLY A1022      -9.423  12.028  -9.883  1.00118.22           O  
ANISOU 1023  O   GLY A1022    12618  18259  14042    821   -995   -444       O  
ATOM   1024  N   TYR A1023      -8.954  13.362  -8.124  1.00122.57           N  
ANISOU 1024  N   TYR A1023    13274  18679  14618    883   -985   -282       N  
ATOM   1025  CA  TYR A1023      -7.633  12.795  -7.875  1.00112.16           C  
ANISOU 1025  CA  TYR A1023    11991  17277  13349    859  -1042   -418       C  
ATOM   1026  C   TYR A1023      -7.754  11.622  -6.913  1.00 97.65           C  
ANISOU 1026  C   TYR A1023    10190  15288  11623    848  -1116   -511       C  
ATOM   1027  O   TYR A1023      -8.456  11.734  -5.915  1.00 97.24           O  
ANISOU 1027  O   TYR A1023    10175  15163  11610    877  -1123   -430       O  
ATOM   1028  CB  TYR A1023      -6.707  13.849  -7.261  1.00123.35           C  
ANISOU 1028  CB  TYR A1023    13462  18660  14744    888  -1026   -345       C  
ATOM   1029  CG  TYR A1023      -6.404  15.010  -8.174  1.00139.88           C  
ANISOU 1029  CG  TYR A1023    15520  20889  16738    897   -957   -256       C  
ATOM   1030  CD1 TYR A1023      -5.358  14.961  -9.090  1.00145.76           C  
ANISOU 1030  CD1 TYR A1023    16240  21700  17443    866   -958   -343       C  
ATOM   1031  CD2 TYR A1023      -7.175  16.159  -8.132  1.00137.09           C  
ANISOU 1031  CD2 TYR A1023    15159  20595  16334    937   -888    -77       C  
ATOM   1032  CE1 TYR A1023      -5.074  16.031  -9.926  1.00138.54           C  
ANISOU 1032  CE1 TYR A1023    15291  20910  16440    873   -896   -255       C  
ATOM   1033  CE2 TYR A1023      -6.912  17.232  -8.971  1.00140.11           C  
ANISOU 1033  CE2 TYR A1023    15505  21097  16634    943   -823     15       C  
ATOM   1034  CZ  TYR A1023      -5.867  17.165  -9.874  1.00135.76           C  
ANISOU 1034  CZ  TYR A1023    14927  20614  16043    910   -829    -75       C  
ATOM   1035  OH  TYR A1023      -5.632  18.245 -10.672  1.00140.76           O  
ANISOU 1035  OH  TYR A1023    15522  21364  16597    916   -766     25       O  
ATOM   1036  N   TYR A1024      -7.054  10.522  -7.212  1.00 95.42           N  
ANISOU 1036  N   TYR A1024     9900  14960  11396    807  -1167   -672       N  
ATOM   1037  CA  TYR A1024      -6.949   9.423  -6.269  1.00106.08           C  
ANISOU 1037  CA  TYR A1024    11289  16153  12864    793  -1238   -761       C  
ATOM   1038  C   TYR A1024      -5.849   9.723  -5.250  1.00113.15           C  
ANISOU 1038  C   TYR A1024    12260  16937  13796    804  -1266   -767       C  
ATOM   1039  O   TYR A1024      -4.734  10.113  -5.605  1.00125.59           O  
ANISOU 1039  O   TYR A1024    13847  18540  15333    797  -1256   -801       O  
ATOM   1040  CB  TYR A1024      -6.731   8.085  -6.977  1.00119.77           C  
ANISOU 1040  CB  TYR A1024    12982  17874  14651    748  -1275   -920       C  
ATOM   1041  CG  TYR A1024      -7.912   7.565  -7.760  1.00149.61           C  
ANISOU 1041  CG  TYR A1024    16694  21736  18416    734  -1261   -928       C  
ATOM   1042  CD1 TYR A1024      -8.132   7.949  -9.076  1.00161.13           C  
ANISOU 1042  CD1 TYR A1024    18089  23359  19775    727  -1208   -919       C  
ATOM   1043  CD2 TYR A1024      -8.791   6.645  -7.204  1.00155.74           C  
ANISOU 1043  CD2 TYR A1024    17468  22427  19279    726  -1302   -949       C  
ATOM   1044  CE1 TYR A1024      -9.208   7.462  -9.809  1.00158.44           C  
ANISOU 1044  CE1 TYR A1024    17685  23098  19415    713  -1195   -931       C  
ATOM   1045  CE2 TYR A1024      -9.878   6.158  -7.917  1.00147.61           C  
ANISOU 1045  CE2 TYR A1024    16376  21473  18235    712  -1290   -958       C  
ATOM   1046  CZ  TYR A1024     -10.080   6.556  -9.228  1.00144.35           C  
ANISOU 1046  CZ  TYR A1024    15902  21227  17719    706  -1236   -953       C  
ATOM   1047  OH  TYR A1024     -11.133   6.063  -9.941  1.00133.64           O  
ANISOU 1047  OH  TYR A1024    14485  19950  16344    691  -1224   -966       O  
ATOM   1048  N   THR A1025      -6.191   9.539  -3.969  1.00114.28           N  
ANISOU 1048  N   THR A1025    12454  16956  14012    824  -1301   -730       N  
ATOM   1049  CA  THR A1025      -5.318   9.881  -2.857  1.00104.24           C  
ANISOU 1049  CA  THR A1025    11309  15514  12782    819  -1290   -701       C  
ATOM   1050  C   THR A1025      -5.233   8.701  -1.897  1.00108.00           C  
ANISOU 1050  C   THR A1025    11822  15826  13386    797  -1358   -780       C  
ATOM   1051  O   THR A1025      -6.107   7.833  -1.897  1.00116.50           O  
ANISOU 1051  O   THR A1025    12850  16897  14519    792  -1397   -813       O  
ATOM   1052  CB  THR A1025      -5.811  11.141  -2.131  1.00111.96           C  
ANISOU 1052  CB  THR A1025    12396  16421  13724    841  -1198   -520       C  
ATOM   1053  OG1 THR A1025      -4.891  11.480  -1.094  1.00121.02           O  
ANISOU 1053  OG1 THR A1025    13660  17415  14907    832  -1187   -503       O  
ATOM   1054  CG2 THR A1025      -7.189  10.984  -1.524  1.00129.46           C  
ANISOU 1054  CG2 THR A1025    14639  18574  15978    852  -1180   -430       C  
ATOM   1055  N   ILE A1026      -4.179   8.706  -1.068  1.00111.67           N  
ANISOU 1055  N   ILE A1026    12373  16160  13896    784  -1370   -803       N  
ATOM   1056  CA  ILE A1026      -3.972   7.732  -0.006  1.00111.47           C  
ANISOU 1056  CA  ILE A1026    12395  15967  13992    763  -1427   -855       C  
ATOM   1057  C   ILE A1026      -2.887   8.243   0.936  1.00118.63           C  
ANISOU 1057  C   ILE A1026    13415  16749  14909    753  -1406   -825       C  
ATOM   1058  O   ILE A1026      -2.140   9.158   0.586  1.00111.00           O  
ANISOU 1058  O   ILE A1026    12472  15840  13863    760  -1364   -802       O  
ATOM   1059  CB  ILE A1026      -3.582   6.359  -0.584  1.00118.49           C  
ANISOU 1059  CB  ILE A1026    13179  16888  14954    742  -1520  -1031       C  
ATOM   1060  CG1 ILE A1026      -3.843   5.239   0.427  1.00135.89           C  
ANISOU 1060  CG1 ILE A1026    15407  18930  17297    724  -1578  -1062       C  
ATOM   1061  CG2 ILE A1026      -2.145   6.372  -1.083  1.00108.73           C  
ANISOU 1061  CG2 ILE A1026    11943  15677  13693    724  -1526  -1124       C  
ATOM   1062  CD1 ILE A1026      -3.636   3.861  -0.133  1.00148.44           C  
ANISOU 1062  CD1 ILE A1026    16942  20491  18968    685  -1619  -1195       C  
ATOM   1063  N   GLY A1027      -2.781   7.607   2.113  1.00119.33           N  
ANISOU 1063  N   GLY A1027    13565  16675  15099    736  -1438   -828       N  
ATOM   1064  CA  GLY A1027      -1.782   7.982   3.101  1.00118.98           C  
ANISOU 1064  CA  GLY A1027    13625  16511  15072    723  -1423   -803       C  
ATOM   1065  C   GLY A1027      -2.080   9.354   3.695  1.00107.24           C  
ANISOU 1065  C   GLY A1027    12241  14991  13516    739  -1329   -651       C  
ATOM   1066  O   GLY A1027      -3.222   9.640   4.038  1.00112.49           O  
ANISOU 1066  O   GLY A1027    12927  15637  14178    754  -1292   -552       O  
ATOM   1067  N   ILE A1028      -1.050  10.199   3.791  1.00114.38           N  
ANISOU 1067  N   ILE A1028    13204  15889  14367    736  -1291   -635       N  
ATOM   1068  CA  ILE A1028      -1.230  11.530   4.343  1.00117.88           C  
ANISOU 1068  CA  ILE A1028    13743  16295  14751    749  -1200   -501       C  
ATOM   1069  C   ILE A1028      -1.183  12.528   3.189  1.00107.57           C  
ANISOU 1069  C   ILE A1028    12396  15136  13339    771  -1149   -467       C  
ATOM   1070  O   ILE A1028      -0.136  13.110   2.890  1.00103.97           O  
ANISOU 1070  O   ILE A1028    11957  14712  12834    766  -1133   -486       O  
ATOM   1071  CB  ILE A1028      -0.201  11.850   5.455  1.00131.80           C  
ANISOU 1071  CB  ILE A1028    15612  17932  16536    727  -1185   -490       C  
ATOM   1072  CG1 ILE A1028      -0.196  10.819   6.592  1.00145.07           C  
ANISOU 1072  CG1 ILE A1028    17321  19478  18322    702  -1239   -519       C  
ATOM   1073  CG2 ILE A1028      -0.427  13.246   5.993  1.00108.00           C  
ANISOU 1073  CG2 ILE A1028    12690  14881  13464    741  -1089   -359       C  
ATOM   1074  CD1 ILE A1028       0.782   9.671   6.399  1.00164.15           C  
ANISOU 1074  CD1 ILE A1028    19685  21884  20802    678  -1325   -657       C  
ATOM   1075  N   GLY A1029      -2.336  12.702   2.537  1.00 88.36           N  
ANISOU 1075  N   GLY A1029     9905  12796  10873    795  -1126   -413       N  
ATOM   1076  CA  GLY A1029      -2.457  13.673   1.463  1.00 91.01           C  
ANISOU 1076  CA  GLY A1029    10194  13277  11111    818  -1072   -359       C  
ATOM   1077  C   GLY A1029      -1.559  13.367   0.267  1.00 86.32           C  
ANISOU 1077  C   GLY A1029     9503  12821  10473    810  -1118   -472       C  
ATOM   1078  O   GLY A1029      -1.051  14.290  -0.379  1.00 91.98           O  
ANISOU 1078  O   GLY A1029    10208  13629  11111    820  -1076   -437       O  
ATOM   1079  N   HIS A1030      -1.385  12.074  -0.038  1.00 77.62           N  
ANISOU 1079  N   HIS A1030     8327  11739   9424    793  -1203   -608       N  
ATOM   1080  CA  HIS A1030      -0.573  11.709  -1.186  1.00 97.21           C  
ANISOU 1080  CA  HIS A1030    10709  14360  11867    786  -1250   -728       C  
ATOM   1081  C   HIS A1030      -1.442  11.542  -2.427  1.00102.28           C  
ANISOU 1081  C   HIS A1030    11222  15182  12457    801  -1255   -742       C  
ATOM   1082  O   HIS A1030      -2.031  10.483  -2.634  1.00109.37           O  
ANISOU 1082  O   HIS A1030    12051  16097  13408    794  -1310   -821       O  
ATOM   1083  CB  HIS A1030       0.294  10.473  -0.912  1.00112.04           C  
ANISOU 1083  CB  HIS A1030    12572  16169  13830    760  -1337   -879       C  
ATOM   1084  CG  HIS A1030       1.194  10.133  -2.057  1.00108.48           C  
ANISOU 1084  CG  HIS A1030    12021  15860  13338    753  -1383  -1007       C  
ATOM   1085  ND1 HIS A1030       2.327  10.868  -2.376  1.00103.33           N  
ANISOU 1085  ND1 HIS A1030    11387  15258  12615    752  -1363  -1008       N  
ATOM   1086  CD2 HIS A1030       1.112   9.167  -2.988  1.00110.03           C  
ANISOU 1086  CD2 HIS A1030    12136  16117  13554    733  -1412  -1115       C  
ATOM   1087  CE1 HIS A1030       2.907  10.352  -3.436  1.00 95.53           C  
ANISOU 1087  CE1 HIS A1030    10337  14351  11608    731  -1376  -1110       C  
ATOM   1088  NE2 HIS A1030       2.192   9.304  -3.821  1.00102.57           N  
ANISOU 1088  NE2 HIS A1030    11181  15232  12557    715  -1393  -1171       N  
ATOM   1089  N   LEU A1031      -1.480  12.597  -3.251  1.00 92.57           N  
ANISOU 1089  N   LEU A1031     9959  14089  11126    819  -1198   -665       N  
ATOM   1090  CA  LEU A1031      -2.235  12.601  -4.491  1.00 87.93           C  
ANISOU 1090  CA  LEU A1031     9243  13695  10472    832  -1194   -664       C  
ATOM   1091  C   LEU A1031      -1.483  11.811  -5.554  1.00 74.81           C  
ANISOU 1091  C   LEU A1031     7506  12116   8801    800  -1233   -813       C  
ATOM   1092  O   LEU A1031      -0.293  11.977  -5.720  1.00 76.58           O  
ANISOU 1092  O   LEU A1031     7753  12337   9007    786  -1237   -861       O  
ATOM   1093  CB  LEU A1031      -2.450  14.056  -4.918  1.00 90.13           C  
ANISOU 1093  CB  LEU A1031     9528  14062  10655    856  -1106   -513       C  
ATOM   1094  CG  LEU A1031      -3.699  14.723  -4.338  1.00100.22           C  
ANISOU 1094  CG  LEU A1031    10866  15275  11938    878  -1034   -355       C  
ATOM   1095  CD1 LEU A1031      -3.545  15.028  -2.847  1.00113.59           C  
ANISOU 1095  CD1 LEU A1031    12714  16747  13698    876  -1006   -293       C  
ATOM   1096  CD2 LEU A1031      -4.042  15.982  -5.117  1.00 99.71           C  
ANISOU 1096  CD2 LEU A1031    10761  15346  11779    903   -956   -221       C  
ATOM   1097  N   LEU A1032      -2.193  10.943  -6.267  1.00 80.99           N  
ANISOU 1097  N   LEU A1032     8232  12937   9604    779  -1238   -873       N  
ATOM   1098  CA  LEU A1032      -1.587  10.158  -7.327  1.00100.05           C  
ANISOU 1098  CA  LEU A1032    10605  15394  12016    742  -1245  -1001       C  
ATOM   1099  C   LEU A1032      -1.854  10.843  -8.670  1.00117.36           C  
ANISOU 1099  C   LEU A1032    12729  17765  14098    744  -1184   -953       C  
ATOM   1100  O   LEU A1032      -1.219  11.846  -9.003  1.00123.95           O  
ANISOU 1100  O   LEU A1032    13567  18671  14856    754  -1147   -894       O  
ATOM   1101  CB  LEU A1032      -2.119   8.717  -7.255  1.00 97.65           C  
ANISOU 1101  CB  LEU A1032    10281  15014  11809    718  -1291  -1106       C  
ATOM   1102  CG  LEU A1032      -1.873   8.002  -5.922  1.00 93.91           C  
ANISOU 1102  CG  LEU A1032     9871  14359  11452    714  -1352  -1146       C  
ATOM   1103  CD1 LEU A1032      -2.709   6.748  -5.780  1.00104.96           C  
ANISOU 1103  CD1 LEU A1032    11244  15691  12946    696  -1390  -1209       C  
ATOM   1104  CD2 LEU A1032      -0.404   7.676  -5.721  1.00 91.04           C  
ANISOU 1104  CD2 LEU A1032     9550  13919  11121    695  -1377  -1236       C  
ATOM   1105  N   THR A1033      -2.810  10.310  -9.436  1.00133.19           N  
ANISOU 1105  N   THR A1033    14670  19843  16093    733  -1172   -975       N  
ATOM   1106  CA  THR A1033      -3.168  10.909 -10.712  1.00158.61           C  
ANISOU 1106  CA  THR A1033    17821  23236  19207    732  -1112   -927       C  
ATOM   1107  C   THR A1033      -4.685  11.083 -10.804  1.00180.53           C  
ANISOU 1107  C   THR A1033    20559  26072  21963    746  -1084   -834       C  
ATOM   1108  O   THR A1033      -5.450  10.328 -10.208  1.00172.35           O  
ANISOU 1108  O   THR A1033    19531  24954  21000    745  -1119   -857       O  
ATOM   1109  CB  THR A1033      -2.589  10.146 -11.916  1.00154.21           C  
ANISOU 1109  CB  THR A1033    17214  22749  18629    701  -1113  -1061       C  
ATOM   1110  OG1 THR A1033      -2.872   8.751 -11.787  1.00145.99           O  
ANISOU 1110  OG1 THR A1033    16165  21625  17678    680  -1161  -1184       O  
ATOM   1111  CG2 THR A1033      -1.105  10.370 -12.116  1.00134.37           C  
ANISOU 1111  CG2 THR A1033    14728  20231  16096    693  -1115  -1113       C  
ATOM   1112  N   LYS A1034      -5.089  12.094 -11.585  1.00179.29           N  
ANISOU 1112  N   LYS A1034    20357  26059  21704    759  -1019   -724       N  
ATOM   1113  CA  LYS A1034      -6.477  12.462 -11.824  1.00140.86           C  
ANISOU 1113  CA  LYS A1034    15450  21273  16797    774   -976   -613       C  
ATOM   1114  C   LYS A1034      -7.152  11.459 -12.766  1.00133.13           C  
ANISOU 1114  C   LYS A1034    14405  20365  15813    744   -982   -708       C  
ATOM   1115  O   LYS A1034      -8.367  11.508 -12.926  1.00127.55           O  
ANISOU 1115  O   LYS A1034    13666  19713  15086    750   -957   -639       O  
ATOM   1116  CB  LYS A1034      -6.527  13.890 -12.381  1.00127.24           C  
ANISOU 1116  CB  LYS A1034    13700  19676  14969    795   -902   -463       C  
ATOM   1117  CG  LYS A1034      -7.883  14.578 -12.363  1.00110.31           C  
ANISOU 1117  CG  LYS A1034    11532  17596  12786    822   -847   -306       C  
ATOM   1118  CD  LYS A1034      -7.807  16.026 -12.787  1.00108.74           C  
ANISOU 1118  CD  LYS A1034    11314  17500  12501    845   -773   -149       C  
ATOM   1119  CE  LYS A1034      -9.096  16.773 -12.528  1.00112.58           C  
ANISOU 1119  CE  LYS A1034    11792  18017  12967    878   -717     24       C  
ATOM   1120  NZ  LYS A1034     -10.163  16.290 -13.436  1.00121.42           N  
ANISOU 1120  NZ  LYS A1034    12846  19246  14044    857   -695     13       N  
ATOM   1121  N   SER A1035      -6.364  10.563 -13.386  1.00126.65           N  
ANISOU 1121  N   SER A1035    13567  19545  15011    713  -1012   -863       N  
ATOM   1122  CA  SER A1035      -6.851   9.585 -14.350  1.00125.54           C  
ANISOU 1122  CA  SER A1035    13362  19475  14863    686  -1016   -967       C  
ATOM   1123  C   SER A1035      -7.990   8.776 -13.742  1.00135.18           C  
ANISOU 1123  C   SER A1035    14583  20617  16160    683  -1049   -977       C  
ATOM   1124  O   SER A1035      -7.782   8.084 -12.751  1.00123.92           O  
ANISOU 1124  O   SER A1035    13206  19037  14840    682  -1106  -1033       O  
ATOM   1125  CB  SER A1035      -5.742   8.683 -14.813  1.00121.91           C  
ANISOU 1125  CB  SER A1035    12898  18988  14435    661  -1049  -1132       C  
ATOM   1126  OG  SER A1035      -4.737   9.443 -15.458  1.00132.71           O  
ANISOU 1126  OG  SER A1035    14259  20441  15723    662  -1015  -1118       O  
ATOM   1127  N   PRO A1036      -9.219   8.849 -14.309  1.00161.98           N  
ANISOU 1127  N   PRO A1036    17925  24117  19504    682  -1014   -920       N  
ATOM   1128  CA  PRO A1036     -10.375   8.143 -13.746  1.00164.72           C  
ANISOU 1128  CA  PRO A1036    18270  24397  19917    681  -1043   -916       C  
ATOM   1129  C   PRO A1036     -10.290   6.632 -13.943  1.00166.55           C  
ANISOU 1129  C   PRO A1036    18482  24567  20233    649  -1098  -1087       C  
ATOM   1130  O   PRO A1036     -11.031   6.071 -14.739  1.00161.12           O  
ANISOU 1130  O   PRO A1036    17735  23963  19522    630  -1087  -1133       O  
ATOM   1131  CB  PRO A1036     -11.555   8.727 -14.547  1.00170.26           C  
ANISOU 1131  CB  PRO A1036    18913  25258  20519    686   -979   -811       C  
ATOM   1132  CG  PRO A1036     -10.951   9.156 -15.877  1.00159.89           C  
ANISOU 1132  CG  PRO A1036    17549  24103  19100    673   -933   -835       C  
ATOM   1133  CD  PRO A1036      -9.560   9.630 -15.512  1.00163.25           C  
ANISOU 1133  CD  PRO A1036    18023  24467  19537    682   -944   -849       C  
ATOM   1134  N   SER A1037      -9.375   5.982 -13.216  1.00169.58           N  
ANISOU 1134  N   SER A1037    18915  24803  20715    642  -1154  -1179       N  
ATOM   1135  CA  SER A1037      -9.128   4.558 -13.369  1.00155.48           C  
ANISOU 1135  CA  SER A1037    17113  22944  19018    614  -1203  -1341       C  
ATOM   1136  C   SER A1037      -8.502   4.018 -12.090  1.00138.02           C  
ANISOU 1136  C   SER A1037    14972  20537  16931    616  -1265  -1380       C  
ATOM   1137  O   SER A1037      -7.319   4.238 -11.834  1.00129.67           O  
ANISOU 1137  O   SER A1037    13955  19429  15883    619  -1274  -1409       O  
ATOM   1138  CB  SER A1037      -8.250   4.281 -14.567  1.00162.92           C  
ANISOU 1138  CB  SER A1037    18013  23981  19908    598  -1185  -1455       C  
ATOM   1139  OG  SER A1037      -7.047   5.033 -14.500  1.00143.09           O  
ANISOU 1139  OG  SER A1037    15538  21469  17359    609  -1172  -1436       O  
ATOM   1140  N   LEU A1038      -9.323   3.327 -11.296  1.00131.13           N  
ANISOU 1140  N   LEU A1038    14112  19561  16152    612  -1306  -1375       N  
ATOM   1141  CA  LEU A1038      -8.881   2.723 -10.049  1.00136.64           C  
ANISOU 1141  CA  LEU A1038    14871  20072  16975    610  -1366  -1405       C  
ATOM   1142  C   LEU A1038      -7.825   1.654 -10.331  1.00152.22           C  
ANISOU 1142  C   LEU A1038    16840  21977  19018    587  -1399  -1566       C  
ATOM   1143  O   LEU A1038      -6.936   1.427  -9.507  1.00165.76           O  
ANISOU 1143  O   LEU A1038    18611  23563  20807    587  -1433  -1595       O  
ATOM   1144  CB  LEU A1038     -10.099   2.148  -9.318  1.00118.76           C  
ANISOU 1144  CB  LEU A1038    12605  17729  14788    608  -1398  -1366       C  
ATOM   1145  CG  LEU A1038      -9.825   1.520  -7.955  1.00116.28           C  
ANISOU 1145  CG  LEU A1038    12351  17222  14608    607  -1460  -1379       C  
ATOM   1146  CD1 LEU A1038      -9.284   2.561  -6.985  1.00122.48           C  
ANISOU 1146  CD1 LEU A1038    13207  17956  15375    636  -1454  -1278       C  
ATOM   1147  CD2 LEU A1038     -11.086   0.874  -7.405  1.00128.73           C  
ANISOU 1147  CD2 LEU A1038    13916  18739  16258    602  -1490  -1344       C  
ATOM   1148  N   ASN A1039      -7.931   1.019 -11.506  1.00155.59           N  
ANISOU 1148  N   ASN A1039    17201  22497  19418    568  -1384  -1667       N  
ATOM   1149  CA  ASN A1039      -7.010  -0.028 -11.919  1.00161.54           C  
ANISOU 1149  CA  ASN A1039    17941  23205  20232    551  -1408  -1823       C  
ATOM   1150  C   ASN A1039      -5.608   0.546 -12.115  1.00154.94           C  
ANISOU 1150  C   ASN A1039    17135  22386  19347    560  -1390  -1843       C  
ATOM   1151  O   ASN A1039      -4.626  -0.057 -11.678  1.00163.78           O  
ANISOU 1151  O   ASN A1039    18290  23392  20547    556  -1422  -1922       O  
ATOM   1152  CB  ASN A1039      -7.495  -0.753 -13.176  1.00172.41           C  
ANISOU 1152  CB  ASN A1039    19235  24693  21578    534  -1390  -1923       C  
ATOM   1153  CG  ASN A1039      -6.656  -1.971 -13.502  1.00180.65           C  
ANISOU 1153  CG  ASN A1039    20263  25673  22703    521  -1417  -2090       C  
ATOM   1154  OD1 ASN A1039      -5.958  -2.503 -12.638  1.00185.10           O  
ANISOU 1154  OD1 ASN A1039    20875  26083  23372    521  -1458  -2128       O  
ATOM   1155  ND2 ASN A1039      -6.724  -2.420 -14.744  1.00174.12           N  
ANISOU 1155  ND2 ASN A1039    19365  24966  21827    512  -1392  -2189       N  
ATOM   1156  N   ALA A1040      -5.537   1.713 -12.768  1.00137.25           N  
ANISOU 1156  N   ALA A1040    14881  20290  16978    572  -1337  -1766       N  
ATOM   1157  CA  ALA A1040      -4.271   2.368 -13.056  1.00139.39           C  
ANISOU 1157  CA  ALA A1040    15175  20598  17189    580  -1315  -1772       C  
ATOM   1158  C   ALA A1040      -3.757   3.125 -11.831  1.00147.25           C  
ANISOU 1158  C   ALA A1040    16251  21487  18210    596  -1330  -1679       C  
ATOM   1159  O   ALA A1040      -2.549   3.280 -11.669  1.00161.03           O  
ANISOU 1159  O   ALA A1040    18034  23191  19959    598  -1335  -1711       O  
ATOM   1160  CB  ALA A1040      -4.391   3.257 -14.272  1.00129.52           C  
ANISOU 1160  CB  ALA A1040    13872  19544  15797    585  -1252  -1727       C  
ATOM   1161  N   ALA A1041      -4.676   3.585 -10.970  1.00159.77           N  
ANISOU 1161  N   ALA A1041    17863  23032  19811    609  -1336  -1564       N  
ATOM   1162  CA  ALA A1041      -4.299   4.287  -9.751  1.00155.72           C  
ANISOU 1162  CA  ALA A1041    17425  22420  19323    628  -1351  -1475       C  
ATOM   1163  C   ALA A1041      -3.588   3.346  -8.777  1.00153.43           C  
ANISOU 1163  C   ALA A1041    17185  21949  19160    616  -1409  -1555       C  
ATOM   1164  O   ALA A1041      -2.635   3.769  -8.122  1.00158.86           O  
ANISOU 1164  O   ALA A1041    17931  22569  19858    624  -1418  -1539       O  
ATOM   1165  CB  ALA A1041      -5.501   4.945  -9.122  1.00142.51           C  
ANISOU 1165  CB  ALA A1041    15760  20754  17635    649  -1340  -1338       C  
ATOM   1166  N   LYS A1042      -4.051   2.085  -8.691  1.00144.87           N  
ANISOU 1166  N   LYS A1042    16079  20791  18175    598  -1446  -1639       N  
ATOM   1167  CA  LYS A1042      -3.422   1.078  -7.845  1.00144.58           C  
ANISOU 1167  CA  LYS A1042    16082  20585  18268    585  -1499  -1716       C  
ATOM   1168  C   LYS A1042      -2.036   0.717  -8.383  1.00155.05           C  
ANISOU 1168  C   LYS A1042    17410  21909  19594    577  -1496  -1827       C  
ATOM   1169  O   LYS A1042      -1.100   0.466  -7.617  1.00183.32           O  
ANISOU 1169  O   LYS A1042    21044  25370  23241    575  -1523  -1853       O  
ATOM   1170  CB  LYS A1042      -4.316  -0.153  -7.667  1.00130.53           C  
ANISOU 1170  CB  LYS A1042    14270  18731  16593    569  -1536  -1770       C  
ATOM   1171  N   SER A1043      -1.909   0.705  -9.711  1.00147.96           N  
ANISOU 1171  N   SER A1043    16453  21149  18618    574  -1460  -1888       N  
ATOM   1172  CA  SER A1043      -0.631   0.396 -10.324  1.00148.89           C  
ANISOU 1172  CA  SER A1043    16565  21280  18724    570  -1452  -1990       C  
ATOM   1173  C   SER A1043       0.332   1.577 -10.191  1.00152.28           C  
ANISOU 1173  C   SER A1043    17042  21746  19073    583  -1427  -1922       C  
ATOM   1174  O   SER A1043       1.526   1.373  -9.992  1.00161.08           O  
ANISOU 1174  O   SER A1043    18190  22797  20215    582  -1438  -1976       O  
ATOM   1175  CB  SER A1043      -0.811  -0.037 -11.750  1.00151.22           C  
ANISOU 1175  CB  SER A1043    16781  21710  18965    564  -1424  -2080       C  
ATOM   1176  OG  SER A1043       0.405  -0.565 -12.249  1.00164.21           O  
ANISOU 1176  OG  SER A1043    18420  23349  20624    563  -1423  -2194       O  
ATOM   1177  N   GLU A1044      -0.191   2.806 -10.316  1.00158.71           N  
ANISOU 1177  N   GLU A1044    17855  22660  19786    596  -1392  -1801       N  
ATOM   1178  CA  GLU A1044       0.598   4.020 -10.134  1.00153.30           C  
ANISOU 1178  CA  GLU A1044    17212  22009  19025    609  -1367  -1721       C  
ATOM   1179  C   GLU A1044       1.096   4.102  -8.695  1.00152.92           C  
ANISOU 1179  C   GLU A1044    17246  21803  19053    613  -1405  -1685       C  
ATOM   1180  O   GLU A1044       2.175   4.636  -8.454  1.00160.13           O  
ANISOU 1180  O   GLU A1044    18204  22698  19941    617  -1399  -1674       O  
ATOM   1181  CB  GLU A1044      -0.195   5.284 -10.478  1.00149.74           C  
ANISOU 1181  CB  GLU A1044    16740  21690  18463    625  -1321  -1589       C  
ATOM   1182  N   LEU A1045       0.304   3.563  -7.755  1.00150.05           N  
ANISOU 1182  N   LEU A1045    16902  21330  18783    612  -1442  -1666       N  
ATOM   1183  CA  LEU A1045       0.692   3.523  -6.351  1.00139.38           C  
ANISOU 1183  CA  LEU A1045    15623  19823  17511    614  -1480  -1636       C  
ATOM   1184  C   LEU A1045       1.689   2.395  -6.094  1.00147.55           C  
ANISOU 1184  C   LEU A1045    16678  20739  18646    596  -1515  -1752       C  
ATOM   1185  O   LEU A1045       2.543   2.527  -5.216  1.00152.18           O  
ANISOU 1185  O   LEU A1045    17326  21228  19269    596  -1534  -1741       O  
ATOM   1186  CB  LEU A1045      -0.538   3.395  -5.441  1.00129.65           C  
ANISOU 1186  CB  LEU A1045    14401  18522  16340    621  -1505  -1564       C  
ATOM   1187  CG  LEU A1045      -0.244   3.381  -3.936  1.00121.21           C  
ANISOU 1187  CG  LEU A1045    13404  17295  15353    625  -1544  -1523       C  
ATOM   1188  CD1 LEU A1045       0.393   4.690  -3.506  1.00107.96           C  
ANISOU 1188  CD1 LEU A1045    11779  15643  13596    645  -1522  -1439       C  
ATOM   1189  CD2 LEU A1045      -1.491   3.108  -3.111  1.00114.38           C  
ANISOU 1189  CD2 LEU A1045    12542  16363  14555    632  -1570  -1459       C  
ATOM   1190  N   ASP A1046       1.569   1.289  -6.845  1.00153.24           N  
ANISOU 1190  N   ASP A1046    17344  21470  19411    583  -1522  -1860       N  
ATOM   1191  CA  ASP A1046       2.438   0.132  -6.663  1.00136.95           C  
ANISOU 1191  CA  ASP A1046    15289  19297  17450    571  -1552  -1972       C  
ATOM   1192  C   ASP A1046       3.896   0.513  -6.938  1.00127.66           C  
ANISOU 1192  C   ASP A1046    14140  18142  16225    574  -1534  -2005       C  
ATOM   1193  O   ASP A1046       4.790   0.111  -6.194  1.00104.71           O  
ANISOU 1193  O   ASP A1046    11279  15117  13389    570  -1559  -2033       O  
ATOM   1194  CB  ASP A1046       1.961  -1.069  -7.485  1.00129.22           C  
ANISOU 1194  CB  ASP A1046    14240  18336  16522    562  -1559  -2083       C  
ATOM   1195  N   LYS A1047       4.112   1.300  -8.006  1.00136.15           N  
ANISOU 1195  N   LYS A1047    15184  19369  17176    581  -1489  -1994       N  
ATOM   1196  CA  LYS A1047       5.427   1.780  -8.413  1.00140.84           C  
ANISOU 1196  CA  LYS A1047    15798  20008  17708    585  -1466  -2014       C  
ATOM   1197  C   LYS A1047       5.976   2.758  -7.376  1.00129.68           C  
ANISOU 1197  C   LYS A1047    14463  18537  16275    589  -1471  -1918       C  
ATOM   1198  O   LYS A1047       7.180   2.799  -7.141  1.00126.87           O  
ANISOU 1198  O   LYS A1047    14146  18136  15923    587  -1473  -1943       O  
ATOM   1199  CB  LYS A1047       5.383   2.393  -9.821  1.00143.45           C  
ANISOU 1199  CB  LYS A1047    16070  20523  17913    590  -1417  -2016       C  
ATOM   1200  CG  LYS A1047       6.620   3.172 -10.274  1.00131.10           C  
ANISOU 1200  CG  LYS A1047    14523  19026  16262    595  -1387  -2006       C  
ATOM   1201  CD  LYS A1047       7.850   2.332 -10.568  1.00117.93           C  
ANISOU 1201  CD  LYS A1047    12854  17316  14638    592  -1395  -2121       C  
ATOM   1202  CE  LYS A1047       8.745   2.987 -11.606  1.00133.74           C  
ANISOU 1202  CE  LYS A1047    14834  19450  16531    598  -1353  -2127       C  
ATOM   1203  NZ  LYS A1047       9.441   2.027 -12.506  1.00118.22           N  
ANISOU 1203  NZ  LYS A1047    12820  17514  14584    600  -1348  -2259       N  
ATOM   1204  N   ALA A1048       5.075   3.518  -6.744  1.00125.56           N  
ANISOU 1204  N   ALA A1048    13961  18015  15732    597  -1471  -1809       N  
ATOM   1205  CA  ALA A1048       5.460   4.565  -5.814  1.00129.34           C  
ANISOU 1205  CA  ALA A1048    14508  18457  16180    606  -1470  -1713       C  
ATOM   1206  C   ALA A1048       5.480   4.047  -4.371  1.00130.95           C  
ANISOU 1206  C   ALA A1048    14771  18489  16497    600  -1518  -1704       C  
ATOM   1207  O   ALA A1048       5.541   4.842  -3.439  1.00138.44           O  
ANISOU 1207  O   ALA A1048    15774  19395  17430    608  -1523  -1620       O  
ATOM   1208  CB  ALA A1048       4.532   5.743  -5.992  1.00122.13           C  
ANISOU 1208  CB  ALA A1048    13580  17651  15174    624  -1439  -1597       C  
ATOM   1209  N   ILE A1049       5.421   2.721  -4.175  1.00134.38           N  
ANISOU 1209  N   ILE A1049    15189  18825  17044    586  -1551  -1788       N  
ATOM   1210  CA  ILE A1049       5.522   2.148  -2.836  1.00134.17           C  
ANISOU 1210  CA  ILE A1049    15213  18633  17132    578  -1595  -1780       C  
ATOM   1211  C   ILE A1049       6.589   1.057  -2.825  1.00146.25           C  
ANISOU 1211  C   ILE A1049    16746  20076  18745    564  -1614  -1884       C  
ATOM   1212  O   ILE A1049       7.232   0.844  -1.802  1.00158.21           O  
ANISOU 1212  O   ILE A1049    18314  21472  20327    556  -1639  -1875       O  
ATOM   1213  CB  ILE A1049       4.165   1.648  -2.275  1.00142.06           C  
ANISOU 1213  CB  ILE A1049    16195  19574  18208    578  -1623  -1746       C  
ATOM   1214  CG1 ILE A1049       4.216   1.244  -0.791  1.00145.26           C  
ANISOU 1214  CG1 ILE A1049    16653  19814  18724    570  -1666  -1712       C  
ATOM   1215  CG2 ILE A1049       3.648   0.487  -3.090  1.00154.88           C  
ANISOU 1215  CG2 ILE A1049    17750  21212  19886    569  -1629  -1838       C  
ATOM   1216  CD1 ILE A1049       4.452   2.395   0.152  1.00166.07           C  
ANISOU 1216  CD1 ILE A1049    19355  22431  21312    582  -1663  -1612       C  
ATOM   1217  N   GLY A1050       6.751   0.349  -3.953  1.00154.70           N  
ANISOU 1217  N   GLY A1050    17758  21208  19814    563  -1601  -1983       N  
ATOM   1218  CA  GLY A1050       7.683  -0.764  -4.034  1.00167.84           C  
ANISOU 1218  CA  GLY A1050    19414  22796  21563    557  -1617  -2087       C  
ATOM   1219  C   GLY A1050       6.982  -2.109  -4.232  1.00186.32           C  
ANISOU 1219  C   GLY A1050    21700  25082  24012    553  -1642  -2168       C  
ATOM   1220  O   GLY A1050       7.248  -2.793  -5.215  1.00225.11           O  
ANISOU 1220  O   GLY A1050    26560  30043  28930    557  -1631  -2270       O  
ATOM   1221  N   ARG A1051       6.099  -2.475  -3.292  1.00175.81           N  
ANISOU 1221  N   ARG A1051    20381  23651  22769    546  -1675  -2121       N  
ATOM   1222  CA  ARG A1051       5.400  -3.751  -3.292  1.00163.71           C  
ANISOU 1222  CA  ARG A1051    18803  22047  21354    541  -1704  -2185       C  
ATOM   1223  C   ARG A1051       4.035  -3.619  -3.973  1.00168.55           C  
ANISOU 1223  C   ARG A1051    19363  22757  21921    542  -1692  -2169       C  
ATOM   1224  O   ARG A1051       3.646  -2.545  -4.431  1.00173.62           O  
ANISOU 1224  O   ARG A1051    20003  23522  22443    548  -1661  -2105       O  
ATOM   1225  CB  ARG A1051       5.292  -4.268  -1.855  1.00144.30           C  
ANISOU 1225  CB  ARG A1051    16386  19419  19022    531  -1747  -2138       C  
ATOM   1226  N   ASN A1052       3.318  -4.744  -4.066  1.00178.95           N  
ANISOU 1226  N   ASN A1052    20635  24022  23337    535  -1716  -2227       N  
ATOM   1227  CA  ASN A1052       1.978  -4.753  -4.629  1.00190.11           C  
ANISOU 1227  CA  ASN A1052    21997  25516  24720    533  -1709  -2213       C  
ATOM   1228  C   ASN A1052       1.010  -4.165  -3.606  1.00188.72           C  
ANISOU 1228  C   ASN A1052    21857  25297  24551    531  -1725  -2083       C  
ATOM   1229  O   ASN A1052       1.064  -4.504  -2.424  1.00201.88           O  
ANISOU 1229  O   ASN A1052    23565  26825  26317    525  -1760  -2043       O  
ATOM   1230  CB  ASN A1052       1.565  -6.154  -5.086  1.00211.92           C  
ANISOU 1230  CB  ASN A1052    24698  28237  27586    527  -1729  -2324       C  
ATOM   1231  CG  ASN A1052       0.248  -6.188  -5.835  1.00239.06           C  
ANISOU 1231  CG  ASN A1052    28075  31775  30980    522  -1718  -2323       C  
ATOM   1232  OD1 ASN A1052      -0.347  -5.147  -6.116  1.00257.38           O  
ANISOU 1232  OD1 ASN A1052    30397  34209  33188    526  -1690  -2240       O  
ATOM   1233  ND2 ASN A1052      -0.225  -7.383  -6.144  1.00260.50           N  
ANISOU 1233  ND2 ASN A1052    30739  34449  33790    516  -1738  -2412       N  
ATOM   1234  N   THR A1053       0.115  -3.293  -4.082  1.00189.57           N  
ANISOU 1234  N   THR A1053    21946  25530  24554    538  -1698  -2015       N  
ATOM   1235  CA  THR A1053      -0.710  -2.483  -3.199  1.00191.09           C  
ANISOU 1235  CA  THR A1053    22173  25707  24726    544  -1704  -1883       C  
ATOM   1236  C   THR A1053      -1.955  -3.240  -2.751  1.00174.60           C  
ANISOU 1236  C   THR A1053    20059  23551  22729    536  -1735  -1861       C  
ATOM   1237  O   THR A1053      -2.230  -3.315  -1.556  1.00166.80           O  
ANISOU 1237  O   THR A1053    19112  22449  21816    535  -1765  -1790       O  
ATOM   1238  CB  THR A1053      -1.076  -1.142  -3.842  1.00193.99           C  
ANISOU 1238  CB  THR A1053    22532  26234  24942    561  -1658  -1807       C  
ATOM   1239  OG1 THR A1053      -1.675  -1.397  -5.116  1.00201.83           O  
ANISOU 1239  OG1 THR A1053    23453  27352  25883    557  -1633  -1861       O  
ATOM   1240  CG2 THR A1053       0.128  -0.240  -3.970  1.00163.65           C  
ANISOU 1240  CG2 THR A1053    18729  22436  21017    570  -1632  -1797       C  
ATOM   1241  N   ASN A1054      -2.710  -3.769  -3.720  1.00155.55           N  
ANISOU 1241  N   ASN A1054    17580  21217  20306    530  -1725  -1918       N  
ATOM   1242  CA  ASN A1054      -4.004  -4.386  -3.467  1.00156.29           C  
ANISOU 1242  CA  ASN A1054    17643  21275  20466    521  -1749  -1892       C  
ATOM   1243  C   ASN A1054      -5.034  -3.297  -3.173  1.00159.75           C  
ANISOU 1243  C   ASN A1054    18093  21785  20822    536  -1732  -1756       C  
ATOM   1244  O   ASN A1054      -6.199  -3.444  -3.542  1.00170.74           O  
ANISOU 1244  O   ASN A1054    19441  23234  22200    533  -1728  -1733       O  
ATOM   1245  CB  ASN A1054      -3.960  -5.462  -2.371  1.00150.28           C  
ANISOU 1245  CB  ASN A1054    16904  20330  19867    509  -1800  -1905       C  
ATOM   1246  CG  ASN A1054      -5.312  -6.060  -2.016  1.00137.46           C  
ANISOU 1246  CG  ASN A1054    15251  18663  18313    499  -1826  -1864       C  
ATOM   1247  OD1 ASN A1054      -6.197  -6.173  -2.857  1.00118.85           O  
ANISOU 1247  OD1 ASN A1054    12840  16405  15914    496  -1812  -1884       O  
ATOM   1248  ND2 ASN A1054      -5.489  -6.437  -0.760  1.00141.45           N  
ANISOU 1248  ND2 ASN A1054    15793  19026  18927    494  -1864  -1803       N  
ATOM   1249  N   GLY A1055      -4.604  -2.230  -2.485  1.00158.11           N  
ANISOU 1249  N   GLY A1055    17943  21569  20563    554  -1722  -1665       N  
ATOM   1250  CA  GLY A1055      -5.520  -1.203  -2.026  1.00170.53           C  
ANISOU 1250  CA  GLY A1055    19533  23189  22071    576  -1708  -1531       C  
ATOM   1251  C   GLY A1055      -5.222  -0.733  -0.605  1.00170.86           C  
ANISOU 1251  C   GLY A1055    19648  23116  22155    589  -1730  -1443       C  
ATOM   1252  O   GLY A1055      -5.225   0.465  -0.366  1.00182.73           O  
ANISOU 1252  O   GLY A1055    21183  24676  23572    616  -1704  -1354       O  
ATOM   1253  N   VAL A1056      -4.959  -1.666   0.321  1.00165.62           N  
ANISOU 1253  N   VAL A1056    19009  22295  21624    572  -1775  -1466       N  
ATOM   1254  CA  VAL A1056      -4.707  -1.293   1.708  1.00160.75           C  
ANISOU 1254  CA  VAL A1056    18459  21565  21052    582  -1797  -1382       C  
ATOM   1255  C   VAL A1056      -3.202  -1.080   1.901  1.00147.97           C  
ANISOU 1255  C   VAL A1056    16885  19908  19428    577  -1795  -1428       C  
ATOM   1256  O   VAL A1056      -2.402  -1.924   1.511  1.00134.15           O  
ANISOU 1256  O   VAL A1056    15120  18121  17730    556  -1804  -1532       O  
ATOM   1257  CB  VAL A1056      -5.308  -2.285   2.733  1.00163.15           C  
ANISOU 1257  CB  VAL A1056    18768  21723  21497    566  -1844  -1353       C  
ATOM   1258  CG1 VAL A1056      -5.072  -1.823   4.165  1.00173.32           C  
ANISOU 1258  CG1 VAL A1056    20125  22905  22823    576  -1864  -1255       C  
ATOM   1259  CG2 VAL A1056      -6.797  -2.546   2.516  1.00146.72           C  
ANISOU 1259  CG2 VAL A1056    16643  19682  19422    569  -1847  -1309       C  
ATOM   1260  N   ILE A1057      -2.835   0.063   2.495  1.00142.89           N  
ANISOU 1260  N   ILE A1057    16297  19276  18720    599  -1782  -1348       N  
ATOM   1261  CA  ILE A1057      -1.452   0.433   2.755  1.00134.81           C  
ANISOU 1261  CA  ILE A1057    15321  18223  17678    595  -1778  -1376       C  
ATOM   1262  C   ILE A1057      -1.289   0.681   4.254  1.00148.92           C  
ANISOU 1262  C   ILE A1057    17173  19886  19523    600  -1806  -1294       C  
ATOM   1263  O   ILE A1057      -2.053   1.429   4.848  1.00164.19           O  
ANISOU 1263  O   ILE A1057    19129  21829  21427    626  -1803  -1191       O  
ATOM   1264  CB  ILE A1057      -1.050   1.656   1.900  1.00116.94           C  
ANISOU 1264  CB  ILE A1057    13058  16108  15265    616  -1730  -1365       C  
ATOM   1265  CG1 ILE A1057      -0.522   1.253   0.519  1.00131.38           C  
ANISOU 1265  CG1 ILE A1057    14837  18028  17053    601  -1706  -1474       C  
ATOM   1266  CG2 ILE A1057      -0.064   2.554   2.626  1.00106.72           C  
ANISOU 1266  CG2 ILE A1057    11832  14784  13933    627  -1726  -1324       C  
ATOM   1267  CD1 ILE A1057      -1.568   0.767  -0.469  1.00145.11           C  
ANISOU 1267  CD1 ILE A1057    16504  19852  18781    597  -1695  -1504       C  
ATOM   1268  N   THR A1058      -0.254   0.079   4.849  1.00156.11           N  
ANISOU 1268  N   THR A1058    18114  20687  20513    576  -1830  -1337       N  
ATOM   1269  CA  THR A1058      -0.043   0.104   6.291  1.00147.32           C  
ANISOU 1269  CA  THR A1058    17057  19447  19471    571  -1859  -1265       C  
ATOM   1270  C   THR A1058       0.359   1.500   6.772  1.00132.50           C  
ANISOU 1270  C   THR A1058    15259  17596  17489    589  -1817  -1179       C  
ATOM   1271  O   THR A1058       0.700   2.371   5.973  1.00125.78           O  
ANISOU 1271  O   THR A1058    14415  16855  16521    604  -1773  -1190       O  
ATOM   1272  CB  THR A1058       0.985  -0.957   6.700  1.00147.31           C  
ANISOU 1272  CB  THR A1058    17064  19329  19577    539  -1884  -1332       C  
ATOM   1273  OG1 THR A1058       2.213  -0.635   6.043  1.00137.42           O  
ANISOU 1273  OG1 THR A1058    15824  18133  18257    536  -1861  -1405       O  
ATOM   1274  CG2 THR A1058       0.546  -2.361   6.342  1.00148.90           C  
ANISOU 1274  CG2 THR A1058    17210  19480  19886    520  -1905  -1397       C  
ATOM   1275  N   LYS A1059       0.320   1.699   8.096  1.00119.61           N  
ANISOU 1275  N   LYS A1059    13712  15846  15888    577  -1796  -1073       N  
ATOM   1276  CA  LYS A1059       0.641   2.987   8.692  1.00128.14           C  
ANISOU 1276  CA  LYS A1059    14903  16917  16865    581  -1717   -967       C  
ATOM   1277  C   LYS A1059       2.096   3.369   8.417  1.00137.97           C  
ANISOU 1277  C   LYS A1059    16173  18188  18061    572  -1709  -1031       C  
ATOM   1278  O   LYS A1059       2.392   4.549   8.251  1.00149.71           O  
ANISOU 1278  O   LYS A1059    17722  19729  19434    583  -1641   -981       O  
ATOM   1279  CB  LYS A1059       0.352   3.027  10.198  1.00117.13           C  
ANISOU 1279  CB  LYS A1059    13586  15398  15520    565  -1702   -853       C  
ATOM   1280  CG  LYS A1059       0.595   4.384  10.850  1.00122.79           C  
ANISOU 1280  CG  LYS A1059    14416  16106  16133    568  -1615   -747       C  
ATOM   1281  CD  LYS A1059       0.689   4.354  12.369  1.00143.50           C  
ANISOU 1281  CD  LYS A1059    17108  18610  18804    544  -1606   -661       C  
ATOM   1282  CE  LYS A1059       1.029   5.695  12.995  1.00137.17           C  
ANISOU 1282  CE  LYS A1059    16415  17801  17902    544  -1520   -573       C  
ATOM   1283  NZ  LYS A1059       2.480   6.011  12.939  1.00121.44           N  
ANISOU 1283  NZ  LYS A1059    14456  15812  15875    527  -1512   -629       N  
ATOM   1284  N   ASP A1060       3.000   2.379   8.395  1.00136.45           N  
ANISOU 1284  N   ASP A1060    15933  17955  17958    553  -1777  -1138       N  
ATOM   1285  CA  ASP A1060       4.420   2.644   8.207  1.00125.81           C  
ANISOU 1285  CA  ASP A1060    14606  16625  16570    543  -1775  -1199       C  
ATOM   1286  C   ASP A1060       4.689   3.082   6.776  1.00116.39           C  
ANISOU 1286  C   ASP A1060    13361  15581  15280    563  -1764  -1278       C  
ATOM   1287  O   ASP A1060       5.473   4.001   6.548  1.00123.65           O  
ANISOU 1287  O   ASP A1060    14329  16553  16100    566  -1720  -1266       O  
ATOM   1288  CB  ASP A1060       5.289   1.438   8.569  1.00143.72           C  
ANISOU 1288  CB  ASP A1060    16832  18809  18966    520  -1850  -1290       C  
ATOM   1289  CG  ASP A1060       5.172   1.034  10.030  1.00167.63           C  
ANISOU 1289  CG  ASP A1060    19908  21696  22088    496  -1861  -1204       C  
ATOM   1290  OD1 ASP A1060       4.025   1.032  10.546  1.00178.91           O  
ANISOU 1290  OD1 ASP A1060    21348  23089  23539    501  -1848  -1115       O  
ATOM   1291  OD2 ASP A1060       6.226   0.727  10.647  1.00176.75           O1-
ANISOU 1291  OD2 ASP A1060    21084  22784  23288    474  -1881  -1222       O1-
ATOM   1292  N   GLU A1061       4.030   2.413   5.828  1.00109.33           N  
ANISOU 1292  N   GLU A1061    12374  14753  14412    572  -1794  -1350       N  
ATOM   1293  CA  GLU A1061       4.206   2.721   4.418  1.00105.95           C  
ANISOU 1293  CA  GLU A1061    11907  14462  13888    581  -1756  -1407       C  
ATOM   1294  C   GLU A1061       3.741   4.144   4.121  1.00 95.57           C  
ANISOU 1294  C   GLU A1061    10606  13264  12443    613  -1715  -1327       C  
ATOM   1295  O   GLU A1061       4.354   4.847   3.317  1.00 83.53           O  
ANISOU 1295  O   GLU A1061     9074  11847  10816    622  -1687  -1350       O  
ATOM   1296  CB  GLU A1061       3.462   1.698   3.566  1.00113.57           C  
ANISOU 1296  CB  GLU A1061    12800  15450  14902    573  -1759  -1469       C  
ATOM   1297  CG  GLU A1061       4.032   0.296   3.686  1.00129.42           C  
ANISOU 1297  CG  GLU A1061    14792  17351  17031    546  -1786  -1554       C  
ATOM   1298  CD  GLU A1061       3.373  -0.699   2.753  1.00124.28           C  
ANISOU 1298  CD  GLU A1061    14070  16729  16423    541  -1788  -1628       C  
ATOM   1299  OE1 GLU A1061       2.372  -0.320   2.152  1.00127.55           O  
ANISOU 1299  OE1 GLU A1061    14448  17236  16777    554  -1771  -1601       O  
ATOM   1300  OE2 GLU A1061       3.850  -1.849   2.662  1.00130.23           O1-
ANISOU 1300  OE2 GLU A1061    14802  17409  17270    526  -1806  -1709       O1-
ATOM   1301  N   ALA A1062       2.666   4.570   4.794  1.00 87.74           N  
ANISOU 1301  N   ALA A1062     9669  12222  11448    621  -1672  -1202       N  
ATOM   1302  CA  ALA A1062       2.156   5.923   4.615  1.00 96.57           C  
ANISOU 1302  CA  ALA A1062    10841  13406  12446    641  -1587  -1086       C  
ATOM   1303  C   ALA A1062       3.138   6.978   5.131  1.00 99.00           C  
ANISOU 1303  C   ALA A1062    11249  13683  12685    635  -1531  -1028       C  
ATOM   1304  O   ALA A1062       3.310   8.017   4.502  1.00 86.98           O  
ANISOU 1304  O   ALA A1062     9739  12254  11056    650  -1477   -991       O  
ATOM   1305  CB  ALA A1062       0.807   6.047   5.267  1.00103.35           C  
ANISOU 1305  CB  ALA A1062    11732  14211  13327    651  -1558   -973       C  
ATOM   1306  N   GLU A1063       3.775   6.701   6.278  1.00109.65           N  
ANISOU 1306  N   GLU A1063    12665  14901  14097    612  -1544  -1016       N  
ATOM   1307  CA  GLU A1063       4.744   7.603   6.884  1.00104.66           C  
ANISOU 1307  CA  GLU A1063    12129  14228  13409    600  -1496   -968       C  
ATOM   1308  C   GLU A1063       5.975   7.703   5.993  1.00103.99           C  
ANISOU 1308  C   GLU A1063    12010  14231  13272    597  -1514  -1064       C  
ATOM   1309  O   GLU A1063       6.626   8.749   5.953  1.00 93.24           O  
ANISOU 1309  O   GLU A1063    10707  12898  11823    597  -1461  -1022       O  
ATOM   1310  CB  GLU A1063       5.117   7.152   8.299  1.00114.45           C  
ANISOU 1310  CB  GLU A1063    13434  15321  14733    572  -1512   -940       C  
ATOM   1311  CG  GLU A1063       4.055   7.472   9.351  1.00132.95           C  
ANISOU 1311  CG  GLU A1063    15838  17582  17094    573  -1470   -816       C  
ATOM   1312  CD  GLU A1063       3.813   8.945   9.662  1.00136.80           C  
ANISOU 1312  CD  GLU A1063    16416  18079  17483    585  -1374   -702       C  
ATOM   1313  OE1 GLU A1063       4.626   9.789   9.222  1.00131.94           O  
ANISOU 1313  OE1 GLU A1063    15830  17516  16786    587  -1336   -709       O  
ATOM   1314  OE2 GLU A1063       2.805   9.252  10.336  1.00130.69           O1-
ANISOU 1314  OE2 GLU A1063    15681  17260  16716    592  -1337   -605       O1-
ATOM   1315  N   LYS A1064       6.275   6.611   5.278  1.00109.67           N  
ANISOU 1315  N   LYS A1064    12631  14993  14047    594  -1590  -1194       N  
ATOM   1316  CA  LYS A1064       7.396   6.589   4.349  1.00119.20           C  
ANISOU 1316  CA  LYS A1064    13789  16295  15206    593  -1616  -1298       C  
ATOM   1317  C   LYS A1064       7.102   7.516   3.172  1.00116.59           C  
ANISOU 1317  C   LYS A1064    13422  16124  14755    618  -1572  -1277       C  
ATOM   1318  O   LYS A1064       7.960   8.321   2.813  1.00 99.33           O  
ANISOU 1318  O   LYS A1064    11260  13999  12481    619  -1542  -1271       O  
ATOM   1319  CB  LYS A1064       7.714   5.165   3.881  1.00134.30           C  
ANISOU 1319  CB  LYS A1064    15618  18197  17214    580  -1684  -1431       C  
ATOM   1320  CG  LYS A1064       9.009   5.036   3.082  1.00127.71           C  
ANISOU 1320  CG  LYS A1064    14781  17404  16337    564  -1661  -1506       C  
ATOM   1321  CD  LYS A1064       9.133   3.740   2.297  1.00126.57           C  
ANISOU 1321  CD  LYS A1064    14580  17249  16263    551  -1667  -1604       C  
ATOM   1322  CE  LYS A1064       9.136   2.485   3.148  1.00110.02           C  
ANISOU 1322  CE  LYS A1064    12486  15005  14311    532  -1708  -1634       C  
ATOM   1323  NZ  LYS A1064       8.828   1.278   2.341  1.00 99.86           N  
ANISOU 1323  NZ  LYS A1064    11132  13719  13092    529  -1714  -1720       N  
ATOM   1324  N   LEU A1065       5.895   7.388   2.590  1.00104.58           N  
ANISOU 1324  N   LEU A1065    11836  14670  13229    637  -1570  -1262       N  
ATOM   1325  CA  LEU A1065       5.468   8.235   1.479  1.00105.10           C  
ANISOU 1325  CA  LEU A1065    11855  14894  13184    660  -1527  -1229       C  
ATOM   1326  C   LEU A1065       5.277   9.681   1.943  1.00 98.04           C  
ANISOU 1326  C   LEU A1065    11061  13978  12210    670  -1434  -1077       C  
ATOM   1327  O   LEU A1065       5.490  10.632   1.185  1.00 88.56           O  
ANISOU 1327  O   LEU A1065     9849  12892  10910    684  -1391  -1040       O  
ATOM   1328  CB  LEU A1065       4.215   7.671   0.796  1.00 92.12           C  
ANISOU 1328  CB  LEU A1065    10115  13325  11560    675  -1548  -1251       C  
ATOM   1329  N   PHE A1066       4.906   9.839   3.214  1.00 98.81           N  
ANISOU 1329  N   PHE A1066    11256  13932  12357    662  -1405   -989       N  
ATOM   1330  CA  PHE A1066       4.717  11.161   3.789  1.00 92.32           C  
ANISOU 1330  CA  PHE A1066    10532  13070  11473    670  -1317   -851       C  
ATOM   1331  C   PHE A1066       6.036  11.934   3.838  1.00 94.02           C  
ANISOU 1331  C   PHE A1066    10804  13290  11629    658  -1290   -852       C  
ATOM   1332  O   PHE A1066       6.061  13.121   3.509  1.00 90.09           O  
ANISOU 1332  O   PHE A1066    10335  12848  11048    671  -1225   -774       O  
ATOM   1333  CB  PHE A1066       4.010  11.062   5.141  1.00 82.45           C  
ANISOU 1333  CB  PHE A1066     9363  11674  10292    663  -1297   -770       C  
ATOM   1334  CG  PHE A1066       3.774  12.402   5.777  1.00 80.96           C  
ANISOU 1334  CG  PHE A1066     9274  11441  10048    670  -1205   -637       C  
ATOM   1335  CD1 PHE A1066       3.038  13.379   5.131  1.00 77.52           C  
ANISOU 1335  CD1 PHE A1066     8826  11089   9539    699  -1142   -553       C  
ATOM   1336  CD2 PHE A1066       4.318  12.699   7.013  1.00 92.75           C  
ANISOU 1336  CD2 PHE A1066    10869  12810  11564    648  -1180   -598       C  
ATOM   1337  CE1 PHE A1066       2.837  14.620   5.710  1.00 72.91           C  
ANISOU 1337  CE1 PHE A1066     8331  10457   8914    707  -1055   -435       C  
ATOM   1338  CE2 PHE A1066       4.115  13.940   7.592  1.00 90.79           C  
ANISOU 1338  CE2 PHE A1066    10709  12520  11269    654  -1094   -486       C  
ATOM   1339  CZ  PHE A1066       3.371  14.898   6.940  1.00 77.02           C  
ANISOU 1339  CZ  PHE A1066     8952  10851   9460    684  -1031   -406       C  
ATOM   1340  N   ASN A1067       7.119  11.258   4.243  1.00 98.86           N  
ANISOU 1340  N   ASN A1067    11431  13844  12289    633  -1341   -938       N  
ATOM   1341  CA  ASN A1067       8.446  11.854   4.233  1.00 99.19           C  
ANISOU 1341  CA  ASN A1067    11517  13896  12274    619  -1326   -953       C  
ATOM   1342  C   ASN A1067       8.858  12.247   2.820  1.00100.30           C  
ANISOU 1342  C   ASN A1067    11578  14204  12326    634  -1330   -997       C  
ATOM   1343  O   ASN A1067       9.518  13.277   2.635  1.00 90.95           O  
ANISOU 1343  O   ASN A1067    10434  13059  11063    634  -1284   -950       O  
ATOM   1344  CB  ASN A1067       9.509  10.931   4.832  1.00106.59           C  
ANISOU 1344  CB  ASN A1067    12467  14752  13280    590  -1387  -1044       C  
ATOM   1345  CG  ASN A1067       9.480  10.946   6.339  1.00107.35           C  
ANISOU 1345  CG  ASN A1067    12663  14691  13433    568  -1365   -977       C  
ATOM   1346  OD1 ASN A1067       8.402  10.855   6.924  1.00117.79           O  
ANISOU 1346  OD1 ASN A1067    14003  15952  14797    574  -1347   -912       O  
ATOM   1347  ND2 ASN A1067      10.646  11.120   6.942  1.00 90.84           N  
ANISOU 1347  ND2 ASN A1067    10634  12546  11333    542  -1361   -989       N  
ATOM   1348  N   GLN A1068       8.475  11.407   1.845  1.00 90.93           N  
ANISOU 1348  N   GLN A1068    10276  13120  11155    646  -1386  -1087       N  
ATOM   1349  CA  GLN A1068       8.838  11.647   0.460  1.00 99.89           C  
ANISOU 1349  CA  GLN A1068    11316  14431  12205    659  -1397  -1139       C  
ATOM   1350  C   GLN A1068       8.210  12.971   0.021  1.00102.91           C  
ANISOU 1350  C   GLN A1068    11710  14893  12498    681  -1317  -1011       C  
ATOM   1351  O   GLN A1068       8.897  13.830  -0.555  1.00 81.62           O  
ANISOU 1351  O   GLN A1068     9010  12285   9716    685  -1288   -986       O  
ATOM   1352  CB  GLN A1068       8.401  10.485  -0.439  1.00114.29           C  
ANISOU 1352  CB  GLN A1068    13012  16346  14068    665  -1466  -1259       C  
ATOM   1353  CG  GLN A1068       9.091   9.145  -0.185  1.00113.62           C  
ANISOU 1353  CG  GLN A1068    12938  16146  14086    632  -1502  -1365       C  
ATOM   1354  CD  GLN A1068       8.494   8.005  -0.989  1.00125.95           C  
ANISOU 1354  CD  GLN A1068    14429  17722  15704    622  -1509  -1438       C  
ATOM   1355  OE1 GLN A1068       7.650   8.196  -1.870  1.00123.42           O  
ANISOU 1355  OE1 GLN A1068    14048  17509  15338    635  -1484  -1418       O  
ATOM   1356  NE2 GLN A1068       8.909   6.785  -0.680  1.00120.84           N  
ANISOU 1356  NE2 GLN A1068    13786  16968  15159    600  -1541  -1519       N  
ATOM   1357  N   ASP A1069       6.909  13.117   0.329  1.00100.81           N  
ANISOU 1357  N   ASP A1069    11457  14590  12255    696  -1281   -926       N  
ATOM   1358  CA  ASP A1069       6.124  14.255  -0.124  1.00110.62           C  
ANISOU 1358  CA  ASP A1069    12696  15910  13426    721  -1207   -802       C  
ATOM   1359  C   ASP A1069       6.649  15.556   0.474  1.00100.20           C  
ANISOU 1359  C   ASP A1069    11483  14524  12063    718  -1132   -695       C  
ATOM   1360  O   ASP A1069       6.705  16.569  -0.220  1.00 85.98           O  
ANISOU 1360  O   ASP A1069     9663  12822  10185    733  -1084   -626       O  
ATOM   1361  CB  ASP A1069       4.634  14.062   0.164  1.00118.69           C  
ANISOU 1361  CB  ASP A1069    13712  16896  14488    736  -1188   -737       C  
ATOM   1362  CG  ASP A1069       4.045  12.867  -0.552  1.00123.26           C  
ANISOU 1362  CG  ASP A1069    14175  17555  15101    739  -1256   -839       C  
ATOM   1363  OD1 ASP A1069       4.560  12.540  -1.643  1.00124.01           O  
ANISOU 1363  OD1 ASP A1069    14170  17791  15155    739  -1298   -934       O  
ATOM   1364  OD2 ASP A1069       3.091  12.271  -0.010  1.00125.46           O1-
ANISOU 1364  OD2 ASP A1069    14462  17759  15449    740  -1268   -825       O1-
ATOM   1365  N   VAL A1070       6.998  15.524   1.764  1.00 86.85           N  
ANISOU 1365  N   VAL A1070     9902  12670  10427    698  -1122   -678       N  
ATOM   1366  CA  VAL A1070       7.502  16.705   2.444  1.00 81.40           C  
ANISOU 1366  CA  VAL A1070     9317  11904   9705    691  -1051   -587       C  
ATOM   1367  C   VAL A1070       8.902  17.078   1.934  1.00 87.63           C  
ANISOU 1367  C   VAL A1070    10102  12760  10436    678  -1062   -633       C  
ATOM   1368  O   VAL A1070       9.220  18.264   1.765  1.00 84.92           O  
ANISOU 1368  O   VAL A1070     9792  12441  10032    683  -1002   -553       O  
ATOM   1369  CB  VAL A1070       7.431  16.531   3.967  1.00 67.67           C  
ANISOU 1369  CB  VAL A1070     7687   9987   8038    671  -1037   -560       C  
ATOM   1370  CG1 VAL A1070       7.967  17.753   4.696  1.00 59.23           C  
ANISOU 1370  CG1 VAL A1070     6725   8841   6937    660   -962   -476       C  
ATOM   1371  CG2 VAL A1070       6.001  16.250   4.384  1.00 70.25           C  
ANISOU 1371  CG2 VAL A1070     8012  10266   8414    687  -1024   -504       C  
ATOM   1372  N   ASP A1071       9.737  16.069   1.655  1.00 78.37           N  
ANISOU 1372  N   ASP A1071     8881  11616   9281    662  -1141   -762       N  
ATOM   1373  CA  ASP A1071      11.063  16.357   1.124  1.00 82.62           C  
ANISOU 1373  CA  ASP A1071     9407  12227   9759    650  -1157   -811       C  
ATOM   1374  C   ASP A1071      10.937  16.918  -0.294  1.00 83.22           C  
ANISOU 1374  C   ASP A1071     9383  12488   9747    673  -1147   -793       C  
ATOM   1375  O   ASP A1071      11.737  17.767  -0.714  1.00 69.15           O  
ANISOU 1375  O   ASP A1071     7607  10770   7895    671  -1122   -762       O  
ATOM   1376  CB  ASP A1071      12.008  15.151   1.245  1.00 79.99           C  
ANISOU 1376  CB  ASP A1071     9050  11871   9471    628  -1241   -951       C  
ATOM   1377  N   ALA A1072       9.932  16.410  -1.030  1.00 83.40           N  
ANISOU 1377  N   ALA A1072     9309  12603   9776    694  -1168   -812       N  
ATOM   1378  CA  ALA A1072       9.655  16.865  -2.384  1.00 76.75           C  
ANISOU 1378  CA  ALA A1072     8358  11952   8852    715  -1159   -791       C  
ATOM   1379  C   ALA A1072       9.055  18.274  -2.362  1.00 76.87           C  
ANISOU 1379  C   ALA A1072     8413  11970   8823    733  -1065   -627       C  
ATOM   1380  O   ALA A1072       9.161  19.001  -3.345  1.00 77.51           O  
ANISOU 1380  O   ALA A1072     8428  12196   8828    747  -1042   -579       O  
ATOM   1381  CB  ALA A1072       8.781  15.874  -3.096  1.00 58.00           C  
ANISOU 1381  CB  ALA A1072     5869   9670   6498    727  -1208   -865       C  
ATOM   1382  N   ALA A1073       8.469  18.677  -1.225  1.00 76.52           N  
ANISOU 1382  N   ALA A1073     8477  11768   8831    733  -1011   -539       N  
ATOM   1383  CA  ALA A1073       7.868  19.999  -1.104  1.00 77.65           C  
ANISOU 1383  CA  ALA A1073     8663  11894   8947    752   -919   -387       C  
ATOM   1384  C   ALA A1073       8.941  21.061  -0.908  1.00 74.01           C  
ANISOU 1384  C   ALA A1073     8269  11404   8446    739   -877   -338       C  
ATOM   1385  O   ALA A1073       8.873  22.146  -1.475  1.00 69.68           O  
ANISOU 1385  O   ALA A1073     7700  10928   7846    755   -821   -239       O  
ATOM   1386  CB  ALA A1073       6.864  20.041   0.022  1.00 69.94           C  
ANISOU 1386  CB  ALA A1073     7771  10765   8037    756   -878   -319       C  
ATOM   1387  N   VAL A1074       9.926  20.738  -0.077  1.00 75.98           N  
ANISOU 1387  N   VAL A1074     8599  11546   8724    710   -902   -403       N  
ATOM   1388  CA  VAL A1074      10.953  21.716   0.218  1.00 82.83           C  
ANISOU 1388  CA  VAL A1074     9538  12374   9558    694   -862   -360       C  
ATOM   1389  C   VAL A1074      11.859  21.845  -0.997  1.00 84.47           C  
ANISOU 1389  C   VAL A1074     9658  12749   9689    695   -897   -401       C  
ATOM   1390  O   VAL A1074      12.377  22.927  -1.233  1.00 95.90           O  
ANISOU 1390  O   VAL A1074    11123  14225  11089    695   -850   -326       O  
ATOM   1391  CB  VAL A1074      11.728  21.396   1.513  1.00 81.07           C  
ANISOU 1391  CB  VAL A1074     9428  11990   9383    661   -872   -408       C  
ATOM   1392  CG1 VAL A1074      10.800  21.472   2.716  1.00 92.08           C  
ANISOU 1392  CG1 VAL A1074    10908  13232  10844    661   -827   -348       C  
ATOM   1393  CG2 VAL A1074      12.396  20.029   1.454  1.00 95.25           C  
ANISOU 1393  CG2 VAL A1074    11185  13802  11203    643   -966   -553       C  
ATOM   1394  N   ARG A1075      12.062  20.752  -1.749  1.00 85.44           N  
ANISOU 1394  N   ARG A1075     9682  12981   9801    695   -978   -519       N  
ATOM   1395  CA  ARG A1075      12.895  20.809  -2.947  1.00 93.01           C  
ANISOU 1395  CA  ARG A1075    10544  14115  10681    696  -1016   -567       C  
ATOM   1396  C   ARG A1075      12.243  21.698  -4.002  1.00101.54           C  
ANISOU 1396  C   ARG A1075    11537  15344  11699    723   -971   -462       C  
ATOM   1397  O   ARG A1075      12.960  22.390  -4.725  1.00109.10           O  
ANISOU 1397  O   ARG A1075    12453  16413  12586    723   -963   -430       O  
ATOM   1398  CB  ARG A1075      13.254  19.427  -3.504  1.00 85.24           C  
ANISOU 1398  CB  ARG A1075     9469  13214   9703    690  -1112   -727       C  
ATOM   1399  CG  ARG A1075      14.384  18.735  -2.758  1.00 83.76           C  
ANISOU 1399  CG  ARG A1075     9348  12925   9554    661  -1160   -830       C  
ATOM   1400  CD  ARG A1075      14.873  17.452  -3.394  1.00 86.76           C  
ANISOU 1400  CD  ARG A1075     9644  13374   9949    653  -1240   -983       C  
ATOM   1401  NE  ARG A1075      13.814  16.456  -3.431  1.00 98.01           N  
ANISOU 1401  NE  ARG A1075    11024  14772  11444    659  -1261  -1030       N  
ATOM   1402  CZ  ARG A1075      13.599  15.525  -2.500  1.00107.53           C  
ANISOU 1402  CZ  ARG A1075    12268  15852  12738    651  -1303  -1092       C  
ATOM   1403  NH1 ARG A1075      14.419  15.424  -1.463  1.00 95.86           N  
ANISOU 1403  NH1 ARG A1075    10879  14251  11292    631  -1319  -1112       N  
ATOM   1404  NH2 ARG A1075      12.586  14.676  -2.637  1.00108.35           N  
ANISOU 1404  NH2 ARG A1075    12323  15942  12903    657  -1319  -1126       N  
ATOM   1405  N   GLY A1076      10.899  21.671  -4.066  1.00 97.87           N  
ANISOU 1405  N   GLY A1076    11043  14883  11260    745   -942   -403       N  
ATOM   1406  CA  GLY A1076      10.124  22.533  -4.948  1.00 93.64           C  
ANISOU 1406  CA  GLY A1076    10430  14475  10675    772   -891   -286       C  
ATOM   1407  C   GLY A1076      10.314  24.019  -4.630  1.00 92.99           C  
ANISOU 1407  C   GLY A1076    10420  14332  10579    776   -804   -140       C  
ATOM   1408  O   GLY A1076      10.521  24.845  -5.522  1.00 85.27           O  
ANISOU 1408  O   GLY A1076     9373  13486   9540    787   -779    -64       O  
ATOM   1409  N   ILE A1077      10.242  24.335  -3.332  1.00 95.69           N  
ANISOU 1409  N   ILE A1077    10899  14475  10985    766   -760   -102       N  
ATOM   1410  CA  ILE A1077      10.319  25.701  -2.848  1.00 86.60           C  
ANISOU 1410  CA  ILE A1077     9829  13235   9840    768   -673     28       C  
ATOM   1411  C   ILE A1077      11.693  26.252  -3.190  1.00 83.64           C  
ANISOU 1411  C   ILE A1077     9457  12909   9413    750   -682     19       C  
ATOM   1412  O   ILE A1077      11.800  27.357  -3.703  1.00 88.76           O  
ANISOU 1412  O   ILE A1077    10080  13616  10029    760   -631    127       O  
ATOM   1413  CB  ILE A1077      10.022  25.770  -1.334  1.00 86.72           C  
ANISOU 1413  CB  ILE A1077     9986  13032   9933    756   -632     44       C  
ATOM   1414  CG1 ILE A1077       8.574  25.347  -1.049  1.00 82.57           C  
ANISOU 1414  CG1 ILE A1077     9451  12467   9454    778   -617     73       C  
ATOM   1415  CG2 ILE A1077      10.375  27.151  -0.768  1.00 82.02           C  
ANISOU 1415  CG2 ILE A1077     9481  12336   9347    751   -547    151       C  
ATOM   1416  CD1 ILE A1077       8.219  25.219   0.418  1.00 96.57           C  
ANISOU 1416  CD1 ILE A1077    11348  14043  11300    767   -590     75       C  
ATOM   1417  N   LEU A1078      12.739  25.471  -2.898  1.00 89.27           N  
ANISOU 1417  N   LEU A1078    10199  13598  10123    722   -747   -105       N  
ATOM   1418  CA  LEU A1078      14.105  25.938  -3.097  1.00 93.80           C  
ANISOU 1418  CA  LEU A1078    10787  14204  10647    701   -758   -120       C  
ATOM   1419  C   LEU A1078      14.449  25.958  -4.585  1.00 95.29           C  
ANISOU 1419  C   LEU A1078    10833  14619  10753    713   -798   -130       C  
ATOM   1420  O   LEU A1078      15.442  26.569  -4.954  1.00 86.55           O  
ANISOU 1420  O   LEU A1078     9719  13570   9596    702   -797   -109       O  
ATOM   1421  CB  LEU A1078      15.090  25.063  -2.314  1.00 84.05           C  
ANISOU 1421  CB  LEU A1078     9624  12877   9436    669   -815   -248       C  
ATOM   1422  CG  LEU A1078      14.913  25.030  -0.795  1.00 78.89           C  
ANISOU 1422  CG  LEU A1078     9109  12010   8857    650   -779   -243       C  
ATOM   1423  CD1 LEU A1078      15.860  24.032  -0.144  1.00 77.10           C  
ANISOU 1423  CD1 LEU A1078     8929  11716   8650    619   -844   -370       C  
ATOM   1424  CD2 LEU A1078      15.081  26.409  -0.169  1.00 91.90           C  
ANISOU 1424  CD2 LEU A1078    10851  13554  10511    643   -691   -127       C  
ATOM   1425  N   ARG A1079      13.642  25.292  -5.428  1.00101.40           N  
ANISOU 1425  N   ARG A1079    11490  15526  11510    734   -832   -162       N  
ATOM   1426  CA  ARG A1079      13.856  25.298  -6.873  1.00102.87           C  
ANISOU 1426  CA  ARG A1079    11526  15946  11612    746   -868   -170       C  
ATOM   1427  C   ARG A1079      12.928  26.312  -7.546  1.00116.52           C  
ANISOU 1427  C   ARG A1079    13187  17768  13319    774   -801    -14       C  
ATOM   1428  O   ARG A1079      12.751  26.257  -8.764  1.00157.34           O  
ANISOU 1428  O   ARG A1079    18214  23143  18423    787   -825     -7       O  
ATOM   1429  CB  ARG A1079      13.665  23.909  -7.500  1.00 86.68           C  
ANISOU 1429  CB  ARG A1079     9373  14012   9550    748   -953   -316       C  
ATOM   1430  N   ASN A1080      12.331  27.221  -6.760  1.00 96.66           N  
ANISOU 1430  N   ASN A1080    10766  15104  10858    782   -717    111       N  
ATOM   1431  CA  ASN A1080      11.435  28.252  -7.263  1.00 81.72           C  
ANISOU 1431  CA  ASN A1080     8820  13271   8958    809   -644    271       C  
ATOM   1432  C   ASN A1080      12.061  29.627  -7.025  1.00 76.41           C  
ANISOU 1432  C   ASN A1080     8209  12534   8290    804   -578    391       C  
ATOM   1433  O   ASN A1080      12.544  29.919  -5.937  1.00 78.24           O  
ANISOU 1433  O   ASN A1080     8574  12584   8570    785   -551    383       O  
ATOM   1434  CB  ASN A1080      10.052  28.117  -6.625  1.00 85.69           C  
ANISOU 1434  CB  ASN A1080     9366  13664   9528    828   -600    317       C  
ATOM   1435  CG  ASN A1080       8.998  29.017  -7.227  1.00 95.91           C  
ANISOU 1435  CG  ASN A1080    10589  15036  10815    860   -530    475       C  
ATOM   1436  OD1 ASN A1080       9.203  30.222  -7.346  1.00 87.41           O  
ANISOU 1436  OD1 ASN A1080     9522  13953   9738    866   -468    601       O  
ATOM   1437  ND2 ASN A1080       7.840  28.455  -7.552  1.00 98.87           N  
ANISOU 1437  ND2 ASN A1080    10897  15475  11193    879   -537    475       N  
ATOM   1438  N   ALA A1081      12.016  30.487  -8.044  1.00 82.92           N  
ANISOU 1438  N   ALA A1081     8930  13510   9067    820   -550    505       N  
ATOM   1439  CA  ALA A1081      12.622  31.811  -8.011  1.00 83.61           C  
ANISOU 1439  CA  ALA A1081     9050  13561   9157    815   -491    626       C  
ATOM   1440  C   ALA A1081      11.877  32.730  -7.052  1.00 82.66           C  
ANISOU 1440  C   ALA A1081     9036  13246   9123    827   -394    743       C  
ATOM   1441  O   ALA A1081      12.489  33.634  -6.476  1.00 86.27           O  
ANISOU 1441  O   ALA A1081     9581  13584   9613    813   -347    798       O  
ATOM   1442  CB  ALA A1081      12.607  32.419  -9.392  1.00 95.36           C  
ANISOU 1442  CB  ALA A1081    10382  15272  10576    832   -488    728       C  
ATOM   1443  N   LYS A1082      10.564  32.499  -6.918  1.00 79.77           N  
ANISOU 1443  N   LYS A1082     8659  12858   8795    851   -366    778       N  
ATOM   1444  CA  LYS A1082       9.686  33.380  -6.163  1.00104.80           C  
ANISOU 1444  CA  LYS A1082    11906  15870  12043    869   -271    898       C  
ATOM   1445  C   LYS A1082       9.447  32.871  -4.735  1.00105.93           C  
ANISOU 1445  C   LYS A1082    12195  15800  12255    856   -264    818       C  
ATOM   1446  O   LYS A1082       8.831  33.586  -3.946  1.00102.77           O  
ANISOU 1446  O   LYS A1082    11875  15250  11922    867   -186    900       O  
ATOM   1447  CB  LYS A1082       8.365  33.583  -6.917  1.00110.79           C  
ANISOU 1447  CB  LYS A1082    12556  16742  12798    906   -236   1007       C  
ATOM   1448  N   LEU A1083       9.913  31.648  -4.408  1.00101.05           N  
ANISOU 1448  N   LEU A1083    11604  15170  11621    834   -343    661       N  
ATOM   1449  CA  LEU A1083       9.621  31.017  -3.122  1.00 87.85           C  
ANISOU 1449  CA  LEU A1083    10051  13318  10010    821   -345    586       C  
ATOM   1450  C   LEU A1083      10.865  30.856  -2.250  1.00 93.46           C  
ANISOU 1450  C   LEU A1083    10869  13912  10730    782   -370    494       C  
ATOM   1451  O   LEU A1083      10.714  30.792  -1.025  1.00 93.33           O  
ANISOU 1451  O   LEU A1083    10969  13722  10772    769   -343    472       O  
ATOM   1452  CB  LEU A1083       8.927  29.663  -3.297  1.00 80.07           C  
ANISOU 1452  CB  LEU A1083     9012  12392   9019    828   -411    489       C  
ATOM   1453  CG  LEU A1083       7.532  29.699  -3.935  1.00 80.57           C  
ANISOU 1453  CG  LEU A1083     8986  12547   9081    864   -385    572       C  
ATOM   1454  CD1 LEU A1083       6.970  28.297  -4.087  1.00 72.29           C  
ANISOU 1454  CD1 LEU A1083     7886  11553   8028    865   -457    460       C  
ATOM   1455  CD2 LEU A1083       6.549  30.586  -3.176  1.00 77.89           C  
ANISOU 1455  CD2 LEU A1083     8720  12068   8807    885   -290    697       C  
ATOM   1456  N   LYS A1084      12.062  30.785  -2.870  1.00 88.60           N  
ANISOU 1456  N   LYS A1084    10213  13397  10054    764   -420    443       N  
ATOM   1457  CA  LYS A1084      13.306  30.584  -2.135  1.00 88.27           C  
ANISOU 1457  CA  LYS A1084    10263  13263  10012    726   -448    354       C  
ATOM   1458  C   LYS A1084      13.642  31.785  -1.244  1.00 87.45           C  
ANISOU 1458  C   LYS A1084    10273  13002   9951    711   -366    434       C  
ATOM   1459  O   LYS A1084      13.886  31.605  -0.046  1.00103.15           O  
ANISOU 1459  O   LYS A1084    12376  14834  11981    687   -355    382       O  
ATOM   1460  CB  LYS A1084      14.501  30.180  -3.006  1.00 86.97           C  
ANISOU 1460  CB  LYS A1084    10026  13247   9770    710   -523    276       C  
ATOM   1461  CG  LYS A1084      15.739  29.854  -2.178  1.00 92.76           C  
ANISOU 1461  CG  LYS A1084    10859  13881  10505    671   -555    178       C  
ATOM   1462  CD  LYS A1084      16.982  29.449  -2.920  1.00123.26           C  
ANISOU 1462  CD  LYS A1084    14663  17876  14295    654   -629     97       C  
ATOM   1463  CE  LYS A1084      17.694  30.587  -3.624  1.00144.26           C  
ANISOU 1463  CE  LYS A1084    17285  20622  16904    652   -601    189       C  
ATOM   1464  NZ  LYS A1084      18.012  31.731  -2.740  1.00118.73           N  
ANISOU 1464  NZ  LYS A1084    14167  17233  13712    634   -523    272       N  
ATOM   1465  N   PRO A1085      13.671  33.031  -1.779  1.00 83.29           N  
ANISOU 1465  N   PRO A1085     9715  12514   9419    724   -306    561       N  
ATOM   1466  CA  PRO A1085      13.987  34.216  -0.973  1.00 87.88           C  
ANISOU 1466  CA  PRO A1085    10398  12945  10049    709   -225    635       C  
ATOM   1467  C   PRO A1085      13.089  34.418   0.248  1.00 91.85           C  
ANISOU 1467  C   PRO A1085    11002  13263  10632    714   -159    657       C  
ATOM   1468  O   PRO A1085      13.576  34.823   1.307  1.00 85.85           O  
ANISOU 1468  O   PRO A1085    10356  12354   9910    686   -122    639       O  
ATOM   1469  CB  PRO A1085      13.839  35.415  -1.919  1.00 75.29           C  
ANISOU 1469  CB  PRO A1085     8721  11438   8446    732   -172    781       C  
ATOM   1470  CG  PRO A1085      13.049  34.855  -3.076  1.00 92.83           C  
ANISOU 1470  CG  PRO A1085    10804  13844  10625    765   -211    799       C  
ATOM   1471  CD  PRO A1085      13.406  33.384  -3.180  1.00 86.62           C  
ANISOU 1471  CD  PRO A1085     9994  13126   9790    751   -311    642       C  
ATOM   1472  N   VAL A1086      11.792  34.110   0.096  1.00 91.46           N  
ANISOU 1472  N   VAL A1086    10910  13234  10607    747   -146    693       N  
ATOM   1473  CA  VAL A1086      10.848  34.281   1.187  1.00 88.53           C  
ANISOU 1473  CA  VAL A1086    10625  12703  10308    755    -86    720       C  
ATOM   1474  C   VAL A1086      10.992  33.135   2.186  1.00 85.71           C  
ANISOU 1474  C   VAL A1086    10343  12261   9963    729   -138    590       C  
ATOM   1475  O   VAL A1086      10.942  33.371   3.391  1.00 89.62           O  
ANISOU 1475  O   VAL A1086    10945  12598  10507    712    -95    579       O  
ATOM   1476  CB  VAL A1086       9.404  34.446   0.686  1.00 91.79           C  
ANISOU 1476  CB  VAL A1086    10966  13167  10742    800    -49    817       C  
ATOM   1477  CG1 VAL A1086       9.024  33.304  -0.224  1.00 97.36           C  
ANISOU 1477  CG1 VAL A1086    11563  14034  11394    815   -129    761       C  
ATOM   1478  CG2 VAL A1086       8.399  34.571   1.827  1.00103.40           C  
ANISOU 1478  CG2 VAL A1086    12525  14479  12285    810     11    841       C  
ATOM   1479  N   TYR A1087      11.199  31.905   1.688  1.00 79.95           N  
ANISOU 1479  N   TYR A1087     9552  11635   9189    725   -229    491       N  
ATOM   1480  CA  TYR A1087      11.375  30.756   2.570  1.00 72.50           C  
ANISOU 1480  CA  TYR A1087     8667  10616   8262    701   -285    371       C  
ATOM   1481  C   TYR A1087      12.645  30.891   3.409  1.00 70.55           C  
ANISOU 1481  C   TYR A1087     8517  10275   8015    657   -288    310       C  
ATOM   1482  O   TYR A1087      12.665  30.577   4.588  1.00 68.56           O  
ANISOU 1482  O   TYR A1087     8355   9895   7801    634   -281    265       O  
ATOM   1483  CB  TYR A1087      11.414  29.451   1.781  1.00 68.38           C  
ANISOU 1483  CB  TYR A1087     8051  10228   7701    706   -382    276       C  
ATOM   1484  CG  TYR A1087      11.692  28.216   2.600  1.00 66.45           C  
ANISOU 1484  CG  TYR A1087     7854   9913   7480    680   -445    153       C  
ATOM   1485  CD1 TYR A1087      10.651  27.490   3.143  1.00 73.53           C  
ANISOU 1485  CD1 TYR A1087     8761  10752   8424    691   -455    137       C  
ATOM   1486  CD2 TYR A1087      12.975  27.740   2.802  1.00 59.35           C  
ANISOU 1486  CD2 TYR A1087     6983   9010   6558    646   -499     57       C  
ATOM   1487  CE1 TYR A1087      10.870  26.335   3.875  1.00 70.19           C  
ANISOU 1487  CE1 TYR A1087     8371  10266   8030    668   -515     32       C  
ATOM   1488  CE2 TYR A1087      13.211  26.572   3.499  1.00 55.44           C  
ANISOU 1488  CE2 TYR A1087     6519   8455   6089    624   -559    -49       C  
ATOM   1489  CZ  TYR A1087      12.156  25.876   4.054  1.00 67.08           C  
ANISOU 1489  CZ  TYR A1087     8002   9869   7617    634   -566    -60       C  
ATOM   1490  OH  TYR A1087      12.320  24.744   4.801  1.00 88.55           O  
ANISOU 1490  OH  TYR A1087    10749  12522  10374    613   -622   -152       O  
ATOM   1491  N   ASP A1088      13.708  31.387   2.792  1.00 79.68           N  
ANISOU 1491  N   ASP A1088     9651  11502   9124    643   -298    315       N  
ATOM   1492  CA  ASP A1088      14.967  31.536   3.495  1.00 97.96           C  
ANISOU 1492  CA  ASP A1088    12050  13741  11428    600   -302    260       C  
ATOM   1493  C   ASP A1088      14.869  32.612   4.570  1.00 90.40           C  
ANISOU 1493  C   ASP A1088    11200  12623  10523    586   -209    322       C  
ATOM   1494  O   ASP A1088      15.664  32.604   5.509  1.00 92.60           O  
ANISOU 1494  O   ASP A1088    11568  12808  10808    547   -206    267       O  
ATOM   1495  CB  ASP A1088      16.128  31.776   2.525  1.00108.09           C  
ANISOU 1495  CB  ASP A1088    13276  15148  12643    590   -340    250       C  
ATOM   1496  CG  ASP A1088      16.455  30.556   1.682  1.00121.23           C  
ANISOU 1496  CG  ASP A1088    14849  16957  14256    594   -440    153       C  
ATOM   1497  OD1 ASP A1088      15.961  29.451   1.992  1.00133.16           O  
ANISOU 1497  OD1 ASP A1088    16354  18450  15789    597   -485     78       O  
ATOM   1498  OD2 ASP A1088      17.179  30.722   0.712  1.00132.59           O1-
ANISOU 1498  OD2 ASP A1088    16218  18525  15635    595   -472    153       O1-
ATOM   1499  N   SER A1089      13.935  33.556   4.399  1.00 80.93           N  
ANISOU 1499  N   SER A1089     9987  11401   9361    617   -133    435       N  
ATOM   1500  CA  SER A1089      13.786  34.662   5.339  1.00 83.21           C  
ANISOU 1500  CA  SER A1089    10369  11541   9706    607    -39    496       C  
ATOM   1501  C   SER A1089      12.810  34.310   6.465  1.00 89.79           C  
ANISOU 1501  C   SER A1089    11266  12254  10595    610    -11    480       C  
ATOM   1502  O   SER A1089      12.839  34.924   7.527  1.00 83.84           O  
ANISOU 1502  O   SER A1089    10604  11367   9884    591     53    487       O  
ATOM   1503  CB  SER A1089      13.353  35.914   4.642  1.00 81.90           C  
ANISOU 1503  CB  SER A1089    10158  11400   9561    637     32    628       C  
ATOM   1504  OG  SER A1089      12.090  35.711   4.015  1.00 81.54           O  
ANISOU 1504  OG  SER A1089    10033  11422   9526    683     36    689       O  
ATOM   1505  N   LEU A1090      11.930  33.328   6.225  1.00 86.16           N  
ANISOU 1505  N   LEU A1090    10755  11848  10135    635    -57    457       N  
ATOM   1506  CA  LEU A1090      10.961  32.932   7.230  1.00 72.58           C  
ANISOU 1506  CA  LEU A1090     9085  10027   8464    640    -37    447       C  
ATOM   1507  C   LEU A1090      11.643  32.121   8.335  1.00 75.57           C  
ANISOU 1507  C   LEU A1090     9539  10329   8844    596    -79    339       C  
ATOM   1508  O   LEU A1090      12.618  31.405   8.093  1.00 76.40           O  
ANISOU 1508  O   LEU A1090     9629  10491   8909    572   -150    258       O  
ATOM   1509  CB  LEU A1090       9.831  32.151   6.554  1.00 70.73           C  
ANISOU 1509  CB  LEU A1090     8764   9882   8227    679    -76    462       C  
ATOM   1510  CG  LEU A1090       8.839  33.001   5.757  1.00 82.02           C  
ANISOU 1510  CG  LEU A1090    10132  11363   9671    725    -16    586       C  
ATOM   1511  CD1 LEU A1090       7.759  32.132   5.122  1.00 86.03           C  
ANISOU 1511  CD1 LEU A1090    10553  11965  10168    758    -59    590       C  
ATOM   1512  CD2 LEU A1090       8.197  34.091   6.616  1.00 84.35           C  
ANISOU 1512  CD2 LEU A1090    10500  11521  10028    734     87    667       C  
ATOM   1513  N   ASP A1091      11.106  32.245   9.559  1.00 70.66           N  
ANISOU 1513  N   ASP A1091     8994   9582   8270    586    -32    341       N  
ATOM   1514  CA  ASP A1091      11.483  31.422  10.697  1.00 67.67           C  
ANISOU 1514  CA  ASP A1091     8678   9133   7901    548    -67    254       C  
ATOM   1515  C   ASP A1091      10.966  29.995  10.498  1.00 76.75           C  
ANISOU 1515  C   ASP A1091     9772  10340   9051    560   -152    201       C  
ATOM   1516  O   ASP A1091      10.129  29.735   9.626  1.00 81.13           O  
ANISOU 1516  O   ASP A1091    10249  10973   9604    599   -171    236       O  
ATOM   1517  CB  ASP A1091      10.944  32.019  11.991  1.00 67.29           C  
ANISOU 1517  CB  ASP A1091     8715   8951   7901    537     10    280       C  
ATOM   1518  CG  ASP A1091       9.499  32.454  11.854  1.00 78.41           C  
ANISOU 1518  CG  ASP A1091    10100  10344   9349    584     64    368       C  
ATOM   1519  OD1 ASP A1091       9.262  33.613  11.448  1.00 76.73           O  
ANISOU 1519  OD1 ASP A1091     9882  10120   9151    606    136    450       O  
ATOM   1520  OD2 ASP A1091       8.611  31.620  12.134  1.00 87.56           O1-
ANISOU 1520  OD2 ASP A1091    11240  11503  10525    599     33    358       O1-
ATOM   1521  N   ALA A1092      11.453  29.070  11.337  1.00 71.38           N  
ANISOU 1521  N   ALA A1092     9128   9617   8377    525   -203    117       N  
ATOM   1522  CA  ALA A1092      11.148  27.653  11.189  1.00 62.94           C  
ANISOU 1522  CA  ALA A1092     8005   8593   7316    530   -290     56       C  
ATOM   1523  C   ALA A1092       9.640  27.415  11.263  1.00 65.68           C  
ANISOU 1523  C   ALA A1092     8324   8929   7702    567   -276    107       C  
ATOM   1524  O   ALA A1092       9.138  26.547  10.565  1.00 71.31           O  
ANISOU 1524  O   ALA A1092     8962   9717   8416    589   -336     87       O  
ATOM   1525  CB  ALA A1092      11.902  26.843  12.213  1.00 62.57           C  
ANISOU 1525  CB  ALA A1092     8006   8487   7279    485   -334    -24       C  
ATOM   1526  N   VAL A1093       8.927  28.198  12.094  1.00 64.73           N  
ANISOU 1526  N   VAL A1093     8264   8718   7614    572   -197    171       N  
ATOM   1527  CA  VAL A1093       7.494  28.038  12.260  1.00 61.82           C  
ANISOU 1527  CA  VAL A1093     7876   8334   7280    606   -178    224       C  
ATOM   1528  C   VAL A1093       6.783  28.502  10.993  1.00 64.05           C  
ANISOU 1528  C   VAL A1093     8084   8705   7547    653   -159    296       C  
ATOM   1529  O   VAL A1093       5.987  27.758  10.430  1.00 54.96           O  
ANISOU 1529  O   VAL A1093     6864   7619   6399    680   -203    298       O  
ATOM   1530  CB  VAL A1093       6.962  28.763  13.507  1.00 67.60           C  
ANISOU 1530  CB  VAL A1093     8690   8949   8048    599    -98    268       C  
ATOM   1531  CG1 VAL A1093       5.477  28.460  13.736  1.00 75.19           C  
ANISOU 1531  CG1 VAL A1093     9629   9896   9043    633    -88    318       C  
ATOM   1532  CG2 VAL A1093       7.789  28.403  14.730  1.00 78.16           C  
ANISOU 1532  CG2 VAL A1093    10095  10212   9390    547   -112    199       C  
ATOM   1533  N   ARG A1094       7.085  29.724  10.545  1.00 69.60           N  
ANISOU 1533  N   ARG A1094     8796   9414   8236    662    -93    356       N  
ATOM   1534  CA  ARG A1094       6.463  30.278   9.349  1.00 67.46           C  
ANISOU 1534  CA  ARG A1094     8448   9232   7950    706    -67    438       C  
ATOM   1535  C   ARG A1094       6.969  29.590   8.086  1.00 64.02           C  
ANISOU 1535  C   ARG A1094     7920   8940   7466    710   -146    394       C  
ATOM   1536  O   ARG A1094       6.340  29.706   7.051  1.00 71.06           O  
ANISOU 1536  O   ARG A1094     8728   9931   8339    745   -145    448       O  
ATOM   1537  CB  ARG A1094       6.650  31.794   9.262  1.00 69.16           C  
ANISOU 1537  CB  ARG A1094     8696   9408   8174    713     26    522       C  
ATOM   1538  CG  ARG A1094       5.724  32.562  10.202  1.00 74.60           C  
ANISOU 1538  CG  ARG A1094     9447   9981   8917    727    115    588       C  
ATOM   1539  CD  ARG A1094       5.888  34.065  10.124  1.00 66.93           C  
ANISOU 1539  CD  ARG A1094     8503   8960   7968    735    210    668       C  
ATOM   1540  NE  ARG A1094       6.754  34.574  11.163  1.00 64.05           N  
ANISOU 1540  NE  ARG A1094     8232   8486   7619    693    247    623       N  
ATOM   1541  CZ  ARG A1094       6.331  35.222  12.229  1.00 62.21           C  
ANISOU 1541  CZ  ARG A1094     8071   8134   7434    688    321    642       C  
ATOM   1542  NH1 ARG A1094       5.038  35.440  12.377  1.00 61.08           N  
ANISOU 1542  NH1 ARG A1094     7916   7964   7327    727    366    709       N  
ATOM   1543  NH2 ARG A1094       7.198  35.663  13.127  1.00 55.10           N  
ANISOU 1543  NH2 ARG A1094     7248   7146   6540    645    352    592       N  
ATOM   1544  N   ARG A1095       8.098  28.885   8.162  1.00 62.07           N  
ANISOU 1544  N   ARG A1095     7680   8709   7195    675   -213    296       N  
ATOM   1545  CA  ARG A1095       8.524  28.028   7.067  1.00 66.62           C  
ANISOU 1545  CA  ARG A1095     8165   9418   7730    679   -298    234       C  
ATOM   1546  C   ARG A1095       7.565  26.850   6.909  1.00 67.33           C  
ANISOU 1546  C   ARG A1095     8197   9547   7839    697   -356    201       C  
ATOM   1547  O   ARG A1095       7.176  26.543   5.785  1.00 75.66           O  
ANISOU 1547  O   ARG A1095     9155  10726   8868    722   -388    206       O  
ATOM   1548  CB  ARG A1095       9.940  27.492   7.287  1.00 69.66           C  
ANISOU 1548  CB  ARG A1095     8576   9800   8092    637   -356    133       C  
ATOM   1549  CG  ARG A1095      11.049  28.480   6.969  1.00 68.16           C  
ANISOU 1549  CG  ARG A1095     8407   9627   7862    621   -324    153       C  
ATOM   1550  CD  ARG A1095      12.367  27.762   7.159  1.00 69.50           C  
ANISOU 1550  CD  ARG A1095     8595   9805   8008    582   -391     47       C  
ATOM   1551  NE  ARG A1095      13.500  28.618   6.841  1.00 70.92           N  
ANISOU 1551  NE  ARG A1095     8794  10008   8145    564   -369     59       N  
ATOM   1552  CZ  ARG A1095      14.756  28.217   6.887  1.00 67.27           C  
ANISOU 1552  CZ  ARG A1095     8346   9563   7650    530   -419    -19       C  
ATOM   1553  NH1 ARG A1095      15.035  26.973   7.244  1.00 71.39           N  
ANISOU 1553  NH1 ARG A1095     8863  10078   8183    513   -491   -115       N  
ATOM   1554  NH2 ARG A1095      15.716  29.052   6.552  1.00 65.16           N  
ANISOU 1554  NH2 ARG A1095     8092   9322   7342    516   -396      2       N  
ATOM   1555  N   ALA A1096       7.180  26.220   8.033  1.00 67.02           N  
ANISOU 1555  N   ALA A1096     8213   9406   7846    682   -368    170       N  
ATOM   1556  CA  ALA A1096       6.228  25.118   8.025  1.00 76.17           C  
ANISOU 1556  CA  ALA A1096     9323  10584   9034    697   -420    144       C  
ATOM   1557  C   ALA A1096       4.882  25.558   7.441  1.00 78.43           C  
ANISOU 1557  C   ALA A1096     9559  10919   9320    741   -376    239       C  
ATOM   1558  O   ALA A1096       4.217  24.764   6.776  1.00 71.83           O  
ANISOU 1558  O   ALA A1096     8644  10166   8483    760   -425    220       O  
ATOM   1559  CB  ALA A1096       6.057  24.521   9.403  1.00 73.18           C  
ANISOU 1559  CB  ALA A1096     9014  10084   8706    672   -431    113       C  
ATOM   1560  N   ALA A1097       4.497  26.821   7.682  1.00 71.44           N  
ANISOU 1560  N   ALA A1097     8719   9985   8440    757   -283    339       N  
ATOM   1561  CA  ALA A1097       3.271  27.355   7.115  1.00 74.15           C  
ANISOU 1561  CA  ALA A1097     9015  10374   8784    800   -233    440       C  
ATOM   1562  C   ALA A1097       3.396  27.471   5.595  1.00 77.32           C  
ANISOU 1562  C   ALA A1097     9309  10935   9134    821   -253    458       C  
ATOM   1563  O   ALA A1097       2.431  27.217   4.878  1.00 83.50           O  
ANISOU 1563  O   ALA A1097    10015  11806   9907    851   -261    496       O  
ATOM   1564  CB  ALA A1097       2.903  28.665   7.761  1.00 70.51           C  
ANISOU 1564  CB  ALA A1097     8625   9816   8349    812   -129    537       C  
ATOM   1565  N   LEU A1098       4.588  27.837   5.107  1.00 76.84           N  
ANISOU 1565  N   LEU A1098     9240  10919   9036    803   -263    430       N  
ATOM   1566  CA  LEU A1098       4.827  27.948   3.675  1.00 70.61           C  
ANISOU 1566  CA  LEU A1098     8344  10292   8192    819   -286    443       C  
ATOM   1567  C   LEU A1098       4.897  26.576   3.014  1.00 65.27           C  
ANISOU 1567  C   LEU A1098     7583   9725   7493    814   -386    338       C  
ATOM   1568  O   LEU A1098       4.382  26.407   1.911  1.00 62.07           O  
ANISOU 1568  O   LEU A1098     7072   9460   7053    837   -404    358       O  
ATOM   1569  CB  LEU A1098       6.104  28.742   3.405  1.00 77.56           C  
ANISOU 1569  CB  LEU A1098     9243  11186   9040    800   -269    446       C  
ATOM   1570  CG  LEU A1098       6.241  29.170   1.945  1.00 88.20           C  
ANISOU 1570  CG  LEU A1098    10478  12703  10331    820   -273    495       C  
ATOM   1571  CD1 LEU A1098       5.048  30.004   1.516  1.00100.08           C  
ANISOU 1571  CD1 LEU A1098    11939  14239  11846    860   -199    631       C  
ATOM   1572  CD2 LEU A1098       7.528  29.935   1.705  1.00 97.17           C  
ANISOU 1572  CD2 LEU A1098    11631  13852  11436    800   -260    499       C  
ATOM   1573  N   ILE A1099       5.516  25.606   3.699  1.00 66.02           N  
ANISOU 1573  N   ILE A1099     7720   9756   7610    783   -449    227       N  
ATOM   1574  CA  ILE A1099       5.542  24.228   3.224  1.00 69.74           C  
ANISOU 1574  CA  ILE A1099     8116  10304   8077    777   -543    119       C  
ATOM   1575  C   ILE A1099       4.127  23.673   3.201  1.00 68.94           C  
ANISOU 1575  C   ILE A1099     7974  10215   8005    801   -549    145       C  
ATOM   1576  O   ILE A1099       3.805  22.915   2.300  1.00 74.38           O  
ANISOU 1576  O   ILE A1099     8563  11022   8675    811   -604     98       O  
ATOM   1577  CB  ILE A1099       6.439  23.307   4.077  1.00 78.94           C  
ANISOU 1577  CB  ILE A1099     9338  11381   9275    739   -605      6       C  
ATOM   1578  CG1 ILE A1099       7.866  23.832   4.179  1.00 77.34           C  
ANISOU 1578  CG1 ILE A1099     9182  11163   9042    712   -599    -22       C  
ATOM   1579  CG2 ILE A1099       6.413  21.866   3.562  1.00 83.06           C  
ANISOU 1579  CG2 ILE A1099     9775  11976   9807    735   -701   -107       C  
ATOM   1580  CD1 ILE A1099       8.639  23.176   5.280  1.00 77.37           C  
ANISOU 1580  CD1 ILE A1099     9262  11053   9082    675   -635   -102       C  
ATOM   1581  N   ASN A1100       3.306  24.044   4.194  1.00 75.09           N  
ANISOU 1581  N   ASN A1100     8828  10874   8828    809   -493    216       N  
ATOM   1582  CA  ASN A1100       1.943  23.545   4.315  1.00 71.13           C  
ANISOU 1582  CA  ASN A1100     8299  10370   8357    831   -496    248       C  
ATOM   1583  C   ASN A1100       1.151  23.897   3.061  1.00 67.86           C  
ANISOU 1583  C   ASN A1100     7783  10102   7899    866   -475    316       C  
ATOM   1584  O   ASN A1100       0.439  23.046   2.559  1.00 72.59           O  
ANISOU 1584  O   ASN A1100     8305  10777   8498    876   -522    285       O  
ATOM   1585  CB  ASN A1100       1.229  24.048   5.570  1.00 66.85           C  
ANISOU 1585  CB  ASN A1100     7855   9683   7862    835   -431    322       C  
ATOM   1586  CG  ASN A1100      -0.090  23.346   5.783  1.00 72.86           C  
ANISOU 1586  CG  ASN A1100     8590  10439   8655    853   -448    341       C  
ATOM   1587  OD1 ASN A1100      -1.044  23.564   5.043  1.00 80.36           O  
ANISOU 1587  OD1 ASN A1100     9475  11474   9585    885   -425    408       O  
ATOM   1588  ND2 ASN A1100      -0.155  22.505   6.796  1.00 79.87           N  
ANISOU 1588  ND2 ASN A1100     9525  11231   9593    832   -489    288       N  
ATOM   1589  N   MET A1101       1.282  25.139   2.571  1.00 61.59           N  
ANISOU 1589  N   MET A1101     6982   9348   7070    882   -405    411       N  
ATOM   1590  CA  MET A1101       0.545  25.572   1.398  1.00 64.82           C  
ANISOU 1590  CA  MET A1101     7289   9901   7437    914   -379    493       C  
ATOM   1591  C   MET A1101       1.036  24.814   0.164  1.00 76.96           C  
ANISOU 1591  C   MET A1101     8709  11611   8921    908   -456    405       C  
ATOM   1592  O   MET A1101       0.224  24.358  -0.634  1.00 80.38           O  
ANISOU 1592  O   MET A1101     9045  12165   9332    925   -477    411       O  
ATOM   1593  CB  MET A1101       0.684  27.073   1.160  1.00 62.59           C  
ANISOU 1593  CB  MET A1101     7022   9620   7138    931   -289    616       C  
ATOM   1594  CG  MET A1101       0.008  27.916   2.183  1.00 65.58           C  
ANISOU 1594  CG  MET A1101     7496   9853   7568    945   -203    711       C  
ATOM   1595  SD  MET A1101       0.239  29.692   1.820  1.00 89.24           S  
ANISOU 1595  SD  MET A1101    10501  12849  10559    965    -98    853       S  
ATOM   1596  CE  MET A1101      -0.749  29.868   0.337  1.00102.73           C  
ANISOU 1596  CE  MET A1101    12060  14753  12220   1004    -86    952       C  
ATOM   1597  N   VAL A1102       2.357  24.676   0.001  1.00 74.18           N  
ANISOU 1597  N   VAL A1102     8362  11277   8547    882   -497    323       N  
ATOM   1598  CA  VAL A1102       2.894  23.962  -1.147  1.00 64.93           C  
ANISOU 1598  CA  VAL A1102     7076  10269   7324    875   -571    231       C  
ATOM   1599  C   VAL A1102       2.439  22.504  -1.107  1.00 67.79           C  
ANISOU 1599  C   VAL A1102     7397  10644   7716    867   -650    119       C  
ATOM   1600  O   VAL A1102       2.214  21.905  -2.155  1.00 68.39           O  
ANISOU 1600  O   VAL A1102     7356  10874   7755    873   -697     69       O  
ATOM   1601  CB  VAL A1102       4.424  24.094  -1.205  1.00 65.76           C  
ANISOU 1601  CB  VAL A1102     7206  10377   7404    848   -599    163       C  
ATOM   1602  CG1 VAL A1102       5.078  23.212  -2.255  1.00 56.06           C  
ANISOU 1602  CG1 VAL A1102     5868   9305   6128    838   -684     45       C  
ATOM   1603  CG2 VAL A1102       4.853  25.546  -1.362  1.00 76.34           C  
ANISOU 1603  CG2 VAL A1102     8574  11718   8716    856   -523    277       C  
ATOM   1604  N   PHE A1103       2.264  21.949   0.101  1.00 65.09           N  
ANISOU 1604  N   PHE A1103     7146  10142   7442    853   -663     84       N  
ATOM   1605  CA  PHE A1103       1.821  20.573   0.240  1.00 68.40           C  
ANISOU 1605  CA  PHE A1103     7530  10554   7903    845   -737    -14       C  
ATOM   1606  C   PHE A1103       0.380  20.419  -0.232  1.00 68.94           C  
ANISOU 1606  C   PHE A1103     7529  10696   7968    872   -723     45       C  
ATOM   1607  O   PHE A1103       0.035  19.397  -0.813  1.00 71.60           O  
ANISOU 1607  O   PHE A1103     7778  11118   8308    870   -787    -37       O  
ATOM   1608  CB  PHE A1103       1.986  20.059   1.669  1.00 62.76           C  
ANISOU 1608  CB  PHE A1103     6924   9657   7264    823   -754    -51       C  
ATOM   1609  CG  PHE A1103       1.953  18.558   1.769  1.00 64.27           C  
ANISOU 1609  CG  PHE A1103     7074   9839   7505    806   -845   -174       C  
ATOM   1610  CD1 PHE A1103       0.756  17.865   1.880  1.00 75.36           C  
ANISOU 1610  CD1 PHE A1103     8446  11237   8950    817   -864   -168       C  
ATOM   1611  CD2 PHE A1103       3.122  17.821   1.719  1.00 61.51           C  
ANISOU 1611  CD2 PHE A1103     6715   9490   7168    780   -913   -297       C  
ATOM   1612  CE1 PHE A1103       0.717  16.473   1.968  1.00 79.18           C  
ANISOU 1612  CE1 PHE A1103     8887  11706   9490    801   -949   -280       C  
ATOM   1613  CE2 PHE A1103       3.091  16.435   1.806  1.00 69.13           C  
ANISOU 1613  CE2 PHE A1103     7636  10438   8191    765   -996   -410       C  
ATOM   1614  CZ  PHE A1103       1.894  15.757   1.950  1.00 74.34           C  
ANISOU 1614  CZ  PHE A1103     8265  11084   8898    775  -1014   -402       C  
ATOM   1615  N   GLN A1104      -0.450  21.441   0.001  1.00 68.76           N  
ANISOU 1615  N   GLN A1104     7542  10642   7940    897   -638    184       N  
ATOM   1616  CA  GLN A1104      -1.841  21.396  -0.432  1.00 89.11           C  
ANISOU 1616  CA  GLN A1104    10058  13292  10510    924   -617    255       C  
ATOM   1617  C   GLN A1104      -1.984  21.778  -1.911  1.00 98.53           C  
ANISOU 1617  C   GLN A1104    11123  14690  11626    941   -607    290       C  
ATOM   1618  O   GLN A1104      -2.563  21.027  -2.696  1.00106.20           O  
ANISOU 1618  O   GLN A1104    11990  15785  12576    945   -650    245       O  
ATOM   1619  CB  GLN A1104      -2.723  22.259   0.468  1.00 83.47           C  
ANISOU 1619  CB  GLN A1104     9432  12458   9827    945   -532    387       C  
ATOM   1620  CG  GLN A1104      -4.193  22.119   0.133  1.00 88.41           C  
ANISOU 1620  CG  GLN A1104     9999  13145  10447    972   -513    458       C  
ATOM   1621  CD  GLN A1104      -5.067  23.080   0.900  1.00 89.63           C  
ANISOU 1621  CD  GLN A1104    10231  13198  10626    997   -423    596       C  
ATOM   1622  OE1 GLN A1104      -4.603  24.050   1.509  1.00 70.14           O  
ANISOU 1622  OE1 GLN A1104     7848  10632   8171    998   -363    651       O  
ATOM   1623  NE2 GLN A1104      -6.362  22.807   0.852  1.00 98.68           N  
ANISOU 1623  NE2 GLN A1104    11345  14372  11779   1017   -414    648       N  
ATOM   1624  N   MET A1105      -1.475  22.959  -2.283  1.00 88.47           N  
ANISOU 1624  N   MET A1105     9851  13452  10310    951   -548    374       N  
ATOM   1625  CA  MET A1105      -1.691  23.516  -3.609  1.00 83.17           C  
ANISOU 1625  CA  MET A1105     9061  12974   9567    970   -525    440       C  
ATOM   1626  C   MET A1105      -0.611  23.035  -4.578  1.00 89.35           C  
ANISOU 1626  C   MET A1105     9753  13901  10296    950   -593    329       C  
ATOM   1627  O   MET A1105      -0.888  22.287  -5.510  1.00102.72           O  
ANISOU 1627  O   MET A1105    11328  15749  11951    949   -645    263       O  
ATOM   1628  CB  MET A1105      -1.726  25.044  -3.555  1.00 84.77           C  
ANISOU 1628  CB  MET A1105     9301  13147   9759    990   -427    597       C  
ATOM   1629  CG  MET A1105      -2.756  25.561  -2.543  1.00102.05           C  
ANISOU 1629  CG  MET A1105    11582  15187  12005   1011   -355    702       C  
ATOM   1630  SD  MET A1105      -2.891  27.375  -2.401  1.00109.54           S  
ANISOU 1630  SD  MET A1105    12578  16081  12962   1038   -233    886       S  
ATOM   1631  CE  MET A1105      -3.452  27.747  -4.063  1.00109.58           C  
ANISOU 1631  CE  MET A1105    12411  16334  12890   1063   -217    979       C  
ATOM   1632  N   GLY A1106       0.632  23.451  -4.352  1.00 86.84           N  
ANISOU 1632  N   GLY A1106     9490  13534   9973    933   -595    302       N  
ATOM   1633  CA  GLY A1106       1.716  23.074  -5.246  1.00 83.67           C  
ANISOU 1633  CA  GLY A1106     9006  13268   9517    916   -657    201       C  
ATOM   1634  C   GLY A1106       2.758  24.184  -5.313  1.00 93.68           C  
ANISOU 1634  C   GLY A1106    10310  14529  10755    912   -617    262       C  
ATOM   1635  O   GLY A1106       2.478  25.315  -4.895  1.00 97.56           O  
ANISOU 1635  O   GLY A1106    10865  14941  11263    927   -535    395       O  
ATOM   1636  N   GLU A1107       3.948  23.855  -5.839  1.00 89.99           N  
ANISOU 1636  N   GLU A1107     9801  14144  10247    892   -675    163       N  
ATOM   1637  CA  GLU A1107       5.032  24.823  -5.913  1.00 98.79           C  
ANISOU 1637  CA  GLU A1107    10948  15257  11332    884   -646    209       C  
ATOM   1638  C   GLU A1107       4.611  26.014  -6.777  1.00102.57           C  
ANISOU 1638  C   GLU A1107    11350  15860  11762    909   -578    365       C  
ATOM   1639  O   GLU A1107       4.690  27.168  -6.359  1.00110.59           O  
ANISOU 1639  O   GLU A1107    12435  16787  12798    916   -504    484       O  
ATOM   1640  CB  GLU A1107       6.328  24.178  -6.413  1.00 95.57           C  
ANISOU 1640  CB  GLU A1107    10496  14935  10883    859   -726     72       C  
ATOM   1641  N   THR A1108       4.146  25.729  -7.995  1.00106.75           N  
ANISOU 1641  N   THR A1108    11731  16599  12230    921   -603    365       N  
ATOM   1642  CA  THR A1108       3.807  26.800  -8.921  1.00104.77           C  
ANISOU 1642  CA  THR A1108    11387  16493  11928    942   -545    513       C  
ATOM   1643  C   THR A1108       2.475  27.446  -8.546  1.00102.55           C  
ANISOU 1643  C   THR A1108    11135  16141  11689    971   -463    659       C  
ATOM   1644  O   THR A1108       2.213  28.565  -8.965  1.00111.67           O  
ANISOU 1644  O   THR A1108    12254  17348  12829    990   -394    810       O  
ATOM   1645  CB  THR A1108       3.867  26.352 -10.386  1.00 95.63           C  
ANISOU 1645  CB  THR A1108    10050  15604  10680    943   -597    468       C  
ATOM   1646  OG1 THR A1108       3.125  25.141 -10.466  1.00102.66           O  
ANISOU 1646  OG1 THR A1108    10897  16529  11580    941   -649    362       O  
ATOM   1647  CG2 THR A1108       5.275  26.094 -10.868  1.00 96.59           C  
ANISOU 1647  CG2 THR A1108    10136  15813  10751    919   -661    363       C  
ATOM   1648  N   GLY A1109       1.641  26.734  -7.782  1.00107.52           N  
ANISOU 1648  N   GLY A1109    11825  16656  12372    974   -470    616       N  
ATOM   1649  CA  GLY A1109       0.368  27.256  -7.294  1.00112.02           C  
ANISOU 1649  CA  GLY A1109    12435  17142  12986   1000   -396    743       C  
ATOM   1650  C   GLY A1109       0.506  28.412  -6.294  1.00108.54           C  
ANISOU 1650  C   GLY A1109    12126  16510  12605   1008   -313    850       C  
ATOM   1651  O   GLY A1109      -0.075  29.479  -6.492  1.00 90.09           O  
ANISOU 1651  O   GLY A1109     9772  14184  10275   1033   -233   1004       O  
ATOM   1652  N   VAL A1110       1.272  28.196  -5.216  1.00106.42           N  
ANISOU 1652  N   VAL A1110    11985  16067  12384    984   -330    768       N  
ATOM   1653  CA  VAL A1110       1.411  29.187  -4.157  1.00105.76           C  
ANISOU 1653  CA  VAL A1110    12031  15793  12359    986   -255    848       C  
ATOM   1654  C   VAL A1110       2.288  30.347  -4.621  1.00111.70           C  
ANISOU 1654  C   VAL A1110    12768  16584  13089    985   -214    928       C  
ATOM   1655  O   VAL A1110       2.250  31.415  -4.012  1.00107.74           O  
ANISOU 1655  O   VAL A1110    12345  15956  12634    993   -136   1026       O  
ATOM   1656  CB  VAL A1110       1.951  28.589  -2.843  1.00109.20           C  
ANISOU 1656  CB  VAL A1110    12601  16041  12849    958   -286    737       C  
ATOM   1657  CG1 VAL A1110       1.053  27.490  -2.334  1.00116.38           C  
ANISOU 1657  CG1 VAL A1110    13525  16905  13790    960   -324    672       C  
ATOM   1658  CG2 VAL A1110       3.378  28.084  -2.986  1.00125.98           C  
ANISOU 1658  CG2 VAL A1110    14729  18194  14943    925   -357    612       C  
ATOM   1659  N   ALA A1111       3.084  30.124  -5.681  1.00121.28           N  
ANISOU 1659  N   ALA A1111    13880  17969  14232    974   -268    881       N  
ATOM   1660  CA  ALA A1111       3.929  31.163  -6.262  1.00117.93           C  
ANISOU 1660  CA  ALA A1111    13421  17609  13778    972   -239    959       C  
ATOM   1661  C   ALA A1111       3.086  32.282  -6.885  1.00118.96           C  
ANISOU 1661  C   ALA A1111    13478  17811  13909   1005   -157   1144       C  
ATOM   1662  O   ALA A1111       3.585  33.384  -7.114  1.00107.95           O  
ANISOU 1662  O   ALA A1111    12079  16419  12519   1008   -108   1245       O  
ATOM   1663  CB  ALA A1111       4.921  30.571  -7.239  1.00111.96           C  
ANISOU 1663  CB  ALA A1111    12567  17030  12943    952   -321    861       C  
ATOM   1664  N   GLY A1112       1.798  31.999  -7.128  1.00112.07           N  
ANISOU 1664  N   GLY A1112    12550  16993  13038   1030   -140   1191       N  
ATOM   1665  CA  GLY A1112       0.847  32.953  -7.662  1.00104.31           C  
ANISOU 1665  CA  GLY A1112    11497  16075  12061   1064    -61   1367       C  
ATOM   1666  C   GLY A1112       0.514  34.057  -6.666  1.00115.01           C  
ANISOU 1666  C   GLY A1112    12968  17224  13504   1080     35   1480       C  
ATOM   1667  O   GLY A1112       0.085  35.129  -7.073  1.00160.93           O  
ANISOU 1667  O   GLY A1112    18737  23072  19339   1105    110   1638       O  
ATOM   1668  N   PHE A1113       0.699  33.800  -5.366  1.00116.16           N  
ANISOU 1668  N   PHE A1113    13261  17164  13708   1065     36   1400       N  
ATOM   1669  CA  PHE A1113       0.351  34.772  -4.337  1.00105.60           C  
ANISOU 1669  CA  PHE A1113    12037  15628  12456   1078    126   1488       C  
ATOM   1670  C   PHE A1113       1.444  35.825  -4.244  1.00101.48           C  
ANISOU 1670  C   PHE A1113    11556  15046  11956   1064    163   1531       C  
ATOM   1671  O   PHE A1113       2.003  36.052  -3.173  1.00117.52           O  
ANISOU 1671  O   PHE A1113    13715  16901  14037   1044    181   1482       O  
ATOM   1672  CB  PHE A1113       0.170  34.116  -2.968  1.00102.88           C  
ANISOU 1672  CB  PHE A1113    11829  15099  12161   1064    113   1385       C  
ATOM   1673  CG  PHE A1113      -0.994  33.166  -2.865  1.00112.93           C  
ANISOU 1673  CG  PHE A1113    13081  16398  13431   1078     86   1355       C  
ATOM   1674  CD1 PHE A1113      -0.850  31.826  -3.209  1.00111.96           C  
ANISOU 1674  CD1 PHE A1113    12910  16372  13260   1060    -11   1223       C  
ATOM   1675  CD2 PHE A1113      -2.235  33.618  -2.436  1.00113.09           C  
ANISOU 1675  CD2 PHE A1113    13124  16346  13497   1110    157   1458       C  
ATOM   1676  CE1 PHE A1113      -1.919  30.950  -3.110  1.00 99.87           C  
ANISOU 1676  CE1 PHE A1113    11357  14860  11730   1071    -37   1195       C  
ATOM   1677  CE2 PHE A1113      -3.306  32.741  -2.340  1.00115.31           C  
ANISOU 1677  CE2 PHE A1113    13386  16654  13774   1122    130   1433       C  
ATOM   1678  CZ  PHE A1113      -3.140  31.411  -2.672  1.00106.35           C  
ANISOU 1678  CZ  PHE A1113    12205  15612  12593   1102     33   1302       C  
ATOM   1679  N   THR A1114       1.707  36.472  -5.383  1.00 96.87           N  
ANISOU 1679  N   THR A1114    10856  14616  11334   1074    176   1627       N  
ATOM   1680  CA  THR A1114       2.716  37.515  -5.503  1.00108.45           C  
ANISOU 1680  CA  THR A1114    12335  16055  12817   1062    209   1687       C  
ATOM   1681  C   THR A1114       2.490  38.578  -4.433  1.00111.24           C  
ANISOU 1681  C   THR A1114    12807  16187  13272   1071    305   1764       C  
ATOM   1682  O   THR A1114       3.443  39.115  -3.865  1.00 96.65           O  
ANISOU 1682  O   THR A1114    11043  14224  11457   1047    322   1739       O  
ATOM   1683  CB  THR A1114       2.662  38.150  -6.897  1.00101.78           C  
ANISOU 1683  CB  THR A1114    11332  15413  11928   1081    224   1819       C  
ATOM   1684  OG1 THR A1114       2.917  37.061  -7.783  1.00101.14           O  
ANISOU 1684  OG1 THR A1114    11147  15531  11749   1068    129   1720       O  
ATOM   1685  CG2 THR A1114       3.652  39.279  -7.110  1.00 92.53           C  
ANISOU 1685  CG2 THR A1114    10157  14223  10777   1071    259   1899       C  
ATOM   1686  N   ASN A1115       1.207  38.858  -4.187  1.00119.99           N  
ANISOU 1686  N   ASN A1115    13917  17246  14429   1105    368   1853       N  
ATOM   1687  CA  ASN A1115       0.813  39.965  -3.343  1.00130.11           C  
ANISOU 1687  CA  ASN A1115    15285  18342  15810   1122    469   1947       C  
ATOM   1688  C   ASN A1115       1.217  39.667  -1.898  1.00132.29           C  
ANISOU 1688  C   ASN A1115    15722  18414  16129   1094    465   1822       C  
ATOM   1689  O   ASN A1115       1.750  40.534  -1.203  1.00129.59           O  
ANISOU 1689  O   ASN A1115    15465  17924  15849   1082    520   1839       O  
ATOM   1690  CB  ASN A1115      -0.665  40.286  -3.560  1.00138.27           C  
ANISOU 1690  CB  ASN A1115    16264  19397  16875   1167    532   2076       C  
ATOM   1691  CG  ASN A1115      -1.039  41.659  -3.055  1.00159.49           C  
ANISOU 1691  CG  ASN A1115    18999  21934  19667   1191    645   2208       C  
ATOM   1692  OD1 ASN A1115      -2.207  41.916  -2.769  1.00165.15           O  
ANISOU 1692  OD1 ASN A1115    19721  22599  20430   1225    705   2287       O  
ATOM   1693  ND2 ASN A1115      -0.056  42.534  -2.912  1.00176.75           N  
ANISOU 1693  ND2 ASN A1115    21220  24044  21893   1173    675   2229       N  
ATOM   1694  N   SER A1116       0.977  38.421  -1.469  1.00132.00           N  
ANISOU 1694  N   SER A1116    15720  18378  16058   1082    398   1697       N  
ATOM   1695  CA  SER A1116       1.194  37.989  -0.094  1.00118.78           C  
ANISOU 1695  CA  SER A1116    14184  16527  14419   1057    389   1583       C  
ATOM   1696  C   SER A1116       2.673  37.694   0.169  1.00107.66           C  
ANISOU 1696  C   SER A1116    12829  15094  12982   1011    333   1464       C  
ATOM   1697  O   SER A1116       3.179  38.010   1.245  1.00 95.17           O  
ANISOU 1697  O   SER A1116    11363  13352  11446    987    361   1418       O  
ATOM   1698  CB  SER A1116       0.311  36.801   0.257  1.00127.19           C  
ANISOU 1698  CB  SER A1116    15257  17602  15467   1063    342   1511       C  
ATOM   1699  OG  SER A1116      -1.076  37.098   0.118  1.00126.63           O  
ANISOU 1699  OG  SER A1116    15148  17543  15424   1105    398   1622       O  
ATOM   1700  N   LEU A1117       3.364  37.082  -0.808  1.00 96.49           N  
ANISOU 1700  N   LEU A1117    11328  13843  11490    997    254   1412       N  
ATOM   1701  CA  LEU A1117       4.737  36.633  -0.618  1.00 87.71           C  
ANISOU 1701  CA  LEU A1117    10259  12725  10343    955    190   1291       C  
ATOM   1702  C   LEU A1117       5.661  37.819  -0.366  1.00 89.57           C  
ANISOU 1702  C   LEU A1117    10547  12874  10613    938    245   1340       C  
ATOM   1703  O   LEU A1117       6.619  37.693   0.382  1.00 90.71           O  
ANISOU 1703  O   LEU A1117    10782  12923  10760    902    226   1248       O  
ATOM   1704  CB  LEU A1117       5.219  35.869  -1.853  1.00 90.94           C  
ANISOU 1704  CB  LEU A1117    10547  13343  10663    949    102   1241       C  
ATOM   1705  CG  LEU A1117       4.585  34.502  -2.106  1.00 95.24           C  
ANISOU 1705  CG  LEU A1117    11039  13977  11168    955     29   1153       C  
ATOM   1706  CD1 LEU A1117       5.052  33.954  -3.439  1.00 83.52           C  
ANISOU 1706  CD1 LEU A1117     9422  12713   9599    952    -45   1116       C  
ATOM   1707  CD2 LEU A1117       4.930  33.529  -0.987  1.00 99.30           C  
ANISOU 1707  CD2 LEU A1117    11661  14367  11702    925    -21   1008       C  
ATOM   1708  N   ARG A1118       5.379  38.964  -0.997  1.00 94.06           N  
ANISOU 1708  N   ARG A1118    11054  13475  11208    964    313   1487       N  
ATOM   1709  CA  ARG A1118       6.227  40.138  -0.861  1.00108.88           C  
ANISOU 1709  CA  ARG A1118    12968  15277  13124    949    367   1544       C  
ATOM   1710  C   ARG A1118       6.190  40.665   0.577  1.00118.57           C  
ANISOU 1710  C   ARG A1118    14340  16276  14435    936    434   1521       C  
ATOM   1711  O   ARG A1118       7.224  40.951   1.187  1.00109.36           O  
ANISOU 1711  O   ARG A1118    13255  15017  13280    899    436   1462       O  
ATOM   1712  CB  ARG A1118       5.811  41.209  -1.876  1.00123.82           C  
ANISOU 1712  CB  ARG A1118    14751  17258  15037    983    426   1718       C  
ATOM   1713  CG  ARG A1118       6.606  42.505  -1.788  1.00145.12           C  
ANISOU 1713  CG  ARG A1118    17476  19873  17789    970    487   1795       C  
ATOM   1714  CD  ARG A1118       8.081  42.242  -2.043  1.00169.02           C  
ANISOU 1714  CD  ARG A1118    20508  22960  20752    929    417   1708       C  
ATOM   1715  NE  ARG A1118       8.955  43.403  -1.882  1.00171.81           N  
ANISOU 1715  NE  ARG A1118    20897  23228  21154    910    468   1765       N  
ATOM   1716  CZ  ARG A1118      10.259  43.417  -2.154  1.00162.98           C  
ANISOU 1716  CZ  ARG A1118    19778  22160  19988    876    420   1718       C  
ATOM   1717  NH1 ARG A1118      10.856  42.329  -2.613  1.00159.24           N  
ANISOU 1717  NH1 ARG A1118    19267  21822  19415    858    321   1610       N  
ATOM   1718  NH2 ARG A1118      10.961  44.521  -1.963  1.00156.01           N  
ANISOU 1718  NH2 ARG A1118    18930  21189  19159    859    472   1777       N  
ATOM   1719  N   MET A1119       4.975  40.808   1.111  1.00134.11           N  
ANISOU 1719  N   MET A1119    16335  18161  16459    965    491   1569       N  
ATOM   1720  CA  MET A1119       4.794  41.390   2.430  1.00128.69           C  
ANISOU 1720  CA  MET A1119    15772  17269  15855    957    563   1557       C  
ATOM   1721  C   MET A1119       5.161  40.392   3.533  1.00125.54           C  
ANISOU 1721  C   MET A1119    15475  16788  15436    921    511   1401       C  
ATOM   1722  O   MET A1119       5.325  40.802   4.679  1.00121.06           O  
ANISOU 1722  O   MET A1119    15015  16062  14922    902    559   1365       O  
ATOM   1723  CB  MET A1119       3.368  41.924   2.611  1.00126.57           C  
ANISOU 1723  CB  MET A1119    15493  16945  15654   1003    644   1666       C  
ATOM   1724  CG  MET A1119       2.288  40.997   2.055  1.00147.23           C  
ANISOU 1724  CG  MET A1119    18032  19685  18225   1033    601   1678       C  
ATOM   1725  SD  MET A1119       0.622  41.729   2.083  1.00160.26           S  
ANISOU 1725  SD  MET A1119    19652  21291  19947   1091    699   1829       S  
ATOM   1726  CE  MET A1119       0.821  43.103   0.948  1.00176.84           C  
ANISOU 1726  CE  MET A1119    21650  23462  22081   1114    764   2001       C  
ATOM   1727  N   LEU A1120       5.299  39.095   3.192  1.00111.81           N  
ANISOU 1727  N   LEU A1120    13699  15158  13623    911    414   1308       N  
ATOM   1728  CA  LEU A1120       5.827  38.110   4.133  1.00100.90           C  
ANISOU 1728  CA  LEU A1120    12402  13713  12222    873    355   1163       C  
ATOM   1729  C   LEU A1120       7.341  38.271   4.276  1.00114.09           C  
ANISOU 1729  C   LEU A1120    14116  15365  13867    828    329   1094       C  
ATOM   1730  O   LEU A1120       7.879  38.131   5.380  1.00109.43           O  
ANISOU 1730  O   LEU A1120    13629  14657  13294    793    330   1010       O  
ATOM   1731  CB  LEU A1120       5.472  36.686   3.693  1.00 85.28           C  
ANISOU 1731  CB  LEU A1120    10364  11852  10185    878    262   1089       C  
ATOM   1732  CG  LEU A1120       4.056  36.210   4.032  1.00 86.63           C  
ANISOU 1732  CG  LEU A1120    10531  12001  10382    908    274   1112       C  
ATOM   1733  CD1 LEU A1120       3.816  34.798   3.522  1.00 71.80           C  
ANISOU 1733  CD1 LEU A1120     8588  10245   8450    909    177   1033       C  
ATOM   1734  CD2 LEU A1120       3.788  36.273   5.527  1.00 90.02           C  
ANISOU 1734  CD2 LEU A1120    11081  12255  10869    894    315   1073       C  
ATOM   1735  N   GLN A1121       8.014  38.546   3.145  1.00121.13           N  
ANISOU 1735  N   GLN A1121    14925  16383  14714    829    303   1132       N  
ATOM   1736  CA  GLN A1121       9.461  38.721   3.113  1.00125.22           C  
ANISOU 1736  CA  GLN A1121    15470  16906  15200    789    275   1077       C  
ATOM   1737  C   GLN A1121       9.847  39.985   3.884  1.00117.77           C  
ANISOU 1737  C   GLN A1121    14614  15809  14325    772    363   1122       C  
ATOM   1738  O   GLN A1121      10.938  40.067   4.454  1.00104.25           O  
ANISOU 1738  O   GLN A1121    12973  14033  12603    730    353   1050       O  
ATOM   1739  CB  GLN A1121       9.982  38.705   1.671  1.00125.01           C  
ANISOU 1739  CB  GLN A1121    15324  17068  15108    797    225   1115       C  
ATOM   1740  CG  GLN A1121      11.502  38.671   1.573  1.00122.67           C  
ANISOU 1740  CG  GLN A1121    15048  16798  14763    756    178   1045       C  
ATOM   1741  CD  GLN A1121      12.073  38.677   0.178  1.00128.80           C  
ANISOU 1741  CD  GLN A1121    15704  17766  15470    762    128   1079       C  
ATOM   1742  OE1 GLN A1121      11.362  38.601  -0.824  1.00130.17           O  
ANISOU 1742  OE1 GLN A1121    15763  18074  15620    796    119   1149       O  
ATOM   1743  NE2 GLN A1121      13.389  38.773   0.113  1.00133.73           N  
ANISOU 1743  NE2 GLN A1121    16349  18408  16056    727     94   1031       N  
ATOM   1744  N   GLN A1122       8.932  40.964   3.899  1.00105.73           N  
ANISOU 1744  N   GLN A1122    13079  14223  12871    806    452   1240       N  
ATOM   1745  CA  GLN A1122       9.174  42.250   4.536  1.00110.54           C  
ANISOU 1745  CA  GLN A1122    13757  14686  13558    795    545   1291       C  
ATOM   1746  C   GLN A1122       8.791  42.240   6.019  1.00102.76           C  
ANISOU 1746  C   GLN A1122    12890  13528  12627    780    591   1227       C  
ATOM   1747  O   GLN A1122       8.709  43.306   6.630  1.00 87.17           O  
ANISOU 1747  O   GLN A1122    10970  11422  10730    778    679   1270       O  
ATOM   1748  CB  GLN A1122       8.394  43.338   3.799  1.00121.42           C  
ANISOU 1748  CB  GLN A1122    15058  16082  14995    840    620   1453       C  
ATOM   1749  CG  GLN A1122       8.895  43.572   2.388  1.00137.19           C  
ANISOU 1749  CG  GLN A1122    16937  18245  16944    849    586   1531       C  
ATOM   1750  CD  GLN A1122       8.079  44.624   1.686  1.00152.20           C  
ANISOU 1750  CD  GLN A1122    18755  20167  18908    893    662   1700       C  
ATOM   1751  OE1 GLN A1122       6.928  44.879   2.044  1.00156.90           O  
ANISOU 1751  OE1 GLN A1122    19360  20691  19563    926    723   1757       O  
ATOM   1752  NE2 GLN A1122       8.684  45.243   0.686  1.00168.59           N  
ANISOU 1752  NE2 GLN A1122    20745  22341  20969    894    659   1787       N  
ATOM   1753  N   LYS A1123       8.538  41.044   6.579  1.00 91.19           N  
ANISOU 1753  N   LYS A1123    11457  12067  11125    770    532   1126       N  
ATOM   1754  CA  LYS A1123       8.200  40.848   7.983  1.00 87.53           C  
ANISOU 1754  CA  LYS A1123    11096  11465  10699    753    561   1057       C  
ATOM   1755  C   LYS A1123       6.847  41.472   8.346  1.00 94.55           C  
ANISOU 1755  C   LYS A1123    11991  12273  11663    794    646   1142       C  
ATOM   1756  O   LYS A1123       6.528  41.618   9.528  1.00103.14           O  
ANISOU 1756  O   LYS A1123    13161  13234  12794    782    691   1103       O  
ATOM   1757  CB  LYS A1123       9.304  41.372   8.912  1.00 85.02           C  
ANISOU 1757  CB  LYS A1123    10874  11033  10398    701    590    991       C  
ATOM   1758  CG  LYS A1123      10.726  40.880   8.657  1.00 74.02           C  
ANISOU 1758  CG  LYS A1123     9485   9705   8934    658    515    909       C  
ATOM   1759  CD  LYS A1123      10.848  39.398   8.796  1.00 69.33           C  
ANISOU 1759  CD  LYS A1123     8888   9178   8276    644    418    807       C  
ATOM   1760  CE  LYS A1123      12.251  38.903   9.047  1.00 66.62           C  
ANISOU 1760  CE  LYS A1123     8584   8850   7878    592    358    704       C  
ATOM   1761  NZ  LYS A1123      12.250  37.423   8.912  1.00 83.94           N  
ANISOU 1761  NZ  LYS A1123    10748  11128  10018    589    259    621       N  
ATOM   1762  N   ARG A1124       6.049  41.845   7.342  1.00 91.79           N  
ANISOU 1762  N   ARG A1124    11548  12000  11326    842    669   1260       N  
ATOM   1763  CA  ARG A1124       4.763  42.465   7.620  1.00101.51           C  
ANISOU 1763  CA  ARG A1124    12779  13160  12629    884    752   1349       C  
ATOM   1764  C   ARG A1124       3.688  41.378   7.664  1.00109.52           C  
ANISOU 1764  C   ARG A1124    13769  14231  13613    908    706   1330       C  
ATOM   1765  O   ARG A1124       3.056  41.100   6.641  1.00101.70           O  
ANISOU 1765  O   ARG A1124    12682  13365  12594    943    682   1399       O  
ATOM   1766  CB  ARG A1124       4.468  43.579   6.607  1.00105.34           C  
ANISOU 1766  CB  ARG A1124    13182  13684  13157    921    813   1498       C  
ATOM   1767  CG  ARG A1124       5.397  44.782   6.716  1.00110.59           C  
ANISOU 1767  CG  ARG A1124    13879  14264  13876    898    872   1527       C  
ATOM   1768  CD  ARG A1124       4.974  45.964   5.864  1.00117.98           C  
ANISOU 1768  CD  ARG A1124    14735  15214  14877    937    945   1687       C  
ATOM   1769  NE  ARG A1124       4.866  45.590   4.462  1.00142.68           N  
ANISOU 1769  NE  ARG A1124    17739  18531  17942    961    890   1760       N  
ATOM   1770  CZ  ARG A1124       4.461  46.396   3.486  1.00157.16           C  
ANISOU 1770  CZ  ARG A1124    19474  20429  19811    997    934   1910       C  
ATOM   1771  NH1 ARG A1124       4.134  47.649   3.753  1.00153.58           N  
ANISOU 1771  NH1 ARG A1124    19034  19852  19465   1016   1036   2005       N  
ATOM   1772  NH2 ARG A1124       4.388  45.946   2.244  1.00169.07           N  
ANISOU 1772  NH2 ARG A1124    20864  22125  21248   1014    876   1963       N  
ATOM   1773  N   TRP A1125       3.491  40.787   8.859  1.00107.82           N  
ANISOU 1773  N   TRP A1125    13636  13927  13403    888    696   1239       N  
ATOM   1774  CA  TRP A1125       2.688  39.583   9.042  1.00102.10           C  
ANISOU 1774  CA  TRP A1125    12899  13251  12645    900    637   1197       C  
ATOM   1775  C   TRP A1125       1.196  39.891   8.965  1.00105.61           C  
ANISOU 1775  C   TRP A1125    13310  13685  13130    952    693   1297       C  
ATOM   1776  O   TRP A1125       0.426  39.176   8.328  1.00112.79           O  
ANISOU 1776  O   TRP A1125    14150  14698  14006    979    650   1325       O  
ATOM   1777  CB  TRP A1125       3.024  38.899  10.370  1.00 91.03           C  
ANISOU 1777  CB  TRP A1125    11590  11759  11238    858    608   1076       C  
ATOM   1778  CG  TRP A1125       4.489  38.793  10.652  1.00 78.37           C  
ANISOU 1778  CG  TRP A1125    10034  10139   9605    805    572    984       C  
ATOM   1779  CD1 TRP A1125       5.154  39.299  11.729  1.00 73.17           C  
ANISOU 1779  CD1 TRP A1125     9466   9361   8973    766    614    928       C  
ATOM   1780  CD2 TRP A1125       5.475  38.131   9.844  1.00 75.76           C  
ANISOU 1780  CD2 TRP A1125     9658   9919   9208    784    487    934       C  
ATOM   1781  NE1 TRP A1125       6.486  38.998  11.650  1.00 70.27           N  
ANISOU 1781  NE1 TRP A1125     9116   9023   8560    722    561    853       N  
ATOM   1782  CE2 TRP A1125       6.716  38.286  10.502  1.00 75.63           C  
ANISOU 1782  CE2 TRP A1125     9713   9841   9183    733    483    855       C  
ATOM   1783  CE3 TRP A1125       5.434  37.429   8.632  1.00 79.68           C  
ANISOU 1783  CE3 TRP A1125    10057  10566   9650    803    415    945       C  
ATOM   1784  CZ2 TRP A1125       7.903  37.756   9.989  1.00 78.94           C  
ANISOU 1784  CZ2 TRP A1125    10112  10339   9541    702    408    791       C  
ATOM   1785  CZ3 TRP A1125       6.607  36.915   8.118  1.00 86.18           C  
ANISOU 1785  CZ3 TRP A1125    10859  11471  10416    773    342    876       C  
ATOM   1786  CH2 TRP A1125       7.823  37.076   8.791  1.00 90.93           C  
ANISOU 1786  CH2 TRP A1125    11535  12004  11011    724    338    802       C  
ATOM   1787  N   ASP A1126       0.796  40.947   9.674  1.00114.32           N  
ANISOU 1787  N   ASP A1126    14466  14660  14309    964    791   1345       N  
ATOM   1788  CA  ASP A1126      -0.613  41.258   9.839  1.00129.06           C  
ANISOU 1788  CA  ASP A1126    16320  16496  16222   1011    851   1430       C  
ATOM   1789  C   ASP A1126      -1.233  41.700   8.514  1.00123.95           C  
ANISOU 1789  C   ASP A1126    15564  15955  15578   1058    873   1565       C  
ATOM   1790  O   ASP A1126      -2.390  41.406   8.235  1.00118.01           O  
ANISOU 1790  O   ASP A1126    14764  15252  14821   1097    877   1627       O  
ATOM   1791  CB  ASP A1126      -0.809  42.245  10.989  1.00135.78           C  
ANISOU 1791  CB  ASP A1126    17256  17181  17154   1008    949   1432       C  
ATOM   1792  CG  ASP A1126      -0.313  41.674  12.304  1.00135.69           C  
ANISOU 1792  CG  ASP A1126    17340  17089  17129    961    921   1299       C  
ATOM   1793  OD1 ASP A1126       0.910  41.762  12.568  1.00137.20           O  
ANISOU 1793  OD1 ASP A1126    17573  17252  17306    914    904   1224       O  
ATOM   1794  OD2 ASP A1126      -1.146  41.145  13.052  1.00127.82           O1-
ANISOU 1794  OD2 ASP A1126    16369  16063  16133    970    917   1275       O1-
ATOM   1795  N   GLU A1127      -0.456  42.395   7.685  1.00120.24           N  
ANISOU 1795  N   GLU A1127    15049  15526  15110   1054    886   1615       N  
ATOM   1796  CA  GLU A1127      -0.951  42.862   6.403  1.00111.75           C  
ANISOU 1796  CA  GLU A1127    13862  14562  14036   1095    907   1751       C  
ATOM   1797  C   GLU A1127      -1.157  41.661   5.480  1.00116.77           C  
ANISOU 1797  C   GLU A1127    14410  15375  14580   1100    811   1731       C  
ATOM   1798  O   GLU A1127      -2.095  41.653   4.685  1.00117.32           O  
ANISOU 1798  O   GLU A1127    14393  15543  14641   1140    821   1829       O  
ATOM   1799  CB  GLU A1127       0.029  43.900   5.857  1.00132.26           C  
ANISOU 1799  CB  GLU A1127    16436  17154  16663   1083    943   1804       C  
ATOM   1800  CG  GLU A1127      -0.372  44.541   4.539  1.00145.26           C  
ANISOU 1800  CG  GLU A1127    17960  18913  18318   1123    972   1958       C  
ATOM   1801  CD  GLU A1127       0.617  45.571   4.009  1.00141.08           C  
ANISOU 1801  CD  GLU A1127    17404  18379  17822   1109   1004   2017       C  
ATOM   1802  OE1 GLU A1127       1.539  45.970   4.771  1.00145.53           O  
ANISOU 1802  OE1 GLU A1127    18056  18823  18418   1072   1021   1944       O  
ATOM   1803  OE2 GLU A1127       0.463  45.978   2.839  1.00129.60           O1-
ANISOU 1803  OE2 GLU A1127    15837  17044  16361   1135   1012   2139       O1-
ATOM   1804  N   ALA A1128      -0.277  40.658   5.585  1.00114.10           N  
ANISOU 1804  N   ALA A1128    14095  15081  14178   1060    719   1603       N  
ATOM   1805  CA  ALA A1128      -0.348  39.460   4.762  1.00118.90           C  
ANISOU 1805  CA  ALA A1128    14624  15850  14703   1059    623   1561       C  
ATOM   1806  C   ALA A1128      -1.482  38.542   5.217  1.00109.69           C  
ANISOU 1806  C   ALA A1128    13466  14682  13528   1076    597   1534       C  
ATOM   1807  O   ALA A1128      -2.050  37.798   4.419  1.00114.35           O  
ANISOU 1807  O   ALA A1128    13971  15406  14070   1093    547   1547       O  
ATOM   1808  CB  ALA A1128       0.982  38.743   4.767  1.00131.63           C  
ANISOU 1808  CB  ALA A1128    16258  17496  16260   1011    538   1435       C  
ATOM   1809  N   ALA A1129      -1.806  38.598   6.509  1.00110.43           N  
ANISOU 1809  N   ALA A1129    13660  14629  13669   1069    633   1495       N  
ATOM   1810  CA  ALA A1129      -2.857  37.759   7.057  1.00104.83           C  
ANISOU 1810  CA  ALA A1129    12965  13909  12956   1082    609   1472       C  
ATOM   1811  C   ALA A1129      -4.214  38.107   6.432  1.00111.23           C  
ANISOU 1811  C   ALA A1129    13702  14778  13780   1136    658   1602       C  
ATOM   1812  O   ALA A1129      -4.966  37.204   6.060  1.00 95.07           O  
ANISOU 1812  O   ALA A1129    11602  12824  11695   1150    607   1599       O  
ATOM   1813  CB  ALA A1129      -2.856  37.868   8.558  1.00 96.21           C  
ANISOU 1813  CB  ALA A1129    11989  12655  11910   1062    642   1411       C  
ATOM   1814  N   VAL A1130      -4.515  39.409   6.301  1.00122.58           N  
ANISOU 1814  N   VAL A1130    15133  16164  15276   1165    756   1718       N  
ATOM   1815  CA  VAL A1130      -5.779  39.866   5.734  1.00127.11           C  
ANISOU 1815  CA  VAL A1130    15638  16788  15871   1217    812   1854       C  
ATOM   1816  C   VAL A1130      -5.774  39.658   4.223  1.00142.52           C  
ANISOU 1816  C   VAL A1130    17459  18928  17763   1231    773   1918       C  
ATOM   1817  O   VAL A1130      -6.833  39.474   3.618  1.00153.56           O  
ANISOU 1817  O   VAL A1130    18782  20421  19143   1266    779   1999       O  
ATOM   1818  CB  VAL A1130      -6.117  41.330   6.096  1.00119.22           C  
ANISOU 1818  CB  VAL A1130    14669  15665  14963   1245    932   1960       C  
ATOM   1819  CG1 VAL A1130      -5.122  42.332   5.528  1.00109.10           C  
ANISOU 1819  CG1 VAL A1130    13364  14381  13710   1235    968   2006       C  
ATOM   1820  CG2 VAL A1130      -7.533  41.702   5.676  1.00120.64           C  
ANISOU 1820  CG2 VAL A1130    14785  15885  15167   1300    991   2098       C  
ATOM   1821  N   ASN A1131      -4.575  39.702   3.626  1.00133.82           N  
ANISOU 1821  N   ASN A1131    16330  17887  16629   1202    734   1880       N  
ATOM   1822  CA  ASN A1131      -4.433  39.557   2.190  1.00113.11           C  
ANISOU 1822  CA  ASN A1131    13578  15453  13946   1211    696   1934       C  
ATOM   1823  C   ASN A1131      -4.687  38.111   1.773  1.00111.26           C  
ANISOU 1823  C   ASN A1131    13293  15350  13633   1201    596   1848       C  
ATOM   1824  O   ASN A1131      -5.299  37.871   0.731  1.00133.81           O  
ANISOU 1824  O   ASN A1131    16036  18363  16444   1224    579   1913       O  
ATOM   1825  CB  ASN A1131      -3.085  40.086   1.730  1.00112.92           C  
ANISOU 1825  CB  ASN A1131    13541  15451  13913   1184    687   1922       C  
ATOM   1826  CG  ASN A1131      -2.993  40.193   0.231  1.00125.50           C  
ANISOU 1826  CG  ASN A1131    14992  17240  15452   1198    665   2005       C  
ATOM   1827  OD1 ASN A1131      -2.457  39.302  -0.421  1.00127.55           O  
ANISOU 1827  OD1 ASN A1131    15195  17635  15634   1177    577   1926       O  
ATOM   1828  ND2 ASN A1131      -3.539  41.268  -0.307  1.00129.15           N  
ANISOU 1828  ND2 ASN A1131    15391  17723  15959   1233    746   2164       N  
ATOM   1829  N   LEU A1132      -4.222  37.156   2.593  1.00110.74           N  
ANISOU 1829  N   LEU A1132    13305  15220  13552   1167    530   1703       N  
ATOM   1830  CA  LEU A1132      -4.398  35.733   2.321  1.00114.63           C  
ANISOU 1830  CA  LEU A1132    13757  15815  13984   1154    432   1608       C  
ATOM   1831  C   LEU A1132      -5.859  35.298   2.458  1.00115.50           C  
ANISOU 1831  C   LEU A1132    13846  15940  14098   1185    442   1654       C  
ATOM   1832  O   LEU A1132      -6.236  34.274   1.893  1.00111.89           O  
ANISOU 1832  O   LEU A1132    13320  15603  13590   1185    373   1612       O  
ATOM   1833  CB  LEU A1132      -3.498  34.896   3.236  1.00114.16           C  
ANISOU 1833  CB  LEU A1132    13788  15668  13920   1109    365   1452       C  
ATOM   1834  CG  LEU A1132      -2.025  34.810   2.841  1.00119.27           C  
ANISOU 1834  CG  LEU A1132    14428  16358  14532   1073    315   1374       C  
ATOM   1835  CD1 LEU A1132      -1.209  34.198   3.967  1.00119.22           C  
ANISOU 1835  CD1 LEU A1132    14527  16233  14538   1031    271   1241       C  
ATOM   1836  CD2 LEU A1132      -1.840  34.012   1.557  1.00127.00           C  
ANISOU 1836  CD2 LEU A1132    15285  17532  15437   1071    236   1342       C  
ATOM   1837  N   ALA A1133      -6.672  36.051   3.215  1.00119.82           N  
ANISOU 1837  N   ALA A1133    14452  16367  14707   1212    527   1735       N  
ATOM   1838  CA  ALA A1133      -8.086  35.721   3.378  1.00120.61           C  
ANISOU 1838  CA  ALA A1133    14535  16478  14812   1244    542   1788       C  
ATOM   1839  C   ALA A1133      -8.874  36.081   2.117  1.00123.72           C  
ANISOU 1839  C   ALA A1133    14804  17027  15178   1281    572   1919       C  
ATOM   1840  O   ALA A1133      -9.929  35.506   1.853  1.00139.65           O  
ANISOU 1840  O   ALA A1133    16771  19120  17170   1302    555   1949       O  
ATOM   1841  CB  ALA A1133      -8.664  36.381   4.611  1.00114.90           C  
ANISOU 1841  CB  ALA A1133    13914  15583  14161   1259    621   1825       C  
ATOM   1842  N   LYS A1134      -8.350  37.022   1.324  1.00118.26           N  
ANISOU 1842  N   LYS A1134    14055  16389  14489   1289    613   2001       N  
ATOM   1843  CA  LYS A1134      -9.043  37.438   0.117  1.00115.94           C  
ANISOU 1843  CA  LYS A1134    13633  16249  14168   1323    646   2137       C  
ATOM   1844  C   LYS A1134      -8.689  36.494  -1.035  1.00121.85           C  
ANISOU 1844  C   LYS A1134    14271  17201  14827   1305    554   2078       C  
ATOM   1845  O   LYS A1134      -8.615  36.934  -2.179  1.00137.80           O  
ANISOU 1845  O   LYS A1134    16177  19367  16812   1316    567   2166       O  
ATOM   1846  CB  LYS A1134      -8.667  38.881  -0.250  1.00111.36           C  
ANISOU 1846  CB  LYS A1134    13031  15643  13638   1340    732   2262       C  
ATOM   1847  CG  LYS A1134      -8.854  39.943   0.827  1.00100.46           C  
ANISOU 1847  CG  LYS A1134    11756  14058  12357   1356    828   2313       C  
ATOM   1848  CD  LYS A1134      -8.247  41.283   0.449  1.00 94.11           C  
ANISOU 1848  CD  LYS A1134    10928  13222  11606   1364    900   2414       C  
ATOM   1849  CE  LYS A1134      -8.158  42.263   1.602  1.00 93.40           C  
ANISOU 1849  CE  LYS A1134    10953  12916  11619   1368    986   2426       C  
ATOM   1850  NZ  LYS A1134      -9.491  42.548   2.184  1.00110.43           N  
ANISOU 1850  NZ  LYS A1134    13137  14994  13826   1409   1054   2500       N  
ATOM   1851  N   SER A1135      -8.502  35.196  -0.743  1.00116.36           N  
ANISOU 1851  N   SER A1135    13599  16519  14093   1276    462   1933       N  
ATOM   1852  CA  SER A1135      -7.978  34.266  -1.733  1.00119.79           C  
ANISOU 1852  CA  SER A1135    13938  17128  14449   1253    370   1849       C  
ATOM   1853  C   SER A1135      -9.009  33.212  -2.131  1.00110.69           C  
ANISOU 1853  C   SER A1135    12716  16090  13253   1261    321   1826       C  
ATOM   1854  O   SER A1135     -10.031  33.057  -1.479  1.00 94.73           O  
ANISOU 1854  O   SER A1135    10738  13994  11260   1280    346   1856       O  
ATOM   1855  CB  SER A1135      -6.697  33.621  -1.262  1.00135.06           C  
ANISOU 1855  CB  SER A1135    15939  19002  16377   1209    297   1690       C  
ATOM   1856  OG  SER A1135      -5.704  34.600  -0.990  1.00160.61           O  
ANISOU 1856  OG  SER A1135    19230  22148  19646   1198    340   1711       O  
ATOM   1857  N   ARG A1136      -8.710  32.497  -3.221  1.00114.63           N  
ANISOU 1857  N   ARG A1136    13101  16775  13679   1246    251   1771       N  
ATOM   1858  CA  ARG A1136      -9.463  31.322  -3.636  1.00135.27           C  
ANISOU 1858  CA  ARG A1136    15645  19505  16247   1243    187   1712       C  
ATOM   1859  C   ARG A1136      -9.204  30.187  -2.649  1.00131.94           C  
ANISOU 1859  C   ARG A1136    15316  18964  15851   1215    113   1556       C  
ATOM   1860  O   ARG A1136     -10.079  29.356  -2.405  1.00120.25           O  
ANISOU 1860  O   ARG A1136    13832  17485  14371   1217     82   1525       O  
ATOM   1861  CB  ARG A1136      -9.101  30.891  -5.068  1.00134.13           C  
ANISOU 1861  CB  ARG A1136    15350  19594  16019   1232    131   1681       C  
ATOM   1862  CG  ARG A1136      -7.726  30.249  -5.241  1.00137.16           C  
ANISOU 1862  CG  ARG A1136    15734  20003  16376   1193     48   1528       C  
ATOM   1863  CD  ARG A1136      -6.621  31.271  -5.461  1.00145.24           C  
ANISOU 1863  CD  ARG A1136    16767  21016  17403   1187     82   1573       C  
ATOM   1864  NE  ARG A1136      -5.294  30.756  -5.800  1.00133.62           N  
ANISOU 1864  NE  ARG A1136    15278  19598  15894   1153      6   1442       N  
ATOM   1865  CZ  ARG A1136      -4.204  31.496  -6.016  1.00128.70           C  
ANISOU 1865  CZ  ARG A1136    14660  18975  15265   1142     20   1461       C  
ATOM   1866  NH1 ARG A1136      -4.255  32.820  -5.970  1.00132.00           N  
ANISOU 1866  NH1 ARG A1136    15095  19343  15717   1163    109   1607       N  
ATOM   1867  NH2 ARG A1136      -3.054  30.904  -6.280  1.00112.39           N  
ANISOU 1867  NH2 ARG A1136    12580  16959  13163   1111    -55   1333       N  
ATOM   1868  N   TRP A1137      -7.984  30.176  -2.097  1.00127.81           N  
ANISOU 1868  N   TRP A1137    14871  18339  15349   1186     87   1464       N  
ATOM   1869  CA  TRP A1137      -7.527  29.184  -1.139  1.00109.73           C  
ANISOU 1869  CA  TRP A1137    12670  15933  13089   1155     19   1320       C  
ATOM   1870  C   TRP A1137      -8.356  29.266   0.135  1.00112.73           C  
ANISOU 1870  C   TRP A1137    13157  16145  13530   1167     60   1354       C  
ATOM   1871  O   TRP A1137      -8.706  28.230   0.695  1.00 93.27           O  
ANISOU 1871  O   TRP A1137    10721  13639  11081   1154      3   1272       O  
ATOM   1872  CB  TRP A1137      -6.037  29.390  -0.846  1.00 95.95           C  
ANISOU 1872  CB  TRP A1137    10984  14121  11351   1124     -1   1241       C  
ATOM   1873  CG  TRP A1137      -5.507  28.581   0.300  1.00 87.95           C  
ANISOU 1873  CG  TRP A1137    10075  12964  10377   1093    -55   1114       C  
ATOM   1874  CD1 TRP A1137      -5.595  27.229   0.484  1.00 82.21           C  
ANISOU 1874  CD1 TRP A1137     9338  12246   9651   1073   -141    996       C  
ATOM   1875  CD2 TRP A1137      -4.797  29.098   1.438  1.00 73.95           C  
ANISOU 1875  CD2 TRP A1137     8428  11018   8653   1076    -23   1096       C  
ATOM   1876  NE1 TRP A1137      -4.999  26.872   1.664  1.00 76.50           N  
ANISOU 1876  NE1 TRP A1137     8724  11369   8974   1046   -164    915       N  
ATOM   1877  CE2 TRP A1137      -4.474  27.995   2.253  1.00 73.81           C  
ANISOU 1877  CE2 TRP A1137     8466  10921   8657   1046    -94    970       C  
ATOM   1878  CE3 TRP A1137      -4.361  30.371   1.819  1.00 73.27           C  
ANISOU 1878  CE3 TRP A1137     8405  10841   8594   1081     58   1171       C  
ATOM   1879  CZ2 TRP A1137      -3.749  28.133   3.434  1.00 78.97           C  
ANISOU 1879  CZ2 TRP A1137     9235  11417   9352   1020    -86    922       C  
ATOM   1880  CZ3 TRP A1137      -3.644  30.512   2.986  1.00 79.94           C  
ANISOU 1880  CZ3 TRP A1137     9367  11527   9480   1055     66   1115       C  
ATOM   1881  CH2 TRP A1137      -3.341  29.403   3.779  1.00 82.77           C  
ANISOU 1881  CH2 TRP A1137     9777  11819   9852   1025     -5    993       C  
ATOM   1882  N   TYR A1138      -8.637  30.497   0.588  1.00118.99           N  
ANISOU 1882  N   TYR A1138    14005  16843  14361   1192    156   1471       N  
ATOM   1883  CA  TYR A1138      -9.316  30.714   1.854  1.00122.60           C  
ANISOU 1883  CA  TYR A1138    14568  17136  14877   1203    202   1502       C  
ATOM   1884  C   TYR A1138     -10.782  30.314   1.745  1.00124.80           C  
ANISOU 1884  C   TYR A1138    14803  17466  15148   1231    209   1564       C  
ATOM   1885  O   TYR A1138     -11.336  29.782   2.705  1.00133.58           O  
ANISOU 1885  O   TYR A1138    15982  18482  16292   1229    194   1532       O  
ATOM   1886  CB  TYR A1138      -9.166  32.160   2.323  1.00114.93           C  
ANISOU 1886  CB  TYR A1138    13662  16052  13954   1221    305   1601       C  
ATOM   1887  CG  TYR A1138      -9.856  32.460   3.629  1.00111.93           C  
ANISOU 1887  CG  TYR A1138    13386  15508  13634   1234    358   1630       C  
ATOM   1888  CD1 TYR A1138      -9.231  32.256   4.848  1.00112.65           C  
ANISOU 1888  CD1 TYR A1138    13588  15452  13761   1204    343   1538       C  
ATOM   1889  CD2 TYR A1138     -11.144  32.971   3.643  1.00108.47           C  
ANISOU 1889  CD2 TYR A1138    12930  15069  13212   1276    426   1752       C  
ATOM   1890  CE1 TYR A1138      -9.876  32.567   6.037  1.00113.42           C  
ANISOU 1890  CE1 TYR A1138    13774  15412  13909   1215    394   1564       C  
ATOM   1891  CE2 TYR A1138     -11.812  33.262   4.821  1.00101.83           C  
ANISOU 1891  CE2 TYR A1138    12179  14086  12423   1290    476   1779       C  
ATOM   1892  CZ  TYR A1138     -11.168  33.064   6.025  1.00109.29           C  
ANISOU 1892  CZ  TYR A1138    13233  14891  13403   1259    459   1682       C  
ATOM   1893  OH  TYR A1138     -11.815  33.356   7.187  1.00117.57           O  
ANISOU 1893  OH  TYR A1138    14362  15811  14497   1271    508   1705       O  
ATOM   1894  N   ASN A1139     -11.387  30.558   0.572  1.00124.04           N  
ANISOU 1894  N   ASN A1139    14592  17528  15008   1256    229   1654       N  
ATOM   1895  CA  ASN A1139     -12.812  30.330   0.379  1.00108.32           C  
ANISOU 1895  CA  ASN A1139    12553  15598  13005   1286    247   1732       C  
ATOM   1896  C   ASN A1139     -13.096  28.863   0.065  1.00100.12           C  
ANISOU 1896  C   ASN A1139    11459  14653  11929   1265    147   1625       C  
ATOM   1897  O   ASN A1139     -14.188  28.377   0.354  1.00103.28           O  
ANISOU 1897  O   ASN A1139    11858  15050  12334   1278    142   1649       O  
ATOM   1898  CB  ASN A1139     -13.426  31.285  -0.648  1.00113.08           C  
ANISOU 1898  CB  ASN A1139    13059  16325  13582   1322    320   1888       C  
ATOM   1899  CG  ASN A1139     -13.395  32.735  -0.211  1.00110.50           C  
ANISOU 1899  CG  ASN A1139    12790  15883  13310   1349    427   2007       C  
ATOM   1900  OD1 ASN A1139     -12.543  33.132   0.577  1.00108.88           O  
ANISOU 1900  OD1 ASN A1139    12681  15537  13150   1332    441   1960       O  
ATOM   1901  ND2 ASN A1139     -14.275  33.550  -0.763  1.00103.36           N  
ANISOU 1901  ND2 ASN A1139    11822  15043  12406   1388    503   2162       N  
ATOM   1902  N   GLN A1140     -12.123  28.166  -0.535  1.00 99.85           N  
ANISOU 1902  N   GLN A1140    11375  14702  11861   1232     70   1508       N  
ATOM   1903  CA  GLN A1140     -12.288  26.766  -0.911  1.00110.88           C  
ANISOU 1903  CA  GLN A1140    12709  16189  13230   1210    -27   1394       C  
ATOM   1904  C   GLN A1140     -12.202  25.914   0.357  1.00112.40           C  
ANISOU 1904  C   GLN A1140    13006  16223  13478   1188    -77   1294       C  
ATOM   1905  O   GLN A1140     -13.086  25.105   0.625  1.00120.21           O  
ANISOU 1905  O   GLN A1140    13987  17211  14477   1189   -111   1277       O  
ATOM   1906  CB  GLN A1140     -11.261  26.377  -1.986  1.00113.46           C  
ANISOU 1906  CB  GLN A1140    12944  16659  13505   1185    -87   1303       C  
ATOM   1907  CG  GLN A1140     -11.344  24.937  -2.493  1.00119.29           C  
ANISOU 1907  CG  GLN A1140    13604  17501  14217   1161   -188   1173       C  
ATOM   1908  CD  GLN A1140     -12.362  24.677  -3.576  1.00140.62           C  
ANISOU 1908  CD  GLN A1140    16175  20391  16862   1176   -189   1222       C  
ATOM   1909  OE1 GLN A1140     -13.522  25.066  -3.479  1.00165.31           O  
ANISOU 1909  OE1 GLN A1140    19298  23522  19990   1205   -133   1339       O  
ATOM   1910  NE2 GLN A1140     -11.943  23.977  -4.620  1.00156.30           N  
ANISOU 1910  NE2 GLN A1140    18048  22541  18797   1156   -254   1128       N  
ATOM   1911  N   THR A1141     -11.128  26.112   1.133  1.00105.33           N  
ANISOU 1911  N   THR A1141    12203  15199  12619   1166    -82   1233       N  
ATOM   1912  CA  THR A1141     -10.870  25.330   2.329  1.00100.34           C  
ANISOU 1912  CA  THR A1141    11663  14424  12038   1140   -132   1137       C  
ATOM   1913  C   THR A1141     -10.620  26.296   3.483  1.00 87.70           C  
ANISOU 1913  C   THR A1141    10184  12655  10483   1145    -60   1189       C  
ATOM   1914  O   THR A1141      -9.493  26.700   3.751  1.00 90.91           O  
ANISOU 1914  O   THR A1141    10642  13002  10900   1125    -54   1147       O  
ATOM   1915  CB  THR A1141      -9.730  24.330   2.101  1.00113.57           C  
ANISOU 1915  CB  THR A1141    13317  16127  13708   1101   -227    983       C  
ATOM   1916  OG1 THR A1141      -8.576  25.051   1.658  1.00138.70           O  
ANISOU 1916  OG1 THR A1141    16498  19334  16868   1092   -207    975       O  
ATOM   1917  CG2 THR A1141     -10.072  23.230   1.119  1.00105.07           C  
ANISOU 1917  CG2 THR A1141    12123  15199  12598   1093   -303    914       C  
ATOM   1918  N   PRO A1142     -11.681  26.721   4.191  1.00 84.79           N  
ANISOU 1918  N   PRO A1142     9864  12212  10142   1172     -1   1281       N  
ATOM   1919  CA  PRO A1142     -11.564  27.833   5.139  1.00 94.07           C  
ANISOU 1919  CA  PRO A1142    11138  13245  11357   1182     84   1344       C  
ATOM   1920  C   PRO A1142     -10.930  27.465   6.484  1.00 94.70           C  
ANISOU 1920  C   PRO A1142    11326  13175  11482   1150     56   1255       C  
ATOM   1921  O   PRO A1142     -10.198  28.260   7.077  1.00 77.00           O  
ANISOU 1921  O   PRO A1142     9157  10835   9263   1141    104   1255       O  
ATOM   1922  CB  PRO A1142     -13.024  28.301   5.272  1.00 93.43           C  
ANISOU 1922  CB  PRO A1142    11051  13164  11284   1225    150   1471       C  
ATOM   1923  CG  PRO A1142     -13.854  27.050   5.003  1.00 86.75           C  
ANISOU 1923  CG  PRO A1142    10144  12399  10417   1222     75   1435       C  
ATOM   1924  CD  PRO A1142     -13.044  26.195   4.058  1.00 80.55           C  
ANISOU 1924  CD  PRO A1142     9280  11729   9596   1193    -10   1329       C  
ATOM   1925  N   ASN A1143     -11.204  26.239   6.949  1.00 96.50           N  
ANISOU 1925  N   ASN A1143    11555  13388  11722   1131    -21   1180       N  
ATOM   1926  CA  ASN A1143     -10.755  25.798   8.258  1.00 93.43           C  
ANISOU 1926  CA  ASN A1143    11257  12868  11376   1100    -50   1108       C  
ATOM   1927  C   ASN A1143      -9.249  25.591   8.253  1.00 90.18           C  
ANISOU 1927  C   ASN A1143    10866  12437  10963   1061    -93   1003       C  
ATOM   1928  O   ASN A1143      -8.599  25.867   9.246  1.00 96.55           O  
ANISOU 1928  O   ASN A1143    11757  13131  11797   1040    -76    972       O  
ATOM   1929  CB  ASN A1143     -11.475  24.530   8.703  1.00100.80           C  
ANISOU 1929  CB  ASN A1143    12176  13797  12328   1091   -124   1067       C  
ATOM   1930  CG  ASN A1143     -12.973  24.730   8.754  1.00114.55           C  
ANISOU 1930  CG  ASN A1143    13900  15558  14067   1129    -81   1173       C  
ATOM   1931  OD1 ASN A1143     -13.439  25.871   8.761  1.00 99.86           O  
ANISOU 1931  OD1 ASN A1143    12061  13681  12202   1161     10   1276       O  
ATOM   1932  ND2 ASN A1143     -13.722  23.635   8.781  1.00137.23           N  
ANISOU 1932  ND2 ASN A1143    16732  18463  16945   1126   -147   1150       N  
ATOM   1933  N   ARG A1144      -8.721  25.107   7.125  1.00101.03           N  
ANISOU 1933  N   ARG A1144    12157  13927  12302   1053   -148    948       N  
ATOM   1934  CA  ARG A1144      -7.299  24.831   6.994  1.00 82.44           C  
ANISOU 1934  CA  ARG A1144     9810  11571   9941   1017   -196    845       C  
ATOM   1935  C   ARG A1144      -6.547  26.129   6.771  1.00 78.43           C  
ANISOU 1935  C   ARG A1144     9333  11050   9418   1022   -123    893       C  
ATOM   1936  O   ARG A1144      -5.447  26.272   7.275  1.00 89.72           O  
ANISOU 1936  O   ARG A1144    10821  12411  10857    993   -129    834       O  
ATOM   1937  CB  ARG A1144      -6.998  23.878   5.838  1.00 71.90           C  
ANISOU 1937  CB  ARG A1144     8372  10373   8575   1007   -279    766       C  
ATOM   1938  CG  ARG A1144      -5.540  23.450   5.752  1.00 66.95           C  
ANISOU 1938  CG  ARG A1144     7751   9743   7944    971   -337    650       C  
ATOM   1939  CD  ARG A1144      -5.291  22.740   4.438  1.00 90.65           C  
ANISOU 1939  CD  ARG A1144    10638  12899  10906    968   -404    583       C  
ATOM   1940  NE  ARG A1144      -3.882  22.478   4.200  1.00 95.08           N  
ANISOU 1940  NE  ARG A1144    11197  13474  11455    938   -451    482       N  
ATOM   1941  CZ  ARG A1144      -3.346  21.268   4.189  1.00 89.56           C  
ANISOU 1941  CZ  ARG A1144    10470  12782  10775    911   -542    358       C  
ATOM   1942  NH1 ARG A1144      -4.105  20.205   4.382  1.00 77.45           N  
ANISOU 1942  NH1 ARG A1144     8907  11244   9278    909   -595    321       N  
ATOM   1943  NH2 ARG A1144      -2.051  21.132   3.972  1.00105.73           N  
ANISOU 1943  NH2 ARG A1144    12519  14844  12809    886   -578    274       N  
ATOM   1944  N   ALA A1145      -7.138  27.050   6.002  1.00 81.11           N  
ANISOU 1944  N   ALA A1145     9626  11458   9733   1058    -56   1001       N  
ATOM   1945  CA  ALA A1145      -6.463  28.289   5.644  1.00 84.68           C  
ANISOU 1945  CA  ALA A1145    10090  11910  10175   1064     12   1056       C  
ATOM   1946  C   ALA A1145      -6.270  29.156   6.877  1.00 84.70           C  
ANISOU 1946  C   ALA A1145    10207  11751  10223   1059     83   1084       C  
ATOM   1947  O   ALA A1145      -5.206  29.747   7.047  1.00 82.75           O  
ANISOU 1947  O   ALA A1145    10004  11457   9981   1039    103   1060       O  
ATOM   1948  CB  ALA A1145      -7.208  29.043   4.568  1.00 93.77           C  
ANISOU 1948  CB  ALA A1145    11158  13172  11299   1104     68   1176       C  
ATOM   1949  N   LYS A1146      -7.311  29.224   7.721  1.00 90.56           N  
ANISOU 1949  N   LYS A1146    10994  12416  10999   1077    119   1134       N  
ATOM   1950  CA  LYS A1146      -7.277  30.087   8.894  1.00 78.21           C  
ANISOU 1950  CA  LYS A1146     9530  10707   9479   1076    193   1163       C  
ATOM   1951  C   LYS A1146      -6.165  29.619   9.844  1.00 76.98           C  
ANISOU 1951  C   LYS A1146     9449  10463   9336   1027    149   1049       C  
ATOM   1952  O   LYS A1146      -5.510  30.448  10.455  1.00 71.62           O  
ANISOU 1952  O   LYS A1146     8840   9695   8678   1013    203   1046       O  
ATOM   1953  CB  LYS A1146      -8.686  30.284   9.479  1.00 59.54           C  
ANISOU 1953  CB  LYS A1146     7185   8298   7141   1109    243   1245       C  
ATOM   1954  N   ARG A1147      -5.921  28.302   9.931  1.00 72.44           N  
ANISOU 1954  N   ARG A1147     8855   9917   8753   1001     53    954       N  
ATOM   1955  CA  ARG A1147      -4.845  27.757  10.744  1.00 71.15           C  
ANISOU 1955  CA  ARG A1147     8749   9684   8601    954      4    849       C  
ATOM   1956  C   ARG A1147      -3.470  28.155  10.194  1.00 73.32           C  
ANISOU 1956  C   ARG A1147     9022   9984   8851    932     -1    804       C  
ATOM   1957  O   ARG A1147      -2.562  28.481  10.963  1.00 54.48           O  
ANISOU 1957  O   ARG A1147     6709   7514   6477    901     15    761       O  
ATOM   1958  CB  ARG A1147      -4.914  26.229  10.792  1.00 70.47           C  
ANISOU 1958  CB  ARG A1147     8624   9632   8517    935   -101    766       C  
ATOM   1959  CG  ARG A1147      -6.030  25.716  11.679  1.00 74.62           C  
ANISOU 1959  CG  ARG A1147     9171  10106   9075    943   -107    792       C  
ATOM   1960  CD  ARG A1147      -5.882  24.240  11.955  1.00 84.62           C  
ANISOU 1960  CD  ARG A1147    10414  11379  10360    915   -211    703       C  
ATOM   1961  NE  ARG A1147      -6.126  23.465  10.761  1.00 82.43           N  
ANISOU 1961  NE  ARG A1147    10038  11218  10062    926   -273    677       N  
ATOM   1962  CZ  ARG A1147      -7.319  23.001  10.421  1.00104.23           C  
ANISOU 1962  CZ  ARG A1147    12745  14032  12825    951   -289    719       C  
ATOM   1963  NH1 ARG A1147      -8.381  23.235  11.184  1.00 97.53           N  
ANISOU 1963  NH1 ARG A1147    11932  13129  11996    970   -248    793       N  
ATOM   1964  NH2 ARG A1147      -7.437  22.310   9.303  1.00134.11           N  
ANISOU 1964  NH2 ARG A1147    16438  17931  16589    957   -346    684       N  
ATOM   1965  N   VAL A1148      -3.316  28.088   8.865  1.00 66.06           N  
ANISOU 1965  N   VAL A1148     8016   9190   7894    946    -26    812       N  
ATOM   1966  CA  VAL A1148      -2.055  28.420   8.238  1.00 66.13           C  
ANISOU 1966  CA  VAL A1148     8012   9241   7873    927    -37    773       C  
ATOM   1967  C   VAL A1148      -1.800  29.920   8.348  1.00 72.33           C  
ANISOU 1967  C   VAL A1148     8843   9971   8669    937     62    854       C  
ATOM   1968  O   VAL A1148      -0.677  30.341   8.619  1.00 70.72           O  
ANISOU 1968  O   VAL A1148     8686   9720   8463    908     71    814       O  
ATOM   1969  CB  VAL A1148      -1.994  27.908   6.790  1.00 69.59           C  
ANISOU 1969  CB  VAL A1148     8335   9840   8264    938    -94    757       C  
ATOM   1970  CG1 VAL A1148      -0.680  28.288   6.101  1.00 66.65           C  
ANISOU 1970  CG1 VAL A1148     7944   9523   7856    920   -105    722       C  
ATOM   1971  CG2 VAL A1148      -2.188  26.397   6.779  1.00 69.26           C  
ANISOU 1971  CG2 VAL A1148     8254   9838   8225    924   -192    664       C  
ATOM   1972  N   ILE A1149      -2.850  30.721   8.157  1.00 77.93           N  
ANISOU 1972  N   ILE A1149     9536  10680   9393    977    136    967       N  
ATOM   1973  CA  ILE A1149      -2.725  32.169   8.198  1.00 76.11           C  
ANISOU 1973  CA  ILE A1149     9338  10394   9186    991    234   1052       C  
ATOM   1974  C   ILE A1149      -2.349  32.605   9.611  1.00 74.20           C  
ANISOU 1974  C   ILE A1149     9210   9996   8986    966    278   1019       C  
ATOM   1975  O   ILE A1149      -1.553  33.522   9.748  1.00 87.48           O  
ANISOU 1975  O   ILE A1149    10933  11625  10681    952    327   1026       O  
ATOM   1976  CB  ILE A1149      -3.998  32.873   7.683  1.00 75.02           C  
ANISOU 1976  CB  ILE A1149     9151  10292   9061   1042    303   1185       C  
ATOM   1977  CG1 ILE A1149      -4.268  32.588   6.209  1.00 77.10           C  
ANISOU 1977  CG1 ILE A1149     9293  10725   9276   1064    268   1224       C  
ATOM   1978  CG2 ILE A1149      -3.896  34.357   7.912  1.00 72.86           C  
ANISOU 1978  CG2 ILE A1149     8919   9933   8829   1056    409   1269       C  
ATOM   1979  CD1 ILE A1149      -5.628  33.059   5.754  1.00 84.73           C  
ANISOU 1979  CD1 ILE A1149    10205  11737  10251   1113    326   1351       C  
ATOM   1980  N   THR A1150      -2.919  31.962  10.642  1.00 73.31           N  
ANISOU 1980  N   THR A1150     9143   9816   8894    958    260    984       N  
ATOM   1981  CA  THR A1150      -2.605  32.275  12.032  1.00 80.43           C  
ANISOU 1981  CA  THR A1150    10146  10585   9830    931    297    946       C  
ATOM   1982  C   THR A1150      -1.123  32.007  12.289  1.00 83.89           C  
ANISOU 1982  C   THR A1150    10620  11004  10250    880    252    846       C  
ATOM   1983  O   THR A1150      -0.449  32.795  12.956  1.00 82.31           O  
ANISOU 1983  O   THR A1150    10489  10718  10068    858    305    832       O  
ATOM   1984  CB  THR A1150      -3.470  31.483  13.029  1.00 81.62           C  
ANISOU 1984  CB  THR A1150    10323  10690   9998    930    272    925       C  
ATOM   1985  OG1 THR A1150      -4.849  31.807  12.855  1.00 83.88           O  
ANISOU 1985  OG1 THR A1150    10581  10988  10300    977    319   1022       O  
ATOM   1986  CG2 THR A1150      -3.097  31.698  14.483  1.00 76.86           C  
ANISOU 1986  CG2 THR A1150     9814   9967   9422    896    301    878       C  
ATOM   1987  N   THR A1151      -0.631  30.883  11.751  1.00 74.68           N  
ANISOU 1987  N   THR A1151     9405   9919   9049    863    156    774       N  
ATOM   1988  CA  THR A1151       0.763  30.491  11.896  1.00 70.60           C  
ANISOU 1988  CA  THR A1151     8914   9399   8513    817    104    678       C  
ATOM   1989  C   THR A1151       1.664  31.545  11.249  1.00 70.25           C  
ANISOU 1989  C   THR A1151     8870   9372   8452    814    148    704       C  
ATOM   1990  O   THR A1151       2.730  31.840  11.773  1.00 77.48           O  
ANISOU 1990  O   THR A1151     9843  10232   9365    777    156    653       O  
ATOM   1991  CB  THR A1151       0.965  29.048  11.411  1.00 65.79           C  
ANISOU 1991  CB  THR A1151     8244   8874   7879    806     -6    601       C  
ATOM   1992  OG1 THR A1151       0.053  28.240  12.164  1.00 61.76           O  
ANISOU 1992  OG1 THR A1151     7742   8327   7396    809    -33    593       O  
ATOM   1993  CG2 THR A1151       2.379  28.547  11.585  1.00 55.95           C  
ANISOU 1993  CG2 THR A1151     7020   7625   6615    760    -63    500       C  
ATOM   1994  N   PHE A1152       1.249  32.103  10.107  1.00 74.33           N  
ANISOU 1994  N   PHE A1152     9316   9970   8955    851    175    785       N  
ATOM   1995  CA  PHE A1152       1.985  33.190   9.471  1.00 80.53           C  
ANISOU 1995  CA  PHE A1152    10092  10772   9732    852    223    829       C  
ATOM   1996  C   PHE A1152       1.942  34.461  10.310  1.00 73.62           C  
ANISOU 1996  C   PHE A1152     9297   9769   8907    851    326    879       C  
ATOM   1997  O   PHE A1152       2.936  35.172  10.409  1.00 78.95           O  
ANISOU 1997  O   PHE A1152    10008  10404   9584    826    355    866       O  
ATOM   1998  CB  PHE A1152       1.459  33.506   8.067  1.00 86.12           C  
ANISOU 1998  CB  PHE A1152    10697  11606  10418    893    231    917       C  
ATOM   1999  CG  PHE A1152       1.958  32.578   6.992  1.00 86.97           C  
ANISOU 1999  CG  PHE A1152    10719  11859  10468    886    138    861       C  
ATOM   2000  CD1 PHE A1152       3.312  32.483   6.705  1.00 98.87           C  
ANISOU 2000  CD1 PHE A1152    12227  13398  11941    853     96    793       C  
ATOM   2001  CD2 PHE A1152       1.076  31.781   6.283  1.00 84.97           C  
ANISOU 2001  CD2 PHE A1152    10381  11712  10193    912     93    871       C  
ATOM   2002  CE1 PHE A1152       3.768  31.625   5.715  1.00105.39           C  
ANISOU 2002  CE1 PHE A1152    12969  14360  12713    849     11    735       C  
ATOM   2003  CE2 PHE A1152       1.536  30.922   5.298  1.00 91.07           C  
ANISOU 2003  CE2 PHE A1152    11068  12619  10913    905      9    809       C  
ATOM   2004  CZ  PHE A1152       2.881  30.848   5.010  1.00 92.35           C  
ANISOU 2004  CZ  PHE A1152    11231  12814  11044    874    -32    740       C  
ATOM   2005  N   ARG A1153       0.785  34.739  10.903  1.00 69.42           N  
ANISOU 2005  N   ARG A1153     8787   9173   8415    878    380    934       N  
ATOM   2006  CA  ARG A1153       0.547  36.004  11.564  1.00 71.78           C  
ANISOU 2006  CA  ARG A1153     9146   9359   8769    886    486    992       C  
ATOM   2007  C   ARG A1153       1.320  36.021  12.873  1.00 75.02           C  
ANISOU 2007  C   ARG A1153     9652   9659   9192    838    494    903       C  
ATOM   2008  O   ARG A1153       1.902  37.051  13.201  1.00 80.66           O  
ANISOU 2008  O   ARG A1153    10414  10298   9935    823    560    910       O  
ATOM   2009  CB  ARG A1153      -0.961  36.179  11.753  1.00 82.31           C  
ANISOU 2009  CB  ARG A1153    10465  10672  10136    932    534   1073       C  
ATOM   2010  CG  ARG A1153      -1.419  37.491  12.372  1.00 94.40           C  
ANISOU 2010  CG  ARG A1153    12046  12088  11732    950    648   1140       C  
ATOM   2011  CD  ARG A1153      -2.940  37.532  12.486  1.00106.52           C  
ANISOU 2011  CD  ARG A1153    13559  13619  13293    998    686   1220       C  
ATOM   2012  NE  ARG A1153      -3.464  36.506  13.387  1.00116.66           N  
ANISOU 2012  NE  ARG A1153    14874  14885  14565    986    638   1159       N  
ATOM   2013  CZ  ARG A1153      -3.496  36.616  14.717  1.00126.79           C  
ANISOU 2013  CZ  ARG A1153    16237  16063  15876    964    668   1110       C  
ATOM   2014  NH1 ARG A1153      -3.072  37.727  15.304  1.00129.11           N  
ANISOU 2014  NH1 ARG A1153    16588  16255  16212    953    750   1110       N  
ATOM   2015  NH2 ARG A1153      -3.962  35.618  15.451  1.00112.04           N  
ANISOU 2015  NH2 ARG A1153    14384  14194  13993    954    616   1063       N  
ATOM   2016  N   THR A1154       1.319  34.892  13.605  1.00 77.79           N  
ANISOU 2016  N   THR A1154    10027  10003   9525    813    428    822       N  
ATOM   2017  CA  THR A1154       1.839  34.855  14.972  1.00 79.52           C  
ANISOU 2017  CA  THR A1154    10332  10124   9757    768    440    747       C  
ATOM   2018  C   THR A1154       3.215  34.189  15.062  1.00 73.56           C  
ANISOU 2018  C   THR A1154     9594   9393   8963    717    369    648       C  
ATOM   2019  O   THR A1154       4.021  34.526  15.923  1.00 77.89           O  
ANISOU 2019  O   THR A1154    10209   9871   9515    676    393    595       O  
ATOM   2020  CB  THR A1154       0.856  34.198  15.945  1.00 76.19           C  
ANISOU 2020  CB  THR A1154     9931   9666   9351    773    430    736       C  
ATOM   2021  OG1 THR A1154       0.684  32.853  15.497  1.00 89.48           O  
ANISOU 2021  OG1 THR A1154    11559  11434  11004    775    330    704       O  
ATOM   2022  CG2 THR A1154      -0.481  34.904  15.993  1.00 76.58           C  
ANISOU 2022  CG2 THR A1154     9973   9684   9441    822    506    830       C  
ATOM   2023  N   GLY A1155       3.486  33.223  14.186  1.00 72.68           N  
ANISOU 2023  N   GLY A1155     9420   9384   8813    719    280    619       N  
ATOM   2024  CA  GLY A1155       4.735  32.480  14.255  1.00 68.08           C  
ANISOU 2024  CA  GLY A1155     8847   8827   8195    674    207    525       C  
ATOM   2025  C   GLY A1155       4.701  31.418  15.356  1.00 73.64           C  
ANISOU 2025  C   GLY A1155     9583   9493   8904    643    155    454       C  
ATOM   2026  O   GLY A1155       5.750  31.014  15.859  1.00 80.55           O  
ANISOU 2026  O   GLY A1155    10491  10352   9761    597    119    378       O  
ATOM   2027  N   THR A1156       3.491  30.966  15.720  1.00 65.71           N  
ANISOU 2027  N   THR A1156     8564   8478   7924    668    152    484       N  
ATOM   2028  CA  THR A1156       3.325  29.971  16.766  1.00 59.48           C  
ANISOU 2028  CA  THR A1156     7797   7657   7146    642    105    433       C  
ATOM   2029  C   THR A1156       2.448  28.839  16.246  1.00 56.02           C  
ANISOU 2029  C   THR A1156     7288   7285   6711    669     32    440       C  
ATOM   2030  O   THR A1156       1.915  28.940  15.139  1.00 59.69           O  
ANISOU 2030  O   THR A1156     7693   7820   7168    708     30    487       O  
ATOM   2031  CB  THR A1156       2.707  30.610  18.015  1.00 62.33           C  
ANISOU 2031  CB  THR A1156     8221   7924   7537    638    181    459       C  
ATOM   2032  OG1 THR A1156       1.400  31.083  17.667  1.00 64.17           O  
ANISOU 2032  OG1 THR A1156     8428   8160   7792    690    229    546       O  
ATOM   2033  CG2 THR A1156       3.540  31.740  18.588  1.00 57.55           C  
ANISOU 2033  CG2 THR A1156     7685   7249   6934    608    257    444       C  
ATOM   2034  N   TRP A1157       2.289  27.790  17.070  1.00 52.56           N  
ANISOU 2034  N   TRP A1157     6855   6827   6289    647    -24    397       N  
ATOM   2035  CA  TRP A1157       1.438  26.651  16.744  1.00 52.88           C  
ANISOU 2035  CA  TRP A1157     6831   6917   6342    668    -95    400       C  
ATOM   2036  C   TRP A1157       0.082  26.721  17.440  1.00 62.75           C  
ANISOU 2036  C   TRP A1157     8092   8129   7620    692    -60    462       C  
ATOM   2037  O   TRP A1157      -0.568  25.692  17.593  1.00 63.44           O  
ANISOU 2037  O   TRP A1157     8142   8235   7726    697   -121    457       O  
ATOM   2038  CB  TRP A1157       2.108  25.317  17.098  1.00 44.67           C  
ANISOU 2038  CB  TRP A1157     5775   5886   5311    630   -192    317       C  
ATOM   2039  CG  TRP A1157       3.436  25.136  16.464  1.00 44.98           C  
ANISOU 2039  CG  TRP A1157     5801   5965   5323    606   -233    250       C  
ATOM   2040  CD1 TRP A1157       4.658  25.165  17.071  1.00 46.29           C  
ANISOU 2040  CD1 TRP A1157     6014   6095   5477    560   -239    193       C  
ATOM   2041  CD2 TRP A1157       3.675  24.941  15.063  1.00 46.67           C  
ANISOU 2041  CD2 TRP A1157     5948   6272   5513    627   -272    235       C  
ATOM   2042  NE1 TRP A1157       5.649  24.979  16.139  1.00 41.87           N  
ANISOU 2042  NE1 TRP A1157     5424   5597   4890    552   -281    144       N  
ATOM   2043  CE2 TRP A1157       5.083  24.865  14.898  1.00 44.19           C  
ANISOU 2043  CE2 TRP A1157     5646   5970   5173    593   -301    168       C  
ATOM   2044  CE3 TRP A1157       2.834  24.820  13.947  1.00 41.18           C  
ANISOU 2044  CE3 TRP A1157     5180   5656   4810    670   -284    273       C  
ATOM   2045  CZ2 TRP A1157       5.678  24.668  13.653  1.00 43.29           C  
ANISOU 2045  CZ2 TRP A1157     5473   5948   5028    602   -344    134       C  
ATOM   2046  CZ3 TRP A1157       3.428  24.632  12.722  1.00 46.15           C  
ANISOU 2046  CZ3 TRP A1157     5748   6380   5407    677   -325    238       C  
ATOM   2047  CH2 TRP A1157       4.825  24.554  12.579  1.00 46.38           C  
ANISOU 2047  CH2 TRP A1157     5789   6420   5412    644   -355    169       C  
ATOM   2048  N   ASP A1158      -0.333  27.921  17.862  1.00 72.76           N  
ANISOU 2048  N   ASP A1158     9408   9343   8894    707     37    519       N  
ATOM   2049  CA  ASP A1158      -1.567  28.103  18.605  1.00 72.70           C  
ANISOU 2049  CA  ASP A1158     9416   9296   8911    730     79    577       C  
ATOM   2050  C   ASP A1158      -2.769  27.599  17.804  1.00 79.63           C  
ANISOU 2050  C   ASP A1158    10226  10238   9793    775     49    632       C  
ATOM   2051  O   ASP A1158      -3.721  27.096  18.397  1.00101.57           O  
ANISOU 2051  O   ASP A1158    12998  13005  12589    785     35    658       O  
ATOM   2052  CB  ASP A1158      -1.720  29.554  19.068  1.00 77.61           C  
ANISOU 2052  CB  ASP A1158    10096   9849   9543    740    192    622       C  
ATOM   2053  CG  ASP A1158      -0.782  29.900  20.207  1.00 86.37           C  
ANISOU 2053  CG  ASP A1158    11275  10888  10652    690    220    562       C  
ATOM   2054  OD1 ASP A1158       0.178  29.128  20.410  1.00105.75           O  
ANISOU 2054  OD1 ASP A1158    13731  13357  13093    648    153    491       O  
ATOM   2055  OD2 ASP A1158      -1.021  30.926  20.882  1.00 83.66           O1-
ANISOU 2055  OD2 ASP A1158    10981  10480  10325    692    308    586       O1-
ATOM   2056  N   ALA A1159      -2.741  27.739  16.469  1.00 66.77           N  
ANISOU 2056  N   ALA A1159     8542   8683   8144    802     41    654       N  
ATOM   2057  CA  ALA A1159      -3.878  27.337  15.658  1.00 56.53           C  
ANISOU 2057  CA  ALA A1159     7175   7457   6845    844     19    709       C  
ATOM   2058  C   ALA A1159      -3.996  25.815  15.556  1.00 58.99           C  
ANISOU 2058  C   ALA A1159     7436   7816   7163    830    -88    653       C  
ATOM   2059  O   ALA A1159      -4.950  25.333  14.945  1.00 60.63           O  
ANISOU 2059  O   ALA A1159     7583   8083   7370    860   -115    689       O  
ATOM   2060  CB  ALA A1159      -3.843  27.988  14.307  1.00 50.22           C  
ANISOU 2060  CB  ALA A1159     6326   6732   6021    875     48    754       C  
ATOM   2061  N   TYR A1160      -3.050  25.067  16.160  1.00 52.83           N  
ANISOU 2061  N   TYR A1160     6675   7005   6391    785   -148    569       N  
ATOM   2062  CA  TYR A1160      -3.076  23.608  16.152  1.00 49.15           C  
ANISOU 2062  CA  TYR A1160     6160   6568   5945    768   -250    512       C  
ATOM   2063  C   TYR A1160      -3.155  23.052  17.569  1.00 59.46           C  
ANISOU 2063  C   TYR A1160     7507   7801   7284    738   -271    496       C  
ATOM   2064  O   TYR A1160      -3.099  21.841  17.764  1.00 71.99           O  
ANISOU 2064  O   TYR A1160     9059   9396   8899    718   -355    451       O  
ATOM   2065  CB  TYR A1160      -1.883  23.015  15.404  1.00 39.12           C  
ANISOU 2065  CB  TYR A1160     4855   5347   4662    745   -317    426       C  
ATOM   2066  CG  TYR A1160      -1.945  23.271  13.922  1.00 45.73           C  
ANISOU 2066  CG  TYR A1160     5628   6283   5466    775   -317    440       C  
ATOM   2067  CD1 TYR A1160      -1.595  24.509  13.387  1.00 44.64           C  
ANISOU 2067  CD1 TYR A1160     5507   6159   5295    790   -244    481       C  
ATOM   2068  CD2 TYR A1160      -2.392  22.296  13.042  1.00 54.47           C  
ANISOU 2068  CD2 TYR A1160     6648   7472   6575    789   -388    414       C  
ATOM   2069  CE1 TYR A1160      -1.688  24.785  12.031  1.00 45.98           C  
ANISOU 2069  CE1 TYR A1160     5609   6429   5431    817   -241    504       C  
ATOM   2070  CE2 TYR A1160      -2.492  22.552  11.678  1.00 55.44           C  
ANISOU 2070  CE2 TYR A1160     6703   7699   6661    816   -385    429       C  
ATOM   2071  CZ  TYR A1160      -2.125  23.797  11.165  1.00 52.18           C  
ANISOU 2071  CZ  TYR A1160     6307   7308   6212    830   -312    477       C  
ATOM   2072  OH  TYR A1160      -2.224  24.064   9.820  1.00 50.25           O  
ANISOU 2072  OH  TYR A1160     5988   7178   5929    855   -309    499       O  
ATOM   2073  N   SER A 261      -3.259  23.940  18.561  1.00 68.98           N  
ANISOU 2073  N   SER A 261     8782   8939   8489    732   -195    530       N  
ATOM   2074  CA  SER A 261      -3.297  23.540  19.962  1.00 75.14           C  
ANISOU 2074  CA  SER A 261     9598   9659   9292    700   -207    518       C  
ATOM   2075  C   SER A 261      -4.738  23.259  20.378  1.00 75.29           C  
ANISOU 2075  C   SER A 261     9599   9677   9331    728   -205    585       C  
ATOM   2076  O   SER A 261      -5.670  23.877  19.889  1.00 74.66           O  
ANISOU 2076  O   SER A 261     9510   9616   9241    771   -155    651       O  
ATOM   2077  CB  SER A 261      -2.670  24.586  20.860  1.00 84.36           C  
ANISOU 2077  CB  SER A 261    10843  10763  10447    675   -129    512       C  
ATOM   2078  OG  SER A 261      -2.579  24.115  22.195  1.00102.71           O  
ANISOU 2078  OG  SER A 261    13192  13046  12787    638   -147    493       O  
ATOM   2079  N   GLU A 262      -4.907  22.318  21.307  1.00 72.03           N  
ANISOU 2079  N   GLU A 262     9178   9245   8946    702   -262    571       N  
ATOM   2080  CA  GLU A 262      -6.198  22.015  21.895  1.00 60.61           C  
ANISOU 2080  CA  GLU A 262     7717   7794   7518    721   -264    633       C  
ATOM   2081  C   GLU A 262      -6.373  22.889  23.137  1.00 62.20           C  
ANISOU 2081  C   GLU A 262     7982   7940   7710    711   -186    662       C  
ATOM   2082  O   GLU A 262      -5.440  23.044  23.921  1.00 62.56           O  
ANISOU 2082  O   GLU A 262     8068   7951   7751    670   -176    616       O  
ATOM   2083  CB  GLU A 262      -6.233  20.532  22.265  1.00 58.59           C  
ANISOU 2083  CB  GLU A 262     7412   7547   7302    695   -368    605       C  
ATOM   2084  CG  GLU A 262      -6.252  19.595  21.066  1.00 64.44           C  
ANISOU 2084  CG  GLU A 262     8081   8343   8061    707   -447    574       C  
ATOM   2085  CD  GLU A 262      -6.812  18.197  21.320  1.00 86.55           C  
ANISOU 2085  CD  GLU A 262    10821  11152  10912    698   -541    573       C  
ATOM   2086  OE1 GLU A 262      -6.042  17.324  21.762  1.00 93.94           O  
ANISOU 2086  OE1 GLU A 262    11742  12068  11884    659   -607    519       O  
ATOM   2087  OE2 GLU A 262      -8.030  17.971  21.078  1.00 99.61           O1-
ANISOU 2087  OE2 GLU A 262    12441  12833  12573    730   -548    629       O1-
ATOM   2088  N   GLN A 263      -7.592  23.407  23.340  1.00 67.84           N  
ANISOU 2088  N   GLN A 263     8703   8652   8421    749   -133    735       N  
ATOM   2089  CA  GLN A 263      -7.907  24.373  24.381  1.00 56.61           C  
ANISOU 2089  CA  GLN A 263     7337   7183   6989    749    -48    764       C  
ATOM   2090  C   GLN A 263      -7.843  23.742  25.767  1.00 56.41           C  
ANISOU 2090  C   GLN A 263     7318   7140   6976    708    -82    748       C  
ATOM   2091  O   GLN A 263      -7.648  24.459  26.749  1.00 49.22           O  
ANISOU 2091  O   GLN A 263     6455   6193   6053    689    -20    739       O  
ATOM   2092  CB  GLN A 263      -9.340  24.875  24.186  1.00 64.48           C  
ANISOU 2092  CB  GLN A 263     8324   8190   7984    803      3    851       C  
ATOM   2093  N   TRP A 264      -8.059  22.417  25.846  1.00 53.49           N  
ANISOU 2093  N   TRP A 264     6895   6798   6631    695   -180    746       N  
ATOM   2094  CA  TRP A 264      -8.098  21.767  27.140  1.00 53.11           C  
ANISOU 2094  CA  TRP A 264     6840   6742   6598    658   -217    746       C  
ATOM   2095  C   TRP A 264      -6.706  21.584  27.722  1.00 62.21           C  
ANISOU 2095  C   TRP A 264     8013   7876   7750    600   -236    675       C  
ATOM   2096  O   TRP A 264      -6.578  21.363  28.923  1.00 75.04           O  
ANISOU 2096  O   TRP A 264     9642   9494   9376    564   -242    673       O  
ATOM   2097  CB  TRP A 264      -8.843  20.444  27.092  1.00 52.65           C  
ANISOU 2097  CB  TRP A 264     6714   6715   6576    663   -312    777       C  
ATOM   2098  CG  TRP A 264      -8.213  19.390  26.250  1.00 57.75           C  
ANISOU 2098  CG  TRP A 264     7311   7379   7253    649   -402    728       C  
ATOM   2099  CD1 TRP A 264      -8.468  19.159  24.935  1.00 67.63           C  
ANISOU 2099  CD1 TRP A 264     8526   8660   8509    681   -428    725       C  
ATOM   2100  CD2 TRP A 264      -7.295  18.369  26.665  1.00 64.92           C  
ANISOU 2100  CD2 TRP A 264     8191   8279   8195    601   -481    678       C  
ATOM   2101  NE1 TRP A 264      -7.746  18.082  24.490  1.00 70.74           N  
ANISOU 2101  NE1 TRP A 264     8875   9065   8938    657   -516    667       N  
ATOM   2102  CE2 TRP A 264      -7.014  17.578  25.528  1.00 71.45           C  
ANISOU 2102  CE2 TRP A 264     8970   9128   9051    608   -550    638       C  
ATOM   2103  CE3 TRP A 264      -6.653  18.051  27.866  1.00 75.67           C  
ANISOU 2103  CE3 TRP A 264     9561   9622   9567    551   -499    661       C  
ATOM   2104  CZ2 TRP A 264      -6.115  16.513  25.552  1.00 72.76           C  
ANISOU 2104  CZ2 TRP A 264     9098   9288   9259    571   -634    582       C  
ATOM   2105  CZ3 TRP A 264      -5.761  16.997  27.890  1.00 70.00           C  
ANISOU 2105  CZ3 TRP A 264     8805   8902   8890    513   -581    613       C  
ATOM   2106  CH2 TRP A 264      -5.494  16.243  26.749  1.00 70.59           C  
ANISOU 2106  CH2 TRP A 264     8834   8988   8997    524   -648    573       C  
ATOM   2107  N   ILE A 265      -5.668  21.639  26.880  1.00 67.10           N  
ANISOU 2107  N   ILE A 265     8639   8493   8364    591   -247    619       N  
ATOM   2108  CA  ILE A 265      -4.315  21.475  27.387  1.00 61.47           C  
ANISOU 2108  CA  ILE A 265     7945   7764   7646    536   -264    553       C  
ATOM   2109  C   ILE A 265      -3.917  22.647  28.284  1.00 58.64           C  
ANISOU 2109  C   ILE A 265     7652   7374   7253    515   -171    540       C  
ATOM   2110  O   ILE A 265      -3.328  22.431  29.328  1.00 57.38           O  
ANISOU 2110  O   ILE A 265     7503   7210   7090    467   -179    514       O  
ATOM   2111  CB  ILE A 265      -3.317  21.267  26.250  1.00 65.83           C  
ANISOU 2111  CB  ILE A 265     8487   8328   8198    533   -299    496       C  
ATOM   2112  CG1 ILE A 265      -3.712  20.068  25.389  1.00 67.85           C  
ANISOU 2112  CG1 ILE A 265     8670   8617   8491    552   -393    497       C  
ATOM   2113  CG2 ILE A 265      -1.926  21.109  26.844  1.00 60.91           C  
ANISOU 2113  CG2 ILE A 265     7885   7689   7567    476   -315    433       C  
ATOM   2114  CD1 ILE A 265      -3.396  18.753  26.041  1.00 65.74           C  
ANISOU 2114  CD1 ILE A 265     8360   8351   8269    513   -484    477       C  
ATOM   2115  N   PHE A 266      -4.224  23.879  27.889  1.00 53.75           N  
ANISOU 2115  N   PHE A 266     7075   6735   6613    548    -81    558       N  
ATOM   2116  CA  PHE A 266      -3.880  25.026  28.710  1.00 55.02           C  
ANISOU 2116  CA  PHE A 266     7296   6860   6749    528     12    540       C  
ATOM   2117  C   PHE A 266      -4.682  25.005  30.016  1.00 67.77           C  
ANISOU 2117  C   PHE A 266     8910   8477   8363    519     32    572       C  
ATOM   2118  O   PHE A 266      -4.233  25.524  31.034  1.00 70.31           O  
ANISOU 2118  O   PHE A 266     9265   8784   8665    482     80    541       O  
ATOM   2119  CB  PHE A 266      -4.189  26.289  27.918  1.00 52.53           C  
ANISOU 2119  CB  PHE A 266     7013   6519   6425    573    100    564       C  
ATOM   2120  CG  PHE A 266      -3.843  27.595  28.570  1.00 58.00           C  
ANISOU 2120  CG  PHE A 266     7768   7165   7103    559    203    541       C  
ATOM   2121  CD1 PHE A 266      -2.595  28.163  28.365  1.00 66.55           C  
ANISOU 2121  CD1 PHE A 266     8889   8226   8173    528    232    484       C  
ATOM   2122  CD2 PHE A 266      -4.773  28.278  29.347  1.00 58.56           C  
ANISOU 2122  CD2 PHE A 266     7858   7215   7176    577    274    576       C  
ATOM   2123  CE1 PHE A 266      -2.280  29.385  28.946  1.00 73.34           C  
ANISOU 2123  CE1 PHE A 266     9803   9038   9025    514    329    460       C  
ATOM   2124  CE2 PHE A 266      -4.454  29.486  29.947  1.00 60.82           C  
ANISOU 2124  CE2 PHE A 266     8197   7455   7456    563    371    546       C  
ATOM   2125  CZ  PHE A 266      -3.216  30.045  29.726  1.00 70.64           C  
ANISOU 2125  CZ  PHE A 266     9477   8672   8690    532    399    488       C  
ATOM   2126  N   ARG A 267      -5.880  24.414  30.002  1.00 70.98           N  
ANISOU 2126  N   ARG A 267     9275   8908   8787    552     -4    633       N  
ATOM   2127  CA  ARG A 267      -6.639  24.270  31.242  1.00 78.75           C  
ANISOU 2127  CA  ARG A 267    10248   9905   9767    542      3    667       C  
ATOM   2128  C   ARG A 267      -6.006  23.197  32.138  1.00 75.04           C  
ANISOU 2128  C   ARG A 267     9745   9462   9306    484    -74    643       C  
ATOM   2129  O   ARG A 267      -6.276  23.138  33.331  1.00 77.05           O  
ANISOU 2129  O   ARG A 267     9992   9735   9549    459    -65    656       O  
ATOM   2130  CB  ARG A 267      -8.116  23.904  31.005  1.00 75.30           C  
ANISOU 2130  CB  ARG A 267     9774   9492   9346    592    -18    745       C  
ATOM   2131  CG  ARG A 267      -8.991  25.005  30.415  1.00 60.31           C  
ANISOU 2131  CG  ARG A 267     7902   7573   7439    650     68    788       C  
ATOM   2132  CD  ARG A 267      -9.083  26.309  31.162  1.00 59.04           C  
ANISOU 2132  CD  ARG A 267     7794   7378   7259    652    177    779       C  
ATOM   2133  NE  ARG A 267     -10.133  27.039  30.465  1.00 63.73           N  
ANISOU 2133  NE  ARG A 267     8394   7960   7859    715    236    839       N  
ATOM   2134  CZ  ARG A 267     -11.421  27.025  30.789  1.00 63.85           C  
ANISOU 2134  CZ  ARG A 267     8392   7994   7876    751    248    905       C  
ATOM   2135  NH1 ARG A 267     -11.834  26.367  31.859  1.00 66.90           N  
ANISOU 2135  NH1 ARG A 267     8753   8412   8255    729    208    918       N  
ATOM   2136  NH2 ARG A 267     -12.289  27.703  30.063  1.00 63.96           N  
ANISOU 2136  NH2 ARG A 267     8410   7999   7895    809    303    961       N  
ATOM   2137  N   LEU A 268      -5.186  22.320  31.558  1.00 70.76           N  
ANISOU 2137  N   LEU A 268     9176   8926   8784    464   -152    610       N  
ATOM   2138  CA  LEU A 268      -4.538  21.294  32.355  1.00 68.10           C  
ANISOU 2138  CA  LEU A 268     8802   8610   8462    410   -225    592       C  
ATOM   2139  C   LEU A 268      -3.258  21.838  32.977  1.00 64.83           C  
ANISOU 2139  C   LEU A 268     8430   8185   8016    357   -183    529       C  
ATOM   2140  O   LEU A 268      -2.817  21.367  34.017  1.00 71.44           O  
ANISOU 2140  O   LEU A 268     9248   9047   8851    307   -208    521       O  
ATOM   2141  CB  LEU A 268      -4.257  20.047  31.516  1.00 69.16           C  
ANISOU 2141  CB  LEU A 268     8883   8754   8642    411   -328    584       C  
ATOM   2142  CG  LEU A 268      -4.092  18.769  32.337  1.00 70.87           C  
ANISOU 2142  CG  LEU A 268     9039   8993   8896    369   -417    598       C  
ATOM   2143  CD1 LEU A 268      -5.174  18.657  33.418  1.00 71.98           C  
ANISOU 2143  CD1 LEU A 268     9154   9159   9034    371   -411    666       C  
ATOM   2144  CD2 LEU A 268      -4.137  17.546  31.424  1.00 65.94           C  
ANISOU 2144  CD2 LEU A 268     8355   8371   8330    383   -517    598       C  
ATOM   2145  N   TYR A 269      -2.666  22.845  32.335  1.00 64.87           N  
ANISOU 2145  N   TYR A 269     8490   8160   7997    366   -117    487       N  
ATOM   2146  CA  TYR A 269      -1.560  23.570  32.931  1.00 61.61           C  
ANISOU 2146  CA  TYR A 269     8124   7734   7550    319    -61    428       C  
ATOM   2147  C   TYR A 269      -2.028  24.399  34.129  1.00 64.97           C  
ANISOU 2147  C   TYR A 269     8576   8162   7948    306     19    435       C  
ATOM   2148  O   TYR A 269      -1.342  24.430  35.149  1.00 77.32           O  
ANISOU 2148  O   TYR A 269    10146   9745   9489    251     31    401       O  
ATOM   2149  CB  TYR A 269      -0.838  24.413  31.879  1.00 61.40           C  
ANISOU 2149  CB  TYR A 269     8145   7674   7511    334    -16    388       C  
ATOM   2150  CG  TYR A 269      -0.224  23.634  30.741  1.00 60.83           C  
ANISOU 2150  CG  TYR A 269     8044   7610   7457    341    -93    368       C  
ATOM   2151  CD1 TYR A 269       0.231  22.327  30.897  1.00 56.14           C  
ANISOU 2151  CD1 TYR A 269     7401   7042   6888    311   -190    357       C  
ATOM   2152  CD2 TYR A 269      -0.058  24.236  29.506  1.00 64.30           C  
ANISOU 2152  CD2 TYR A 269     8504   8034   7892    376    -66    359       C  
ATOM   2153  CE1 TYR A 269       0.795  21.623  29.845  1.00 53.16           C  
ANISOU 2153  CE1 TYR A 269     6995   6672   6531    318   -258    330       C  
ATOM   2154  CE2 TYR A 269       0.538  23.560  28.450  1.00 60.99           C  
ANISOU 2154  CE2 TYR A 269     8056   7632   7484    382   -135    334       C  
ATOM   2155  CZ  TYR A 269       0.956  22.249  28.614  1.00 60.31           C  
ANISOU 2155  CZ  TYR A 269     7921   7569   7424    353   -231    315       C  
ATOM   2156  OH  TYR A 269       1.494  21.599  27.535  1.00 60.78           O  
ANISOU 2156  OH  TYR A 269     7949   7646   7499    362   -296    284       O  
ATOM   2157  N   VAL A 270      -3.185  25.064  34.016  1.00 61.59           N  
ANISOU 2157  N   VAL A 270     8160   7719   7522    356     75    478       N  
ATOM   2158  CA  VAL A 270      -3.667  25.913  35.096  1.00 64.11           C  
ANISOU 2158  CA  VAL A 270     8503   8040   7818    348    156    477       C  
ATOM   2159  C   VAL A 270      -4.092  25.039  36.269  1.00 58.59           C  
ANISOU 2159  C   VAL A 270     7750   7397   7114    318    104    507       C  
ATOM   2160  O   VAL A 270      -4.081  25.491  37.411  1.00 67.57           O  
ANISOU 2160  O   VAL A 270     8895   8557   8223    285    153    488       O  
ATOM   2161  CB  VAL A 270      -4.778  26.899  34.679  1.00 67.94           C  
ANISOU 2161  CB  VAL A 270     9013   8492   8310    410    233    515       C  
ATOM   2162  CG1 VAL A 270      -4.357  27.918  33.621  1.00 69.76           C  
ANISOU 2162  CG1 VAL A 270     9293   8668   8547    438    297    492       C  
ATOM   2163  CG2 VAL A 270      -6.005  26.163  34.206  1.00 91.79           C  
ANISOU 2163  CG2 VAL A 270    11987  11534  11354    460    178    592       C  
ATOM   2164  N   ALA A 271      -4.439  23.778  35.989  1.00 62.66           N  
ANISOU 2164  N   ALA A 271     8208   7940   7661    325      5    553       N  
ATOM   2165  CA  ALA A 271      -4.768  22.831  37.052  1.00 60.69           C  
ANISOU 2165  CA  ALA A 271     7898   7745   7415    294    -56    591       C  
ATOM   2166  C   ALA A 271      -3.503  22.314  37.755  1.00 60.38           C  
ANISOU 2166  C   ALA A 271     7842   7734   7366    223    -92    548       C  
ATOM   2167  O   ALA A 271      -3.571  21.878  38.912  1.00 60.13           O  
ANISOU 2167  O   ALA A 271     7768   7756   7322    183   -112    568       O  
ATOM   2168  CB  ALA A 271      -5.669  21.728  36.540  1.00 43.01           C  
ANISOU 2168  CB  ALA A 271     5601   5520   5221    329   -145    659       C  
ATOM   2169  N   ILE A 272      -2.345  22.399  37.071  1.00 50.78           N  
ANISOU 2169  N   ILE A 272     6656   6487   6150    206    -96    492       N  
ATOM   2170  CA  ILE A 272      -1.082  21.952  37.646  1.00 49.08           C  
ANISOU 2170  CA  ILE A 272     6428   6296   5923    140   -126    451       C  
ATOM   2171  C   ILE A 272      -0.423  23.100  38.403  1.00 55.44           C  
ANISOU 2171  C   ILE A 272     7287   7105   6674    101    -30    392       C  
ATOM   2172  O   ILE A 272      -0.025  22.919  39.553  1.00 61.66           O  
ANISOU 2172  O   ILE A 272     8050   7944   7435     45    -30    384       O  
ATOM   2173  CB  ILE A 272      -0.140  21.364  36.585  1.00 46.57           C  
ANISOU 2173  CB  ILE A 272     6110   5952   5633    138   -186    420       C  
ATOM   2174  CG1 ILE A 272      -0.655  20.024  36.050  1.00 45.40           C  
ANISOU 2174  CG1 ILE A 272     5895   5811   5546    162   -292    469       C  
ATOM   2175  CG2 ILE A 272       1.248  21.217  37.173  1.00 42.94           C  
ANISOU 2175  CG2 ILE A 272     5653   5512   5149     71   -193    371       C  
ATOM   2176  CD1 ILE A 272       0.107  19.474  34.871  1.00 44.63           C  
ANISOU 2176  CD1 ILE A 272     5792   5686   5479    171   -349    434       C  
ATOM   2177  N   GLY A 273      -0.320  24.269  37.752  1.00 55.28           N  
ANISOU 2177  N   GLY A 273     7333   7032   6639    128     50    354       N  
ATOM   2178  CA  GLY A 273       0.263  25.452  38.360  1.00 49.19           C  
ANISOU 2178  CA  GLY A 273     6614   6251   5823     95    147    292       C  
ATOM   2179  C   GLY A 273      -0.471  25.940  39.611  1.00 52.28           C  
ANISOU 2179  C   GLY A 273     6996   6681   6189     82    205    299       C  
ATOM   2180  O   GLY A 273       0.165  26.249  40.599  1.00 61.38           O  
ANISOU 2180  O   GLY A 273     8151   7868   7301     25    241    254       O  
ATOM   2181  N   TRP A 274      -1.804  26.030  39.595  1.00 54.69           N  
ANISOU 2181  N   TRP A 274     7285   6984   6509    133    215    354       N  
ATOM   2182  CA  TRP A 274      -2.542  26.564  40.738  1.00 51.21           C  
ANISOU 2182  CA  TRP A 274     6836   6581   6042    126    274    356       C  
ATOM   2183  C   TRP A 274      -3.287  25.475  41.500  1.00 54.28           C  
ANISOU 2183  C   TRP A 274     7146   7043   6433    118    200    425       C  
ATOM   2184  O   TRP A 274      -3.581  25.648  42.690  1.00 45.10           O  
ANISOU 2184  O   TRP A 274     5957   5942   5237     88    229    422       O  
ATOM   2185  CB  TRP A 274      -3.533  27.629  40.290  1.00 50.22           C  
ANISOU 2185  CB  TRP A 274     6750   6402   5928    189    356    366       C  
ATOM   2186  CG  TRP A 274      -2.901  28.797  39.602  1.00 61.62           C  
ANISOU 2186  CG  TRP A 274     8264   7771   7376    199    437    308       C  
ATOM   2187  CD1 TRP A 274      -3.010  29.144  38.285  1.00 62.61           C  
ANISOU 2187  CD1 TRP A 274     8422   7832   7534    252    447    325       C  
ATOM   2188  CD2 TRP A 274      -2.077  29.801  40.214  1.00 59.72           C  
ANISOU 2188  CD2 TRP A 274     8066   7516   7107    154    522    225       C  
ATOM   2189  NE1 TRP A 274      -2.325  30.305  38.042  1.00 69.52           N  
ANISOU 2189  NE1 TRP A 274     9356   8652   8407    244    531    265       N  
ATOM   2190  CE2 TRP A 274      -1.746  30.731  39.207  1.00 61.04           C  
ANISOU 2190  CE2 TRP A 274     8292   7603   7298    184    579    200       C  
ATOM   2191  CE3 TRP A 274      -1.622  30.014  41.514  1.00 59.85           C  
ANISOU 2191  CE3 TRP A 274     8072   7586   7081     91    556    171       C  
ATOM   2192  CZ2 TRP A 274      -0.958  31.848  39.453  1.00 65.93           C  
ANISOU 2192  CZ2 TRP A 274     8962   8184   7906    153    667    123       C  
ATOM   2193  CZ3 TRP A 274      -0.838  31.117  41.762  1.00 70.10           C  
ANISOU 2193  CZ3 TRP A 274     9421   8850   8362     58    644     88       C  
ATOM   2194  CH2 TRP A 274      -0.512  32.019  40.745  1.00 73.85           C  
ANISOU 2194  CH2 TRP A 274     9956   9235   8867     89    698     64       C  
ATOM   2195  N   GLY A 275      -3.582  24.358  40.806  1.00 54.99           N  
ANISOU 2195  N   GLY A 275     7197   7132   6565    143    103    484       N  
ATOM   2196  CA  GLY A 275      -4.399  23.291  41.371  1.00 61.87           C  
ANISOU 2196  CA  GLY A 275     7992   8063   7453    143     27    560       C  
ATOM   2197  C   GLY A 275      -3.629  22.338  42.282  1.00 64.51           C  
ANISOU 2197  C   GLY A 275     8266   8465   7780     74    -39    566       C  
ATOM   2198  O   GLY A 275      -4.022  22.100  43.427  1.00 68.73           O  
ANISOU 2198  O   GLY A 275     8749   9074   8292     46    -45    597       O  
ATOM   2199  N   VAL A 276      -2.518  21.808  41.763  1.00 62.63           N  
ANISOU 2199  N   VAL A 276     8030   8205   7561     48    -86    538       N  
ATOM   2200  CA  VAL A 276      -1.737  20.832  42.506  1.00 59.67           C  
ANISOU 2200  CA  VAL A 276     7593   7888   7190    -15   -153    551       C  
ATOM   2201  C   VAL A 276      -1.133  21.422  43.787  1.00 60.28           C  
ANISOU 2201  C   VAL A 276     7670   8031   7203    -79    -92    509       C  
ATOM   2202  O   VAL A 276      -1.158  20.742  44.810  1.00 63.29           O  
ANISOU 2202  O   VAL A 276     7979   8493   7577   -122   -132    551       O  
ATOM   2203  CB  VAL A 276      -0.687  20.155  41.615  1.00 62.56           C  
ANISOU 2203  CB  VAL A 276     7963   8214   7594    -25   -216    527       C  
ATOM   2204  CG1 VAL A 276       0.284  19.278  42.395  1.00 55.65           C  
ANISOU 2204  CG1 VAL A 276     7029   7394   6721    -93   -272    534       C  
ATOM   2205  CG2 VAL A 276      -1.362  19.404  40.480  1.00 65.06           C  
ANISOU 2205  CG2 VAL A 276     8260   8484   7975     33   -287    571       C  
ATOM   2206  N   PRO A 277      -0.580  22.658  43.831  1.00 57.83           N  
ANISOU 2206  N   PRO A 277     7431   7696   6847    -92      6    428       N  
ATOM   2207  CA  PRO A 277      -0.157  23.237  45.110  1.00 61.73           C  
ANISOU 2207  CA  PRO A 277     7917   8261   7278   -153     69    385       C  
ATOM   2208  C   PRO A 277      -1.242  23.190  46.191  1.00 65.37           C  
ANISOU 2208  C   PRO A 277     8320   8801   7717   -154     77    433       C  
ATOM   2209  O   PRO A 277      -0.972  22.913  47.367  1.00 60.67           O  
ANISOU 2209  O   PRO A 277     7666   8302   7083   -212     71    439       O  
ATOM   2210  CB  PRO A 277       0.158  24.693  44.761  1.00 53.40           C  
ANISOU 2210  CB  PRO A 277     6951   7143   6195   -142    178    299       C  
ATOM   2211  CG  PRO A 277       0.591  24.604  43.336  1.00 61.16           C  
ANISOU 2211  CG  PRO A 277     7982   8038   7219   -104    151    291       C  
ATOM   2212  CD  PRO A 277      -0.269  23.534  42.693  1.00 53.00           C  
ANISOU 2212  CD  PRO A 277     6902   6994   6242    -55     60    374       C  
ATOM   2213  N   LEU A 278      -2.475  23.492  45.791  1.00 65.89           N  
ANISOU 2213  N   LEU A 278     8401   8833   7803    -88     95    467       N  
ATOM   2214  CA  LEU A 278      -3.581  23.502  46.736  1.00 68.67           C  
ANISOU 2214  CA  LEU A 278     8701   9257   8132    -81    105    512       C  
ATOM   2215  C   LEU A 278      -3.764  22.116  47.344  1.00 67.61           C  
ANISOU 2215  C   LEU A 278     8467   9205   8016   -110      0    599       C  
ATOM   2216  O   LEU A 278      -4.366  21.973  48.403  1.00 72.17           O  
ANISOU 2216  O   LEU A 278     8982   9875   8563   -129     -2    637       O  
ATOM   2217  CB  LEU A 278      -4.842  23.904  45.972  1.00 64.81           C  
ANISOU 2217  CB  LEU A 278     8246   8707   7673      0    127    545       C  
ATOM   2218  CG  LEU A 278      -5.855  24.801  46.681  1.00 58.49           C  
ANISOU 2218  CG  LEU A 278     7449   7938   6836     22    206    538       C  
ATOM   2219  CD1 LEU A 278      -5.234  25.825  47.635  1.00 55.22           C  
ANISOU 2219  CD1 LEU A 278     7055   7561   6363    -29    302    445       C  
ATOM   2220  CD2 LEU A 278      -6.629  25.553  45.615  1.00 57.13           C  
ANISOU 2220  CD2 LEU A 278     7342   7670   6695    100    256    539       C  
ATOM   2221  N   LEU A 279      -3.243  21.097  46.668  1.00 69.51           N  
ANISOU 2221  N   LEU A 279     8687   9413   8309   -112    -88    632       N  
ATOM   2222  CA  LEU A 279      -3.544  19.724  47.032  1.00 63.55           C  
ANISOU 2222  CA  LEU A 279     7837   8715   7595   -126   -195    725       C  
ATOM   2223  C   LEU A 279      -2.645  19.263  48.170  1.00 55.78           C  
ANISOU 2223  C   LEU A 279     6787   7827   6581   -208   -216    729       C  
ATOM   2224  O   LEU A 279      -2.987  18.328  48.872  1.00 56.54           O  
ANISOU 2224  O   LEU A 279     6791   7999   6694   -230   -285    811       O  
ATOM   2225  CB  LEU A 279      -3.337  18.886  45.774  1.00 67.65           C  
ANISOU 2225  CB  LEU A 279     8362   9150   8190    -93   -274    747       C  
ATOM   2226  CG  LEU A 279      -3.908  17.485  45.738  1.00 70.47           C  
ANISOU 2226  CG  LEU A 279     8632   9526   8615    -84   -387    845       C  
ATOM   2227  CD1 LEU A 279      -4.111  17.141  44.279  1.00 59.01           C  
ANISOU 2227  CD1 LEU A 279     7215   7978   7227    -27   -428    844       C  
ATOM   2228  CD2 LEU A 279      -2.906  16.532  46.382  1.00 81.06           C  
ANISOU 2228  CD2 LEU A 279     9903  10921   9976   -151   -452    867       C  
ATOM   2229  N   PHE A 280      -1.479  19.885  48.334  1.00 64.48           N  
ANISOU 2229  N   PHE A 280     7931   8929   7639   -253   -160    647       N  
ATOM   2230  CA  PHE A 280      -0.604  19.495  49.433  1.00 60.42           C  
ANISOU 2230  CA  PHE A 280     7352   8516   7089   -333   -174    651       C  
ATOM   2231  C   PHE A 280      -0.380  20.613  50.437  1.00 56.38           C  
ANISOU 2231  C   PHE A 280     6859   8077   6489   -377    -72    579       C  
ATOM   2232  O   PHE A 280      -0.013  20.303  51.559  1.00 51.09           O  
ANISOU 2232  O   PHE A 280     6114   7521   5778   -440    -81    598       O  
ATOM   2233  CB  PHE A 280       0.731  18.936  48.946  1.00 60.20           C  
ANISOU 2233  CB  PHE A 280     7332   8453   7088   -367   -217    629       C  
ATOM   2234  CG  PHE A 280       1.570  19.824  48.072  1.00 65.88           C  
ANISOU 2234  CG  PHE A 280     8154   9084   7791   -358   -155    531       C  
ATOM   2235  CD1 PHE A 280       2.499  20.708  48.606  1.00 74.16           C  
ANISOU 2235  CD1 PHE A 280     9242  10165   8771   -410    -75    449       C  
ATOM   2236  CD2 PHE A 280       1.478  19.728  46.682  1.00 76.65           C  
ANISOU 2236  CD2 PHE A 280     9574  10338   9212   -298   -181    523       C  
ATOM   2237  CE1 PHE A 280       3.302  21.479  47.764  1.00 69.11           C  
ANISOU 2237  CE1 PHE A 280     8695   9442   8123   -402    -24    365       C  
ATOM   2238  CE2 PHE A 280       2.255  20.513  45.833  1.00 64.54           C  
ANISOU 2238  CE2 PHE A 280     8130   8728   7666   -288   -129    440       C  
ATOM   2239  CZ  PHE A 280       3.167  21.394  46.384  1.00 64.48           C  
ANISOU 2239  CZ  PHE A 280     8161   8748   7592   -340    -51    364       C  
ATOM   2240  N   VAL A 281      -0.635  21.865  50.043  1.00 57.39           N  
ANISOU 2240  N   VAL A 281     7075   8141   6590   -342     22    501       N  
ATOM   2241  CA  VAL A 281      -0.456  22.986  50.948  1.00 60.72           C  
ANISOU 2241  CA  VAL A 281     7515   8620   6936   -380    125    421       C  
ATOM   2242  C   VAL A 281      -1.534  23.004  52.030  1.00 72.75           C  
ANISOU 2242  C   VAL A 281     8967  10249   8424   -382    135    463       C  
ATOM   2243  O   VAL A 281      -1.200  23.239  53.197  1.00 94.63           O  
ANISOU 2243  O   VAL A 281    11690  13134  11130   -445    171    434       O  
ATOM   2244  CB  VAL A 281      -0.345  24.332  50.215  1.00 59.08           C  
ANISOU 2244  CB  VAL A 281     7419   8307   6722   -345    224    325       C  
ATOM   2245  CG1 VAL A 281      -0.467  25.504  51.187  1.00 60.47           C  
ANISOU 2245  CG1 VAL A 281     7606   8539   6831   -374    332    245       C  
ATOM   2246  CG2 VAL A 281       0.968  24.415  49.448  1.00 64.41           C  
ANISOU 2246  CG2 VAL A 281     8152   8912   7408   -366    224    272       C  
ATOM   2247  N   VAL A 282      -2.804  22.760  51.667  1.00 63.49           N  
ANISOU 2247  N   VAL A 282     7785   9049   7290   -317    105    530       N  
ATOM   2248  CA  VAL A 282      -3.868  22.916  52.652  1.00 58.44           C  
ANISOU 2248  CA  VAL A 282     7086   8507   6611   -313    124    563       C  
ATOM   2249  C   VAL A 282      -3.815  21.819  53.705  1.00 56.65           C  
ANISOU 2249  C   VAL A 282     6737   8420   6369   -369     45    647       C  
ATOM   2250  O   VAL A 282      -4.062  22.116  54.870  1.00 68.29           O  
ANISOU 2250  O   VAL A 282     8153  10016   7779   -407     81    638       O  
ATOM   2251  CB  VAL A 282      -5.296  23.130  52.115  1.00 57.67           C  
ANISOU 2251  CB  VAL A 282     7011   8354   6545   -230    129    605       C  
ATOM   2252  CG1 VAL A 282      -5.340  24.173  51.007  1.00 64.83           C  
ANISOU 2252  CG1 VAL A 282     8032   9124   7476   -174    203    535       C  
ATOM   2253  CG2 VAL A 282      -6.016  21.841  51.739  1.00 55.00           C  
ANISOU 2253  CG2 VAL A 282     6614   8017   6268   -197     14    728       C  
ATOM   2254  N   PRO A 283      -3.508  20.540  53.389  1.00 51.43           N  
ANISOU 2254  N   PRO A 283     6024   7753   5766   -378    -62    732       N  
ATOM   2255  CA  PRO A 283      -3.365  19.548  54.454  1.00 55.82           C  
ANISOU 2255  CA  PRO A 283     6456   8445   6310   -437   -131    815       C  
ATOM   2256  C   PRO A 283      -2.152  19.809  55.356  1.00 70.42           C  
ANISOU 2256  C   PRO A 283     8277  10389   8092   -524    -91    757       C  
ATOM   2257  O   PRO A 283      -2.205  19.462  56.542  1.00 80.03           O  
ANISOU 2257  O   PRO A 283     9391  11754   9264   -577   -106    803       O  
ATOM   2258  CB  PRO A 283      -3.396  18.177  53.771  1.00 47.43           C  
ANISOU 2258  CB  PRO A 283     5351   7330   5342   -417   -251    915       C  
ATOM   2259  CG  PRO A 283      -3.732  18.507  52.314  1.00 53.77           C  
ANISOU 2259  CG  PRO A 283     6257   7975   6198   -340   -241    881       C  
ATOM   2260  CD  PRO A 283      -3.309  19.954  52.055  1.00 55.35           C  
ANISOU 2260  CD  PRO A 283     6565   8121   6344   -334   -123    755       C  
ATOM   2261  N   TRP A 284      -1.094  20.455  54.814  1.00 73.08           N  
ANISOU 2261  N   TRP A 284     8701  10649   8417   -539    -36    659       N  
ATOM   2262  CA  TRP A 284       0.036  20.913  55.616  1.00 64.20           C  
ANISOU 2262  CA  TRP A 284     7565   9608   7220   -619     20    587       C  
ATOM   2263  C   TRP A 284      -0.415  21.970  56.613  1.00 67.70           C  
ANISOU 2263  C   TRP A 284     8000  10145   7578   -640    115    520       C  
ATOM   2264  O   TRP A 284      -0.058  21.900  57.793  1.00 68.03           O  
ANISOU 2264  O   TRP A 284     7959  10335   7553   -711    127    519       O  
ATOM   2265  CB  TRP A 284       1.172  21.460  54.764  1.00 63.41           C  
ANISOU 2265  CB  TRP A 284     7567   9399   7126   -624     61    495       C  
ATOM   2266  CG  TRP A 284       2.193  22.199  55.576  1.00 67.76           C  
ANISOU 2266  CG  TRP A 284     8123  10030   7594   -701    139    403       C  
ATOM   2267  CD1 TRP A 284       3.229  21.664  56.286  1.00 66.78           C  
ANISOU 2267  CD1 TRP A 284     7931  10006   7434   -780    113    419       C  
ATOM   2268  CD2 TRP A 284       2.274  23.623  55.770  1.00 67.94           C  
ANISOU 2268  CD2 TRP A 284     8218  10038   7559   -707    258    280       C  
ATOM   2269  NE1 TRP A 284       3.945  22.654  56.904  1.00 68.79           N  
ANISOU 2269  NE1 TRP A 284     8212  10317   7608   -837    208    312       N  
ATOM   2270  CE2 TRP A 284       3.384  23.868  56.605  1.00 65.43           C  
ANISOU 2270  CE2 TRP A 284     7872   9818   7169   -794    297    223       C  
ATOM   2271  CE3 TRP A 284       1.515  24.712  55.333  1.00 73.23           C  
ANISOU 2271  CE3 TRP A 284     8968  10622   8234   -649    335    215       C  
ATOM   2272  CZ2 TRP A 284       3.751  25.156  56.998  1.00 61.83           C  
ANISOU 2272  CZ2 TRP A 284     7469   9373   6650   -825    410     96       C  
ATOM   2273  CZ3 TRP A 284       1.887  25.985  55.717  1.00 71.29           C  
ANISOU 2273  CZ3 TRP A 284     8773  10380   7933   -678    447     93       C  
ATOM   2274  CH2 TRP A 284       2.986  26.202  56.547  1.00 57.49           C  
ANISOU 2274  CH2 TRP A 284     6997   8729   6116   -766    484     31       C  
ATOM   2275  N   GLY A 285      -1.214  22.924  56.115  1.00 66.54           N  
ANISOU 2275  N   GLY A 285     7933   9912   7436   -577    182    464       N  
ATOM   2276  CA  GLY A 285      -1.759  23.993  56.935  1.00 74.19           C  
ANISOU 2276  CA  GLY A 285     8902  10949   8337   -585    277    392       C  
ATOM   2277  C   GLY A 285      -2.633  23.453  58.069  1.00 73.32           C  
ANISOU 2277  C   GLY A 285     8671  10997   8191   -602    240    472       C  
ATOM   2278  O   GLY A 285      -2.603  23.972  59.188  1.00 76.00           O  
ANISOU 2278  O   GLY A 285     8959  11466   8451   -653    297    421       O  
ATOM   2279  N   ILE A 286      -3.413  22.406  57.767  1.00 69.31           N  
ANISOU 2279  N   ILE A 286     8113  10482   7740   -562    142    596       N  
ATOM   2280  CA  ILE A 286      -4.388  21.882  58.710  1.00 69.64           C  
ANISOU 2280  CA  ILE A 286     8043  10661   7757   -567    100    685       C  
ATOM   2281  C   ILE A 286      -3.671  21.127  59.830  1.00 77.55           C  
ANISOU 2281  C   ILE A 286     8922  11829   8714   -655     55    736       C  
ATOM   2282  O   ILE A 286      -3.997  21.324  61.002  1.00 75.71           O  
ANISOU 2282  O   ILE A 286     8605  11754   8407   -695     81    736       O  
ATOM   2283  CB  ILE A 286      -5.480  21.073  57.978  1.00 65.43           C  
ANISOU 2283  CB  ILE A 286     7501  10058   7302   -493     15    799       C  
ATOM   2284  CG1 ILE A 286      -6.432  22.025  57.236  1.00 63.86           C  
ANISOU 2284  CG1 ILE A 286     7400   9746   7117   -411     81    749       C  
ATOM   2285  CG2 ILE A 286      -6.216  20.134  58.924  1.00 59.86           C  
ANISOU 2285  CG2 ILE A 286     6658   9500   6584   -512    -63    922       C  
ATOM   2286  CD1 ILE A 286      -7.306  21.373  56.203  1.00 57.71           C  
ANISOU 2286  CD1 ILE A 286     6642   8865   6420   -335      9    838       C  
ATOM   2287  N   VAL A 287      -2.666  20.310  59.485  1.00 75.04           N  
ANISOU 2287  N   VAL A 287     8592  11481   8438   -688     -8    775       N  
ATOM   2288  CA  VAL A 287      -1.960  19.566  60.520  1.00 74.17           C  
ANISOU 2288  CA  VAL A 287     8360  11528   8292   -772    -52    833       C  
ATOM   2289  C   VAL A 287      -1.110  20.514  61.351  1.00 72.07           C  
ANISOU 2289  C   VAL A 287     8098  11359   7925   -844     46    717       C  
ATOM   2290  O   VAL A 287      -0.950  20.279  62.537  1.00 72.75           O  
ANISOU 2290  O   VAL A 287     8071  11624   7946   -910     43    747       O  
ATOM   2291  CB  VAL A 287      -1.107  18.418  59.961  1.00 75.83           C  
ANISOU 2291  CB  VAL A 287     8550  11683   8580   -788   -144    908       C  
ATOM   2292  CG1 VAL A 287      -1.993  17.353  59.347  1.00 69.90           C  
ANISOU 2292  CG1 VAL A 287     7765  10865   7927   -728   -249   1032       C  
ATOM   2293  CG2 VAL A 287      -0.093  18.922  58.941  1.00 75.36           C  
ANISOU 2293  CG2 VAL A 287     8614  11477   8542   -779   -104    809       C  
ATOM   2294  N   LYS A 288      -0.561  21.560  60.726  1.00 75.46           N  
ANISOU 2294  N   LYS A 288     8652  11676   8345   -832    132    587       N  
ATOM   2295  CA  LYS A 288       0.264  22.520  61.451  1.00 86.72           C  
ANISOU 2295  CA  LYS A 288    10088  13180   9679   -899    230    465       C  
ATOM   2296  C   LYS A 288      -0.616  23.471  62.254  1.00 83.39           C  
ANISOU 2296  C   LYS A 288     9649  12846   9190   -895    312    398       C  
ATOM   2297  O   LYS A 288      -0.109  24.376  62.888  1.00119.29           O  
ANISOU 2297  O   LYS A 288    14204  17459  13661   -946    402    284       O  
ATOM   2298  CB  LYS A 288       1.182  23.334  60.517  1.00 87.81           C  
ANISOU 2298  CB  LYS A 288    10362  13167   9834   -890    294    349       C  
ATOM   2299  CG  LYS A 288       2.356  22.587  59.893  1.00 78.50           C  
ANISOU 2299  CG  LYS A 288     9200  11927   8698   -915    233    383       C  
ATOM   2300  CD  LYS A 288       3.388  22.114  60.894  1.00 80.42           C  
ANISOU 2300  CD  LYS A 288     9347  12328   8880  -1012    219    402       C  
ATOM   2301  CE  LYS A 288       4.189  23.293  61.388  1.00 88.54           C  
ANISOU 2301  CE  LYS A 288    10420  13401   9822  -1070    331    259       C  
ATOM   2302  NZ  LYS A 288       5.194  22.984  62.432  1.00 95.98           N  
ANISOU 2302  NZ  LYS A 288    11268  14512  10689  -1171    332    265       N  
ATOM   2303  N   TYR A 289      -1.936  23.297  62.221  1.00 90.15           N  
ANISOU 2303  N   TYR A 289    10481  13701  10071   -834    284    462       N  
ATOM   2304  CA  TYR A 289      -2.817  24.148  63.016  1.00 91.19           C  
ANISOU 2304  CA  TYR A 289    10587  13923  10137   -828    357    403       C  
ATOM   2305  C   TYR A 289      -3.450  23.352  64.147  1.00 82.56           C  
ANISOU 2305  C   TYR A 289     9341  13028   9002   -860    296    511       C  
ATOM   2306  O   TYR A 289      -3.680  23.895  65.223  1.00 83.49           O  
ANISOU 2306  O   TYR A 289     9392  13297   9032   -900    353    457       O  
ATOM   2307  CB  TYR A 289      -3.931  24.741  62.159  1.00 93.35           C  
ANISOU 2307  CB  TYR A 289    10954  14052  10464   -730    388    384       C  
ATOM   2308  CG  TYR A 289      -4.942  25.601  62.875  1.00 83.90           C  
ANISOU 2308  CG  TYR A 289     9736  12931   9213   -711    461    327       C  
ATOM   2309  CD1 TYR A 289      -4.625  26.879  63.311  1.00 79.73           C  
ANISOU 2309  CD1 TYR A 289     9248  12419   8628   -739    581    174       C  
ATOM   2310  CD2 TYR A 289      -6.235  25.139  63.072  1.00 84.83           C  
ANISOU 2310  CD2 TYR A 289     9793  13099   9340   -664    411    425       C  
ATOM   2311  CE1 TYR A 289      -5.566  27.687  63.927  1.00 81.07           C  
ANISOU 2311  CE1 TYR A 289     9398  12649   8755   -718    651    114       C  
ATOM   2312  CE2 TYR A 289      -7.193  25.938  63.674  1.00 87.75           C  
ANISOU 2312  CE2 TYR A 289    10147  13533   9662   -641    479    372       C  
ATOM   2313  CZ  TYR A 289      -6.857  27.217  64.095  1.00 88.96           C  
ANISOU 2313  CZ  TYR A 289    10341  13698   9763   -667    600    214       C  
ATOM   2314  OH  TYR A 289      -7.794  28.005  64.695  1.00 86.02           O  
ANISOU 2314  OH  TYR A 289     9947  13388   9347   -643    668    155       O  
ATOM   2315  N   LEU A 290      -3.725  22.073  63.872  1.00 70.51           N  
ANISOU 2315  N   LEU A 290     7755  11497   7538   -842    179    661       N  
ATOM   2316  CA  LEU A 290      -4.266  21.185  64.878  1.00 71.19           C  
ANISOU 2316  CA  LEU A 290     7687  11765   7595   -873    107    785       C  
ATOM   2317  C   LEU A 290      -3.157  20.579  65.736  1.00 70.20           C  
ANISOU 2317  C   LEU A 290     7456  11792   7426   -971     78    820       C  
ATOM   2318  O   LEU A 290      -3.371  20.376  66.925  1.00 81.22           O  
ANISOU 2318  O   LEU A 290     8722  13390   8750  -1024     70    862       O  
ATOM   2319  CB  LEU A 290      -5.135  20.118  64.205  1.00 66.49           C  
ANISOU 2319  CB  LEU A 290     7074  11094   7096   -808     -3    930       C  
ATOM   2320  CG  LEU A 290      -6.326  20.617  63.380  1.00 61.00           C  
ANISOU 2320  CG  LEU A 290     6471  10265   6443   -711     19    914       C  
ATOM   2321  CD1 LEU A 290      -7.053  19.463  62.707  1.00 54.91           C  
ANISOU 2321  CD1 LEU A 290     5674   9423   5766   -657    -96   1060       C  
ATOM   2322  CD2 LEU A 290      -7.297  21.484  64.174  1.00 57.64           C  
ANISOU 2322  CD2 LEU A 290     6019   9942   5939   -698     90    862       C  
ATOM   2323  N   TYR A 291      -1.971  20.305  65.165  1.00 86.21           N  
ANISOU 2323  N   TYR A 291     9531  13733   9491   -998     63    806       N  
ATOM   2324  CA  TYR A 291      -1.001  19.431  65.830  1.00100.40           C  
ANISOU 2324  CA  TYR A 291    11217  15658  11270  -1080      9    881       C  
ATOM   2325  C   TYR A 291       0.404  20.016  65.985  1.00 91.28           C  
ANISOU 2325  C   TYR A 291    10103  14519  10059  -1149     79    769       C  
ATOM   2326  O   TYR A 291       1.246  19.371  66.596  1.00 99.56           O  
ANISOU 2326  O   TYR A 291    11058  15687  11084  -1222     44    826       O  
ATOM   2327  CB  TYR A 291      -0.900  18.056  65.162  1.00100.88           C  
ANISOU 2327  CB  TYR A 291    11247  15638  11443  -1057   -114   1026       C  
ATOM   2328  CG  TYR A 291      -2.206  17.311  65.074  1.00 96.89           C  
ANISOU 2328  CG  TYR A 291    10684  15131  10998   -999   -196   1153       C  
ATOM   2329  CD1 TYR A 291      -2.715  16.595  66.146  1.00 93.80           C  
ANISOU 2329  CD1 TYR A 291    10134  14927  10580  -1035   -253   1274       C  
ATOM   2330  CD2 TYR A 291      -2.950  17.357  63.908  1.00103.55           C  
ANISOU 2330  CD2 TYR A 291    11631  15790  11922   -908   -214   1151       C  
ATOM   2331  CE1 TYR A 291      -3.934  15.950  66.056  1.00106.77           C  
ANISOU 2331  CE1 TYR A 291    11726  16566  12276   -982   -327   1390       C  
ATOM   2332  CE2 TYR A 291      -4.153  16.685  63.792  1.00106.05           C  
ANISOU 2332  CE2 TYR A 291    11898  16102  12293   -855   -288   1266       C  
ATOM   2333  CZ  TYR A 291      -4.658  15.995  64.877  1.00112.07           C  
ANISOU 2333  CZ  TYR A 291    12506  17046  13028   -892   -344   1384       C  
ATOM   2334  OH  TYR A 291      -5.857  15.349  64.773  1.00115.18           O  
ANISOU 2334  OH  TYR A 291    12851  17438  13475   -841   -418   1498       O  
ATOM   2335  N   GLU A 292       0.676  21.179  65.396  1.00 98.75           N  
ANISOU 2335  N   GLU A 292    11186  15342  10991  -1126    173    620       N  
ATOM   2336  CA  GLU A 292       1.941  21.862  65.617  1.00107.50           C  
ANISOU 2336  CA  GLU A 292    12334  16474  12038  -1193    250    503       C  
ATOM   2337  C   GLU A 292       1.755  23.366  65.427  1.00113.04           C  
ANISOU 2337  C   GLU A 292    13149  17102  12701  -1170    372    334       C  
ATOM   2338  O   GLU A 292       2.127  23.910  64.380  1.00114.34           O  
ANISOU 2338  O   GLU A 292    13446  17084  12913  -1130    406    260       O  
ATOM   2339  CB  GLU A 292       3.010  21.375  64.635  1.00107.72           C  
ANISOU 2339  CB  GLU A 292    12432  16363  12134  -1192    208    519       C  
ATOM   2340  CG  GLU A 292       3.775  20.133  65.092  1.00117.32           C  
ANISOU 2340  CG  GLU A 292    13530  17685  13359  -1254    121    642       C  
ATOM   2341  CD  GLU A 292       4.996  19.858  64.226  1.00116.34           C  
ANISOU 2341  CD  GLU A 292    13480  17438  13284  -1263    101    627       C  
ATOM   2342  OE1 GLU A 292       5.639  20.846  63.857  1.00106.86           O  
ANISOU 2342  OE1 GLU A 292    12387  16163  12050  -1270    184    494       O  
ATOM   2343  OE2 GLU A 292       5.296  18.683  63.905  1.00122.30           O1-
ANISOU 2343  OE2 GLU A 292    14186  18167  14113  -1261      4    744       O1-
ATOM   2344  N   ASP A 293       1.194  24.031  66.446  1.00101.00           N  
ANISOU 2344  N   ASP A 293    11563  15719  11092  -1195    436    275       N  
ATOM   2345  CA  ASP A 293       0.868  25.441  66.304  1.00114.83           C  
ANISOU 2345  CA  ASP A 293    13412  17397  12820  -1167    551    119       C  
ATOM   2346  C   ASP A 293       1.682  26.259  67.301  1.00128.67           C  
ANISOU 2346  C   ASP A 293    15131  19290  14467  -1258    645    -11       C  
ATOM   2347  O   ASP A 293       1.328  26.329  68.479  1.00156.74           O  
ANISOU 2347  O   ASP A 293    18572  23043  17940  -1306    665    -18       O  
ATOM   2348  CB  ASP A 293      -0.638  25.662  66.471  1.00122.21           C  
ANISOU 2348  CB  ASP A 293    14327  18346  13762  -1102    556    141       C  
ATOM   2349  CG  ASP A 293      -1.133  27.069  66.173  1.00118.24           C  
ANISOU 2349  CG  ASP A 293    13930  17738  13259  -1055    668     -5       C  
ATOM   2350  OD1 ASP A 293      -0.875  27.560  65.068  1.00116.22           O  
ANISOU 2350  OD1 ASP A 293    13805  17285  13068  -1007    698    -58       O  
ATOM   2351  OD2 ASP A 293      -1.795  27.660  67.052  1.00124.79           O1-
ANISOU 2351  OD2 ASP A 293    14704  18686  14025  -1066    726    -63       O1-
ATOM   2352  N   GLU A 294       2.777  26.871  66.832  1.00111.05           N  
ANISOU 2352  N   GLU A 294    12994  16963  12235  -1285    702   -114       N  
ATOM   2353  CA  GLU A 294       3.639  27.610  67.745  1.00111.46           C  
ANISOU 2353  CA  GLU A 294    13015  17147  12188  -1377    790   -239       C  
ATOM   2354  C   GLU A 294       4.524  28.583  66.967  1.00119.07           C  
ANISOU 2354  C   GLU A 294    14121  17946  13173  -1377    869   -373       C  
ATOM   2355  O   GLU A 294       5.534  28.194  66.374  1.00115.17           O  
ANISOU 2355  O   GLU A 294    13672  17380  12706  -1395    835   -348       O  
ATOM   2356  CB  GLU A 294       4.411  26.649  68.653  1.00 93.22           C  
ANISOU 2356  CB  GLU A 294    10567  15039   9813  -1469    732   -150       C  
ATOM   2357  N   GLY A 295       4.107  29.856  66.968  1.00118.94           N  
ANISOU 2357  N   GLY A 295    14172  17869  13150  -1353    973   -514       N  
ATOM   2358  CA  GLY A 295       4.829  30.927  66.294  1.00116.02           C  
ANISOU 2358  CA  GLY A 295    13933  17344  12804  -1351   1059   -650       C  
ATOM   2359  C   GLY A 295       4.779  30.817  64.768  1.00118.07           C  
ANISOU 2359  C   GLY A 295    14321  17364  13175  -1264   1021   -603       C  
ATOM   2360  O   GLY A 295       5.806  30.610  64.122  1.00114.76           O  
ANISOU 2360  O   GLY A 295    13960  16866  12779  -1281   1000   -597       O  
ATOM   2361  N   CYS A 296       3.574  30.999  64.204  1.00106.39           N  
ANISOU 2361  N   CYS A 296    12884  15778  11762  -1171   1017   -575       N  
ATOM   2362  CA  CYS A 296       3.275  30.921  62.777  1.00 90.17           C  
ANISOU 2362  CA  CYS A 296    10938  13510   9811  -1080    983   -526       C  
ATOM   2363  C   CYS A 296       3.863  29.657  62.181  1.00 86.08           C  
ANISOU 2363  C   CYS A 296    10409  12968   9329  -1081    870   -399       C  
ATOM   2364  O   CYS A 296       4.176  29.659  60.998  1.00102.05           O  
ANISOU 2364  O   CYS A 296    12528  14824  11421  -1034    852   -388       O  
ATOM   2365  CB  CYS A 296       3.783  32.108  61.966  1.00 86.95           C  
ANISOU 2365  CB  CYS A 296    10663  12930   9443  -1059   1072   -649       C  
ATOM   2366  SG  CYS A 296       3.484  33.723  62.736  1.00117.51           S  
ANISOU 2366  SG  CYS A 296    14549  16824  13274  -1081   1222   -832       S  
ATOM   2367  N   TRP A 297       3.967  28.601  63.001  1.00 87.96           N  
ANISOU 2367  N   TRP A 297    10524  13373   9523  -1132    796   -303       N  
ATOM   2368  CA  TRP A 297       4.427  27.287  62.580  1.00 97.49           C  
ANISOU 2368  CA  TRP A 297    11697  14575  10770  -1135    683   -171       C  
ATOM   2369  C   TRP A 297       5.865  27.361  62.063  1.00113.03           C  
ANISOU 2369  C   TRP A 297    13730  16478  12739  -1176    692   -216       C  
ATOM   2370  O   TRP A 297       6.220  26.670  61.107  1.00109.52           O  
ANISOU 2370  O   TRP A 297    13327  15926  12361  -1143    621   -147       O  
ATOM   2371  CB  TRP A 297       3.493  26.725  61.499  1.00114.67           C  
ANISOU 2371  CB  TRP A 297    13916  16607  13045  -1035    610    -73       C  
ATOM   2372  CG  TRP A 297       2.023  26.886  61.742  1.00118.04           C  
ANISOU 2372  CG  TRP A 297    14313  17053  13481   -977    616    -45       C  
ATOM   2373  CD1 TRP A 297       1.375  26.731  62.930  1.00124.85           C  
ANISOU 2373  CD1 TRP A 297    15063  18093  14282  -1008    616    -18       C  
ATOM   2374  CD2 TRP A 297       1.002  27.199  60.772  1.00114.81           C  
ANISOU 2374  CD2 TRP A 297    13986  16491  13147   -878    619    -33       C  
ATOM   2375  NE1 TRP A 297       0.029  26.936  62.767  1.00125.62           N  
ANISOU 2375  NE1 TRP A 297    15167  18152  14409   -935    619      6       N  
ATOM   2376  CE2 TRP A 297      -0.230  27.224  61.457  1.00108.20           C  
ANISOU 2376  CE2 TRP A 297    13080  15743  12286   -854    622     -1       C  
ATOM   2377  CE3 TRP A 297       0.993  27.480  59.400  1.00122.29           C  
ANISOU 2377  CE3 TRP A 297    15051  17241  14173   -808    622    -45       C  
ATOM   2378  CZ2 TRP A 297      -1.437  27.505  60.822  1.00104.29           C  
ANISOU 2378  CZ2 TRP A 297    12635  15146  11846   -764    628     21       C  
ATOM   2379  CZ3 TRP A 297      -0.204  27.766  58.772  1.00118.84           C  
ANISOU 2379  CZ3 TRP A 297    14659  16706  13789   -720    629    -22       C  
ATOM   2380  CH2 TRP A 297      -1.405  27.779  59.476  1.00104.84           C  
ANISOU 2380  CH2 TRP A 297    12820  15022  11993   -698    633     11       C  
ATOM   2381  N   THR A 298       6.690  28.233  62.665  1.00125.12           N  
ANISOU 2381  N   THR A 298    15273  18072  14196  -1247    781   -339       N  
ATOM   2382  CA  THR A 298       8.049  28.455  62.185  1.00107.22           C  
ANISOU 2382  CA  THR A 298    13074  15741  11922  -1287    801   -395       C  
ATOM   2383  C   THR A 298       8.946  27.315  62.661  1.00114.45           C  
ANISOU 2383  C   THR A 298    13897  16784  12805  -1357    724   -303       C  
ATOM   2384  O   THR A 298       9.899  26.936  61.977  1.00129.11           O  
ANISOU 2384  O   THR A 298    15800  18567  14689  -1364    688   -282       O  
ATOM   2385  CB  THR A 298       8.547  29.839  62.616  1.00 85.15           C  
ANISOU 2385  CB  THR A 298    10329  12958   9067  -1335    927   -562       C  
ATOM   2386  N   ARG A 299       8.632  26.792  63.854  1.00130.18           N  
ANISOU 2386  N   ARG A 299    15754  18972  14736  -1407    702   -247       N  
ATOM   2387  CA  ARG A 299       9.363  25.689  64.465  1.00124.38           C  
ANISOU 2387  CA  ARG A 299    14907  18381  13969  -1476    630   -145       C  
ATOM   2388  C   ARG A 299       8.826  24.387  63.878  1.00112.68           C  
ANISOU 2388  C   ARG A 299    13390  16843  12580  -1417    508     15       C  
ATOM   2389  O   ARG A 299       8.158  23.607  64.559  1.00114.43           O  
ANISOU 2389  O   ARG A 299    13493  17187  12798  -1423    449    121       O  
ATOM   2390  CB  ARG A 299       9.296  25.755  65.998  1.00111.20           C  
ANISOU 2390  CB  ARG A 299    13103  16956  12193  -1560    664   -156       C  
ATOM   2391  N   ASN A 300       9.107  24.197  62.587  1.00110.48           N  
ANISOU 2391  N   ASN A 300    13214  16378  12386  -1358    472     28       N  
ATOM   2392  CA  ASN A 300       8.624  23.037  61.851  1.00128.32           C  
ANISOU 2392  CA  ASN A 300    15456  18556  14745  -1296    360    161       C  
ATOM   2393  C   ASN A 300       9.604  21.882  62.033  1.00128.31           C  
ANISOU 2393  C   ASN A 300    15376  18623  14754  -1349    281    258       C  
ATOM   2394  O   ASN A 300      10.200  21.400  61.069  1.00143.70           O  
ANISOU 2394  O   ASN A 300    17380  20450  16768  -1323    231    284       O  
ATOM   2395  CB  ASN A 300       8.369  23.330  60.368  1.00124.53           C  
ANISOU 2395  CB  ASN A 300    15111  17853  14353  -1205    355    131       C  
ATOM   2396  N   SER A 301       9.743  21.440  63.287  1.00114.76           N  
ANISOU 2396  N   SER A 301    13524  17107  12972  -1424    269    314       N  
ATOM   2397  CA  SER A 301      10.757  20.465  63.629  1.00127.74           C  
ANISOU 2397  CA  SER A 301    15083  18839  14613  -1487    210    401       C  
ATOM   2398  C   SER A 301      10.190  19.438  64.607  1.00125.90           C  
ANISOU 2398  C   SER A 301    14683  18773  14380  -1515    138    544       C  
ATOM   2399  O   SER A 301      10.422  19.528  65.814  1.00130.90           O  
ANISOU 2399  O   SER A 301    15212  19604  14921  -1593    169    548       O  
ATOM   2400  CB  SER A 301      11.975  21.178  64.165  1.00137.12           C  
ANISOU 2400  CB  SER A 301    16285  20115  15701  -1573    290    300       C  
ATOM   2401  N   ASN A 302       9.457  18.462  64.057  1.00123.02           N  
ANISOU 2401  N   ASN A 302    14292  18328  14121  -1451     42    662       N  
ATOM   2402  CA  ASN A 302       8.774  17.488  64.889  1.00150.59           C  
ANISOU 2402  CA  ASN A 302    17630  21960  17629  -1466    -32    806       C  
ATOM   2403  C   ASN A 302       8.564  16.173  64.144  1.00153.70           C  
ANISOU 2403  C   ASN A 302    17995  22248  18156  -1415   -151    942       C  
ATOM   2404  O   ASN A 302       9.126  15.156  64.541  1.00158.71           O  
ANISOU 2404  O   ASN A 302    18521  22961  18819  -1460   -218   1054       O  
ATOM   2405  CB  ASN A 302       7.486  18.043  65.508  1.00169.41           C  
ANISOU 2405  CB  ASN A 302    19982  24422  19966  -1444      5    788       C  
ATOM   2406  CG  ASN A 302       6.788  17.080  66.447  1.00193.21           C  
ANISOU 2406  CG  ASN A 302    22826  27599  22984  -1466    -69    939       C  
ATOM   2407  OD1 ASN A 302       7.426  16.238  67.078  1.00241.91           O  
ANISOU 2407  OD1 ASN A 302    28875  33892  29148  -1529   -118   1039       O  
ATOM   2408  ND2 ASN A 302       5.472  17.190  66.541  1.00175.68           N  
ANISOU 2408  ND2 ASN A 302    20592  25381  20776  -1413    -78    963       N  
ATOM   2409  N   MET A 303       7.744  16.173  63.084  1.00142.64           N  
ANISOU 2409  N   MET A 303    16683  20673  16840  -1324   -178    935       N  
ATOM   2410  CA  MET A 303       7.205  14.907  62.601  1.00131.25           C  
ANISOU 2410  CA  MET A 303    15185  19163  15520  -1276   -293   1072       C  
ATOM   2411  C   MET A 303       7.073  14.962  61.082  1.00127.96           C  
ANISOU 2411  C   MET A 303    14904  18520  15195  -1191   -312   1025       C  
ATOM   2412  O   MET A 303       7.783  15.738  60.448  1.00135.57           O  
ANISOU 2412  O   MET A 303    15985  19393  16132  -1187   -252    909       O  
ATOM   2413  CB  MET A 303       5.836  14.663  63.241  1.00129.07           C  
ANISOU 2413  CB  MET A 303    14819  18976  15245  -1254   -323   1155       C  
ATOM   2414  CG  MET A 303       5.534  13.220  63.624  1.00144.76           C  
ANISOU 2414  CG  MET A 303    16658  21029  17314  -1263   -438   1333       C  
ATOM   2415  SD  MET A 303       4.038  13.098  64.674  1.00157.97           S  
ANISOU 2415  SD  MET A 303    18208  22860  18952  -1258   -457   1425       S  
ATOM   2416  CE  MET A 303       4.373  11.580  65.578  1.00111.90           C  
ANISOU 2416  CE  MET A 303    12169  17179  13169  -1322   -564   1623       C  
ATOM   2417  N   ASN A 304       6.161  14.161  60.518  1.00132.65           N  
ANISOU 2417  N   ASN A 304    15068  18253  17081   -245   -210    220       N  
ATOM   2418  CA  ASN A 304       6.062  13.998  59.071  1.00121.92           C  
ANISOU 2418  CA  ASN A 304    13793  16793  15737   -222   -233    239       C  
ATOM   2419  C   ASN A 304       5.521  15.266  58.415  1.00115.16           C  
ANISOU 2419  C   ASN A 304    12960  15865  14932   -274   -199    214       C  
ATOM   2420  O   ASN A 304       5.448  15.322  57.193  1.00114.20           O  
ANISOU 2420  O   ASN A 304    12905  15660  14825   -265   -211    223       O  
ATOM   2421  CB  ASN A 304       5.195  12.797  58.657  1.00109.26           C  
ANISOU 2421  CB  ASN A 304    12254  15105  14155   -177   -309    314       C  
ATOM   2422  CG  ASN A 304       5.441  11.522  59.440  1.00109.17           C  
ANISOU 2422  CG  ASN A 304    12218  15156  14106   -129   -351    348       C  
ATOM   2423  OD1 ASN A 304       5.666  11.571  60.651  1.00111.42           O  
ANISOU 2423  OD1 ASN A 304    12429  15535  14371   -143   -332    332       O  
ATOM   2424  ND2 ASN A 304       5.382  10.381  58.765  1.00 97.63           N  
ANISOU 2424  ND2 ASN A 304    10817  13642  12636    -74   -410    396       N  
ATOM   2425  N   TYR A 305       5.166  16.278  59.223  1.00113.80           N  
ANISOU 2425  N   TYR A 305    12730  15724  14783   -330   -156    181       N  
ATOM   2426  CA  TYR A 305       4.459  17.459  58.741  1.00113.13           C  
ANISOU 2426  CA  TYR A 305    12663  15566  14755   -382   -128    163       C  
ATOM   2427  C   TYR A 305       5.349  18.325  57.847  1.00118.50           C  
ANISOU 2427  C   TYR A 305    13355  16248  15423   -400    -83    111       C  
ATOM   2428  O   TYR A 305       4.848  19.091  57.024  1.00130.73           O  
ANISOU 2428  O   TYR A 305    14942  17713  17016   -431    -72    105       O  
ATOM   2429  CB  TYR A 305       3.821  18.241  59.895  1.00 97.93           C  
ANISOU 2429  CB  TYR A 305    10673  13677  12860   -433    -97    144       C  
ATOM   2430  CG  TYR A 305       3.068  17.376  60.871  1.00104.88           C  
ANISOU 2430  CG  TYR A 305    11533  14571  13745   -415   -138    192       C  
ATOM   2431  CD1 TYR A 305       2.120  16.451  60.453  1.00114.99           C  
ANISOU 2431  CD1 TYR A 305    12874  15763  15054   -382   -202    262       C  
ATOM   2432  CD2 TYR A 305       3.308  17.475  62.227  1.00105.38           C  
ANISOU 2432  CD2 TYR A 305    11516  14739  13784   -430   -114    169       C  
ATOM   2433  CE1 TYR A 305       1.462  15.627  61.351  1.00106.81           C  
ANISOU 2433  CE1 TYR A 305    11817  14744  14021   -364   -242    308       C  
ATOM   2434  CE2 TYR A 305       2.645  16.674  63.144  1.00 92.56           C  
ANISOU 2434  CE2 TYR A 305     9871  13135  12163   -414   -151    214       C  
ATOM   2435  CZ  TYR A 305       1.747  15.719  62.701  1.00 99.34           C  
ANISOU 2435  CZ  TYR A 305    10789  13906  13048   -379   -216    284       C  
ATOM   2436  OH  TYR A 305       1.060  14.921  63.564  1.00108.00           O  
ANISOU 2436  OH  TYR A 305    11867  15018  14151   -362   -256    332       O  
ATOM   2437  N   TRP A 306       6.668  18.187  58.015  1.00108.61           N  
ANISOU 2437  N   TRP A 306    12068  15089  14110   -381    -58     75       N  
ATOM   2438  CA  TRP A 306       7.644  18.845  57.164  1.00 97.02           C  
ANISOU 2438  CA  TRP A 306    10611  13631  12622   -389    -19     29       C  
ATOM   2439  C   TRP A 306       7.666  18.196  55.776  1.00 88.75           C  
ANISOU 2439  C   TRP A 306     9651  12497  11573   -347    -58     63       C  
ATOM   2440  O   TRP A 306       7.877  18.871  54.769  1.00 68.68           O  
ANISOU 2440  O   TRP A 306     7143   9908   9043   -364    -37     42       O  
ATOM   2441  CB  TRP A 306       9.022  18.783  57.842  1.00110.94           C  
ANISOU 2441  CB  TRP A 306    12309  15523  14319   -378     16    -14       C  
ATOM   2442  CG  TRP A 306      10.117  19.435  57.056  1.00129.71           C  
ANISOU 2442  CG  TRP A 306    14691  17923  16671   -385     57    -61       C  
ATOM   2443  CD1 TRP A 306      11.126  18.807  56.384  1.00124.79           C  
ANISOU 2443  CD1 TRP A 306    14094  17321  16000   -339     49    -61       C  
ATOM   2444  CD2 TRP A 306      10.289  20.848  56.827  1.00143.91           C  
ANISOU 2444  CD2 TRP A 306    16467  19721  18492   -441    112   -113       C  
ATOM   2445  NE1 TRP A 306      11.925  19.731  55.766  1.00137.44           N  
ANISOU 2445  NE1 TRP A 306    15690  18938  17592   -362     96   -110       N  
ATOM   2446  CE2 TRP A 306      11.443  20.990  56.025  1.00144.01           C  
ANISOU 2446  CE2 TRP A 306    16492  19758  18466   -425    134   -142       C  
ATOM   2447  CE3 TRP A 306       9.599  22.005  57.222  1.00154.60           C  
ANISOU 2447  CE3 TRP A 306    17790  21057  19894   -502    144   -139       C  
ATOM   2448  CZ2 TRP A 306      11.912  22.240  55.616  1.00146.57           C  
ANISOU 2448  CZ2 TRP A 306    16799  20090  18799   -469    186   -193       C  
ATOM   2449  CZ3 TRP A 306      10.062  23.238  56.813  1.00154.18           C  
ANISOU 2449  CZ3 TRP A 306    17721  21009  19851   -545    195   -191       C  
ATOM   2450  CH2 TRP A 306      11.210  23.351  56.028  1.00151.62           C  
ANISOU 2450  CH2 TRP A 306    17409  20711  19488   -529    215   -217       C  
ATOM   2451  N   LEU A 307       7.441  16.876  55.738  1.00 85.19           N  
ANISOU 2451  N   LEU A 307     9235  12025  11107   -293   -116    117       N  
ATOM   2452  CA  LEU A 307       7.647  16.085  54.535  1.00 77.84           C  
ANISOU 2452  CA  LEU A 307     8381  11031  10163   -244   -155    147       C  
ATOM   2453  C   LEU A 307       6.521  16.320  53.528  1.00 72.93           C  
ANISOU 2453  C   LEU A 307     7835  10275   9601   -258   -182    181       C  
ATOM   2454  O   LEU A 307       6.735  16.134  52.335  1.00 75.53           O  
ANISOU 2454  O   LEU A 307     8228  10544   9926   -236   -197    190       O  
ATOM   2455  CB  LEU A 307       7.739  14.593  54.896  1.00 85.63           C  
ANISOU 2455  CB  LEU A 307     9379  12042  11117   -182   -211    194       C  
ATOM   2456  CG  LEU A 307       9.112  13.997  55.240  1.00 90.24           C  
ANISOU 2456  CG  LEU A 307     9924  12731  11630   -143   -199    171       C  
ATOM   2457  CD1 LEU A 307       8.982  12.507  55.547  1.00 68.97           C  
ANISOU 2457  CD1 LEU A 307     7246  10042   8916    -84   -262    225       C  
ATOM   2458  CD2 LEU A 307      10.172  14.241  54.150  1.00 87.16           C  
ANISOU 2458  CD2 LEU A 307     9565  12343  11209   -129   -174    138       C  
ATOM   2459  N   ILE A 308       5.334  16.727  54.001  1.00 68.90           N  
ANISOU 2459  N   ILE A 308     7316   9719   9146   -295   -189    201       N  
ATOM   2460  CA  ILE A 308       4.183  16.838  53.129  1.00 69.47           C  
ANISOU 2460  CA  ILE A 308     7458   9661   9276   -307   -221    240       C  
ATOM   2461  C   ILE A 308       4.260  18.108  52.299  1.00 66.05           C  
ANISOU 2461  C   ILE A 308     7040   9186   8871   -355   -176    201       C  
ATOM   2462  O   ILE A 308       3.512  18.233  51.342  1.00 61.86           O  
ANISOU 2462  O   ILE A 308     6575   8547   8384   -362   -200    229       O  
ATOM   2463  CB  ILE A 308       2.854  16.735  53.899  1.00 84.23           C  
ANISOU 2463  CB  ILE A 308     9317  11492  11196   -326   -247    281       C  
ATOM   2464  CG1 ILE A 308       2.712  17.788  54.993  1.00 78.50           C  
ANISOU 2464  CG1 ILE A 308     8511  10829  10487   -382   -195    238       C  
ATOM   2465  CG2 ILE A 308       2.679  15.330  54.452  1.00120.20           C  
ANISOU 2465  CG2 ILE A 308    13876  16067  15728   -272   -304    333       C  
ATOM   2466  CD1 ILE A 308       1.480  17.565  55.849  1.00 66.55           C  
ANISOU 2466  CD1 ILE A 308     6981   9290   9016   -395   -222    280       C  
ATOM   2467  N   ILE A 309       5.175  19.025  52.639  1.00 74.48           N  
ANISOU 2467  N   ILE A 309     8048  10337   9915   -386   -115    137       N  
ATOM   2468  CA  ILE A 309       5.360  20.224  51.823  1.00 82.77           C  
ANISOU 2468  CA  ILE A 309     9109  11352  10988   -429    -73     97       C  
ATOM   2469  C   ILE A 309       6.673  20.197  51.018  1.00 79.72           C  
ANISOU 2469  C   ILE A 309     8737  11003  10549   -405    -53     66       C  
ATOM   2470  O   ILE A 309       6.836  20.960  50.064  1.00 69.91           O  
ANISOU 2470  O   ILE A 309     7523   9717   9322   -429    -30     44       O  
ATOM   2471  CB  ILE A 309       5.191  21.505  52.663  1.00 74.63           C  
ANISOU 2471  CB  ILE A 309     8007  10364   9985   -494    -19     50       C  
ATOM   2472  CG1 ILE A 309       4.884  22.710  51.770  1.00 75.04           C  
ANISOU 2472  CG1 ILE A 309     8084  10344  10085   -545     10     27       C  
ATOM   2473  CG2 ILE A 309       6.426  21.722  53.508  1.00 92.47           C  
ANISOU 2473  CG2 ILE A 309    10190  12756  12188   -495     26     -3       C  
ATOM   2474  CD1 ILE A 309       3.889  23.679  52.334  1.00 77.09           C  
ANISOU 2474  CD1 ILE A 309     8312  10573  10406   -604     31     18       C  
ATOM   2475  N   ARG A 310       7.587  19.295  51.393  1.00 77.89           N  
ANISOU 2475  N   ARG A 310     8486  10852  10256   -356    -62     65       N  
ATOM   2476  CA  ARG A 310       8.920  19.235  50.820  1.00 75.33           C  
ANISOU 2476  CA  ARG A 310     8164  10581   9877   -330    -39     33       C  
ATOM   2477  C   ARG A 310       9.046  18.103  49.805  1.00 74.27           C  
ANISOU 2477  C   ARG A 310     8107  10390   9720   -269    -89     75       C  
ATOM   2478  O   ARG A 310       9.934  18.154  48.953  1.00 81.99           O  
ANISOU 2478  O   ARG A 310     9109  11378  10667   -252    -74     54       O  
ATOM   2479  CB  ARG A 310       9.945  19.046  51.941  1.00 77.24           C  
ANISOU 2479  CB  ARG A 310     8327  10956  10064   -319    -11      0       C  
ATOM   2480  CG  ARG A 310      10.129  20.261  52.839  1.00 77.21           C  
ANISOU 2480  CG  ARG A 310     8244  11021  10071   -378     47    -53       C  
ATOM   2481  CD  ARG A 310      11.192  21.224  52.359  1.00 83.78           C  
ANISOU 2481  CD  ARG A 310     9054  11896  10881   -402    102   -110       C  
ATOM   2482  NE  ARG A 310      10.816  22.059  51.231  1.00 88.65           N  
ANISOU 2482  NE  ARG A 310     9719  12425  11540   -434    113   -117       N  
ATOM   2483  CZ  ARG A 310      10.308  23.285  51.343  1.00 95.80           C  
ANISOU 2483  CZ  ARG A 310    10601  13307  12493   -496    147   -144       C  
ATOM   2484  NH1 ARG A 310      10.066  23.806  52.536  1.00 84.12           N  
ANISOU 2484  NH1 ARG A 310     9053  11882  11027   -532    172   -167       N  
ATOM   2485  NH2 ARG A 310      10.025  23.981  50.256  1.00103.51           N  
ANISOU 2485  NH2 ARG A 310    11622  14203  13505   -522    154   -148       N  
ATOM   2486  N   LEU A 311       8.176  17.089  49.888  1.00 70.77           N  
ANISOU 2486  N   LEU A 311     7704   9891   9295   -237   -149    133       N  
ATOM   2487  CA  LEU A 311       8.241  15.981  48.938  1.00 70.13           C  
ANISOU 2487  CA  LEU A 311     7698   9753   9194   -178   -200    174       C  
ATOM   2488  C   LEU A 311       7.563  16.338  47.618  1.00 69.57           C  
ANISOU 2488  C   LEU A 311     7707   9561   9166   -192   -216    193       C  
ATOM   2489  O   LEU A 311       8.067  15.983  46.560  1.00 74.98           O  
ANISOU 2489  O   LEU A 311     8447  10216   9827   -160   -228    197       O  
ATOM   2490  CB  LEU A 311       7.643  14.701  49.522  1.00 67.62           C  
ANISOU 2490  CB  LEU A 311     7392   9425   8875   -134   -261    230       C  
ATOM   2491  CG  LEU A 311       8.531  13.963  50.517  1.00 71.16           C  
ANISOU 2491  CG  LEU A 311     7782   9988   9267    -99   -259    220       C  
ATOM   2492  CD1 LEU A 311       7.825  12.726  51.032  1.00 80.05           C  
ANISOU 2492  CD1 LEU A 311     8923  11093  10399    -59   -323    280       C  
ATOM   2493  CD2 LEU A 311       9.878  13.599  49.936  1.00 68.73           C  
ANISOU 2493  CD2 LEU A 311     7483   9732   8900    -59   -246    194       C  
ATOM   2494  N   PRO A 312       6.403  17.026  47.591  1.00 67.94           N  
ANISOU 2494  N   PRO A 312     7513   9278   9024   -239   -218    208       N  
ATOM   2495  CA  PRO A 312       5.855  17.495  46.329  1.00 68.50           C  
ANISOU 2495  CA  PRO A 312     7653   9239   9135   -259   -226    220       C  
ATOM   2496  C   PRO A 312       6.729  18.523  45.615  1.00 68.45           C  
ANISOU 2496  C   PRO A 312     7639   9255   9114   -288   -172    166       C  
ATOM   2497  O   PRO A 312       6.760  18.517  44.389  1.00 76.52           O  
ANISOU 2497  O   PRO A 312     8727  10207  10140   -278   -184    176       O  
ATOM   2498  CB  PRO A 312       4.473  18.054  46.696  1.00 72.63           C  
ANISOU 2498  CB  PRO A 312     8175   9693   9730   -307   -235    244       C  
ATOM   2499  CG  PRO A 312       4.170  17.461  48.048  1.00 62.29           C  
ANISOU 2499  CG  PRO A 312     6813   8442   8414   -294   -251    262       C  
ATOM   2500  CD  PRO A 312       5.519  17.348  48.718  1.00 74.16           C  
ANISOU 2500  CD  PRO A 312     8251  10075   9851   -275   -215    216       C  
ATOM   2501  N   ILE A 313       7.451  19.374  46.356  1.00 67.73           N  
ANISOU 2501  N   ILE A 313     7470   9259   9006   -321   -114    111       N  
ATOM   2502  CA  ILE A 313       8.373  20.305  45.703  1.00 62.67           C  
ANISOU 2502  CA  ILE A 313     6819   8647   8348   -345    -64     60       C  
ATOM   2503  C   ILE A 313       9.588  19.554  45.169  1.00 57.87           C  
ANISOU 2503  C   ILE A 313     6229   8087   7672   -289    -67     52       C  
ATOM   2504  O   ILE A 313      10.077  19.904  44.109  1.00 63.24           O  
ANISOU 2504  O   ILE A 313     6945   8742   8342   -290    -53     36       O  
ATOM   2505  CB  ILE A 313       8.782  21.507  46.575  1.00 52.86           C  
ANISOU 2505  CB  ILE A 313     5489   7485   7109   -400     -1      3       C  
ATOM   2506  CG1 ILE A 313       7.595  22.434  46.816  1.00 51.94           C  
ANISOU 2506  CG1 ILE A 313     5363   7305   7065   -461      7      6       C  
ATOM   2507  CG2 ILE A 313       9.908  22.272  45.923  1.00 50.37           C  
ANISOU 2507  CG2 ILE A 313     5162   7212   6766   -414     47    -47       C  
ATOM   2508  CD1 ILE A 313       7.904  23.567  47.750  1.00 45.71           C  
ANISOU 2508  CD1 ILE A 313     4490   6595   6284   -514     65    -48       C  
ATOM   2509  N   LEU A 314      10.050  18.533  45.902  1.00 57.79           N  
ANISOU 2509  N   LEU A 314     6195   8146   7618   -241    -86     63       N  
ATOM   2510  CA  LEU A 314      11.160  17.707  45.450  1.00 65.31           C  
ANISOU 2510  CA  LEU A 314     7165   9143   8507   -183    -94     59       C  
ATOM   2511  C   LEU A 314      10.777  16.958  44.173  1.00 63.97           C  
ANISOU 2511  C   LEU A 314     7092   8871   8342   -144   -144    103       C  
ATOM   2512  O   LEU A 314      11.621  16.782  43.276  1.00 53.86           O  
ANISOU 2512  O   LEU A 314     5844   7597   7025   -115   -137     90       O  
ATOM   2513  CB  LEU A 314      11.641  16.741  46.549  1.00 61.12           C  
ANISOU 2513  CB  LEU A 314     6588   8702   7933   -142   -108     67       C  
ATOM   2514  CG  LEU A 314      12.895  15.954  46.161  1.00 53.42           C  
ANISOU 2514  CG  LEU A 314     5621   7784   6891    -84   -110     57       C  
ATOM   2515  CD1 LEU A 314      14.058  16.925  45.990  1.00 57.89           C  
ANISOU 2515  CD1 LEU A 314     6144   8423   7428   -109    -45     -3       C  
ATOM   2516  CD2 LEU A 314      13.227  14.909  47.200  1.00 51.78           C  
ANISOU 2516  CD2 LEU A 314     5374   7652   6647    -42   -133     72       C  
ATOM   2517  N   PHE A 315       9.505  16.522  44.118  1.00 64.22           N  
ANISOU 2517  N   PHE A 315     7169   8811   8421   -143   -194    154       N  
ATOM   2518  CA  PHE A 315       8.968  15.829  42.959  1.00 63.91           C  
ANISOU 2518  CA  PHE A 315     7224   8666   8394   -110   -245    200       C  
ATOM   2519  C   PHE A 315       8.990  16.765  41.753  1.00 68.47           C  
ANISOU 2519  C   PHE A 315     7842   9181   8991   -144   -220    180       C  
ATOM   2520  O   PHE A 315       9.389  16.347  40.663  1.00 78.37           O  
ANISOU 2520  O   PHE A 315     9157  10399  10221   -110   -236    188       O  
ATOM   2521  CB  PHE A 315       7.548  15.321  43.212  1.00 57.46           C  
ANISOU 2521  CB  PHE A 315     6440   7763   7628   -110   -300    257       C  
ATOM   2522  CG  PHE A 315       6.911  14.672  42.012  1.00 58.48           C  
ANISOU 2522  CG  PHE A 315     6669   7776   7776    -81   -355    306       C  
ATOM   2523  CD1 PHE A 315       7.188  13.350  41.699  1.00 58.50           C  
ANISOU 2523  CD1 PHE A 315     6716   7771   7740    -13   -404    338       C  
ATOM   2524  CD2 PHE A 315       6.063  15.385  41.181  1.00 58.79           C  
ANISOU 2524  CD2 PHE A 315     6757   7714   7869   -122   -358    318       C  
ATOM   2525  CE1 PHE A 315       6.638  12.739  40.584  1.00 55.58           C  
ANISOU 2525  CE1 PHE A 315     6438   7296   7385     16   -454    381       C  
ATOM   2526  CE2 PHE A 315       5.523  14.779  40.058  1.00 65.31           C  
ANISOU 2526  CE2 PHE A 315     7673   8433   8707    -95   -408    362       C  
ATOM   2527  CZ  PHE A 315       5.811  13.463  39.759  1.00 60.17           C  
ANISOU 2527  CZ  PHE A 315     7067   7776   8017    -26   -456    393       C  
ATOM   2528  N   ALA A 316       8.565  18.025  41.956  1.00 57.53           N  
ANISOU 2528  N   ALA A 316     6423   7785   7652   -211   -182    155       N  
ATOM   2529  CA  ALA A 316       8.547  18.999  40.875  1.00 59.98           C  
ANISOU 2529  CA  ALA A 316     6766   8039   7986   -249   -157    136       C  
ATOM   2530  C   ALA A 316       9.964  19.329  40.385  1.00 67.10           C  
ANISOU 2530  C   ALA A 316     7650   9013   8832   -239   -113     88       C  
ATOM   2531  O   ALA A 316      10.164  19.639  39.199  1.00 66.03           O  
ANISOU 2531  O   ALA A 316     7564   8829   8697   -242   -108     84       O  
ATOM   2532  CB  ALA A 316       7.773  20.226  41.271  1.00 50.11           C  
ANISOU 2532  CB  ALA A 316     5480   6763   6797   -322   -127    121       C  
ATOM   2533  N   CYS A 317      10.948  19.219  41.287  1.00 60.57           N  
ANISOU 2533  N   CYS A 317     6753   8303   7958   -224    -83     55       N  
ATOM   2534  CA  CYS A 317      12.312  19.583  40.959  1.00 48.74           C  
ANISOU 2534  CA  CYS A 317     5228   6882   6409   -216    -37      8       C  
ATOM   2535  C   CYS A 317      13.024  18.445  40.243  1.00 49.25           C  
ANISOU 2535  C   CYS A 317     5343   6950   6418   -146    -66     25       C  
ATOM   2536  O   CYS A 317      13.829  18.702  39.355  1.00 51.97           O  
ANISOU 2536  O   CYS A 317     5708   7305   6735   -138    -44      3       O  
ATOM   2537  CB  CYS A 317      13.044  20.030  42.206  1.00 52.01           C  
ANISOU 2537  CB  CYS A 317     5547   7417   6799   -235      8    -35       C  
ATOM   2538  SG  CYS A 317      12.587  21.731  42.623  1.00 61.37           S  
ANISOU 2538  SG  CYS A 317     6675   8602   8041   -325     60    -75       S  
ATOM   2539  N   ILE A 318      12.729  17.198  40.632  1.00 48.65           N  
ANISOU 2539  N   ILE A 318     5287   6868   6329    -95   -116     65       N  
ATOM   2540  CA  ILE A 318      13.330  16.039  39.998  1.00 44.29           C  
ANISOU 2540  CA  ILE A 318     4785   6316   5728    -25   -148     84       C  
ATOM   2541  C   ILE A 318      12.853  16.011  38.557  1.00 51.93           C  
ANISOU 2541  C   ILE A 318     5843   7172   6715    -20   -174    108       C  
ATOM   2542  O   ILE A 318      13.664  15.775  37.667  1.00 61.10           O  
ANISOU 2542  O   ILE A 318     7039   8341   7837     12   -168     97       O  
ATOM   2543  CB  ILE A 318      12.991  14.724  40.732  1.00 44.75           C  
ANISOU 2543  CB  ILE A 318     4847   6383   5775     25   -200    125       C  
ATOM   2544  CG1 ILE A 318      13.780  14.533  42.021  1.00 46.38           C  
ANISOU 2544  CG1 ILE A 318     4967   6712   5943     35   -176    100       C  
ATOM   2545  CG2 ILE A 318      13.161  13.507  39.833  1.00 42.06           C  
ANISOU 2545  CG2 ILE A 318     4582   5995   5403     93   -250    159       C  
ATOM   2546  CD1 ILE A 318      13.211  13.416  42.897  1.00 54.62           C  
ANISOU 2546  CD1 ILE A 318     6005   7758   6990     69   -227    142       C  
ATOM   2547  N   VAL A 319      11.549  16.231  38.330  1.00 57.09           N  
ANISOU 2547  N   VAL A 319     6537   7725   7430    -51   -204    142       N  
ATOM   2548  CA  VAL A 319      11.031  16.173  36.970  1.00 67.90           C  
ANISOU 2548  CA  VAL A 319     7996   8984   8820    -47   -233    169       C  
ATOM   2549  C   VAL A 319      11.576  17.354  36.182  1.00 76.13           C  
ANISOU 2549  C   VAL A 319     9033  10030   9862    -89   -181    127       C  
ATOM   2550  O   VAL A 319      11.855  17.211  35.002  1.00 90.59           O  
ANISOU 2550  O   VAL A 319    10926  11818  11678    -70   -189    131       O  
ATOM   2551  CB  VAL A 319       9.493  16.135  36.850  1.00 71.20           C  
ANISOU 2551  CB  VAL A 319     8461   9287   9306    -72   -278    218       C  
ATOM   2552  CG1 VAL A 319       8.878  14.848  37.371  1.00 75.98           C  
ANISOU 2552  CG1 VAL A 319     9088   9868   9911    -24   -339    269       C  
ATOM   2553  CG2 VAL A 319       8.832  17.346  37.473  1.00 81.18           C  
ANISOU 2553  CG2 VAL A 319     9673  10546  10624   -145   -244    202       C  
ATOM   2554  N   ASN A 320      11.712  18.517  36.832  1.00 76.02           N  
ANISOU 2554  N   ASN A 320     8948  10068   9869   -147   -129     88       N  
ATOM   2555  CA  ASN A 320      12.264  19.687  36.158  1.00 77.50           C  
ANISOU 2555  CA  ASN A 320     9123  10266  10058   -190    -79     47       C  
ATOM   2556  C   ASN A 320      13.682  19.428  35.648  1.00 73.85           C  
ANISOU 2556  C   ASN A 320     8658   9875   9526   -149    -55     17       C  
ATOM   2557  O   ASN A 320      14.034  19.882  34.563  1.00 82.89           O  
ANISOU 2557  O   ASN A 320     9838  10993  10665   -158    -39      5       O  
ATOM   2558  CB  ASN A 320      12.179  20.956  37.001  1.00 88.74           C  
ANISOU 2558  CB  ASN A 320    10468  11735  11515   -257    -29      9       C  
ATOM   2559  CG  ASN A 320      10.851  21.651  36.827  1.00103.97           C  
ANISOU 2559  CG  ASN A 320    12420  13566  13520   -313    -42     30       C  
ATOM   2560  OD1 ASN A 320      10.234  21.542  35.769  1.00129.67           O  
ANISOU 2560  OD1 ASN A 320    15750  16720  16800   -313    -72     61       O  
ATOM   2561  ND2 ASN A 320      10.385  22.327  37.864  1.00 92.40           N  
ANISOU 2561  ND2 ASN A 320    10892  12125  12090   -359    -20     16       N  
ATOM   2562  N   PHE A 321      14.483  18.689  36.424  1.00 67.79           N  
ANISOU 2562  N   PHE A 321     7849   9199   8708   -105    -52      7       N  
ATOM   2563  CA  PHE A 321      15.826  18.332  35.992  1.00 67.41           C  
ANISOU 2563  CA  PHE A 321     7799   9221   8594    -61    -31    -17       C  
ATOM   2564  C   PHE A 321      15.795  17.230  34.937  1.00 64.05           C  
ANISOU 2564  C   PHE A 321     7461   8730   8143      0    -79     18       C  
ATOM   2565  O   PHE A 321      16.707  17.160  34.107  1.00 71.82           O  
ANISOU 2565  O   PHE A 321     8467   9737   9085     26    -63      1       O  
ATOM   2566  CB  PHE A 321      16.728  17.936  37.169  1.00 69.00           C  
ANISOU 2566  CB  PHE A 321     7925   9543   8750    -35    -11    -40       C  
ATOM   2567  CG  PHE A 321      17.391  19.114  37.824  1.00 63.85           C  
ANISOU 2567  CG  PHE A 321     7187   8977   8094    -85     52    -92       C  
ATOM   2568  CD1 PHE A 321      18.312  19.891  37.129  1.00 67.95           C  
ANISOU 2568  CD1 PHE A 321     7696   9530   8591   -101     98   -130       C  
ATOM   2569  CD2 PHE A 321      17.026  19.498  39.098  1.00 61.22           C  
ANISOU 2569  CD2 PHE A 321     6788   8688   7787   -120     66   -102       C  
ATOM   2570  CE1 PHE A 321      18.869  21.023  37.702  1.00 65.15           C  
ANISOU 2570  CE1 PHE A 321     7265   9249   8238   -151    154   -176       C  
ATOM   2571  CE2 PHE A 321      17.593  20.624  39.682  1.00 75.00           C  
ANISOU 2571  CE2 PHE A 321     8456  10509   9532   -169    123   -151       C  
ATOM   2572  CZ  PHE A 321      18.522  21.379  38.990  1.00 74.48           C  
ANISOU 2572  CZ  PHE A 321     8381  10475   9443   -184    167   -187       C  
ATOM   2573  N   LEU A 322      14.773  16.363  34.986  1.00 52.86           N  
ANISOU 2573  N   LEU A 322     6094   7238   6752     24   -138     68       N  
ATOM   2574  CA  LEU A 322      14.665  15.346  33.955  1.00 56.31           C  
ANISOU 2574  CA  LEU A 322     6618   7606   7170     79   -187    103       C  
ATOM   2575  C   LEU A 322      14.274  16.001  32.628  1.00 56.53           C  
ANISOU 2575  C   LEU A 322     6711   7544   7225     49   -185    107       C  
ATOM   2576  O   LEU A 322      14.780  15.603  31.584  1.00 49.22           O  
ANISOU 2576  O   LEU A 322     5839   6597   6265     86   -193    108       O  
ATOM   2577  CB  LEU A 322      13.708  14.232  34.382  1.00 57.60           C  
ANISOU 2577  CB  LEU A 322     6817   7716   7354    113   -252    155       C  
ATOM   2578  CG  LEU A 322      14.153  13.420  35.604  1.00 65.63           C  
ANISOU 2578  CG  LEU A 322     7776   8821   8338    151   -259    155       C  
ATOM   2579  CD1 LEU A 322      13.134  12.348  35.951  1.00 59.07           C  
ANISOU 2579  CD1 LEU A 322     6983   7929   7533    181   -327    211       C  
ATOM   2580  CD2 LEU A 322      15.534  12.797  35.425  1.00 61.63           C  
ANISOU 2580  CD2 LEU A 322     7259   8396   7761    207   -244    132       C  
ATOM   2581  N   ILE A 323      13.444  17.050  32.677  1.00 54.18           N  
ANISOU 2581  N   ILE A 323     6402   7197   6987    -18   -171    105       N  
ATOM   2582  CA  ILE A 323      13.081  17.794  31.485  1.00 57.35           C  
ANISOU 2582  CA  ILE A 323     6855   7517   7417    -54   -165    107       C  
ATOM   2583  C   ILE A 323      14.292  18.583  31.014  1.00 61.35           C  
ANISOU 2583  C   ILE A 323     7330   8094   7886    -68   -107     57       C  
ATOM   2584  O   ILE A 323      14.587  18.618  29.821  1.00 72.98           O  
ANISOU 2584  O   ILE A 323     8858   9529   9342    -57   -108     57       O  
ATOM   2585  CB  ILE A 323      11.866  18.704  31.732  1.00 60.34           C  
ANISOU 2585  CB  ILE A 323     7226   7828   7872   -123   -165    119       C  
ATOM   2586  CG1 ILE A 323      10.613  17.913  32.138  1.00 70.71           C  
ANISOU 2586  CG1 ILE A 323     8575   9067   9225   -110   -225    173       C  
ATOM   2587  CG2 ILE A 323      11.606  19.596  30.524  1.00 58.98           C  
ANISOU 2587  CG2 ILE A 323     7098   7583   7729   -167   -153    115       C  
ATOM   2588  CD1 ILE A 323      10.288  16.694  31.271  1.00 76.12           C  
ANISOU 2588  CD1 ILE A 323     9353   9675   9895    -51   -287    220       C  
ATOM   2589  N   PHE A 324      14.993  19.197  31.969  1.00 67.09           N  
ANISOU 2589  N   PHE A 324     7969   8924   8599    -90    -58     15       N  
ATOM   2590  CA  PHE A 324      16.243  19.897  31.691  1.00 78.29           C  
ANISOU 2590  CA  PHE A 324     9346  10422   9978   -100     -2    -33       C  
ATOM   2591  C   PHE A 324      17.190  19.071  30.810  1.00 77.78           C  
ANISOU 2591  C   PHE A 324     9327  10376   9849    -35    -10    -33       C  
ATOM   2592  O   PHE A 324      17.680  19.567  29.799  1.00 73.94           O  
ANISOU 2592  O   PHE A 324     8865   9880   9349    -44     12    -50       O  
ATOM   2593  CB  PHE A 324      16.916  20.262  33.011  1.00 66.80           C  
ANISOU 2593  CB  PHE A 324     7793   9083   8506   -114     40    -70       C  
ATOM   2594  CG  PHE A 324      18.266  20.910  32.898  1.00 64.12           C  
ANISOU 2594  CG  PHE A 324     7403   8839   8122   -120     97   -119       C  
ATOM   2595  CD1 PHE A 324      18.364  22.294  32.858  1.00 64.03           C  
ANISOU 2595  CD1 PHE A 324     7349   8841   8139   -186    143   -153       C  
ATOM   2596  CD2 PHE A 324      19.423  20.148  32.879  1.00 55.55           C  
ANISOU 2596  CD2 PHE A 324     6309   7828   6969    -61    104   -131       C  
ATOM   2597  CE1 PHE A 324      19.602  22.915  32.853  1.00 66.58           C  
ANISOU 2597  CE1 PHE A 324     7619   9255   8423   -194    196   -198       C  
ATOM   2598  CE2 PHE A 324      20.658  20.772  32.851  1.00 59.55           C  
ANISOU 2598  CE2 PHE A 324     6763   8425   7437    -69    157   -175       C  
ATOM   2599  CZ  PHE A 324      20.748  22.149  32.835  1.00 61.91           C  
ANISOU 2599  CZ  PHE A 324     7020   8739   7764   -135    203   -208       C  
ATOM   2600  N   VAL A 325      17.420  17.807  31.186  1.00 72.78           N  
ANISOU 2600  N   VAL A 325     8705   9768   9179     29    -43    -14       N  
ATOM   2601  CA  VAL A 325      18.366  16.947  30.494  1.00 67.14           C  
ANISOU 2601  CA  VAL A 325     8027   9080   8402     95    -50    -15       C  
ATOM   2602  C   VAL A 325      17.792  16.524  29.152  1.00 63.60           C  
ANISOU 2602  C   VAL A 325     7680   8522   7963    115    -92     18       C  
ATOM   2603  O   VAL A 325      18.506  16.522  28.163  1.00 57.95           O  
ANISOU 2603  O   VAL A 325     6996   7810   7210    136    -78      5       O  
ATOM   2604  CB  VAL A 325      18.739  15.740  31.368  1.00 71.42           C  
ANISOU 2604  CB  VAL A 325     8548   9681   8907    155    -75     -4       C  
ATOM   2605  CG1 VAL A 325      19.311  14.572  30.572  1.00 63.33           C  
ANISOU 2605  CG1 VAL A 325     7584   8648   7831    231   -104     11       C  
ATOM   2606  CG2 VAL A 325      19.665  16.180  32.498  1.00 72.24           C  
ANISOU 2606  CG2 VAL A 325     8552   9909   8986    142    -25    -45       C  
ATOM   2607  N   ARG A 326      16.496  16.199  29.127  1.00 69.39           N  
ANISOU 2607  N   ARG A 326     8462   9158   8746    106   -141     61       N  
ATOM   2608  CA  ARG A 326      15.874  15.706  27.910  1.00 71.07           C  
ANISOU 2608  CA  ARG A 326     8773   9262   8969    126   -187     97       C  
ATOM   2609  C   ARG A 326      15.875  16.796  26.838  1.00 63.21           C  
ANISOU 2609  C   ARG A 326     7802   8225   7991     77   -157     81       C  
ATOM   2610  O   ARG A 326      16.214  16.533  25.678  1.00 50.51           O  
ANISOU 2610  O   ARG A 326     6254   6582   6354    104   -165     85       O  
ATOM   2611  CB  ARG A 326      14.480  15.119  28.182  1.00 79.20           C  
ANISOU 2611  CB  ARG A 326     9845  10199  10049    126   -247    149       C  
ATOM   2612  CG  ARG A 326      13.839  14.421  26.986  1.00 98.79           C  
ANISOU 2612  CG  ARG A 326    12432  12568  12537    156   -302    191       C  
ATOM   2613  CD  ARG A 326      14.700  13.432  26.205  1.00109.99           C  
ANISOU 2613  CD  ARG A 326    13899  14001  13891    228   -317    191       C  
ATOM   2614  NE  ARG A 326      15.478  12.543  27.068  1.00122.69           N  
ANISOU 2614  NE  ARG A 326    15465  15700  15453    284   -319    182       N  
ATOM   2615  CZ  ARG A 326      16.505  11.790  26.674  1.00130.38           C  
ANISOU 2615  CZ  ARG A 326    16454  16721  16364    346   -318    169       C  
ATOM   2616  NH1 ARG A 326      16.897  11.801  25.410  1.00127.70           N  
ANISOU 2616  NH1 ARG A 326    16173  16349  15999    362   -314    163       N  
ATOM   2617  NH2 ARG A 326      17.139  11.031  27.552  1.00133.00           N  
ANISOU 2617  NH2 ARG A 326    16741  17133  16660    390   -320    162       N  
ATOM   2618  N   VAL A 327      15.491  18.011  27.254  1.00 62.00           N  
ANISOU 2618  N   VAL A 327     7599   8074   7885      6   -124     63       N  
ATOM   2619  CA  VAL A 327      15.428  19.169  26.375  1.00 60.03           C  
ANISOU 2619  CA  VAL A 327     7361   7788   7661    -50    -94     47       C  
ATOM   2620  C   VAL A 327      16.803  19.409  25.774  1.00 62.47           C  
ANISOU 2620  C   VAL A 327     7655   8171   7910    -31    -50      9       C  
ATOM   2621  O   VAL A 327      16.886  19.656  24.580  1.00 73.60           O  
ANISOU 2621  O   VAL A 327     9117   9534   9315    -36    -49     10       O  
ATOM   2622  CB  VAL A 327      14.932  20.429  27.107  1.00 63.81           C  
ANISOU 2622  CB  VAL A 327     7774   8275   8196   -127    -60     29       C  
ATOM   2623  CG1 VAL A 327      15.359  21.735  26.422  1.00 57.54           C  
ANISOU 2623  CG1 VAL A 327     6961   7490   7412   -182    -12     -5       C  
ATOM   2624  CG2 VAL A 327      13.429  20.379  27.377  1.00 59.77           C  
ANISOU 2624  CG2 VAL A 327     7291   7666   7753   -156   -103     70       C  
ATOM   2625  N   ILE A 328      17.864  19.337  26.596  1.00 60.63           N  
ANISOU 2625  N   ILE A 328     7350   8053   7633    -10    -15    -25       N  
ATOM   2626  CA  ILE A 328      19.213  19.575  26.102  1.00 55.14           C  
ANISOU 2626  CA  ILE A 328     6634   7436   6881      8     29    -62       C  
ATOM   2627  C   ILE A 328      19.617  18.573  25.023  1.00 54.26           C  
ANISOU 2627  C   ILE A 328     6600   7296   6721     74      0    -45       C  
ATOM   2628  O   ILE A 328      20.223  18.985  24.031  1.00 51.92           O  
ANISOU 2628  O   ILE A 328     6325   7002   6401     71     25    -62       O  
ATOM   2629  CB  ILE A 328      20.240  19.671  27.231  1.00 58.97           C  
ANISOU 2629  CB  ILE A 328     7027   8048   7330     17     70    -99       C  
ATOM   2630  CG1 ILE A 328      19.991  20.938  28.056  1.00 71.24           C  
ANISOU 2630  CG1 ILE A 328     8506   9633   8930    -57    109   -125       C  
ATOM   2631  CG2 ILE A 328      21.647  19.677  26.664  1.00 67.97           C  
ANISOU 2631  CG2 ILE A 328     8155   9264   8405     49    107   -130       C  
ATOM   2632  CD1 ILE A 328      20.911  21.119  29.261  1.00 67.93           C  
ANISOU 2632  CD1 ILE A 328     7992   9337   8481    -56    149   -161       C  
ATOM   2633  N   CYS A 329      19.263  17.288  25.194  1.00 55.96           N  
ANISOU 2633  N   CYS A 329     6857   7480   6923    132    -51    -12       N  
ATOM   2634  CA  CYS A 329      19.575  16.304  24.168  1.00 62.65           C  
ANISOU 2634  CA  CYS A 329     7783   8295   7728    195    -81      5       C  
ATOM   2635  C   CYS A 329      18.842  16.615  22.868  1.00 73.79           C  
ANISOU 2635  C   CYS A 329     9275   9595   9167    171   -103     27       C  
ATOM   2636  O   CYS A 329      19.398  16.367  21.802  1.00 87.72           O  
ANISOU 2636  O   CYS A 329    11088  11350  10893    202   -101     23       O  
ATOM   2637  CB  CYS A 329      19.174  14.898  24.563  1.00 66.75           C  
ANISOU 2637  CB  CYS A 329     8336   8788   8237    256   -139     41       C  
ATOM   2638  SG  CYS A 329      20.260  14.246  25.846  1.00 90.28           S  
ANISOU 2638  SG  CYS A 329    11235  11900  11166    303   -119     17       S  
ATOM   2639  N   ILE A 330      17.608  17.141  22.972  1.00 68.96           N  
ANISOU 2639  N   ILE A 330     8677   8902   8624    117   -123     51       N  
ATOM   2640  CA  ILE A 330      16.770  17.425  21.813  1.00 55.50           C  
ANISOU 2640  CA  ILE A 330     7050   7084   6954     90   -148     77       C  
ATOM   2641  C   ILE A 330      17.316  18.643  21.086  1.00 53.20           C  
ANISOU 2641  C   ILE A 330     6740   6813   6661     42    -97     44       C  
ATOM   2642  O   ILE A 330      17.435  18.603  19.869  1.00 59.05           O  
ANISOU 2642  O   ILE A 330     7544   7508   7385     52   -104     51       O  
ATOM   2643  CB  ILE A 330      15.301  17.599  22.241  1.00 62.39           C  
ANISOU 2643  CB  ILE A 330     7936   7869   7900     48   -184    113       C  
ATOM   2644  CG1 ILE A 330      14.684  16.294  22.774  1.00 74.58           C  
ANISOU 2644  CG1 ILE A 330     9512   9378   9445    100   -244    154       C  
ATOM   2645  CG2 ILE A 330      14.436  18.290  21.194  1.00 52.93           C  
ANISOU 2645  CG2 ILE A 330     6797   6564   6751     -3   -197    133       C  
ATOM   2646  CD1 ILE A 330      15.064  15.027  22.004  1.00 81.99           C  
ANISOU 2646  CD1 ILE A 330    10524  10297  10332    177   -282    172       C  
ATOM   2647  N   VAL A 331      17.689  19.686  21.832  1.00 50.17           N  
ANISOU 2647  N   VAL A 331     6271   6501   6292     -8    -46      9       N  
ATOM   2648  CA  VAL A 331      18.123  20.931  21.228  1.00 56.55           C  
ANISOU 2648  CA  VAL A 331     7055   7325   7107    -61      1    -21       C  
ATOM   2649  C   VAL A 331      19.439  20.720  20.475  1.00 66.74           C  
ANISOU 2649  C   VAL A 331     8352   8679   8325    -18     29    -46       C  
ATOM   2650  O   VAL A 331      19.570  21.179  19.348  1.00 65.14           O  
ANISOU 2650  O   VAL A 331     8189   8442   8119    -34     38    -48       O  
ATOM   2651  CB  VAL A 331      18.230  22.063  22.266  1.00 56.35           C  
ANISOU 2651  CB  VAL A 331     6934   7365   7114   -122     47    -53       C  
ATOM   2652  CG1 VAL A 331      18.909  23.290  21.686  1.00 68.49           C  
ANISOU 2652  CG1 VAL A 331     8439   8938   8648   -169    100    -88       C  
ATOM   2653  CG2 VAL A 331      16.879  22.449  22.806  1.00 51.66           C  
ANISOU 2653  CG2 VAL A 331     6337   6696   6594   -173     24    -29       C  
ATOM   2654  N   VAL A 332      20.405  20.021  21.088  1.00 79.50           N  
ANISOU 2654  N   VAL A 332     9932  10389   9887     37     41    -64       N  
ATOM   2655  CA  VAL A 332      21.712  19.796  20.474  1.00 80.17           C  
ANISOU 2655  CA  VAL A 332    10016  10541   9902     81     70    -89       C  
ATOM   2656  C   VAL A 332      21.569  18.873  19.265  1.00 82.85           C  
ANISOU 2656  C   VAL A 332    10455  10809  10214    132     29    -61       C  
ATOM   2657  O   VAL A 332      22.406  18.917  18.373  1.00 97.58           O  
ANISOU 2657  O   VAL A 332    12341  12700  12035    153     51    -77       O  
ATOM   2658  CB  VAL A 332      22.767  19.243  21.459  1.00 79.99           C  
ANISOU 2658  CB  VAL A 332     9930  10635   9829    127     92   -113       C  
ATOM   2659  CG1 VAL A 332      22.922  20.108  22.701  1.00 69.09           C  
ANISOU 2659  CG1 VAL A 332     8450   9327   8473     78    131   -140       C  
ATOM   2660  CG2 VAL A 332      22.497  17.790  21.847  1.00 92.00           C  
ANISOU 2660  CG2 VAL A 332    11487  12138  11332    195     41    -84       C  
ATOM   2661  N   SER A 333      20.527  18.032  19.248  1.00 77.31           N  
ANISOU 2661  N   SER A 333     9816  10020   9539    154    -30    -20       N  
ATOM   2662  CA  SER A 333      20.248  17.200  18.088  1.00 77.15           C  
ANISOU 2662  CA  SER A 333     9895   9920   9499    197    -73      9       C  
ATOM   2663  C   SER A 333      19.724  18.065  16.954  1.00 78.86           C  
ANISOU 2663  C   SER A 333    10158  10058   9749    144    -71     17       C  
ATOM   2664  O   SER A 333      20.190  17.943  15.826  1.00 87.86           O  
ANISOU 2664  O   SER A 333    11347  11183  10851    166    -68     14       O  
ATOM   2665  CB  SER A 333      19.290  16.088  18.398  1.00 74.22           C  
ANISOU 2665  CB  SER A 333     9574   9477   9148    233   -138     52       C  
ATOM   2666  OG  SER A 333      19.945  15.138  19.218  1.00 83.41           O  
ANISOU 2666  OG  SER A 333    10706  10717  10270    294   -143     45       O  
ATOM   2667  N   LYS A 334      18.750  18.925  17.265  1.00 72.36           N  
ANISOU 2667  N   LYS A 334     9317   9182   8994     75    -73     27       N  
ATOM   2668  CA  LYS A 334      18.097  19.739  16.250  1.00 73.59           C  
ANISOU 2668  CA  LYS A 334     9518   9253   9189     20    -76     40       C  
ATOM   2669  C   LYS A 334      19.066  20.781  15.687  1.00 63.80           C  
ANISOU 2669  C   LYS A 334     8241   8075   7927    -12    -17      1       C  
ATOM   2670  O   LYS A 334      19.002  21.124  14.505  1.00 61.44           O  
ANISOU 2670  O   LYS A 334     7993   7725   7627    -29    -18      7       O  
ATOM   2671  CB  LYS A 334      16.771  20.300  16.775  1.00 73.68           C  
ANISOU 2671  CB  LYS A 334     9522   9192   9283    -43    -96     64       C  
ATOM   2672  CG  LYS A 334      15.711  19.240  17.070  1.00 75.00           C  
ANISOU 2672  CG  LYS A 334     9743   9280   9475    -11   -160    110       C  
ATOM   2673  CD  LYS A 334      14.404  19.809  17.598  1.00 78.19           C  
ANISOU 2673  CD  LYS A 334    10137   9612   9959    -73   -179    135       C  
ATOM   2674  CE  LYS A 334      13.733  20.827  16.696  1.00100.40           C  
ANISOU 2674  CE  LYS A 334    12982  12344  12823   -141   -175    144       C  
ATOM   2675  NZ  LYS A 334      13.062  20.211  15.525  1.00108.82           N  
ANISOU 2675  NZ  LYS A 334    14153  13300  13893   -121   -227    185       N  
ATOM   2676  N   LEU A 335      19.988  21.249  16.536  1.00 59.48           N  
ANISOU 2676  N   LEU A 335     7603   7638   7358    -18     32    -38       N  
ATOM   2677  CA  LEU A 335      20.984  22.211  16.101  1.00 61.23           C  
ANISOU 2677  CA  LEU A 335     7782   7928   7555    -45     88    -75       C  
ATOM   2678  C   LEU A 335      22.015  21.550  15.183  1.00 65.00           C  
ANISOU 2678  C   LEU A 335     8299   8439   7958     17     95    -84       C  
ATOM   2679  O   LEU A 335      22.357  22.132  14.142  1.00 63.08           O  
ANISOU 2679  O   LEU A 335     8077   8187   7703     -2    115    -92       O  
ATOM   2680  CB  LEU A 335      21.623  22.879  17.313  1.00 54.75           C  
ANISOU 2680  CB  LEU A 335     6855   7212   6735    -71    136   -112       C  
ATOM   2681  CG  LEU A 335      20.720  23.914  17.981  1.00 61.95           C  
ANISOU 2681  CG  LEU A 335     7723   8093   7723   -149    143   -111       C  
ATOM   2682  CD1 LEU A 335      21.316  24.354  19.308  1.00 68.93           C  
ANISOU 2682  CD1 LEU A 335     8506   9081   8604   -163    183   -145       C  
ATOM   2683  CD2 LEU A 335      20.481  25.124  17.075  1.00 55.29           C  
ANISOU 2683  CD2 LEU A 335     6888   7204   6915   -216    162   -116       C  
ATOM   2684  N   LYS A 336      22.472  20.340  15.555  1.00 59.28           N  
ANISOU 2684  N   LYS A 336     7585   7752   7186     92     76    -80       N  
ATOM   2685  CA  LYS A 336      23.479  19.636  14.775  1.00 64.87           C  
ANISOU 2685  CA  LYS A 336     8327   8498   7822    157     83    -90       C  
ATOM   2686  C   LYS A 336      22.904  19.241  13.418  1.00 72.16           C  
ANISOU 2686  C   LYS A 336     9355   9319   8745    170     44    -60       C  
ATOM   2687  O   LYS A 336      23.625  19.286  12.420  1.00 84.55           O  
ANISOU 2687  O   LYS A 336    10952  10905  10270    189     62    -72       O  
ATOM   2688  CB  LYS A 336      24.100  18.430  15.488  1.00 63.96           C  
ANISOU 2688  CB  LYS A 336     8199   8446   7659    233     71    -93       C  
ATOM   2689  CG  LYS A 336      25.159  17.708  14.638  1.00 62.87           C  
ANISOU 2689  CG  LYS A 336     8097   8346   7446    301     79   -104       C  
ATOM   2690  CD  LYS A 336      26.376  17.136  15.363  1.00 59.93           C  
ANISOU 2690  CD  LYS A 336     7667   8088   7016    357    106   -130       C  
ATOM   2691  CE  LYS A 336      27.655  17.311  14.576  1.00 57.37           C  
ANISOU 2691  CE  LYS A 336     7337   7832   6631    382    149   -158       C  
ATOM   2692  NZ  LYS A 336      28.534  16.133  14.686  1.00 69.53           N  
ANISOU 2692  NZ  LYS A 336     8884   9428   8108    466    144   -164       N  
ATOM   2693  N   ALA A 337      21.615  18.867  13.398  1.00 81.49           N  
ANISOU 2693  N   ALA A 337     7871  13801   9290   -112    795  -1999       N  
ATOM   2694  CA  ALA A 337      20.973  18.388  12.185  1.00 81.80           C  
ANISOU 2694  CA  ALA A 337     7928  13861   9291    -99    799  -1942       C  
ATOM   2695  C   ALA A 337      20.427  19.536  11.322  1.00 88.60           C  
ANISOU 2695  C   ALA A 337     8798  14789  10078   -324    915  -1833       C  
ATOM   2696  O   ALA A 337      19.751  19.281  10.324  1.00 88.05           O  
ANISOU 2696  O   ALA A 337     8759  14714   9984   -327    931  -1765       O  
ATOM   2697  CB  ALA A 337      19.921  17.380  12.546  1.00 72.04           C  
ANISOU 2697  CB  ALA A 337     6814  12362   8196    163    718  -1877       C  
ATOM   2698  N   ASN A 338      20.750  20.796  11.683  1.00 86.76           N  
ANISOU 2698  N   ASN A 338     8551  14615   9800   -533    993  -1807       N  
ATOM   2699  CA  ASN A 338      20.240  21.984  11.017  1.00 87.73           C  
ANISOU 2699  CA  ASN A 338     8722  14763   9849   -791   1093  -1673       C  
ATOM   2700  C   ASN A 338      18.719  21.983  10.919  1.00 86.08           C  
ANISOU 2700  C   ASN A 338     8643  14323   9739   -697   1114  -1524       C  
ATOM   2701  O   ASN A 338      18.162  22.612  10.027  1.00 90.86           O  
ANISOU 2701  O   ASN A 338     9368  14855  10299   -872   1130  -1375       O  
ATOM   2702  CB  ASN A 338      20.976  22.297   9.718  1.00 94.47           C  
ANISOU 2702  CB  ASN A 338     9511  15852  10531  -1035   1122  -1690       C  
ATOM   2703  CG  ASN A 338      22.210  23.130   9.997  1.00119.14           C  
ANISOU 2703  CG  ASN A 338    12567  19145  13556  -1245   1141  -1754       C  
ATOM   2704  OD1 ASN A 338      22.161  24.032  10.827  1.00140.57           O  
ANISOU 2704  OD1 ASN A 338    15326  21784  16300  -1337   1175  -1698       O  
ATOM   2705  ND2 ASN A 338      23.322  22.851   9.333  1.00140.19           N  
ANISOU 2705  ND2 ASN A 338    15129  22033  16105  -1322   1118  -1865       N  
ATOM   2706  N   LEU A 339      18.060  21.342  11.888  1.00 91.41           N  
ANISOU 2706  N   LEU A 339     9379  14776  10575   -414   1056  -1526       N  
ATOM   2707  CA  LEU A 339      16.608  21.439  12.014  1.00 87.73           C  
ANISOU 2707  CA  LEU A 339     9137  13947  10248   -303   1007  -1336       C  
ATOM   2708  C   LEU A 339      16.211  22.728  12.739  1.00 94.22           C  
ANISOU 2708  C   LEU A 339    10156  14508  11136   -436    993  -1171       C  
ATOM   2709  O   LEU A 339      15.050  23.131  12.718  1.00 99.45           O  
ANISOU 2709  O   LEU A 339    11024  14873  11891   -422    963   -984       O  
ATOM   2710  CB  LEU A 339      16.053  20.229  12.766  1.00 71.45           C  
ANISOU 2710  CB  LEU A 339     7062  11752   8331     56    949  -1405       C  
ATOM   2711  CG  LEU A 339      16.381  18.880  12.143  1.00 72.34           C  
ANISOU 2711  CG  LEU A 339     7103  11968   8413    198    879  -1500       C  
ATOM   2712  CD1 LEU A 339      15.871  17.764  13.042  1.00 79.76           C  
ANISOU 2712  CD1 LEU A 339     8157  12635   9513    495    753  -1489       C  
ATOM   2713  CD2 LEU A 339      15.772  18.782  10.757  1.00 76.72           C  
ANISOU 2713  CD2 LEU A 339     7666  12590   8896    124    922  -1424       C  
ATOM   2714  N   MET A 340      17.177  23.378  13.391  1.00 97.63           N  
ANISOU 2714  N   MET A 340    10526  15048  11520   -564   1013  -1237       N  
ATOM   2715  CA  MET A 340      16.851  24.533  14.208  1.00 96.59           C  
ANISOU 2715  CA  MET A 340    10575  14669  11455   -665    994  -1090       C  
ATOM   2716  C   MET A 340      18.024  25.511  14.182  1.00 85.84           C  
ANISOU 2716  C   MET A 340     9138  13522   9954   -947   1040  -1131       C  
ATOM   2717  O   MET A 340      19.180  25.100  14.284  1.00 82.61           O  
ANISOU 2717  O   MET A 340     8525  13396   9467   -950   1067  -1316       O  
ATOM   2718  CB  MET A 340      16.525  24.085  15.642  1.00 97.52           C  
ANISOU 2718  CB  MET A 340    10741  14565  11746   -393    940  -1121       C  
ATOM   2719  CG  MET A 340      16.171  25.208  16.584  1.00103.74           C  
ANISOU 2719  CG  MET A 340    11720  15082  12614   -470    916   -971       C  
ATOM   2720  SD  MET A 340      16.086  24.577  18.293  1.00105.89           S  
ANISOU 2720  SD  MET A 340    12003  15159  13072   -154    860  -1056       S  
ATOM   2721  CE  MET A 340      14.657  23.497  18.235  1.00105.82           C  
ANISOU 2721  CE  MET A 340    12090  14899  13219    158    807   -997       C  
ATOM   2722  N   CYS A 341      17.687  26.796  14.006  1.00 77.51           N  
ANISOU 2722  N   CYS A 341     8252  12331   8868  -1183   1045   -953       N  
ATOM   2723  CA  CYS A 341      18.638  27.880  14.134  1.00 83.30           C  
ANISOU 2723  CA  CYS A 341     8959  13205   9487  -1449   1076   -954       C  
ATOM   2724  C   CYS A 341      18.499  28.492  15.517  1.00 88.10           C  
ANISOU 2724  C   CYS A 341     9694  13573  10206  -1395   1036   -885       C  
ATOM   2725  O   CYS A 341      17.455  28.341  16.162  1.00 90.46           O  
ANISOU 2725  O   CYS A 341    10151  13558  10663  -1209    989   -783       O  
ATOM   2726  CB  CYS A 341      18.442  28.936  13.059  1.00 79.21           C  
ANISOU 2726  CB  CYS A 341     8540  12709   8848  -1757   1105   -810       C  
ATOM   2727  SG  CYS A 341      19.177  28.407  11.486  1.00124.17           S  
ANISOU 2727  SG  CYS A 341    14028  18791  14359  -1895   1168   -939       S  
ATOM   2728  N   LYS A 342      19.567  29.184  15.937  1.00 87.25           N  
ANISOU 2728  N   LYS A 342     9518  13619  10014  -1562   1057   -940       N  
ATOM   2729  CA  LYS A 342      19.602  29.808  17.252  1.00 91.25           C  
ANISOU 2729  CA  LYS A 342    10133  13927  10611  -1531   1023   -884       C  
ATOM   2730  C   LYS A 342      18.678  31.028  17.312  1.00 90.61           C  
ANISOU 2730  C   LYS A 342    10311  13556  10560  -1678    999   -641       C  
ATOM   2731  O   LYS A 342      18.517  31.637  18.370  1.00 85.92           O  
ANISOU 2731  O   LYS A 342     9846  12751  10048  -1656    967   -558       O  
ATOM   2732  CB  LYS A 342      21.040  30.072  17.707  1.00 87.26           C  
ANISOU 2732  CB  LYS A 342     9467  13676  10011  -1643   1049  -1024       C  
ATOM   2733  CG  LYS A 342      21.792  28.833  18.187  1.00 84.78           C  
ANISOU 2733  CG  LYS A 342     8939  13541   9734  -1420   1052  -1256       C  
ATOM   2734  CD  LYS A 342      23.111  29.121  18.894  1.00 79.46           C  
ANISOU 2734  CD  LYS A 342     8136  13052   9003  -1501   1067  -1380       C  
ATOM   2735  CE  LYS A 342      23.733  27.850  19.429  1.00 83.67           C  
ANISOU 2735  CE  LYS A 342     8473  13726   9591  -1258   1063  -1605       C  
ATOM   2736  NZ  LYS A 342      24.739  28.094  20.493  1.00 97.10           N  
ANISOU 2736  NZ  LYS A 342    10103  15486  11302  -1267   1058  -1700       N  
ATOM   2737  N   THR A 343      18.023  31.324  16.184  1.00 96.53           N  
ANISOU 2737  N   THR A 343    11142  14283  11251  -1812   1013   -527       N  
ATOM   2738  CA  THR A 343      17.158  32.483  16.013  1.00115.10           C  
ANISOU 2738  CA  THR A 343    13731  16392  13609  -1981    995   -299       C  
ATOM   2739  C   THR A 343      15.683  32.143  16.272  1.00107.47           C  
ANISOU 2739  C   THR A 343    12949  15068  12815  -1769    950   -163       C  
ATOM   2740  O   THR A 343      14.851  33.050  16.284  1.00 99.65           O  
ANISOU 2740  O   THR A 343    12172  13833  11858  -1873    928     33       O  
ATOM   2741  CB  THR A 343      17.420  33.143  14.647  1.00129.45           C  
ANISOU 2741  CB  THR A 343    15530  18406  15249  -2287   1037   -257       C  
ATOM   2742  OG1 THR A 343      16.551  34.274  14.555  1.00169.20           O  
ANISOU 2742  OG1 THR A 343    20802  23188  20296  -2443   1014    -36       O  
ATOM   2743  CG2 THR A 343      17.174  32.229  13.466  1.00106.40           C  
ANISOU 2743  CG2 THR A 343    12512  15622  12294  -2234   1063   -321       C  
ATOM   2744  N   ASP A 344      15.370  30.847  16.457  1.00100.71           N  
ANISOU 2744  N   ASP A 344    12012  14188  12066  -1479    935   -265       N  
ATOM   2745  CA  ASP A 344      14.002  30.346  16.566  1.00 94.14           C  
ANISOU 2745  CA  ASP A 344    11327  13052  11390  -1263    894   -155       C  
ATOM   2746  C   ASP A 344      13.465  30.490  18.000  1.00 83.62           C  
ANISOU 2746  C   ASP A 344    10138  11406  10229  -1080    844    -84       C  
ATOM   2747  O   ASP A 344      14.243  30.536  18.943  1.00 74.74           O  
ANISOU 2747  O   ASP A 344     8945  10337   9117  -1041    840   -179       O  
ATOM   2748  CB  ASP A 344      13.905  28.938  15.964  1.00 94.57           C  
ANISOU 2748  CB  ASP A 344    11232  13240  11461  -1061    900   -288       C  
ATOM   2749  CG  ASP A 344      14.156  28.891  14.453  1.00 95.28           C  
ANISOU 2749  CG  ASP A 344    11233  13574  11397  -1248    946   -310       C  
ATOM   2750  OD1 ASP A 344      13.928  29.918  13.788  1.00 94.74           O  
ANISOU 2750  OD1 ASP A 344    11279  13470  11249  -1503    961   -171       O  
ATOM   2751  OD2 ASP A 344      14.589  27.828  13.935  1.00 85.94           O1-
ANISOU 2751  OD2 ASP A 344     9865  12616  10170  -1141    965   -467       O1-
ATOM   2752  N   ILE A 345      12.131  30.559  18.181  1.00 76.77           N  
ANISOU 2752  N   ILE A 345     9473  10199   9496   -964    805     85       N  
ATOM   2753  CA  ILE A 345      11.544  30.717  19.513  1.00 83.25           C  
ANISOU 2753  CA  ILE A 345    10445  10705  10484   -790    758    165       C  
ATOM   2754  C   ILE A 345      11.902  29.524  20.377  1.00 81.09           C  
ANISOU 2754  C   ILE A 345    10031  10471  10308   -496    740    -17       C  
ATOM   2755  O   ILE A 345      12.193  29.707  21.550  1.00 82.42           O  
ANISOU 2755  O   ILE A 345    10226  10539  10549   -418    719    -42       O  
ATOM   2756  CB  ILE A 345      10.007  30.865  19.522  1.00 82.64           C  
ANISOU 2756  CB  ILE A 345    10598  10259  10542   -693    720    370       C  
ATOM   2757  CG1 ILE A 345       9.364  30.145  18.327  1.00 98.98           C  
ANISOU 2757  CG1 ILE A 345    12640  12371  12598   -647    728    380       C  
ATOM   2758  CG2 ILE A 345       9.610  32.328  19.634  1.00 74.00           C  
ANISOU 2758  CG2 ILE A 345     9717   8974   9426   -921    714    576       C  
ATOM   2759  CD1 ILE A 345       7.983  29.549  18.578  1.00116.62           C  
ANISOU 2759  CD1 ILE A 345    15017  14284  15009   -394    682    488       C  
ATOM   2760  N   ALA A 346      11.808  28.323  19.794  1.00 75.73           N  
ANISOU 2760  N   ALA A 346     9220   9919   9635   -333    743   -133       N  
ATOM   2761  CA  ALA A 346      12.074  27.092  20.517  1.00 70.70           C  
ANISOU 2761  CA  ALA A 346     8449   9326   9088    -42    720   -311       C  
ATOM   2762  C   ALA A 346      13.457  27.121  21.193  1.00 73.11           C  
ANISOU 2762  C   ALA A 346     8590   9858   9331    -85    739   -487       C  
ATOM   2763  O   ALA A 346      13.628  26.645  22.318  1.00 65.61           O  
ANISOU 2763  O   ALA A 346     7615   8824   8490    116    710   -577       O  
ATOM   2764  CB  ALA A 346      11.912  25.931  19.575  1.00 60.24           C  
ANISOU 2764  CB  ALA A 346     6994   8160   7734     80    727   -407       C  
ATOM   2765  N   PHE A 347      14.453  27.675  20.493  1.00 75.16           N  
ANISOU 2765  N   PHE A 347     8737  10405   9415   -348    788   -538       N  
ATOM   2766  CA  PHE A 347      15.803  27.739  21.010  1.00 74.46           C  
ANISOU 2766  CA  PHE A 347     8486  10551   9253   -412    810   -700       C  
ATOM   2767  C   PHE A 347      15.927  28.859  22.047  1.00 75.13           C  
ANISOU 2767  C   PHE A 347     8715  10453   9379   -511    794   -595       C  
ATOM   2768  O   PHE A 347      16.582  28.680  23.079  1.00 71.06           O  
ANISOU 2768  O   PHE A 347     8137   9951   8913   -416    781   -704       O  
ATOM   2769  CB  PHE A 347      16.833  27.853  19.884  1.00 72.94           C  
ANISOU 2769  CB  PHE A 347     8114  10740   8862   -645    868   -799       C  
ATOM   2770  CG  PHE A 347      18.227  27.973  20.440  1.00 76.50           C  
ANISOU 2770  CG  PHE A 347     8403  11426   9239   -718    890   -958       C  
ATOM   2771  CD1 PHE A 347      18.861  26.866  20.987  1.00 71.71           C  
ANISOU 2771  CD1 PHE A 347     7617  10955   8674   -505    883  -1168       C  
ATOM   2772  CD2 PHE A 347      18.851  29.211  20.540  1.00 77.06           C  
ANISOU 2772  CD2 PHE A 347     8517  11549   9212   -986    910   -888       C  
ATOM   2773  CE1 PHE A 347      20.113  26.994  21.562  1.00 73.90           C  
ANISOU 2773  CE1 PHE A 347     7756  11426   8897   -568    901  -1308       C  
ATOM   2774  CE2 PHE A 347      20.115  29.324  21.097  1.00 73.36           C  
ANISOU 2774  CE2 PHE A 347     7907  11282   8684  -1047    927  -1026       C  
ATOM   2775  CZ  PHE A 347      20.745  28.214  21.601  1.00 73.42           C  
ANISOU 2775  CZ  PHE A 347     7733  11426   8736   -839    923  -1236       C  
ATOM   2776  N   ARG A 348      15.333  30.021  21.755  1.00 71.81           N  
ANISOU 2776  N   ARG A 348     8486   9868   8932   -709    793   -386       N  
ATOM   2777  CA  ARG A 348      15.418  31.141  22.685  1.00 75.27           C  
ANISOU 2777  CA  ARG A 348     9073  10130   9398   -815    775   -271       C  
ATOM   2778  C   ARG A 348      14.633  30.861  23.974  1.00 69.26           C  
ANISOU 2778  C   ARG A 348     8452   9023   8840   -551    723   -218       C  
ATOM   2779  O   ARG A 348      15.083  31.206  25.055  1.00 67.59           O  
ANISOU 2779  O   ARG A 348     8269   8736   8677   -527    706   -235       O  
ATOM   2780  CB  ARG A 348      14.992  32.447  22.017  1.00 73.01           C  
ANISOU 2780  CB  ARG A 348     8953   9766   9021  -1097    785    -65       C  
ATOM   2781  CG  ARG A 348      15.908  32.888  20.887  1.00 73.63           C  
ANISOU 2781  CG  ARG A 348     8899  10186   8892  -1385    836   -118       C  
ATOM   2782  CD  ARG A 348      15.354  34.112  20.195  1.00 72.73           C  
ANISOU 2782  CD  ARG A 348     8962   9973   8699  -1648    840     87       C  
ATOM   2783  NE  ARG A 348      14.059  33.798  19.634  1.00 79.48           N  
ANISOU 2783  NE  ARG A 348     9941  10622   9636  -1552    824    203       N  
ATOM   2784  CZ  ARG A 348      13.378  34.577  18.813  1.00 90.81           C  
ANISOU 2784  CZ  ARG A 348    11520  11964  11018  -1740    827    370       C  
ATOM   2785  NH1 ARG A 348      13.885  35.731  18.418  1.00119.00           N  
ANISOU 2785  NH1 ARG A 348    15126  15645  14443  -2044    845    437       N  
ATOM   2786  NH2 ARG A 348      12.200  34.188  18.367  1.00 83.55           N  
ANISOU 2786  NH2 ARG A 348    10707  10849  10188  -1628    809    467       N  
ATOM   2787  N   LEU A 349      13.469  30.228  23.868  1.00 56.46           N  
ANISOU 2787  N   LEU A 349     6920   7190   7341   -352    695   -153       N  
ATOM   2788  CA  LEU A 349      12.715  29.815  25.041  1.00 54.85           C  
ANISOU 2788  CA  LEU A 349     6834   6674   7335    -79    645   -120       C  
ATOM   2789  C   LEU A 349      13.482  28.757  25.832  1.00 54.16           C  
ANISOU 2789  C   LEU A 349     6567   6708   7302    139    635   -347       C  
ATOM   2790  O   LEU A 349      13.415  28.736  27.059  1.00 59.64           O  
ANISOU 2790  O   LEU A 349     7332   7207   8123    287    602   -353       O  
ATOM   2791  CB  LEU A 349      11.336  29.286  24.613  1.00 58.41           C  
ANISOU 2791  CB  LEU A 349     7398   6904   7890     83    620    -11       C  
ATOM   2792  CG  LEU A 349      10.363  28.939  25.736  1.00 52.84           C  
ANISOU 2792  CG  LEU A 349     6844   5839   7393    356    566     57       C  
ATOM   2793  CD1 LEU A 349      10.019  30.182  26.553  1.00 52.10           C  
ANISOU 2793  CD1 LEU A 349     6970   5474   7353    252    549    241       C  
ATOM   2794  CD2 LEU A 349       9.105  28.305  25.174  1.00 65.17           C  
ANISOU 2794  CD2 LEU A 349     8486   7234   9040    513    544    144       C  
ATOM   2795  N   ALA A 350      14.196  27.860  25.135  1.00 54.65           N  
ANISOU 2795  N   ALA A 350     6402   7089   7273    163    663   -536       N  
ATOM   2796  CA  ALA A 350      15.033  26.875  25.808  1.00 56.72           C  
ANISOU 2796  CA  ALA A 350     6479   7503   7569    347    656   -765       C  
ATOM   2797  C   ALA A 350      16.222  27.556  26.480  1.00 53.69           C  
ANISOU 2797  C   ALA A 350     6036   7240   7123    198    673   -832       C  
ATOM   2798  O   ALA A 350      16.703  27.123  27.536  1.00 47.05           O  
ANISOU 2798  O   ALA A 350     5140   6374   6365    352    651   -956       O  
ATOM   2799  CB  ALA A 350      15.461  25.795  24.854  1.00 51.59           C  
ANISOU 2799  CB  ALA A 350     5612   7159   6831    401    680   -937       C  
ATOM   2800  N   LYS A 351      16.662  28.654  25.873  1.00 61.45           N  
ANISOU 2800  N   LYS A 351     7042   8343   7961   -104    708   -741       N  
ATOM   2801  CA  LYS A 351      17.811  29.400  26.368  1.00 66.76           C  
ANISOU 2801  CA  LYS A 351     7662   9152   8553   -280    726   -787       C  
ATOM   2802  C   LYS A 351      17.500  30.000  27.739  1.00 62.14           C  
ANISOU 2802  C   LYS A 351     7258   8249   8102   -208    685   -685       C  
ATOM   2803  O   LYS A 351      18.401  30.172  28.544  1.00 64.34           O  
ANISOU 2803  O   LYS A 351     7479   8590   8380   -225    683   -772       O  
ATOM   2804  CB  LYS A 351      18.249  30.439  25.321  1.00 65.05           C  
ANISOU 2804  CB  LYS A 351     7440   9129   8148   -621    769   -702       C  
ATOM   2805  CG  LYS A 351      19.624  31.032  25.501  1.00 61.57           C  
ANISOU 2805  CG  LYS A 351     6882   8931   7581   -822    797   -787       C  
ATOM   2806  CD  LYS A 351      20.360  31.261  24.203  1.00 64.84           C  
ANISOU 2806  CD  LYS A 351     7151   9693   7795  -1071    850   -837       C  
ATOM   2807  CE  LYS A 351      19.746  32.223  23.210  1.00 69.01           C  
ANISOU 2807  CE  LYS A 351     7817  10176   8229  -1307    864   -645       C  
ATOM   2808  NZ  LYS A 351      19.761  33.616  23.728  1.00 70.04           N  
ANISOU 2808  NZ  LYS A 351     8123  10156   8335  -1502    849   -477       N  
ATOM   2809  N   SER A 352      16.228  30.323  27.983  1.00 63.87           N  
ANISOU 2809  N   SER A 352     7701   8130   8437   -132    652   -496       N  
ATOM   2810  CA  SER A 352      15.782  30.966  29.210  1.00 73.10           C  
ANISOU 2810  CA  SER A 352     9070   8969   9734    -71    613   -368       C  
ATOM   2811  C   SER A 352      15.301  29.936  30.219  1.00 69.75           C  
ANISOU 2811  C   SER A 352     8659   8342   9503    266    571   -452       C  
ATOM   2812  O   SER A 352      15.550  30.093  31.411  1.00 75.09           O  
ANISOU 2812  O   SER A 352     9390   8870  10271    350    546   -469       O  
ATOM   2813  CB  SER A 352      14.697  31.993  28.964  1.00 76.60           C  
ANISOU 2813  CB  SER A 352     9760   9151  10194   -191    600   -108       C  
ATOM   2814  OG  SER A 352      15.202  33.095  28.213  1.00 95.74           O  
ANISOU 2814  OG  SER A 352    12194  11741  12443   -516    633    -25       O  
ATOM   2815  N   THR A 353      14.563  28.928  29.739  1.00 70.17           N  
ANISOU 2815  N   THR A 353     8675   8371   9615    455    560   -491       N  
ATOM   2816  CA  THR A 353      13.980  27.934  30.624  1.00 64.75           C  
ANISOU 2816  CA  THR A 353     8012   7479   9111    780    516   -559       C  
ATOM   2817  C   THR A 353      15.071  27.034  31.189  1.00 63.58           C  
ANISOU 2817  C   THR A 353     7652   7538   8968    908    516   -815       C  
ATOM   2818  O   THR A 353      14.992  26.680  32.363  1.00 63.26           O  
ANISOU 2818  O   THR A 353     7663   7322   9050   1095    474   -853       O  
ATOM   2819  CB  THR A 353      12.876  27.107  29.959  1.00 53.65           C  
ANISOU 2819  CB  THR A 353     6630   5989   7766    949    500   -525       C  
ATOM   2820  OG1 THR A 353      11.916  28.040  29.488  1.00 48.55           O  
ANISOU 2820  OG1 THR A 353     6187   5142   7116    812    501   -283       O  
ATOM   2821  CG2 THR A 353      12.202  26.184  30.940  1.00 41.40           C  
ANISOU 2821  CG2 THR A 353     5208   4371   6153   1160    365   -487       C  
ATOM   2822  N   LEU A 354      16.074  26.692  30.360  1.00 58.91           N  
ANISOU 2822  N   LEU A 354     6839   7322   8223    792    556   -970       N  
ATOM   2823  CA  LEU A 354      17.189  25.857  30.796  1.00 58.63           C  
ANISOU 2823  CA  LEU A 354     6589   7514   8175    891    560  -1219       C  
ATOM   2824  C   LEU A 354      18.028  26.561  31.859  1.00 59.73           C  
ANISOU 2824  C   LEU A 354     6752   7614   8328    809    557  -1238       C  
ATOM   2825  O   LEU A 354      18.726  25.894  32.627  1.00 51.36           O  
ANISOU 2825  O   LEU A 354     5573   6620   7320    947    543  -1421       O  
ATOM   2826  CB  LEU A 354      18.039  25.470  29.587  1.00 56.81           C  
ANISOU 2826  CB  LEU A 354     6131   7689   7765    756    608  -1355       C  
ATOM   2827  CG  LEU A 354      17.460  24.334  28.755  1.00 59.34           C  
ANISOU 2827  CG  LEU A 354     6366   8092   8090    919    604  -1421       C  
ATOM   2828  CD1 LEU A 354      18.388  24.039  27.611  1.00 68.23           C  
ANISOU 2828  CD1 LEU A 354     7271   9619   9033    769    654  -1553       C  
ATOM   2829  CD2 LEU A 354      17.241  23.077  29.596  1.00 59.64           C  
ANISOU 2829  CD2 LEU A 354     6532   7959   8169   1076    489  -1329       C  
ATOM   2830  N   THR A 355      17.894  27.898  31.915  1.00 62.88           N  
ANISOU 2830  N   THR A 355     7317   7887   8686    591    565  -1042       N  
ATOM   2831  CA  THR A 355      18.583  28.733  32.884  1.00 54.02           C  
ANISOU 2831  CA  THR A 355     6254   6698   7573    490    559  -1018       C  
ATOM   2832  C   THR A 355      17.828  28.724  34.208  1.00 56.19           C  
ANISOU 2832  C   THR A 355     6716   6585   8048    701    508   -943       C  
ATOM   2833  O   THR A 355      18.435  28.541  35.258  1.00 61.41           O  
ANISOU 2833  O   THR A 355     7347   7205   8783    793    489  -1048       O  
ATOM   2834  CB  THR A 355      18.815  30.145  32.329  1.00 57.00           C  
ANISOU 2834  CB  THR A 355     6721   7131   7807    162    588   -847       C  
ATOM   2835  OG1 THR A 355      19.582  30.100  31.113  1.00 58.65           O  
ANISOU 2835  OG1 THR A 355     6743   7713   7830    -29    637   -933       O  
ATOM   2836  CG2 THR A 355      19.488  31.063  33.324  1.00 51.81           C  
ANISOU 2836  CG2 THR A 355     6139   6392   7153     53    577   -802       C  
ATOM   2837  N   LEU A 356      16.498  28.878  34.155  1.00 63.61           N  
ANISOU 2837  N   LEU A 356     7848   7239   9082    784    484   -766       N  
ATOM   2838  CA  LEU A 356      15.673  28.994  35.354  1.00 56.78           C  
ANISOU 2838  CA  LEU A 356     7197   6020   8356    947    421   -642       C  
ATOM   2839  C   LEU A 356      15.589  27.683  36.129  1.00 52.68           C  
ANISOU 2839  C   LEU A 356     6721   5704   7593   1073    327   -608       C  
ATOM   2840  O   LEU A 356      15.522  27.714  37.355  1.00 51.17           O  
ANISOU 2840  O   LEU A 356     6688   5488   7268   1085    283   -500       O  
ATOM   2841  CB  LEU A 356      14.291  29.531  34.976  1.00 53.23           C  
ANISOU 2841  CB  LEU A 356     6969   5399   7858    893    365   -391       C  
ATOM   2842  CG  LEU A 356      14.331  31.004  34.586  1.00 65.64           C  
ANISOU 2842  CG  LEU A 356     8661   6823   9458    649    445   -222       C  
ATOM   2843  CD1 LEU A 356      13.050  31.427  33.924  1.00 72.37           C  
ANISOU 2843  CD1 LEU A 356     9686   7487  10323    610    438    -10       C  
ATOM   2844  CD2 LEU A 356      14.665  31.910  35.770  1.00 71.62           C  
ANISOU 2844  CD2 LEU A 356     9556   7393  10265    594    426   -141       C  
ATOM   2845  N   ILE A 357      15.607  26.551  35.418  1.00 43.81           N  
ANISOU 2845  N   ILE A 357     5473   4760   6412   1126    358   -666       N  
ATOM   2846  CA  ILE A 357      15.421  25.277  36.092  1.00 42.84           C  
ANISOU 2846  CA  ILE A 357     5370   4716   6193   1150    349   -591       C  
ATOM   2847  C   ILE A 357      16.542  25.016  37.100  1.00 52.25           C  
ANISOU 2847  C   ILE A 357     6470   5967   7416   1125    324   -697       C  
ATOM   2848  O   ILE A 357      16.256  24.756  38.269  1.00 68.85           O  
ANISOU 2848  O   ILE A 357     8619   7996   9544   1111    261   -660       O  
ATOM   2849  CB  ILE A 357      15.211  24.103  35.119  1.00 37.67           C  
ANISOU 2849  CB  ILE A 357     4588   4189   5535   1165    350   -644       C  
ATOM   2850  CG1 ILE A 357      13.900  24.257  34.337  1.00 33.31           C  
ANISOU 2850  CG1 ILE A 357     4146   3551   4958   1187    362   -514       C  
ATOM   2851  CG2 ILE A 357      15.326  22.772  35.866  1.00 30.26           C  
ANISOU 2851  CG2 ILE A 357     3567   3315   4617   1154    253   -721       C  
ATOM   2852  CD1 ILE A 357      13.725  23.277  33.219  1.00 31.26           C  
ANISOU 2852  CD1 ILE A 357     3772   3409   4698   1199    374   -560       C  
ATOM   2853  N   PRO A 358      17.847  25.045  36.733  1.00 55.08           N  
ANISOU 2853  N   PRO A 358     6658   6484   7786   1110    354   -873       N  
ATOM   2854  CA  PRO A 358      18.877  24.755  37.722  1.00 54.01           C  
ANISOU 2854  CA  PRO A 358     6469   6406   7647   1086    327   -945       C  
ATOM   2855  C   PRO A 358      19.043  25.918  38.688  1.00 63.52           C  
ANISOU 2855  C   PRO A 358     7783   7455   8897   1067    327   -903       C  
ATOM   2856  O   PRO A 358      19.657  25.773  39.744  1.00 70.18           O  
ANISOU 2856  O   PRO A 358     8625   8294   9745   1050    295   -921       O  
ATOM   2857  CB  PRO A 358      20.118  24.536  36.855  1.00 50.76           C  
ANISOU 2857  CB  PRO A 358     5784   6257   7247   1054    333  -1222       C  
ATOM   2858  CG  PRO A 358      19.885  25.417  35.685  1.00 47.24           C  
ANISOU 2858  CG  PRO A 358     5233   5869   6847   1029    400  -1338       C  
ATOM   2859  CD  PRO A 358      18.406  25.311  35.398  1.00 47.16           C  
ANISOU 2859  CD  PRO A 358     5418   5663   6839   1086    387  -1114       C  
ATOM   2860  N   LEU A 359      18.485  27.076  38.313  1.00 67.22           N  
ANISOU 2860  N   LEU A 359     8326   7773   9443   1052    338   -876       N  
ATOM   2861  CA  LEU A 359      18.593  28.264  39.140  1.00 68.44           C  
ANISOU 2861  CA  LEU A 359     8605   7738   9661   1003    324   -821       C  
ATOM   2862  C   LEU A 359      17.630  28.154  40.322  1.00 69.37           C  
ANISOU 2862  C   LEU A 359     8976   7768   9613   1028    274   -577       C  
ATOM   2863  O   LEU A 359      17.950  28.586  41.424  1.00 85.05           O  
ANISOU 2863  O   LEU A 359    11014   9685  11617    997    246   -554       O  
ATOM   2864  CB  LEU A 359      18.267  29.466  38.257  1.00 70.89           C  
ANISOU 2864  CB  LEU A 359     8919   7867  10149    914    380   -840       C  
ATOM   2865  CG  LEU A 359      18.701  30.831  38.776  1.00 75.98           C  
ANISOU 2865  CG  LEU A 359     9668   8327  10876    756    412   -772       C  
ATOM   2866  CD1 LEU A 359      20.222  30.951  38.685  1.00 74.39           C  
ANISOU 2866  CD1 LEU A 359     9272   8452  10540    591    441   -925       C  
ATOM   2867  CD2 LEU A 359      18.025  31.926  37.947  1.00 76.21           C  
ANISOU 2867  CD2 LEU A 359     9850   8299  10809    538    428   -531       C  
ATOM   2868  N   LEU A 360      16.447  27.570  40.085  1.00 63.21           N  
ANISOU 2868  N   LEU A 360     8222   6977   8817   1049    249   -499       N  
ATOM   2869  CA  LEU A 360      15.383  27.541  41.072  1.00 58.37           C  
ANISOU 2869  CA  LEU A 360     7705   6282   8190   1033    200   -390       C  
ATOM   2870  C   LEU A 360      15.249  26.164  41.703  1.00 56.06           C  
ANISOU 2870  C   LEU A 360     7294   6072   7936   1043    183   -435       C  
ATOM   2871  O   LEU A 360      14.689  26.081  42.778  1.00 65.88           O  
ANISOU 2871  O   LEU A 360     8580   7273   9180   1024    155   -383       O  
ATOM   2872  CB  LEU A 360      14.063  27.935  40.416  1.00 58.02           C  
ANISOU 2872  CB  LEU A 360     7760   6193   8093   1008    154   -292       C  
ATOM   2873  CG  LEU A 360      13.695  29.418  40.371  1.00 70.43           C  
ANISOU 2873  CG  LEU A 360     9452   7640   9666    921     67   -220       C  
ATOM   2874  CD1 LEU A 360      14.667  30.232  39.541  1.00 87.49           C  
ANISOU 2874  CD1 LEU A 360    11628   9750  11863    885     82   -260       C  
ATOM   2875  CD2 LEU A 360      12.322  29.567  39.737  1.00 92.86           C  
ANISOU 2875  CD2 LEU A 360    12322  10449  12513    878      3   -148       C  
ATOM   2876  N   CYS A 361      15.746  25.099  41.065  1.00 55.68           N  
ANISOU 2876  N   CYS A 361     7099   6146   7910   1062    174   -546       N  
ATOM   2877  CA  CYS A 361      15.491  23.751  41.556  1.00 54.95           C  
ANISOU 2877  CA  CYS A 361     6923   6126   7832   1060     98   -603       C  
ATOM   2878  C   CYS A 361      16.719  23.069  42.168  1.00 60.14           C  
ANISOU 2878  C   CYS A 361     7456   6882   8512   1051     33   -750       C  
ATOM   2879  O   CYS A 361      16.611  21.950  42.685  1.00 61.83           O  
ANISOU 2879  O   CYS A 361     7613   7155   8723   1046    -58   -813       O  
ATOM   2880  CB  CYS A 361      14.832  22.865  40.503  1.00 56.40           C  
ANISOU 2880  CB  CYS A 361     7062   6372   7994   1081     87   -614       C  
ATOM   2881  SG  CYS A 361      13.043  22.759  40.768  1.00 93.47           S  
ANISOU 2881  SG  CYS A 361    11869  10977  12668   1071     87   -469       S  
ATOM   2882  N   THR A 362      17.879  23.738  42.120  1.00 65.41           N  
ANISOU 2882  N   THR A 362     8087   7573   9194   1045     72   -813       N  
ATOM   2883  CA  THR A 362      19.119  23.108  42.557  1.00 55.90           C  
ANISOU 2883  CA  THR A 362     6753   6483   8004   1033     16   -967       C  
ATOM   2884  C   THR A 362      19.161  22.945  44.076  1.00 55.12           C  
ANISOU 2884  C   THR A 362     6681   6328   7934   1009    -53   -954       C  
ATOM   2885  O   THR A 362      19.533  21.884  44.583  1.00 54.91           O  
ANISOU 2885  O   THR A 362     6567   6387   7909   1002   -149  -1056       O  
ATOM   2886  CB  THR A 362      20.348  23.802  41.964  1.00 56.58           C  
ANISOU 2886  CB  THR A 362     6769   6644   8084   1026     89  -1056       C  
ATOM   2887  OG1 THR A 362      21.379  22.819  41.979  1.00 57.53           O  
ANISOU 2887  OG1 THR A 362     6732   6933   8194   1014     26  -1227       O  
ATOM   2888  CG2 THR A 362      20.778  25.040  42.717  1.00 57.68           C  
ANISOU 2888  CG2 THR A 362     6998   6672   8247   1005    137  -1001       C  
ATOM   2889  N   HIS A 363      18.778  24.011  44.785  1.00 54.13           N  
ANISOU 2889  N   HIS A 363     6679   6068   7821    996     -8   -830       N  
ATOM   2890  CA  HIS A 363      18.819  24.035  46.237  1.00 56.89           C  
ANISOU 2890  CA  HIS A 363     7057   6367   8192    971    -56   -807       C  
ATOM   2891  C   HIS A 363      17.965  22.914  46.829  1.00 60.58           C  
ANISOU 2891  C   HIS A 363     7508   6861   8648    969   -142   -808       C  
ATOM   2892  O   HIS A 363      18.374  22.269  47.795  1.00 63.23           O  
ANISOU 2892  O   HIS A 363     7788   7235   9000    953   -222   -876       O  
ATOM   2893  CB  HIS A 363      18.365  25.406  46.756  1.00 66.83           C  
ANISOU 2893  CB  HIS A 363     8464   7485   9442    957      8   -665       C  
ATOM   2894  CG  HIS A 363      18.403  25.503  48.246  1.00 87.26           C  
ANISOU 2894  CG  HIS A 363    11079  10030  12046    933    -30   -640       C  
ATOM   2895  ND1 HIS A 363      17.296  25.240  49.039  1.00103.65           N  
ANISOU 2895  ND1 HIS A 363    13205  12074  14104    925    -55   -567       N  
ATOM   2896  CD2 HIS A 363      19.416  25.765  49.096  1.00 84.30           C  
ANISOU 2896  CD2 HIS A 363    10676   9652  11703    914    -48   -688       C  
ATOM   2897  CE1 HIS A 363      17.622  25.362  50.310  1.00 99.34           C  
ANISOU 2897  CE1 HIS A 363    12662  11507  13575    905    -86   -569       C  
ATOM   2898  NE2 HIS A 363      18.916  25.685  50.365  1.00 90.81           N  
ANISOU 2898  NE2 HIS A 363    11538  10439  12527    898    -84   -638       N  
ATOM   2899  N   GLU A 364      16.757  22.724  46.281  1.00 57.62           N  
ANISOU 2899  N   GLU A 364     7187   6463   8243    981   -124   -730       N  
ATOM   2900  CA  GLU A 364      15.805  21.788  46.846  1.00 59.99           C  
ANISOU 2900  CA  GLU A 364     7490   6779   8523    974   -194   -720       C  
ATOM   2901  C   GLU A 364      16.345  20.358  46.773  1.00 63.92           C  
ANISOU 2901  C   GLU A 364     7871   7404   9013    979   -308   -868       C  
ATOM   2902  O   GLU A 364      16.139  19.550  47.706  1.00 59.54           O  
ANISOU 2902  O   GLU A 364     7296   6876   8449    964   -399   -906       O  
ATOM   2903  CB  GLU A 364      14.499  21.907  46.075  1.00 67.34           C  
ANISOU 2903  CB  GLU A 364     8493   7671   9422    986   -143   -618       C  
ATOM   2904  CG  GLU A 364      13.376  21.162  46.748  1.00 89.11           C  
ANISOU 2904  CG  GLU A 364    11272  10431  12155    975   -197   -590       C  
ATOM   2905  CD  GLU A 364      12.947  21.754  48.082  1.00 98.82           C  
ANISOU 2905  CD  GLU A 364    12567  11591  13389    951   -183   -519       C  
ATOM   2906  OE1 GLU A 364      13.095  22.998  48.266  1.00 78.88           O  
ANISOU 2906  OE1 GLU A 364    10111   8987  10871    945   -106   -443       O  
ATOM   2907  OE2 GLU A 364      12.410  20.975  48.921  1.00 99.99           O1-
ANISOU 2907  OE2 GLU A 364    12703  11767  13523    938   -253   -541       O1-
ATOM   2908  N   VAL A 365      17.075  20.088  45.678  1.00 62.15           N  
ANISOU 2908  N   VAL A 365     7570   7263   8782    998   -303   -958       N  
ATOM   2909  CA  VAL A 365      17.588  18.754  45.402  1.00 65.76           C  
ANISOU 2909  CA  VAL A 365     7917   7856   9212   1005   -409  -1106       C  
ATOM   2910  C   VAL A 365      18.840  18.474  46.234  1.00 69.04           C  
ANISOU 2910  C   VAL A 365     8246   8333   9653    985   -477  -1227       C  
ATOM   2911  O   VAL A 365      19.016  17.366  46.743  1.00 78.71           O  
ANISOU 2911  O   VAL A 365     9412   9636  10860    976   -595  -1323       O  
ATOM   2912  CB  VAL A 365      17.854  18.524  43.902  1.00 59.45           C  
ANISOU 2912  CB  VAL A 365     7060   7145   8383   1031   -378  -1165       C  
ATOM   2913  CG1 VAL A 365      18.492  17.162  43.680  1.00 47.11           C  
ANISOU 2913  CG1 VAL A 365     5383   5738   6779   1036   -495  -1331       C  
ATOM   2914  CG2 VAL A 365      16.575  18.633  43.086  1.00 60.82           C  
ANISOU 2914  CG2 VAL A 365     7312   7263   8532   1050   -325  -1050       C  
ATOM   2915  N   ILE A 366      19.716  19.474  46.350  1.00 58.11           N  
ANISOU 2915  N   ILE A 366     6854   6917   8308    976   -406  -1225       N  
ATOM   2916  CA  ILE A 366      20.986  19.290  47.036  1.00 60.53           C  
ANISOU 2916  CA  ILE A 366     7071   7286   8642    954   -458  -1343       C  
ATOM   2917  C   ILE A 366      20.746  18.984  48.514  1.00 55.36           C  
ANISOU 2917  C   ILE A 366     6443   6583   8009    931   -535  -1320       C  
ATOM   2918  O   ILE A 366      21.280  18.017  49.039  1.00 60.88           O  
ANISOU 2918  O   ILE A 366     7058   7367   8706    917   -646  -1436       O  
ATOM   2919  CB  ILE A 366      21.916  20.498  46.778  1.00 61.63           C  
ANISOU 2919  CB  ILE A 366     7204   7400   8810    948   -353  -1341       C  
ATOM   2920  CG1 ILE A 366      22.449  20.418  45.338  1.00 54.22           C  
ANISOU 2920  CG1 ILE A 366     6184   6581   7836    963   -305  -1430       C  
ATOM   2921  CG2 ILE A 366      23.030  20.582  47.813  1.00 58.02           C  
ANISOU 2921  CG2 ILE A 366     6692   6960   8394    920   -392  -1416       C  
ATOM   2922  CD1 ILE A 366      23.069  21.670  44.791  1.00 47.40           C  
ANISOU 2922  CD1 ILE A 366     5330   5700   6980    959   -181  -1412       C  
ATOM   2923  N   PHE A 367      19.921  19.795  49.170  1.00 54.09           N  
ANISOU 2923  N   PHE A 367     6396   6295   7862    925   -480  -1175       N  
ATOM   2924  CA  PHE A 367      19.630  19.577  50.573  1.00 64.55           C  
ANISOU 2924  CA  PHE A 367     7745   7582   9199    902   -541  -1148       C  
ATOM   2925  C   PHE A 367      18.292  18.857  50.764  1.00 79.13           C  
ANISOU 2925  C   PHE A 367     9639   9423  11004    904   -590  -1098       C  
ATOM   2926  O   PHE A 367      17.466  19.310  51.540  1.00 87.00           O  
ANISOU 2926  O   PHE A 367    10718  10340  11997    894   -561   -994       O  
ATOM   2927  CB  PHE A 367      19.592  20.938  51.261  1.00 64.69           C  
ANISOU 2927  CB  PHE A 367     7856   7479   9245    891   -450  -1029       C  
ATOM   2928  CG  PHE A 367      20.861  21.738  51.131  1.00 69.20           C  
ANISOU 2928  CG  PHE A 367     8396   8044   9853    886   -398  -1069       C  
ATOM   2929  CD1 PHE A 367      21.958  21.474  51.942  1.00 64.92           C  
ANISOU 2929  CD1 PHE A 367     7773   7545   9347    865   -458  -1164       C  
ATOM   2930  CD2 PHE A 367      20.963  22.754  50.198  1.00 68.05           C  
ANISOU 2930  CD2 PHE A 367     8300   7853   9702    899   -291  -1015       C  
ATOM   2931  CE1 PHE A 367      23.111  22.233  51.844  1.00 60.80           C  
ANISOU 2931  CE1 PHE A 367     7225   7020   8856    857   -405  -1202       C  
ATOM   2932  CE2 PHE A 367      22.125  23.510  50.111  1.00 66.47           C  
ANISOU 2932  CE2 PHE A 367     8077   7651   9529    891   -242  -1057       C  
ATOM   2933  CZ  PHE A 367      23.191  23.254  50.932  1.00 58.61           C  
ANISOU 2933  CZ  PHE A 367     7002   6698   8568    869   -296  -1150       C  
ATOM   2934  N   ALA A 368      18.076  17.735  50.064  1.00 91.29           N  
ANISOU 2934  N   ALA A 368    11128  11055  12504    918   -662  -1178       N  
ATOM   2935  CA  ALA A 368      16.745  17.156  49.971  1.00 81.19           C  
ANISOU 2935  CA  ALA A 368     9904   9767  11177    924   -688  -1122       C  
ATOM   2936  C   ALA A 368      16.200  16.750  51.341  1.00 90.34           C  
ANISOU 2936  C   ALA A 368    11086  10909  12330    899   -759  -1105       C  
ATOM   2937  O   ALA A 368      15.072  17.123  51.664  1.00112.28           O  
ANISOU 2937  O   ALA A 368    13951  13620  15093    895   -712   -996       O  
ATOM   2938  CB  ALA A 368      16.690  16.019  48.985  1.00 81.47           C  
ANISOU 2938  CB  ALA A 368     9884   9909  11164    943   -759  -1216       C  
ATOM   2939  N   PHE A 369      16.965  15.997  52.146  1.00 78.50           N  
ANISOU 2939  N   PHE A 369     9509   9476  10841    881   -870  -1215       N  
ATOM   2940  CA  PHE A 369      16.401  15.492  53.400  1.00 77.05           C  
ANISOU 2940  CA  PHE A 369     9342   9288  10645    859   -947  -1208       C  
ATOM   2941  C   PHE A 369      17.155  16.027  54.625  1.00 84.25           C  
ANISOU 2941  C   PHE A 369    10235  10164  11610    835   -950  -1208       C  
ATOM   2942  O   PHE A 369      17.363  15.320  55.609  1.00 71.01           O  
ANISOU 2942  O   PHE A 369     8514   8531   9936    814  -1054  -1272       O  
ATOM   2943  CB  PHE A 369      16.297  13.961  53.398  1.00 71.57           C  
ANISOU 2943  CB  PHE A 369     8587   8704   9900    856  -1095  -1325       C  
ATOM   2944  CG  PHE A 369      15.327  13.398  52.396  1.00 63.95           C  
ANISOU 2944  CG  PHE A 369     7660   7767   8872    878  -1097  -1308       C  
ATOM   2945  CD1 PHE A 369      13.982  13.259  52.709  1.00 71.43           C  
ANISOU 2945  CD1 PHE A 369     8684   8676   9779    874  -1090  -1226       C  
ATOM   2946  CD2 PHE A 369      15.751  13.048  51.120  1.00 67.25           C  
ANISOU 2946  CD2 PHE A 369     8036   8250   9268    903  -1099  -1373       C  
ATOM   2947  CE1 PHE A 369      13.080  12.780  51.765  1.00 81.93           C  
ANISOU 2947  CE1 PHE A 369    10051  10027  11052    893  -1085  -1205       C  
ATOM   2948  CE2 PHE A 369      14.852  12.576  50.173  1.00 66.75           C  
ANISOU 2948  CE2 PHE A 369     8010   8208   9145    924  -1094  -1350       C  
ATOM   2949  CZ  PHE A 369      13.517  12.442  50.496  1.00 76.26           C  
ANISOU 2949  CZ  PHE A 369     9293   9367  10313    919  -1087  -1264       C  
ATOM   2950  N   VAL A 370      17.529  17.309  54.570  1.00 92.17           N  
ANISOU 2950  N   VAL A 370    11281  11088  12654    837   -835  -1132       N  
ATOM   2951  CA  VAL A 370      18.230  17.981  55.646  1.00 87.27           C  
ANISOU 2951  CA  VAL A 370    10657  10421  12079    818   -819  -1117       C  
ATOM   2952  C   VAL A 370      17.275  19.007  56.253  1.00 89.78           C  
ANISOU 2952  C   VAL A 370    11089  10634  12388    815   -726   -970       C  
ATOM   2953  O   VAL A 370      16.729  19.852  55.546  1.00 80.27           O  
ANISOU 2953  O   VAL A 370     9961   9368  11170    830   -621   -875       O  
ATOM   2954  CB  VAL A 370      19.545  18.604  55.134  1.00 69.20           C  
ANISOU 2954  CB  VAL A 370     8321   8137   9836    822   -771  -1163       C  
ATOM   2955  N   MET A 371      17.042  18.891  57.569  1.00111.41           N  
ANISOU 2955  N   MET A 371    13839  13361  15131    795   -770   -956       N  
ATOM   2956  CA  MET A 371      16.063  19.734  58.252  1.00107.40           C  
ANISOU 2956  CA  MET A 371    13433  12771  14603    792   -694   -833       C  
ATOM   2957  C   MET A 371      16.594  21.160  58.459  1.00106.58           C  
ANISOU 2957  C   MET A 371    13387  12583  14526    793   -589   -757       C  
ATOM   2958  O   MET A 371      15.854  22.108  58.201  1.00 98.27           O  
ANISOU 2958  O   MET A 371    12428  11460  13450    802   -489   -650       O  
ATOM   2959  CB  MET A 371      15.549  19.110  59.559  1.00 84.16           C  
ANISOU 2959  CB  MET A 371    10483   9849  11646    772   -774   -847       C  
ATOM   2960  N   ASP A 372      17.861  21.293  58.902  1.00100.30           N  
ANISOU 2960  N   ASP A 372    12535  11797  13776    782   -616   -816       N  
ATOM   2961  CA  ASP A 372      18.668  22.517  58.908  1.00100.11           C  
ANISOU 2961  CA  ASP A 372    12551  11708  13779    782   -531   -771       C  
ATOM   2962  C   ASP A 372      19.764  22.414  59.982  1.00103.59           C  
ANISOU 2962  C   ASP A 372    12931  12165  14265    762   -589   -834       C  
ATOM   2963  O   ASP A 372      19.476  22.757  61.158  1.00 89.00           O  
ANISOU 2963  O   ASP A 372    11126  10278  12411    751   -588   -783       O  
ATOM   2964  CB  ASP A 372      17.883  23.830  59.056  1.00 85.67           C  
ANISOU 2964  CB  ASP A 372    10853   9781  11917    789   -419   -634       C  
ATOM   2965  N   ARG A 380      29.744  29.841  58.960  1.00111.42           N  
ANISOU 2965  N   ARG A 380    14019  12854  15461    673   -167   -946       N  
ATOM   2966  CA  ARG A 380      28.869  29.271  57.906  1.00 95.73           C  
ANISOU 2966  CA  ARG A 380    12005  10916  13451    698   -163   -958       C  
ATOM   2967  C   ARG A 380      27.535  30.009  57.893  1.00115.80           C  
ANISOU 2967  C   ARG A 380    14709  13359  15929    707   -123   -801       C  
ATOM   2968  O   ARG A 380      26.830  29.962  56.893  1.00118.81           O  
ANISOU 2968  O   ARG A 380    15115  13747  16281    723    -95   -780       O  
ATOM   2969  CB  ARG A 380      28.664  27.780  58.179  1.00 83.18           C  
ANISOU 2969  CB  ARG A 380    10270   9438  11896    709   -254  -1049       C  
ATOM   2970  N   PHE A 381      27.202  30.683  59.005  1.00145.74           N  
ANISOU 2970  N   PHE A 381    18606  17071  19697    695   -120   -698       N  
ATOM   2971  CA  PHE A 381      25.925  31.362  59.200  1.00148.53           C  
ANISOU 2971  CA  PHE A 381    19102  17350  19983    700    -88   -562       C  
ATOM   2972  C   PHE A 381      25.697  32.399  58.102  1.00149.42           C  
ANISOU 2972  C   PHE A 381    19338  17392  20042    688    -25   -496       C  
ATOM   2973  O   PHE A 381      24.684  32.342  57.400  1.00126.35           O  
ANISOU 2973  O   PHE A 381    16454  14469  17084    704     -8   -451       O  
ATOM   2974  CB  PHE A 381      25.863  32.011  60.587  1.00144.53           C  
ANISOU 2974  CB  PHE A 381    18676  16783  19456    685    -90   -487       C  
ATOM   2975  N   ILE A 382      26.683  33.299  57.953  1.00163.29           N  
ANISOU 2975  N   ILE A 382    21158  19091  21794    653     -2   -497       N  
ATOM   2976  CA  ILE A 382      26.683  34.418  57.020  1.00159.41           C  
ANISOU 2976  CA  ILE A 382    20807  18515  21246    613     36   -437       C  
ATOM   2977  C   ILE A 382      26.545  33.888  55.595  1.00158.08           C  
ANISOU 2977  C   ILE A 382    20574  18400  21089    629     51   -505       C  
ATOM   2978  O   ILE A 382      25.875  34.507  54.773  1.00156.45           O  
ANISOU 2978  O   ILE A 382    20477  18139  20828    610     67   -434       O  
ATOM   2979  CB  ILE A 382      27.977  35.259  57.162  1.00144.86           C  
ANISOU 2979  CB  ILE A 382    19023  16611  19406    551     42   -456       C  
ATOM   2980  CG1 ILE A 382      28.463  35.361  58.614  1.00137.26           C  
ANISOU 2980  CG1 ILE A 382    18054  15637  18463    550     23   -441       C  
ATOM   2981  CG2 ILE A 382      27.825  36.630  56.510  1.00136.60           C  
ANISOU 2981  CG2 ILE A 382    18174  15449  18280    468     52   -355       C  
ATOM   2982  CD1 ILE A 382      29.892  35.844  58.784  1.00103.43           C  
ANISOU 2982  CD1 ILE A 382    13780  11320  14200    495     23   -494       C  
ATOM   2983  N   LYS A 383      27.224  32.769  55.321  1.00156.06           N  
ANISOU 2983  N   LYS A 383    20137  18259  20898    659     39   -649       N  
ATOM   2984  CA  LYS A 383      27.293  32.211  53.981  1.00153.83           C  
ANISOU 2984  CA  LYS A 383    19767  18056  20624    676     61   -745       C  
ATOM   2985  C   LYS A 383      25.928  31.639  53.596  1.00137.14           C  
ANISOU 2985  C   LYS A 383    17652  15966  18489    718     52   -686       C  
ATOM   2986  O   LYS A 383      25.507  31.792  52.459  1.00136.32           O  
ANISOU 2986  O   LYS A 383    17580  15860  18356    723     83   -679       O  
ATOM   2987  CB  LYS A 383      28.420  31.175  53.882  1.00150.52           C  
ANISOU 2987  CB  LYS A 383    19145  17781  20264    689     44   -928       C  
ATOM   2988  N   LEU A 384      25.247  30.961  54.532  1.00 99.40           N  
ANISOU 2988  N   LEU A 384    12836  11211  13721    740      9   -653       N  
ATOM   2989  CA  LEU A 384      23.924  30.436  54.211  1.00 86.97           C  
ANISOU 2989  CA  LEU A 384    11270   9655  12120    768      2   -600       C  
ATOM   2990  C   LEU A 384      22.862  31.536  54.240  1.00 84.74           C  
ANISOU 2990  C   LEU A 384    11166   9267  11766    756     37   -450       C  
ATOM   2991  O   LEU A 384      21.812  31.381  53.638  1.00 79.08           O  
ANISOU 2991  O   LEU A 384    10479   8553  11015    774     47   -404       O  
ATOM   2992  CB  LEU A 384      23.547  29.212  55.051  1.00 70.17           C  
ANISOU 2992  CB  LEU A 384     9038   7601  10021    782    -66   -642       C  
ATOM   2993  CG  LEU A 384      23.117  28.022  54.181  1.00 66.71           C  
ANISOU 2993  CG  LEU A 384     8496   7259   9592    807    -97   -714       C  
ATOM   2994  CD1 LEU A 384      23.452  26.685  54.820  1.00 66.03           C  
ANISOU 2994  CD1 LEU A 384     8271   7271   9547    805   -192   -824       C  
ATOM   2995  CD2 LEU A 384      21.656  28.086  53.736  1.00 71.99           C  
ANISOU 2995  CD2 LEU A 384     9248   7894  10211    822    -72   -614       C  
ATOM   2996  N   PHE A 385      23.168  32.688  54.858  1.00 97.17           N  
ANISOU 2996  N   PHE A 385    12860  10751  13309    721     49   -381       N  
ATOM   2997  CA  PHE A 385      22.281  33.840  54.809  1.00 80.00           C  
ANISOU 2997  CA  PHE A 385    10859   8485  11053    697     64   -255       C  
ATOM   2998  C   PHE A 385      22.130  34.379  53.383  1.00 86.85           C  
ANISOU 2998  C   PHE A 385    11787   9327  11886    667     65   -234       C  
ATOM   2999  O   PHE A 385      21.272  35.227  53.152  1.00 91.93           O  
ANISOU 2999  O   PHE A 385    12527   9941  12460    622     38   -139       O  
ATOM   3000  CB  PHE A 385      22.813  34.956  55.707  1.00 84.84           C  
ANISOU 3000  CB  PHE A 385    11567   9034  11636    644     59   -198       C  
ATOM   3001  N   THR A 386      22.939  33.887  52.430  1.00 92.39           N  
ANISOU 3001  N   THR A 386    12407  10064  12634    677     80   -335       N  
ATOM   3002  CA  THR A 386      22.944  34.363  51.058  1.00102.52           C  
ANISOU 3002  CA  THR A 386    13746  11311  13894    640     82   -336       C  
ATOM   3003  C   THR A 386      21.844  33.716  50.211  1.00115.42           C  
ANISOU 3003  C   THR A 386    15344  12995  15515    689     87   -324       C  
ATOM   3004  O   THR A 386      21.535  34.213  49.125  1.00108.58           O  
ANISOU 3004  O   THR A 386    14536  12095  14624    646     72   -294       O  
ATOM   3005  CB  THR A 386      24.286  34.092  50.370  1.00106.18           C  
ANISOU 3005  CB  THR A 386    14117  11821  14406    623    112   -481       C  
ATOM   3006  OG1 THR A 386      24.492  32.686  50.212  1.00 97.85           O  
ANISOU 3006  OG1 THR A 386    12860  10916  13402    702    134   -609       O  
ATOM   3007  CG2 THR A 386      25.463  34.750  51.054  1.00111.28           C  
ANISOU 3007  CG2 THR A 386    14803  12415  15063    557    106   -506       C  
ATOM   3008  N   GLU A 387      21.234  32.630  50.696  1.00111.72           N  
ANISOU 3008  N   GLU A 387    14774  12608  15066    751     94   -342       N  
ATOM   3009  CA  GLU A 387      20.083  32.051  50.022  1.00 97.87           C  
ANISOU 3009  CA  GLU A 387    13004  10891  13290    787     96   -316       C  
ATOM   3010  C   GLU A 387      18.921  33.049  49.951  1.00 92.72           C  
ANISOU 3010  C   GLU A 387    12486  10179  12564    740     59   -190       C  
ATOM   3011  O   GLU A 387      18.136  33.039  49.006  1.00100.40           O  
ANISOU 3011  O   GLU A 387    13474  11161  13514    738     43   -164       O  
ATOM   3012  CB  GLU A 387      19.653  30.767  50.723  1.00109.20           C  
ANISOU 3012  CB  GLU A 387    14320  12411  14759    826     85   -353       C  
ATOM   3013  CG  GLU A 387      18.478  30.091  50.045  1.00145.42           C  
ANISOU 3013  CG  GLU A 387    18891  17037  19326    855     87   -328       C  
ATOM   3014  CD  GLU A 387      17.700  29.165  50.961  1.00164.60           C  
ANISOU 3014  CD  GLU A 387    21266  19509  21765    866     61   -324       C  
ATOM   3015  OE1 GLU A 387      18.062  29.068  52.158  1.00181.51           O  
ANISOU 3015  OE1 GLU A 387    23385  21651  23931    852     35   -340       O  
ATOM   3016  OE2 GLU A 387      16.762  28.513  50.465  1.00188.38           O1-
ANISOU 3016  OE2 GLU A 387    24259  22555  24764    883     59   -311       O1-
ATOM   3017  N   LEU A 388      18.828  33.925  50.952  1.00 80.41           N  
ANISOU 3017  N   LEU A 388    11005   8575  10971    696     30   -125       N  
ATOM   3018  CA  LEU A 388      17.782  34.935  51.005  1.00 82.64           C  
ANISOU 3018  CA  LEU A 388    11376   8820  11203    639    -50    -34       C  
ATOM   3019  C   LEU A 388      17.971  35.979  49.904  1.00 87.85           C  
ANISOU 3019  C   LEU A 388    12069   9416  11894    542   -121     10       C  
ATOM   3020  O   LEU A 388      17.001  36.576  49.456  1.00 97.63           O  
ANISOU 3020  O   LEU A 388    13289  10631  13176    483   -187     83       O  
ATOM   3021  CB  LEU A 388      17.767  35.559  52.401  1.00 88.79           C  
ANISOU 3021  CB  LEU A 388    12203   9578  11956    618    -74      3       C  
ATOM   3022  CG  LEU A 388      17.549  34.545  53.528  1.00 90.36           C  
ANISOU 3022  CG  LEU A 388    12347   9828  12158    686     10    -23       C  
ATOM   3023  CD1 LEU A 388      17.978  35.076  54.890  1.00 97.80           C  
ANISOU 3023  CD1 LEU A 388    13323  10744  13093    669     25     -2       C  
ATOM   3024  CD2 LEU A 388      16.115  34.043  53.538  1.00 79.78           C  
ANISOU 3024  CD2 LEU A 388    10998   8527  10788    713      3     -1       C  
ATOM   3025  N   SER A 389      19.209  36.167  49.438  1.00 95.73           N  
ANISOU 3025  N   SER A 389    13081  10383  12909    508    -90    -26       N  
ATOM   3026  CA  SER A 389      19.482  37.099  48.354  1.00104.64           C  
ANISOU 3026  CA  SER A 389    14237  11447  14075    381   -138     31       C  
ATOM   3027  C   SER A 389      18.980  36.579  46.999  1.00109.22           C  
ANISOU 3027  C   SER A 389    14788  12044  14666    394   -115     14       C  
ATOM   3028  O   SER A 389      18.416  37.331  46.203  1.00116.66           O  
ANISOU 3028  O   SER A 389    15735  12950  15642    286   -155    116       O  
ATOM   3029  CB  SER A 389      20.944  37.442  48.315  1.00113.77           C  
ANISOU 3029  CB  SER A 389    15426  12562  15241    310   -118     -9       C  
ATOM   3030  OG  SER A 389      21.718  36.323  47.920  1.00126.38           O  
ANISOU 3030  OG  SER A 389    16968  14200  16852    404    -26   -162       O  
ATOM   3031  N   PHE A 390      19.187  35.286  46.725  1.00 98.70           N  
ANISOU 3031  N   PHE A 390    13394  10780  13325    522    -38   -106       N  
ATOM   3032  CA  PHE A 390      18.824  34.721  45.436  1.00100.25           C  
ANISOU 3032  CA  PHE A 390    13553  11005  13534    550    -15   -143       C  
ATOM   3033  C   PHE A 390      17.315  34.530  45.336  1.00112.82           C  
ANISOU 3033  C   PHE A 390    15133  12625  15109    574    -51    -69       C  
ATOM   3034  O   PHE A 390      16.740  34.715  44.268  1.00148.71           O  
ANISOU 3034  O   PHE A 390    19684  17150  19671    529    -67    -26       O  
ATOM   3035  CB  PHE A 390      19.665  33.477  45.142  1.00100.23           C  
ANISOU 3035  CB  PHE A 390    13440  11094  13547    672     77   -308       C  
ATOM   3036  CG  PHE A 390      20.783  33.750  44.163  1.00118.92           C  
ANISOU 3036  CG  PHE A 390    15622  13361  16202    573    205   -457       C  
ATOM   3037  CD1 PHE A 390      21.810  34.646  44.449  1.00122.64           C  
ANISOU 3037  CD1 PHE A 390    16082  13703  16813    425    265   -490       C  
ATOM   3038  CD2 PHE A 390      20.752  33.165  42.905  1.00137.09           C  
ANISOU 3038  CD2 PHE A 390    17748  15705  18635    587    297   -599       C  
ATOM   3039  CE1 PHE A 390      22.785  34.932  43.506  1.00132.68           C  
ANISOU 3039  CE1 PHE A 390    17184  15185  18044    214    349   -597       C  
ATOM   3040  CE2 PHE A 390      21.739  33.438  41.968  1.00147.14           C  
ANISOU 3040  CE2 PHE A 390    18840  17198  19869    390    379   -721       C  
ATOM   3041  CZ  PHE A 390      22.753  34.321  42.271  1.00148.00           C  
ANISOU 3041  CZ  PHE A 390    18948  17403  19884    185    385   -693       C  
ATOM   3042  N   THR A 391      16.688  34.142  46.449  1.00101.70           N  
ANISOU 3042  N   THR A 391    13710  11259  13673    631    -58    -59       N  
ATOM   3043  CA  THR A 391      15.256  33.886  46.446  1.00 94.78           C  
ANISOU 3043  CA  THR A 391    12817  10409  12786    645    -92    -15       C  
ATOM   3044  C   THR A 391      14.494  35.203  46.286  1.00 87.21           C  
ANISOU 3044  C   THR A 391    11885   9377  11875    531   -153    102       C  
ATOM   3045  O   THR A 391      13.345  35.198  45.827  1.00 95.76           O  
ANISOU 3045  O   THR A 391    12947  10464  12972    521   -160    148       O  
ATOM   3046  CB  THR A 391      14.809  33.078  47.672  1.00 91.43           C  
ANISOU 3046  CB  THR A 391    12374  10044  12320    715    -70    -39       C  
ATOM   3047  OG1 THR A 391      15.227  33.802  48.824  1.00106.63           O  
ANISOU 3047  OG1 THR A 391    14341  11931  14242    682    -92    -16       O  
ATOM   3048  CG2 THR A 391      15.391  31.682  47.728  1.00 93.52           C  
ANISOU 3048  CG2 THR A 391    12559  10387  12589    801     27   -116       C  
ATOM   3049  N   SER A 392      15.138  36.322  46.657  1.00 68.74           N  
ANISOU 3049  N   SER A 392     9579   6977   9562    444   -175    158       N  
ATOM   3050  CA  SER A 392      14.495  37.630  46.594  1.00 68.54           C  
ANISOU 3050  CA  SER A 392     9554   6903   9587    336   -192    288       C  
ATOM   3051  C   SER A 392      14.530  38.169  45.168  1.00 73.28           C  
ANISOU 3051  C   SER A 392    10175   7475  10195    240   -176    363       C  
ATOM   3052  O   SER A 392      13.515  38.645  44.651  1.00 89.30           O  
ANISOU 3052  O   SER A 392    12201   9500  12228    202   -165    445       O  
ATOM   3053  CB  SER A 392      15.064  38.625  47.587  1.00 63.57           C  
ANISOU 3053  CB  SER A 392     8920   6237   8997    277   -203    340       C  
ATOM   3054  OG  SER A 392      16.453  38.839  47.378  1.00 47.35           O  
ANISOU 3054  OG  SER A 392     6888   4157   6944    224   -208    321       O  
ATOM   3055  N   PHE A 393      15.710  38.056  44.545  1.00 70.76           N  
ANISOU 3055  N   PHE A 393     9878   7138   9869    195   -169    328       N  
ATOM   3056  CA  PHE A 393      15.944  38.464  43.168  1.00 68.74           C  
ANISOU 3056  CA  PHE A 393     9634   6862   9620     69   -151    398       C  
ATOM   3057  C   PHE A 393      15.331  37.484  42.148  1.00 68.88           C  
ANISOU 3057  C   PHE A 393     9653   6906   9613    141   -132    341       C  
ATOM   3058  O   PHE A 393      15.377  37.727  40.940  1.00 71.06           O  
ANISOU 3058  O   PHE A 393     9937   7172   9889     28   -116    403       O  
ATOM   3059  CB  PHE A 393      17.447  38.689  42.997  1.00 64.64           C  
ANISOU 3059  CB  PHE A 393     9138   6302   9122    -39   -126    381       C  
ATOM   3060  CG  PHE A 393      17.886  40.011  43.567  1.00 74.41           C  
ANISOU 3060  CG  PHE A 393    10318   7543  10410   -166   -124    510       C  
ATOM   3061  CD1 PHE A 393      17.784  41.180  42.820  1.00 78.06           C  
ANISOU 3061  CD1 PHE A 393    10759   8013  10887   -322    -15    680       C  
ATOM   3062  CD2 PHE A 393      18.374  40.088  44.862  1.00 77.76           C  
ANISOU 3062  CD2 PHE A 393    10744   7952  10848   -103   -150    461       C  
ATOM   3063  CE1 PHE A 393      18.176  42.396  43.363  1.00 86.87           C  
ANISOU 3063  CE1 PHE A 393    11874   9135  11999   -390     62    776       C  
ATOM   3064  CE2 PHE A 393      18.775  41.305  45.393  1.00 76.03           C  
ANISOU 3064  CE2 PHE A 393    10487   7720  10680   -192    -82    577       C  
ATOM   3065  CZ  PHE A 393      18.670  42.459  44.649  1.00 80.27           C  
ANISOU 3065  CZ  PHE A 393    11039   8268  11192   -325     32    727       C  
ATOM   3066  N   GLN A 394      14.756  36.373  42.624  1.00 59.47           N  
ANISOU 3066  N   GLN A 394     8427   5763   8404    308   -125    239       N  
ATOM   3067  CA  GLN A 394      14.309  35.315  41.745  1.00 55.51           C  
ANISOU 3067  CA  GLN A 394     7892   5306   7894    396    -98    174       C  
ATOM   3068  C   GLN A 394      13.319  35.877  40.729  1.00 57.92           C  
ANISOU 3068  C   GLN A 394     8218   5590   8200    305   -103    290       C  
ATOM   3069  O   GLN A 394      13.420  35.592  39.536  1.00 53.61           O  
ANISOU 3069  O   GLN A 394     7675   5039   7653    277    -83    287       O  
ATOM   3070  CB  GLN A 394      13.628  34.215  42.558  1.00 67.36           C  
ANISOU 3070  CB  GLN A 394     9332   6887   9374    536    -97     99       C  
ATOM   3071  CG  GLN A 394      14.519  33.035  42.889  1.00 67.29           C  
ANISOU 3071  CG  GLN A 394     9273   6955   9337    658    -55    -37       C  
ATOM   3072  CD  GLN A 394      13.754  31.989  43.660  1.00 72.81           C  
ANISOU 3072  CD  GLN A 394     9929   7738   9997    744    -51    -66       C  
ATOM   3073  OE1 GLN A 394      12.636  32.203  44.111  1.00 80.64           O  
ANISOU 3073  OE1 GLN A 394    10930   8718  10992    717    -93     -8       O  
ATOM   3074  NE2 GLN A 394      14.361  30.833  43.828  1.00 90.42           N  
ANISOU 3074  NE2 GLN A 394    12099  10054  12204    835     20   -149       N  
ATOM   3075  N   GLY A 395      12.344  36.657  41.219  1.00 66.04           N  
ANISOU 3075  N   GLY A 395     9255   6610   9228    265   -122    384       N  
ATOM   3076  CA  GLY A 395      11.280  37.194  40.381  1.00 62.94           C  
ANISOU 3076  CA  GLY A 395     8875   6213   8825    200   -118    483       C  
ATOM   3077  C   GLY A 395      11.806  38.176  39.341  1.00 61.00           C  
ANISOU 3077  C   GLY A 395     8650   5947   8580     30   -107    596       C  
ATOM   3078  O   GLY A 395      11.301  38.219  38.229  1.00 63.46           O  
ANISOU 3078  O   GLY A 395     8964   6272   8876    -23    -95    649       O  
ATOM   3079  N   LEU A 396      12.846  38.936  39.710  1.00 66.74           N  
ANISOU 3079  N   LEU A 396     9371   6659   9328    -66   -101    641       N  
ATOM   3080  CA  LEU A 396      13.474  39.872  38.796  1.00 66.51           C  
ANISOU 3080  CA  LEU A 396     9309   6649   9312   -251    -42    769       C  
ATOM   3081  C   LEU A 396      14.046  39.120  37.594  1.00 65.50           C  
ANISOU 3081  C   LEU A 396     9265   6464   9157   -327     45    751       C  
ATOM   3082  O   LEU A 396      13.823  39.525  36.457  1.00 63.43           O  
ANISOU 3082  O   LEU A 396     9027   6216   8858   -462    132    855       O  
ATOM   3083  CB  LEU A 396      14.557  40.667  39.528  1.00 64.17           C  
ANISOU 3083  CB  LEU A 396     8993   6344   9043   -325      2    808       C  
ATOM   3084  CG  LEU A 396      15.477  41.482  38.623  1.00 73.85           C  
ANISOU 3084  CG  LEU A 396    10307   7550  10204   -550    161    920       C  
ATOM   3085  CD1 LEU A 396      14.699  42.555  37.871  1.00 75.29           C  
ANISOU 3085  CD1 LEU A 396    10436   7824  10347   -596    215   1029       C  
ATOM   3086  CD2 LEU A 396      16.601  42.124  39.435  1.00 84.07           C  
ANISOU 3086  CD2 LEU A 396    11657   8814  11471   -637    202    928       C  
ATOM   3087  N   MET A 397      14.749  38.012  37.856  1.00 65.64           N  
ANISOU 3087  N   MET A 397     9346   6399   9196   -220    134    599       N  
ATOM   3088  CA  MET A 397      15.417  37.257  36.810  1.00 66.85           C  
ANISOU 3088  CA  MET A 397     9529   6490   9381   -278    399    520       C  
ATOM   3089  C   MET A 397      14.399  36.578  35.895  1.00 63.26           C  
ANISOU 3089  C   MET A 397     9036   6068   8933   -178    380    521       C  
ATOM   3090  O   MET A 397      14.607  36.418  34.689  1.00 68.32           O  
ANISOU 3090  O   MET A 397     9588   6890   9479   -309    457    490       O  
ATOM   3091  CB  MET A 397      16.415  36.238  37.372  1.00 74.39           C  
ANISOU 3091  CB  MET A 397    10291   7583  10392   -126    419    272       C  
ATOM   3092  CG  MET A 397      17.316  35.672  36.278  1.00115.00           C  
ANISOU 3092  CG  MET A 397    15168  13146  15382   -231    463     88       C  
ATOM   3093  SD  MET A 397      19.084  35.361  36.642  1.00157.75           S  
ANISOU 3093  SD  MET A 397    20338  18887  20713   -289    483   -151       S  
ATOM   3094  CE  MET A 397      19.818  36.915  36.132  1.00128.88           C  
ANISOU 3094  CE  MET A 397    16729  15394  16846   -677    503     -9       C  
ATOM   3095  N   VAL A 398      13.269  36.181  36.468  1.00 61.63           N  
ANISOU 3095  N   VAL A 398     8773   5944   8701     12    142    488       N  
ATOM   3096  CA  VAL A 398      12.228  35.592  35.649  1.00 63.29           C  
ANISOU 3096  CA  VAL A 398     8954   6205   8888     78     95    484       C  
ATOM   3097  C   VAL A 398      11.679  36.645  34.679  1.00 73.11           C  
ANISOU 3097  C   VAL A 398    10243   7458  10079   -127     83    659       C  
ATOM   3098  O   VAL A 398      11.425  36.345  33.509  1.00 66.39           O  
ANISOU 3098  O   VAL A 398     9408   6604   9213   -169    186    691       O  
ATOM   3099  CB  VAL A 398      11.137  34.970  36.535  1.00 54.40           C  
ANISOU 3099  CB  VAL A 398     7769   5173   7727    243    -55    400       C  
ATOM   3100  CG1 VAL A 398       9.924  34.559  35.707  1.00 64.23           C  
ANISOU 3100  CG1 VAL A 398     9001   6446   8959    277    -49    427       C  
ATOM   3101  CG2 VAL A 398      11.685  33.791  37.336  1.00 46.54           C  
ANISOU 3101  CG2 VAL A 398     6708   4227   6751    420    -47    237       C  
ATOM   3102  N   ALA A 399      11.506  37.886  35.170  1.00 76.19           N  
ANISOU 3102  N   ALA A 399    10575   7921  10452   -234    -23    753       N  
ATOM   3103  CA  ALA A 399      11.040  38.994  34.345  1.00 70.79           C  
ANISOU 3103  CA  ALA A 399     9828   7302   9768   -371     16    904       C  
ATOM   3104  C   ALA A 399      12.042  39.328  33.244  1.00 74.57           C  
ANISOU 3104  C   ALA A 399    10429   7734  10168   -601    225    995       C  
ATOM   3105  O   ALA A 399      11.635  39.594  32.109  1.00 70.31           O  
ANISOU 3105  O   ALA A 399     9889   7254   9572   -696    282   1059       O  
ATOM   3106  CB  ALA A 399      10.743  40.204  35.185  1.00 73.96           C  
ANISOU 3106  CB  ALA A 399    10230   7685  10187   -367     52    969       C  
ATOM   3107  N   ILE A 400      13.341  39.276  33.577  1.00 70.85           N  
ANISOU 3107  N   ILE A 400    10069   7235   9614   -724    340    934       N  
ATOM   3108  CA  ILE A 400      14.387  39.522  32.595  1.00 81.08           C  
ANISOU 3108  CA  ILE A 400    11454   8653  10700  -1079    490    923       C  
ATOM   3109  C   ILE A 400      14.353  38.457  31.496  1.00 80.07           C  
ANISOU 3109  C   ILE A 400    11132   8753  10536  -1018    523    776       C  
ATOM   3110  O   ILE A 400      14.174  38.799  30.327  1.00 72.34           O  
ANISOU 3110  O   ILE A 400    10142   7908   9434  -1202    546    832       O  
ATOM   3111  CB  ILE A 400      15.770  39.614  33.269  1.00 91.45           C  
ANISOU 3111  CB  ILE A 400    12640  10149  11958  -1132    495    789       C  
ATOM   3112  CG1 ILE A 400      15.842  40.798  34.236  1.00 95.50           C  
ANISOU 3112  CG1 ILE A 400    13302  10496  12487  -1193    449    935       C  
ATOM   3113  CG2 ILE A 400      16.890  39.645  32.236  1.00100.35           C  
ANISOU 3113  CG2 ILE A 400    13550  11694  12884  -1353    539    660       C  
ATOM   3114  CD1 ILE A 400      15.618  42.145  33.589  1.00 92.94           C  
ANISOU 3114  CD1 ILE A 400    12948  10308  12056  -1321    423   1052       C  
ATOM   3115  N   LEU A 401      14.511  37.176  31.877  1.00 72.41           N  
ANISOU 3115  N   LEU A 401    10018   7821   9673   -760    523    591       N  
ATOM   3116  CA  LEU A 401      14.711  36.114  30.903  1.00 70.28           C  
ANISOU 3116  CA  LEU A 401     9537   7812   9355   -703    554    424       C  
ATOM   3117  C   LEU A 401      13.462  35.873  30.059  1.00 72.14           C  
ANISOU 3117  C   LEU A 401     9861   7921   9628   -653    552    533       C  
ATOM   3118  O   LEU A 401      13.583  35.437  28.924  1.00 83.94           O  
ANISOU 3118  O   LEU A 401    11222   9645  11027   -718    582    461       O  
ATOM   3119  CB  LEU A 401      15.159  34.835  31.610  1.00 64.92           C  
ANISOU 3119  CB  LEU A 401     8696   7185   8784   -432    546    206       C  
ATOM   3120  CG  LEU A 401      16.486  34.925  32.345  1.00 64.68           C  
ANISOU 3120  CG  LEU A 401     8545   7317   8712   -476    552     68       C  
ATOM   3121  CD1 LEU A 401      16.787  33.598  33.004  1.00 68.12           C  
ANISOU 3121  CD1 LEU A 401     8833   7782   9268   -194    540   -146       C  
ATOM   3122  CD2 LEU A 401      17.598  35.279  31.376  1.00 77.94           C  
ANISOU 3122  CD2 LEU A 401    10053   9382  10181   -744    597    -11       C  
ATOM   3123  N   TYR A 402      12.272  36.157  30.605  1.00 75.08           N  
ANISOU 3123  N   TYR A 402    10459   7927  10141   -540    516    709       N  
ATOM   3124  CA  TYR A 402      11.032  35.847  29.912  1.00 64.71           C  
ANISOU 3124  CA  TYR A 402     9237   6465   8887   -462    509    811       C  
ATOM   3125  C   TYR A 402      10.347  37.113  29.402  1.00 67.63           C  
ANISOU 3125  C   TYR A 402     9617   6907   9171   -631    383    972       C  
ATOM   3126  O   TYR A 402       9.194  37.049  28.983  1.00 67.98           O  
ANISOU 3126  O   TYR A 402     9594   6977   9258   -544    251   1011       O  
ATOM   3127  CB  TYR A 402      10.083  35.085  30.841  1.00 60.06           C  
ANISOU 3127  CB  TYR A 402     8587   5840   8393   -144    313    723       C  
ATOM   3128  CG  TYR A 402      10.322  33.598  30.941  1.00 53.01           C  
ANISOU 3128  CG  TYR A 402     7596   4929   7617    103    397    563       C  
ATOM   3129  CD1 TYR A 402      10.892  32.908  29.898  1.00 60.08           C  
ANISOU 3129  CD1 TYR A 402     8339   6014   8475     74    503    455       C  
ATOM   3130  CD2 TYR A 402       9.946  32.868  32.068  1.00 52.93           C  
ANISOU 3130  CD2 TYR A 402     7509   5004   7597    310    215    422       C  
ATOM   3131  CE1 TYR A 402      11.115  31.544  29.993  1.00 62.32           C  
ANISOU 3131  CE1 TYR A 402     8448   6413   8818    310    499    255       C  
ATOM   3132  CE2 TYR A 402      10.146  31.501  32.182  1.00 42.00           C  
ANISOU 3132  CE2 TYR A 402     5999   3698   6260    516    227    256       C  
ATOM   3133  CZ  TYR A 402      10.739  30.838  31.128  1.00 50.94           C  
ANISOU 3133  CZ  TYR A 402     7032   4801   7521    581    436    195       C  
ATOM   3134  OH  TYR A 402      10.994  29.500  31.178  1.00 46.45           O  
ANISOU 3134  OH  TYR A 402     6287   4398   6965    782    411     -7       O  
ATOM   3135  N   CYS A 403      11.013  38.272  29.473  1.00 67.65           N  
ANISOU 3135  N   CYS A 403     9632   6982   9089   -835    418   1040       N  
ATOM   3136  CA  CYS A 403      10.385  39.460  28.913  1.00 77.62           C  
ANISOU 3136  CA  CYS A 403    10823   8326  10344   -884    393   1149       C  
ATOM   3137  C   CYS A 403      11.412  40.434  28.342  1.00 83.92           C  
ANISOU 3137  C   CYS A 403    11688   9268  10929  -1190    466   1160       C  
ATOM   3138  O   CYS A 403      11.446  40.686  27.141  1.00 82.34           O  
ANISOU 3138  O   CYS A 403    11489   9199  10599  -1368    498   1173       O  
ATOM   3139  CB  CYS A 403       9.492  40.175  29.918  1.00 74.68           C  
ANISOU 3139  CB  CYS A 403    10297   7945  10132   -668    294   1171       C  
ATOM   3140  SG  CYS A 403       8.558  41.538  29.166  1.00 91.61           S  
ANISOU 3140  SG  CYS A 403    12515  10093  12199   -732    351   1246       S  
ATOM   3141  N   PHE A 404      12.244  40.999  29.220  1.00 84.65           N  
ANISOU 3141  N   PHE A 404    11805   9369  10989  -1253    462   1149       N  
ATOM   3142  CA  PHE A 404      13.029  42.170  28.854  1.00 81.00           C  
ANISOU 3142  CA  PHE A 404    11357   9065  10355  -1496    474   1170       C  
ATOM   3143  C   PHE A 404      14.046  41.864  27.757  1.00 84.90           C  
ANISOU 3143  C   PHE A 404    11810   9820  10630  -1835    537   1111       C  
ATOM   3144  O   PHE A 404      14.386  42.750  26.978  1.00 94.61           O  
ANISOU 3144  O   PHE A 404    13013  11217  11716  -2015    532   1126       O  
ATOM   3145  CB  PHE A 404      13.640  42.795  30.102  1.00 82.61           C  
ANISOU 3145  CB  PHE A 404    11581   9219  10587  -1463    449   1173       C  
ATOM   3146  CG  PHE A 404      12.610  43.283  31.091  1.00 85.99           C  
ANISOU 3146  CG  PHE A 404    11958   9494  11222  -1157    410   1218       C  
ATOM   3147  CD1 PHE A 404      11.742  44.316  30.764  1.00 86.43           C  
ANISOU 3147  CD1 PHE A 404    11986   9558  11297  -1095    408   1268       C  
ATOM   3148  CD2 PHE A 404      12.498  42.695  32.341  1.00 84.75           C  
ANISOU 3148  CD2 PHE A 404    11748   9223  11231   -953    378   1191       C  
ATOM   3149  CE1 PHE A 404      10.806  44.767  31.675  1.00 89.49           C  
ANISOU 3149  CE1 PHE A 404    12433   9837  11732   -961    350   1276       C  
ATOM   3150  CE2 PHE A 404      11.561  43.153  33.252  1.00 88.80           C  
ANISOU 3150  CE2 PHE A 404    12220   9664  11858   -767    332   1210       C  
ATOM   3151  CZ  PHE A 404      10.729  44.193  32.918  1.00 93.23           C  
ANISOU 3151  CZ  PHE A 404    12868  10225  12330   -802    322   1247       C  
ATOM   3152  N   VAL A 405      14.529  40.616  27.692  1.00 84.85           N  
ANISOU 3152  N   VAL A 405    11728   9901  10611  -1872    601   1000       N  
ATOM   3153  CA  VAL A 405      15.513  40.227  26.693  1.00 78.15           C  
ANISOU 3153  CA  VAL A 405    10641   9446   9607  -2003    647    832       C  
ATOM   3154  C   VAL A 405      14.855  39.433  25.572  1.00 84.67           C  
ANISOU 3154  C   VAL A 405    11401  10332  10437  -1941    669    796       C  
ATOM   3155  O   VAL A 405      15.539  38.991  24.652  1.00 92.32           O  
ANISOU 3155  O   VAL A 405    12175  11614  11288  -2027    709    657       O  
ATOM   3156  CB  VAL A 405      16.682  39.431  27.293  1.00 73.07           C  
ANISOU 3156  CB  VAL A 405     9782   9009   8973  -1883    661    608       C  
ATOM   3157  CG1 VAL A 405      17.478  40.254  28.287  1.00 78.49           C  
ANISOU 3157  CG1 VAL A 405    10515   9675   9631  -1977    643    636       C  
ATOM   3158  CG2 VAL A 405      16.230  38.128  27.917  1.00 71.88           C  
ANISOU 3158  CG2 VAL A 405     9580   8724   9007  -1538    647    498       C  
ATOM   3159  N   ASN A 406      13.536  39.241  25.653  1.00 99.94           N  
ANISOU 3159  N   ASN A 406    13499  11965  12509  -1789    643    922       N  
ATOM   3160  CA  ASN A 406      12.790  38.584  24.586  1.00111.14           C  
ANISOU 3160  CA  ASN A 406    14888  13404  13937  -1738    658    919       C  
ATOM   3161  C   ASN A 406      12.851  39.450  23.331  1.00112.37           C  
ANISOU 3161  C   ASN A 406    15067  13712  13915  -2054    683   1005       C  
ATOM   3162  O   ASN A 406      12.640  40.660  23.386  1.00118.21           O  
ANISOU 3162  O   ASN A 406    15886  14382  14648  -2066    624   1089       O  
ATOM   3163  CB  ASN A 406      11.331  38.297  24.975  1.00109.66           C  
ANISOU 3163  CB  ASN A 406    14888  12841  13935  -1520    622   1056       C  
ATOM   3164  CG  ASN A 406      10.529  37.636  23.872  1.00101.07           C  
ANISOU 3164  CG  ASN A 406    13780  11761  12860  -1468    634   1065       C  
ATOM   3165  OD1 ASN A 406       9.443  38.088  23.523  1.00 95.22           O  
ANISOU 3165  OD1 ASN A 406    13065  10906  12207  -1342    574   1160       O  
ATOM   3166  ND2 ASN A 406      11.060  36.560  23.320  1.00102.03           N  
ANISOU 3166  ND2 ASN A 406    13682  12137  12947  -1380    662    876       N  
ATOM   3167  N   ASN A 407      13.106  38.813  22.184  1.00108.99           N  
ANISOU 3167  N   ASN A 407    14475  13535  13401  -2097    720    892       N  
ATOM   3168  CA  ASN A 407      13.247  39.551  20.938  1.00 95.03           C  
ANISOU 3168  CA  ASN A 407    12709  11937  11460  -2397    747    950       C  
ATOM   3169  C   ASN A 407      11.899  40.061  20.435  1.00 93.21           C  
ANISOU 3169  C   ASN A 407    12615  11465  11335  -2228    670   1064       C  
ATOM   3170  O   ASN A 407      11.848  41.111  19.811  1.00 95.91           O  
ANISOU 3170  O   ASN A 407    12984  11849  11610  -2306    629   1092       O  
ATOM   3171  CB  ASN A 407      13.907  38.702  19.858  1.00 95.94           C  
ANISOU 3171  CB  ASN A 407    12589  12392  11472  -2424    794    770       C  
ATOM   3172  CG  ASN A 407      15.264  38.181  20.260  1.00100.72           C  
ANISOU 3172  CG  ASN A 407    12965  13281  12022  -2386    818    560       C  
ATOM   3173  OD1 ASN A 407      15.562  38.020  21.449  1.00112.47           O  
ANISOU 3173  OD1 ASN A 407    14450  14681  13602  -2236    796    516       O  
ATOM   3174  ND2 ASN A 407      16.082  37.921  19.257  1.00 87.19           N  
ANISOU 3174  ND2 ASN A 407    11062  11905  10160  -2524    863    431       N  
ATOM   3175  N   GLU A 408      10.812  39.321  20.690  1.00 97.73           N  
ANISOU 3175  N   GLU A 408    13253  11804  12077  -1988    654   1111       N  
ATOM   3176  CA  GLU A 408       9.508  39.717  20.179  1.00 91.19           C  
ANISOU 3176  CA  GLU A 408    12482  10805  11362  -1807    599   1187       C  
ATOM   3177  C   GLU A 408       9.043  41.019  20.825  1.00102.64           C  
ANISOU 3177  C   GLU A 408    13979  12126  12895  -1687    544   1242       C  
ATOM   3178  O   GLU A 408       8.476  41.854  20.127  1.00113.32           O  
ANISOU 3178  O   GLU A 408    15340  13475  14240  -1685    524   1269       O  
ATOM   3179  CB  GLU A 408       8.475  38.610  20.367  1.00 92.13           C  
ANISOU 3179  CB  GLU A 408    12614  10739  11653  -1553    593   1211       C  
ATOM   3180  CG  GLU A 408       8.658  37.476  19.382  1.00108.21           C  
ANISOU 3180  CG  GLU A 408    14608  12906  13601  -1664    653   1163       C  
ATOM   3181  CD  GLU A 408       9.788  36.513  19.707  1.00111.03           C  
ANISOU 3181  CD  GLU A 408    14830  13472  13885  -1708    717   1009       C  
ATOM   3182  OE1 GLU A 408      10.349  36.603  20.820  1.00122.11           O  
ANISOU 3182  OE1 GLU A 408    16212  14855  15328  -1634    704    956       O  
ATOM   3183  OE2 GLU A 408      10.101  35.665  18.847  1.00 95.41           O1-
ANISOU 3183  OE2 GLU A 408    12680  11721  11849  -1679    746    878       O1-
ATOM   3184  N   VAL A 409       9.291  41.201  22.132  1.00 96.87           N  
ANISOU 3184  N   VAL A 409    13266  11304  12239  -1590    529   1248       N  
ATOM   3185  CA  VAL A 409       8.825  42.403  22.804  1.00 94.09           C  
ANISOU 3185  CA  VAL A 409    12924  10857  11968  -1466    496   1288       C  
ATOM   3186  C   VAL A 409       9.636  43.605  22.331  1.00 91.67           C  
ANISOU 3186  C   VAL A 409    12650  10697  11483  -1705    482   1281       C  
ATOM   3187  O   VAL A 409       9.113  44.716  22.208  1.00101.86           O  
ANISOU 3187  O   VAL A 409    13964  11954  12783  -1670    454   1308       O  
ATOM   3188  CB  VAL A 409       8.797  42.257  24.339  1.00 95.82           C  
ANISOU 3188  CB  VAL A 409    13126  10950  12330  -1278    484   1292       C  
ATOM   3189  CG1 VAL A 409       8.138  40.961  24.777  1.00 92.57           C  
ANISOU 3189  CG1 VAL A 409    12658  10429  12085  -1061    476   1286       C  
ATOM   3190  CG2 VAL A 409      10.152  42.428  24.993  1.00 98.48           C  
ANISOU 3190  CG2 VAL A 409    13507  11362  12550  -1452    485   1262       C  
ATOM   3191  N   GLN A 410      10.913  43.364  22.036  1.00 88.45           N  
ANISOU 3191  N   GLN A 410    12225  10482  10900  -1962    502   1232       N  
ATOM   3192  CA  GLN A 410      11.774  44.427  21.556  1.00 98.13           C  
ANISOU 3192  CA  GLN A 410    13451  11886  11950  -2194    484   1214       C  
ATOM   3193  C   GLN A 410      11.289  44.907  20.191  1.00100.38           C  
ANISOU 3193  C   GLN A 410    13739  12232  12168  -2267    468   1219       C  
ATOM   3194  O   GLN A 410      11.490  46.072  19.859  1.00114.67           O  
ANISOU 3194  O   GLN A 410    15578  14100  13889  -2368    430   1226       O  
ATOM   3195  CB  GLN A 410      13.235  43.973  21.538  1.00111.06           C  
ANISOU 3195  CB  GLN A 410    15003  13771  13424  -2437    529   1137       C  
ATOM   3196  CG  GLN A 410      13.802  43.703  22.924  1.00128.05           C  
ANISOU 3196  CG  GLN A 410    17157  15864  15632  -2385    540   1126       C  
ATOM   3197  CD  GLN A 410      15.236  43.226  22.921  1.00134.30           C  
ANISOU 3197  CD  GLN A 410    17816  16940  16273  -2616    603   1024       C  
ATOM   3198  OE1 GLN A 410      15.833  42.969  21.873  1.00134.67           O  
ANISOU 3198  OE1 GLN A 410    17738  17257  16175  -2801    648    944       O  
ATOM   3199  NE2 GLN A 410      15.791  43.075  24.114  1.00138.20           N  
ANISOU 3199  NE2 GLN A 410    18310  17390  16810  -2586    612   1008       N  
ATOM   3200  N   LEU A 411      10.689  44.005  19.392  1.00 95.85           N  
ANISOU 3200  N   LEU A 411    13137  11648  11632  -2222    495   1213       N  
ATOM   3201  CA  LEU A 411      10.114  44.375  18.106  1.00 98.13           C  
ANISOU 3201  CA  LEU A 411    13433  11969  11881  -2265    480   1219       C  
ATOM   3202  C   LEU A 411       8.929  45.304  18.327  1.00 95.00           C  
ANISOU 3202  C   LEU A 411    13090  11386  11619  -2066    443   1274       C  
ATOM   3203  O   LEU A 411       8.727  46.213  17.539  1.00 86.21           O  
ANISOU 3203  O   LEU A 411    12034  10322  10399  -2190    393   1275       O  
ATOM   3204  CB  LEU A 411       9.642  43.135  17.339  1.00107.91           C  
ANISOU 3204  CB  LEU A 411    14631  13214  13157  -2224    519   1205       C  
ATOM   3205  CG  LEU A 411      10.727  42.280  16.693  1.00105.21           C  
ANISOU 3205  CG  LEU A 411    14188  13131  12655  -2446    575   1125       C  
ATOM   3206  CD1 LEU A 411      10.171  40.946  16.221  1.00103.88           C  
ANISOU 3206  CD1 LEU A 411    13980  12936  12552  -2358    617   1116       C  
ATOM   3207  CD2 LEU A 411      11.321  43.037  15.528  1.00112.14           C  
ANISOU 3207  CD2 LEU A 411    15035  14218  13356  -2672    563   1083       C  
ATOM   3208  N   GLU A 412       8.148  45.047  19.380  1.00 99.25           N  
ANISOU 3208  N   GLU A 412    13666  11748  12298  -1864    428   1305       N  
ATOM   3209  CA  GLU A 412       6.942  45.815  19.649  1.00 98.47           C  
ANISOU 3209  CA  GLU A 412    13676  11516  12220  -1788    353   1335       C  
ATOM   3210  C   GLU A 412       7.280  47.250  20.056  1.00 97.98           C  
ANISOU 3210  C   GLU A 412    13696  11484  12048  -1908    290   1343       C  
ATOM   3211  O   GLU A 412       6.563  48.180  19.683  1.00 92.31           O  
ANISOU 3211  O   GLU A 412    13063  10742  11269  -1956    223   1355       O  
ATOM   3212  CB  GLU A 412       6.081  45.088  20.684  1.00 94.15           C  
ANISOU 3212  CB  GLU A 412    13126  10808  11840  -1547    358   1350       C  
ATOM   3213  CG  GLU A 412       5.623  43.718  20.219  1.00 98.03           C  
ANISOU 3213  CG  GLU A 412    13545  11267  12435  -1426    404   1345       C  
ATOM   3214  CD  GLU A 412       4.863  43.718  18.900  1.00111.95           C  
ANISOU 3214  CD  GLU A 412    15330  13049  14158  -1472    390   1349       C  
ATOM   3215  OE1 GLU A 412       3.950  44.560  18.751  1.00121.20           O  
ANISOU 3215  OE1 GLU A 412    16582  14167  15301  -1476    331   1362       O  
ATOM   3216  OE2 GLU A 412       5.175  42.868  18.029  1.00117.11           O1-
ANISOU 3216  OE2 GLU A 412    15914  13773  14808  -1505    439   1336       O1-
ATOM   3217  N   PHE A 413       8.376  47.428  20.808  1.00 95.66           N  
ANISOU 3217  N   PHE A 413    13373  11248  11727  -1958    308   1333       N  
ATOM   3218  CA  PHE A 413       8.794  48.757  21.220  1.00105.22           C  
ANISOU 3218  CA  PHE A 413    14656  12494  12829  -2075    246   1341       C  
ATOM   3219  C   PHE A 413       9.311  49.568  20.023  1.00103.65           C  
ANISOU 3219  C   PHE A 413    14471  12456  12456  -2306    216   1323       C  
ATOM   3220  O   PHE A 413       8.993  50.751  19.898  1.00116.85           O  
ANISOU 3220  O   PHE A 413    16234  14127  14036  -2390    137   1334       O  
ATOM   3221  CB  PHE A 413       9.817  48.679  22.354  1.00115.72           C  
ANISOU 3221  CB  PHE A 413    15949  13839  14182  -2060    274   1335       C  
ATOM   3222  CG  PHE A 413       9.250  48.331  23.704  1.00112.45           C  
ANISOU 3222  CG  PHE A 413    15555  13259  13913  -1849    272   1353       C  
ATOM   3223  CD1 PHE A 413       8.657  49.299  24.499  1.00108.28           C  
ANISOU 3223  CD1 PHE A 413    15119  12640  13382  -1803    203   1374       C  
ATOM   3224  CD2 PHE A 413       9.339  47.038  24.197  1.00118.83           C  
ANISOU 3224  CD2 PHE A 413    16282  14012  14856  -1702    336   1342       C  
ATOM   3225  CE1 PHE A 413       8.146  48.972  25.749  1.00102.55           C  
ANISOU 3225  CE1 PHE A 413    14400  11782  12784  -1613    204   1379       C  
ATOM   3226  CE2 PHE A 413       8.830  46.712  25.447  1.00112.72           C  
ANISOU 3226  CE2 PHE A 413    15520  13098  14213  -1509    328   1349       C  
ATOM   3227  CZ  PHE A 413       8.229  47.679  26.221  1.00103.12           C  
ANISOU 3227  CZ  PHE A 413    14390  11803  12990  -1465    264   1365       C  
ATOM   3228  N   ARG A 414      10.106  48.936  19.145  1.00 87.28           N  
ANISOU 3228  N   ARG A 414    12299  10530  10331  -2409    277   1287       N  
ATOM   3229  CA  ARG A 414      10.612  49.610  17.959  1.00 91.84           C  
ANISOU 3229  CA  ARG A 414    12875  11276  10742  -2625    251   1259       C  
ATOM   3230  C   ARG A 414       9.482  49.851  16.960  1.00 90.43           C  
ANISOU 3230  C   ARG A 414    12765  11046  10546  -2629    205   1270       C  
ATOM   3231  O   ARG A 414       9.415  50.881  16.317  1.00101.26           O  
ANISOU 3231  O   ARG A 414    14204  12478  11790  -2772    138   1265       O  
ATOM   3232  CB  ARG A 414      11.806  48.873  17.348  1.00 95.93           C  
ANISOU 3232  CB  ARG A 414    13268  11995  11185  -2756    323   1204       C  
ATOM   3233  CG  ARG A 414      12.296  49.472  16.032  1.00124.05           C  
ANISOU 3233  CG  ARG A 414    16820  15747  14566  -2982    297   1163       C  
ATOM   3234  CD  ARG A 414      12.595  50.958  15.785  1.00166.31           C  
ANISOU 3234  CD  ARG A 414    22242  21167  19783  -3125    221   1163       C  
ATOM   3235  NE  ARG A 414      13.344  51.727  16.779  1.00203.42           N  
ANISOU 3235  NE  ARG A 414    26964  25891  24435  -3170    190   1172       N  
ATOM   3236  CZ  ARG A 414      13.433  53.063  16.807  1.00201.94           C  
ANISOU 3236  CZ  ARG A 414    26871  25731  24124  -3291    100   1183       C  
ATOM   3237  NH1 ARG A 414      12.824  53.801  15.895  1.00204.65           N  
ANISOU 3237  NH1 ARG A 414    27295  26084  24377  -3383     30   1183       N  
ATOM   3238  NH2 ARG A 414      14.138  53.671  17.747  1.00187.75           N  
ANISOU 3238  NH2 ARG A 414    25089  23954  22293  -3322     76   1193       N  
ATOM   3239  N   LYS A 415       8.562  48.905  16.838  1.00101.60           N  
ANISOU 3239  N   LYS A 415    14166  12347  12090  -2471    236   1284       N  
ATOM   3240  CA  LYS A 415       7.442  49.050  15.919  1.00106.44           C  
ANISOU 3240  CA  LYS A 415    14838  12905  12700  -2461    196   1294       C  
ATOM   3241  C   LYS A 415       6.508  50.156  16.408  1.00 97.97           C  
ANISOU 3241  C   LYS A 415    13886  11718  11619  -2427    107   1323       C  
ATOM   3242  O   LYS A 415       5.919  50.866  15.606  1.00 99.13           O  
ANISOU 3242  O   LYS A 415    14101  11875  11688  -2509     48   1322       O  
ATOM   3243  CB  LYS A 415       6.718  47.709  15.748  1.00126.53           C  
ANISOU 3243  CB  LYS A 415    17329  15358  15389  -2289    253   1302       C  
ATOM   3244  CG  LYS A 415       5.643  47.659  14.673  1.00134.88           C  
ANISOU 3244  CG  LYS A 415    18428  16374  16447  -2279    224   1308       C  
ATOM   3245  CD  LYS A 415       5.016  46.280  14.546  1.00149.79           C  
ANISOU 3245  CD  LYS A 415    20256  18180  18477  -2107    281   1316       C  
ATOM   3246  CE  LYS A 415       4.081  45.902  15.681  1.00150.77           C  
ANISOU 3246  CE  LYS A 415    20400  18132  18753  -1883    275   1344       C  
ATOM   3247  NZ  LYS A 415       3.563  44.521  15.526  1.00138.57           N  
ANISOU 3247  NZ  LYS A 415    18788  16525  17336  -1724    327   1348       N  
ATOM   3248  N   SER A 416       6.375  50.305  17.725  1.00105.97           N  
ANISOU 3248  N   SER A 416    14923  12631  12709  -2308     98   1344       N  
ATOM   3249  CA  SER A 416       5.550  51.357  18.299  1.00113.82           C  
ANISOU 3249  CA  SER A 416    16019  13532  13694  -2275     18   1364       C  
ATOM   3250  C   SER A 416       6.214  52.727  18.116  1.00125.36           C  
ANISOU 3250  C   SER A 416    17545  15100  14988  -2476    -52   1356       C  
ATOM   3251  O   SER A 416       5.542  53.717  17.800  1.00130.62           O  
ANISOU 3251  O   SER A 416    18299  15748  15584  -2535   -130   1360       O  
ATOM   3252  CB  SER A 416       5.250  51.063  19.744  1.00111.33           C  
ANISOU 3252  CB  SER A 416    15701  13092  13508  -2090     33   1381       C  
ATOM   3253  OG  SER A 416       4.331  52.004  20.258  1.00130.18           O  
ANISOU 3253  OG  SER A 416    18176  15394  15892  -2049    -37   1395       O  
ATOM   3254  N   TRP A 417       7.541  52.771  18.315  1.00131.43           N  
ANISOU 3254  N   TRP A 417    18263  15984  15688  -2582    -25   1342       N  
ATOM   3255  CA  TRP A 417       8.320  53.992  18.144  1.00127.04           C  
ANISOU 3255  CA  TRP A 417    17753  15549  14967  -2779    -88   1330       C  
ATOM   3256  C   TRP A 417       8.328  54.436  16.684  1.00118.53           C  
ANISOU 3256  C   TRP A 417    16693  14590  13752  -2955   -123   1305       C  
ATOM   3257  O   TRP A 417       8.398  55.628  16.415  1.00125.27           O  
ANISOU 3257  O   TRP A 417    17623  15501  14475  -3094   -205   1299       O  
ATOM   3258  CB  TRP A 417       9.745  53.852  18.707  1.00125.95           C  
ANISOU 3258  CB  TRP A 417    17544  15518  14793  -2844    -45   1317       C  
ATOM   3259  N   GLU A 418       8.256  53.471  15.759  1.00126.19           N  
ANISOU 3259  N   GLU A 418    17595  15599  14754  -2946    -62   1287       N  
ATOM   3260  CA  GLU A 418       8.233  53.736  14.331  1.00141.41           C  
ANISOU 3260  CA  GLU A 418    19532  17634  16563  -3098    -85   1258       C  
ATOM   3261  C   GLU A 418       6.908  54.388  13.948  1.00145.61           C  
ANISOU 3261  C   GLU A 418    20171  18061  17092  -3071   -163   1275       C  
ATOM   3262  O   GLU A 418       6.906  55.274  13.098  1.00165.93           O  
ANISOU 3262  O   GLU A 418    22803  20717  19527  -3229   -228   1256       O  
ATOM   3263  CB  GLU A 418       8.455  52.444  13.535  1.00168.95           C  
ANISOU 3263  CB  GLU A 418    22914  21180  20101  -3074      4   1234       C  
ATOM   3264  CG  GLU A 418       8.716  52.652  12.056  1.00210.32           C  
ANISOU 3264  CG  GLU A 418    28143  26565  25206  -3250     -8   1194       C  
ATOM   3265  CD  GLU A 418      10.050  53.313  11.775  1.00239.99           C  
ANISOU 3265  CD  GLU A 418    31866  30524  28795  -3458    -19   1152       C  
ATOM   3266  OE1 GLU A 418      10.974  53.127  12.592  1.00246.65           O  
ANISOU 3266  OE1 GLU A 418    32644  31420  29650  -3452     22   1147       O  
ATOM   3267  OE2 GLU A 418      10.166  54.000  10.739  1.00271.17           O1-
ANISOU 3267  OE2 GLU A 418    35852  34580  32600  -3622    -67   1123       O1-
ATOM   3268  N   ARG A 419       5.795  53.927  14.547  1.00144.45           N  
ANISOU 3268  N   ARG A 419    20045  17745  17095  -2873   -154   1305       N  
ATOM   3269  CA  ARG A 419       4.482  54.476  14.260  1.00152.84           C  
ANISOU 3269  CA  ARG A 419    21196  18710  18166  -2832   -220   1318       C  
ATOM   3270  C   ARG A 419       4.410  55.929  14.722  1.00165.31           C  
ANISOU 3270  C   ARG A 419    22874  20291  19644  -2920   -316   1322       C  
ATOM   3271  O   ARG A 419       3.693  56.736  14.121  1.00188.91           O  
ANISOU 3271  O   ARG A 419    25943  23274  22560  -2987   -390   1316       O  
ATOM   3272  CB  ARG A 419       3.381  53.660  14.944  1.00154.19           C  
ANISOU 3272  CB  ARG A 419    21353  18715  18518  -2597   -185   1343       C  
ATOM   3273  CG  ARG A 419       3.367  52.191  14.559  1.00160.72           C  
ANISOU 3273  CG  ARG A 419    22085  19527  19454  -2494    -95   1341       C  
ATOM   3274  CD  ARG A 419       2.828  51.994  13.162  1.00155.63           C  
ANISOU 3274  CD  ARG A 419    21449  18912  18772  -2552   -103   1328       C  
ATOM   3275  NE  ARG A 419       2.857  50.620  12.677  1.00157.76           N  
ANISOU 3275  NE  ARG A 419    21629  19180  19131  -2471    -23   1324       N  
ATOM   3276  CZ  ARG A 419       2.045  49.624  13.043  1.00157.89           C  
ANISOU 3276  CZ  ARG A 419    21609  19079  19303  -2273     18   1342       C  
ATOM   3277  NH1 ARG A 419       1.092  49.801  13.945  1.00157.43           N  
ANISOU 3277  NH1 ARG A 419    21589  18894  19335  -2126     -7   1363       N  
ATOM   3278  NH2 ARG A 419       2.196  48.434  12.490  1.00158.45           N  
ANISOU 3278  NH2 ARG A 419    21601  19170  19434  -2225     85   1336       N  
ATOM   3279  N   TRP A 420       5.131  56.244  15.803  1.00164.32           N  
ANISOU 3279  N   TRP A 420    22743  20174  19518  -2915   -317   1331       N  
ATOM   3280  CA  TRP A 420       5.077  57.584  16.362  1.00156.86           C  
ANISOU 3280  CA  TRP A 420    21889  19225  18487  -2985   -409   1336       C  
ATOM   3281  C   TRP A 420       5.679  58.610  15.404  1.00148.44           C  
ANISOU 3281  C   TRP A 420    20869  18308  17225  -3222   -479   1309       C  
ATOM   3282  O   TRP A 420       5.142  59.707  15.247  1.00143.08           O  
ANISOU 3282  O   TRP A 420    20284  17620  16461  -3294   -571   1305       O  
ATOM   3283  CB  TRP A 420       5.694  57.657  17.763  1.00156.56           C  
ANISOU 3283  CB  TRP A 420    21834  19153  18497  -2918   -394   1353       C  
ATOM   3284  CG  TRP A 420       5.326  58.945  18.433  1.00150.12           C  
ANISOU 3284  CG  TRP A 420    21116  18296  17625  -2946   -488   1362       C  
ATOM   3285  CD1 TRP A 420       6.002  60.128  18.344  1.00147.97           C  
ANISOU 3285  CD1 TRP A 420    20899  18125  17197  -3125   -566   1351       C  
ATOM   3286  CD2 TRP A 420       4.156  59.209  19.232  1.00155.47           C  
ANISOU 3286  CD2 TRP A 420    21846  18832  18393  -2800   -517   1379       C  
ATOM   3287  NE1 TRP A 420       5.352  61.102  19.054  1.00142.03           N  
ANISOU 3287  NE1 TRP A 420    20232  17297  16435  -3097   -643   1362       N  
ATOM   3288  CE2 TRP A 420       4.215  60.570  19.606  1.00155.69           C  
ANISOU 3288  CE2 TRP A 420    21961  18881  18313  -2901   -613   1378       C  
ATOM   3289  CE3 TRP A 420       3.077  58.434  19.686  1.00167.97           C  
ANISOU 3289  CE3 TRP A 420    23406  20280  20133  -2596   -472   1392       C  
ATOM   3290  CZ2 TRP A 420       3.234  61.162  20.409  1.00163.78           C  
ANISOU 3290  CZ2 TRP A 420    23048  19797  19384  -2805   -660   1388       C  
ATOM   3291  CZ3 TRP A 420       2.108  59.020  20.475  1.00164.55           C  
ANISOU 3291  CZ3 TRP A 420    23031  19748  19743  -2503   -516   1401       C  
ATOM   3292  CH2 TRP A 420       2.190  60.368  20.834  1.00160.36           C  
ANISOU 3292  CH2 TRP A 420    22585  19240  19104  -2607   -607   1399       C  
ATOM   3293  N   ARG A 421       6.804  58.233  14.792  1.00134.55           N  
ANISOU 3293  N   ARG A 421    19038  16692  15392  -3341   -434   1285       N  
ATOM   3294  CA  ARG A 421       7.484  59.052  13.798  1.00135.14           C  
ANISOU 3294  CA  ARG A 421    19138  16933  15278  -3569   -488   1250       C  
ATOM   3295  C   ARG A 421       6.656  59.154  12.513  1.00142.78           C  
ANISOU 3295  C   ARG A 421    20149  17904  16196  -3622   -520   1232       C  
ATOM   3296  O   ARG A 421       6.401  60.259  12.045  1.00174.24           O  
ANISOU 3296  O   ARG A 421    24223  21927  20053  -3747   -613   1218       O  
ATOM   3297  CB  ARG A 421       8.915  58.561  13.548  1.00120.67           C  
ANISOU 3297  CB  ARG A 421    17202  15264  13384  -3674   -422   1222       C  
ATOM   3298  N   LEU A 422       6.248  58.013  11.938  1.00148.23           N  
ANISOU 3298  N   LEU A 422    20780  18558  16984  -3530   -446   1231       N  
ATOM   3299  CA  LEU A 422       5.487  57.999  10.694  1.00130.78           C  
ANISOU 3299  CA  LEU A 422    18605  16349  14736  -3572   -468   1215       C  
ATOM   3300  C   LEU A 422       3.987  58.051  11.006  1.00120.80           C  
ANISOU 3300  C   LEU A 422    17407  14911  13582  -3416   -501   1244       C  
ATOM   3301  O   LEU A 422       3.557  59.094  11.536  1.00108.19           O  
ANISOU 3301  O   LEU A 422    15895  13270  11943  -3431   -582   1253       O  
ATOM   3302  CB  LEU A 422       5.838  56.747   9.883  1.00122.05           C  
ANISOU 3302  CB  LEU A 422    17398  15300  13675  -3558   -374   1197       C  
TER    3303      LEU A 422                                                      
ATOM   3304  N   SER B 136      62.102  -2.028  18.646  1.00102.66           N  
ANISOU 3304  N   SER B 136    14390  11418  13200    -66   -593   -345       N  
ATOM   3305  CA  SER B 136      60.884  -2.232  17.783  1.00129.76           C  
ANISOU 3305  CA  SER B 136    17822  14843  16638   -106   -596   -327       C  
ATOM   3306  C   SER B 136      59.857  -1.135  18.053  1.00136.72           C  
ANISOU 3306  C   SER B 136    18669  15732  17547    -97   -573   -330       C  
ATOM   3307  O   SER B 136      59.656  -0.751  19.202  1.00139.83           O  
ANISOU 3307  O   SER B 136    19054  16127  17949    -78   -559   -336       O  
ATOM   3308  CB  SER B 136      60.283  -3.605  17.966  1.00119.92           C  
ANISOU 3308  CB  SER B 136    16618  13579  15369   -152   -617   -304       C  
ATOM   3309  N   PRO B 137      59.187  -0.588  17.009  1.00142.16           N  
ANISOU 3309  N   PRO B 137    19335  16425  18253   -110   -567   -326       N  
ATOM   3310  CA  PRO B 137      58.217   0.494  17.202  1.00135.36           C  
ANISOU 3310  CA  PRO B 137    18439  15570  17421   -101   -545   -329       C  
ATOM   3311  C   PRO B 137      56.902   0.002  17.805  1.00135.89           C  
ANISOU 3311  C   PRO B 137    18519  15623  17492   -136   -544   -310       C  
ATOM   3312  O   PRO B 137      56.360   0.621  18.715  1.00120.24           O  
ANISOU 3312  O   PRO B 137    16518  13641  15528   -120   -525   -315       O  
ATOM   3313  CB  PRO B 137      57.997   1.030  15.778  1.00133.75           C  
ANISOU 3313  CB  PRO B 137    18214  15374  17230   -111   -546   -328       C  
ATOM   3314  CG  PRO B 137      58.283  -0.157  14.874  1.00133.99           C  
ANISOU 3314  CG  PRO B 137    18279  15395  17235   -147   -570   -313       C  
ATOM   3315  CD  PRO B 137      59.344  -0.967  15.592  1.00140.41           C  
ANISOU 3315  CD  PRO B 137    19122  16203  18024   -134   -582   -319       C  
ATOM   3316  N   GLU B 138      56.405  -1.124  17.282  1.00148.53           N  
ANISOU 3316  N   GLU B 138    20151  17211  19073   -184   -565   -286       N  
ATOM   3317  CA  GLU B 138      55.145  -1.706  17.712  1.00151.63           C  
ANISOU 3317  CA  GLU B 138    20558  17590  19463   -225   -568   -263       C  
ATOM   3318  C   GLU B 138      55.279  -2.274  19.125  1.00157.37           C  
ANISOU 3318  C   GLU B 138    21309  18310  20176   -221   -570   -262       C  
ATOM   3319  O   GLU B 138      54.311  -2.259  19.872  1.00152.28           O  
ANISOU 3319  O   GLU B 138    20662  17658  19539   -237   -562   -252       O  
ATOM   3320  CB  GLU B 138      54.656  -2.754  16.707  1.00145.67           C  
ANISOU 3320  CB  GLU B 138    19832  16829  18687   -278   -592   -235       C  
ATOM   3321  N   GLU B 139      56.475  -2.770  19.481  1.00146.46           N  
ANISOU 3321  N   GLU B 139    19948  16928  18772   -201   -581   -273       N  
ATOM   3322  CA  GLU B 139      56.713  -3.377  20.783  1.00118.60           C  
ANISOU 3322  CA  GLU B 139    16444  13391  15226   -199   -587   -272       C  
ATOM   3323  C   GLU B 139      56.668  -2.316  21.879  1.00125.27           C  
ANISOU 3323  C   GLU B 139    17259  14243  16095   -159   -559   -291       C  
ATOM   3324  O   GLU B 139      56.255  -2.616  22.997  1.00121.24           O  
ANISOU 3324  O   GLU B 139    16760  13724  15580   -167   -557   -286       O  
ATOM   3325  CB  GLU B 139      58.040  -4.133  20.805  1.00 98.29           C  
ANISOU 3325  CB  GLU B 139    13901  10818  12627   -188   -606   -279       C  
ATOM   3326  N   GLN B 140      57.087  -1.085  21.548  1.00128.43           N  
ANISOU 3326  N   GLN B 140    17620  14658  16520   -118   -539   -312       N  
ATOM   3327  CA  GLN B 140      57.092   0.018  22.503  1.00111.71           C  
ANISOU 3327  CA  GLN B 140    15471  12550  14424    -77   -513   -330       C  
ATOM   3328  C   GLN B 140      55.660   0.374  22.908  1.00101.47           C  
ANISOU 3328  C   GLN B 140    14159  11246  13151    -95   -496   -321       C  
ATOM   3329  O   GLN B 140      55.364   0.473  24.096  1.00 98.82           O  
ANISOU 3329  O   GLN B 140    13823  10906  12820    -87   -484   -324       O  
ATOM   3330  CB  GLN B 140      57.860   1.237  21.978  1.00 94.75           C  
ANISOU 3330  CB  GLN B 140    13286  10423  12293    -32   -499   -352       C  
ATOM   3331  N   LEU B 141      54.774   0.552  21.919  1.00 87.88           N  
ANISOU 3331  N   LEU B 141    12424   9522  11444   -121   -496   -309       N  
ATOM   3332  CA  LEU B 141      53.406   0.976  22.181  1.00 81.00           C  
ANISOU 3332  CA  LEU B 141    11534   8645  10599   -139   -480   -300       C  
ATOM   3333  C   LEU B 141      52.612  -0.139  22.878  1.00 96.64           C  
ANISOU 3333  C   LEU B 141    13548  10609  12562   -186   -492   -276       C  
ATOM   3334  O   LEU B 141      51.665   0.145  23.597  1.00 95.05           O  
ANISOU 3334  O   LEU B 141    13335  10401  12380   -195   -477   -271       O  
ATOM   3335  CB  LEU B 141      52.754   1.446  20.875  1.00 65.26           C  
ANISOU 3335  CB  LEU B 141     9518   6655   8624   -157   -479   -292       C  
ATOM   3336  N   LEU B 142      53.004  -1.408  22.692  1.00106.08           N  
ANISOU 3336  N   LEU B 142    14786  11798  13721   -217   -521   -260       N  
ATOM   3337  CA  LEU B 142      52.310  -2.518  23.336  1.00102.43           C  
ANISOU 3337  CA  LEU B 142    14359  11324  13237   -264   -538   -235       C  
ATOM   3338  C   LEU B 142      52.768  -2.674  24.784  1.00101.65           C  
ANISOU 3338  C   LEU B 142    14273  11221  13128   -243   -533   -247       C  
ATOM   3339  O   LEU B 142      51.982  -3.051  25.638  1.00 86.19           O  
ANISOU 3339  O   LEU B 142    12326   9254  11166   -271   -533   -233       O  
ATOM   3340  CB  LEU B 142      52.554  -3.817  22.558  1.00105.01           C  
ANISOU 3340  CB  LEU B 142    14726  11646  13525   -304   -572   -213       C  
ATOM   3341  N   PHE B 143      54.043  -2.397  25.060  1.00104.47           N  
ANISOU 3341  N   PHE B 143    14628  11585  13479   -198   -530   -270       N  
ATOM   3342  CA  PHE B 143      54.558  -2.565  26.408  1.00112.72           C  
ANISOU 3342  CA  PHE B 143    15687  12628  14514   -179   -528   -280       C  
ATOM   3343  C   PHE B 143      53.943  -1.549  27.370  1.00120.16           C  
ANISOU 3343  C   PHE B 143    16596  13572  15487   -155   -496   -293       C  
ATOM   3344  O   PHE B 143      53.617  -1.884  28.511  1.00124.84           O  
ANISOU 3344  O   PHE B 143    17203  14157  16074   -166   -494   -289       O  
ATOM   3345  CB  PHE B 143      56.079  -2.466  26.417  1.00116.09           C  
ANISOU 3345  CB  PHE B 143    16117  13064  14929   -137   -532   -299       C  
ATOM   3346  CG  PHE B 143      56.676  -2.836  27.747  1.00127.50           C  
ANISOU 3346  CG  PHE B 143    17582  14505  16358   -124   -535   -305       C  
ATOM   3347  CD1 PHE B 143      56.808  -4.170  28.105  1.00133.93           C  
ANISOU 3347  CD1 PHE B 143    18443  15308  17137   -160   -565   -288       C  
ATOM   3348  CD2 PHE B 143      57.076  -1.861  28.648  1.00122.91           C  
ANISOU 3348  CD2 PHE B 143    16974  13933  15793    -78   -510   -326       C  
ATOM   3349  CE1 PHE B 143      57.362  -4.527  29.326  1.00134.63           C  
ANISOU 3349  CE1 PHE B 143    18551  15393  17211   -149   -569   -293       C  
ATOM   3350  CE2 PHE B 143      57.627  -2.220  29.870  1.00126.45           C  
ANISOU 3350  CE2 PHE B 143    17442  14378  16226    -68   -514   -331       C  
ATOM   3351  CZ  PHE B 143      57.767  -3.549  30.209  1.00126.34           C  
ANISOU 3351  CZ  PHE B 143    17474  14350  16178   -104   -543   -314       C  
ATOM   3352  N   LEU B 144      53.786  -0.307  26.904  1.00115.01           N  
ANISOU 3352  N   LEU B 144    15901  12930  14869   -123   -471   -308       N  
ATOM   3353  CA  LEU B 144      53.151   0.731  27.706  1.00112.59           C  
ANISOU 3353  CA  LEU B 144    15559  12625  14594    -99   -440   -321       C  
ATOM   3354  C   LEU B 144      51.659   0.455  27.894  1.00125.54           C  
ANISOU 3354  C   LEU B 144    17200  14251  16247   -145   -436   -301       C  
ATOM   3355  O   LEU B 144      51.096   0.833  28.916  1.00157.10           O  
ANISOU 3355  O   LEU B 144    21185  18244  20261   -139   -417   -306       O  
ATOM   3356  CB  LEU B 144      53.390   2.099  27.067  1.00101.91           C  
ANISOU 3356  CB  LEU B 144    14161  11289  13271    -54   -417   -341       C  
ATOM   3357  CG  LEU B 144      54.858   2.398  26.771  1.00123.04           C  
ANISOU 3357  CG  LEU B 144    16834  13982  15933    -13   -423   -358       C  
ATOM   3358  CD1 LEU B 144      54.994   3.255  25.529  1.00135.37           C  
ANISOU 3358  CD1 LEU B 144    18366  15558  17511      4   -418   -365       C  
ATOM   3359  CD2 LEU B 144      55.589   3.003  27.962  1.00104.27           C  
ANISOU 3359  CD2 LEU B 144    14445  11617  13557     33   -406   -377       C  
ATOM   3360  N   TYR B 145      51.024  -0.206  26.916  1.00117.82           N  
ANISOU 3360  N   TYR B 145    16237  13268  15261   -193   -456   -275       N  
ATOM   3361  CA  TYR B 145      49.625  -0.596  27.020  1.00 92.61           C  
ANISOU 3361  CA  TYR B 145    13077  10053  12057   -247   -478   -246       C  
ATOM   3362  C   TYR B 145      49.430  -1.602  28.156  1.00 81.87           C  
ANISOU 3362  C   TYR B 145    11780   8673  10652   -282   -510   -228       C  
ATOM   3363  O   TYR B 145      48.355  -1.634  28.754  1.00 75.08           O  
ANISOU 3363  O   TYR B 145    10975   7785   9765   -319   -543   -207       O  
ATOM   3364  CB  TYR B 145      49.096  -1.116  25.679  1.00 85.20           C  
ANISOU 3364  CB  TYR B 145    12145   9115  11112   -292   -496   -219       C  
ATOM   3365  CG  TYR B 145      47.743  -1.779  25.744  1.00 96.18           C  
ANISOU 3365  CG  TYR B 145    13604  10477  12462   -364   -547   -175       C  
ATOM   3366  CD1 TYR B 145      46.584  -1.032  25.609  1.00 99.15           C  
ANISOU 3366  CD1 TYR B 145    13993  10833  12845   -382   -562   -159       C  
ATOM   3367  CD2 TYR B 145      47.609  -3.149  25.961  1.00102.51           C  
ANISOU 3367  CD2 TYR B 145    14458  11275  13217   -417   -579   -145       C  
ATOM   3368  CE1 TYR B 145      45.331  -1.625  25.668  1.00 99.76           C  
ANISOU 3368  CE1 TYR B 145    14129  10889  12886   -457   -606   -113       C  
ATOM   3369  CE2 TYR B 145      46.364  -3.754  26.052  1.00 97.83           C  
ANISOU 3369  CE2 TYR B 145    13925  10663  12583   -490   -623   -100       C  
ATOM   3370  CZ  TYR B 145      45.223  -2.987  25.899  1.00101.51           C  
ANISOU 3370  CZ  TYR B 145    14399  11112  13057   -513   -636    -82       C  
ATOM   3371  OH  TYR B 145      43.986  -3.565  25.954  1.00106.55           O  
ANISOU 3371  OH  TYR B 145    15090  11739  13656   -594   -676    -31       O  
ATOM   3372  N   ILE B 146      50.460  -2.407  28.454  1.00 73.32           N  
ANISOU 3372  N   ILE B 146    10691   7608   9561   -275   -502   -236       N  
ATOM   3373  CA  ILE B 146      50.393  -3.397  29.520  1.00 79.05           C  
ANISOU 3373  CA  ILE B 146    11473   8320  10243   -307   -532   -221       C  
ATOM   3374  C   ILE B 146      50.430  -2.704  30.878  1.00 80.98           C  
ANISOU 3374  C   ILE B 146    11725   8554  10491   -275   -521   -240       C  
ATOM   3375  O   ILE B 146      49.531  -2.898  31.699  1.00 83.28           O  
ANISOU 3375  O   ILE B 146    12077   8818  10748   -312   -553   -222       O  
ATOM   3376  CB  ILE B 146      51.510  -4.451  29.372  1.00 81.30           C  
ANISOU 3376  CB  ILE B 146    11768   8617  10506   -308   -542   -222       C  
ATOM   3377  CG1 ILE B 146      51.344  -5.254  28.080  1.00 76.30           C  
ANISOU 3377  CG1 ILE B 146    11154   7983   9851   -347   -569   -198       C  
ATOM   3378  CG2 ILE B 146      51.610  -5.353  30.593  1.00 82.84           C  
ANISOU 3378  CG2 ILE B 146    11999   8805  10670   -331   -558   -214       C  
ATOM   3379  CD1 ILE B 146      49.993  -5.917  27.952  1.00 77.92           C  
ANISOU 3379  CD1 ILE B 146    11387   8182  10038   -414   -590   -160       C  
ATOM   3380  N   ILE B 147      51.466  -1.886  31.094  1.00 87.49           N  
ANISOU 3380  N   ILE B 147    12485   9402  11355   -211   -476   -275       N  
ATOM   3381  CA  ILE B 147      51.662  -1.222  32.376  1.00107.74           C  
ANISOU 3381  CA  ILE B 147    15047  11963  13926   -175   -460   -296       C  
ATOM   3382  C   ILE B 147      50.506  -0.257  32.668  1.00 98.33           C  
ANISOU 3382  C   ILE B 147    13878  10746  12736   -171   -469   -296       C  
ATOM   3383  O   ILE B 147      50.245   0.060  33.823  1.00114.70           O  
ANISOU 3383  O   ILE B 147    15978  12805  14799   -161   -472   -304       O  
ATOM   3384  CB  ILE B 147      53.055  -0.557  32.460  1.00112.57           C  
ANISOU 3384  CB  ILE B 147    15617  12598  14555   -112   -433   -325       C  
ATOM   3385  CG1 ILE B 147      53.259   0.498  31.369  1.00139.67           C  
ANISOU 3385  CG1 ILE B 147    19011  16044  18013    -76   -417   -338       C  
ATOM   3386  CG2 ILE B 147      54.161  -1.604  32.431  1.00101.62           C  
ANISOU 3386  CG2 ILE B 147    14273  11211  13128   -120   -464   -318       C  
ATOM   3387  CD1 ILE B 147      52.806   1.887  31.754  1.00148.83           C  
ANISOU 3387  CD1 ILE B 147    20123  17212  19213    -36   -380   -357       C  
ATOM   3388  N   TYR B 148      49.817   0.204  31.619  1.00 86.02           N  
ANISOU 3388  N   TYR B 148    12310   9183  11193   -180   -474   -287       N  
ATOM   3389  CA  TYR B 148      48.684   1.105  31.749  1.00 81.95           C  
ANISOU 3389  CA  TYR B 148    11812   8642  10684   -179   -485   -285       C  
ATOM   3390  C   TYR B 148      47.444   0.331  32.189  1.00 82.60           C  
ANISOU 3390  C   TYR B 148    11979   8688  10718   -255   -536   -248       C  
ATOM   3391  O   TYR B 148      46.713   0.766  33.070  1.00 81.13           O  
ANISOU 3391  O   TYR B 148    11828   8477  10521   -261   -547   -248       O  
ATOM   3392  CB  TYR B 148      48.435   1.854  30.436  1.00 81.17           C  
ANISOU 3392  CB  TYR B 148    11668   8553  10620   -166   -472   -288       C  
ATOM   3393  CG  TYR B 148      47.321   2.872  30.456  1.00 83.87           C  
ANISOU 3393  CG  TYR B 148    12018   8872  10977   -158   -482   -288       C  
ATOM   3394  CD1 TYR B 148      47.574   4.190  30.799  1.00 85.62           C  
ANISOU 3394  CD1 TYR B 148    12192   9106  11236    -88   -448   -322       C  
ATOM   3395  CD2 TYR B 148      46.022   2.532  30.102  1.00 81.49           C  
ANISOU 3395  CD2 TYR B 148    11768   8540  10656   -224   -525   -251       C  
ATOM   3396  CE1 TYR B 148      46.568   5.139  30.811  1.00 89.43           C  
ANISOU 3396  CE1 TYR B 148    12678   9567  11736    -75   -459   -325       C  
ATOM   3397  CE2 TYR B 148      45.004   3.471  30.101  1.00 80.04           C  
ANISOU 3397  CE2 TYR B 148    11587   8333  10491   -220   -536   -250       C  
ATOM   3398  CZ  TYR B 148      45.281   4.781  30.452  1.00 86.59           C  
ANISOU 3398  CZ  TYR B 148    12369   9172  11360   -141   -504   -290       C  
ATOM   3399  OH  TYR B 148      44.302   5.730  30.474  1.00 89.08           O  
ANISOU 3399  OH  TYR B 148    12683   9465  11699   -128   -517   -293       O  
ATOM   3400  N   THR B 149      47.199  -0.818  31.553  1.00 85.98           N  
ANISOU 3400  N   THR B 149    12439   9116  11115   -319   -565   -213       N  
ATOM   3401  CA  THR B 149      45.991  -1.579  31.831  1.00 87.50           C  
ANISOU 3401  CA  THR B 149    12705   9283  11258   -405   -613   -169       C  
ATOM   3402  C   THR B 149      46.109  -2.308  33.167  1.00 89.68           C  
ANISOU 3402  C   THR B 149    13032   9550  11491   -431   -629   -164       C  
ATOM   3403  O   THR B 149      45.119  -2.395  33.897  1.00 73.73           O  
ANISOU 3403  O   THR B 149    11068   7509   9439   -485   -655   -141       O  
ATOM   3404  CB  THR B 149      45.625  -2.502  30.669  1.00 84.87           C  
ANISOU 3404  CB  THR B 149    12384   8958  10906   -464   -637   -131       C  
ATOM   3405  OG1 THR B 149      46.826  -3.219  30.386  1.00 95.53           O  
ANISOU 3405  OG1 THR B 149    13707  10332  12257   -439   -622   -146       O  
ATOM   3406  CG2 THR B 149      45.111  -1.749  29.460  1.00 73.50           C  
ANISOU 3406  CG2 THR B 149    10907   7519   9500   -459   -630   -126       C  
ATOM   3407  N   VAL B 150      47.321  -2.783  33.499  1.00 87.59           N  
ANISOU 3407  N   VAL B 150    12747   9305  11229   -396   -611   -185       N  
ATOM   3408  CA  VAL B 150      47.545  -3.406  34.797  1.00 90.61           C  
ANISOU 3408  CA  VAL B 150    13172   9681  11576   -414   -624   -184       C  
ATOM   3409  C   VAL B 150      47.540  -2.348  35.895  1.00 98.34           C  
ANISOU 3409  C   VAL B 150    14145  10649  12572   -367   -601   -215       C  
ATOM   3410  O   VAL B 150      47.257  -2.671  37.046  1.00108.04           O  
ANISOU 3410  O   VAL B 150    15423  11863  13765   -398   -617   -209       O  
ATOM   3411  CB  VAL B 150      48.821  -4.269  34.859  1.00 81.23           C  
ANISOU 3411  CB  VAL B 150    11961   8516  10385   -394   -615   -195       C  
ATOM   3412  CG1 VAL B 150      48.863  -5.285  33.732  1.00 82.95           C  
ANISOU 3412  CG1 VAL B 150    12181   8746  10588   -433   -634   -169       C  
ATOM   3413  CG2 VAL B 150      50.093  -3.442  34.907  1.00 78.08           C  
ANISOU 3413  CG2 VAL B 150    11487   8141  10039   -308   -564   -238       C  
ATOM   3414  N   GLY B 151      47.873  -1.102  35.533  1.00 96.73           N  
ANISOU 3414  N   GLY B 151    13879  10454  12420   -294   -563   -247       N  
ATOM   3415  CA  GLY B 151      47.797   0.019  36.456  1.00 83.40           C  
ANISOU 3415  CA  GLY B 151    12179   8757  10751   -243   -539   -277       C  
ATOM   3416  C   GLY B 151      46.351   0.265  36.884  1.00 75.91           C  
ANISOU 3416  C   GLY B 151    11293   7774   9777   -293   -568   -259       C  
ATOM   3417  O   GLY B 151      46.078   0.446  38.068  1.00 74.65           O  
ANISOU 3417  O   GLY B 151    11168   7598   9598   -297   -569   -268       O  
ATOM   3418  N   TYR B 152      45.426   0.253  35.914  1.00 71.15           N  
ANISOU 3418  N   TYR B 152    10701   7159   9174   -338   -591   -231       N  
ATOM   3419  CA  TYR B 152      44.020   0.449  36.235  1.00 78.34           C  
ANISOU 3419  CA  TYR B 152    11664   8039  10061   -401   -620   -206       C  
ATOM   3420  C   TYR B 152      43.368  -0.830  36.758  1.00 89.41           C  
ANISOU 3420  C   TYR B 152    13140   9434  11398   -512   -661   -159       C  
ATOM   3421  O   TYR B 152      42.346  -0.755  37.441  1.00 88.57           O  
ANISOU 3421  O   TYR B 152    13002   9396  11256   -550   -653   -132       O  
ATOM   3422  CB  TYR B 152      43.247   1.006  35.046  1.00 83.31           C  
ANISOU 3422  CB  TYR B 152    12271   8662  10720   -412   -628   -189       C  
ATOM   3423  CG  TYR B 152      43.421   2.484  34.816  1.00 80.95           C  
ANISOU 3423  CG  TYR B 152    11912   8364  10481   -317   -595   -233       C  
ATOM   3424  CD1 TYR B 152      42.648   3.413  35.492  1.00 84.77           C  
ANISOU 3424  CD1 TYR B 152    12325   8918  10968   -286   -564   -237       C  
ATOM   3425  CD2 TYR B 152      44.310   2.954  33.866  1.00 79.30           C  
ANISOU 3425  CD2 TYR B 152    11631   8184  10316   -250   -565   -257       C  
ATOM   3426  CE1 TYR B 152      42.788   4.774  35.259  1.00 83.06           C  
ANISOU 3426  CE1 TYR B 152    12043   8711  10804   -196   -534   -275       C  
ATOM   3427  CE2 TYR B 152      44.451   4.308  33.613  1.00 79.29           C  
ANISOU 3427  CE2 TYR B 152    11568   8191  10366   -169   -535   -293       C  
ATOM   3428  CZ  TYR B 152      43.698   5.224  34.318  1.00 78.49           C  
ANISOU 3428  CZ  TYR B 152    11478   8067  10277   -142   -537   -310       C  
ATOM   3429  OH  TYR B 152      43.854   6.557  34.066  1.00 90.54           O  
ANISOU 3429  OH  TYR B 152    12938   9609  11854    -56   -509   -346       O  
ATOM   3430  N   ALA B 153      43.942  -1.999  36.426  1.00 92.30           N  
ANISOU 3430  N   ALA B 153    13512   9819  11739   -539   -675   -140       N  
ATOM   3431  CA  ALA B 153      43.466  -3.253  37.000  1.00 80.35           C  
ANISOU 3431  CA  ALA B 153    12062   8308  10160   -637   -713    -98       C  
ATOM   3432  C   ALA B 153      43.796  -3.316  38.499  1.00 81.63           C  
ANISOU 3432  C   ALA B 153    12255   8463  10298   -631   -708   -119       C  
ATOM   3433  O   ALA B 153      42.953  -3.690  39.312  1.00 69.44           O  
ANISOU 3433  O   ALA B 153    10757   6919   8705   -712   -730    -91       O  
ATOM   3434  CB  ALA B 153      44.028  -4.433  36.238  1.00 65.39           C  
ANISOU 3434  CB  ALA B 153    10162   6435   8248   -655   -729    -77       C  
ATOM   3435  N   LEU B 154      45.034  -2.950  38.869  1.00 76.21           N  
ANISOU 3435  N   LEU B 154    11527   7784   9644   -539   -674   -164       N  
ATOM   3436  CA  LEU B 154      45.456  -2.947  40.262  1.00 72.50           C  
ANISOU 3436  CA  LEU B 154    11079   7311   9158   -524   -664   -186       C  
ATOM   3437  C   LEU B 154      44.732  -1.848  41.041  1.00 79.88           C  
ANISOU 3437  C   LEU B 154    12028   8223  10099   -514   -650   -207       C  
ATOM   3438  O   LEU B 154      44.480  -2.011  42.229  1.00 87.54           O  
ANISOU 3438  O   LEU B 154    13021   9207  11033   -544   -649   -206       O  
ATOM   3439  CB  LEU B 154      46.972  -2.744  40.337  1.00 65.88           C  
ANISOU 3439  CB  LEU B 154    10178   6493   8359   -430   -627   -225       C  
ATOM   3440  CG  LEU B 154      47.810  -4.008  40.487  1.00 67.20           C  
ANISOU 3440  CG  LEU B 154    10353   6678   8503   -451   -643   -212       C  
ATOM   3441  CD1 LEU B 154      47.390  -5.036  39.459  1.00 69.55           C  
ANISOU 3441  CD1 LEU B 154    10671   6981   8773   -516   -678   -172       C  
ATOM   3442  CD2 LEU B 154      49.310  -3.699  40.390  1.00 65.50           C  
ANISOU 3442  CD2 LEU B 154    10064   6489   8335   -364   -602   -247       C  
ATOM   3443  N   SER B 155      44.432  -0.717  40.382  1.00 82.90           N  
ANISOU 3443  N   SER B 155    12372   8600  10528   -461   -629   -225       N  
ATOM   3444  CA  SER B 155      43.745   0.395  41.026  1.00 75.92           C  
ANISOU 3444  CA  SER B 155    11386   7811   9648   -413   -578   -233       C  
ATOM   3445  C   SER B 155      42.281   0.039  41.296  1.00 74.27           C  
ANISOU 3445  C   SER B 155    11117   7717   9384   -491   -574   -178       C  
ATOM   3446  O   SER B 155      41.790   0.257  42.396  1.00 76.67           O  
ANISOU 3446  O   SER B 155    11376   8096   9658   -495   -547   -175       O  
ATOM   3447  CB  SER B 155      43.873   1.677  40.227  1.00 68.67           C  
ANISOU 3447  CB  SER B 155    10411   6887   8794   -325   -550   -265       C  
ATOM   3448  OG  SER B 155      45.218   2.128  40.182  1.00 65.17           O  
ANISOU 3448  OG  SER B 155    10001   6363   8398   -243   -543   -318       O  
ATOM   3449  N   PHE B 156      41.594  -0.516  40.292  1.00 74.95           N  
ANISOU 3449  N   PHE B 156    11205   7818   9457   -554   -601   -133       N  
ATOM   3450  CA  PHE B 156      40.181  -0.831  40.400  1.00 76.34           C  
ANISOU 3450  CA  PHE B 156    11323   8101   9583   -628   -598    -78       C  
ATOM   3451  C   PHE B 156      39.965  -1.817  41.536  1.00 74.56           C  
ANISOU 3451  C   PHE B 156    11133   7907   9289   -701   -614    -54       C  
ATOM   3452  O   PHE B 156      39.100  -1.606  42.389  1.00 66.30           O  
ANISOU 3452  O   PHE B 156    10023   6959   8208   -721   -588    -39       O  
ATOM   3453  CB  PHE B 156      39.635  -1.449  39.110  1.00 81.69           C  
ANISOU 3453  CB  PHE B 156    12015   8769  10253   -691   -631    -31       C  
ATOM   3454  CG  PHE B 156      38.167  -1.803  39.141  1.00 86.58           C  
ANISOU 3454  CG  PHE B 156    12578   9497  10822   -769   -631     29       C  
ATOM   3455  CD1 PHE B 156      37.196  -0.856  38.822  1.00 94.26           C  
ANISOU 3455  CD1 PHE B 156    13448  10551  11814   -744   -597     39       C  
ATOM   3456  CD2 PHE B 156      37.760  -3.090  39.467  1.00 81.40           C  
ANISOU 3456  CD2 PHE B 156    11971   8860  10099   -867   -666     75       C  
ATOM   3457  CE1 PHE B 156      35.849  -1.189  38.848  1.00100.16           C  
ANISOU 3457  CE1 PHE B 156    14143  11397  12515   -816   -597     94       C  
ATOM   3458  CE2 PHE B 156      36.413  -3.424  39.492  1.00 84.49           C  
ANISOU 3458  CE2 PHE B 156    12311   9351  10440   -939   -666    131       C  
ATOM   3459  CZ  PHE B 156      35.461  -2.473  39.186  1.00 94.92           C  
ANISOU 3459  CZ  PHE B 156    13530  10752  11783   -913   -631    140       C  
ATOM   3460  N   SER B 157      40.759  -2.892  41.517  1.00 74.33           N  
ANISOU 3460  N   SER B 157    11206   7794   9243   -742   -658    -52       N  
ATOM   3461  CA  SER B 157      40.639  -3.931  42.528  1.00 78.53           C  
ANISOU 3461  CA  SER B 157    11783   8344   9709   -817   -682    -29       C  
ATOM   3462  C   SER B 157      40.886  -3.358  43.919  1.00 77.42           C  
ANISOU 3462  C   SER B 157    11616   8236   9565   -775   -646    -64       C  
ATOM   3463  O   SER B 157      40.088  -3.590  44.825  1.00 74.29           O  
ANISOU 3463  O   SER B 157    11185   7926   9116   -825   -637    -40       O  
ATOM   3464  CB  SER B 157      41.547  -5.079  42.238  1.00 72.82           C  
ANISOU 3464  CB  SER B 157    11173   7517   8978   -858   -736    -28       C  
ATOM   3465  OG  SER B 157      41.142  -5.696  41.034  1.00 75.30           O  
ANISOU 3465  OG  SER B 157    11508   7817   9286   -911   -768     12       O  
ATOM   3466  N   ALA B 158      41.982  -2.604  44.056  1.00 74.49           N  
ANISOU 3466  N   ALA B 158    11260   7794   9249   -683   -627   -121       N  
ATOM   3467  CA  ALA B 158      42.378  -2.024  45.330  1.00 78.80           C  
ANISOU 3467  CA  ALA B 158    11788   8356   9797   -635   -593   -158       C  
ATOM   3468  C   ALA B 158      41.311  -1.055  45.854  1.00 80.18           C  
ANISOU 3468  C   ALA B 158    11849   8652   9965   -613   -541   -153       C  
ATOM   3469  O   ALA B 158      41.053  -1.014  47.057  1.00 87.91           O  
ANISOU 3469  O   ALA B 158    12805   9687  10910   -628   -521   -156       O  
ATOM   3470  CB  ALA B 158      43.741  -1.371  45.220  1.00 76.68           C  
ANISOU 3470  CB  ALA B 158    11557   7986   9591   -539   -583   -216       C  
ATOM   3471  N   LEU B 159      40.682  -0.287  44.956  1.00 68.01           N  
ANISOU 3471  N   LEU B 159    10235   7151   8455   -580   -520   -147       N  
ATOM   3472  CA  LEU B 159      39.700   0.693  45.376  1.00 66.15           C  
ANISOU 3472  CA  LEU B 159     9888   7026   8220   -553   -472   -146       C  
ATOM   3473  C   LEU B 159      38.383   0.019  45.765  1.00 68.79           C  
ANISOU 3473  C   LEU B 159    10187   7465   8487   -651   -478    -92       C  
ATOM   3474  O   LEU B 159      37.674   0.477  46.664  1.00 59.11           O  
ANISOU 3474  O   LEU B 159     8890   6332   7239   -652   -442    -93       O  
ATOM   3475  CB  LEU B 159      39.513   1.720  44.260  1.00 69.14           C  
ANISOU 3475  CB  LEU B 159    10206   7407   8659   -487   -453   -158       C  
ATOM   3476  CG  LEU B 159      40.668   2.708  44.087  1.00 70.41           C  
ANISOU 3476  CG  LEU B 159    10376   7491   8887   -377   -433   -217       C  
ATOM   3477  CD1 LEU B 159      40.588   3.387  42.729  1.00 70.67           C  
ANISOU 3477  CD1 LEU B 159    10374   7503   8973   -333   -433   -222       C  
ATOM   3478  CD2 LEU B 159      40.683   3.748  45.207  1.00 74.08           C  
ANISOU 3478  CD2 LEU B 159    10775   8007   9363   -309   -382   -254       C  
ATOM   3479  N   VAL B 160      38.044  -1.082  45.086  1.00 71.22           N  
ANISOU 3479  N   VAL B 160    10543   7759   8760   -735   -523    -46       N  
ATOM   3480  CA  VAL B 160      36.816  -1.784  45.424  1.00 72.15           C  
ANISOU 3480  CA  VAL B 160    10632   7973   8809   -831   -533      7       C  
ATOM   3481  C   VAL B 160      37.012  -2.517  46.752  1.00 71.50           C  
ANISOU 3481  C   VAL B 160    10594   7901   8670   -882   -544      8       C  
ATOM   3482  O   VAL B 160      36.101  -2.568  47.571  1.00 70.04           O  
ANISOU 3482  O   VAL B 160    10358   7817   8439   -927   -526     27       O  
ATOM   3483  CB  VAL B 160      36.333  -2.703  44.277  1.00 73.50           C  
ANISOU 3483  CB  VAL B 160    10838   8131   8959   -905   -578     60       C  
ATOM   3484  CG1 VAL B 160      35.132  -3.544  44.680  1.00 64.72           C  
ANISOU 3484  CG1 VAL B 160     9707   7113   7769  -1009   -592    117       C  
ATOM   3485  CG2 VAL B 160      36.028  -1.917  43.005  1.00 71.21           C  
ANISOU 3485  CG2 VAL B 160    10496   7839   8724   -859   -564     62       C  
ATOM   3486  N   ILE B 161      38.210  -3.074  46.971  1.00 72.54           N  
ANISOU 3486  N   ILE B 161    10821   7931   8808   -876   -573    -15       N  
ATOM   3487  CA  ILE B 161      38.543  -3.745  48.225  1.00 78.46           C  
ANISOU 3487  CA  ILE B 161    11621   8677   9511   -920   -587    -20       C  
ATOM   3488  C   ILE B 161      38.542  -2.729  49.367  1.00 74.86           C  
ANISOU 3488  C   ILE B 161    11102   8275   9068   -862   -532    -58       C  
ATOM   3489  O   ILE B 161      37.948  -2.977  50.419  1.00 68.91           O  
ANISOU 3489  O   ILE B 161    10324   7597   8261   -914   -523    -45       O  
ATOM   3490  CB  ILE B 161      39.899  -4.480  48.138  1.00 82.88           C  
ANISOU 3490  CB  ILE B 161    12297   9108  10087   -918   -630    -40       C  
ATOM   3491  CG1 ILE B 161      39.836  -5.733  47.261  1.00 84.29           C  
ANISOU 3491  CG1 ILE B 161    12547   9242  10237   -998   -691      2       C  
ATOM   3492  CG2 ILE B 161      40.432  -4.801  49.530  1.00 78.52           C  
ANISOU 3492  CG2 ILE B 161    11785   8543   9506   -935   -633    -60       C  
ATOM   3493  CD1 ILE B 161      41.209  -6.326  46.959  1.00 88.95           C  
ANISOU 3493  CD1 ILE B 161    13244   9697  10856   -984   -731    -23       C  
ATOM   3494  N   ALA B 162      39.205  -1.587  49.132  1.00 73.05           N  
ANISOU 3494  N   ALA B 162    10844   8005   8906   -755   -497   -105       N  
ATOM   3495  CA  ALA B 162      39.327  -0.548  50.140  1.00 73.73           C  
ANISOU 3495  CA  ALA B 162    10873   8131   9011   -689   -445   -145       C  
ATOM   3496  C   ALA B 162      37.945  -0.027  50.512  1.00 70.70           C  
ANISOU 3496  C   ALA B 162    10379   7882   8600   -710   -406   -125       C  
ATOM   3497  O   ALA B 162      37.656   0.144  51.692  1.00 73.37           O  
ANISOU 3497  O   ALA B 162    10686   8282   8908   -723   -379   -134       O  
ATOM   3498  CB  ALA B 162      40.242   0.564  49.673  1.00 79.96           C  
ANISOU 3498  CB  ALA B 162    11651   8852   9877   -572   -418   -195       C  
ATOM   3499  N   SER B 163      37.106   0.209  49.497  1.00 64.07           N  
ANISOU 3499  N   SER B 163     9484   7086   7772   -715   -404    -98       N  
ATOM   3500  CA  SER B 163      35.775   0.737  49.749  1.00 69.02           C  
ANISOU 3500  CA  SER B 163    10005   7841   8380   -732   -368    -80       C  
ATOM   3501  C   SER B 163      34.923  -0.289  50.488  1.00 76.15           C  
ANISOU 3501  C   SER B 163    10916   8819   9200   -844   -387    -37       C  
ATOM   3502  O   SER B 163      34.064   0.091  51.288  1.00 75.62           O  
ANISOU 3502  O   SER B 163    10773   8854   9106   -860   -352    -35       O  
ATOM   3503  CB  SER B 163      35.110   1.230  48.509  1.00 64.58           C  
ANISOU 3503  CB  SER B 163     9384   7303   7852   -712   -364    -62       C  
ATOM   3504  OG  SER B 163      35.139   0.216  47.528  1.00 83.95           O  
ANISOU 3504  OG  SER B 163    11904   9705  10288   -773   -415    -23       O  
ATOM   3505  N   ALA B 164      35.187  -1.582  50.241  1.00 83.74           N  
ANISOU 3505  N   ALA B 164    11969   9727  10121   -921   -443     -5       N  
ATOM   3506  CA  ALA B 164      34.499  -2.652  50.956  1.00 85.47           C  
ANISOU 3506  CA  ALA B 164    12210  10007  10259  -1031   -468     35       C  
ATOM   3507  C   ALA B 164      34.893  -2.640  52.429  1.00 88.22           C  
ANISOU 3507  C   ALA B 164    12570  10367  10581  -1035   -452      7       C  
ATOM   3508  O   ALA B 164      34.079  -2.952  53.297  1.00 90.59           O  
ANISOU 3508  O   ALA B 164    12840  10758  10823  -1102   -445     26       O  
ATOM   3509  CB  ALA B 164      34.785  -3.998  50.339  1.00 75.10           C  
ANISOU 3509  CB  ALA B 164    10995   8627   8914  -1106   -534     73       C  
ATOM   3510  N   ILE B 165      36.155  -2.298  52.704  1.00 82.94           N  
ANISOU 3510  N   ILE B 165    11952   9606   9957   -967   -447    -39       N  
ATOM   3511  CA  ILE B 165      36.628  -2.285  54.076  1.00 82.89           C  
ANISOU 3511  CA  ILE B 165    11965   9600   9930   -969   -433    -66       C  
ATOM   3512  C   ILE B 165      35.955  -1.150  54.847  1.00 86.25           C  
ANISOU 3512  C   ILE B 165    12282  10127  10363   -927   -368    -89       C  
ATOM   3513  O   ILE B 165      35.487  -1.375  55.961  1.00 81.95           O  
ANISOU 3513  O   ILE B 165    11719   9651   9767   -981   -356    -84       O  
ATOM   3514  CB  ILE B 165      38.162  -2.203  54.119  1.00 82.97           C  
ANISOU 3514  CB  ILE B 165    12056   9480   9987   -904   -445   -108       C  
ATOM   3515  CG1 ILE B 165      38.817  -3.450  53.527  1.00 77.36           C  
ANISOU 3515  CG1 ILE B 165    11457   8673   9263   -958   -512    -86       C  
ATOM   3516  CG2 ILE B 165      38.677  -1.903  55.517  1.00 86.27           C  
ANISOU 3516  CG2 ILE B 165    12481   9899  10398   -887   -419   -142       C  
ATOM   3517  CD1 ILE B 165      40.320  -3.262  53.320  1.00 83.84           C  
ANISOU 3517  CD1 ILE B 165    12352   9362  10143   -883   -522   -130       C  
ATOM   3518  N   LEU B 166      35.914   0.058  54.260  1.00 85.66           N  
ANISOU 3518  N   LEU B 166    12136  10060  10350   -833   -327   -115       N  
ATOM   3519  CA  LEU B 166      35.345   1.234  54.912  1.00 87.48           C  
ANISOU 3519  CA  LEU B 166    12260  10380  10597   -781   -265   -141       C  
ATOM   3520  C   LEU B 166      33.850   1.044  55.171  1.00 92.73           C  
ANISOU 3520  C   LEU B 166    12849  11177  11208   -857   -253   -104       C  
ATOM   3521  O   LEU B 166      33.325   1.525  56.178  1.00101.38           O  
ANISOU 3521  O   LEU B 166    13880  12357  12285   -860   -212   -118       O  
ATOM   3522  CB  LEU B 166      35.598   2.487  54.059  1.00 75.75           C  
ANISOU 3522  CB  LEU B 166    10720   8871   9190   -669   -233   -172       C  
ATOM   3523  CG  LEU B 166      37.066   2.863  53.872  1.00 62.06           C  
ANISOU 3523  CG  LEU B 166     9050   7015   7513   -583   -236   -214       C  
ATOM   3524  CD1 LEU B 166      37.197   4.258  53.298  1.00 58.85           C  
ANISOU 3524  CD1 LEU B 166     8574   6609   7180   -471   -196   -249       C  
ATOM   3525  CD2 LEU B 166      37.796   2.780  55.197  1.00 64.38           C  
ANISOU 3525  CD2 LEU B 166     9386   7285   7790   -580   -225   -242       C  
ATOM   3526  N   LEU B 167      33.169   0.332  54.268  1.00 95.92           N  
ANISOU 3526  N   LEU B 167    13261  11597  11587   -920   -288    -57       N  
ATOM   3527  CA  LEU B 167      31.746   0.074  54.453  1.00 92.04           C  
ANISOU 3527  CA  LEU B 167    12702  11228  11042   -996   -281    -18       C  
ATOM   3528  C   LEU B 167      31.517  -1.116  55.391  1.00 86.26           C  
ANISOU 3528  C   LEU B 167    12024  10525  10226  -1106   -312      9       C  
ATOM   3529  O   LEU B 167      30.580  -1.100  56.175  1.00 80.14           O  
ANISOU 3529  O   LEU B 167    11189   9856   9405  -1156   -289     19       O  
ATOM   3530  CB  LEU B 167      31.086  -0.171  53.090  1.00 89.86           C  
ANISOU 3530  CB  LEU B 167    12411  10959  10774  -1018   -305     23       C  
ATOM   3531  CG  LEU B 167      30.915   1.046  52.184  1.00 79.35           C  
ANISOU 3531  CG  LEU B 167    11002   9633   9516   -926   -271      4       C  
ATOM   3532  CD1 LEU B 167      30.379   0.624  50.834  1.00 67.64           C  
ANISOU 3532  CD1 LEU B 167     9522   8141   8036   -960   -304     49       C  
ATOM   3533  CD2 LEU B 167      29.993   2.088  52.809  1.00 75.46           C  
ANISOU 3533  CD2 LEU B 167    10388   9254   9031   -897   -213    -14       C  
ATOM   3534  N   GLY B 168      32.353  -2.159  55.295  1.00 86.31           N  
ANISOU 3534  N   GLY B 168    12142  10439  10213  -1147   -366     21       N  
ATOM   3535  CA  GLY B 168      32.139  -3.397  56.035  1.00 77.43           C  
ANISOU 3535  CA  GLY B 168    11076   9335   9008  -1258   -406     52       C  
ATOM   3536  C   GLY B 168      32.166  -3.193  57.549  1.00 78.42           C  
ANISOU 3536  C   GLY B 168    11185   9509   9104  -1273   -377     25       C  
ATOM   3537  O   GLY B 168      31.216  -3.534  58.249  1.00 90.27           O  
ANISOU 3537  O   GLY B 168    12648  11109  10541  -1350   -372     46       O  
ATOM   3538  N   PHE B 169      33.275  -2.640  58.045  1.00 73.69           N  
ANISOU 3538  N   PHE B 169    10613   8837   8548  -1200   -358    -23       N  
ATOM   3539  CA  PHE B 169      33.473  -2.459  59.469  1.00 68.30           C  
ANISOU 3539  CA  PHE B 169     9926   8183   7842  -1211   -332    -51       C  
ATOM   3540  C   PHE B 169      32.729  -1.222  59.970  1.00 76.11           C  
ANISOU 3540  C   PHE B 169    10794   9274   8849  -1161   -261    -76       C  
ATOM   3541  O   PHE B 169      32.892  -0.118  59.439  1.00 81.18           O  
ANISOU 3541  O   PHE B 169    11380   9905   9558  -1062   -223   -104       O  
ATOM   3542  CB  PHE B 169      34.952  -2.295  59.749  1.00 65.31           C  
ANISOU 3542  CB  PHE B 169     9623   7685   7508  -1148   -338    -91       C  
ATOM   3543  CG  PHE B 169      35.800  -3.455  59.319  1.00 75.18           C  
ANISOU 3543  CG  PHE B 169    10992   8825   8747  -1190   -406    -73       C  
ATOM   3544  CD1 PHE B 169      35.847  -4.614  60.069  1.00 86.41           C  
ANISOU 3544  CD1 PHE B 169    12484  10243  10104  -1291   -451    -51       C  
ATOM   3545  CD2 PHE B 169      36.606  -3.362  58.197  1.00 90.21           C  
ANISOU 3545  CD2 PHE B 169    12940  10628  10709  -1126   -425    -81       C  
ATOM   3546  CE1 PHE B 169      36.678  -5.660  59.700  1.00 96.48           C  
ANISOU 3546  CE1 PHE B 169    13871  11414  11374  -1327   -515    -38       C  
ATOM   3547  CE2 PHE B 169      37.451  -4.402  57.839  1.00 97.34           C  
ANISOU 3547  CE2 PHE B 169    13953  11425  11606  -1161   -487    -70       C  
ATOM   3548  CZ  PHE B 169      37.482  -5.553  58.590  1.00 97.50           C  
ANISOU 3548  CZ  PHE B 169    14042  11443  11563  -1261   -532    -48       C  
ATOM   3549  N   ARG B 170      31.919  -1.425  61.014  1.00 79.20           N  
ANISOU 3549  N   ARG B 170    11146   9766   9180  -1233   -246    -68       N  
ATOM   3550  CA  ARG B 170      30.985  -0.405  61.461  1.00 86.51           C  
ANISOU 3550  CA  ARG B 170    11952  10805  10112  -1206   -183    -85       C  
ATOM   3551  C   ARG B 170      31.754   0.773  62.066  1.00 89.74           C  
ANISOU 3551  C   ARG B 170    12332  11186  10580  -1103   -130   -142       C  
ATOM   3552  O   ARG B 170      31.322   1.925  61.979  1.00 85.86           O  
ANISOU 3552  O   ARG B 170    11744  10750  10130  -1032    -77   -166       O  
ATOM   3553  CB  ARG B 170      29.925  -1.002  62.396  1.00 79.33           C  
ANISOU 3553  CB  ARG B 170    11012  10009   9119  -1316   -183    -61       C  
ATOM   3554  N   HIS B 171      32.915   0.491  62.669  1.00 88.35           N  
ANISOU 3554  N   HIS B 171    12242  10920  10408  -1094   -146   -163       N  
ATOM   3555  CA  HIS B 171      33.663   1.526  63.382  1.00 95.17           C  
ANISOU 3555  CA  HIS B 171    13085  11756  11319  -1005    -98   -215       C  
ATOM   3556  C   HIS B 171      34.263   2.557  62.429  1.00 94.73           C  
ANISOU 3556  C   HIS B 171    13007  11639  11349   -880    -76   -242       C  
ATOM   3557  O   HIS B 171      34.682   3.634  62.853  1.00 99.91           O  
ANISOU 3557  O   HIS B 171    13621  12290  12050   -794    -28   -284       O  
ATOM   3558  CB  HIS B 171      34.692   0.907  64.335  1.00 95.45           C  
ANISOU 3558  CB  HIS B 171    13218  11716  11333  -1037   -122   -227       C  
ATOM   3559  CG  HIS B 171      34.027   0.150  65.435  1.00 98.87           C  
ANISOU 3559  CG  HIS B 171    13655  12226  11685  -1152   -132   -208       C  
ATOM   3560  ND1 HIS B 171      33.424  -1.087  65.227  1.00102.94           N  
ANISOU 3560  ND1 HIS B 171    14210  12769  12135  -1263   -186   -161       N  
ATOM   3561  CD2 HIS B 171      33.779   0.479  66.723  1.00 90.22           C  
ANISOU 3561  CD2 HIS B 171    12521  11196  10562  -1175    -94   -229       C  
ATOM   3562  CE1 HIS B 171      32.867  -1.490  66.348  1.00 93.71           C  
ANISOU 3562  CE1 HIS B 171    13030  11676  10901  -1350   -182   -154       C  
ATOM   3563  NE2 HIS B 171      33.077  -0.556  67.267  1.00 91.58           N  
ANISOU 3563  NE2 HIS B 171    12714  11430  10654  -1300   -126   -196       N  
ATOM   3564  N   LEU B 172      34.283   2.219  61.138  1.00 88.26           N  
ANISOU 3564  N   LEU B 172    12212  10773  10549   -874   -112   -218       N  
ATOM   3565  CA  LEU B 172      34.885   3.075  60.136  1.00 76.64           C  
ANISOU 3565  CA  LEU B 172    10729   9236   9155   -764   -100   -241       C  
ATOM   3566  C   LEU B 172      33.848   4.020  59.528  1.00 79.68           C  
ANISOU 3566  C   LEU B 172    10996   9709   9568   -723    -61   -241       C  
ATOM   3567  O   LEU B 172      34.176   4.783  58.628  1.00 95.02           O  
ANISOU 3567  O   LEU B 172    12917  11611  11574   -636    -51   -257       O  
ATOM   3568  CB  LEU B 172      35.507   2.181  59.061  1.00 80.25           C  
ANISOU 3568  CB  LEU B 172    11282   9591   9620   -783   -162   -217       C  
ATOM   3569  CG  LEU B 172      36.625   1.238  59.505  1.00 84.91           C  
ANISOU 3569  CG  LEU B 172    11992  10078  10190   -817   -206   -219       C  
ATOM   3570  CD1 LEU B 172      37.067   0.370  58.342  1.00 86.76           C  
ANISOU 3570  CD1 LEU B 172    12308  10225  10432   -839   -265   -193       C  
ATOM   3571  CD2 LEU B 172      37.824   2.005  60.032  1.00 89.51           C  
ANISOU 3571  CD2 LEU B 172    12600  10586  10824   -725   -179   -269       C  
ATOM   3572  N   HIS B 173      32.602   3.980  60.007  1.00 74.95           N  
ANISOU 3572  N   HIS B 173    10322   9232   8924   -785    -41   -222       N  
ATOM   3573  CA  HIS B 173      31.551   4.808  59.439  1.00 74.94           C  
ANISOU 3573  CA  HIS B 173    10208   9317   8947   -753     -7   -219       C  
ATOM   3574  C   HIS B 173      31.611   6.208  60.032  1.00 75.69           C  
ANISOU 3574  C   HIS B 173    10218   9450   9090   -660     57   -268       C  
ATOM   3575  O   HIS B 173      30.900   6.513  60.985  1.00100.36           O  
ANISOU 3575  O   HIS B 173    13276  12671  12187   -686     95   -278       O  
ATOM   3576  CB  HIS B 173      30.172   4.191  59.685  1.00 86.13           C  
ANISOU 3576  CB  HIS B 173    11578  10849  10297   -858    -12   -179       C  
ATOM   3577  CG  HIS B 173      29.879   2.993  58.848  1.00 92.91           C  
ANISOU 3577  CG  HIS B 173    12497  11686  11117   -940    -71   -126       C  
ATOM   3578  ND1 HIS B 173      29.224   1.881  59.341  1.00 94.05           N  
ANISOU 3578  ND1 HIS B 173    12669  11885  11181  -1057   -100    -88       N  
ATOM   3579  CD2 HIS B 173      30.153   2.731  57.554  1.00 97.19           C  
ANISOU 3579  CD2 HIS B 173    13079  12158  11689   -922   -107   -105       C  
ATOM   3580  CE1 HIS B 173      29.111   0.992  58.381  1.00 94.51           C  
ANISOU 3580  CE1 HIS B 173    12781  11907  11221  -1106   -152    -45       C  
ATOM   3581  NE2 HIS B 173      29.653   1.497  57.270  1.00 85.23           N  
ANISOU 3581  NE2 HIS B 173    11613  10657  10114  -1026   -156    -54       N  
ATOM   3582  N   CYS B 174      32.458   7.060  59.453  1.00 64.67           N  
ANISOU 3582  N   CYS B 174     8826   7980   7767   -553     68   -300       N  
ATOM   3583  CA  CYS B 174      32.535   8.449  59.872  1.00 58.76           C  
ANISOU 3583  CA  CYS B 174     7995   7262   7068   -456    126   -346       C  
ATOM   3584  C   CYS B 174      32.686   9.321  58.637  1.00 55.83           C  
ANISOU 3584  C   CYS B 174     7588   6857   6770   -364    130   -358       C  
ATOM   3585  O   CYS B 174      33.072   8.803  57.576  1.00 47.86           O  
ANISOU 3585  O   CYS B 174     6639   5773   5774   -368     86   -337       O  
ATOM   3586  CB  CYS B 174      33.680   8.675  60.854  1.00 67.79           C  
ANISOU 3586  CB  CYS B 174     9192   8343   8220   -414    143   -383       C  
ATOM   3587  SG  CYS B 174      35.286   8.044  60.292  1.00 87.61           S  
ANISOU 3587  SG  CYS B 174    11844  10689  10755   -385     91   -386       S  
ATOM   3588  N   THR B 175      32.394  10.624  58.807  1.00 61.06           N  
ANISOU 3588  N   THR B 175     8151   7571   7477   -283    181   -393       N  
ATOM   3589  CA  THR B 175      32.393  11.601  57.716  1.00 70.31           C  
ANISOU 3589  CA  THR B 175     9269   8726   8719   -194    188   -407       C  
ATOM   3590  C   THR B 175      33.721  11.573  56.941  1.00 70.30           C  
ANISOU 3590  C   THR B 175     9358   8592   8761   -133    157   -420       C  
ATOM   3591  O   THR B 175      33.728  11.669  55.710  1.00 65.21           O  
ANISOU 3591  O   THR B 175     8715   7910   8151   -109    132   -408       O  
ATOM   3592  CB  THR B 175      31.953  12.997  58.188  1.00 70.90           C  
ANISOU 3592  CB  THR B 175     9227   8877   8833   -117    247   -446       C  
ATOM   3593  OG1 THR B 175      33.047  13.480  58.954  1.00105.05           O  
ANISOU 3593  OG1 THR B 175    13589  13146  13178    -51    270   -486       O  
ATOM   3594  CG2 THR B 175      30.742  13.009  59.097  1.00 69.97           C  
ANISOU 3594  CG2 THR B 175     9025   8887   8672   -179    281   -440       C  
ATOM   3595  N   ARG B 176      34.848  11.413  57.662  1.00 71.36           N  
ANISOU 3595  N   ARG B 176     9569   8653   8891   -110    157   -443       N  
ATOM   3596  CA  ARG B 176      36.153  11.344  57.026  1.00 66.21           C  
ANISOU 3596  CA  ARG B 176     9006   7873   8276    -55    128   -457       C  
ATOM   3597  C   ARG B 176      36.219  10.191  56.017  1.00 74.51           C  
ANISOU 3597  C   ARG B 176    10135   8867   9309   -121     68   -417       C  
ATOM   3598  O   ARG B 176      36.766  10.361  54.918  1.00 86.28           O  
ANISOU 3598  O   ARG B 176    11655  10283  10843    -73     45   -421       O  
ATOM   3599  CB  ARG B 176      37.283  11.273  58.042  1.00 56.44           C  
ANISOU 3599  CB  ARG B 176     7839   6572   7034    -30    136   -485       C  
ATOM   3600  CG  ARG B 176      38.629  10.922  57.409  1.00 60.19           C  
ANISOU 3600  CG  ARG B 176     8422   6910   7538      7     98   -494       C  
ATOM   3601  CD  ARG B 176      39.806  10.797  58.360  1.00 65.43           C  
ANISOU 3601  CD  ARG B 176     9163   7499   8198     30    102   -519       C  
ATOM   3602  NE  ARG B 176      39.323  10.245  59.625  1.00 71.69           N  
ANISOU 3602  NE  ARG B 176     9953   8355   8930    -51    114   -507       N  
ATOM   3603  CZ  ARG B 176      39.287   8.946  59.901  1.00 67.24           C  
ANISOU 3603  CZ  ARG B 176     9462   7776   8311   -153     74   -476       C  
ATOM   3604  NH1 ARG B 176      39.764   8.073  59.024  1.00 63.39           N  
ANISOU 3604  NH1 ARG B 176     9058   7206   7823   -183     20   -455       N  
ATOM   3605  NH2 ARG B 176      38.790   8.553  61.063  1.00 61.84           N  
ANISOU 3605  NH2 ARG B 176     8767   7158   7572   -224     88   -467       N  
ATOM   3606  N   ASN B 177      35.665   9.023  56.382  1.00 73.10           N  
ANISOU 3606  N   ASN B 177     9990   8723   9063   -232     43   -378       N  
ATOM   3607  CA  ASN B 177      35.728   7.869  55.499  1.00 73.09           C  
ANISOU 3607  CA  ASN B 177    10065   8668   9039   -300    -15   -338       C  
ATOM   3608  C   ASN B 177      34.674   7.940  54.393  1.00 71.88           C  
ANISOU 3608  C   ASN B 177     9849   8569   8894   -321    -24   -307       C  
ATOM   3609  O   ASN B 177      34.870   7.359  53.317  1.00 61.25           O  
ANISOU 3609  O   ASN B 177     8556   7162   7554   -342    -67   -282       O  
ATOM   3610  CB  ASN B 177      35.678   6.552  56.262  1.00 73.83           C  
ANISOU 3610  CB  ASN B 177    10230   8764   9060   -408    -45   -309       C  
ATOM   3611  CG  ASN B 177      36.924   6.290  57.076  1.00 73.36           C  
ANISOU 3611  CG  ASN B 177    10257   8618   8997   -391    -52   -336       C  
ATOM   3612  OD1 ASN B 177      38.005   6.786  56.768  1.00 73.79           O  
ANISOU 3612  OD1 ASN B 177    10350   8583   9104   -308    -51   -368       O  
ATOM   3613  ND2 ASN B 177      36.773   5.501  58.128  1.00 87.50           N  
ANISOU 3613  ND2 ASN B 177    12081  10436  10727   -472    -61   -322       N  
ATOM   3614  N   TYR B 178      33.565   8.644  54.659  1.00 72.55           N  
ANISOU 3614  N   TYR B 178     9822   8764   8978   -318     15   -307       N  
ATOM   3615  CA  TYR B 178      32.536   8.816  53.638  1.00 74.31           C  
ANISOU 3615  CA  TYR B 178     9979   9042   9215   -333      9   -279       C  
ATOM   3616  C   TYR B 178      33.075   9.679  52.494  1.00 75.82           C  
ANISOU 3616  C   TYR B 178    10159   9169   9482   -239      7   -301       C  
ATOM   3617  O   TYR B 178      32.774   9.408  51.324  1.00 60.23           O  
ANISOU 3617  O   TYR B 178     8191   7175   7520   -259    -23   -272       O  
ATOM   3618  CB  TYR B 178      31.251   9.416  54.212  1.00 68.99           C  
ANISOU 3618  CB  TYR B 178     9186   8501   8527   -348     53   -278       C  
ATOM   3619  CG  TYR B 178      30.501   8.531  55.169  1.00 72.24           C  
ANISOU 3619  CG  TYR B 178     9599   8989   8861   -453     52   -250       C  
ATOM   3620  CD1 TYR B 178      30.138   7.239  54.817  1.00 79.76           C  
ANISOU 3620  CD1 TYR B 178    10610   9937   9757   -554      5   -200       C  
ATOM   3621  CD2 TYR B 178      30.156   8.983  56.434  1.00 79.14           C  
ANISOU 3621  CD2 TYR B 178    10416   9941   9715   -452     97   -275       C  
ATOM   3622  CE1 TYR B 178      29.445   6.423  55.696  1.00 85.01           C  
ANISOU 3622  CE1 TYR B 178    11278  10675  10348   -652      2   -175       C  
ATOM   3623  CE2 TYR B 178      29.470   8.179  57.334  1.00 84.61           C  
ANISOU 3623  CE2 TYR B 178    11108  10705  10333   -551     96   -251       C  
ATOM   3624  CZ  TYR B 178      29.101   6.899  56.953  1.00 92.41           C  
ANISOU 3624  CZ  TYR B 178    12156  11691  11266   -652     47   -201       C  
ATOM   3625  OH  TYR B 178      28.399   6.106  57.814  1.00 97.55           O  
ANISOU 3625  OH  TYR B 178    12807  12416  11841   -752     43   -177       O  
ATOM   3626  N   ILE B 179      33.874  10.706  52.846  1.00 68.16           N  
ANISOU 3626  N   ILE B 179     9174   8164   8560   -139     38   -351       N  
ATOM   3627  CA  ILE B 179      34.504  11.542  51.833  1.00 67.87           C  
ANISOU 3627  CA  ILE B 179     9133   8061   8594    -47     35   -376       C  
ATOM   3628  C   ILE B 179      35.486  10.719  50.991  1.00 62.98           C  
ANISOU 3628  C   ILE B 179     8628   7322   7978    -60    -16   -364       C  
ATOM   3629  O   ILE B 179      35.562  10.920  49.776  1.00 51.02           O  
ANISOU 3629  O   ILE B 179     7114   5767   6503    -35    -37   -359       O  
ATOM   3630  CB  ILE B 179      35.141  12.794  52.455  1.00 67.09           C  
ANISOU 3630  CB  ILE B 179     8995   7955   8540     61     79   -430       C  
ATOM   3631  CG1 ILE B 179      34.055  13.675  53.068  1.00 62.01           C  
ANISOU 3631  CG1 ILE B 179     8228   7433   7901     75    127   -441       C  
ATOM   3632  CG2 ILE B 179      35.974  13.556  51.421  1.00 66.81           C  
ANISOU 3632  CG2 ILE B 179     8974   7837   8575    155     69   -457       C  
ATOM   3633  CD1 ILE B 179      34.601  14.805  53.928  1.00 58.97           C  
ANISOU 3633  CD1 ILE B 179     7804   7053   7549    169    174   -492       C  
ATOM   3634  N   HIS B 180      36.185   9.768  51.636  1.00 60.09           N  
ANISOU 3634  N   HIS B 180     8356   6903   7572   -104    -37   -360       N  
ATOM   3635  CA  HIS B 180      37.081   8.852  50.950  1.00 65.20           C  
ANISOU 3635  CA  HIS B 180     9115   7440   8217   -128    -87   -348       C  
ATOM   3636  C   HIS B 180      36.317   8.002  49.943  1.00 66.48           C  
ANISOU 3636  C   HIS B 180     9288   7617   8356   -209   -126   -297       C  
ATOM   3637  O   HIS B 180      36.779   7.832  48.811  1.00 66.73           O  
ANISOU 3637  O   HIS B 180     9364   7573   8417   -196   -157   -292       O  
ATOM   3638  CB  HIS B 180      37.861   7.962  51.928  1.00 71.26           C  
ANISOU 3638  CB  HIS B 180     9976   8157   8943   -169   -102   -351       C  
ATOM   3639  CG  HIS B 180      38.860   8.696  52.757  1.00 70.52           C  
ANISOU 3639  CG  HIS B 180     9895   8021   8878    -86    -72   -400       C  
ATOM   3640  ND1 HIS B 180      38.920  10.066  52.771  1.00 81.75           N  
ANISOU 3640  ND1 HIS B 180    11242   9468  10353     13    -29   -437       N  
ATOM   3641  CD2 HIS B 180      39.789   8.266  53.635  1.00 69.71           C  
ANISOU 3641  CD2 HIS B 180     9869   7859   8758    -90    -77   -416       C  
ATOM   3642  CE1 HIS B 180      39.853  10.460  53.608  1.00 84.52           C  
ANISOU 3642  CE1 HIS B 180    11622   9774  10716     69     -8   -474       C  
ATOM   3643  NE2 HIS B 180      40.401   9.369  54.158  1.00 79.74           N  
ANISOU 3643  NE2 HIS B 180    11111   9118  10070      7    -37   -462       N  
ATOM   3644  N   LEU B 181      35.155   7.486  50.365  1.00 58.62           N  
ANISOU 3644  N   LEU B 181     8250   6716   7305   -293   -123   -260       N  
ATOM   3645  CA  LEU B 181      34.366   6.598  49.522  1.00 62.00           C  
ANISOU 3645  CA  LEU B 181     8690   7164   7702   -379   -160   -206       C  
ATOM   3646  C   LEU B 181      33.926   7.295  48.238  1.00 63.32           C  
ANISOU 3646  C   LEU B 181     8800   7338   7922   -339   -160   -201       C  
ATOM   3647  O   LEU B 181      33.898   6.649  47.192  1.00 55.69           O  
ANISOU 3647  O   LEU B 181     7878   6328   6954   -379   -199   -169       O  
ATOM   3648  CB  LEU B 181      33.150   6.084  50.297  1.00 65.79           C  
ANISOU 3648  CB  LEU B 181     9124   7757   8117   -467   -151   -172       C  
ATOM   3649  CG  LEU B 181      33.447   4.998  51.324  1.00 65.30           C  
ANISOU 3649  CG  LEU B 181     9137   7685   7989   -541   -170   -160       C  
ATOM   3650  CD1 LEU B 181      32.291   4.824  52.296  1.00 62.53           C  
ANISOU 3650  CD1 LEU B 181     8722   7456   7580   -609   -147   -141       C  
ATOM   3651  CD2 LEU B 181      33.806   3.702  50.620  1.00 62.12           C  
ANISOU 3651  CD2 LEU B 181     8838   7208   7558   -611   -230   -123       C  
ATOM   3652  N   ASN B 182      33.596   8.597  48.322  1.00 70.96           N  
ANISOU 3652  N   ASN B 182     9670   8357   8935   -263   -117   -231       N  
ATOM   3653  CA  ASN B 182      33.254   9.380  47.137  1.00 75.11           C  
ANISOU 3653  CA  ASN B 182    10138   8883   9516   -218   -117   -232       C  
ATOM   3654  C   ASN B 182      34.480   9.620  46.255  1.00 72.81           C  
ANISOU 3654  C   ASN B 182     9913   8473   9278   -152   -139   -258       C  
ATOM   3655  O   ASN B 182      34.364   9.607  45.032  1.00 63.71           O  
ANISOU 3655  O   ASN B 182     8764   7289   8152   -155   -164   -241       O  
ATOM   3656  CB  ASN B 182      32.580  10.709  47.464  1.00 68.19           C  
ANISOU 3656  CB  ASN B 182     9139   8093   8676   -154    -68   -258       C  
ATOM   3657  CG  ASN B 182      31.193  10.554  48.052  1.00 70.82           C  
ANISOU 3657  CG  ASN B 182     9394   8550   8966   -220    -48   -229       C  
ATOM   3658  OD1 ASN B 182      30.190  10.860  47.404  1.00 60.29           O  
ANISOU 3658  OD1 ASN B 182     7987   7275   7646   -236    -46   -207       O  
ATOM   3659  ND2 ASN B 182      31.134  10.105  49.292  1.00 77.06           N  
ANISOU 3659  ND2 ASN B 182    10197   9379   9704   -260    -32   -231       N  
ATOM   3660  N   LEU B 183      35.648   9.826  46.883  1.00 67.66           N  
ANISOU 3660  N   LEU B 183     9313   7756   8639    -94   -130   -300       N  
ATOM   3661  CA  LEU B 183      36.877   9.978  46.126  1.00 67.55           C  
ANISOU 3661  CA  LEU B 183     9369   7627   8671    -35   -151   -327       C  
ATOM   3662  C   LEU B 183      37.247   8.657  45.445  1.00 75.44           C  
ANISOU 3662  C   LEU B 183    10471   8551   9642   -109   -204   -293       C  
ATOM   3663  O   LEU B 183      37.704   8.666  44.300  1.00 79.17           O  
ANISOU 3663  O   LEU B 183    10978   8953  10149    -90   -230   -294       O  
ATOM   3664  CB  LEU B 183      37.987  10.477  47.054  1.00 66.46           C  
ANISOU 3664  CB  LEU B 183     9261   7442   8549     40   -128   -376       C  
ATOM   3665  CG  LEU B 183      39.392  10.594  46.450  1.00 57.24           C  
ANISOU 3665  CG  LEU B 183     8174   6150   7424    103   -149   -409       C  
ATOM   3666  CD1 LEU B 183      39.529  11.835  45.580  1.00 53.44           C  
ANISOU 3666  CD1 LEU B 183     7637   5657   7011    193   -136   -438       C  
ATOM   3667  CD2 LEU B 183      40.428  10.616  47.559  1.00 56.81           C  
ANISOU 3667  CD2 LEU B 183     8173   6049   7364    142   -133   -444       C  
ATOM   3668  N   PHE B 184      37.030   7.522  46.131  1.00 67.75           N  
ANISOU 3668  N   PHE B 184     9545   7594   8604   -196   -221   -263       N  
ATOM   3669  CA  PHE B 184      37.329   6.231  45.541  1.00 58.15           C  
ANISOU 3669  CA  PHE B 184     8424   6311   7357   -270   -272   -229       C  
ATOM   3670  C   PHE B 184      36.414   5.989  44.359  1.00 59.48           C  
ANISOU 3670  C   PHE B 184     8564   6510   7527   -319   -293   -186       C  
ATOM   3671  O   PHE B 184      36.862   5.471  43.345  1.00 62.85           O  
ANISOU 3671  O   PHE B 184     9053   6859   7966   -336   -331   -174       O  
ATOM   3672  CB  PHE B 184      37.115   5.103  46.540  1.00 61.94           C  
ANISOU 3672  CB  PHE B 184     8950   6818   7766   -358   -286   -203       C  
ATOM   3673  CG  PHE B 184      38.016   5.157  47.745  1.00 67.94           C  
ANISOU 3673  CG  PHE B 184     9751   7545   8519   -326   -271   -240       C  
ATOM   3674  CD1 PHE B 184      39.227   5.847  47.698  1.00 67.13           C  
ANISOU 3674  CD1 PHE B 184     9678   7357   8469   -232   -260   -289       C  
ATOM   3675  CD2 PHE B 184      37.654   4.499  48.914  1.00 61.96           C  
ANISOU 3675  CD2 PHE B 184     9003   6838   7699   -393   -268   -224       C  
ATOM   3676  CE1 PHE B 184      40.068   5.879  48.799  1.00 63.78           C  
ANISOU 3676  CE1 PHE B 184     9295   6899   8039   -204   -247   -321       C  
ATOM   3677  CE2 PHE B 184      38.493   4.529  50.013  1.00 64.72           C  
ANISOU 3677  CE2 PHE B 184     9393   7154   8043   -367   -256   -256       C  
ATOM   3678  CZ  PHE B 184      39.692   5.218  49.953  1.00 69.87           C  
ANISOU 3678  CZ  PHE B 184    10076   7721   8751   -272   -245   -304       C  
ATOM   3679  N   ALA B 185      35.136   6.356  44.502  1.00 64.81           N  
ANISOU 3679  N   ALA B 185     9144   7294   8188   -344   -270   -163       N  
ATOM   3680  CA  ALA B 185      34.164   6.107  43.441  1.00 67.71           C  
ANISOU 3680  CA  ALA B 185     9479   7697   8552   -396   -289   -117       C  
ATOM   3681  C   ALA B 185      34.564   6.836  42.164  1.00 64.41           C  
ANISOU 3681  C   ALA B 185     9052   7219   8203   -334   -297   -134       C  
ATOM   3682  O   ALA B 185      34.431   6.276  41.086  1.00 54.20           O  
ANISOU 3682  O   ALA B 185     7794   5890   6911   -378   -331   -102       O  
ATOM   3683  CB  ALA B 185      32.771   6.500  43.868  1.00 68.03           C  
ANISOU 3683  CB  ALA B 185     9412   7864   8572   -423   -259    -95       C  
ATOM   3684  N   SER B 186      35.068   8.069  42.308  1.00 63.29           N  
ANISOU 3684  N   SER B 186     8866   7066   8116   -233   -265   -185       N  
ATOM   3685  CA  SER B 186      35.485   8.852  41.158  1.00 67.21           C  
ANISOU 3685  CA  SER B 186     9351   7507   8678   -169   -272   -207       C  
ATOM   3686  C   SER B 186      36.677   8.198  40.456  1.00 65.98           C  
ANISOU 3686  C   SER B 186     9307   7228   8533   -169   -311   -215       C  
ATOM   3687  O   SER B 186      36.776   8.302  39.236  1.00 63.38           O  
ANISOU 3687  O   SER B 186     8989   6854   8239   -165   -333   -209       O  
ATOM   3688  CB  SER B 186      35.768  10.275  41.531  1.00 69.94           C  
ANISOU 3688  CB  SER B 186     9627   7870   9075    -63   -232   -259       C  
ATOM   3689  OG  SER B 186      36.884  10.343  42.409  1.00 81.91           O  
ANISOU 3689  OG  SER B 186    11197   9334  10591    -13   -220   -301       O  
ATOM   3690  N   PHE B 187      37.565   7.530  41.217  1.00 65.14           N  
ANISOU 3690  N   PHE B 187     9283   7067   8399   -176   -319   -230       N  
ATOM   3691  CA  PHE B 187      38.652   6.742  40.642  1.00 69.15           C  
ANISOU 3691  CA  PHE B 187     9901   7461   8911   -189   -359   -235       C  
ATOM   3692  C   PHE B 187      38.131   5.421  40.064  1.00 76.84           C  
ANISOU 3692  C   PHE B 187    10926   8430   9839   -297   -401   -178       C  
ATOM   3693  O   PHE B 187      38.640   4.954  39.041  1.00 95.44           O  
ANISOU 3693  O   PHE B 187    13345  10707  12212   -313   -435   -172       O  
ATOM   3694  CB  PHE B 187      39.810   6.522  41.630  1.00 60.66           C  
ANISOU 3694  CB  PHE B 187     8896   6324   7827   -156   -355   -272       C  
ATOM   3695  CG  PHE B 187      40.717   7.709  41.773  1.00 60.55           C  
ANISOU 3695  CG  PHE B 187     8866   6270   7871    -43   -328   -332       C  
ATOM   3696  CD1 PHE B 187      41.704   7.968  40.831  1.00 66.36           C  
ANISOU 3696  CD1 PHE B 187     9650   6909   8656      8   -346   -361       C  
ATOM   3697  CD2 PHE B 187      40.538   8.616  42.806  1.00 67.40           C  
ANISOU 3697  CD2 PHE B 187     9665   7201   8744     13   -283   -358       C  
ATOM   3698  CE1 PHE B 187      42.532   9.081  40.920  1.00 58.67           C  
ANISOU 3698  CE1 PHE B 187     8660   5898   7732    113   -323   -415       C  
ATOM   3699  CE2 PHE B 187      41.350   9.738  42.898  1.00 69.95           C  
ANISOU 3699  CE2 PHE B 187     9971   7487   9119    119   -258   -411       C  
ATOM   3700  CZ  PHE B 187      42.342   9.967  41.956  1.00 66.31           C  
ANISOU 3700  CZ  PHE B 187     9562   6930   8705    169   -279   -439       C  
ATOM   3701  N   ILE B 188      37.147   4.798  40.733  1.00 61.84           N  
ANISOU 3701  N   ILE B 188     9001   6614   7880   -373   -399   -137       N  
ATOM   3702  CA  ILE B 188      36.597   3.541  40.259  1.00 61.58           C  
ANISOU 3702  CA  ILE B 188     9014   6585   7799   -477   -438    -80       C  
ATOM   3703  C   ILE B 188      35.884   3.768  38.925  1.00 68.69           C  
ANISOU 3703  C   ILE B 188     9874   7499   8725   -494   -449    -50       C  
ATOM   3704  O   ILE B 188      36.106   2.996  37.996  1.00 76.17           O  
ANISOU 3704  O   ILE B 188    10887   8386   9670   -540   -488    -25       O  
ATOM   3705  CB  ILE B 188      35.661   2.896  41.301  1.00 60.41           C  
ANISOU 3705  CB  ILE B 188     8842   6530   7580   -553   -432    -44       C  
ATOM   3706  CG1 ILE B 188      36.454   2.330  42.478  1.00 52.94           C  
ANISOU 3706  CG1 ILE B 188     7963   5550   6600   -560   -436    -65       C  
ATOM   3707  CG2 ILE B 188      34.792   1.827  40.637  1.00 55.52           C  
ANISOU 3707  CG2 ILE B 188     8244   5937   6916   -657   -468     21       C  
ATOM   3708  CD1 ILE B 188      35.599   1.849  43.618  1.00 45.79           C  
ANISOU 3708  CD1 ILE B 188     7029   4739   5629   -626   -426    -38       C  
ATOM   3709  N   LEU B 189      35.020   4.802  38.849  1.00 64.46           N  
ANISOU 3709  N   LEU B 189     9232   7044   8216   -460   -416    -51       N  
ATOM   3710  CA  LEU B 189      34.330   5.169  37.622  1.00 64.78           C  
ANISOU 3710  CA  LEU B 189     9225   7099   8287   -469   -424    -26       C  
ATOM   3711  C   LEU B 189      35.331   5.481  36.514  1.00 64.46           C  
ANISOU 3711  C   LEU B 189     9233   6954   8305   -419   -444    -55       C  
ATOM   3712  O   LEU B 189      35.084   5.170  35.357  1.00 63.68           O  
ANISOU 3712  O   LEU B 189     9151   6828   8217   -458   -471    -25       O  
ATOM   3713  CB  LEU B 189      33.453   6.399  37.862  1.00 69.19           C  
ANISOU 3713  CB  LEU B 189     9662   7752   8875   -422   -383    -38       C  
ATOM   3714  CG  LEU B 189      31.956   6.148  37.990  1.00 82.91           C  
ANISOU 3714  CG  LEU B 189    11330   9599  10574   -493   -376     14       C  
ATOM   3715  CD1 LEU B 189      31.656   5.446  39.313  1.00 92.58           C  
ANISOU 3715  CD1 LEU B 189    12565  10881  11730   -543   -366     27       C  
ATOM   3716  CD2 LEU B 189      31.175   7.460  37.866  1.00 84.76           C  
ANISOU 3716  CD2 LEU B 189    11444   9906  10854   -439   -341      0       C  
ATOM   3717  N   ARG B 190      36.424   6.162  36.857  1.00 60.53           N  
ANISOU 3717  N   ARG B 190     8754   6401   7845   -332   -428   -113       N  
ATOM   3718  CA  ARG B 190      37.413   6.513  35.861  1.00 65.47           C  
ANISOU 3718  CA  ARG B 190     9423   6928   8525   -281   -445   -146       C  
ATOM   3719  C   ARG B 190      37.988   5.235  35.266  1.00 77.88           C  
ANISOU 3719  C   ARG B 190    11104   8415  10073   -346   -490   -123       C  
ATOM   3720  O   ARG B 190      38.178   5.180  34.054  1.00 78.97           O  
ANISOU 3720  O   ARG B 190    11267   8498  10240   -355   -514   -117       O  
ATOM   3721  CB  ARG B 190      38.497   7.400  36.481  1.00 71.09           C  
ANISOU 3721  CB  ARG B 190    10139   7598   9274   -179   -420   -211       C  
ATOM   3722  CG  ARG B 190      39.605   7.816  35.526  1.00 65.72           C  
ANISOU 3722  CG  ARG B 190     9506   6816   8651   -120   -436   -250       C  
ATOM   3723  CD  ARG B 190      40.633   8.644  36.254  1.00 67.72           C  
ANISOU 3723  CD  ARG B 190     9762   7033   8933    -21   -410   -312       C  
ATOM   3724  NE  ARG B 190      41.684   9.048  35.340  1.00 82.74           N  
ANISOU 3724  NE  ARG B 190    11710   8841  10888     34   -426   -350       N  
ATOM   3725  CZ  ARG B 190      42.665   9.897  35.634  1.00 94.25           C  
ANISOU 3725  CZ  ARG B 190    13172  10254  12383    128   -408   -406       C  
ATOM   3726  NH1 ARG B 190      42.740  10.471  36.829  1.00 99.63           N  
ANISOU 3726  NH1 ARG B 190    13817  10979  13060    181   -373   -431       N  
ATOM   3727  NH2 ARG B 190      43.561  10.185  34.707  1.00110.85           N  
ANISOU 3727  NH2 ARG B 190    15317  12271  14529    169   -427   -437       N  
ATOM   3728  N   ALA B 191      38.275   4.235  36.122  1.00 79.88           N  
ANISOU 3728  N   ALA B 191    11421   8656  10274   -392   -502   -113       N  
ATOM   3729  CA  ALA B 191      38.825   2.962  35.665  1.00 73.17           C  
ANISOU 3729  CA  ALA B 191    10675   7727   9398   -456   -547    -93       C  
ATOM   3730  C   ALA B 191      37.810   2.238  34.786  1.00 73.45           C  
ANISOU 3730  C   ALA B 191    10706   7795   9406   -547   -573    -29       C  
ATOM   3731  O   ALA B 191      38.176   1.706  33.748  1.00 73.54           O  
ANISOU 3731  O   ALA B 191    10777   7736   9429   -576   -606    -17       O  
ATOM   3732  CB  ALA B 191      39.265   2.093  36.818  1.00 77.11           C  
ANISOU 3732  CB  ALA B 191    11236   8214   9848   -486   -555    -94       C  
ATOM   3733  N   LEU B 192      36.528   2.277  35.178  1.00 76.32           N  
ANISOU 3733  N   LEU B 192    10996   8266   9735   -589   -557     11       N  
ATOM   3734  CA  LEU B 192      35.457   1.668  34.402  1.00 73.32           C  
ANISOU 3734  CA  LEU B 192    10602   7929   9329   -674   -578     75       C  
ATOM   3735  C   LEU B 192      35.388   2.285  32.996  1.00 74.43           C  
ANISOU 3735  C   LEU B 192    10719   8037   9526   -651   -585     75       C  
ATOM   3736  O   LEU B 192      35.084   1.580  32.041  1.00 76.71           O  
ANISOU 3736  O   LEU B 192    11042   8302   9803   -717   -616    118       O  
ATOM   3737  CB  LEU B 192      34.136   1.792  35.174  1.00 62.68           C  
ANISOU 3737  CB  LEU B 192     9170   6706   7941   -709   -553    108       C  
ATOM   3738  N   SER B 193      35.684   3.588  32.855  1.00 70.87           N  
ANISOU 3738  N   SER B 193    10211   7582   9136   -561   -557     28       N  
ATOM   3739  CA  SER B 193      35.733   4.246  31.558  1.00 62.93           C  
ANISOU 3739  CA  SER B 193     9185   6540   8187   -535   -565     21       C  
ATOM   3740  C   SER B 193      36.886   3.703  30.737  1.00 70.00           C  
ANISOU 3740  C   SER B 193    10180   7316   9101   -537   -598      4       C  
ATOM   3741  O   SER B 193      36.757   3.568  29.535  1.00 76.57           O  
ANISOU 3741  O   SER B 193    11027   8113   9953   -568   -621     25       O  
ATOM   3742  CB  SER B 193      35.898   5.717  31.679  1.00 61.86           C  
ANISOU 3742  CB  SER B 193     8973   6422   8109   -436   -531    -29       C  
ATOM   3743  OG  SER B 193      34.742   6.259  32.250  1.00 66.87           O  
ANISOU 3743  OG  SER B 193     9509   7167   8733   -438   -502    -10       O  
ATOM   3744  N   VAL B 194      38.023   3.453  31.379  1.00 79.36           N  
ANISOU 3744  N   VAL B 194    11432   8438  10283   -501   -600    -38       N  
ATOM   3745  CA  VAL B 194      39.187   2.962  30.664  1.00 86.41           C  
ANISOU 3745  CA  VAL B 194    12420   9215  11196   -498   -630    -61       C  
ATOM   3746  C   VAL B 194      38.908   1.545  30.162  1.00 90.68           C  
ANISOU 3746  C   VAL B 194    13030   9733  11691   -602   -671     -6       C  
ATOM   3747  O   VAL B 194      39.285   1.211  29.044  1.00105.92           O  
ANISOU 3747  O   VAL B 194    15009  11593  13642   -625   -698     -1       O  
ATOM   3748  CB  VAL B 194      40.461   3.059  31.527  1.00 84.79           C  
ANISOU 3748  CB  VAL B 194    12267   8950  11001   -433   -622   -118       C  
ATOM   3749  CG1 VAL B 194      41.681   2.486  30.831  1.00 90.30           C  
ANISOU 3749  CG1 VAL B 194    13041   9555  11715   -426   -644   -142       C  
ATOM   3750  CG2 VAL B 194      40.724   4.494  31.936  1.00 82.01           C  
ANISOU 3750  CG2 VAL B 194    11846   8619  10695   -329   -583   -170       C  
ATOM   3751  N   PHE B 195      38.238   0.720  30.975  1.00 87.08           N  
ANISOU 3751  N   PHE B 195    12578   9338  11173   -667   -675     35       N  
ATOM   3752  CA  PHE B 195      37.946  -0.646  30.575  1.00 87.74           C  
ANISOU 3752  CA  PHE B 195    12726   9404  11208   -766   -714     89       C  
ATOM   3753  C   PHE B 195      36.870  -0.661  29.490  1.00 85.41           C  
ANISOU 3753  C   PHE B 195    12390   9149  10914   -821   -723    143       C  
ATOM   3754  O   PHE B 195      36.883  -1.539  28.634  1.00 79.02           O  
ANISOU 3754  O   PHE B 195    11639   8294  10091   -886   -758    176       O  
ATOM   3755  CB  PHE B 195      37.556  -1.510  31.776  1.00 93.67           C  
ANISOU 3755  CB  PHE B 195    13494  10208  11889   -820   -718    116       C  
ATOM   3756  CG  PHE B 195      38.589  -1.585  32.870  1.00 94.77           C  
ANISOU 3756  CG  PHE B 195    13678  10306  12024   -775   -712     68       C  
ATOM   3757  CD1 PHE B 195      39.912  -1.913  32.580  1.00 86.46           C  
ANISOU 3757  CD1 PHE B 195    12713   9140  10997   -749   -735     29       C  
ATOM   3758  CD2 PHE B 195      38.231  -1.342  34.193  1.00 80.01           C  
ANISOU 3758  CD2 PHE B 195    11765   8510  10125   -761   -685     62       C  
ATOM   3759  CE1 PHE B 195      40.857  -1.979  33.590  1.00 84.40           C  
ANISOU 3759  CE1 PHE B 195    12495   8840  10735   -709   -730    -14       C  
ATOM   3760  CE2 PHE B 195      39.181  -1.426  35.202  1.00 84.02           C  
ANISOU 3760  CE2 PHE B 195    12318   8978  10629   -724   -680     20       C  
ATOM   3761  CZ  PHE B 195      40.496  -1.739  34.900  1.00 84.67           C  
ANISOU 3761  CZ  PHE B 195    12486   8945  10738   -697   -703    -18       C  
ATOM   3762  N   PHE B 196      35.948   0.309  29.530  1.00 78.24           N  
ANISOU 3762  N   PHE B 196    11379   8324  10023   -796   -693    150       N  
ATOM   3763  CA  PHE B 196      34.874   0.373  28.559  1.00 81.97           C  
ANISOU 3763  CA  PHE B 196    11806   8840  10500   -845   -699    201       C  
ATOM   3764  C   PHE B 196      35.411   0.821  27.203  1.00 82.81           C  
ANISOU 3764  C   PHE B 196    11930   8868  10666   -821   -713    182       C  
ATOM   3765  O   PHE B 196      34.988   0.304  26.172  1.00106.57           O  
ANISOU 3765  O   PHE B 196    14960  11861  13672   -885   -738    227       O  
ATOM   3766  CB  PHE B 196      33.728   1.261  29.050  1.00 94.61           C  
ANISOU 3766  CB  PHE B 196    13292  10553  12103   -826   -664    214       C  
ATOM   3767  CG  PHE B 196      32.417   1.017  28.337  1.00134.53           C  
ANISOU 3767  CG  PHE B 196    18304  15671  17142   -900   -673    281       C  
ATOM   3768  CD1 PHE B 196      32.146   1.631  27.117  1.00129.80           C  
ANISOU 3768  CD1 PHE B 196    17671  15054  16593   -893   -678    288       C  
ATOM   3769  CD2 PHE B 196      31.467   0.140  28.855  1.00145.69           C  
ANISOU 3769  CD2 PHE B 196    19713  17156  18487   -980   -680    338       C  
ATOM   3770  CE1 PHE B 196      30.951   1.391  26.449  1.00125.08           C  
ANISOU 3770  CE1 PHE B 196    17036  14509  15980   -963   -687    352       C  
ATOM   3771  CE2 PHE B 196      30.275  -0.103  28.183  1.00132.43           C  
ANISOU 3771  CE2 PHE B 196    17996  15530  16791  -1048   -689    401       C  
ATOM   3772  CZ  PHE B 196      30.016   0.528  26.983  1.00127.82           C  
ANISOU 3772  CZ  PHE B 196    17378  14927  16260  -1039   -692    409       C  
ATOM   3773  N   LYS B 197      36.319   1.802  27.213  1.00 81.64           N  
ANISOU 3773  N   LYS B 197    11772   8674  10573   -729   -696    117       N  
ATOM   3774  CA  LYS B 197      36.950   2.308  26.002  1.00 79.69           C  
ANISOU 3774  CA  LYS B 197    11543   8349  10385   -698   -708     90       C  
ATOM   3775  C   LYS B 197      37.744   1.189  25.341  1.00 78.71           C  
ANISOU 3775  C   LYS B 197    11527   8131  10248   -747   -745     96       C  
ATOM   3776  O   LYS B 197      37.684   1.038  24.128  1.00 80.65           O  
ANISOU 3776  O   LYS B 197    11743   8395  10504   -759   -744    112       O  
ATOM   3777  CB  LYS B 197      37.868   3.503  26.293  1.00 81.59           C  
ANISOU 3777  CB  LYS B 197    11761   8560  10681   -588   -683     16       C  
ATOM   3778  CG  LYS B 197      38.539   4.150  25.081  1.00 89.40           C  
ANISOU 3778  CG  LYS B 197    12763   9473  11732   -550   -694    -18       C  
ATOM   3779  CD  LYS B 197      39.077   5.546  25.349  1.00 94.79           C  
ANISOU 3779  CD  LYS B 197    13393  10154  12468   -442   -667    -82       C  
ATOM   3780  CE  LYS B 197      39.387   6.334  24.093  1.00 97.17           C  
ANISOU 3780  CE  LYS B 197    13648  10451  12820   -403   -657   -104       C  
ATOM   3781  NZ  LYS B 197      40.681   5.953  23.476  1.00 85.17           N  
ANISOU 3781  NZ  LYS B 197    12105   8966  11289   -364   -617   -132       N  
ATOM   3782  N   ASP B 198      38.469   0.411  26.155  1.00 85.38           N  
ANISOU 3782  N   ASP B 198    12409   8977  11054   -736   -740     79       N  
ATOM   3783  CA  ASP B 198      39.318  -0.668  25.674  1.00 89.06           C  
ANISOU 3783  CA  ASP B 198    12881   9466  11491   -732   -733     75       C  
ATOM   3784  C   ASP B 198      38.457  -1.805  25.140  1.00 93.50           C  
ANISOU 3784  C   ASP B 198    13470  10050  12005   -832   -763    143       C  
ATOM   3785  O   ASP B 198      38.810  -2.416  24.136  1.00106.79           O  
ANISOU 3785  O   ASP B 198    15139  11754  13683   -833   -760    148       O  
ATOM   3786  CB  ASP B 198      40.273  -1.189  26.751  1.00 97.26           C  
ANISOU 3786  CB  ASP B 198    13948  10501  12503   -697   -724     42       C  
ATOM   3787  CG  ASP B 198      41.192  -2.303  26.279  1.00103.06           C  
ANISOU 3787  CG  ASP B 198    14684  11259  13214   -691   -719     37       C  
ATOM   3788  OD1 ASP B 198      41.553  -2.291  25.084  1.00107.47           O  
ANISOU 3788  OD1 ASP B 198    15205  11834  13796   -671   -705     30       O  
ATOM   3789  OD2 ASP B 198      41.527  -3.179  27.110  1.00127.26           O1-
ANISOU 3789  OD2 ASP B 198    17788  14325  16238   -709   -730     40       O1-
ATOM   3790  N   ALA B 199      37.344  -2.087  25.825  1.00 89.84           N  
ANISOU 3790  N   ALA B 199    13042   9588  11507   -917   -790    197       N  
ATOM   3791  CA  ALA B 199      36.473  -3.187  25.455  1.00 90.94           C  
ANISOU 3791  CA  ALA B 199    13202   9758  11592  -1016   -817    267       C  
ATOM   3792  C   ALA B 199      35.732  -2.878  24.154  1.00 97.18           C  
ANISOU 3792  C   ALA B 199    13950  10566  12407  -1043   -819    302       C  
ATOM   3793  O   ALA B 199      35.346  -3.807  23.458  1.00112.29           O  
ANISOU 3793  O   ALA B 199    15869  12511  14286  -1096   -832    345       O  
ATOM   3794  CB  ALA B 199      35.534  -3.523  26.589  1.00 82.64           C  
ANISOU 3794  CB  ALA B 199    12166   8743  10490  -1086   -829    313       C  
ATOM   3795  N   ALA B 200      35.556  -1.591  23.813  1.00102.33           N  
ANISOU 3795  N   ALA B 200    14560  11201  13121  -1004   -807    282       N  
ATOM   3796  CA  ALA B 200      34.864  -1.196  22.591  1.00 96.00           C  
ANISOU 3796  CA  ALA B 200    13712  10415  12348  -1027   -809    312       C  
ATOM   3797  C   ALA B 200      35.786  -1.271  21.368  1.00 98.74           C  
ANISOU 3797  C   ALA B 200    14032  10769  12718   -965   -788    273       C  
ATOM   3798  O   ALA B 200      35.311  -1.249  20.232  1.00104.44           O  
ANISOU 3798  O   ALA B 200    14722  11510  13452   -989   -789    299       O  
ATOM   3799  CB  ALA B 200      34.226   0.167  22.753  1.00 86.10           C  
ANISOU 3799  CB  ALA B 200    12382   9193  11140   -990   -790    303       C  
ATOM   3800  N   LEU B 201      37.102  -1.386  21.593  1.00100.29           N  
ANISOU 3800  N   LEU B 201    14233  10953  12918   -890   -766    212       N  
ATOM   3801  CA  LEU B 201      38.047  -1.545  20.500  1.00105.77           C  
ANISOU 3801  CA  LEU B 201    14897  11660  13630   -840   -743    178       C  
ATOM   3802  C   LEU B 201      37.802  -2.871  19.791  1.00129.17           C  
ANISOU 3802  C   LEU B 201    17880  14653  16547   -899   -758    220       C  
ATOM   3803  O   LEU B 201      38.033  -2.954  18.588  1.00180.50           O  
ANISOU 3803  O   LEU B 201    24350  21169  23062   -888   -746    216       O  
ATOM   3804  CB  LEU B 201      39.483  -1.549  21.023  1.00116.63           C  
ANISOU 3804  CB  LEU B 201    16271  13028  15013   -760   -717    115       C  
ATOM   3805  CG  LEU B 201      39.983  -0.277  21.693  1.00126.52           C  
ANISOU 3805  CG  LEU B 201    17500  14261  16312   -684   -694     62       C  
ATOM   3806  CD1 LEU B 201      41.422  -0.476  22.157  1.00130.18           C  
ANISOU 3806  CD1 LEU B 201    17956  14730  16776   -615   -665      9       C  
ATOM   3807  CD2 LEU B 201      39.863   0.912  20.755  1.00115.25           C  
ANISOU 3807  CD2 LEU B 201    16016  12835  14940   -648   -677     44       C  
ATOM   3808  N   LYS B 202      37.400  -3.909  20.543  1.00115.71           N  
ANISOU 3808  N   LYS B 202    16224  12955  14784   -959   -784    259       N  
ATOM   3809  CA  LYS B 202      37.065  -5.196  19.957  1.00113.99           C  
ANISOU 3809  CA  LYS B 202    16027  12767  14517  -1017   -803    302       C  
ATOM   3810  C   LYS B 202      35.717  -5.070  19.241  1.00114.93           C  
ANISOU 3810  C   LYS B 202    16127  12908  14633  -1085   -817    363       C  
ATOM   3811  O   LYS B 202      34.664  -5.005  19.877  1.00103.27           O  
ANISOU 3811  O   LYS B 202    14663  11440  13135  -1148   -836    412       O  
ATOM   3812  CB  LYS B 202      37.141  -6.308  21.010  1.00130.02           C  
ANISOU 3812  CB  LYS B 202    18113  14802  16487  -1054   -825    319       C  
ATOM   3813  CG  LYS B 202      36.914  -7.726  20.490  1.00139.22           C  
ANISOU 3813  CG  LYS B 202    19303  15999  17597  -1107   -847    358       C  
ATOM   3814  CD  LYS B 202      36.742  -8.765  21.588  1.00126.99           C  
ANISOU 3814  CD  LYS B 202    17808  14458  15984  -1157   -876    384       C  
ATOM   3815  CE  LYS B 202      36.598 -10.179  21.064  1.00123.50           C  
ANISOU 3815  CE  LYS B 202    17389  14046  15488  -1202   -899    416       C  
ATOM   3816  NZ  LYS B 202      36.237 -11.131  22.143  1.00119.41           N  
ANISOU 3816  NZ  LYS B 202    16923  13543  14905  -1261   -931    449       N  
ATOM   3817  N   TRP B 203      35.781  -5.011  17.901  1.00119.88           N  
ANISOU 3817  N   TRP B 203    16718  13548  15281  -1072   -805    360       N  
ATOM   3818  CA  TRP B 203      34.633  -4.830  17.021  1.00117.92           C  
ANISOU 3818  CA  TRP B 203    16443  13324  15038  -1125   -814    411       C  
ATOM   3819  C   TRP B 203      33.854  -3.560  17.398  1.00106.40           C  
ANISOU 3819  C   TRP B 203    14955  11852  13619  -1134   -814    424       C  
ATOM   3820  O   TRP B 203      34.321  -2.473  17.020  1.00100.87           O  
ANISOU 3820  O   TRP B 203    14219  11131  12977  -1073   -794    379       O  
ATOM   3821  CB  TRP B 203      33.741  -6.083  17.024  1.00133.72           C  
ANISOU 3821  CB  TRP B 203    18473  15362  16972  -1208   -841    477       C  
ATOM   3822  N   GLY B 216      35.623  -2.796   7.795  1.00 97.07           N  
ANISOU 3822  N   GLY B 216    13529  10762  12590   -993   -687    322       N  
ATOM   3823  CA  GLY B 216      34.275  -3.080   7.266  1.00108.14           C  
ANISOU 3823  CA  GLY B 216    14927  12187  13974  -1058   -707    383       C  
ATOM   3824  C   GLY B 216      33.237  -2.066   7.747  1.00118.89           C  
ANISOU 3824  C   GLY B 216    16270  13542  15361  -1082   -721    412       C  
ATOM   3825  O   GLY B 216      32.778  -1.224   6.969  1.00119.20           O  
ANISOU 3825  O   GLY B 216    16268  13587  15436  -1082   -713    415       O  
ATOM   3826  N   LEU B 217      32.867  -2.158   9.033  1.00107.91           N  
ANISOU 3826  N   LEU B 217    14907  12140  13952  -1106   -741    433       N  
ATOM   3827  CA  LEU B 217      31.861  -1.267   9.602  1.00106.82           C  
ANISOU 3827  CA  LEU B 217    14751  11998  13839  -1135   -756    465       C  
ATOM   3828  C   LEU B 217      32.519  -0.005  10.175  1.00112.07           C  
ANISOU 3828  C   LEU B 217    15398  12628  14556  -1074   -744    411       C  
ATOM   3829  O   LEU B 217      33.707   0.222   9.949  1.00109.58           O  
ANISOU 3829  O   LEU B 217    15078  12298  14258  -1010   -720    352       O  
ATOM   3830  CB  LEU B 217      31.021  -2.020  10.640  1.00 96.96           C  
ANISOU 3830  CB  LEU B 217    13537  10762  12541  -1199   -783    522       C  
ATOM   3831  N   LEU B 218      31.725   0.799  10.912  1.00119.68           N  
ANISOU 3831  N   LEU B 218    16347  13582  15544  -1096   -761    435       N  
ATOM   3832  CA  LEU B 218      32.034   2.161  11.348  1.00107.67           C  
ANISOU 3832  CA  LEU B 218    14799  12031  14080  -1045   -755    393       C  
ATOM   3833  C   LEU B 218      33.119   2.159  12.420  1.00102.53           C  
ANISOU 3833  C   LEU B 218    14181  11350  13424   -989   -747    341       C  
ATOM   3834  O   LEU B 218      32.940   1.491  13.431  1.00 99.41           O  
ANISOU 3834  O   LEU B 218    13827  10951  12992  -1020   -762    364       O  
ATOM   3835  CB  LEU B 218      30.759   2.787  11.926  1.00 85.10           C  
ANISOU 3835  CB  LEU B 218    11917   9174  11243  -1096   -781    444       C  
ATOM   3836  N   SER B 219      34.187   2.948  12.207  1.00100.88           N  
ANISOU 3836  N   SER B 219    13952  11125  13252   -910   -721    274       N  
ATOM   3837  CA  SER B 219      35.329   3.059  13.114  1.00108.77           C  
ANISOU 3837  CA  SER B 219    14973  12102  14253   -846   -706    218       C  
ATOM   3838  C   SER B 219      34.901   3.550  14.499  1.00108.87           C  
ANISOU 3838  C   SER B 219    15001  12087  14275   -848   -726    223       C  
ATOM   3839  O   SER B 219      33.891   4.240  14.610  1.00101.41           O  
ANISOU 3839  O   SER B 219    14033  11138  13360   -880   -748    254       O  
ATOM   3840  CB  SER B 219      36.415   3.946  12.548  1.00116.33           C  
ANISOU 3840  CB  SER B 219    15893  13059  15248   -765   -672    151       C  
ATOM   3841  N   TYR B 220      35.672   3.175  15.540  1.00108.69           N  
ANISOU 3841  N   TYR B 220    15016  12050  14230   -815   -720    193       N  
ATOM   3842  CA  TYR B 220      35.358   3.538  16.917  1.00 98.53           C  
ANISOU 3842  CA  TYR B 220    13751  10737  12948   -814   -737    194       C  
ATOM   3843  C   TYR B 220      35.543   5.044  17.113  1.00102.75           C  
ANISOU 3843  C   TYR B 220    14245  11250  13547   -745   -730    147       C  
ATOM   3844  O   TYR B 220      34.828   5.659  17.906  1.00109.74           O  
ANISOU 3844  O   TYR B 220    15126  12115  14456   -757   -753    161       O  
ATOM   3845  CB  TYR B 220      36.146   2.713  17.948  1.00 87.84           C  
ANISOU 3845  CB  TYR B 220    12448   9375  11551   -796   -730    174       C  
ATOM   3846  CG  TYR B 220      35.871   3.087  19.389  1.00 87.86           C  
ANISOU 3846  CG  TYR B 220    12477   9351  11556   -793   -745    170       C  
ATOM   3847  CD1 TYR B 220      34.623   2.875  19.950  1.00 88.05           C  
ANISOU 3847  CD1 TYR B 220    12519   9376  11562   -878   -776    234       C  
ATOM   3848  CD2 TYR B 220      36.834   3.685  20.194  1.00 85.54           C  
ANISOU 3848  CD2 TYR B 220    12184   9037  11281   -708   -725    106       C  
ATOM   3849  CE1 TYR B 220      34.341   3.232  21.259  1.00 97.41           C  
ANISOU 3849  CE1 TYR B 220    13668  10611  12731   -845   -756    223       C  
ATOM   3850  CE2 TYR B 220      36.577   4.038  21.511  1.00 85.05           C  
ANISOU 3850  CE2 TYR B 220    12146   8949  11220   -701   -737    100       C  
ATOM   3851  CZ  TYR B 220      35.321   3.805  22.049  1.00 95.48           C  
ANISOU 3851  CZ  TYR B 220    13430  10342  12507   -757   -737    155       C  
ATOM   3852  OH  TYR B 220      35.010   4.153  23.332  1.00 91.97           O  
ANISOU 3852  OH  TYR B 220    12933   9971  12042   -717   -707    143       O  
ATOM   3853  N   GLN B 221      36.497   5.634  16.378  1.00 96.17           N  
ANISOU 3853  N   GLN B 221    13376  10424  12739   -675   -699     93       N  
ATOM   3854  CA  GLN B 221      36.797   7.053  16.522  1.00 91.57           C  
ANISOU 3854  CA  GLN B 221    12752   9830  12212   -600   -688     43       C  
ATOM   3855  C   GLN B 221      35.611   7.889  16.040  1.00 97.52           C  
ANISOU 3855  C   GLN B 221    13464  10578  13011   -635   -718     76       C  
ATOM   3856  O   GLN B 221      35.411   8.998  16.520  1.00100.93           O  
ANISOU 3856  O   GLN B 221    13864  10991  13493   -592   -730     51       O  
ATOM   3857  CB  GLN B 221      38.092   7.418  15.791  1.00 96.77           C  
ANISOU 3857  CB  GLN B 221    13379  10511  12877   -529   -643    -14       C  
ATOM   3858  N   ASP B 222      34.829   7.346  15.094  1.00106.41           N  
ANISOU 3858  N   ASP B 222    14584  11724  14123   -710   -730    131       N  
ATOM   3859  CA  ASP B 222      33.748   8.065  14.433  1.00105.22           C  
ANISOU 3859  CA  ASP B 222    14384  11578  14015   -748   -754    166       C  
ATOM   3860  C   ASP B 222      32.437   7.899  15.203  1.00101.01           C  
ANISOU 3860  C   ASP B 222    13854  11039  13487   -826   -793    232       C  
ATOM   3861  O   ASP B 222      31.501   8.668  15.007  1.00 99.92           O  
ANISOU 3861  O   ASP B 222    13638  10945  13383   -831   -795    253       O  
ATOM   3862  CB  ASP B 222      33.626   7.641  12.963  1.00 85.72           C  
ANISOU 3862  CB  ASP B 222    11899   9142  11529   -783   -741    188       C  
ATOM   3863  N   SER B 223      32.375   6.893  16.077  1.00110.10           N  
ANISOU 3863  N   SER B 223    15052  12198  14582   -861   -793    258       N  
ATOM   3864  CA  SER B 223      31.135   6.540  16.752  1.00113.13           C  
ANISOU 3864  CA  SER B 223    15382  12678  14922   -903   -780    314       C  
ATOM   3865  C   SER B 223      30.774   7.587  17.799  1.00107.38           C  
ANISOU 3865  C   SER B 223    14560  12031  14210   -825   -745    281       C  
ATOM   3866  O   SER B 223      31.626   8.356  18.234  1.00 98.79           O  
ANISOU 3866  O   SER B 223    13464  10920  13152   -738   -731    215       O  
ATOM   3867  CB  SER B 223      31.219   5.165  17.363  1.00122.26           C  
ANISOU 3867  CB  SER B 223    16611  13834  16007   -957   -785    346       C  
ATOM   3868  OG  SER B 223      32.180   5.134  18.405  1.00110.93           O  
ANISOU 3868  OG  SER B 223    15209  12381  14558   -893   -769    292       O  
ATOM   3869  N   LEU B 224      29.499   7.583  18.205  1.00112.59           N  
ANISOU 3869  N   LEU B 224    15148  12784  14847   -858   -733    329       N  
ATOM   3870  CA  LEU B 224      29.030   8.471  19.255  1.00103.16           C  
ANISOU 3870  CA  LEU B 224    13861  11674  13662   -794   -699    304       C  
ATOM   3871  C   LEU B 224      29.314   7.871  20.626  1.00107.29           C  
ANISOU 3871  C   LEU B 224    14410  12227  14127   -779   -678    292       C  
ATOM   3872  O   LEU B 224      29.442   8.633  21.579  1.00114.71           O  
ANISOU 3872  O   LEU B 224    15297  13209  15079   -705   -649    249       O  
ATOM   3873  CB  LEU B 224      27.535   8.775  19.092  1.00 92.45           C  
ANISOU 3873  CB  LEU B 224    12411  10406  12309   -836   -694    357       C  
ATOM   3874  CG  LEU B 224      26.943   9.687  20.171  1.00 92.78           C  
ANISOU 3874  CG  LEU B 224    12351  10542  12361   -775   -658    333       C  
ATOM   3875  CD1 LEU B 224      26.188  10.879  19.616  1.00100.19           C  
ANISOU 3875  CD1 LEU B 224    13189  11518  13362   -751   -656    331       C  
ATOM   3876  CD2 LEU B 224      26.132   8.898  21.179  1.00 77.79           C  
ANISOU 3876  CD2 LEU B 224    10438   8724  10393   -821   -641    375       C  
ATOM   3877  N   ALA B 225      29.376   6.529  20.712  1.00104.73           N  
ANISOU 3877  N   ALA B 225    14166  11884  13744   -851   -694    332       N  
ATOM   3878  CA  ALA B 225      29.663   5.805  21.940  1.00 95.03           C  
ANISOU 3878  CA  ALA B 225    12974  10676  12456   -850   -682    327       C  
ATOM   3879  C   ALA B 225      30.989   6.273  22.530  1.00 96.04           C  
ANISOU 3879  C   ALA B 225    13134  10750  12606   -760   -669    250       C  
ATOM   3880  O   ALA B 225      31.113   6.416  23.736  1.00 89.95           O  
ANISOU 3880  O   ALA B 225    12343  10020  11814   -718   -644    224       O  
ATOM   3881  CB  ALA B 225      29.700   4.321  21.660  1.00102.03           C  
ANISOU 3881  CB  ALA B 225    13953  11527  13286   -940   -710    377       C  
ATOM   3882  N   CYS B 226      31.969   6.503  21.655  1.00101.88           N  
ANISOU 3882  N   CYS B 226    13924  11396  13389   -733   -687    215       N  
ATOM   3883  CA  CYS B 226      33.303   6.902  22.060  1.00 95.59           C  
ANISOU 3883  CA  CYS B 226    13167  10537  12616   -651   -679    144       C  
ATOM   3884  C   CYS B 226      33.294   8.292  22.696  1.00 98.41           C  
ANISOU 3884  C   CYS B 226    13437  10942  13014   -555   -647     94       C  
ATOM   3885  O   CYS B 226      33.973   8.505  23.694  1.00 90.87           O  
ANISOU 3885  O   CYS B 226    12490   9985  12052   -493   -626     49       O  
ATOM   3886  CB  CYS B 226      34.234   6.885  20.859  1.00 92.74           C  
ANISOU 3886  CB  CYS B 226    12872  10071  12293   -650   -707    121       C  
ATOM   3887  SG  CYS B 226      35.870   7.538  21.250  1.00 99.91           S  
ANISOU 3887  SG  CYS B 226    13822  10901  13238   -543   -697     30       S  
ATOM   3888  N   ARG B 227      32.501   9.217  22.141  1.00 93.00           N  
ANISOU 3888  N   ARG B 227    12665  10300  12371   -545   -643    103       N  
ATOM   3889  CA  ARG B 227      32.424  10.582  22.637  1.00 75.91           C  
ANISOU 3889  CA  ARG B 227    10412   8182  10250   -456   -615     57       C  
ATOM   3890  C   ARG B 227      31.739  10.625  24.002  1.00 77.33           C  
ANISOU 3890  C   ARG B 227    10532   8458  10393   -443   -582     65       C  
ATOM   3891  O   ARG B 227      32.081  11.470  24.819  1.00 76.19           O  
ANISOU 3891  O   ARG B 227    10345   8337  10267   -361   -554     15       O  
ATOM   3892  CB  ARG B 227      31.671  11.441  21.625  1.00 79.97           C  
ANISOU 3892  CB  ARG B 227    10853   8717  10817   -462   -625     72       C  
ATOM   3893  CG  ARG B 227      32.184  11.283  20.203  1.00 87.95           C  
ANISOU 3893  CG  ARG B 227    11922   9638  11859   -493   -661     75       C  
ATOM   3894  CD  ARG B 227      31.459  12.118  19.166  1.00 76.98           C  
ANISOU 3894  CD  ARG B 227    10464   8263  10522   -504   -674     90       C  
ATOM   3895  NE  ARG B 227      31.843  11.662  17.840  1.00 80.77           N  
ANISOU 3895  NE  ARG B 227    11012   8660  11017   -558   -710    106       N  
ATOM   3896  CZ  ARG B 227      32.920  12.059  17.175  1.00 98.14           C  
ANISOU 3896  CZ  ARG B 227    13257  10776  13255   -519   -725     58       C  
ATOM   3897  NH1 ARG B 227      33.748  12.947  17.703  1.00115.58           N  
ANISOU 3897  NH1 ARG B 227    15450  12971  15493   -422   -709     -9       N  
ATOM   3898  NH2 ARG B 227      33.172  11.567  15.974  1.00113.74           N  
ANISOU 3898  NH2 ARG B 227    15294  12682  15241   -579   -756     78       N  
ATOM   3899  N   LEU B 228      30.787   9.711  24.253  1.00 77.85           N  
ANISOU 3899  N   LEU B 228    10596   8580  10405   -526   -584    126       N  
ATOM   3900  CA  LEU B 228      30.106   9.630  25.540  1.00 81.58           C  
ANISOU 3900  CA  LEU B 228    11016   9144  10835   -525   -554    136       C  
ATOM   3901  C   LEU B 228      31.014   9.021  26.604  1.00 74.52           C  
ANISOU 3901  C   LEU B 228    10191   8224   9900   -505   -544    107       C  
ATOM   3902  O   LEU B 228      31.044   9.488  27.736  1.00 71.69           O  
ANISOU 3902  O   LEU B 228     9790   7914   9533   -453   -513     77       O  
ATOM   3903  CB  LEU B 228      28.794   8.843  25.417  1.00 90.90           C  
ANISOU 3903  CB  LEU B 228    12175  10393  11972   -622   -561    211       C  
ATOM   3904  CG  LEU B 228      27.650   9.521  24.651  1.00 84.42           C  
ANISOU 3904  CG  LEU B 228    11264   9623  11188   -642   -563    242       C  
ATOM   3905  CD1 LEU B 228      26.386   8.672  24.728  1.00 82.37           C  
ANISOU 3905  CD1 LEU B 228    10986   9435  10876   -736   -568    315       C  
ATOM   3906  CD2 LEU B 228      27.369  10.921  25.195  1.00 70.18           C  
ANISOU 3906  CD2 LEU B 228     9354   7880   9432   -558   -532    198       C  
ATOM   3907  N   VAL B 229      31.745   7.969  26.244  1.00 74.30           N  
ANISOU 3907  N   VAL B 229    10268   8119   9845   -548   -572    118       N  
ATOM   3908  CA  VAL B 229      32.692   7.349  27.159  1.00 76.33           C  
ANISOU 3908  CA  VAL B 229    10598   8337  10066   -531   -568     91       C  
ATOM   3909  C   VAL B 229      33.805   8.343  27.471  1.00 72.61           C  
ANISOU 3909  C   VAL B 229    10125   7821   9642   -425   -551     16       C  
ATOM   3910  O   VAL B 229      34.280   8.391  28.591  1.00 81.57           O  
ANISOU 3910  O   VAL B 229    11268   8966  10759   -383   -530    -16       O  
ATOM   3911  CB  VAL B 229      33.218   6.012  26.596  1.00 75.86           C  
ANISOU 3911  CB  VAL B 229    10651   8201   9973   -603   -605    119       C  
ATOM   3912  CG1 VAL B 229      34.371   5.446  27.399  1.00 62.61           C  
ANISOU 3912  CG1 VAL B 229     9055   6466   8270   -579   -607     83       C  
ATOM   3913  CG2 VAL B 229      32.102   4.980  26.507  1.00 88.91           C  
ANISOU 3913  CG2 VAL B 229    12305   9908  11568   -707   -620    194       C  
ATOM   3914  N   PHE B 230      34.187   9.163  26.490  1.00 75.98           N  
ANISOU 3914  N   PHE B 230    10539   8200  10129   -382   -560    -11       N  
ATOM   3915  CA  PHE B 230      35.176  10.213  26.697  1.00 80.79           C  
ANISOU 3915  CA  PHE B 230    11140   8771  10787   -279   -545    -81       C  
ATOM   3916  C   PHE B 230      34.592  11.347  27.535  1.00 76.29           C  
ANISOU 3916  C   PHE B 230    10463   8289  10236   -215   -507   -103       C  
ATOM   3917  O   PHE B 230      35.308  11.943  28.324  1.00 75.41           O  
ANISOU 3917  O   PHE B 230    10347   8170  10137   -136   -485   -155       O  
ATOM   3918  CB  PHE B 230      35.700  10.742  25.362  1.00 86.38           C  
ANISOU 3918  CB  PHE B 230    11864   9405  11551   -258   -568   -102       C  
ATOM   3919  CG  PHE B 230      36.798  11.766  25.464  1.00 78.05           C  
ANISOU 3919  CG  PHE B 230    10809   8301  10544   -155   -557   -174       C  
ATOM   3920  CD1 PHE B 230      37.945  11.513  26.199  1.00 86.69           C  
ANISOU 3920  CD1 PHE B 230    11971   9343  11625   -111   -550   -215       C  
ATOM   3921  CD2 PHE B 230      36.690  12.981  24.814  1.00 80.18           C  
ANISOU 3921  CD2 PHE B 230    11016   8577  10874   -104   -557   -199       C  
ATOM   3922  CE1 PHE B 230      38.950  12.465  26.301  1.00 83.74           C  
ANISOU 3922  CE1 PHE B 230    11597   8925  11294    -15   -540   -280       C  
ATOM   3923  CE2 PHE B 230      37.709  13.924  24.892  1.00 78.88           C  
ANISOU 3923  CE2 PHE B 230    10853   8368  10751     -9   -549   -264       C  
ATOM   3924  CZ  PHE B 230      38.835  13.669  25.644  1.00 76.81           C  
ANISOU 3924  CZ  PHE B 230    10657   8056  10473     37   -539   -304       C  
ATOM   3925  N   LEU B 231      33.297  11.635  27.369  1.00 76.55           N  
ANISOU 3925  N   LEU B 231    10411   8405  10271   -249   -501    -64       N  
ATOM   3926  CA  LEU B 231      32.633  12.634  28.190  1.00 72.74           C  
ANISOU 3926  CA  LEU B 231     9823   8013   9803   -196   -465    -82       C  
ATOM   3927  C   LEU B 231      32.498  12.163  29.641  1.00 68.43           C  
ANISOU 3927  C   LEU B 231     9276   7521   9202   -201   -438    -81       C  
ATOM   3928  O   LEU B 231      32.683  12.969  30.553  1.00 66.89           O  
ANISOU 3928  O   LEU B 231     9033   7362   9020   -128   -406   -122       O  
ATOM   3929  CB  LEU B 231      31.296  13.066  27.578  1.00 64.37           C  
ANISOU 3929  CB  LEU B 231     8672   7022   8763   -233   -467    -42       C  
ATOM   3930  CG  LEU B 231      30.575  14.144  28.391  1.00 69.07           C  
ANISOU 3930  CG  LEU B 231     9152   7712   9379   -177   -431    -62       C  
ATOM   3931  CD1 LEU B 231      31.315  15.472  28.358  1.00 63.97           C  
ANISOU 3931  CD1 LEU B 231     8472   7039   8795    -71   -420   -128       C  
ATOM   3932  CD2 LEU B 231      29.142  14.340  27.935  1.00 65.15           C  
ANISOU 3932  CD2 LEU B 231     8571   7292   8892   -228   -433    -15       C  
ATOM   3933  N   LEU B 232      32.217  10.870  29.850  1.00 67.06           N  
ANISOU 3933  N   LEU B 232     9159   7353   8967   -286   -451    -34       N  
ATOM   3934  CA  LEU B 232      32.191  10.299  31.191  1.00 76.50           C  
ANISOU 3934  CA  LEU B 232    10369   8591  10106   -299   -431    -33       C  
ATOM   3935  C   LEU B 232      33.585  10.327  31.823  1.00 84.14           C  
ANISOU 3935  C   LEU B 232    11405   9489  11077   -236   -424    -87       C  
ATOM   3936  O   LEU B 232      33.722  10.599  33.013  1.00 88.71           O  
ANISOU 3936  O   LEU B 232    11960  10105  11640   -196   -395   -114       O  
ATOM   3937  CB  LEU B 232      31.642   8.872  31.141  1.00 73.95           C  
ANISOU 3937  CB  LEU B 232    10099   8280   9718   -408   -454     30       C  
ATOM   3938  CG  LEU B 232      31.513   8.157  32.485  1.00 70.92           C  
ANISOU 3938  CG  LEU B 232     9732   7944   9269   -437   -439     39       C  
ATOM   3939  CD1 LEU B 232      30.646   8.930  33.466  1.00 70.32           C  
ANISOU 3939  CD1 LEU B 232     9551   7976   9191   -409   -398     30       C  
ATOM   3940  CD2 LEU B 232      30.970   6.743  32.287  1.00 73.97           C  
ANISOU 3940  CD2 LEU B 232    10175   8338   9593   -548   -468    104       C  
ATOM   3941  N   MET B 233      34.619  10.041  31.028  1.00 83.87           N  
ANISOU 3941  N   MET B 233    11454   9351  11063   -227   -452   -104       N  
ATOM   3942  CA  MET B 233      35.994  10.075  31.501  1.00 75.52           C  
ANISOU 3942  CA  MET B 233    10464   8216  10013   -166   -449   -156       C  
ATOM   3943  C   MET B 233      36.335  11.492  31.969  1.00 77.88           C  
ANISOU 3943  C   MET B 233    10696   8535  10360    -59   -417   -214       C  
ATOM   3944  O   MET B 233      36.890  11.656  33.053  1.00 84.54           O  
ANISOU 3944  O   MET B 233    11549   9380  11191    -11   -393   -247       O  
ATOM   3945  CB  MET B 233      36.949   9.591  30.405  1.00 76.16           C  
ANISOU 3945  CB  MET B 233    10638   8187  10114   -179   -486   -164       C  
ATOM   3946  CG  MET B 233      38.415   9.952  30.593  1.00 89.65           C  
ANISOU 3946  CG  MET B 233    12404   9809  11851    -99   -484   -227       C  
ATOM   3947  SD  MET B 233      39.520   8.537  30.961  1.00105.30           S  
ANISOU 3947  SD  MET B 233    14520  11700  13789   -139   -509   -229       S  
ATOM   3948  CE  MET B 233      39.038   7.350  29.702  1.00110.77           C  
ANISOU 3948  CE  MET B 233    15266  12361  14460   -250   -553   -169       C  
ATOM   3949  N   GLN B 234      35.972  12.512  31.176  1.00 77.07           N  
ANISOU 3949  N   GLN B 234    10525   8447  10311    -23   -416   -223       N  
ATOM   3950  CA  GLN B 234      36.221  13.899  31.541  1.00 76.87           C  
ANISOU 3950  CA  GLN B 234    10431   8443  10332     78   -388   -275       C  
ATOM   3951  C   GLN B 234      35.492  14.250  32.836  1.00 77.53           C  
ANISOU 3951  C   GLN B 234    10438   8627  10392     94   -348   -275       C  
ATOM   3952  O   GLN B 234      35.998  15.048  33.616  1.00 83.55           O  
ANISOU 3952  O   GLN B 234    11174   9397  11172    176   -321   -322       O  
ATOM   3953  CB  GLN B 234      35.791  14.867  30.440  1.00 81.94           C  
ANISOU 3953  CB  GLN B 234    11008   9093  11033    101   -398   -278       C  
ATOM   3954  CG  GLN B 234      36.744  14.906  29.256  1.00 90.22           C  
ANISOU 3954  CG  GLN B 234    12124  10038  12118    116   -431   -299       C  
ATOM   3955  CD  GLN B 234      38.127  15.372  29.636  1.00 94.86           C  
ANISOU 3955  CD  GLN B 234    12759  10557  12726    203   -423   -361       C  
ATOM   3956  OE1 GLN B 234      38.313  16.175  30.540  1.00 95.85           O  
ANISOU 3956  OE1 GLN B 234    12840  10717  12863    278   -392   -398       O  
ATOM   3957  NE2 GLN B 234      39.127  14.881  28.925  1.00115.14           N  
ANISOU 3957  NE2 GLN B 234    15419  13027  15301    196   -451   -375       N  
ATOM   3958  N   TYR B 235      34.310  13.664  33.050  1.00 64.66           N  
ANISOU 3958  N   TYR B 235     8772   7075   8723     17   -346   -224       N  
ATOM   3959  CA  TYR B 235      33.579  13.887  34.282  1.00 63.07           C  
ANISOU 3959  CA  TYR B 235     8501   6971   8494     22   -309   -222       C  
ATOM   3960  C   TYR B 235      34.324  13.288  35.482  1.00 63.71           C  
ANISOU 3960  C   TYR B 235     8645   7033   8531     28   -295   -240       C  
ATOM   3961  O   TYR B 235      34.396  13.913  36.540  1.00 61.89           O  
ANISOU 3961  O   TYR B 235     8370   6845   8300     83   -260   -272       O  
ATOM   3962  CB  TYR B 235      32.148  13.361  34.168  1.00 57.22           C  
ANISOU 3962  CB  TYR B 235     7709   6314   7720    -66   -312   -162       C  
ATOM   3963  CG  TYR B 235      31.355  13.534  35.433  1.00 55.42           C  
ANISOU 3963  CG  TYR B 235     7408   6188   7459    -69   -274   -160       C  
ATOM   3964  CD1 TYR B 235      30.858  14.783  35.787  1.00 52.21           C  
ANISOU 3964  CD1 TYR B 235     6896   5849   7093     -4   -242   -188       C  
ATOM   3965  CD2 TYR B 235      31.147  12.464  36.293  1.00 53.49           C  
ANISOU 3965  CD2 TYR B 235     7205   5972   7146   -135   -271   -132       C  
ATOM   3966  CE1 TYR B 235      30.134  14.961  36.954  1.00 55.65           C  
ANISOU 3966  CE1 TYR B 235     7264   6381   7501     -7   -206   -189       C  
ATOM   3967  CE2 TYR B 235      30.445  12.629  37.472  1.00 57.15           C  
ANISOU 3967  CE2 TYR B 235     7603   6530   7580   -139   -236   -133       C  
ATOM   3968  CZ  TYR B 235      29.930  13.875  37.801  1.00 59.49           C  
ANISOU 3968  CZ  TYR B 235     7792   6895   7917    -75   -202   -162       C  
ATOM   3969  OH  TYR B 235      29.239  14.003  38.977  1.00 55.34           O  
ANISOU 3969  OH  TYR B 235     7204   6464   7360    -83   -167   -163       O  
ATOM   3970  N   CYS B 236      34.868  12.076  35.319  1.00 61.24           N  
ANISOU 3970  N   CYS B 236     8434   6654   8179    -30   -324   -219       N  
ATOM   3971  CA  CYS B 236      35.547  11.415  36.421  1.00 64.35           C  
ANISOU 3971  CA  CYS B 236     8892   7027   8530    -34   -316   -232       C  
ATOM   3972  C   CYS B 236      36.797  12.178  36.830  1.00 63.77           C  
ANISOU 3972  C   CYS B 236     8843   6894   8493     66   -300   -295       C  
ATOM   3973  O   CYS B 236      37.082  12.279  38.024  1.00 63.53           O  
ANISOU 3973  O   CYS B 236     8811   6885   8443     95   -274   -318       O  
ATOM   3974  CB  CYS B 236      35.975  10.005  36.058  1.00 75.42           C  
ANISOU 3974  CB  CYS B 236    10403   8362   9892   -112   -355   -201       C  
ATOM   3975  SG  CYS B 236      34.548   8.921  35.847  1.00 90.16           S  
ANISOU 3975  SG  CYS B 236    12254  10302  11700   -236   -373   -123       S  
ATOM   3976  N   VAL B 237      37.524  12.690  35.829  1.00 62.50           N  
ANISOU 3976  N   VAL B 237     8705   6659   8384    115   -317   -322       N  
ATOM   3977  CA  VAL B 237      38.744  13.444  36.062  1.00 61.84           C  
ANISOU 3977  CA  VAL B 237     8646   6511   8337    211   -306   -382       C  
ATOM   3978  C   VAL B 237      38.473  14.708  36.885  1.00 64.85           C  
ANISOU 3978  C   VAL B 237     8933   6964   8743    291   -263   -416       C  
ATOM   3979  O   VAL B 237      39.156  14.927  37.883  1.00 71.26           O  
ANISOU 3979  O   VAL B 237     9763   7764   9548    342   -240   -449       O  
ATOM   3980  CB  VAL B 237      39.506  13.706  34.751  1.00 55.60           C  
ANISOU 3980  CB  VAL B 237     7899   5631   7595    240   -336   -401       C  
ATOM   3981  CG1 VAL B 237      40.587  14.763  34.918  1.00 46.47           C  
ANISOU 3981  CG1 VAL B 237     6745   4427   6485    349   -321   -464       C  
ATOM   3982  CG2 VAL B 237      40.100  12.387  34.247  1.00 58.59           C  
ANISOU 3982  CG2 VAL B 237     8390   5927   7946    172   -373   -380       C  
ATOM   3983  N   ALA B 238      37.471  15.506  36.489  1.00 55.66           N  
ANISOU 3983  N   ALA B 238     7670   5871   7607    300   -253   -406       N  
ATOM   3984  CA  ALA B 238      37.084  16.685  37.246  1.00 47.82           C  
ANISOU 3984  CA  ALA B 238     6579   4953   6636    370   -213   -435       C  
ATOM   3985  C   ALA B 238      36.593  16.290  38.648  1.00 49.59           C  
ANISOU 3985  C   ALA B 238     6782   5251   6809    341   -182   -423       C  
ATOM   3986  O   ALA B 238      36.737  17.044  39.619  1.00 35.81           O  
ANISOU 3986  O   ALA B 238     4992   3542   5071    405   -146   -458       O  
ATOM   3987  CB  ALA B 238      36.034  17.443  36.479  1.00 43.30           C  
ANISOU 3987  CB  ALA B 238     5910   4441   6101    369   -215   -420       C  
ATOM   3988  N   ALA B 239      35.999  15.094  38.756  1.00 52.53           N  
ANISOU 3988  N   ALA B 239     7186   5645   7126    242   -196   -374       N  
ATOM   3989  CA  ALA B 239      35.517  14.626  40.040  1.00 50.84           C  
ANISOU 3989  CA  ALA B 239     6958   5500   6859    204   -171   -361       C  
ATOM   3990  C   ALA B 239      36.697  14.300  40.938  1.00 51.25           C  
ANISOU 3990  C   ALA B 239     7090   5492   6892    234   -164   -392       C  
ATOM   3991  O   ALA B 239      36.634  14.533  42.137  1.00 54.64           O  
ANISOU 3991  O   ALA B 239     7490   5969   7300    254   -131   -408       O  
ATOM   3992  CB  ALA B 239      34.584  13.446  39.877  1.00 53.66           C  
ANISOU 3992  CB  ALA B 239     7330   5897   7163     91   -192   -300       C  
ATOM   3993  N   ASN B 240      37.761  13.750  40.356  1.00 55.83           N  
ANISOU 3993  N   ASN B 240     7769   5966   7478    235   -196   -400       N  
ATOM   3994  CA  ASN B 240      38.946  13.402  41.120  1.00 56.38           C  
ANISOU 3994  CA  ASN B 240     7922   5967   7533    262   -194   -429       C  
ATOM   3995  C   ASN B 240      39.504  14.663  41.758  1.00 56.18           C  
ANISOU 3995  C   ASN B 240     7853   5947   7547    370   -157   -483       C  
ATOM   3996  O   ASN B 240      39.805  14.643  42.946  1.00 56.73           O  
ANISOU 3996  O   ASN B 240     7931   6030   7592    386   -132   -499       O  
ATOM   3997  CB  ASN B 240      40.003  12.721  40.253  1.00 67.31           C  
ANISOU 3997  CB  ASN B 240     9413   7233   8927    252   -235   -432       C  
ATOM   3998  CG  ASN B 240      39.546  11.369  39.740  1.00 69.13           C  
ANISOU 3998  CG  ASN B 240     9697   7454   9114    143   -272   -379       C  
ATOM   3999  OD1 ASN B 240      38.703  10.731  40.364  1.00 69.77           O  
ANISOU 3999  OD1 ASN B 240     9761   7605   9145     73   -267   -343       O  
ATOM   4000  ND2 ASN B 240      40.073  10.924  38.611  1.00 58.22           N  
ANISOU 4000  ND2 ASN B 240     8381   5990   7750    125   -309   -374       N  
ATOM   4001  N   TYR B 241      39.593  15.744  40.965  1.00 61.32           N  
ANISOU 4001  N   TYR B 241     8455   6588   8255    440   -155   -508       N  
ATOM   4002  CA  TYR B 241      40.215  16.995  41.386  1.00 69.52           C  
ANISOU 4002  CA  TYR B 241     9457   7621   9335    549   -126   -560       C  
ATOM   4003  C   TYR B 241      39.353  17.761  42.388  1.00 65.45           C  
ANISOU 4003  C   TYR B 241     8838   7214   8816    573    -81   -567       C  
ATOM   4004  O   TYR B 241      39.887  18.485  43.222  1.00 72.10           O  
ANISOU 4004  O   TYR B 241     9665   8059   9671    647    -51   -605       O  
ATOM   4005  CB  TYR B 241      40.626  17.880  40.200  1.00 79.59           C  
ANISOU 4005  CB  TYR B 241    10719   8849  10673    613   -142   -586       C  
ATOM   4006  CG  TYR B 241      41.799  17.343  39.425  1.00 86.53           C  
ANISOU 4006  CG  TYR B 241    11705   9610  11563    615   -178   -598       C  
ATOM   4007  CD1 TYR B 241      43.098  17.507  39.877  1.00 85.30           C  
ANISOU 4007  CD1 TYR B 241    11613   9379  11416    680   -173   -639       C  
ATOM   4008  CD2 TYR B 241      41.603  16.618  38.267  1.00 93.83           C  
ANISOU 4008  CD2 TYR B 241    12669  10498  12486    549   -217   -566       C  
ATOM   4009  CE1 TYR B 241      44.176  16.966  39.197  1.00 89.78           C  
ANISOU 4009  CE1 TYR B 241    12280   9838  11993    679   -205   -651       C  
ATOM   4010  CE2 TYR B 241      42.667  16.074  37.570  1.00100.79           C  
ANISOU 4010  CE2 TYR B 241    13649  11272  13376    546   -250   -578       C  
ATOM   4011  CZ  TYR B 241      43.959  16.265  38.028  1.00 93.29           C  
ANISOU 4011  CZ  TYR B 241    12760  10249  12437    612   -244   -622       C  
ATOM   4012  OH  TYR B 241      45.021  15.765  37.339  1.00108.70           O  
ANISOU 4012  OH  TYR B 241    14757  12160  14384    582   -246   -610       O  
ATOM   4013  N   TYR B 242      38.030  17.608  42.311  1.00 64.39           N  
ANISOU 4013  N   TYR B 242     8632   7169   8664    512    -77   -530       N  
ATOM   4014  CA  TYR B 242      37.148  18.325  43.226  1.00 57.32           C  
ANISOU 4014  CA  TYR B 242     7634   6380   7765    531    -35   -537       C  
ATOM   4015  C   TYR B 242      36.921  17.551  44.515  1.00 56.07           C  
ANISOU 4015  C   TYR B 242     7494   6264   7545    476    -14   -522       C  
ATOM   4016  O   TYR B 242      36.840  18.182  45.562  1.00 62.57           O  
ANISOU 4016  O   TYR B 242     8267   7140   8367    519     25   -547       O  
ATOM   4017  CB  TYR B 242      35.873  18.814  42.534  1.00 48.69           C  
ANISOU 4017  CB  TYR B 242     6440   5365   6694    510    -35   -514       C  
ATOM   4018  CG  TYR B 242      36.113  20.078  41.750  1.00 42.65           C  
ANISOU 4018  CG  TYR B 242     5625   4581   5998    598    -37   -548       C  
ATOM   4019  CD1 TYR B 242      36.010  21.316  42.380  1.00 38.88           C  
ANISOU 4019  CD1 TYR B 242     5064   4156   5554    680     -1   -586       C  
ATOM   4020  CD2 TYR B 242      36.524  20.019  40.424  1.00 36.50           C  
ANISOU 4020  CD2 TYR B 242     4889   3729   5252    598    -77   -543       C  
ATOM   4021  CE1 TYR B 242      36.284  22.493  41.713  1.00 39.83           C  
ANISOU 4021  CE1 TYR B 242     5140   4257   5735    763     -5   -619       C  
ATOM   4022  CE2 TYR B 242      36.802  21.185  39.737  1.00 38.95           C  
ANISOU 4022  CE2 TYR B 242     5156   4019   5622    678    -81   -577       C  
ATOM   4023  CZ  TYR B 242      36.686  22.415  40.385  1.00 44.94           C  
ANISOU 4023  CZ  TYR B 242     5831   4831   6412    761    -46   -614       C  
ATOM   4024  OH  TYR B 242      36.972  23.572  39.704  1.00 47.96           O  
ANISOU 4024  OH  TYR B 242     6173   5194   6855    839    -53   -647       O  
ATOM   4025  N   TRP B 243      36.831  16.213  44.440  1.00 55.94           N  
ANISOU 4025  N   TRP B 243     7550   6226   7479    383    -42   -482       N  
ATOM   4026  CA  TRP B 243      36.790  15.398  45.649  1.00 66.16           C  
ANISOU 4026  CA  TRP B 243     8878   7546   8713    329    -30   -470       C  
ATOM   4027  C   TRP B 243      38.117  15.474  46.397  1.00 68.75           C  
ANISOU 4027  C   TRP B 243     9278   7801   9044    386    -20   -509       C  
ATOM   4028  O   TRP B 243      38.133  15.273  47.614  1.00 63.65           O  
ANISOU 4028  O   TRP B 243     8635   7187   8362    372      4   -514       O  
ATOM   4029  CB  TRP B 243      36.355  13.952  45.381  1.00 62.30           C  
ANISOU 4029  CB  TRP B 243     8449   7053   8169    214    -65   -417       C  
ATOM   4030  CG  TRP B 243      34.864  13.819  45.374  1.00 71.12           C  
ANISOU 4030  CG  TRP B 243     9483   8279   9260    148    -57   -378       C  
ATOM   4031  CD1 TRP B 243      34.079  13.649  44.272  1.00 69.71           C  
ANISOU 4031  CD1 TRP B 243     9277   8118   9091    105    -81   -342       C  
ATOM   4032  CD2 TRP B 243      33.960  13.929  46.494  1.00 76.81           C  
ANISOU 4032  CD2 TRP B 243    10133   9106   9946    120    -21   -372       C  
ATOM   4033  NE1 TRP B 243      32.760  13.590  44.623  1.00 63.37           N  
ANISOU 4033  NE1 TRP B 243     8395   7424   8260     51    -64   -313       N  
ATOM   4034  CE2 TRP B 243      32.652  13.762  45.979  1.00 76.14           C  
ANISOU 4034  CE2 TRP B 243     9982   9098   9849     59    -27   -332       C  
ATOM   4035  CE3 TRP B 243      34.107  14.124  47.878  1.00 81.48           C  
ANISOU 4035  CE3 TRP B 243    10710   9735  10514    137     15   -397       C  
ATOM   4036  CZ2 TRP B 243      31.515  13.810  46.800  1.00 78.02           C  
ANISOU 4036  CZ2 TRP B 243    10141   9450  10054     17      3   -318       C  
ATOM   4037  CZ3 TRP B 243      32.982  14.160  48.686  1.00 78.23           C  
ANISOU 4037  CZ3 TRP B 243    10220   9436  10068     94     45   -383       C  
ATOM   4038  CH2 TRP B 243      31.700  14.009  48.153  1.00 70.92           C  
ANISOU 4038  CH2 TRP B 243     9229   8587   9132     35     39   -345       C  
ATOM   4039  N   LEU B 244      39.204  15.755  45.655  1.00 71.24           N  
ANISOU 4039  N   LEU B 244     9649   8018   9401    446    -40   -535       N  
ATOM   4040  CA  LEU B 244      40.494  16.079  46.251  1.00 72.28           C  
ANISOU 4040  CA  LEU B 244     9837   8078   9548    518    -28   -578       C  
ATOM   4041  C   LEU B 244      40.436  17.473  46.895  1.00 71.51           C  
ANISOU 4041  C   LEU B 244     9653   8034   9485    612     18   -618       C  
ATOM   4042  O   LEU B 244      41.140  17.731  47.873  1.00 61.33           O  
ANISOU 4042  O   LEU B 244     8386   6727   8192    657     42   -646       O  
ATOM   4043  CB  LEU B 244      41.606  15.971  45.194  1.00 68.64           C  
ANISOU 4043  CB  LEU B 244     9457   7501   9121    552    -64   -594       C  
ATOM   4044  CG  LEU B 244      43.040  16.278  45.653  1.00 60.13           C  
ANISOU 4044  CG  LEU B 244     8447   6337   8064    629    -58   -639       C  
ATOM   4045  CD1 LEU B 244      43.512  15.327  46.742  1.00 53.00           C  
ANISOU 4045  CD1 LEU B 244     7617   5407   7112    584    -57   -632       C  
ATOM   4046  CD2 LEU B 244      43.998  16.217  44.477  1.00 56.73           C  
ANISOU 4046  CD2 LEU B 244     8085   5799   7669    659    -94   -654       C  
ATOM   4047  N   LEU B 245      39.579  18.363  46.362  1.00 63.74           N  
ANISOU 4047  N   LEU B 245     8569   7116   8534    638     29   -618       N  
ATOM   4048  CA  LEU B 245      39.464  19.701  46.907  1.00 58.80           C  
ANISOU 4048  CA  LEU B 245     7856   6543   7943    726     70   -656       C  
ATOM   4049  C   LEU B 245      38.756  19.647  48.255  1.00 62.50           C  
ANISOU 4049  C   LEU B 245     8272   7103   8371    696    110   -650       C  
ATOM   4050  O   LEU B 245      39.193  20.255  49.219  1.00 68.61           O  
ANISOU 4050  O   LEU B 245     9033   7887   9150    755    144   -682       O  
ATOM   4051  CB  LEU B 245      38.673  20.611  45.970  1.00 56.59           C  
ANISOU 4051  CB  LEU B 245     7482   6311   7709    755     68   -656       C  
ATOM   4052  CG  LEU B 245      38.480  22.006  46.555  1.00 59.10           C  
ANISOU 4052  CG  LEU B 245     7703   6689   8063    844    110   -694       C  
ATOM   4053  CD1 LEU B 245      39.849  22.613  46.778  1.00 64.46           C  
ANISOU 4053  CD1 LEU B 245     8433   7288   8769    939    116   -739       C  
ATOM   4054  CD2 LEU B 245      37.669  22.901  45.638  1.00 61.12           C  
ANISOU 4054  CD2 LEU B 245     7863   6993   8366    870    104   -695       C  
ATOM   4055  N   VAL B 246      37.643  18.930  48.316  1.00 61.73           N  
ANISOU 4055  N   VAL B 246     8145   7076   8234    603    106   -609       N  
ATOM   4056  CA  VAL B 246      36.929  18.823  49.577  1.00 71.05           C  
ANISOU 4056  CA  VAL B 246     9277   8346   9372    567    142   -603       C  
ATOM   4057  C   VAL B 246      37.745  17.986  50.569  1.00 65.28           C  
ANISOU 4057  C   VAL B 246     8638   7567   8596    537    143   -605       C  
ATOM   4058  O   VAL B 246      37.596  18.136  51.781  1.00 55.35           O  
ANISOU 4058  O   VAL B 246     7355   6362   7314    537    178   -617       O  
ATOM   4059  CB  VAL B 246      35.500  18.270  49.375  1.00 74.68           C  
ANISOU 4059  CB  VAL B 246     9680   8896   9800    473    136   -558       C  
ATOM   4060  CG1 VAL B 246      34.759  18.999  48.264  1.00 64.20           C  
ANISOU 4060  CG1 VAL B 246     8272   7602   8520    496    128   -553       C  
ATOM   4061  CG2 VAL B 246      35.511  16.780  49.106  1.00 79.53           C  
ANISOU 4061  CG2 VAL B 246    10384   9473  10362    371     96   -514       C  
ATOM   4062  N   GLU B 247      38.599  17.100  50.043  1.00 61.98           N  
ANISOU 4062  N   GLU B 247     8330   7052   8169    511    102   -594       N  
ATOM   4063  CA  GLU B 247      39.464  16.295  50.884  1.00 52.91           C  
ANISOU 4063  CA  GLU B 247     7276   5845   6983    485     96   -596       C  
ATOM   4064  C   GLU B 247      40.452  17.209  51.606  1.00 54.16           C  
ANISOU 4064  C   GLU B 247     7440   5967   7171    584    128   -645       C  
ATOM   4065  O   GLU B 247      40.818  16.936  52.754  1.00 53.34           O  
ANISOU 4065  O   GLU B 247     7368   5861   7037    573    146   -653       O  
ATOM   4066  CB  GLU B 247      40.194  15.272  50.028  1.00 53.25           C  
ANISOU 4066  CB  GLU B 247     7429   5786   7020    446     45   -578       C  
ATOM   4067  CG  GLU B 247      40.927  14.251  50.850  1.00 66.16           C  
ANISOU 4067  CG  GLU B 247     9162   7366   8611    400     31   -573       C  
ATOM   4068  CD  GLU B 247      40.025  13.331  51.648  1.00 75.63           C  
ANISOU 4068  CD  GLU B 247    10353   8639   9744    295     32   -536       C  
ATOM   4069  OE1 GLU B 247      39.259  12.585  51.020  1.00 75.36           O  
ANISOU 4069  OE1 GLU B 247    10318   8631   9684    217      4   -496       O  
ATOM   4070  OE2 GLU B 247      40.106  13.366  52.895  1.00 84.52           O1-
ANISOU 4070  OE2 GLU B 247    11476   9795  10844    292     60   -549       O1-
ATOM   4071  N   GLY B 248      40.874  18.285  50.918  1.00 46.56           N  
ANISOU 4071  N   GLY B 248     6447   4975   6268    679    133   -676       N  
ATOM   4072  CA  GLY B 248      41.677  19.327  51.526  1.00 42.63           C  
ANISOU 4072  CA  GLY B 248     5938   4456   5803    781    165   -721       C  
ATOM   4073  C   GLY B 248      40.856  20.263  52.411  1.00 46.90           C  
ANISOU 4073  C   GLY B 248     6368   5105   6347    811    216   -736       C  
ATOM   4074  O   GLY B 248      41.304  20.645  53.496  1.00 57.95           O  
ANISOU 4074  O   GLY B 248     7768   6509   7740    851    249   -760       O  
ATOM   4075  N   VAL B 249      39.652  20.635  51.958  1.00 49.11           N  
ANISOU 4075  N   VAL B 249     6552   5472   6636    792    222   -721       N  
ATOM   4076  CA  VAL B 249      38.811  21.561  52.715  1.00 49.78           C  
ANISOU 4076  CA  VAL B 249     6524   5663   6729    821    269   -737       C  
ATOM   4077  C   VAL B 249      38.377  20.930  54.030  1.00 52.58           C  
ANISOU 4077  C   VAL B 249     6878   6076   7025    752    295   -724       C  
ATOM   4078  O   VAL B 249      38.372  21.614  55.051  1.00 50.01           O  
ANISOU 4078  O   VAL B 249     6506   5795   6701    794    338   -750       O  
ATOM   4079  CB  VAL B 249      37.580  22.080  51.962  1.00 49.20           C  
ANISOU 4079  CB  VAL B 249     6344   5669   6679    813    269   -724       C  
ATOM   4080  CG1 VAL B 249      36.850  23.005  52.901  1.00 40.85           C  
ANISOU 4080  CG1 VAL B 249     5179   4715   5628    845    320   -746       C  
ATOM   4081  CG2 VAL B 249      37.951  22.864  50.701  1.00 55.05           C  
ANISOU 4081  CG2 VAL B 249     7073   6360   7482    885    245   -741       C  
ATOM   4082  N   TYR B 250      38.048  19.629  53.993  1.00 58.95           N  
ANISOU 4082  N   TYR B 250     7739   6880   7780    647    267   -684       N  
ATOM   4083  CA  TYR B 250      37.690  18.894  55.199  1.00 65.27           C  
ANISOU 4083  CA  TYR B 250     8551   7728   8519    571    284   -669       C  
ATOM   4084  C   TYR B 250      38.850  18.908  56.198  1.00 76.57           C  
ANISOU 4084  C   TYR B 250    10052   9098   9944    608    300   -695       C  
ATOM   4085  O   TYR B 250      38.651  19.160  57.395  1.00 88.55           O  
ANISOU 4085  O   TYR B 250    11535  10670  11439    606    339   -709       O  
ATOM   4086  CB  TYR B 250      37.311  17.452  54.881  1.00 60.56           C  
ANISOU 4086  CB  TYR B 250     8017   7123   7871    456    243   -621       C  
ATOM   4087  CG  TYR B 250      37.000  16.632  56.109  1.00 69.85           C  
ANISOU 4087  CG  TYR B 250     9213   8343   8981    372    255   -605       C  
ATOM   4088  CD1 TYR B 250      35.814  16.825  56.799  1.00 66.75           C  
ANISOU 4088  CD1 TYR B 250     8730   8070   8563    331    288   -598       C  
ATOM   4089  CD2 TYR B 250      37.898  15.680  56.594  1.00 67.90           C  
ANISOU 4089  CD2 TYR B 250     9078   8020   8701    333    232   -599       C  
ATOM   4090  CE1 TYR B 250      35.519  16.080  57.926  1.00 65.91           C  
ANISOU 4090  CE1 TYR B 250     8641   8006   8394    252    298   -585       C  
ATOM   4091  CE2 TYR B 250      37.611  14.918  57.714  1.00 66.10           C  
ANISOU 4091  CE2 TYR B 250     8871   7833   8413    253    239   -584       C  
ATOM   4092  CZ  TYR B 250      36.411  15.126  58.377  1.00 64.77           C  
ANISOU 4092  CZ  TYR B 250     8609   7784   8215    211    273   -577       C  
ATOM   4093  OH  TYR B 250      36.060  14.417  59.483  1.00 70.43           O  
ANISOU 4093  OH  TYR B 250     9341   8549   8872    129    281   -563       O  
ATOM   4094  N   LEU B 251      40.062  18.634  55.689  1.00 71.52           N  
ANISOU 4094  N   LEU B 251     9510   8343   9323    641    269   -704       N  
ATOM   4095  CA  LEU B 251      41.254  18.540  56.515  1.00 67.78           C  
ANISOU 4095  CA  LEU B 251     9114   7795   8843    674    277   -726       C  
ATOM   4096  C   LEU B 251      41.495  19.873  57.212  1.00 64.52           C  
ANISOU 4096  C   LEU B 251     8639   7412   8465    773    327   -768       C  
ATOM   4097  O   LEU B 251      41.846  19.875  58.404  1.00 51.32           O  
ANISOU 4097  O   LEU B 251     6985   5744   6771    773    355   -780       O  
ATOM   4098  CB  LEU B 251      42.439  18.131  55.631  1.00 72.38           C  
ANISOU 4098  CB  LEU B 251     9802   8251   9450    700    233   -730       C  
ATOM   4099  CG  LEU B 251      43.840  18.168  56.248  1.00 66.40           C  
ANISOU 4099  CG  LEU B 251     9130   7399   8701    752    237   -758       C  
ATOM   4100  CD1 LEU B 251      43.955  17.164  57.395  1.00 65.08           C  
ANISOU 4100  CD1 LEU B 251     9022   7228   8476    671    236   -741       C  
ATOM   4101  CD2 LEU B 251      44.893  17.891  55.173  1.00 61.11           C  
ANISOU 4101  CD2 LEU B 251     8547   6611   8061    783    194   -764       C  
ATOM   4102  N   TYR B 252      41.281  20.976  56.464  1.00 60.96           N  
ANISOU 4102  N   TYR B 252     8114   6981   8066    851    336   -787       N  
ATOM   4103  CA  TYR B 252      41.578  22.299  56.987  1.00 60.72           C  
ANISOU 4103  CA  TYR B 252     8026   6972   8074    954    379   -828       C  
ATOM   4104  C   TYR B 252      40.676  22.578  58.174  1.00 68.75           C  
ANISOU 4104  C   TYR B 252     8961   8099   9063    927    427   -830       C  
ATOM   4105  O   TYR B 252      41.165  23.010  59.217  1.00 79.90           O  
ANISOU 4105  O   TYR B 252    10377   9510  10473    966    461   -854       O  
ATOM   4106  CB  TYR B 252      41.423  23.412  55.954  1.00 62.69           C  
ANISOU 4106  CB  TYR B 252     8207   7230   8384   1037    377   -847       C  
ATOM   4107  CG  TYR B 252      41.731  24.774  56.526  1.00 72.72           C  
ANISOU 4107  CG  TYR B 252     9417   8523   9690   1143    419   -889       C  
ATOM   4108  CD1 TYR B 252      43.034  25.257  56.587  1.00 90.76           C  
ANISOU 4108  CD1 TYR B 252    11762  10719  12002   1230    420   -918       C  
ATOM   4109  CD2 TYR B 252      40.723  25.577  57.034  1.00 83.44           C  
ANISOU 4109  CD2 TYR B 252    10658   9990  11055   1158    460   -899       C  
ATOM   4110  CE1 TYR B 252      43.318  26.492  57.150  1.00107.22           C  
ANISOU 4110  CE1 TYR B 252    13793  12827  14117   1323    460   -952       C  
ATOM   4111  CE2 TYR B 252      40.991  26.807  57.612  1.00103.06           C  
ANISOU 4111  CE2 TYR B 252    13087  12498  13572   1253    499   -936       C  
ATOM   4112  CZ  TYR B 252      42.292  27.268  57.665  1.00109.83           C  
ANISOU 4112  CZ  TYR B 252    14008  13267  14455   1338    499   -963       C  
ATOM   4113  OH  TYR B 252      42.530  28.495  58.212  1.00134.05           O  
ANISOU 4113  OH  TYR B 252    17022  16369  17542   1364    543   -943       O  
ATOM   4114  N   THR B 253      39.377  22.290  58.006  1.00 68.67           N  
ANISOU 4114  N   THR B 253     8881   8180   9031    856    427   -804       N  
ATOM   4115  CA  THR B 253      38.405  22.529  59.061  1.00 67.10           C  
ANISOU 4115  CA  THR B 253     8597   8093   8806    823    471   -806       C  
ATOM   4116  C   THR B 253      38.654  21.587  60.243  1.00 67.34           C  
ANISOU 4116  C   THR B 253     8693   8116   8776    748    478   -794       C  
ATOM   4117  O   THR B 253      38.378  21.936  61.390  1.00 61.06           O  
ANISOU 4117  O   THR B 253     7854   7383   7963    747    522   -809       O  
ATOM   4118  CB  THR B 253      36.971  22.430  58.527  1.00 73.60           C  
ANISOU 4118  CB  THR B 253     9333   9011   9622    765    467   -782       C  
ATOM   4119  OG1 THR B 253      36.778  21.112  58.013  1.00 74.10           O  
ANISOU 4119  OG1 THR B 253     9464   9048   9645    667    422   -739       O  
ATOM   4120  CG2 THR B 253      36.651  23.457  57.466  1.00 81.50           C  
ANISOU 4120  CG2 THR B 253    10256  10026  10684    838    463   -796       C  
ATOM   4121  N   LEU B 254      39.173  20.384  59.964  1.00 66.48           N  
ANISOU 4121  N   LEU B 254     8692   7933   8636    684    434   -768       N  
ATOM   4122  CA  LEU B 254      39.471  19.424  61.015  1.00 65.53           C  
ANISOU 4122  CA  LEU B 254     8643   7797   8460    610    433   -755       C  
ATOM   4123  C   LEU B 254      40.576  19.950  61.941  1.00 66.06           C  
ANISOU 4123  C   LEU B 254     8750   7809   8541    678    461   -788       C  
ATOM   4124  O   LEU B 254      40.540  19.695  63.144  1.00 59.27           O  
ANISOU 4124  O   LEU B 254     7899   6979   7644    637    486   -790       O  
ATOM   4125  CB  LEU B 254      39.833  18.091  60.357  1.00 68.65           C  
ANISOU 4125  CB  LEU B 254     9142   8115   8827    536    375   -721       C  
ATOM   4126  CG  LEU B 254      39.998  16.899  61.298  1.00 72.70           C  
ANISOU 4126  CG  LEU B 254     9732   8614   9277    439    362   -700       C  
ATOM   4127  CD1 LEU B 254      38.680  16.547  61.960  1.00 77.67           C  
ANISOU 4127  CD1 LEU B 254    10293   9363   9856    349    380   -679       C  
ATOM   4128  CD2 LEU B 254      40.530  15.692  60.543  1.00 73.88           C  
ANISOU 4128  CD2 LEU B 254     9989   8673   9410    383    301   -671       C  
ATOM   4129  N   LEU B 255      41.553  20.681  61.372  1.00 75.68           N  
ANISOU 4129  N   LEU B 255     9993   8949   9812    781    457   -814       N  
ATOM   4130  CA  LEU B 255      42.652  21.284  62.125  1.00 70.30           C  
ANISOU 4130  CA  LEU B 255     9349   8211   9150    858    483   -846       C  
ATOM   4131  C   LEU B 255      42.153  22.505  62.912  1.00 69.29           C  
ANISOU 4131  C   LEU B 255     9115   8172   9039    917    542   -875       C  
ATOM   4132  O   LEU B 255      42.778  22.900  63.895  1.00 62.22           O  
ANISOU 4132  O   LEU B 255     8238   7260   8144    956    573   -896       O  
ATOM   4133  CB  LEU B 255      43.819  21.659  61.189  1.00 55.17           C  
ANISOU 4133  CB  LEU B 255     7494   6185   7284    947    456   -864       C  
ATOM   4134  CG  LEU B 255      44.514  20.524  60.425  1.00 51.64           C  
ANISOU 4134  CG  LEU B 255     7159   5636   6827    901    399   -843       C  
ATOM   4135  CD1 LEU B 255      45.391  21.036  59.308  1.00 48.72           C  
ANISOU 4135  CD1 LEU B 255     6823   5180   6511    989    375   -862       C  
ATOM   4136  CD2 LEU B 255      45.371  19.662  61.320  1.00 47.11           C  
ANISOU 4136  CD2 LEU B 255     6689   4993   6219    859    390   -838       C  
ATOM   4137  N   ALA B 256      41.023  23.099  62.483  1.00 61.58           N  
ANISOU 4137  N   ALA B 256     8029   7291   8079    923    557   -875       N  
ATOM   4138  CA  ALA B 256      40.525  24.346  63.052  1.00 68.06           C  
ANISOU 4138  CA  ALA B 256     8740   8194   8924    988    609   -905       C  
ATOM   4139  C   ALA B 256      39.554  24.119  64.224  1.00 70.83           C  
ANISOU 4139  C   ALA B 256     9034   8651   9229    912    647   -898       C  
ATOM   4140  O   ALA B 256      39.256  25.036  64.996  1.00 63.37           O  
ANISOU 4140  O   ALA B 256     8011   7771   8296    956    696   -925       O  
ATOM   4141  CB  ALA B 256      39.908  25.183  61.961  1.00 74.08           C  
ANISOU 4141  CB  ALA B 256     9416   8995   9735   1042    604   -912       C  
ATOM   4142  N   PHE B 257      39.042  22.891  64.358  1.00 60.12           N  
ANISOU 4142  N   PHE B 257     8010   5611   9222    819    617   -659       N  
ATOM   4143  CA  PHE B 257      38.151  22.578  65.458  1.00 56.31           C  
ANISOU 4143  CA  PHE B 257     7470   5237   8686    739    577   -581       C  
ATOM   4144  C   PHE B 257      38.971  22.029  66.613  1.00 60.71           C  
ANISOU 4144  C   PHE B 257     7962   5939   9168    643    498   -597       C  
ATOM   4145  O   PHE B 257      39.983  21.374  66.395  1.00 71.81           O  
ANISOU 4145  O   PHE B 257     9372   7341  10573    659    397   -610       O  
ATOM   4146  CB  PHE B 257      37.114  21.540  65.036  1.00 61.92           C  
ANISOU 4146  CB  PHE B 257     8200   5897   9430    791    424   -423       C  
ATOM   4147  CG  PHE B 257      35.852  21.579  65.857  1.00 69.10           C  
ANISOU 4147  CG  PHE B 257     9070   6879  10305    733    436   -348       C  
ATOM   4148  CD1 PHE B 257      34.873  22.523  65.596  1.00 69.22           C  
ANISOU 4148  CD1 PHE B 257     9107   6844  10349    755    577   -363       C  
ATOM   4149  CD2 PHE B 257      35.672  20.710  66.923  1.00 69.25           C  
ANISOU 4149  CD2 PHE B 257     9028   7023  10262    652    312   -269       C  
ATOM   4150  CE1 PHE B 257      33.723  22.566  66.363  1.00 72.84           C  
ANISOU 4150  CE1 PHE B 257     9528   7374  10774    700    589   -298       C  
ATOM   4151  CE2 PHE B 257      34.519  20.749  67.694  1.00 61.97           C  
ANISOU 4151  CE2 PHE B 257     8068   6173   9306    596    323   -202       C  
ATOM   4152  CZ  PHE B 257      33.552  21.685  67.411  1.00 74.37           C  
ANISOU 4152  CZ  PHE B 257     9660   7692  10905    620    464   -218       C  
ATOM   4153  N   ASN B1001      38.502  22.280  67.839  1.00 63.95           N  
ANISOU 4153  N   ASN B1001     8311   6474   9514    544    542   -594       N  
ATOM   4154  CA  ASN B1001      39.214  21.922  69.060  1.00 60.25           C  
ANISOU 4154  CA  ASN B1001     7774   6150   8967    442    492   -619       C  
ATOM   4155  C   ASN B1001      38.236  21.995  70.239  1.00 59.56           C  
ANISOU 4155  C   ASN B1001     7627   6180   8823    351    510   -568       C  
ATOM   4156  O   ASN B1001      37.026  22.144  70.042  1.00 53.10           O  
ANISOU 4156  O   ASN B1001     6822   5325   8027    375    534   -499       O  
ATOM   4157  CB  ASN B1001      40.463  22.795  69.235  1.00 56.57           C  
ANISOU 4157  CB  ASN B1001     7301   5711   8481    412    620   -776       C  
ATOM   4158  CG  ASN B1001      40.137  24.275  69.186  1.00 62.98           C  
ANISOU 4158  CG  ASN B1001     8125   6500   9304    408    839   -876       C  
ATOM   4159  OD1 ASN B1001      39.077  24.693  69.620  1.00 80.71           O  
ANISOU 4159  OD1 ASN B1001    10353   8777  11538    378    903   -843       O  
ATOM   4160  ND2 ASN B1001      41.007  25.095  68.633  1.00 70.29           N  
ANISOU 4160  ND2 ASN B1001     9083   7370  10254    439    955   -998       N  
ATOM   4161  N   ILE B1002      38.781  21.902  71.462  1.00 59.75           N  
ANISOU 4161  N   ILE B1002     7585   6344   8772    248    500   -604       N  
ATOM   4162  CA  ILE B1002      38.001  21.918  72.688  1.00 59.22           C  
ANISOU 4162  CA  ILE B1002     7455   6405   8643    152    509   -561       C  
ATOM   4163  C   ILE B1002      37.322  23.275  72.851  1.00 66.10           C  
ANISOU 4163  C   ILE B1002     8324   7276   9516    136    711   -630       C  
ATOM   4164  O   ILE B1002      36.185  23.354  73.321  1.00 74.89           O  
ANISOU 4164  O   ILE B1002     9411   8431  10611    105    726   -566       O  
ATOM   4165  CB  ILE B1002      38.879  21.585  73.910  1.00 62.25           C  
ANISOU 4165  CB  ILE B1002     7772   6933   8948     48    462   -599       C  
ATOM   4166  CG1 ILE B1002      38.059  21.523  75.192  1.00 66.17           C  
ANISOU 4166  CG1 ILE B1002     8201   7564   9378    -53    460   -547       C  
ATOM   4167  CG2 ILE B1002      39.996  22.599  74.084  1.00 60.25           C  
ANISOU 4167  CG2 ILE B1002     7512   6700   8679     23    612   -759       C  
ATOM   4168  CD1 ILE B1002      36.862  20.612  75.138  1.00 66.49           C  
ANISOU 4168  CD1 ILE B1002     8241   7596   9426    -39    326   -391       C  
ATOM   4169  N   PHE B1003      38.020  24.345  72.458  1.00 65.00           N  
ANISOU 4169  N   PHE B1003     8210   7091   9397    159    865   -763       N  
ATOM   4170  CA  PHE B1003      37.457  25.675  72.611  1.00 65.49           C  
ANISOU 4170  CA  PHE B1003     8271   7153   9460    144   1060   -839       C  
ATOM   4171  C   PHE B1003      36.232  25.845  71.729  1.00 66.26           C  
ANISOU 4171  C   PHE B1003     8418   7139   9618    223   1082   -769       C  
ATOM   4172  O   PHE B1003      35.311  26.561  72.094  1.00 72.17           O  
ANISOU 4172  O   PHE B1003     9152   7914  10356    197   1187   -774       O  
ATOM   4173  CB  PHE B1003      38.483  26.748  72.266  1.00 61.11           C  
ANISOU 4173  CB  PHE B1003     7740   6560   8919    158   1212   -992       C  
ATOM   4174  CG  PHE B1003      39.696  26.717  73.155  1.00 64.31           C  
ANISOU 4174  CG  PHE B1003     8097   7076   9264     79   1211  -1073       C  
ATOM   4175  CD1 PHE B1003      39.670  27.287  74.428  1.00 63.73           C  
ANISOU 4175  CD1 PHE B1003     7957   7136   9122    -25   1298  -1126       C  
ATOM   4176  CD2 PHE B1003      40.859  26.105  72.716  1.00 62.96           C  
ANISOU 4176  CD2 PHE B1003     7944   6873   9104    108   1119  -1096       C  
ATOM   4177  CE1 PHE B1003      40.784  27.247  75.245  1.00 58.46           C  
ANISOU 4177  CE1 PHE B1003     7244   6567   8399    -97   1295  -1200       C  
ATOM   4178  CE2 PHE B1003      41.988  26.099  73.528  1.00 63.43           C  
ANISOU 4178  CE2 PHE B1003     7959   7032   9108     36   1121  -1175       C  
ATOM   4179  CZ  PHE B1003      41.941  26.661  74.787  1.00 63.26           C  
ANISOU 4179  CZ  PHE B1003     7874   7142   9020    -66   1208  -1225       C  
ATOM   4180  N   GLU B1004      36.249  25.214  70.552  1.00 63.49           N  
ANISOU 4180  N   GLU B1004     8129   6663   9333    321    986   -710       N  
ATOM   4181  CA  GLU B1004      35.124  25.318  69.636  1.00 68.09           C  
ANISOU 4181  CA  GLU B1004     8763   7130   9977    403    999   -642       C  
ATOM   4182  C   GLU B1004      34.021  24.367  70.076  1.00 66.23           C  
ANISOU 4182  C   GLU B1004     8499   6942   9723    381    865   -494       C  
ATOM   4183  O   GLU B1004      32.850  24.659  69.843  1.00 69.53           O  
ANISOU 4183  O   GLU B1004     8933   7321  10166    407    908   -444       O  
ATOM   4184  CB  GLU B1004      35.560  25.100  68.185  1.00 71.12           C  
ANISOU 4184  CB  GLU B1004     9224   7358  10440    519    962   -642       C  
ATOM   4185  CG  GLU B1004      36.623  26.090  67.732  1.00 86.99           C  
ANISOU 4185  CG  GLU B1004    11263   9320  12468    540   1101   -790       C  
ATOM   4186  CD  GLU B1004      36.352  27.558  68.038  1.00 94.40           C  
ANISOU 4186  CD  GLU B1004    12197  10276  13396    507   1313   -899       C  
ATOM   4187  OE1 GLU B1004      35.197  27.991  67.846  1.00106.76           O  
ANISOU 4187  OE1 GLU B1004    13779  11802  14985    530   1374   -862       O  
ATOM   4188  OE2 GLU B1004      37.295  28.260  68.501  1.00118.13           O1-
ANISOU 4188  OE2 GLU B1004    15181  13337  16368    457   1414  -1019       O1-
ATOM   4189  N   MET B1005      34.420  23.245  70.697  1.00 64.66           N  
ANISOU 4189  N   MET B1005     8259   6827   9481    333    703   -427       N  
ATOM   4190  CA  MET B1005      33.497  22.251  71.210  1.00 56.99           C  
ANISOU 4190  CA  MET B1005     7256   5915   8483    301    561   -286       C  
ATOM   4191  C   MET B1005      32.689  22.855  72.360  1.00 74.19           C  
ANISOU 4191  C   MET B1005     9374   8212  10603    208    655   -294       C  
ATOM   4192  O   MET B1005      31.458  22.761  72.360  1.00 87.08           O  
ANISOU 4192  O   MET B1005    11005   9837  12243    216    644   -208       O  
ATOM   4193  CB  MET B1005      34.244  21.013  71.698  1.00 52.38           C  
ANISOU 4193  CB  MET B1005     6640   5402   7860    261    378   -231       C  
ATOM   4194  CG  MET B1005      33.332  19.877  72.132  1.00 54.76           C  
ANISOU 4194  CG  MET B1005     6913   5754   8137    235    213    -77       C  
ATOM   4195  SD  MET B1005      34.295  18.541  72.851  1.00 54.23           S  
ANISOU 4195  SD  MET B1005     6804   5786   8015    174     12    -30       S  
ATOM   4196  CE  MET B1005      33.124  17.222  73.091  1.00 67.25           C  
ANISOU 4196  CE  MET B1005     8437   7462   9651    163   -184    159       C  
ATOM   4197  N   LEU B1006      33.375  23.491  73.325  1.00 73.74           N  
ANISOU 4197  N   LEU B1006     9266   8264  10487    122    751   -398       N  
ATOM   4198  CA  LEU B1006      32.703  24.050  74.493  1.00 76.05           C  
ANISOU 4198  CA  LEU B1006     9495   8681  10718     28    837   -411       C  
ATOM   4199  C   LEU B1006      31.863  25.271  74.131  1.00 82.69           C  
ANISOU 4199  C   LEU B1006    10363   9466  11591     60   1013   -462       C  
ATOM   4200  O   LEU B1006      30.857  25.521  74.782  1.00108.84           O  
ANISOU 4200  O   LEU B1006    13637  12846  14871     13   1052   -427       O  
ATOM   4201  CB  LEU B1006      33.713  24.440  75.570  1.00 75.81           C  
ANISOU 4201  CB  LEU B1006     9408   8776  10620    -68    896   -515       C  
ATOM   4202  CG  LEU B1006      34.319  23.292  76.364  1.00 82.59           C  
ANISOU 4202  CG  LEU B1006    10219   9737  11425   -134    731   -460       C  
ATOM   4203  CD1 LEU B1006      35.470  23.810  77.207  1.00 68.09           C  
ANISOU 4203  CD1 LEU B1006     8339   7997   9534   -210    809   -583       C  
ATOM   4204  CD2 LEU B1006      33.262  22.596  77.209  1.00 75.69           C  
ANISOU 4204  CD2 LEU B1006     9295   8959  10504   -197    634   -338       C  
ATOM   4205  N   ARG B1007      32.296  26.063  73.143  1.00 81.91           N  
ANISOU 4205  N   ARG B1007    10324   9249  11550    136   1122   -551       N  
ATOM   4206  CA  ARG B1007      31.569  27.277  72.797  1.00 77.12           C  
ANISOU 4206  CA  ARG B1007     9743   8587  10972    166   1294   -610       C  
ATOM   4207  C   ARG B1007      30.196  26.915  72.240  1.00 75.20           C  
ANISOU 4207  C   ARG B1007     9530   8274  10769    223   1242   -493       C  
ATOM   4208  O   ARG B1007      29.281  27.730  72.302  1.00 79.05           O  
ANISOU 4208  O   ARG B1007    10019   8756  11262    222   1357   -511       O  
ATOM   4209  CB  ARG B1007      32.369  28.197  71.866  1.00 77.80           C  
ANISOU 4209  CB  ARG B1007     9889   8563  11110    232   1420   -732       C  
ATOM   4210  N   ILE B1008      30.061  25.694  71.709  1.00 68.06           N  
ANISOU 4210  N   ILE B1008     8648   7318   9893    271   1067   -374       N  
ATOM   4211  CA  ILE B1008      28.789  25.236  71.170  1.00 70.39           C  
ANISOU 4211  CA  ILE B1008     8972   7547  10227    326   1001   -254       C  
ATOM   4212  C   ILE B1008      27.923  24.757  72.330  1.00 70.32           C  
ANISOU 4212  C   ILE B1008     8893   7673  10152    237    937   -167       C  
ATOM   4213  O   ILE B1008      26.764  25.129  72.426  1.00 79.60           O  
ANISOU 4213  O   ILE B1008    10063   8851  11329    237    992   -132       O  
ATOM   4214  CB  ILE B1008      28.976  24.168  70.070  1.00 61.59           C  
ANISOU 4214  CB  ILE B1008     7913   6314   9173    420    844   -164       C  
ATOM   4215  CG1 ILE B1008      29.670  24.731  68.827  1.00 61.62           C  
ANISOU 4215  CG1 ILE B1008     7991   6174   9249    515    920   -248       C  
ATOM   4216  CG2 ILE B1008      27.666  23.524  69.700  1.00 57.18           C  
ANISOU 4216  CG2 ILE B1008     7373   5710   8644    463    752    -26       C  
ATOM   4217  CD1 ILE B1008      29.012  25.970  68.243  1.00 66.44           C  
ANISOU 4217  CD1 ILE B1008     8643   6699   9902    563   1096   -314       C  
ATOM   4218  N   ASP B1009      28.499  23.961  73.225  1.00 64.66           N  
ANISOU 4218  N   ASP B1009     8121   7071   9375    160    825   -137       N  
ATOM   4219  CA  ASP B1009      27.712  23.341  74.274  1.00 66.71           C  
ANISOU 4219  CA  ASP B1009     8317   7456   9573     78    740    -41       C  
ATOM   4220  C   ASP B1009      27.337  24.356  75.350  1.00 63.75           C  
ANISOU 4220  C   ASP B1009     7884   7199   9140    -11    890   -115       C  
ATOM   4221  O   ASP B1009      26.217  24.366  75.829  1.00 77.95           O  
ANISOU 4221  O   ASP B1009     9652   9051  10914    -44    894    -53       O  
ATOM   4222  CB  ASP B1009      28.432  22.130  74.861  1.00 69.72           C  
ANISOU 4222  CB  ASP B1009     8662   7919   9911     26    565     19       C  
ATOM   4223  CG  ASP B1009      28.630  20.984  73.886  1.00 76.17           C  
ANISOU 4223  CG  ASP B1009     9530   8631  10780    109    394    114       C  
ATOM   4224  OD1 ASP B1009      27.841  20.876  72.898  1.00 75.14           O  
ANISOU 4224  OD1 ASP B1009     9454   8382  10712    198    376    179       O  
ATOM   4225  OD2 ASP B1009      29.566  20.195  74.130  1.00 76.86           O1-
ANISOU 4225  OD2 ASP B1009     9602   8757  10844     84    276    124       O1-
ATOM   4226  N   GLU B1010      28.273  25.215  75.727  1.00 67.23           N  
ANISOU 4226  N   GLU B1010     8308   7679   9558    -48   1013   -250       N  
ATOM   4227  CA  GLU B1010      28.087  26.131  76.836  1.00 74.74           C  
ANISOU 4227  CA  GLU B1010     9197   8753  10447   -139   1147   -327       C  
ATOM   4228  C   GLU B1010      27.428  27.440  76.410  1.00 77.18           C  
ANISOU 4228  C   GLU B1010     9536   8999  10789    -99   1330   -402       C  
ATOM   4229  O   GLU B1010      26.796  28.095  77.234  1.00 99.61           O  
ANISOU 4229  O   GLU B1010    12330  11932  13586   -162   1424   -429       O  
ATOM   4230  CB  GLU B1010      29.423  26.402  77.519  1.00 81.88           C  
ANISOU 4230  CB  GLU B1010    10066   9738  11306   -203   1187   -435       C  
ATOM   4231  CG  GLU B1010      29.981  25.166  78.199  1.00 93.80           C  
ANISOU 4231  CG  GLU B1010    11533  11338  12768   -263   1013   -364       C  
ATOM   4232  CD  GLU B1010      29.255  24.709  79.453  1.00107.27           C  
ANISOU 4232  CD  GLU B1010    13163  13193  14401   -363    952   -287       C  
ATOM   4233  OE1 GLU B1010      28.356  25.438  79.916  1.00129.81           O  
ANISOU 4233  OE1 GLU B1010    15991  16097  17235   -396   1058   -301       O  
ATOM   4234  OE2 GLU B1010      29.590  23.625  79.971  1.00121.84           O1-
ANISOU 4234  OE2 GLU B1010    14977  15107  16209   -409    797   -215       O1-
ATOM   4235  N   GLY B1011      27.578  27.830  75.143  1.00 75.25           N  
ANISOU 4235  N   GLY B1011     9368   8601  10620      3   1381   -438       N  
ATOM   4236  CA  GLY B1011      26.987  29.064  74.646  1.00 76.62           C  
ANISOU 4236  CA  GLY B1011     9578   8703  10831     48   1551   -511       C  
ATOM   4237  C   GLY B1011      27.733  30.297  75.149  1.00 80.69           C  
ANISOU 4237  C   GLY B1011    10073   9270  11318      0   1722   -666       C  
ATOM   4238  O   GLY B1011      28.773  30.161  75.785  1.00 86.61           O  
ANISOU 4238  O   GLY B1011    10785  10098  12024    -59   1706   -717       O  
ATOM   4239  N   LEU B1012      27.202  31.489  74.841  1.00 81.44           N  
ANISOU 4239  N   LEU B1012    10193   9314  11436     29   1883   -741       N  
ATOM   4240  CA  LEU B1012      27.808  32.743  75.265  1.00 86.76           C  
ANISOU 4240  CA  LEU B1012    10851  10029  12086    -11   2055   -889       C  
ATOM   4241  C   LEU B1012      26.784  33.625  75.967  1.00 86.71           C  
ANISOU 4241  C   LEU B1012    10807  10095  12045    -58   2174   -916       C  
ATOM   4242  O   LEU B1012      25.697  33.836  75.448  1.00 93.69           O  
ANISOU 4242  O   LEU B1012    11721  10912  12964     -7   2199   -872       O  
ATOM   4243  CB  LEU B1012      28.393  33.476  74.053  1.00100.70           C  
ANISOU 4243  CB  LEU B1012    12696  11644  13921     79   2150   -979       C  
ATOM   4244  CG  LEU B1012      29.076  34.815  74.352  1.00109.44           C  
ANISOU 4244  CG  LEU B1012    13797  12775  15009     47   2330  -1136       C  
ATOM   4245  CD1 LEU B1012      30.208  34.647  75.353  1.00104.76           C  
ANISOU 4245  CD1 LEU B1012    13143  12307  14353    -41   2313  -1191       C  
ATOM   4246  CD2 LEU B1012      29.579  35.482  73.082  1.00100.38           C  
ANISOU 4246  CD2 LEU B1012    12733  11473  13934    139   2415  -1215       C  
ATOM   4247  N   ARG B1013      27.171  34.162  77.129  1.00 91.19           N  
ANISOU 4247  N   ARG B1013    11306  10797  12544   -152   2249   -992       N  
ATOM   4248  CA  ARG B1013      26.326  35.082  77.869  1.00 96.79           C  
ANISOU 4248  CA  ARG B1013    11974  11585  13215   -202   2372  -1033       C  
ATOM   4249  C   ARG B1013      27.029  36.421  78.028  1.00109.84           C  
ANISOU 4249  C   ARG B1013    13630  13245  14860   -219   2549  -1192       C  
ATOM   4250  O   ARG B1013      28.214  36.482  78.347  1.00123.68           O  
ANISOU 4250  O   ARG B1013    15366  15035  16590   -254   2561  -1262       O  
ATOM   4251  CB  ARG B1013      25.993  34.537  79.255  1.00100.18           C  
ANISOU 4251  CB  ARG B1013    12312  12188  13563   -309   2303   -975       C  
ATOM   4252  CG  ARG B1013      25.085  33.317  79.238  1.00 95.80           C  
ANISOU 4252  CG  ARG B1013    11748  11644  13008   -303   2140   -817       C  
ATOM   4253  CD  ARG B1013      24.663  33.022  80.677  1.00101.90           C  
ANISOU 4253  CD  ARG B1013    12427  12595  13694   -415   2104   -776       C  
ATOM   4254  NE  ARG B1013      23.700  31.943  80.660  1.00 86.70           N  
ANISOU 4254  NE  ARG B1013    10494  10681  11769   -411   1958   -626       N  
ATOM   4255  CZ  ARG B1013      22.401  32.114  80.461  1.00 92.76           C  
ANISOU 4255  CZ  ARG B1013    11268  11425  12550   -385   1979   -572       C  
ATOM   4256  NH1 ARG B1013      21.895  33.331  80.337  1.00 86.92           N  
ANISOU 4256  NH1 ARG B1013    10542  10661  11823   -367   2140   -656       N  
ATOM   4257  NH2 ARG B1013      21.604  31.059  80.426  1.00109.03           N  
ANISOU 4257  NH2 ARG B1013    13323  13494  14610   -381   1836   -432       N  
ATOM   4258  N   LEU B1014      26.260  37.483  77.793  1.00126.51           N  
ANISOU 4258  N   LEU B1014    15762  15316  16990   -192   2684  -1245       N  
ATOM   4259  CA  LEU B1014      26.753  38.842  77.902  1.00125.17           C  
ANISOU 4259  CA  LEU B1014    15598  15145  16815   -204   2860  -1393       C  
ATOM   4260  C   LEU B1014      26.515  39.376  79.315  1.00130.56           C  
ANISOU 4260  C   LEU B1014    16195  15994  17419   -308   2932  -1437       C  
ATOM   4261  O   LEU B1014      27.366  40.095  79.827  1.00130.41           O  
ANISOU 4261  O   LEU B1014    16153  16029  17369   -354   3027  -1548       O  
ATOM   4262  CB  LEU B1014      26.066  39.709  76.842  1.00130.53           C  
ANISOU 4262  CB  LEU B1014    16351  15686  17560   -116   2965  -1429       C  
ATOM   4263  CG  LEU B1014      26.825  40.963  76.413  1.00133.67           C  
ANISOU 4263  CG  LEU B1014    16790  16017  17980    -90   3124  -1577       C  
ATOM   4264  CD1 LEU B1014      27.979  40.597  75.485  1.00107.27           C  
ANISOU 4264  CD1 LEU B1014    13505  12569  14685    -33   3079  -1597       C  
ATOM   4265  CD2 LEU B1014      25.882  41.944  75.732  1.00131.75           C  
ANISOU 4265  CD2 LEU B1014    16599  15679  17782    -29   3242  -1613       C  
ATOM   4266  N   LYS B1015      25.367  39.039  79.935  1.00132.85           N  
ANISOU 4266  N   LYS B1015    16438  16365  17675   -345   2887  -1352       N  
ATOM   4267  CA  LYS B1015      25.019  39.540  81.266  1.00116.37           C  
ANISOU 4267  CA  LYS B1015    14268  14436  15512   -442   2954  -1388       C  
ATOM   4268  C   LYS B1015      24.983  38.392  82.273  1.00101.63           C  
ANISOU 4268  C   LYS B1015    12327  12704  13583   -523   2811  -1289       C  
ATOM   4269  O   LYS B1015      24.821  37.233  81.890  1.00102.93           O  
ANISOU 4269  O   LYS B1015    12507  12833  13767   -497   2660  -1174       O  
ATOM   4270  CB  LYS B1015      23.671  40.269  81.265  1.00103.65           C  
ANISOU 4270  CB  LYS B1015    12657  12821  13904   -427   3041  -1388       C  
ATOM   4271  CG  LYS B1015      23.527  41.406  80.266  1.00115.00           C  
ANISOU 4271  CG  LYS B1015    14169  14123  15402   -346   3179  -1478       C  
ATOM   4272  CD  LYS B1015      22.281  42.245  80.499  1.00126.60           C  
ANISOU 4272  CD  LYS B1015    15625  15616  16861   -348   3279  -1496       C  
ATOM   4273  CE  LYS B1015      22.079  43.339  79.466  1.00140.97           C  
ANISOU 4273  CE  LYS B1015    17523  17295  18743   -264   3409  -1581       C  
ATOM   4274  NZ  LYS B1015      21.385  44.527  80.020  1.00142.79           N  
ANISOU 4274  NZ  LYS B1015    17738  17584  18932   -296   3469  -1624       N  
ATOM   4275  N   ILE B1016      25.125  38.736  83.558  1.00 94.67           N  
ANISOU 4275  N   ILE B1016    11365  11976  12628   -622   2859  -1336       N  
ATOM   4276  CA  ILE B1016      25.069  37.757  84.633  1.00105.81           C  
ANISOU 4276  CA  ILE B1016    12700  13529  13973   -709   2736  -1251       C  
ATOM   4277  C   ILE B1016      23.671  37.151  84.675  1.00107.40           C  
ANISOU 4277  C   ILE B1016    12887  13748  14170   -705   2654  -1125       C  
ATOM   4278  O   ILE B1016      22.670  37.859  84.538  1.00100.60           O  
ANISOU 4278  O   ILE B1016    12034  12870  13319   -682   2742  -1138       O  
ATOM   4279  CB  ILE B1016      25.467  38.371  85.990  1.00106.97           C  
ANISOU 4279  CB  ILE B1016    12765  13834  14043   -813   2820  -1335       C  
ATOM   4280  CG1 ILE B1016      26.846  39.018  85.912  1.00126.80           C  
ANISOU 4280  CG1 ILE B1016    15293  16322  16561   -814   2908  -1464       C  
ATOM   4281  CG2 ILE B1016      25.398  37.351  87.119  1.00105.53           C  
ANISOU 4281  CG2 ILE B1016    12505  13801  13793   -905   2693  -1247       C  
ATOM   4282  CD1 ILE B1016      27.139  39.937  87.059  1.00141.43           C  
ANISOU 4282  CD1 ILE B1016    17080  18305  18351   -897   3029  -1568       C  
ATOM   4283  N   TYR B1017      23.635  35.829  84.871  1.00102.12           N  
ANISOU 4283  N   TYR B1017    12199  13117  13486   -727   2484  -1004       N  
ATOM   4284  CA  TYR B1017      22.385  35.096  84.885  1.00 99.83           C  
ANISOU 4284  CA  TYR B1017    11897  12842  13191   -724   2385   -872       C  
ATOM   4285  C   TYR B1017      22.398  34.044  85.990  1.00108.13           C  
ANISOU 4285  C   TYR B1017    12872  14039  14172   -819   2250   -783       C  
ATOM   4286  O   TYR B1017      23.395  33.346  86.164  1.00106.50           O  
ANISOU 4286  O   TYR B1017    12659  13854  13954   -844   2160   -773       O  
ATOM   4287  CB  TYR B1017      22.152  34.447  83.525  1.00 91.19           C  
ANISOU 4287  CB  TYR B1017    10886  11586  12176   -618   2296   -792       C  
ATOM   4288  CG  TYR B1017      20.844  33.710  83.421  1.00 97.93           C  
ANISOU 4288  CG  TYR B1017    11735  12441  13032   -605   2196   -656       C  
ATOM   4289  CD1 TYR B1017      19.645  34.387  83.235  1.00102.21           C  
ANISOU 4289  CD1 TYR B1017    12286  12962  13588   -578   2281   -657       C  
ATOM   4290  CD2 TYR B1017      20.808  32.324  83.499  1.00 96.91           C  
ANISOU 4290  CD2 TYR B1017    11595  12334  12894   -619   2012   -526       C  
ATOM   4291  CE1 TYR B1017      18.442  33.701  83.119  1.00111.01           C  
ANISOU 4291  CE1 TYR B1017    13398  14076  14706   -564   2189   -532       C  
ATOM   4292  CE2 TYR B1017      19.618  31.626  83.376  1.00102.18           C  
ANISOU 4292  CE2 TYR B1017    12260  13000  13565   -606   1917   -399       C  
ATOM   4293  CZ  TYR B1017      18.428  32.314  83.186  1.00112.79           C  
ANISOU 4293  CZ  TYR B1017    13612  14322  14922   -579   2006   -401       C  
ATOM   4294  OH  TYR B1017      17.257  31.616  83.062  1.00110.94           O  
ANISOU 4294  OH  TYR B1017    13376  14086  14690   -566   1911   -275       O  
ATOM   4295  N   LYS B1018      21.271  33.939  86.717  1.00103.67           N  
ANISOU 4295  N   LYS B1018    12253  13575  13563   -871   2235   -720       N  
ATOM   4296  CA  LYS B1018      21.079  32.931  87.746  1.00 90.83           C  
ANISOU 4296  CA  LYS B1018    10555  12086  11869   -961   2104   -623       C  
ATOM   4297  C   LYS B1018      20.463  31.694  87.103  1.00 89.65           C  
ANISOU 4297  C   LYS B1018    10439  11872  11751   -915   1937   -473       C  
ATOM   4298  O   LYS B1018      19.321  31.729  86.669  1.00 83.22           O  
ANISOU 4298  O   LYS B1018     9645  11014  10962   -873   1938   -414       O  
ATOM   4299  CB  LYS B1018      20.199  33.488  88.867  1.00 97.01           C  
ANISOU 4299  CB  LYS B1018    11259  13014  12585  -1042   2179   -637       C  
ATOM   4300  N   ASP B1019      21.241  30.610  87.052  1.00101.15           N  
ANISOU 4300  N   ASP B1019    11901  13323  13207   -923   1792   -413       N  
ATOM   4301  CA  ASP B1019      20.900  29.410  86.306  1.00106.64           C  
ANISOU 4301  CA  ASP B1019    12639  13937  13941   -869   1627   -279       C  
ATOM   4302  C   ASP B1019      19.982  28.536  87.153  1.00 98.73           C  
ANISOU 4302  C   ASP B1019    11575  13055  12881   -942   1509   -154       C  
ATOM   4303  O   ASP B1019      19.757  28.847  88.315  1.00 96.32           O  
ANISOU 4303  O   ASP B1019    11195  12896  12506  -1036   1554   -178       O  
ATOM   4304  CB  ASP B1019      22.166  28.681  85.837  1.00119.05           C  
ANISOU 4304  CB  ASP B1019    14248  15448  15540   -842   1527   -277       C  
ATOM   4305  CG  ASP B1019      21.963  27.760  84.645  1.00129.02           C  
ANISOU 4305  CG  ASP B1019    15581  16571  16869   -748   1397   -174       C  
ATOM   4306  OD1 ASP B1019      20.800  27.604  84.212  1.00133.90           O  
ANISOU 4306  OD1 ASP B1019    16219  17145  17513   -707   1374    -93       O  
ATOM   4307  OD2 ASP B1019      22.967  27.192  84.171  1.00135.04           O1-
ANISOU 4307  OD2 ASP B1019    16378  17274  17659   -716   1318   -174       O1-
ATOM   4308  N   THR B1020      19.473  27.453  86.540  1.00108.91           N  
ANISOU 4308  N   THR B1020    12898  14280  14201   -897   1358    -22       N  
ATOM   4309  CA  THR B1020      18.482  26.539  87.090  1.00100.22           C  
ANISOU 4309  CA  THR B1020    11756  13265  13059   -948   1232    114       C  
ATOM   4310  C   THR B1020      18.931  26.008  88.455  1.00109.53           C  
ANISOU 4310  C   THR B1020    12851  14614  14151  -1070   1162    131       C  
ATOM   4311  O   THR B1020      18.101  25.788  89.336  1.00115.34           O  
ANISOU 4311  O   THR B1020    13525  15471  14829  -1144   1133    191       O  
ATOM   4312  CB  THR B1020      18.102  25.457  86.064  1.00 76.34           C  
ANISOU 4312  CB  THR B1020     8792  10122  10092   -868   1079    243       C  
ATOM   4313  N   GLU B1021      20.247  25.828  88.642  1.00117.66           N  
ANISOU 4313  N   GLU B1021    13880  15655  15172  -1091   1138     75       N  
ATOM   4314  CA  GLU B1021      20.781  25.130  89.809  1.00104.38           C  
ANISOU 4314  CA  GLU B1021    12129  14116  13416  -1198   1043    103       C  
ATOM   4315  C   GLU B1021      20.961  26.078  90.999  1.00 97.22           C  
ANISOU 4315  C   GLU B1021    11149  13349  12442  -1290   1179     -3       C  
ATOM   4316  O   GLU B1021      21.203  25.617  92.111  1.00 85.52           O  
ANISOU 4316  O   GLU B1021     9599  12004  10889  -1390   1118     20       O  
ATOM   4317  CB  GLU B1021      22.105  24.420  89.496  1.00114.19           C  
ANISOU 4317  CB  GLU B1021    13401  15310  14675  -1181    942     96       C  
ATOM   4318  CG  GLU B1021      22.099  23.564  88.236  1.00124.80           C  
ANISOU 4318  CG  GLU B1021    14823  16504  16091  -1081    817    182       C  
ATOM   4319  CD  GLU B1021      22.230  24.312  86.914  1.00133.53           C  
ANISOU 4319  CD  GLU B1021    16010  17442  17282   -963    920    114       C  
ATOM   4320  OE1 GLU B1021      22.860  25.405  86.882  1.00147.99           O  
ANISOU 4320  OE1 GLU B1021    17849  19258  19124   -954   1075    -22       O  
ATOM   4321  OE2 GLU B1021      21.692  23.803  85.915  1.00120.06           O1-
ANISOU 4321  OE2 GLU B1021    14363  15622  15635   -880    845    198       O1-
ATOM   4322  N   GLY B1022      20.868  27.395  90.761  1.00103.32           N  
ANISOU 4322  N   GLY B1022    11934  14085  13237  -1257   1362   -118       N  
ATOM   4323  CA  GLY B1022      21.122  28.404  91.783  1.00 96.52           C  
ANISOU 4323  CA  GLY B1022    11011  13342  12321  -1333   1504   -232       C  
ATOM   4324  C   GLY B1022      22.470  29.110  91.612  1.00113.16           C  
ANISOU 4324  C   GLY B1022    13140  15407  14447  -1316   1602   -369       C  
ATOM   4325  O   GLY B1022      22.782  30.024  92.375  1.00117.04           O  
ANISOU 4325  O   GLY B1022    13587  15985  14900  -1371   1730   -475       O  
ATOM   4326  N   TYR B1023      23.266  28.694  90.609  1.00123.55           N  
ANISOU 4326  N   TYR B1023    14525  16594  15823  -1240   1544   -369       N  
ATOM   4327  CA  TYR B1023      24.598  29.253  90.384  1.00113.03           C  
ANISOU 4327  CA  TYR B1023    13218  15218  14510  -1222   1622   -492       C  
ATOM   4328  C   TYR B1023      24.518  30.438  89.429  1.00 99.05           C  
ANISOU 4328  C   TYR B1023    11508  13324  12803  -1134   1781   -589       C  
ATOM   4329  O   TYR B1023      23.818  30.354  88.431  1.00109.65           O  
ANISOU 4329  O   TYR B1023    12907  14550  14203  -1050   1765   -537       O  
ATOM   4330  CB  TYR B1023      25.518  28.186  89.781  1.00118.85           C  
ANISOU 4330  CB  TYR B1023    13998  15880  15278  -1184   1474   -443       C  
ATOM   4331  CG  TYR B1023      25.808  27.024  90.701  1.00121.81           C  
ANISOU 4331  CG  TYR B1023    14320  16372  15592  -1270   1315   -361       C  
ATOM   4332  CD1 TYR B1023      26.837  27.078  91.641  1.00107.94           C  
ANISOU 4332  CD1 TYR B1023    12513  14719  13782  -1350   1326   -431       C  
ATOM   4333  CD2 TYR B1023      25.022  25.882  90.662  1.00122.25           C  
ANISOU 4333  CD2 TYR B1023    14372  16436  15641  -1274   1154   -212       C  
ATOM   4334  CE1 TYR B1023      27.099  26.020  92.498  1.00104.92           C  
ANISOU 4334  CE1 TYR B1023    12081  14442  13342  -1431   1180   -357       C  
ATOM   4335  CE2 TYR B1023      25.265  24.822  91.525  1.00129.63           C  
ANISOU 4335  CE2 TYR B1023    15256  17479  16517  -1356   1006   -136       C  
ATOM   4336  CZ  TYR B1023      26.294  24.894  92.448  1.00126.56           C  
ANISOU 4336  CZ  TYR B1023    14820  17191  16076  -1435   1019   -208       C  
ATOM   4337  OH  TYR B1023      26.496  23.820  93.265  1.00135.94           O  
ANISOU 4337  OH  TYR B1023    15962  18480  17207  -1514    868   -129       O  
ATOM   4338  N   TYR B1024      25.221  31.532  89.731  1.00 84.45           N  
ANISOU 4338  N   TYR B1024     9647  11498  10943  -1152   1931   -728       N  
ATOM   4339  CA  TYR B1024      25.300  32.635  88.786  1.00 96.94           C  
ANISOU 4339  CA  TYR B1024    11292  12956  12587  -1069   2077   -826       C  
ATOM   4340  C   TYR B1024      26.394  32.360  87.753  1.00108.91           C  
ANISOU 4340  C   TYR B1024    12879  14340  14162   -994   2040   -855       C  
ATOM   4341  O   TYR B1024      27.519  32.009  88.110  1.00116.31           O  
ANISOU 4341  O   TYR B1024    13800  15315  15077  -1030   1996   -888       O  
ATOM   4342  CB  TYR B1024      25.521  33.973  89.496  1.00110.38           C  
ANISOU 4342  CB  TYR B1024    12953  14732  14254  -1116   2258   -964       C  
ATOM   4343  CG  TYR B1024      24.339  34.488  90.275  1.00138.11           C  
ANISOU 4343  CG  TYR B1024    16408  18346  17721  -1167   2325   -952       C  
ATOM   4344  CD1 TYR B1024      24.120  34.102  91.591  1.00157.31           C  
ANISOU 4344  CD1 TYR B1024    18753  20945  20073  -1274   2278   -914       C  
ATOM   4345  CD2 TYR B1024      23.457  35.398  89.717  1.00141.52           C  
ANISOU 4345  CD2 TYR B1024    16873  18710  18188  -1111   2441   -986       C  
ATOM   4346  CE1 TYR B1024      23.041  34.577  92.322  1.00161.52           C  
ANISOU 4346  CE1 TYR B1024    19231  21577  20562  -1322   2339   -905       C  
ATOM   4347  CE2 TYR B1024      22.363  35.870  90.425  1.00152.05           C  
ANISOU 4347  CE2 TYR B1024    18154  20140  19480  -1156   2501   -977       C  
ATOM   4348  CZ  TYR B1024      22.160  35.468  91.734  1.00157.53           C  
ANISOU 4348  CZ  TYR B1024    18759  21002  20095  -1262   2451   -938       C  
ATOM   4349  OH  TYR B1024      21.103  35.950  92.446  1.00165.13           O  
ANISOU 4349  OH  TYR B1024    19666  22062  21013  -1308   2512   -934       O  
ATOM   4350  N   THR B1025      26.056  32.553  86.472  1.00118.39           N  
ANISOU 4350  N   THR B1025    14158  15386  15438   -889   2061   -846       N  
ATOM   4351  CA  THR B1025      26.944  32.243  85.358  1.00118.70           C  
ANISOU 4351  CA  THR B1025    14271  15289  15542   -807   2018   -860       C  
ATOM   4352  C   THR B1025      27.042  33.438  84.412  1.00103.22           C  
ANISOU 4352  C   THR B1025    12374  13204  13641   -726   2175   -966       C  
ATOM   4353  O   THR B1025      26.163  34.296  84.413  1.00 99.52           O  
ANISOU 4353  O   THR B1025    11904  12731  13176   -717   2287   -995       O  
ATOM   4354  CB  THR B1025      26.460  30.993  84.606  1.00138.54           C  
ANISOU 4354  CB  THR B1025    16823  17722  18092   -750   1845   -716       C  
ATOM   4355  OG1 THR B1025      27.407  30.668  83.587  1.00151.20           O  
ANISOU 4355  OG1 THR B1025    18492  19202  19753   -675   1799   -734       O  
ATOM   4356  CG2 THR B1025      25.094  31.165  83.968  1.00152.78           C  
ANISOU 4356  CG2 THR B1025    18659  19453  19935   -690   1865   -652       C  
ATOM   4357  N   ILE B1026      28.101  33.447  83.589  1.00 94.41           N  
ANISOU 4357  N   ILE B1026    11315  11986  12572   -669   2176  -1020       N  
ATOM   4358  CA  ILE B1026      28.331  34.443  82.554  1.00 95.08           C  
ANISOU 4358  CA  ILE B1026    11470  11937  12720   -586   2306  -1114       C  
ATOM   4359  C   ILE B1026      29.435  33.953  81.623  1.00 92.01           C  
ANISOU 4359  C   ILE B1026    11140  11440  12380   -522   2240  -1126       C  
ATOM   4360  O   ILE B1026      30.177  33.037  81.965  1.00 81.96           O  
ANISOU 4360  O   ILE B1026     9844  10215  11082   -556   2119  -1089       O  
ATOM   4361  CB  ILE B1026      28.726  35.805  83.168  1.00101.50           C  
ANISOU 4361  CB  ILE B1026    12254  12810  13501   -632   2489  -1260       C  
ATOM   4362  CG1 ILE B1026      28.468  36.950  82.182  1.00 93.59           C  
ANISOU 4362  CG1 ILE B1026    11320  11680  12560   -550   2635  -1341       C  
ATOM   4363  CG2 ILE B1026      30.161  35.783  83.692  1.00 77.49           C  
ANISOU 4363  CG2 ILE B1026     9187   9829  10427   -683   2491  -1340       C  
ATOM   4364  CD1 ILE B1026      28.674  38.324  82.760  1.00 96.07           C  
ANISOU 4364  CD1 ILE B1026    11608  12050  12845   -592   2815  -1478       C  
ATOM   4365  N   GLY B1027      29.558  34.607  80.462  1.00 87.39           N  
ANISOU 4365  N   GLY B1027    10630  10711  11863   -431   2323  -1183       N  
ATOM   4366  CA  GLY B1027      30.574  34.243  79.487  1.00 84.64           C  
ANISOU 4366  CA  GLY B1027    10342  10251  11565   -364   2274  -1202       C  
ATOM   4367  C   GLY B1027      30.276  32.882  78.864  1.00 84.24           C  
ANISOU 4367  C   GLY B1027    10320  10139  11548   -314   2088  -1062       C  
ATOM   4368  O   GLY B1027      29.134  32.604  78.501  1.00 89.34           O  
ANISOU 4368  O   GLY B1027    10983  10743  12218   -277   2048   -971       O  
ATOM   4369  N   ILE B1028      31.307  32.036  78.761  1.00 87.24           N  
ANISOU 4369  N   ILE B1028    10704  10517  11926   -314   1974  -1046       N  
ATOM   4370  CA  ILE B1028      31.120  30.711  78.193  1.00 90.81           C  
ANISOU 4370  CA  ILE B1028    11182  10914  12408   -268   1791   -916       C  
ATOM   4371  C   ILE B1028      31.159  29.695  79.331  1.00 97.44           C  
ANISOU 4371  C   ILE B1028    11949  11896  13177   -360   1655   -837       C  
ATOM   4372  O   ILE B1028      32.207  29.124  79.636  1.00 98.34           O  
ANISOU 4372  O   ILE B1028    12045  12051  13267   -391   1577   -851       O  
ATOM   4373  CB  ILE B1028      32.148  30.399  77.082  1.00 97.06           C  
ANISOU 4373  CB  ILE B1028    12039  11582  13256   -188   1745   -942       C  
ATOM   4374  CG1 ILE B1028      32.164  31.440  75.954  1.00115.46           C  
ANISOU 4374  CG1 ILE B1028    14442  13772  15654   -100   1884  -1026       C  
ATOM   4375  CG2 ILE B1028      31.915  29.004  76.529  1.00 96.97           C  
ANISOU 4375  CG2 ILE B1028    12052  11519  13274   -141   1549   -804       C  
ATOM   4376  CD1 ILE B1028      33.126  32.593  76.158  1.00124.84           C  
ANISOU 4376  CD1 ILE B1028    15628  14978  16829   -126   2043  -1183       C  
ATOM   4377  N   GLY B1029      30.006  29.502  79.978  1.00 85.84           N  
ANISOU 4377  N   GLY B1029    10437  10502  11674   -404   1629   -757       N  
ATOM   4378  CA  GLY B1029      29.883  28.517  81.040  1.00 83.13           C  
ANISOU 4378  CA  GLY B1029    10028  10293  11266   -490   1496   -670       C  
ATOM   4379  C   GLY B1029      30.763  28.822  82.253  1.00 88.03           C  
ANISOU 4379  C   GLY B1029    10581  11053  11815   -593   1543   -756       C  
ATOM   4380  O   GLY B1029      31.276  27.905  82.901  1.00102.89           O  
ANISOU 4380  O   GLY B1029    12423  13016  13653   -650   1417   -710       O  
ATOM   4381  N   HIS B1030      30.922  30.112  82.567  1.00 75.31           N  
ANISOU 4381  N   HIS B1030     8956   9468  10191   -616   1723   -880       N  
ATOM   4382  CA  HIS B1030      31.720  30.476  83.723  1.00 93.39           C  
ANISOU 4382  CA  HIS B1030    11182  11889  12414   -711   1778   -965       C  
ATOM   4383  C   HIS B1030      30.835  30.636  84.955  1.00 98.30           C  
ANISOU 4383  C   HIS B1030    11726  12655  12968   -804   1804   -935       C  
ATOM   4384  O   HIS B1030      30.240  31.691  85.160  1.00 98.99           O  
ANISOU 4384  O   HIS B1030    11802  12761  13050   -813   1948   -995       O  
ATOM   4385  CB  HIS B1030      32.581  31.717  83.453  1.00102.32           C  
ANISOU 4385  CB  HIS B1030    12337  12978  13564   -692   1949  -1122       C  
ATOM   4386  CG  HIS B1030      33.466  32.063  84.603  1.00101.13           C  
ANISOU 4386  CG  HIS B1030    12122  12956  13346   -786   2002  -1210       C  
ATOM   4387  ND1 HIS B1030      34.595  31.320  84.937  1.00 99.39           N  
ANISOU 4387  ND1 HIS B1030    11885  12779  13101   -821   1903  -1216       N  
ATOM   4388  CD2 HIS B1030      33.371  33.044  85.519  1.00107.52           C  
ANISOU 4388  CD2 HIS B1030    12881  13864  14109   -854   2139  -1295       C  
ATOM   4389  CE1 HIS B1030      35.165  31.848  85.998  1.00101.24           C  
ANISOU 4389  CE1 HIS B1030    12061  13131  13276   -905   1981  -1301       C  
ATOM   4390  NE2 HIS B1030      34.445  32.919  86.366  1.00110.37           N  
ANISOU 4390  NE2 HIS B1030    13195  14321  14419   -926   2127  -1352       N  
ATOM   4391  N   LEU B1031      30.796  29.582  85.775  1.00 92.87           N  
ANISOU 4391  N   LEU B1031    10986  12072  12228   -873   1661   -846       N  
ATOM   4392  CA  LEU B1031      30.042  29.579  87.014  1.00 96.47           C  
ANISOU 4392  CA  LEU B1031    11363  12676  12613   -969   1664   -809       C  
ATOM   4393  C   LEU B1031      30.794  30.387  88.070  1.00 89.64           C  
ANISOU 4393  C   LEU B1031    10440  11926  11691  -1052   1780   -931       C  
ATOM   4394  O   LEU B1031      31.996  30.234  88.246  1.00 84.59           O  
ANISOU 4394  O   LEU B1031     9798  11303  11040  -1073   1761   -989       O  
ATOM   4395  CB  LEU B1031      29.829  28.127  87.458  1.00 95.45           C  
ANISOU 4395  CB  LEU B1031    11204  12611  12451  -1011   1463   -672       C  
ATOM   4396  CG  LEU B1031      28.629  27.412  86.834  1.00102.44           C  
ANISOU 4396  CG  LEU B1031    12119  13433  13370   -959   1360   -535       C  
ATOM   4397  CD1 LEU B1031      28.872  27.055  85.368  1.00104.20           C  
ANISOU 4397  CD1 LEU B1031    12430  13484  13676   -842   1305   -508       C  
ATOM   4398  CD2 LEU B1031      28.253  26.171  87.638  1.00106.77           C  
ANISOU 4398  CD2 LEU B1031    12616  14087  13864  -1031   1187   -408       C  
ATOM   4399  N   LEU B1032      30.066  31.250  88.781  1.00 90.66           N  
ANISOU 4399  N   LEU B1032    10524  12137  11786  -1101   1899   -969       N  
ATOM   4400  CA  LEU B1032      30.649  32.030  89.859  1.00110.36           C  
ANISOU 4400  CA  LEU B1032    12959  14751  14223  -1184   2011  -1077       C  
ATOM   4401  C   LEU B1032      30.396  31.324  91.197  1.00123.15           C  
ANISOU 4401  C   LEU B1032    14494  16535  15762  -1293   1918  -1009       C  
ATOM   4402  O   LEU B1032      31.060  30.338  91.518  1.00135.19           O  
ANISOU 4402  O   LEU B1032    16003  18100  17264  -1328   1785   -963       O  
ATOM   4403  CB  LEU B1032      30.098  33.461  89.786  1.00103.46           C  
ANISOU 4403  CB  LEU B1032    12089  13861  13361  -1166   2203  -1171       C  
ATOM   4404  CG  LEU B1032      30.344  34.184  88.453  1.00 91.01           C  
ANISOU 4404  CG  LEU B1032    10598  12118  11862  -1059   2296  -1240       C  
ATOM   4405  CD1 LEU B1032      29.492  35.436  88.297  1.00 81.58           C  
ANISOU 4405  CD1 LEU B1032     9413  10900  10683  -1035   2459  -1302       C  
ATOM   4406  CD2 LEU B1032      31.815  34.518  88.255  1.00 91.17           C  
ANISOU 4406  CD2 LEU B1032    10641  12106  11894  -1050   2343  -1350       C  
ATOM   4407  N   THR B1033      29.420  31.808  91.971  1.00138.65           N  
ANISOU 4407  N   THR B1033    16403  18594  17684  -1347   1985  -1001       N  
ATOM   4408  CA  THR B1033      29.067  31.163  93.230  1.00165.93           C  
ANISOU 4408  CA  THR B1033    19776  22207  21062  -1451   1900   -932       C  
ATOM   4409  C   THR B1033      27.551  30.969  93.322  1.00169.68           C  
ANISOU 4409  C   THR B1033    20233  22708  21528  -1455   1871   -829       C  
ATOM   4410  O   THR B1033      26.785  31.722  92.730  1.00141.00           O  
ANISOU 4410  O   THR B1033    16633  19008  17934  -1398   1970   -850       O  
ATOM   4411  CB  THR B1033      29.633  31.900  94.459  1.00168.98           C  
ANISOU 4411  CB  THR B1033    20092  22730  21384  -1544   2006  -1037       C  
ATOM   4412  OG1 THR B1033      29.340  33.296  94.362  1.00173.32           O  
ANISOU 4412  OG1 THR B1033    20646  23262  21947  -1523   2194  -1143       O  
ATOM   4413  CG2 THR B1033      31.113  31.670  94.678  1.00135.59           C  
ANISOU 4413  CG2 THR B1033    15861  18513  17142  -1568   1979  -1102       C  
ATOM   4414  N   LYS B1034      27.142  29.965  94.111  1.00174.25           N  
ANISOU 4414  N   LYS B1034    20759  23393  22054  -1527   1735   -722       N  
ATOM   4415  CA  LYS B1034      25.752  29.603  94.353  1.00158.85           C  
ANISOU 4415  CA  LYS B1034    18782  21489  20083  -1546   1683   -613       C  
ATOM   4416  C   LYS B1034      25.071  30.614  95.280  1.00162.18           C  
ANISOU 4416  C   LYS B1034    19139  22027  20456  -1609   1823   -672       C  
ATOM   4417  O   LYS B1034      23.851  30.569  95.423  1.00172.87           O  
ANISOU 4417  O   LYS B1034    20472  23414  21796  -1617   1814   -602       O  
ATOM   4418  CB  LYS B1034      25.681  28.184  94.937  1.00141.78           C  
ANISOU 4418  CB  LYS B1034    16584  19408  17877  -1608   1489   -484       C  
ATOM   4419  CG  LYS B1034      24.312  27.524  94.902  1.00131.06           C  
ANISOU 4419  CG  LYS B1034    15218  18067  16513  -1610   1395   -347       C  
ATOM   4420  CD  LYS B1034      24.323  26.085  95.335  1.00150.05           C  
ANISOU 4420  CD  LYS B1034    17599  20532  18882  -1662   1195   -219       C  
ATOM   4421  CE  LYS B1034      22.971  25.425  95.157  1.00180.57           C  
ANISOU 4421  CE  LYS B1034    21464  24397  22748  -1652   1100    -81       C  
ATOM   4422  NZ  LYS B1034      21.916  26.062  95.983  1.00194.11           N  
ANISOU 4422  NZ  LYS B1034    23116  26226  24413  -1713   1191    -85       N  
ATOM   4423  N   SER B1035      25.856  31.509  95.906  1.00167.99           N  
ANISOU 4423  N   SER B1035    19842  22823  21162  -1651   1948   -800       N  
ATOM   4424  CA  SER B1035      25.353  32.483  96.870  1.00157.95           C  
ANISOU 4424  CA  SER B1035    18504  21670  19839  -1716   2081   -866       C  
ATOM   4425  C   SER B1035      24.215  33.293  96.261  1.00147.76           C  
ANISOU 4425  C   SER B1035    17242  20316  18585  -1654   2184   -875       C  
ATOM   4426  O   SER B1035      24.429  33.992  95.278  1.00121.66           O  
ANISOU 4426  O   SER B1035    14002  16881  15342  -1569   2274   -943       O  
ATOM   4427  CB  SER B1035      26.451  33.388  97.364  1.00150.00           C  
ANISOU 4427  CB  SER B1035    17477  20704  18814  -1748   2207  -1010       C  
ATOM   4428  OG  SER B1035      27.450  32.621  98.018  1.00162.74           O  
ANISOU 4428  OG  SER B1035    19058  22387  20388  -1812   2109  -1001       O  
ATOM   4429  N   PRO B1036      22.978  33.207  96.811  1.00170.39           N  
ANISOU 4429  N   PRO B1036    20060  23268  21413  -1695   2170   -805       N  
ATOM   4430  CA  PRO B1036      21.828  33.916  96.243  1.00172.30           C  
ANISOU 4430  CA  PRO B1036    20328  23451  21688  -1637   2259   -807       C  
ATOM   4431  C   PRO B1036      21.912  35.424  96.465  1.00176.72           C  
ANISOU 4431  C   PRO B1036    20875  24027  22243  -1637   2457   -951       C  
ATOM   4432  O   PRO B1036      21.172  35.972  97.279  1.00186.97           O  
ANISOU 4432  O   PRO B1036    22112  25435  23493  -1691   2528   -970       O  
ATOM   4433  CB  PRO B1036      20.635  33.320  97.012  1.00178.46           C  
ANISOU 4433  CB  PRO B1036    21045  24350  22412  -1703   2179   -695       C  
ATOM   4434  CG  PRO B1036      21.216  32.858  98.337  1.00164.33           C  
ANISOU 4434  CG  PRO B1036    19175  22721  20544  -1818   2123   -690       C  
ATOM   4435  CD  PRO B1036      22.622  32.408  97.999  1.00171.10           C  
ANISOU 4435  CD  PRO B1036    20068  23515  21425  -1800   2066   -720       C  
ATOM   4436  N   SER B1037      22.827  36.079  95.736  1.00163.84           N  
ANISOU 4436  N   SER B1037    19302  22288  20663  -1575   2544  -1054       N  
ATOM   4437  CA  SER B1037      23.061  37.507  95.878  1.00148.88           C  
ANISOU 4437  CA  SER B1037    17403  20397  18769  -1570   2729  -1197       C  
ATOM   4438  C   SER B1037      23.689  38.040  94.596  1.00145.94           C  
ANISOU 4438  C   SER B1037    17122  19852  18476  -1467   2796  -1269       C  
ATOM   4439  O   SER B1037      24.876  37.833  94.353  1.00145.99           O  
ANISOU 4439  O   SER B1037    17155  19815  18499  -1457   2774  -1309       O  
ATOM   4440  CB  SER B1037      23.920  37.804  97.080  1.00134.17           C  
ANISOU 4440  CB  SER B1037    15468  18668  16840  -1664   2774  -1275       C  
ATOM   4441  OG  SER B1037      25.128  37.055  97.029  1.00135.88           O  
ANISOU 4441  OG  SER B1037    15700  18868  17062  -1674   2683  -1269       O  
ATOM   4442  N   LEU B1038      22.869  38.711  93.780  1.00141.72           N  
ANISOU 4442  N   LEU B1038    16637  19222  17990  -1393   2876  -1285       N  
ATOM   4443  CA  LEU B1038      23.311  39.308  92.529  1.00126.11           C  
ANISOU 4443  CA  LEU B1038    14749  17077  16089  -1293   2950  -1353       C  
ATOM   4444  C   LEU B1038      24.352  40.392  92.804  1.00138.87           C  
ANISOU 4444  C   LEU B1038    16361  18708  17698  -1309   3092  -1505       C  
ATOM   4445  O   LEU B1038      25.248  40.623  91.986  1.00150.62           O  
ANISOU 4445  O   LEU B1038    17911  20083  19235  -1251   3123  -1566       O  
ATOM   4446  CB  LEU B1038      22.084  39.861  91.797  1.00105.18           C  
ANISOU 4446  CB  LEU B1038    12139  14345  13480  -1223   3012  -1339       C  
ATOM   4447  CG  LEU B1038      22.331  40.480  90.425  1.00100.50           C  
ANISOU 4447  CG  LEU B1038    11644  13572  12971  -1114   3087  -1399       C  
ATOM   4448  CD1 LEU B1038      22.887  39.448  89.469  1.00107.36           C  
ANISOU 4448  CD1 LEU B1038    12575  14324  13892  -1053   2958  -1326       C  
ATOM   4449  CD2 LEU B1038      21.038  41.033  89.852  1.00112.38           C  
ANISOU 4449  CD2 LEU B1038    13179  15012  14507  -1056   3149  -1385       C  
ATOM   4450  N   ASN B1039      24.222  41.042  93.967  1.00139.98           N  
ANISOU 4450  N   ASN B1039    16425  18989  17774  -1390   3176  -1565       N  
ATOM   4451  CA  ASN B1039      25.127  42.114  94.345  1.00137.46           C  
ANISOU 4451  CA  ASN B1039    16093  18697  17440  -1413   3315  -1709       C  
ATOM   4452  C   ASN B1039      26.524  41.565  94.617  1.00143.83           C  
ANISOU 4452  C   ASN B1039    16891  19525  18233  -1448   3255  -1731       C  
ATOM   4453  O   ASN B1039      27.517  42.161  94.206  1.00169.53           O  
ANISOU 4453  O   ASN B1039    20185  22713  21516  -1418   3332  -1831       O  
ATOM   4454  CB  ASN B1039      24.610  42.933  95.524  1.00144.92           C  
ANISOU 4454  CB  ASN B1039    16989  19755  18322  -1461   3343  -1732       C  
ATOM   4455  CG  ASN B1039      25.408  44.206  95.701  1.00155.37           C  
ANISOU 4455  CG  ASN B1039    18365  21022  19647  -1419   3372  -1824       C  
ATOM   4456  OD1 ASN B1039      26.098  44.662  94.785  1.00140.64           O  
ANISOU 4456  OD1 ASN B1039    16578  19022  17835  -1347   3394  -1875       O  
ATOM   4457  ND2 ASN B1039      25.306  44.802  96.876  1.00169.92           N  
ANISOU 4457  ND2 ASN B1039    20166  22965  21432  -1466   3367  -1842       N  
ATOM   4458  N   ALA B1040      26.590  40.412  95.292  1.00141.40           N  
ANISOU 4458  N   ALA B1040    16535  19309  17882  -1511   3112  -1635       N  
ATOM   4459  CA  ALA B1040      27.860  39.763  95.600  1.00133.50           C  
ANISOU 4459  CA  ALA B1040    15523  18336  16864  -1548   3037  -1644       C  
ATOM   4460  C   ALA B1040      28.405  38.988  94.396  1.00129.56           C  
ANISOU 4460  C   ALA B1040    15105  17691  16430  -1468   2937  -1596       C  
ATOM   4461  O   ALA B1040      29.616  38.838  94.259  1.00130.25           O  
ANISOU 4461  O   ALA B1040    15211  17751  16527  -1465   2923  -1645       O  
ATOM   4462  CB  ALA B1040      27.743  38.899  96.834  1.00117.23           C  
ANISOU 4462  CB  ALA B1040    13379  16434  14730  -1650   2930  -1569       C  
ATOM   4463  N   ALA B1041      27.511  38.514  93.518  1.00135.36           N  
ANISOU 4463  N   ALA B1041    15887  18332  17210  -1401   2870  -1501       N  
ATOM   4464  CA  ALA B1041      27.915  37.819  92.302  1.00126.69           C  
ANISOU 4464  CA  ALA B1041    14870  17088  16179  -1316   2778  -1453       C  
ATOM   4465  C   ALA B1041      28.632  38.770  91.340  1.00124.38           C  
ANISOU 4465  C   ALA B1041    14648  16665  15946  -1240   2900  -1569       C  
ATOM   4466  O   ALA B1041      29.595  38.358  90.700  1.00132.29           O  
ANISOU 4466  O   ALA B1041    15695  17585  16982  -1200   2849  -1580       O  
ATOM   4467  CB  ALA B1041      26.735  37.135  91.647  1.00107.67           C  
ANISOU 4467  CB  ALA B1041    12491  14615  13802  -1265   2683  -1326       C  
ATOM   4468  N   LYS B1042      28.164  40.028  91.241  1.00110.07           N  
ANISOU 4468  N   LYS B1042    12844  14834  14144  -1219   3058  -1656       N  
ATOM   4469  CA  LYS B1042      28.811  41.049  90.420  1.00102.75           C  
ANISOU 4469  CA  LYS B1042    11980  13793  13267  -1155   3188  -1774       C  
ATOM   4470  C   LYS B1042      30.187  41.409  90.989  1.00113.84           C  
ANISOU 4470  C   LYS B1042    13359  15253  14642  -1204   3241  -1881       C  
ATOM   4471  O   LYS B1042      31.140  41.670  90.251  1.00130.59           O  
ANISOU 4471  O   LYS B1042    15537  17278  16806  -1155   3276  -1949       O  
ATOM   4472  CB  LYS B1042      27.918  42.280  90.235  1.00 76.19           C  
ANISOU 4472  CB  LYS B1042     8628  10402   9917  -1125   3337  -1837       C  
ATOM   4473  N   SER B1043      30.292  41.415  92.317  1.00117.98           N  
ANISOU 4473  N   SER B1043    13799  15936  15093  -1303   3247  -1895       N  
ATOM   4474  CA  SER B1043      31.559  41.729  92.950  1.00120.97           C  
ANISOU 4474  CA  SER B1043    14146  16377  15438  -1356   3295  -1993       C  
ATOM   4475  C   SER B1043      32.526  40.548  92.838  1.00126.87           C  
ANISOU 4475  C   SER B1043    14903  17114  16188  -1363   3149  -1941       C  
ATOM   4476  O   SER B1043      33.724  40.750  92.664  1.00120.62           O  
ANISOU 4476  O   SER B1043    14132  16292  15406  -1356   3180  -2022       O  
ATOM   4477  CB  SER B1043      31.358  42.163  94.374  1.00127.67           C  
ANISOU 4477  CB  SER B1043    14924  17373  16212  -1439   3303  -2004       C  
ATOM   4478  OG  SER B1043      32.565  42.724  94.862  1.00128.36           O  
ANISOU 4478  OG  SER B1043    15024  17467  16280  -1451   3300  -2078       O  
ATOM   4479  N   GLU B1044      32.001  39.320  92.950  1.00140.04           N  
ANISOU 4479  N   GLU B1044    16555  18809  17844  -1377   2990  -1807       N  
ATOM   4480  CA  GLU B1044      32.790  38.105  92.775  1.00134.42           C  
ANISOU 4480  CA  GLU B1044    15856  18081  17137  -1378   2836  -1744       C  
ATOM   4481  C   GLU B1044      33.313  38.029  91.347  1.00135.58           C  
ANISOU 4481  C   GLU B1044    16095  18057  17361  -1274   2823  -1757       C  
ATOM   4482  O   GLU B1044      34.393  37.493  91.121  1.00140.09           O  
ANISOU 4482  O   GLU B1044    16686  18600  17942  -1267   2756  -1770       O  
ATOM   4483  CB  GLU B1044      31.983  36.844  93.098  1.00139.37           C  
ANISOU 4483  CB  GLU B1044    16453  18762  17739  -1407   2669  -1592       C  
ATOM   4484  N   LEU B1045      32.540  38.570  90.396  1.00144.95           N  
ANISOU 4484  N   LEU B1045    17339  19132  18603  -1195   2887  -1755       N  
ATOM   4485  CA  LEU B1045      32.953  38.621  89.000  1.00161.38           C  
ANISOU 4485  CA  LEU B1045    19510  21045  20760  -1093   2890  -1773       C  
ATOM   4486  C   LEU B1045      33.955  39.751  88.770  1.00168.97           C  
ANISOU 4486  C   LEU B1045    20498  21966  21737  -1077   3039  -1924       C  
ATOM   4487  O   LEU B1045      34.818  39.621  87.903  1.00171.14           O  
ANISOU 4487  O   LEU B1045    20831  22138  22057  -1020   3022  -1955       O  
ATOM   4488  CB  LEU B1045      31.734  38.765  88.077  1.00160.12           C  
ANISOU 4488  CB  LEU B1045    19403  20782  20654  -1014   2900  -1714       C  
ATOM   4489  CG  LEU B1045      32.033  38.816  86.577  1.00143.17           C  
ANISOU 4489  CG  LEU B1045    17351  18455  18590   -904   2903  -1725       C  
ATOM   4490  CD1 LEU B1045      32.686  37.528  86.112  1.00141.71           C  
ANISOU 4490  CD1 LEU B1045    17192  18227  18426   -879   2736  -1646       C  
ATOM   4491  CD2 LEU B1045      30.772  39.069  85.774  1.00142.30           C  
ANISOU 4491  CD2 LEU B1045    17287  18253  18528   -833   2928  -1674       C  
ATOM   4492  N   ASP B1046      33.830  40.854  89.526  1.00170.80           N  
ANISOU 4492  N   ASP B1046    20687  22277  21932  -1126   3182  -2017       N  
ATOM   4493  CA  ASP B1046      34.710  42.005  89.362  1.00145.83           C  
ANISOU 4493  CA  ASP B1046    17550  19079  18781  -1113   3324  -2157       C  
ATOM   4494  C   ASP B1046      36.163  41.617  89.654  1.00134.50           C  
ANISOU 4494  C   ASP B1046    16100  17678  17326  -1149   3290  -2210       C  
ATOM   4495  O   ASP B1046      37.075  42.015  88.922  1.00120.91           O  
ANISOU 4495  O   ASP B1046    14447  15852  15643  -1093   3292  -2260       O  
ATOM   4496  CB  ASP B1046      34.227  43.202  90.185  1.00148.06           C  
ANISOU 4496  CB  ASP B1046    17825  19408  19024  -1136   3343  -2168       C  
ATOM   4497  N   LYS B1047      36.355  40.825  90.722  1.00142.84           N  
ANISOU 4497  N   LYS B1047    17086  18864  18322  -1232   3194  -2160       N  
ATOM   4498  CA  LYS B1047      37.657  40.322  91.150  1.00155.32           C  
ANISOU 4498  CA  LYS B1047    18645  20493  19876  -1274   3137  -2193       C  
ATOM   4499  C   LYS B1047      38.210  39.352  90.106  1.00142.02           C  
ANISOU 4499  C   LYS B1047    17024  18696  18242  -1206   3010  -2137       C  
ATOM   4500  O   LYS B1047      39.416  39.302  89.893  1.00120.63           O  
ANISOU 4500  O   LYS B1047    14334  15959  15540  -1199   3007  -2201       O  
ATOM   4501  CB  LYS B1047      37.556  39.709  92.558  1.00170.55           C  
ANISOU 4501  CB  LYS B1047    20484  22589  21728  -1379   3063  -2145       C  
ATOM   4502  CG  LYS B1047      38.646  38.739  93.024  1.00167.24           C  
ANISOU 4502  CG  LYS B1047    20039  22225  21278  -1425   2943  -2129       C  
ATOM   4503  CD  LYS B1047      39.959  39.399  93.388  1.00160.29           C  
ANISOU 4503  CD  LYS B1047    19149  21376  20380  -1456   3037  -2262       C  
ATOM   4504  CE  LYS B1047      40.666  38.716  94.550  1.00153.17           C  
ANISOU 4504  CE  LYS B1047    18178  20607  19413  -1548   2955  -2255       C  
ATOM   4505  NZ  LYS B1047      41.393  39.670  95.429  1.00136.80           N  
ANISOU 4505  NZ  LYS B1047    16060  18620  17297  -1610   3087  -2381       N  
ATOM   4506  N   ALA B1048      37.313  38.606  89.447  1.00137.79           N  
ANISOU 4506  N   ALA B1048    16520  18094  17740  -1155   2906  -2019       N  
ATOM   4507  CA  ALA B1048      37.705  37.554  88.529  1.00127.30           C  
ANISOU 4507  CA  ALA B1048    15244  16668  16455  -1094   2766  -1948       C  
ATOM   4508  C   ALA B1048      37.754  38.073  87.088  1.00110.00           C  
ANISOU 4508  C   ALA B1048    13143  14309  14344   -986   2828  -1985       C  
ATOM   4509  O   ALA B1048      37.826  37.280  86.155  1.00115.59           O  
ANISOU 4509  O   ALA B1048    13903  14917  15098   -920   2720  -1917       O  
ATOM   4510  CB  ALA B1048      36.765  36.380  88.699  1.00111.30           C  
ANISOU 4510  CB  ALA B1048    13197  14673  14418  -1105   2608  -1796       C  
ATOM   4511  N   ILE B1049      37.702  39.398  86.895  1.00102.16           N  
ANISOU 4511  N   ILE B1049    12169  13281  13365   -968   3001  -2092       N  
ATOM   4512  CA  ILE B1049      37.806  39.967  85.554  1.00107.72           C  
ANISOU 4512  CA  ILE B1049    12959  13828  14143   -870   3069  -2137       C  
ATOM   4513  C   ILE B1049      38.880  41.055  85.540  1.00116.09           C  
ANISOU 4513  C   ILE B1049    14031  14875  15201   -876   3214  -2288       C  
ATOM   4514  O   ILE B1049      39.523  41.267  84.511  1.00106.48           O  
ANISOU 4514  O   ILE B1049    12885  13537  14035   -806   3217  -2321       O  
ATOM   4515  CB  ILE B1049      36.453  40.469  84.994  1.00100.32           C  
ANISOU 4515  CB  ILE B1049    12054  12821  13242   -817   3127  -2099       C  
ATOM   4516  CG1 ILE B1049      36.507  40.860  83.510  1.00103.33           C  
ANISOU 4516  CG1 ILE B1049    12529  13028  13703   -709   3171  -2126       C  
ATOM   4517  CG2 ILE B1049      35.960  41.649  85.802  1.00110.88           C  
ANISOU 4517  CG2 ILE B1049    13347  14240  14541   -869   3279  -2177       C  
ATOM   4518  CD1 ILE B1049      36.742  39.713  82.562  1.00108.39           C  
ANISOU 4518  CD1 ILE B1049    13220  13572  14391   -643   3021  -2037       C  
ATOM   4519  N   GLY B1050      39.050  41.753  86.677  1.00120.52           N  
ANISOU 4519  N   GLY B1050    14542  15546  15703   -951   3251  -2328       N  
ATOM   4520  CA  GLY B1050      40.010  42.842  86.768  1.00116.32           C  
ANISOU 4520  CA  GLY B1050    14049  14982  15165   -949   3247  -2378       C  
ATOM   4521  C   GLY B1050      39.342  44.198  86.979  1.00129.17           C  
ANISOU 4521  C   GLY B1050    15701  16592  16788   -941   3275  -2367       C  
ATOM   4522  O   GLY B1050      39.624  44.866  87.965  1.00153.36           O  
ANISOU 4522  O   GLY B1050    18731  19734  19805   -997   3284  -2395       O  
ATOM   4523  N   ARG B1051      38.464  44.591  86.045  1.00137.59           N  
ANISOU 4523  N   ARG B1051    16825  17552  17902   -870   3286  -2328       N  
ATOM   4524  CA  ARG B1051      37.789  45.878  86.056  1.00141.66           C  
ANISOU 4524  CA  ARG B1051    17369  18035  18418   -853   3309  -2317       C  
ATOM   4525  C   ARG B1051      36.425  45.761  86.740  1.00160.28           C  
ANISOU 4525  C   ARG B1051    19676  20474  20747   -883   3336  -2278       C  
ATOM   4526  O   ARG B1051      36.015  44.684  87.179  1.00172.69           O  
ANISOU 4526  O   ARG B1051    21188  22127  22297   -921   3335  -2252       O  
ATOM   4527  CB  ARG B1051      37.675  46.402  84.621  1.00128.58           C  
ANISOU 4527  CB  ARG B1051    15804  16222  16829   -763   3299  -2296       C  
ATOM   4528  N   ASN B1052      35.727  46.897  86.854  1.00172.01           N  
ANISOU 4528  N   ASN B1052    21181  21943  22229   -871   3356  -2271       N  
ATOM   4529  CA  ASN B1052      34.391  46.907  87.427  1.00170.74           C  
ANISOU 4529  CA  ASN B1052    20979  21850  22043   -892   3379  -2233       C  
ATOM   4530  C   ASN B1052      33.403  46.365  86.398  1.00163.45           C  
ANISOU 4530  C   ASN B1052    20092  20841  21170   -828   3382  -2178       C  
ATOM   4531  O   ASN B1052      33.457  46.751  85.231  1.00186.92           O  
ANISOU 4531  O   ASN B1052    23143  23680  24200   -754   3374  -2172       O  
ATOM   4532  CB  ASN B1052      34.000  48.299  87.924  1.00172.53           C  
ANISOU 4532  CB  ASN B1052    21214  22091  22249   -899   3398  -2248       C  
ATOM   4533  CG  ASN B1052      32.761  48.295  88.794  1.00190.68           C  
ANISOU 4533  CG  ASN B1052    23455  24490  24506   -937   3418  -2217       C  
ATOM   4534  OD1 ASN B1052      32.056  47.292  88.913  1.00218.57           O  
ANISOU 4534  OD1 ASN B1052    26945  28072  28030   -953   3419  -2174       O  
ATOM   4535  ND2 ASN B1052      32.501  49.420  89.448  1.00181.03           N  
ANISOU 4535  ND2 ASN B1052    22226  23303  23256   -954   3433  -2237       N  
ATOM   4536  N   THR B1053      32.499  45.488  86.846  1.00166.70           N  
ANISOU 4536  N   THR B1053    20445  21332  21562   -859   3392  -2134       N  
ATOM   4537  CA  THR B1053      31.679  44.706  85.931  1.00190.97           C  
ANISOU 4537  CA  THR B1053    23542  24333  24684   -804   3393  -2079       C  
ATOM   4538  C   THR B1053      30.441  45.480  85.488  1.00196.32           C  
ANISOU 4538  C   THR B1053    24260  24947  25385   -754   3413  -2047       C  
ATOM   4539  O   THR B1053      30.163  45.564  84.292  1.00192.42           O  
ANISOU 4539  O   THR B1053    23839  24318  24953   -673   3407  -2025       O  
ATOM   4540  CB  THR B1053      31.278  43.355  86.533  1.00192.48           C  
ANISOU 4540  CB  THR B1053    23647  24638  24849   -864   3391  -2036       C  
ATOM   4541  OG1 THR B1053      30.676  43.582  87.810  1.00199.64           O  
ANISOU 4541  OG1 THR B1053    24477  25691  25687   -945   3401  -2024       O  
ATOM   4542  CG2 THR B1053      32.455  42.420  86.643  1.00170.83           C  
ANISOU 4542  CG2 THR B1053    20876  21931  22100   -897   3364  -2060       C  
ATOM   4543  N   ASN B1054      29.687  45.998  86.467  1.00188.34           N  
ANISOU 4543  N   ASN B1054    23199  24037  24324   -803   3431  -2041       N  
ATOM   4544  CA  ASN B1054      28.405  46.636  86.215  1.00168.56           C  
ANISOU 4544  CA  ASN B1054    20718  21496  21831   -767   3450  -2009       C  
ATOM   4545  C   ASN B1054      27.358  45.570  85.901  1.00158.76           C  
ANISOU 4545  C   ASN B1054    19453  20257  20610   -753   3456  -1941       C  
ATOM   4546  O   ASN B1054      26.198  45.731  86.265  1.00161.19           O  
ANISOU 4546  O   ASN B1054    19734  20613  20899   -765   3473  -1906       O  
ATOM   4547  CB  ASN B1054      28.488  47.729  85.139  1.00161.84           C  
ANISOU 4547  CB  ASN B1054    19963  20499  21031   -689   3446  -2027       C  
ATOM   4548  CG  ASN B1054      27.157  48.379  84.817  1.00163.03           C  
ANISOU 4548  CG  ASN B1054    20140  20609  21196   -650   3462  -1996       C  
ATOM   4549  OD1 ASN B1054      26.303  48.518  85.687  1.00179.03           O  
ANISOU 4549  OD1 ASN B1054    22111  22733  23178   -690   3480  -1983       O  
ATOM   4550  ND2 ASN B1054      26.973  48.779  83.570  1.00155.51           N  
ANISOU 4550  ND2 ASN B1054    19269  19514  20303   -572   3451  -1982       N  
ATOM   4551  N   GLY B1055      27.772  44.503  85.202  1.00153.97           N  
ANISOU 4551  N   GLY B1055    18860  19595  20046   -726   3443  -1920       N  
ATOM   4552  CA  GLY B1055      26.876  43.436  84.795  1.00152.22           C  
ANISOU 4552  CA  GLY B1055    18620  19361  19855   -707   3448  -1849       C  
ATOM   4553  C   GLY B1055      27.145  42.950  83.372  1.00149.11           C  
ANISOU 4553  C   GLY B1055    18315  18799  19542   -607   3395  -1814       C  
ATOM   4554  O   GLY B1055      27.098  41.745  83.109  1.00142.88           O  
ANISOU 4554  O   GLY B1055    17532  17990  18765   -592   3244  -1703       O  
ATOM   4555  N   VAL B1056      27.409  43.886  82.447  1.00139.50           N  
ANISOU 4555  N   VAL B1056    17183  17451  18369   -535   3422  -1861       N  
ATOM   4556  CA  VAL B1056      27.643  43.520  81.057  1.00141.53           C  
ANISOU 4556  CA  VAL B1056    17524  17547  18705   -440   3395  -1842       C  
ATOM   4557  C   VAL B1056      29.143  43.309  80.852  1.00131.11           C  
ANISOU 4557  C   VAL B1056    16221  16203  17391   -442   3366  -1891       C  
ATOM   4558  O   VAL B1056      29.943  44.145  81.252  1.00114.49           O  
ANISOU 4558  O   VAL B1056    14119  14132  15252   -477   3362  -1944       O  
ATOM   4559  CB  VAL B1056      27.042  44.527  80.046  1.00149.26           C  
ANISOU 4559  CB  VAL B1056    18591  18393  19726   -363   3385  -1828       C  
ATOM   4560  CG1 VAL B1056      27.254  44.081  78.602  1.00143.32           C  
ANISOU 4560  CG1 VAL B1056    17922  17478  19053   -267   3344  -1796       C  
ATOM   4561  CG2 VAL B1056      25.564  44.799  80.300  1.00142.97           C  
ANISOU 4561  CG2 VAL B1056    17776  17625  18920   -364   3413  -1787       C  
ATOM   4562  N   ILE B1057      29.506  42.178  80.235  1.00139.73           N  
ANISOU 4562  N   ILE B1057    17332  17235  18523   -401   3299  -1845       N  
ATOM   4563  CA  ILE B1057      30.890  41.814  79.962  1.00128.92           C  
ANISOU 4563  CA  ILE B1057    15982  15839  17164   -396   3257  -1883       C  
ATOM   4564  C   ILE B1057      31.051  41.602  78.456  1.00136.91           C  
ANISOU 4564  C   ILE B1057    17087  16674  18258   -287   3226  -1864       C  
ATOM   4565  O   ILE B1057      30.276  40.876  77.840  1.00143.31           O  
ANISOU 4565  O   ILE B1057    17927  17417  19105   -233   3130  -1756       O  
ATOM   4566  CB  ILE B1057      31.290  40.573  80.792  1.00117.56           C  
ANISOU 4566  CB  ILE B1057    14481  14512  15675   -462   3105  -1801       C  
ATOM   4567  CG1 ILE B1057      31.815  40.951  82.181  1.00129.43           C  
ANISOU 4567  CG1 ILE B1057    15901  16175  17100   -569   3160  -1871       C  
ATOM   4568  CG2 ILE B1057      32.283  39.687  80.054  1.00119.93           C  
ANISOU 4568  CG2 ILE B1057    14822  14735  16010   -418   2993  -1773       C  
ATOM   4569  CD1 ILE B1057      30.762  41.413  83.173  1.00148.03           C  
ANISOU 4569  CD1 ILE B1057    18194  18645  19405   -632   3217  -1862       C  
ATOM   4570  N   THR B1058      32.094  42.209  77.881  1.00135.32           N  
ANISOU 4570  N   THR B1058    16937  16406  18072   -263   3227  -1920       N  
ATOM   4571  CA  THR B1058      32.322  42.198  76.442  1.00130.86           C  
ANISOU 4571  CA  THR B1058    16462  15685  17573   -170   3169  -1888       C  
ATOM   4572  C   THR B1058      32.718  40.804  75.947  1.00127.15           C  
ANISOU 4572  C   THR B1058    16003  15157  17152   -119   3122  -1867       C  
ATOM   4573  O   THR B1058      33.056  39.920  76.730  1.00125.81           O  
ANISOU 4573  O   THR B1058    15776  15090  16936   -179   3013  -1814       O  
ATOM   4574  CB  THR B1058      33.360  43.256  76.053  1.00127.87           C  
ANISOU 4574  CB  THR B1058    16123  15279  17180   -176   3142  -1922       C  
ATOM   4575  OG1 THR B1058      34.582  42.910  76.714  1.00141.05           O  
ANISOU 4575  OG1 THR B1058    17751  17024  18816   -228   3140  -1981       O  
ATOM   4576  CG2 THR B1058      32.908  44.659  76.396  1.00110.32           C  
ANISOU 4576  CG2 THR B1058    13901  13093  14923   -210   3175  -1933       C  
ATOM   4577  N   LYS B1059      32.676  40.622  74.622  1.00122.18           N  
ANISOU 4577  N   LYS B1059    15454  14381  16589    -26   3065  -1821       N  
ATOM   4578  CA  LYS B1059      32.977  39.335  74.013  1.00129.99           C  
ANISOU 4578  CA  LYS B1059    16466  15308  17615     24   2928  -1742       C  
ATOM   4579  C   LYS B1059      34.435  38.947  74.252  1.00129.61           C  
ANISOU 4579  C   LYS B1059    16401  15302  17544     -8   2882  -1790       C  
ATOM   4580  O   LYS B1059      34.726  37.765  74.389  1.00128.74           O  
ANISOU 4580  O   LYS B1059    16270  15222  17422    -18   2730  -1707       O  
ATOM   4581  CB  LYS B1059      32.632  39.308  72.520  1.00139.83           C  
ANISOU 4581  CB  LYS B1059    17803  16378  18947    139   2918  -1711       C  
ATOM   4582  CG  LYS B1059      32.870  37.967  71.835  1.00136.71           C  
ANISOU 4582  CG  LYS B1059    17436  15921  18588    192   2743  -1605       C  
ATOM   4583  CD  LYS B1059      32.190  37.841  70.470  1.00121.58           C  
ANISOU 4583  CD  LYS B1059    15601  13842  16754    303   2720  -1548       C  
ATOM   4584  CE  LYS B1059      32.112  36.430  69.913  1.00103.68           C  
ANISOU 4584  CE  LYS B1059    13351  11525  14516    352   2533  -1418       C  
ATOM   4585  NZ  LYS B1059      33.412  35.933  69.395  1.00101.72           N  
ANISOU 4585  NZ  LYS B1059    13128  11234  14287    380   2467  -1445       N  
ATOM   4586  N   ASP B1060      35.336  39.932  74.297  1.00120.78           N  
ANISOU 4586  N   ASP B1060    15289  14192  16409    -30   2980  -1901       N  
ATOM   4587  CA  ASP B1060      36.762  39.688  74.466  1.00105.71           C  
ANISOU 4587  CA  ASP B1060    13369  12317  14481    -58   2951  -1960       C  
ATOM   4588  C   ASP B1060      37.034  39.196  75.882  1.00 93.16           C  
ANISOU 4588  C   ASP B1060    11690  10886  12820   -157   2928  -1968       C  
ATOM   4589  O   ASP B1060      37.805  38.256  76.077  1.00 86.44           O  
ANISOU 4589  O   ASP B1060    10819  10073  11952   -176   2808  -1934       O  
ATOM   4590  CB  ASP B1060      37.601  40.946  74.223  1.00127.86           C  
ANISOU 4590  CB  ASP B1060    16198  15130  17252    -82   2945  -1984       C  
ATOM   4591  CG  ASP B1060      37.376  41.627  72.884  1.00150.93           C  
ANISOU 4591  CG  ASP B1060    19196  17943  20208    -14   2898  -1924       C  
ATOM   4592  OD1 ASP B1060      36.212  41.650  72.426  1.00153.85           O  
ANISOU 4592  OD1 ASP B1060    19592  18256  20609     29   2898  -1865       O  
ATOM   4593  OD2 ASP B1060      38.367  42.143  72.318  1.00167.34           O1-
ANISOU 4593  OD2 ASP B1060    21302  20001  22278     -8   2861  -1934       O1-
ATOM   4594  N   GLU B1061      36.389  39.852  76.857  1.00 93.66           N  
ANISOU 4594  N   GLU B1061    11701  11050  12837   -223   3015  -1993       N  
ATOM   4595  CA  GLU B1061      36.569  39.508  78.258  1.00 96.76           C  
ANISOU 4595  CA  GLU B1061    12006  11608  13151   -327   2977  -1983       C  
ATOM   4596  C   GLU B1061      36.092  38.080  78.522  1.00 89.45           C  
ANISOU 4596  C   GLU B1061    11051  10725  12211   -340   2790  -1837       C  
ATOM   4597  O   GLU B1061      36.708  37.360  79.304  1.00 77.68           O  
ANISOU 4597  O   GLU B1061     9509   9334  10673   -402   2700  -1816       O  
ATOM   4598  CB  GLU B1061      35.835  40.512  79.140  1.00101.38           C  
ANISOU 4598  CB  GLU B1061    12546  12281  13695   -385   3107  -2032       C  
ATOM   4599  CG  GLU B1061      36.419  41.906  79.062  1.00124.64           C  
ANISOU 4599  CG  GLU B1061    15521  15209  16629   -394   3173  -2106       C  
ATOM   4600  CD  GLU B1061      35.753  42.890  80.006  1.00135.14           C  
ANISOU 4600  CD  GLU B1061    16811  16630  17907   -455   3221  -2111       C  
ATOM   4601  OE1 GLU B1061      34.728  42.514  80.586  1.00154.74           O  
ANISOU 4601  OE1 GLU B1061    19244  19177  20371   -482   3253  -2083       O  
ATOM   4602  OE2 GLU B1061      36.242  44.034  80.132  1.00125.76           O1-
ANISOU 4602  OE2 GLU B1061    15641  15445  16697   -475   3222  -2140       O1-
ATOM   4603  N   ALA B1062      35.008  37.675  77.848  1.00 75.33           N  
ANISOU 4603  N   ALA B1062     9298   8859  10466   -279   2732  -1737       N  
ATOM   4604  CA  ALA B1062      34.491  36.323  77.992  1.00 87.79           C  
ANISOU 4604  CA  ALA B1062    10856  10465  12036   -283   2553  -1593       C  
ATOM   4605  C   ALA B1062      35.466  35.269  77.459  1.00100.21           C  
ANISOU 4605  C   ALA B1062    12454  11992  13630   -250   2413  -1556       C  
ATOM   4606  O   ALA B1062      35.631  34.213  78.076  1.00 92.59           O  
ANISOU 4606  O   ALA B1062    11445  11108  12626   -297   2273  -1480       O  
ATOM   4607  CB  ALA B1062      33.150  36.218  77.329  1.00 86.29           C  
ANISOU 4607  CB  ALA B1062    10702  10194  11890   -221   2534  -1504       C  
ATOM   4608  N   GLU B1063      36.102  35.566  76.311  1.00113.30           N  
ANISOU 4608  N   GLU B1063    14183  13519  15347   -170   2449  -1611       N  
ATOM   4609  CA  GLU B1063      37.062  34.665  75.685  1.00107.96           C  
ANISOU 4609  CA  GLU B1063    13536  12787  14696   -129   2327  -1587       C  
ATOM   4610  C   GLU B1063      38.296  34.519  76.573  1.00103.79           C  
ANISOU 4610  C   GLU B1063    12957  12369  14111   -206   2313  -1654       C  
ATOM   4611  O   GLU B1063      38.934  33.461  76.607  1.00 89.09           O  
ANISOU 4611  O   GLU B1063    11086  10526  12240   -211   2171  -1605       O  
ATOM   4612  CB  GLU B1063      37.441  35.153  74.282  1.00102.93           C  
ANISOU 4612  CB  GLU B1063    12985  11989  14135    -28   2388  -1642       C  
ATOM   4613  CG  GLU B1063      36.380  34.899  73.217  1.00110.16           C  
ANISOU 4613  CG  GLU B1063    13960  12778  15116     64   2348  -1552       C  
ATOM   4614  CD  GLU B1063      36.105  33.447  72.838  1.00122.91           C  
ANISOU 4614  CD  GLU B1063    15585  14363  16752    102   2150  -1410       C  
ATOM   4615  OE1 GLU B1063      36.812  32.539  73.350  1.00132.75           O  
ANISOU 4615  OE1 GLU B1063    16794  15683  17962     60   2029  -1379       O  
ATOM   4616  OE2 GLU B1063      35.175  33.214  72.031  1.00114.96           O1-
ANISOU 4616  OE2 GLU B1063    14623  13260  15797    173   2114  -1331       O1-
ATOM   4617  N   LYS B1064      38.608  35.597  77.299  1.00108.72           N  
ANISOU 4617  N   LYS B1064    13547  13066  14696   -267   2462  -1767       N  
ATOM   4618  CA  LYS B1064      39.734  35.585  78.217  1.00108.32           C  
ANISOU 4618  CA  LYS B1064    13445  13125  14587   -345   2467  -1839       C  
ATOM   4619  C   LYS B1064      39.436  34.655  79.390  1.00109.15           C  
ANISOU 4619  C   LYS B1064    13475  13368  14629   -428   2345  -1752       C  
ATOM   4620  O   LYS B1064      40.289  33.847  79.747  1.00 92.95           O  
ANISOU 4620  O   LYS B1064    11399  11368  12550   -460   2239  -1739       O  
ATOM   4621  CB  LYS B1064      40.048  37.007  78.696  1.00119.52           C  
ANISOU 4621  CB  LYS B1064    14847  14585  15982   -387   2660  -1978       C  
ATOM   4622  CG  LYS B1064      41.339  37.175  79.493  1.00117.74           C  
ANISOU 4622  CG  LYS B1064    14577  14453  15704   -457   2689  -2074       C  
ATOM   4623  CD  LYS B1064      42.025  38.544  79.247  1.00125.94           C  
ANISOU 4623  CD  LYS B1064    15642  15455  16754   -449   2871  -2225       C  
ATOM   4624  CE  LYS B1064      42.334  38.842  77.783  1.00123.13           C  
ANISOU 4624  CE  LYS B1064    15374  14936  16473   -347   2905  -2259       C  
ATOM   4625  NZ  LYS B1064      42.313  40.293  77.460  1.00113.59           N  
ANISOU 4625  NZ  LYS B1064    14203  13693  15263   -341   2960  -2268       N  
ATOM   4626  N   LEU B1065      38.234  34.788  79.981  1.00103.54           N  
ANISOU 4626  N   LEU B1065    12729  12717  13895   -463   2363  -1694       N  
ATOM   4627  CA  LEU B1065      37.800  33.946  81.096  1.00 95.65           C  
ANISOU 4627  CA  LEU B1065    11659  11850  12835   -543   2253  -1605       C  
ATOM   4628  C   LEU B1065      37.588  32.509  80.625  1.00 94.16           C  
ANISOU 4628  C   LEU B1065    11489  11620  12668   -505   2055  -1469       C  
ATOM   4629  O   LEU B1065      37.787  31.558  81.386  1.00 91.03           O  
ANISOU 4629  O   LEU B1065    11044  11318  12225   -565   1927  -1406       O  
ATOM   4630  CB  LEU B1065      36.558  34.524  81.789  1.00 90.28           C  
ANISOU 4630  CB  LEU B1065    10938  11239  12125   -587   2331  -1584       C  
ATOM   4631  N   PHE B1066      37.213  32.362  79.348  1.00 91.81           N  
ANISOU 4631  N   PHE B1066    11264  11179  12442   -404   2029  -1426       N  
ATOM   4632  CA  PHE B1066      37.014  31.045  78.769  1.00 83.30           C  
ANISOU 4632  CA  PHE B1066    10211  10046  11393   -356   1845  -1300       C  
ATOM   4633  C   PHE B1066      38.327  30.257  78.727  1.00 89.58           C  
ANISOU 4633  C   PHE B1066    11007  10850  12179   -361   1736  -1314       C  
ATOM   4634  O   PHE B1066      38.348  29.067  79.053  1.00 79.12           O  
ANISOU 4634  O   PHE B1066     9658   9572  10832   -385   1570  -1219       O  
ATOM   4635  CB  PHE B1066      36.328  31.158  77.408  1.00 75.93           C  
ANISOU 4635  CB  PHE B1066     9355   8955  10540   -246   1854  -1259       C  
ATOM   4636  CG  PHE B1066      36.091  29.821  76.755  1.00 79.97           C  
ANISOU 4636  CG  PHE B1066     9896   9403  11085   -190   1666  -1128       C  
ATOM   4637  CD1 PHE B1066      35.348  28.837  77.386  1.00 71.48           C  
ANISOU 4637  CD1 PHE B1066     8779   8405   9976   -233   1530  -1003       C  
ATOM   4638  CD2 PHE B1066      36.614  29.544  75.507  1.00 87.88           C  
ANISOU 4638  CD2 PHE B1066    10968  10271  12152    -95   1622  -1129       C  
ATOM   4639  CE1 PHE B1066      35.137  27.603  76.797  1.00 68.13           C  
ANISOU 4639  CE1 PHE B1066     8382   7923   9581   -182   1353   -881       C  
ATOM   4640  CE2 PHE B1066      36.385  28.319  74.899  1.00 78.04           C  
ANISOU 4640  CE2 PHE B1066     9749   8966  10938    -42   1447  -1007       C  
ATOM   4641  CZ  PHE B1066      35.656  27.346  75.555  1.00 76.62           C  
ANISOU 4641  CZ  PHE B1066     9526   8863  10723    -86   1312   -884       C  
ATOM   4642  N   ASN B1067      39.416  30.928  78.324  1.00 95.60           N  
ANISOU 4642  N   ASN B1067    11797  11568  12959   -339   1829  -1435       N  
ATOM   4643  CA  ASN B1067      40.735  30.319  78.333  1.00 90.93           C  
ANISOU 4643  CA  ASN B1067    11203  10991  12355   -348   1745  -1468       C  
ATOM   4644  C   ASN B1067      41.143  29.919  79.747  1.00 90.01           C  
ANISOU 4644  C   ASN B1067    11007  11036  12158   -459   1695  -1470       C  
ATOM   4645  O   ASN B1067      41.804  28.896  79.927  1.00 83.76           O  
ANISOU 4645  O   ASN B1067    10202  10277  11348   -474   1551  -1430       O  
ATOM   4646  CB  ASN B1067      41.798  31.232  77.724  1.00 94.20           C  
ANISOU 4646  CB  ASN B1067    11657  11337  12797   -312   1871  -1606       C  
ATOM   4647  CG  ASN B1067      41.756  31.210  76.218  1.00 94.64           C  
ANISOU 4647  CG  ASN B1067    11796  11228  12934   -196   1861  -1593       C  
ATOM   4648  OD1 ASN B1067      40.676  31.342  75.650  1.00 99.56           O  
ANISOU 4648  OD1 ASN B1067    12451  11779  13597   -145   1876  -1532       O  
ATOM   4649  ND2 ASN B1067      42.903  30.977  75.593  1.00 87.46           N  
ANISOU 4649  ND2 ASN B1067    10919  10263  12047   -157   1826  -1643       N  
ATOM   4650  N   GLN B1068      40.763  30.750  80.727  1.00 88.53           N  
ANISOU 4650  N   GLN B1068    10768  10947  11923   -533   1815  -1520       N  
ATOM   4651  CA  GLN B1068      41.121  30.505  82.113  1.00 90.73           C  
ANISOU 4651  CA  GLN B1068    10968  11381  12124   -642   1787  -1531       C  
ATOM   4652  C   GLN B1068      40.485  29.185  82.555  1.00 95.77           C  
ANISOU 4652  C   GLN B1068    11575  12076  12736   -671   1602  -1385       C  
ATOM   4653  O   GLN B1068      41.157  28.319  83.141  1.00 98.60           O  
ANISOU 4653  O   GLN B1068    11900  12509  13055   -720   1482  -1361       O  
ATOM   4654  CB  GLN B1068      40.694  31.669  83.010  1.00 92.98           C  
ANISOU 4654  CB  GLN B1068    11206  11754  12367   -708   1953  -1605       C  
ATOM   4655  CG  GLN B1068      41.397  33.003  82.763  1.00106.28           C  
ANISOU 4655  CG  GLN B1068    12912  13402  14066   -695   2138  -1757       C  
ATOM   4656  CD  GLN B1068      40.797  34.139  83.569  1.00118.64           C  
ANISOU 4656  CD  GLN B1068    14435  15045  15596   -752   2296  -1818       C  
ATOM   4657  OE1 GLN B1068      39.964  33.939  84.455  1.00131.81           O  
ANISOU 4657  OE1 GLN B1068    16049  16811  17221   -813   2270  -1756       O  
ATOM   4658  NE2 GLN B1068      41.184  35.367  83.255  1.00109.55           N  
ANISOU 4658  NE2 GLN B1068    13311  13849  14465   -731   2462  -1940       N  
ATOM   4659  N   ASP B1069      39.191  29.040  82.234  1.00 87.41           N  
ANISOU 4659  N   ASP B1069    10530  10979  11701   -639   1580  -1289       N  
ATOM   4660  CA  ASP B1069      38.407  27.907  82.692  1.00 94.03           C  
ANISOU 4660  CA  ASP B1069    11338  11876  12514   -670   1420  -1148       C  
ATOM   4661  C   ASP B1069      38.932  26.607  82.085  1.00 91.35           C  
ANISOU 4661  C   ASP B1069    11030  11480  12199   -625   1232  -1070       C  
ATOM   4662  O   ASP B1069      38.986  25.580  82.763  1.00 81.91           O  
ANISOU 4662  O   ASP B1069     9795  10367  10961   -679   1086   -992       O  
ATOM   4663  CB  ASP B1069      36.919  28.113  82.403  1.00112.46           C  
ANISOU 4663  CB  ASP B1069    13685  14173  14873   -640   1448  -1070       C  
ATOM   4664  CG  ASP B1069      36.326  29.316  83.113  1.00119.86           C  
ANISOU 4664  CG  ASP B1069    14583  15180  15779   -691   1620  -1139       C  
ATOM   4665  OD1 ASP B1069      36.824  29.631  84.210  1.00119.84           O  
ANISOU 4665  OD1 ASP B1069    14520  15299  15715   -780   1669  -1203       O  
ATOM   4666  OD2 ASP B1069      35.380  29.930  82.561  1.00112.25           O1-
ANISOU 4666  OD2 ASP B1069    13650  14148  14853   -642   1703  -1130       O1-
ATOM   4667  N   VAL B1070      39.286  26.653  80.795  1.00 82.57           N  
ANISOU 4667  N   VAL B1070     9990  10226  11157   -524   1233  -1089       N  
ATOM   4668  CA  VAL B1070      39.784  25.476  80.106  1.00 76.28           C  
ANISOU 4668  CA  VAL B1070     9229   9365  10389   -471   1060  -1019       C  
ATOM   4669  C   VAL B1070      41.190  25.101  80.603  1.00 77.79           C  
ANISOU 4669  C   VAL B1070     9394   9620  10541   -517   1007  -1084       C  
ATOM   4670  O   VAL B1070      41.520  23.920  80.748  1.00 79.67           O  
ANISOU 4670  O   VAL B1070     9623   9884  10763   -528    834  -1011       O  
ATOM   4671  CB  VAL B1070      39.696  25.663  78.586  1.00 72.39           C  
ANISOU 4671  CB  VAL B1070     8820   8703   9982   -349   1081  -1020       C  
ATOM   4672  CG1 VAL B1070      40.244  24.460  77.834  1.00 72.58           C  
ANISOU 4672  CG1 VAL B1070     8881   8658  10039   -289    902   -952       C  
ATOM   4673  CG2 VAL B1070      38.271  25.960  78.167  1.00 67.95           C  
ANISOU 4673  CG2 VAL B1070     8279   8084   9454   -308   1123   -949       C  
ATOM   4674  N   ASP B1071      42.026  26.100  80.897  1.00 68.70           N  
ANISOU 4674  N   ASP B1071     8232   8498   9374   -546   1153  -1223       N  
ATOM   4675  CA  ASP B1071      43.352  25.809  81.427  1.00 73.75           C  
ANISOU 4675  CA  ASP B1071     8845   9204   9974   -594   1113  -1291       C  
ATOM   4676  C   ASP B1071      43.228  25.223  82.835  1.00 79.02           C  
ANISOU 4676  C   ASP B1071     9435  10026  10563   -704   1034  -1244       C  
ATOM   4677  O   ASP B1071      44.025  24.359  83.243  1.00 75.09           O  
ANISOU 4677  O   ASP B1071     8916   9582  10033   -738    908  -1231       O  
ATOM   4678  CB  ASP B1071      44.298  27.015  81.346  1.00 69.69           C  
ANISOU 4678  CB  ASP B1071     8339   8677   9462   -595   1288  -1451       C  
ATOM   4679  N   ALA B1072      42.218  25.715  83.576  1.00 82.47           N  
ANISOU 4679  N   ALA B1072     9831  10536  10969   -758   1109  -1221       N  
ATOM   4680  CA  ALA B1072      41.945  25.229  84.921  1.00 69.35           C  
ANISOU 4680  CA  ALA B1072     8094   9022   9233   -864   1044  -1172       C  
ATOM   4681  C   ALA B1072      41.345  23.823  84.866  1.00 67.55           C  
ANISOU 4681  C   ALA B1072     7866   8796   9003   -858    838  -1016       C  
ATOM   4682  O   ALA B1072      41.449  23.078  85.836  1.00 64.67           O  
ANISOU 4682  O   ALA B1072     7449   8542   8580   -937    731   -968       O  
ATOM   4683  CB  ALA B1072      41.075  26.215  85.645  1.00 57.41           C  
ANISOU 4683  CB  ALA B1072     6540   7580   7691   -917   1191  -1199       C  
ATOM   4684  N   ALA B1073      40.758  23.448  83.718  1.00 65.57           N  
ANISOU 4684  N   ALA B1073     7675   8421   8816   -764    778   -939       N  
ATOM   4685  CA  ALA B1073      40.168  22.124  83.569  1.00 73.88           C  
ANISOU 4685  CA  ALA B1073     8733   9464   9872   -750    581   -790       C  
ATOM   4686  C   ALA B1073      41.237  21.058  83.343  1.00 73.03           C  
ANISOU 4686  C   ALA B1073     8641   9342   9765   -734    419   -774       C  
ATOM   4687  O   ALA B1073      41.180  19.960  83.897  1.00 68.15           O  
ANISOU 4687  O   ALA B1073     7994   8791   9110   -780    256   -683       O  
ATOM   4688  CB  ALA B1073      39.160  22.111  82.456  1.00 71.74           C  
ANISOU 4688  CB  ALA B1073     8519   9069   9669   -655    575   -714       C  
ATOM   4689  N   VAL B1074      42.228  21.399  82.528  1.00 74.45           N  
ANISOU 4689  N   VAL B1074     8867   9436   9986   -671    466   -864       N  
ATOM   4690  CA  VAL B1074      43.259  20.425  82.222  1.00 78.46           C  
ANISOU 4690  CA  VAL B1074     9391   9921  10497   -648    316   -855       C  
ATOM   4691  C   VAL B1074      44.143  20.247  83.453  1.00 84.56           C  
ANISOU 4691  C   VAL B1074    10103  10831  11196   -751    293   -910       C  
ATOM   4692  O   VAL B1074      44.644  19.149  83.685  1.00 89.93           O  
ANISOU 4692  O   VAL B1074    10773  11544  11853   -770    126   -859       O  
ATOM   4693  CB  VAL B1074      44.061  20.786  80.955  1.00 68.29           C  
ANISOU 4693  CB  VAL B1074     8170   8500   9275   -549    364   -933       C  
ATOM   4694  CG1 VAL B1074      43.171  20.792  79.734  1.00 71.96           C  
ANISOU 4694  CG1 VAL B1074     8697   8830   9813   -446    361   -863       C  
ATOM   4695  CG2 VAL B1074      44.716  22.144  81.074  1.00 84.58           C  
ANISOU 4695  CG2 VAL B1074    10230  10572  11335   -564    568  -1088       C  
ATOM   4696  N   ARG B1075      44.349  21.330  84.223  1.00 88.76           N  
ANISOU 4696  N   ARG B1075    10595  11438  11691   -815    461  -1017       N  
ATOM   4697  CA  ARG B1075      45.181  21.251  85.417  1.00 89.87           C  
ANISOU 4697  CA  ARG B1075    10676  11709  11761   -914    453  -1076       C  
ATOM   4698  C   ARG B1075      44.510  20.362  86.460  1.00 90.73           C  
ANISOU 4698  C   ARG B1075    10730  11931  11812   -997    324   -964       C  
ATOM   4699  O   ARG B1075      45.218  19.667  87.191  1.00103.59           O  
ANISOU 4699  O   ARG B1075    12325  13643  13393  -1058    220   -963       O  
ATOM   4700  CB  ARG B1075      45.544  22.629  85.979  1.00 84.95           C  
ANISOU 4700  CB  ARG B1075    10024  11138  11115   -961    663  -1215       C  
ATOM   4701  CG  ARG B1075      46.683  23.321  85.248  1.00 82.26           C  
ANISOU 4701  CG  ARG B1075     9725  10721  10810   -906    762  -1345       C  
ATOM   4702  CD  ARG B1075      47.180  24.592  85.909  1.00 82.65           C  
ANISOU 4702  CD  ARG B1075     9741  10834  10829   -961    955  -1484       C  
ATOM   4703  NE  ARG B1075      46.123  25.592  85.972  1.00 93.34           N  
ANISOU 4703  NE  ARG B1075    11090  12184  12192   -963   1102  -1490       N  
ATOM   4704  CZ  ARG B1075      45.901  26.548  85.070  1.00 92.75           C  
ANISOU 4704  CZ  ARG B1075    11063  12006  12172   -892   1238  -1545       C  
ATOM   4705  NH1 ARG B1075      46.717  26.677  84.036  1.00 76.99           N  
ANISOU 4705  NH1 ARG B1075     9124   9903  10224   -815   1252  -1604       N  
ATOM   4706  NH2 ARG B1075      44.892  27.393  85.238  1.00 97.79           N  
ANISOU 4706  NH2 ARG B1075    11691  12653  12813   -901   1361  -1545       N  
ATOM   4707  N   GLY B1076      43.163  20.397  86.511  1.00 75.99           N  
ANISOU 4707  N   GLY B1076     8855  10067   9950   -999    331   -873       N  
ATOM   4708  CA  GLY B1076      42.371  19.552  87.396  1.00 79.50           C  
ANISOU 4708  CA  GLY B1076     9252  10610  10345  -1071    207   -754       C  
ATOM   4709  C   GLY B1076      42.555  18.066  87.091  1.00 81.00           C  
ANISOU 4709  C   GLY B1076     9463  10775  10540  -1048    -22   -645       C  
ATOM   4710  O   GLY B1076      42.753  17.233  87.989  1.00 75.89           O  
ANISOU 4710  O   GLY B1076     8771  10227   9835  -1124   -147   -597       O  
ATOM   4711  N   ILE B1077      42.496  17.757  85.792  1.00 83.57           N  
ANISOU 4711  N   ILE B1077     9855  10962  10935   -940    -75   -607       N  
ATOM   4712  CA  ILE B1077      42.584  16.390  85.316  1.00 83.13           C  
ANISOU 4712  CA  ILE B1077     9828  10863  10896   -901   -289   -500       C  
ATOM   4713  C   ILE B1077      43.960  15.831  85.663  1.00 80.74           C  
ANISOU 4713  C   ILE B1077     9513  10603  10561   -932   -378   -556       C  
ATOM   4714  O   ILE B1077      44.064  14.736  86.187  1.00 77.23           O  
ANISOU 4714  O   ILE B1077     9046  10218  10078   -977   -548   -479       O  
ATOM   4715  CB  ILE B1077      42.285  16.325  83.806  1.00 81.33           C  
ANISOU 4715  CB  ILE B1077     9676  10474  10753   -774   -305   -464       C  
ATOM   4716  CG1 ILE B1077      40.834  16.734  83.527  1.00 72.39           C  
ANISOU 4716  CG1 ILE B1077     8553   9304   9647   -748   -239   -392       C  
ATOM   4717  CG2 ILE B1077      42.656  14.956  83.243  1.00 76.02           C  
ANISOU 4717  CG2 ILE B1077     9036   9749  10100   -726   -523   -376       C  
ATOM   4718  CD1 ILE B1077      40.485  16.863  82.065  1.00 82.07           C  
ANISOU 4718  CD1 ILE B1077     9853  10371  10959   -624   -225   -369       C  
ATOM   4719  N   LEU B1078      45.011  16.595  85.368  1.00 80.15           N  
ANISOU 4719  N   LEU B1078     9455  10498  10503   -908   -262   -692       N  
ATOM   4720  CA  LEU B1078      46.368  16.114  85.575  1.00 88.20           C  
ANISOU 4720  CA  LEU B1078    10468  11545  11497   -927   -340   -755       C  
ATOM   4721  C   LEU B1078      46.706  16.069  87.068  1.00 99.03           C  
ANISOU 4721  C   LEU B1078    11768  13074  12787  -1051   -340   -785       C  
ATOM   4722  O   LEU B1078      47.691  15.426  87.447  1.00 97.30           O  
ANISOU 4722  O   LEU B1078    11535  12899  12535  -1083   -442   -810       O  
ATOM   4723  CB  LEU B1078      47.357  17.002  84.810  1.00 77.56           C  
ANISOU 4723  CB  LEU B1078     9160  10119  10192   -866   -206   -893       C  
ATOM   4724  CG  LEU B1078      47.200  17.035  83.293  1.00 70.84           C  
ANISOU 4724  CG  LEU B1078     8383   9110   9424   -740   -208   -875       C  
ATOM   4725  CD1 LEU B1078      48.119  18.066  82.652  1.00 71.88           C  
ANISOU 4725  CD1 LEU B1078     8547   9176   9589   -692    -53  -1019       C  
ATOM   4726  CD2 LEU B1078      47.490  15.667  82.721  1.00 81.61           C  
ANISOU 4726  CD2 LEU B1078     9778  10423  10806   -690   -426   -785       C  
ATOM   4727  N   ARG B1079      45.899  16.753  87.902  1.00 99.30           N  
ANISOU 4727  N   ARG B1079    12667  13300  11765   -453     -5    504       N  
ATOM   4728  CA  ARG B1079      46.116  16.758  89.345  1.00 93.76           C  
ANISOU 4728  CA  ARG B1079    12015  12579  11031   -472     -5    521       C  
ATOM   4729  C   ARG B1079      45.215  15.734  90.031  1.00 88.49           C  
ANISOU 4729  C   ARG B1079    11380  11943  10300   -601    -41    587       C  
ATOM   4730  O   ARG B1079      45.140  15.735  91.255  1.00105.48           O  
ANISOU 4730  O   ARG B1079    13564  14104  12411   -633    -34    613       O  
ATOM   4731  CB  ARG B1079      45.913  18.143  89.974  1.00 89.03           C  
ANISOU 4731  CB  ARG B1079    11348  12060  10419   -404     90    520       C  
ATOM   4732  N   ASN B1080      44.578  14.857  89.244  1.00 73.29           N  
ANISOU 4732  N   ASN B1080     9451  10031   8366   -673    -83    612       N  
ATOM   4733  CA  ASN B1080      43.695  13.821  89.747  1.00 71.21           C  
ANISOU 4733  CA  ASN B1080     9215   9796   8046   -798   -124    676       C  
ATOM   4734  C   ASN B1080      44.312  12.446  89.481  1.00 71.91           C  
ANISOU 4734  C   ASN B1080     9399   9766   8157   -852   -237    666       C  
ATOM   4735  O   ASN B1080      44.781  12.163  88.394  1.00 82.14           O  
ANISOU 4735  O   ASN B1080    10701  11007   9502   -820   -274    627       O  
ATOM   4736  CB  ASN B1080      42.312  13.976  89.120  1.00 78.29           C  
ANISOU 4736  CB  ASN B1080    10020  10816   8910   -842    -77    720       C  
ATOM   4737  CG  ASN B1080      41.255  13.065  89.701  1.00 91.08           C  
ANISOU 4737  CG  ASN B1080    11653  12485  10466   -970   -104    792       C  
ATOM   4738  OD1 ASN B1080      41.447  11.849  89.782  1.00 83.86           O  
ANISOU 4738  OD1 ASN B1080    10817  11499   9547  -1044   -193    808       O  
ATOM   4739  ND2 ASN B1080      40.134  13.656  90.101  1.00 99.04           N  
ANISOU 4739  ND2 ASN B1080    12585  13619  11427   -997    -29    836       N  
ATOM   4740  N   ALA B1081      44.282  11.572  90.483  1.00 83.83           N  
ANISOU 4740  N   ALA B1081    10983  11239   9630   -938   -294    703       N  
ATOM   4741  CA  ALA B1081      44.898  10.255  90.428  1.00 80.68           C  
ANISOU 4741  CA  ALA B1081    10680  10722   9253   -993   -408    696       C  
ATOM   4742  C   ALA B1081      44.141   9.344  89.473  1.00 88.49           C  
ANISOU 4742  C   ALA B1081    11654  11730  10236  -1066   -454    723       C  
ATOM   4743  O   ALA B1081      44.747   8.441  88.900  1.00 91.00           O  
ANISOU 4743  O   ALA B1081    12031  11950  10595  -1079   -540    695       O  
ATOM   4744  CB  ALA B1081      44.908   9.638  91.806  1.00 87.74           C  
ANISOU 4744  CB  ALA B1081    11649  11587  10102  -1074   -451    738       C  
ATOM   4745  N   LYS B1082      42.821   9.569  89.351  1.00 86.15           N  
ANISOU 4745  N   LYS B1082    11282  11560   9891  -1115   -399    777       N  
ATOM   4746  CA  LYS B1082      41.949   8.693  88.579  1.00 93.39           C  
ANISOU 4746  CA  LYS B1082    12184  12507  10795  -1196   -440    815       C  
ATOM   4747  C   LYS B1082      41.700   9.236  87.164  1.00 94.50           C  
ANISOU 4747  C   LYS B1082    12246  12691  10970  -1135   -399    786       C  
ATOM   4748  O   LYS B1082      41.067   8.543  86.378  1.00 91.98           O  
ANISOU 4748  O   LYS B1082    11913  12388  10646  -1192   -435    809       O  
ATOM   4749  CB  LYS B1082      40.637   8.458  89.338  1.00 92.19           C  
ANISOU 4749  CB  LYS B1082    12003  12459  10566  -1300   -416    897       C  
ATOM   4750  N   LEU B1083      42.180  10.454  86.848  1.00 89.21           N  
ANISOU 4750  N   LEU B1083    11526  12038  10332  -1024   -326    737       N  
ATOM   4751  CA  LEU B1083      41.913  11.099  85.565  1.00 74.70           C  
ANISOU 4751  CA  LEU B1083     9608  10250   8523   -966   -280    713       C  
ATOM   4752  C   LEU B1083      43.164  11.251  84.707  1.00 82.46           C  
ANISOU 4752  C   LEU B1083    10619  11138   9576   -874   -306    635       C  
ATOM   4753  O   LEU B1083      43.027  11.311  83.487  1.00 68.44           O  
ANISOU 4753  O   LEU B1083     8803   9376   7825   -852   -303    615       O  
ATOM   4754  CB  LEU B1083      41.238  12.461  85.750  1.00 68.71           C  
ANISOU 4754  CB  LEU B1083     8751   9611   7745   -917   -169    727       C  
ATOM   4755  CG  LEU B1083      39.821  12.440  86.325  1.00 68.15           C  
ANISOU 4755  CG  LEU B1083     8629   9657   7609  -1002   -129    802       C  
ATOM   4756  CD1 LEU B1083      39.286  13.860  86.486  1.00 58.68           C  
ANISOU 4756  CD1 LEU B1083     7329   8566   6400   -940    -20    804       C  
ATOM   4757  CD2 LEU B1083      38.905  11.632  85.416  1.00 62.31           C  
ANISOU 4757  CD2 LEU B1083     7866   8950   6858  -1079   -166    839       C  
ATOM   4758  N   LYS B1084      44.353  11.335  85.331  1.00 95.98           N  
ANISOU 4758  N   LYS B1084    12395  12756  11317   -823   -328    592       N  
ATOM   4759  CA  LYS B1084      45.600  11.556  84.606  1.00 92.41           C  
ANISOU 4759  CA  LYS B1084    11966  12212  10931   -731   -347    514       C  
ATOM   4760  C   LYS B1084      45.974  10.348  83.746  1.00 93.75           C  
ANISOU 4760  C   LYS B1084    12192  12296  11133   -770   -441    490       C  
ATOM   4761  O   LYS B1084      46.247  10.523  82.559  1.00109.54           O  
ANISOU 4761  O   LYS B1084    14163  14286  13171   -721   -437    447       O  
ATOM   4762  CB  LYS B1084      46.770  11.958  85.507  1.00 97.02           C  
ANISOU 4762  CB  LYS B1084    12604  12717  11542   -667   -348    475       C  
ATOM   4763  CG  LYS B1084      48.069  12.249  84.757  1.00 99.51           C  
ANISOU 4763  CG  LYS B1084    12939  12941  11929   -568   -362    394       C  
ATOM   4764  CD  LYS B1084      49.307  12.383  85.615  1.00113.27           C  
ANISOU 4764  CD  LYS B1084    14751  14582  13704   -516   -385    354       C  
ATOM   4765  CE  LYS B1084      49.791  11.083  86.240  1.00119.94           C  
ANISOU 4765  CE  LYS B1084    15701  15319  14553   -587   -488    358       C  
ATOM   4766  NZ  LYS B1084      49.981   9.982  85.266  1.00104.94           N  
ANISOU 4766  NZ  LYS B1084    13835  13353  12684   -625   -570    334       N  
ATOM   4767  N   PRO B1085      46.005   9.100  84.280  1.00 83.86           N  
ANISOU 4767  N   PRO B1085    11018  10977   9867   -858   -530    514       N  
ATOM   4768  CA  PRO B1085      46.345   7.926  83.470  1.00 81.33           C  
ANISOU 4768  CA  PRO B1085    10749  10573   9579   -895   -624    488       C  
ATOM   4769  C   PRO B1085      45.453   7.707  82.249  1.00 83.75           C  
ANISOU 4769  C   PRO B1085    10997  10945   9877   -926   -618    505       C  
ATOM   4770  O   PRO B1085      45.956   7.304  81.195  1.00 71.62           O  
ANISOU 4770  O   PRO B1085     9474   9353   8384   -903   -659    455       O  
ATOM   4771  CB  PRO B1085      46.231   6.749  84.442  1.00 79.54           C  
ANISOU 4771  CB  PRO B1085    10603  10292   9326   -997   -709    531       C  
ATOM   4772  CG  PRO B1085      45.377   7.271  85.560  1.00 81.42           C  
ANISOU 4772  CG  PRO B1085    10810  10626   9500  -1035   -648    597       C  
ATOM   4773  CD  PRO B1085      45.725   8.741  85.677  1.00 82.37           C  
ANISOU 4773  CD  PRO B1085    10874  10791   9633   -927   -548    565       C  
ATOM   4774  N   VAL B1086      44.147   8.009  82.390  1.00 81.37           N  
ANISOU 4774  N   VAL B1086    10631  10765   9521   -976   -565    572       N  
ATOM   4775  CA  VAL B1086      43.210   7.850  81.288  1.00 70.65           C  
ANISOU 4775  CA  VAL B1086     9215   9477   8153  -1009   -556    594       C  
ATOM   4776  C   VAL B1086      43.366   9.007  80.304  1.00 75.82           C  
ANISOU 4776  C   VAL B1086     9794  10178   8836   -912   -480    552       C  
ATOM   4777  O   VAL B1086      43.327   8.782  79.097  1.00 72.79           O  
ANISOU 4777  O   VAL B1086     9392   9790   8476   -904   -498    528       O  
ATOM   4778  CB  VAL B1086      41.763   7.677  81.775  1.00 66.50           C  
ANISOU 4778  CB  VAL B1086     8649   9057   7563  -1102   -533    681       C  
ATOM   4779  CG1 VAL B1086      41.371   8.796  82.683  1.00 84.70           C  
ANISOU 4779  CG1 VAL B1086    10900  11447   9834  -1073   -440    708       C  
ATOM   4780  CG2 VAL B1086      40.752   7.601  80.649  1.00 71.41           C  
ANISOU 4780  CG2 VAL B1086     9204   9754   8174  -1133   -520    706       C  
ATOM   4781  N   TYR B1087      43.566  10.237  80.814  1.00 74.17           N  
ANISOU 4781  N   TYR B1087     9543  10011   8627   -838   -398    542       N  
ATOM   4782  CA  TYR B1087      43.757  11.398  79.947  1.00 68.24           C  
ANISOU 4782  CA  TYR B1087     8720   9303   7905   -743   -327    503       C  
ATOM   4783  C   TYR B1087      45.036  11.274  79.129  1.00 60.20           C  
ANISOU 4783  C   TYR B1087     7742   8184   6948   -674   -365    423       C  
ATOM   4784  O   TYR B1087      45.057  11.599  77.952  1.00 68.59           O  
ANISOU 4784  O   TYR B1087     8761   9265   8033   -636   -347    394       O  
ATOM   4785  CB  TYR B1087      43.805  12.701  80.735  1.00 66.51           C  
ANISOU 4785  CB  TYR B1087     8454   9139   7678   -676   -240    506       C  
ATOM   4786  CG  TYR B1087      44.097  13.945  79.931  1.00 67.52           C  
ANISOU 4786  CG  TYR B1087     8511   9304   7840   -575   -171    465       C  
ATOM   4787  CD1 TYR B1087      43.070  14.686  79.378  1.00 75.15           C  
ANISOU 4787  CD1 TYR B1087     9381  10382   8788   -573   -106    496       C  
ATOM   4788  CD2 TYR B1087      45.384  14.428  79.768  1.00 64.90           C  
ANISOU 4788  CD2 TYR B1087     8205   8897   7558   -481   -168    397       C  
ATOM   4789  CE1 TYR B1087      43.301  15.862  78.681  1.00 71.56           C  
ANISOU 4789  CE1 TYR B1087     8860   9965   8364   -483    -44    463       C  
ATOM   4790  CE2 TYR B1087      45.635  15.607  79.085  1.00 59.97           C  
ANISOU 4790  CE2 TYR B1087     7513   8309   6962   -390   -104    364       C  
ATOM   4791  CZ  TYR B1087      44.589  16.321  78.534  1.00 62.95           C  
ANISOU 4791  CZ  TYR B1087     7798   8800   7322   -392    -44    397       C  
ATOM   4792  OH  TYR B1087      44.772  17.458  77.813  1.00 73.22           O  
ANISOU 4792  OH  TYR B1087     9030  10140   8650   -309     14    369       O  
ATOM   4793  N   ASP B1088      46.093  10.770  79.749  1.00 61.16           N  
ANISOU 4793  N   ASP B1088     7946   8196   7095   -662   -420    387       N  
ATOM   4794  CA  ASP B1088      47.361  10.633  79.057  1.00 80.94           C  
ANISOU 4794  CA  ASP B1088    10492  10601   9662   -596   -457    308       C  
ATOM   4795  C   ASP B1088      47.269   9.573  77.971  1.00 76.50           C  
ANISOU 4795  C   ASP B1088     9951  10001   9113   -644   -527    291       C  
ATOM   4796  O   ASP B1088      48.061   9.606  77.035  1.00 83.02           O  
ANISOU 4796  O   ASP B1088    10784  10776   9984   -589   -540    227       O  
ATOM   4797  CB  ASP B1088      48.519  10.380  80.031  1.00 91.38           C  
ANISOU 4797  CB  ASP B1088    11896  11813  11012   -570   -499    274       C  
ATOM   4798  CG  ASP B1088      48.843  11.607  80.876  1.00106.08           C  
ANISOU 4798  CG  ASP B1088    13731  13702  12872   -496   -424    271       C  
ATOM   4799  OD1 ASP B1088      48.374  12.706  80.531  1.00124.33           O  
ANISOU 4799  OD1 ASP B1088    15960  16106  15173   -448   -340    280       O  
ATOM   4800  OD2 ASP B1088      49.542  11.460  81.875  1.00112.88           O1-
ANISOU 4800  OD2 ASP B1088    14654  14493  13743   -488   -450    261       O1-
ATOM   4801  N   SER B1089      46.334   8.629  78.123  1.00 74.54           N  
ANISOU 4801  N   SER B1089     9718   9777   8826   -747   -573    349       N  
ATOM   4802  CA  SER B1089      46.191   7.546  77.161  1.00 85.39           C  
ANISOU 4802  CA  SER B1089    11117  11115  10212   -800   -646    337       C  
ATOM   4803  C   SER B1089      45.231   7.923  76.027  1.00 86.08           C  
ANISOU 4803  C   SER B1089    11124  11302  10282   -807   -601    359       C  
ATOM   4804  O   SER B1089      45.285   7.324  74.953  1.00 82.04           O  
ANISOU 4804  O   SER B1089    10619  10764   9787   -822   -644    331       O  
ATOM   4805  CB  SER B1089      45.766   6.280  77.840  1.00 91.75           C  
ANISOU 4805  CB  SER B1089    11984  11885  10992   -906   -729    385       C  
ATOM   4806  OG  SER B1089      44.496   6.461  78.449  1.00101.49           O  
ANISOU 4806  OG  SER B1089    13174  13222  12165   -970   -689    468       O  
ATOM   4807  N   LEU B1090      44.336   8.891  76.275  1.00 79.00           N  
ANISOU 4807  N   LEU B1090    10151  10518   9349   -801   -517    408       N  
ATOM   4808  CA  LEU B1090      43.355   9.286  75.278  1.00 72.07           C  
ANISOU 4808  CA  LEU B1090     9193   9737   8453   -812   -474    434       C  
ATOM   4809  C   LEU B1090      44.030  10.107  74.181  1.00 79.27           C  
ANISOU 4809  C   LEU B1090    10068  10645   9405   -718   -435    370       C  
ATOM   4810  O   LEU B1090      45.005  10.818  74.431  1.00 90.28           O  
ANISOU 4810  O   LEU B1090    11470  12002  10831   -635   -405    322       O  
ATOM   4811  CB  LEU B1090      42.214  10.059  75.948  1.00 67.95           C  
ANISOU 4811  CB  LEU B1090     8600   9331   7884   -833   -399    504       C  
ATOM   4812  CG  LEU B1090      41.217   9.220  76.759  1.00 72.41           C  
ANISOU 4812  CG  LEU B1090     9185   9928   8401   -943   -433    579       C  
ATOM   4813  CD1 LEU B1090      40.134  10.084  77.388  1.00 62.50           C  
ANISOU 4813  CD1 LEU B1090     7853   8792   7103   -956   -351    640       C  
ATOM   4814  CD2 LEU B1090      40.586   8.109  75.926  1.00 75.30           C  
ANISOU 4814  CD2 LEU B1090     9563  10288   8757  -1024   -500    602       C  
ATOM   4815  N   ASP B1091      43.492   9.999  72.956  1.00 76.59           N  
ANISOU 4815  N   ASP B1091     9689  10347   9065   -735   -436    371       N  
ATOM   4816  CA  ASP B1091      43.900  10.818  71.821  1.00 62.92           C  
ANISOU 4816  CA  ASP B1091     7911   8634   7363   -659   -394    322       C  
ATOM   4817  C   ASP B1091      43.383  12.240  72.020  1.00 69.33           C  
ANISOU 4817  C   ASP B1091     8635   9545   8161   -610   -297    351       C  
ATOM   4818  O   ASP B1091      42.539  12.490  72.886  1.00 90.00           O  
ANISOU 4818  O   ASP B1091    11224  12228  10745   -645   -264    411       O  
ATOM   4819  CB  ASP B1091      43.383  10.228  70.517  1.00 62.10           C  
ANISOU 4819  CB  ASP B1091     7793   8548   7256   -703   -427    322       C  
ATOM   4820  CG  ASP B1091      41.932   9.783  70.639  1.00 78.48           C  
ANISOU 4820  CG  ASP B1091     9837  10699   9283   -797   -434    404       C  
ATOM   4821  OD1 ASP B1091      41.037  10.629  70.411  1.00 70.60           O1-
ANISOU 4821  OD1 ASP B1091     8758   9801   8265   -794   -369    445       O1-
ATOM   4822  OD2 ASP B1091      41.703   8.598  70.987  1.00 90.59           O  
ANISOU 4822  OD2 ASP B1091    11426  12190  10803   -875   -507    428       O  
ATOM   4823  N   ALA B1092      43.877  13.170  71.189  1.00 65.09           N  
ANISOU 4823  N   ALA B1092     8055   9023   7653   -530   -251    306       N  
ATOM   4824  CA  ALA B1092      43.552  14.584  71.319  1.00 57.10           C  
ANISOU 4824  CA  ALA B1092     6962   8096   6639   -471   -163    323       C  
ATOM   4825  C   ALA B1092      42.040  14.801  71.254  1.00 66.64           C  
ANISOU 4825  C   ALA B1092     8098   9415   7807   -531   -130    397       C  
ATOM   4826  O   ALA B1092      41.527  15.659  71.956  1.00 75.87           O  
ANISOU 4826  O   ALA B1092     9214  10653   8962   -514    -69    432       O  
ATOM   4827  CB  ALA B1092      44.264  15.379  70.256  1.00 49.41           C  
ANISOU 4827  CB  ALA B1092     5956   7118   5701   -389   -133    266       C  
ATOM   4828  N   VAL B1093      41.331  14.014  70.426  1.00 67.10           N  
ANISOU 4828  N   VAL B1093     8155   9491   7850   -601   -170    421       N  
ATOM   4829  CA  VAL B1093      39.902  14.173  70.257  1.00 62.00           C  
ANISOU 4829  CA  VAL B1093     7441   8946   7171   -660   -143    489       C  
ATOM   4830  C   VAL B1093      39.187  13.704  71.517  1.00 65.30           C  
ANISOU 4830  C   VAL B1093     7873   9386   7550   -728   -150    549       C  
ATOM   4831  O   VAL B1093      38.386  14.448  72.070  1.00 60.39           O  
ANISOU 4831  O   VAL B1093     7188   8848   6908   -731    -91    594       O  
ATOM   4832  CB  VAL B1093      39.375  13.448  69.008  1.00 66.88           C  
ANISOU 4832  CB  VAL B1093     8056   9572   7783   -715   -188    497       C  
ATOM   4833  CG1 VAL B1093      37.887  13.739  68.788  1.00 67.75           C  
ANISOU 4833  CG1 VAL B1093     8088   9789   7863   -769   -154    568       C  
ATOM   4834  CG2 VAL B1093      40.187  13.816  67.778  1.00 67.20           C  
ANISOU 4834  CG2 VAL B1093     8092   9583   7858   -651   -186    432       C  
ATOM   4835  N   ARG B1094      39.493  12.480  71.966  1.00 69.90           N  
ANISOU 4835  N   ARG B1094     8540   9893   8126   -783   -224    549       N  
ATOM   4836  CA  ARG B1094      38.855  11.927  73.153  1.00 66.97           C  
ANISOU 4836  CA  ARG B1094     8190   9538   7716   -856   -238    606       C  
ATOM   4837  C   ARG B1094      39.348  12.617  74.419  1.00 69.68           C  
ANISOU 4837  C   ARG B1094     8540   9876   8058   -809   -195    600       C  
ATOM   4838  O   ARG B1094      38.700  12.498  75.447  1.00 79.67           O  
ANISOU 4838  O   ARG B1094     9802  11180   9287   -859   -183    652       O  
ATOM   4839  CB  ARG B1094      39.068  10.417  73.242  1.00 72.77           C  
ANISOU 4839  CB  ARG B1094     9013  10189   8446   -930   -336    607       C  
ATOM   4840  CG  ARG B1094      38.150   9.631  72.311  1.00 85.25           C  
ANISOU 4840  CG  ARG B1094    10580  11799  10011  -1007   -378    642       C  
ATOM   4841  CD  ARG B1094      38.317   8.125  72.402  1.00 73.21           C  
ANISOU 4841  CD  ARG B1094     9141  10193   8483  -1082   -479    645       C  
ATOM   4842  NE  ARG B1094      39.196   7.613  71.369  1.00 74.13           N  
ANISOU 4842  NE  ARG B1094     9301  10228   8638  -1053   -533    577       N  
ATOM   4843  CZ  ARG B1094      38.772   6.974  70.295  1.00 77.35           C  
ANISOU 4843  CZ  ARG B1094     9706  10638   9046  -1095   -575    580       C  
ATOM   4844  NH1 ARG B1094      37.479   6.764  70.126  1.00 77.00           N  
ANISOU 4844  NH1 ARG B1094     9618  10671   8968  -1167   -572    648       N  
ATOM   4845  NH2 ARG B1094      39.647   6.523  69.416  1.00 75.96           N  
ANISOU 4845  NH2 ARG B1094     9571  10386   8905  -1066   -622    512       N  
ATOM   4846  N   ARG B1095      40.481  13.326  74.352  1.00 69.22           N  
ANISOU 4846  N   ARG B1095     8493   9771   8038   -714   -171    538       N  
ATOM   4847  CA  ARG B1095      40.908  14.173  75.453  1.00 64.03           C  
ANISOU 4847  CA  ARG B1095     7828   9118   7381   -658   -120    531       C  
ATOM   4848  C   ARG B1095      39.953  15.351  75.605  1.00 61.35           C  
ANISOU 4848  C   ARG B1095     7389   8898   7025   -639    -33    571       C  
ATOM   4849  O   ARG B1095      39.561  15.668  76.723  1.00 64.57           O  
ANISOU 4849  O   ARG B1095     7783   9345   7405   -652      2    605       O  
ATOM   4850  CB  ARG B1095      42.328  14.702  75.248  1.00 68.16           C  
ANISOU 4850  CB  ARG B1095     8379   9564   7952   -557   -115    456       C  
ATOM   4851  CG  ARG B1095      43.434  13.719  75.590  1.00 63.09           C  
ANISOU 4851  CG  ARG B1095     7841   8799   7333   -563   -191    414       C  
ATOM   4852  CD  ARG B1095      44.752  14.440  75.423  1.00 69.51           C  
ANISOU 4852  CD  ARG B1095     8666   9550   8193   -457   -172    342       C  
ATOM   4853  NE  ARG B1095      45.886  13.586  75.723  1.00 71.43           N  
ANISOU 4853  NE  ARG B1095     9005   9671   8466   -453   -243    295       N  
ATOM   4854  CZ  ARG B1095      47.145  13.982  75.655  1.00 75.47           C  
ANISOU 4854  CZ  ARG B1095     9543  10109   9022   -369   -241    229       C  
ATOM   4855  NH1 ARG B1095      47.420  15.227  75.298  1.00 71.92           N  
ANISOU 4855  NH1 ARG B1095     9034   9700   8594   -283   -172    205       N  
ATOM   4856  NH2 ARG B1095      48.111  13.135  75.968  1.00 83.23           N  
ANISOU 4856  NH2 ARG B1095    10613  10979  10032   -373   -310    190       N  
ATOM   4857  N   ALA B1096      39.579  15.980  74.483  1.00 61.96           N  
ANISOU 4857  N   ALA B1096     7397   9029   7117   -610     -1    565       N  
ATOM   4858  CA  ALA B1096      38.645  17.101  74.500  1.00 67.45           C  
ANISOU 4858  CA  ALA B1096     7991   9834   7802   -592     77    601       C  
ATOM   4859  C   ALA B1096      37.285  16.665  75.038  1.00 60.17           C  
ANISOU 4859  C   ALA B1096     7041   8988   6834   -686     82    674       C  
ATOM   4860  O   ALA B1096      36.626  17.461  75.695  1.00 62.10           O  
ANISOU 4860  O   ALA B1096     7223   9311   7063   -679    144    705       O  
ATOM   4861  CB  ALA B1096      38.532  17.744  73.134  1.00 66.46           C  
ANISOU 4861  CB  ALA B1096     7804   9744   7703   -551     99    582       C  
ATOM   4862  N   ALA B1097      36.896  15.405  74.787  1.00 57.98           N  
ANISOU 4862  N   ALA B1097     6810   8684   6536   -774     15    701       N  
ATOM   4863  CA  ALA B1097      35.668  14.852  75.352  1.00 64.34           C  
ANISOU 4863  CA  ALA B1097     7600   9552   7297   -871     11    772       C  
ATOM   4864  C   ALA B1097      35.769  14.755  76.874  1.00 61.31           C  
ANISOU 4864  C   ALA B1097     7250   9161   6883   -890     21    791       C  
ATOM   4865  O   ALA B1097      34.806  15.036  77.572  1.00 59.90           O  
ANISOU 4865  O   ALA B1097     7022   9065   6671   -929     64    841       O  
ATOM   4866  CB  ALA B1097      35.306  13.527  74.735  1.00 56.37           C  
ANISOU 4866  CB  ALA B1097     6634   8508   6274   -956    -68    794       C  
ATOM   4867  N   LEU B1098      36.949  14.384  77.376  1.00 68.42           N  
ANISOU 4867  N   LEU B1098     8234   9965   7798   -861    -18    749       N  
ATOM   4868  CA  LEU B1098      37.182  14.276  78.808  1.00 65.50           C  
ANISOU 4868  CA  LEU B1098     7907   9578   7403   -876    -15    762       C  
ATOM   4869  C   LEU B1098      37.249  15.654  79.458  1.00 66.31           C  
ANISOU 4869  C   LEU B1098     7949   9736   7509   -800     73    752       C  
ATOM   4870  O   LEU B1098      36.727  15.819  80.563  1.00 64.17           O  
ANISOU 4870  O   LEU B1098     7666   9515   7201   -832    106    789       O  
ATOM   4871  CB  LEU B1098      38.450  13.463  79.080  1.00 64.31           C  
ANISOU 4871  CB  LEU B1098     7864   9299   7272   -867    -88    718       C  
ATOM   4872  CG  LEU B1098      38.590  13.055  80.543  1.00 70.29           C  
ANISOU 4872  CG  LEU B1098     8679  10032   7997   -908   -104    743       C  
ATOM   4873  CD1 LEU B1098      37.386  12.254  80.983  1.00 69.93           C  
ANISOU 4873  CD1 LEU B1098     8629  10042   7898  -1024   -125    817       C  
ATOM   4874  CD2 LEU B1098      39.868  12.268  80.783  1.00 77.59           C  
ANISOU 4874  CD2 LEU B1098     9708  10824   8948   -897   -181    697       C  
ATOM   4875  N   ILE B1099      37.881  16.620  78.772  1.00 62.16           N  
ANISOU 4875  N   ILE B1099     7388   9204   7027   -702    109    702       N  
ATOM   4876  CA  ILE B1099      37.918  17.999  79.243  1.00 66.94           C  
ANISOU 4876  CA  ILE B1099     7927   9864   7641   -624    191    690       C  
ATOM   4877  C   ILE B1099      36.509  18.571  79.268  1.00 68.07           C  
ANISOU 4877  C   ILE B1099     7972  10132   7759   -659    250    743       C  
ATOM   4878  O   ILE B1099      36.190  19.332  80.174  1.00 71.35           O  
ANISOU 4878  O   ILE B1099     8346  10606   8160   -639    310    756       O  
ATOM   4879  CB  ILE B1099      38.842  18.902  78.400  1.00 75.11           C  
ANISOU 4879  CB  ILE B1099     8940  10869   8730   -517    212    628       C  
ATOM   4880  CG1 ILE B1099      40.269  18.355  78.343  1.00 73.10           C  
ANISOU 4880  CG1 ILE B1099     8781  10489   8506   -480    154    572       C  
ATOM   4881  CG2 ILE B1099      38.825  20.340  78.913  1.00 67.72           C  
ANISOU 4881  CG2 ILE B1099     7933   9993   7806   -438    294    619       C  
ATOM   4882  CD1 ILE B1099      41.093  18.977  77.256  1.00 65.57           C  
ANISOU 4882  CD1 ILE B1099     7808   9502   7602   -393    162    514       C  
ATOM   4883  N   ASN B1100      35.687  18.193  78.278  1.00 74.87           N  
ANISOU 4883  N   ASN B1100     8797  11032   8618   -709    233    770       N  
ATOM   4884  CA  ASN B1100      34.330  18.706  78.147  1.00 71.29           C  
ANISOU 4884  CA  ASN B1100     8247  10693   8147   -742    285    819       C  
ATOM   4885  C   ASN B1100      33.530  18.367  79.399  1.00 72.97           C  
ANISOU 4885  C   ASN B1100     8459  10957   8308   -816    301    871       C  
ATOM   4886  O   ASN B1100      32.824  19.232  79.903  1.00 85.54           O  
ANISOU 4886  O   ASN B1100     9974  12637   9890   -804    370    891       O  
ATOM   4887  CB  ASN B1100      33.612  18.213  76.891  1.00 65.19           C  
ANISOU 4887  CB  ASN B1100     7447   9942   7378   -792    254    842       C  
ATOM   4888  CG  ASN B1100      32.288  18.924  76.682  1.00 79.52           C  
ANISOU 4888  CG  ASN B1100     9153  11874   9186   -812    312    886       C  
ATOM   4889  OD1 ASN B1100      31.320  18.712  77.423  1.00 85.01           O  
ANISOU 4889  OD1 ASN B1100     9822  12632   9844   -878    331    937       O  
ATOM   4890  ND2 ASN B1100      32.224  19.773  75.672  1.00 80.96           N  
ANISOU 4890  ND2 ASN B1100     9270  12086   9405   -756    340    867       N  
ATOM   4891  N   MET B1101      33.646  17.118  79.881  1.00 67.20           N  
ANISOU 4891  N   MET B1101     7813  10172   7547   -893    237    892       N  
ATOM   4892  CA  MET B1101      32.909  16.673  81.051  1.00 64.86           C  
ANISOU 4892  CA  MET B1101     7525   9920   7198   -973    244    944       C  
ATOM   4893  C   MET B1101      33.389  17.433  82.289  1.00 71.59           C  
ANISOU 4893  C   MET B1101     8381  10780   8041   -923    295    926       C  
ATOM   4894  O   MET B1101      32.580  17.875  83.099  1.00 76.18           O  
ANISOU 4894  O   MET B1101     8909  11446   8590   -948    351    959       O  
ATOM   4895  CB  MET B1101      33.087  15.177  81.286  1.00 61.54           C  
ANISOU 4895  CB  MET B1101     7203   9427   6752  -1061    156    966       C  
ATOM   4896  CG  MET B1101      32.476  14.330  80.225  1.00 71.61           C  
ANISOU 4896  CG  MET B1101     8477  10703   8030  -1125    104    993       C  
ATOM   4897  SD  MET B1101      32.709  12.566  80.558  1.00 89.72           S  
ANISOU 4897  SD  MET B1101    10886  12907  10296  -1227     -6   1018       S  
ATOM   4898  CE  MET B1101      31.732  12.373  82.046  1.00 87.08           C  
ANISOU 4898  CE  MET B1101    10540  12651   9896  -1316     24   1087       C  
ATOM   4899  N   VAL B1102      34.708  17.578  82.447  1.00 64.75           N  
ANISOU 4899  N   VAL B1102     7576   9822   7203   -852    276    871       N  
ATOM   4900  CA  VAL B1102      35.237  18.271  83.605  1.00 67.59           C  
ANISOU 4900  CA  VAL B1102     7946  10180   7555   -801    318    852       C  
ATOM   4901  C   VAL B1102      34.788  19.729  83.578  1.00 72.38           C  
ANISOU 4901  C   VAL B1102     8444  10878   8177   -731    409    843       C  
ATOM   4902  O   VAL B1102      34.567  20.325  84.626  1.00 79.35           O  
ANISOU 4902  O   VAL B1102     9301  11811   9036   -720    462    851       O  
ATOM   4903  CB  VAL B1102      36.765  18.108  83.679  1.00 73.17           C  
ANISOU 4903  CB  VAL B1102     8740  10765   8295   -738    274    794       C  
ATOM   4904  CG1 VAL B1102      37.423  18.972  84.737  1.00 65.20           C  
ANISOU 4904  CG1 VAL B1102     7738   9748   7288   -669    320    767       C  
ATOM   4905  CG2 VAL B1102      37.149  16.651  83.864  1.00 77.82           C  
ANISOU 4905  CG2 VAL B1102     9435  11266   8869   -815    182    805       C  
ATOM   4906  N   PHE B1103      34.624  20.296  82.378  1.00 68.31           N  
ANISOU 4906  N   PHE B1103     7866  10388   7702   -685    426    827       N  
ATOM   4907  CA  PHE B1103      34.179  21.674  82.261  1.00 67.64           C  
ANISOU 4907  CA  PHE B1103     7676  10387   7638   -619    505    819       C  
ATOM   4908  C   PHE B1103      32.728  21.821  82.731  1.00 72.06           C  
ANISOU 4908  C   PHE B1103     8158  11063   8160   -686    553    874       C  
ATOM   4909  O   PHE B1103      32.369  22.839  83.311  1.00 83.86           O  
ANISOU 4909  O   PHE B1103     9582  12626   9653   -647    622    872       O  
ATOM   4910  CB  PHE B1103      34.367  22.190  80.841  1.00 58.47           C  
ANISOU 4910  CB  PHE B1103     6469   9220   6527   -561    504    791       C  
ATOM   4911  CG  PHE B1103      34.296  23.686  80.738  1.00 55.39           C  
ANISOU 4911  CG  PHE B1103     5986   8890   6171   -471    576    768       C  
ATOM   4912  CD1 PHE B1103      33.088  24.360  80.627  1.00 61.70           C  
ANISOU 4912  CD1 PHE B1103     6680   9797   6967   -487    630    801       C  
ATOM   4913  CD2 PHE B1103      35.449  24.434  80.768  1.00 60.27           C  
ANISOU 4913  CD2 PHE B1103     6620   9454   6826   -371    588    714       C  
ATOM   4914  CE1 PHE B1103      33.041  25.749  80.526  1.00 66.23           C  
ANISOU 4914  CE1 PHE B1103     7167  10423   7576   -403    692    778       C  
ATOM   4915  CE2 PHE B1103      35.402  25.820  80.672  1.00 62.80           C  
ANISOU 4915  CE2 PHE B1103     6854   9827   7180   -288    650    694       C  
ATOM   4916  CZ  PHE B1103      34.205  26.480  80.543  1.00 60.49           C  
ANISOU 4916  CZ  PHE B1103     6457   9640   6885   -303    700    725       C  
ATOM   4917  N   GLN B1104      31.898  20.804  82.496  1.00 69.57           N  
ANISOU 4917  N   GLN B1104     7855  10767   7813   -787    515    923       N  
ATOM   4918  CA  GLN B1104      30.502  20.843  82.918  1.00 79.46           C  
ANISOU 4918  CA  GLN B1104     9037  12126   9029   -858    556    977       C  
ATOM   4919  C   GLN B1104      30.344  20.451  84.393  1.00 84.07           C  
ANISOU 4919  C   GLN B1104     9659  12725   9557   -914    567   1003       C  
ATOM   4920  O   GLN B1104      29.753  21.198  85.174  1.00 81.68           O  
ANISOU 4920  O   GLN B1104     9292  12505   9236   -907    635   1013       O  
ATOM   4921  CB  GLN B1104      29.624  19.976  82.015  1.00 72.55           C  
ANISOU 4921  CB  GLN B1104     8151  11270   8146   -942    514   1021       C  
ATOM   4922  CG  GLN B1104      28.157  20.093  82.363  1.00 74.88           C  
ANISOU 4922  CG  GLN B1104     8364  11679   8410  -1011    559   1076       C  
ATOM   4923  CD  GLN B1104      27.296  19.115  81.616  1.00 77.38           C  
ANISOU 4923  CD  GLN B1104     8679  12008   8713  -1103    512   1125       C  
ATOM   4924  OE1 GLN B1104      27.773  18.158  81.020  1.00 64.07           O  
ANISOU 4924  OE1 GLN B1104     7068  10244   7031  -1131    438   1122       O  
ATOM   4925  NE2 GLN B1104      25.997  19.350  81.658  1.00 93.34           N  
ANISOU 4925  NE2 GLN B1104    10615  14130  10720  -1152    553   1169       N  
ATOM   4926  N   MET B1105      30.866  19.274  84.771  1.00 84.95           N  
ANISOU 4926  N   MET B1105     9876  12758   9642   -971    497   1013       N  
ATOM   4927  CA  MET B1105      30.663  18.721  86.105  1.00 79.03           C  
ANISOU 4927  CA  MET B1105     9172  12020   8834  -1042    495   1045       C  
ATOM   4928  C   MET B1105      31.744  19.237  87.061  1.00 90.97           C  
ANISOU 4928  C   MET B1105    10732  13484  10349   -973    512   1003       C  
ATOM   4929  O   MET B1105      31.478  20.007  87.985  1.00 91.43           O  
ANISOU 4929  O   MET B1105    10747  13605  10386   -953    578   1002       O  
ATOM   4930  CB  MET B1105      30.668  17.190  86.066  1.00 71.55           C  
ANISOU 4930  CB  MET B1105     8315  11012   7859  -1141    406   1080       C  
ATOM   4931  CG  MET B1105      29.653  16.651  85.047  1.00 98.39           C  
ANISOU 4931  CG  MET B1105    11672  14453  11260  -1206    383   1121       C  
ATOM   4932  SD  MET B1105      29.477  14.846  84.859  1.00102.30           S  
ANISOU 4932  SD  MET B1105    12259  14885  11725  -1328    275   1168       S  
ATOM   4933  CE  MET B1105      28.963  14.439  86.532  1.00112.41           C  
ANISOU 4933  CE  MET B1105    13566  16213  12932  -1417    291   1218       C  
ATOM   4934  N   GLY B1106      32.988  18.830  86.815  1.00 90.62           N  
ANISOU 4934  N   GLY B1106    10775  13323  10332   -934    453    963       N  
ATOM   4935  CA  GLY B1106      34.085  19.186  87.694  1.00 84.61           C  
ANISOU 4935  CA  GLY B1106    10071  12501   9576   -874    457    924       C  
ATOM   4936  C   GLY B1106      35.092  18.044  87.774  1.00 89.82           C  
ANISOU 4936  C   GLY B1106    10853  13036  10238   -901    365    912       C  
ATOM   4937  O   GLY B1106      34.798  16.919  87.345  1.00 90.64           O  
ANISOU 4937  O   GLY B1106    10997  13112  10330   -981    300    942       O  
ATOM   4938  N   GLU B1107      36.280  18.354  88.313  1.00 85.91           N  
ANISOU 4938  N   GLU B1107    10414  12464   9762   -833    358    867       N  
ATOM   4939  CA  GLU B1107      37.350  17.372  88.400  1.00 94.53           C  
ANISOU 4939  CA  GLU B1107    11621  13429  10867   -847    271    847       C  
ATOM   4940  C   GLU B1107      36.901  16.209  89.282  1.00 96.19           C  
ANISOU 4940  C   GLU B1107    11895  13635  11018   -967    222    901       C  
ATOM   4941  O   GLU B1107      36.980  15.054  88.874  1.00102.88           O  
ANISOU 4941  O   GLU B1107    12802  14421  11865  -1031    143    916       O  
ATOM   4942  CB  GLU B1107      38.652  18.012  88.890  1.00100.88           C  
ANISOU 4942  CB  GLU B1107    12467  14158  11703   -751    279    791       C  
ATOM   4943  N   THR B1108      36.400  16.523  90.480  1.00106.16           N  
ANISOU 4943  N   THR B1108    13142  14965  12230  -1000    270    930       N  
ATOM   4944  CA  THR B1108      36.012  15.482  91.422  1.00118.91           C  
ANISOU 4944  CA  THR B1108    14819  16577  13785  -1114    227    983       C  
ATOM   4945  C   THR B1108      34.703  14.815  91.004  1.00112.27           C  
ANISOU 4945  C   THR B1108    13935  15812  12910  -1215    218   1043       C  
ATOM   4946  O   THR B1108      34.437  13.696  91.421  1.00101.87           O  
ANISOU 4946  O   THR B1108    12678  14473  11554  -1317    157   1087       O  
ATOM   4947  CB  THR B1108      35.985  15.990  92.871  1.00111.14           C  
ANISOU 4947  CB  THR B1108    13840  15634  12754  -1119    277    992       C  
ATOM   4948  OG1 THR B1108      35.226  17.195  92.866  1.00112.70           O  
ANISOU 4948  OG1 THR B1108    13926  15948  12948  -1072    377    990       O  
ATOM   4949  CG2 THR B1108      37.364  16.270  93.428  1.00101.80           C  
ANISOU 4949  CG2 THR B1108    12730  14351  11598  -1044    258    942       C  
ATOM   4950  N   GLY B1109      33.893  15.518  90.202  1.00117.04           N  
ANISOU 4950  N   GLY B1109    14436  16503  13530  -1187    277   1046       N  
ATOM   4951  CA  GLY B1109      32.628  15.006  89.692  1.00107.64           C  
ANISOU 4951  CA  GLY B1109    13195  15388  12316  -1272    274   1101       C  
ATOM   4952  C   GLY B1109      32.792  13.849  88.701  1.00107.27           C  
ANISOU 4952  C   GLY B1109    13201  15265  12290  -1318    181   1108       C  
ATOM   4953  O   GLY B1109      32.208  12.783  88.893  1.00107.75           O  
ANISOU 4953  O   GLY B1109    13297  15330  12314  -1424    130   1160       O  
ATOM   4954  N   VAL B1110      33.586  14.062  87.640  1.00102.12           N  
ANISOU 4954  N   VAL B1110    12556  14545  11698  -1238    159   1056       N  
ATOM   4955  CA  VAL B1110      33.745  13.059  86.592  1.00 98.67           C  
ANISOU 4955  CA  VAL B1110    12163  14041  11287  -1271     76   1056       C  
ATOM   4956  C   VAL B1110      34.608  11.897  87.083  1.00101.62           C  
ANISOU 4956  C   VAL B1110    12656  14299  11656  -1316    -18   1052       C  
ATOM   4957  O   VAL B1110      34.568  10.824  86.479  1.00 86.21           O  
ANISOU 4957  O   VAL B1110    10749  12297   9711  -1374    -97   1066       O  
ATOM   4958  CB  VAL B1110      34.311  13.641  85.282  1.00 87.27           C  
ANISOU 4958  CB  VAL B1110    10687  12565   9907  -1175     83   1000       C  
ATOM   4959  CG1 VAL B1110      33.435  14.743  84.756  1.00 82.00           C  
ANISOU 4959  CG1 VAL B1110     9902  12007   9247  -1137    168   1007       C  
ATOM   4960  CG2 VAL B1110      35.728  14.136  85.457  1.00 96.14           C  
ANISOU 4960  CG2 VAL B1110    11859  13600  11071  -1077     81    933       C  
ATOM   4961  N   ALA B1111      35.385  12.126  88.161  1.00 99.90           N  
ANISOU 4961  N   ALA B1111    12490  14039  11428  -1289    -13   1032       N  
ATOM   4962  CA  ALA B1111      36.215  11.085  88.758  1.00103.40           C  
ANISOU 4962  CA  ALA B1111    13047  14372  11866  -1332   -102   1029       C  
ATOM   4963  C   ALA B1111      35.367   9.957  89.357  1.00104.25           C  
ANISOU 4963  C   ALA B1111    13189  14505  11916  -1468   -151   1102       C  
ATOM   4964  O   ALA B1111      35.875   8.856  89.573  1.00 92.39           O  
ANISOU 4964  O   ALA B1111    11778  12911  10415  -1522   -244   1108       O  
ATOM   4965  CB  ALA B1111      37.165  11.673  89.773  1.00101.09           C  
ANISOU 4965  CB  ALA B1111    12796  14037  11577  -1272    -80    995       C  
ATOM   4966  N   GLY B1112      34.075  10.236  89.589  1.00 98.89           N  
ANISOU 4966  N   GLY B1112    12433  13949  11191  -1521    -91   1155       N  
ATOM   4967  CA  GLY B1112      33.128   9.262  90.093  1.00102.33           C  
ANISOU 4967  CA  GLY B1112    12885  14425  11570  -1650   -127   1228       C  
ATOM   4968  C   GLY B1112      32.828   8.150  89.088  1.00122.73           C  
ANISOU 4968  C   GLY B1112    15492  16971  14171  -1711   -211   1250       C  
ATOM   4969  O   GLY B1112      32.412   7.064  89.488  1.00154.53           O  
ANISOU 4969  O   GLY B1112    19567  20987  18162  -1818   -275   1302       O  
ATOM   4970  N   PHE B1113      33.032   8.419  87.788  1.00118.43           N  
ANISOU 4970  N   PHE B1113    14913  16406  13680  -1645   -211   1210       N  
ATOM   4971  CA  PHE B1113      32.696   7.453  86.749  1.00110.94           C  
ANISOU 4971  CA  PHE B1113    13977  15427  12748  -1697   -283   1227       C  
ATOM   4972  C   PHE B1113      33.782   6.391  86.656  1.00108.12           C  
ANISOU 4972  C   PHE B1113    13730  14931  12420  -1709   -393   1198       C  
ATOM   4973  O   PHE B1113      34.333   6.163  85.583  1.00122.42           O  
ANISOU 4973  O   PHE B1113    15556  16676  14281  -1666   -435   1154       O  
ATOM   4974  CB  PHE B1113      32.526   8.113  85.379  1.00103.63           C  
ANISOU 4974  CB  PHE B1113    12977  14531  11868  -1625   -245   1194       C  
ATOM   4975  CG  PHE B1113      31.356   9.054  85.271  1.00112.41           C  
ANISOU 4975  CG  PHE B1113    13975  15777  12959  -1620   -149   1225       C  
ATOM   4976  CD1 PHE B1113      31.492  10.397  85.618  1.00106.33           C  
ANISOU 4976  CD1 PHE B1113    13144  15060  12195  -1535    -54   1195       C  
ATOM   4977  CD2 PHE B1113      30.114   8.591  84.853  1.00115.47           C  
ANISOU 4977  CD2 PHE B1113    14316  16236  13323  -1702   -154   1284       C  
ATOM   4978  CE1 PHE B1113      30.411  11.259  85.527  1.00 90.97           C  
ANISOU 4978  CE1 PHE B1113    11092  13236  10236  -1530     31   1221       C  
ATOM   4979  CE2 PHE B1113      29.035   9.458  84.765  1.00112.04           C  
ANISOU 4979  CE2 PHE B1113    13775  15922  12874  -1698    -67   1310       C  
ATOM   4980  CZ  PHE B1113      29.189  10.785  85.103  1.00 99.79           C  
ANISOU 4980  CZ  PHE B1113    12162  14421  11331  -1612     25   1278       C  
ATOM   4981  N   THR B1114      34.071   5.755  87.795  1.00103.64           N  
ANISOU 4981  N   THR B1114    13237  14320  11820  -1770   -440   1222       N  
ATOM   4982  CA  THR B1114      35.093   4.728  87.904  1.00100.84           C  
ANISOU 4982  CA  THR B1114    12991  13832  11492  -1789   -548   1199       C  
ATOM   4983  C   THR B1114      34.836   3.650  86.859  1.00110.86           C  
ANISOU 4983  C   THR B1114    14280  15059  12783  -1841   -634   1210       C  
ATOM   4984  O   THR B1114      35.775   3.093  86.292  1.00109.35           O  
ANISOU 4984  O   THR B1114    14149  14757  12641  -1813   -708   1161       O  
ATOM   4985  CB  THR B1114      35.070   4.100  89.303  1.00 94.18           C  
ANISOU 4985  CB  THR B1114    12215  12973  10598  -1877   -587   1246       C  
ATOM   4986  OG1 THR B1114      35.318   5.190  90.186  1.00 95.14           O  
ANISOU 4986  OG1 THR B1114    12313  13136  10700  -1819   -502   1229       O  
ATOM   4987  CG2 THR B1114      36.080   2.989  89.513  1.00 86.31           C  
ANISOU 4987  CG2 THR B1114    11332  11835   9627  -1906   -707   1227       C  
ATOM   4988  N   ASN B1115      33.547   3.374  86.628  1.00112.81           N  
ANISOU 4988  N   ASN B1115    14473  15397  12993  -1919   -621   1273       N  
ATOM   4989  CA  ASN B1115      33.135   2.267  85.791  1.00115.46           C  
ANISOU 4989  CA  ASN B1115    14828  15703  13339  -1986   -705   1298       C  
ATOM   4990  C   ASN B1115      33.553   2.547  84.347  1.00112.39           C  
ANISOU 4990  C   ASN B1115    14412  15281  13010  -1903   -705   1237       C  
ATOM   4991  O   ASN B1115      34.093   1.673  83.669  1.00109.47           O  
ANISOU 4991  O   ASN B1115    14099  14819  12678  -1912   -794   1209       O  
ATOM   4992  CB  ASN B1115      31.650   1.971  85.993  1.00122.75           C  
ANISOU 4992  CB  ASN B1115    15699  16735  14207  -2088   -686   1383       C  
ATOM   4993  CG  ASN B1115      31.276   0.584  85.521  1.00144.53           C  
ANISOU 4993  CG  ASN B1115    18502  19449  16966  -2183   -794   1422       C  
ATOM   4994  OD1 ASN B1115      32.138  -0.280  85.364  1.00166.58           O  
ANISOU 4994  OD1 ASN B1115    21377  22125  19790  -2190   -891   1392       O  
ATOM   4995  ND2 ASN B1115      29.994   0.360  85.276  1.00146.80           N  
ANISOU 4995  ND2 ASN B1115    18731  19826  17219  -2256   -779   1486       N  
ATOM   4996  N   SER B1116      33.315   3.788  83.900  1.00116.14           N  
ANISOU 4996  N   SER B1116    14801  15832  13495  -1824   -604   1214       N  
ATOM   4997  CA  SER B1116      33.540   4.203  82.520  1.00104.18           C  
ANISOU 4997  CA  SER B1116    13246  14309  12030  -1748   -589   1164       C  
ATOM   4998  C   SER B1116      35.022   4.491  82.262  1.00 99.53           C  
ANISOU 4998  C   SER B1116    12706  13616  11495  -1649   -605   1078       C  
ATOM   4999  O   SER B1116      35.532   4.150  81.201  1.00 91.66           O  
ANISOU 4999  O   SER B1116    11728  12557  10542  -1618   -651   1033       O  
ATOM   5000  CB  SER B1116      32.664   5.390  82.148  1.00104.91           C  
ANISOU 5000  CB  SER B1116    13226  14523  12111  -1709   -481   1177       C  
ATOM   5001  OG  SER B1116      31.279   5.108  82.299  1.00108.36           O  
ANISOU 5001  OG  SER B1116    13614  15054  12503  -1800   -467   1254       O  
ATOM   5002  N   LEU B1117      35.709   5.121  83.229  1.00 89.52           N  
ANISOU 5002  N   LEU B1117    11458  12330  10224  -1600   -568   1055       N  
ATOM   5003  CA  LEU B1117      37.087   5.557  83.048  1.00 73.92           C  
ANISOU 5003  CA  LEU B1117     9520  10267   8301  -1498   -570    974       C  
ATOM   5004  C   LEU B1117      38.014   4.365  82.830  1.00 74.27           C  
ANISOU 5004  C   LEU B1117     9662  10177   8381  -1520   -686    941       C  
ATOM   5005  O   LEU B1117      38.971   4.479  82.084  1.00 75.63           O  
ANISOU 5005  O   LEU B1117     9853  10276   8606  -1446   -704    872       O  
ATOM   5006  CB  LEU B1117      37.558   6.355  84.264  1.00 77.33           C  
ANISOU 5006  CB  LEU B1117     9959  10706   8718  -1455   -515    966       C  
ATOM   5007  CG  LEU B1117      36.896   7.718  84.480  1.00 88.24           C  
ANISOU 5007  CG  LEU B1117    11243  12207  10077  -1407   -396    979       C  
ATOM   5008  CD1 LEU B1117      37.309   8.315  85.820  1.00 80.68           C  
ANISOU 5008  CD1 LEU B1117    10304  11253   9097  -1382   -354    977       C  
ATOM   5009  CD2 LEU B1117      37.241   8.663  83.336  1.00103.45           C  
ANISOU 5009  CD2 LEU B1117    13110  14145  12052  -1303   -345    923       C  
ATOM   5010  N   ARG B1118      37.731   3.225  83.466  1.00 84.85           N  
ANISOU 5010  N   ARG B1118    11063  11485   9693  -1623   -764    989       N  
ATOM   5011  CA  ARG B1118      38.573   2.042  83.345  1.00 98.39           C  
ANISOU 5011  CA  ARG B1118    12871  13070  11442  -1651   -881    960       C  
ATOM   5012  C   ARG B1118      38.558   1.510  81.910  1.00107.97           C  
ANISOU 5012  C   ARG B1118    14077  14253  12694  -1645   -928    930       C  
ATOM   5013  O   ARG B1118      39.603   1.224  81.308  1.00 99.85           O  
ANISOU 5013  O   ARG B1118    13093  13125  11720  -1594   -978    861       O  
ATOM   5014  CB  ARG B1118      38.128   0.961  84.340  1.00115.16           C  
ANISOU 5014  CB  ARG B1118    15054  15177  13523  -1770   -955   1027       C  
ATOM   5015  CG  ARG B1118      38.926  -0.334  84.272  1.00139.13           C  
ANISOU 5015  CG  ARG B1118    18187  18078  16596  -1810  -1085   1003       C  
ATOM   5016  CD  ARG B1118      40.391  -0.067  84.565  1.00163.70           C  
ANISOU 5016  CD  ARG B1118    21357  21083  19758  -1726  -1101    928       C  
ATOM   5017  NE  ARG B1118      41.289  -1.208  84.396  1.00170.01           N  
ANISOU 5017  NE  ARG B1118    22246  21745  20606  -1747  -1223    890       N  
ATOM   5018  CZ  ARG B1118      42.597  -1.187  84.650  1.00176.26           C  
ANISOU 5018  CZ  ARG B1118    23097  22427  21447  -1686  -1257    825       C  
ATOM   5019  NH1 ARG B1118      43.178  -0.078  85.084  1.00179.24           N  
ANISOU 5019  NH1 ARG B1118    23457  22816  21831  -1599  -1178    791       N  
ATOM   5020  NH2 ARG B1118      43.324  -2.273  84.450  1.00178.51           N  
ANISOU 5020  NH2 ARG B1118    23458  22590  21778  -1711  -1371    792       N  
ATOM   5021  N   MET B1119      37.343   1.366  81.372  1.00125.95           N  
ANISOU 5021  N   MET B1119    16296  16618  14940  -1701   -912    984       N  
ATOM   5022  CA  MET B1119      37.168   0.778  80.057  1.00130.34           C  
ANISOU 5022  CA  MET B1119    16845  17154  15525  -1711   -961    966       C  
ATOM   5023  C   MET B1119      37.551   1.770  78.956  1.00124.67           C  
ANISOU 5023  C   MET B1119    16069  16454  14844  -1605   -894    903       C  
ATOM   5024  O   MET B1119      37.729   1.356  77.817  1.00126.12           O  
ANISOU 5024  O   MET B1119    16258  16602  15061  -1593   -935    868       O  
ATOM   5025  CB  MET B1119      35.742   0.245  79.868  1.00137.66           C  
ANISOU 5025  CB  MET B1119    17733  18164  16408  -1811   -972   1047       C  
ATOM   5026  CG  MET B1119      34.666   1.160  80.428  1.00153.57           C  
ANISOU 5026  CG  MET B1119    19666  20311  18372  -1825   -870   1107       C  
ATOM   5027  SD  MET B1119      32.991   0.437  80.428  1.00163.56           S  
ANISOU 5027  SD  MET B1119    20893  21669  19583  -1954   -889   1209       S  
ATOM   5028  CE  MET B1119      33.206  -0.936  81.561  1.00154.99           C  
ANISOU 5028  CE  MET B1119    19910  20504  18474  -2059  -1000   1250       C  
ATOM   5029  N   LEU B1120      37.681   3.066  79.285  1.00121.57           N  
ANISOU 5029  N   LEU B1120    15626  16119  14448  -1529   -794    888       N  
ATOM   5030  CA  LEU B1120      38.207   4.053  78.344  1.00111.27           C  
ANISOU 5030  CA  LEU B1120    14274  14822  13182  -1423   -734    825       C  
ATOM   5031  C   LEU B1120      39.721   3.895  78.213  1.00115.92           C  
ANISOU 5031  C   LEU B1120    14931  15288  13826  -1353   -779    741       C  
ATOM   5032  O   LEU B1120      40.263   4.032  77.113  1.00107.27           O  
ANISOU 5032  O   LEU B1120    13827  14159  12770  -1295   -783    682       O  
ATOM   5033  CB  LEU B1120      37.860   5.482  78.790  1.00 91.92           C  
ANISOU 5033  CB  LEU B1120    11745  12468  10711  -1365   -618    837       C  
ATOM   5034  CG  LEU B1120      36.447   5.975  78.485  1.00 81.38           C  
ANISOU 5034  CG  LEU B1120    10317  11263   9341  -1400   -554    897       C  
ATOM   5035  CD1 LEU B1120      36.227   7.377  79.020  1.00 70.31           C  
ANISOU 5035  CD1 LEU B1120     8843   9945   7925  -1338   -445    902       C  
ATOM   5036  CD2 LEU B1120      36.175   5.927  76.997  1.00 89.99           C  
ANISOU 5036  CD2 LEU B1120    11370  12368  10456  -1386   -562    879       C  
ATOM   5037  N   GLN B1121      40.393   3.626  79.347  1.00111.66           N  
ANISOU 5037  N   GLN B1121    14458  14682  13286  -1361   -811    737       N  
ATOM   5038  CA  GLN B1121      41.840   3.461  79.379  1.00111.79           C  
ANISOU 5038  CA  GLN B1121    14541  14577  13355  -1299   -856    661       C  
ATOM   5039  C   GLN B1121      42.236   2.214  78.587  1.00105.37           C  
ANISOU 5039  C   GLN B1121    13787  13671  12578  -1334   -963    628       C  
ATOM   5040  O   GLN B1121      43.315   2.176  77.980  1.00 96.55           O  
ANISOU 5040  O   GLN B1121    12700  12470  11516  -1269   -989    551       O  
ATOM   5041  CB  GLN B1121      42.352   3.451  80.825  1.00109.18           C  
ANISOU 5041  CB  GLN B1121    14267  14203  13013  -1307   -867    672       C  
ATOM   5042  CG  GLN B1121      43.870   3.515  80.948  1.00109.56           C  
ANISOU 5042  CG  GLN B1121    14376  14132  13119  -1230   -897    593       C  
ATOM   5043  CD  GLN B1121      44.397   3.542  82.368  1.00117.70           C  
ANISOU 5043  CD  GLN B1121    15464  15118  14140  -1236   -909    603       C  
ATOM   5044  OE1 GLN B1121      43.660   3.694  83.350  1.00109.71           O  
ANISOU 5044  OE1 GLN B1121    14440  14173  13073  -1289   -879    669       O  
ATOM   5045  NE2 GLN B1121      45.705   3.371  82.490  1.00117.50           N  
ANISOU 5045  NE2 GLN B1121    15502  14976  14168  -1184   -955    538       N  
ATOM   5046  N   GLN B1122      41.338   1.217  78.584  1.00102.66           N  
ANISOU 5046  N   GLN B1122    13457  13346  12205  -1438  -1022    688       N  
ATOM   5047  CA  GLN B1122      41.595  -0.070  77.954  1.00101.45           C  
ANISOU 5047  CA  GLN B1122    13360  13106  12081  -1485  -1132    666       C  
ATOM   5048  C   GLN B1122      41.188  -0.079  76.476  1.00105.79           C  
ANISOU 5048  C   GLN B1122    13861  13691  12644  -1472  -1125    646       C  
ATOM   5049  O   GLN B1122      41.092  -1.150  75.873  1.00 98.96           O  
ANISOU 5049  O   GLN B1122    13030  12778  11793  -1524  -1210    642       O  
ATOM   5050  CB  GLN B1122      40.832  -1.163  78.695  1.00 98.24           C  
ANISOU 5050  CB  GLN B1122    12993  12698  11636  -1606  -1206    743       C  
ATOM   5051  CG  GLN B1122      41.289  -1.361  80.123  1.00 94.65           C  
ANISOU 5051  CG  GLN B1122    12600  12194  11169  -1632  -1234    762       C  
ATOM   5052  CD  GLN B1122      40.457  -2.414  80.803  1.00 91.80           C  
ANISOU 5052  CD  GLN B1122    12273  11842  10766  -1757  -1305    843       C  
ATOM   5053  OE1 GLN B1122      39.319  -2.685  80.419  1.00 82.14           O  
ANISOU 5053  OE1 GLN B1122    11006  10695   9507  -1821  -1301    900       O  
ATOM   5054  NE2 GLN B1122      41.044  -3.023  81.816  1.00100.49           N  
ANISOU 5054  NE2 GLN B1122    13450  12860  11870  -1794  -1373    848       N  
ATOM   5055  N   LYS B1123      40.924   1.110  75.908  1.00107.74           N  
ANISOU 5055  N   LYS B1123    14030  14023  12886  -1405  -1024    636       N  
ATOM   5056  CA  LYS B1123      40.588   1.291  74.500  1.00105.57           C  
ANISOU 5056  CA  LYS B1123    13703  13786  12622  -1382  -1005    615       C  
ATOM   5057  C   LYS B1123      39.228   0.677  74.149  1.00104.56           C  
ANISOU 5057  C   LYS B1123    13546  13728  12455  -1477  -1029    688       C  
ATOM   5058  O   LYS B1123      38.891   0.558  72.972  1.00101.67           O  
ANISOU 5058  O   LYS B1123    13149  13383  12097  -1477  -1034    676       O  
ATOM   5059  CB  LYS B1123      41.680   0.749  73.563  1.00 98.32           C  
ANISOU 5059  CB  LYS B1123    12832  12764  11761  -1339  -1068    527       C  
ATOM   5060  CG  LYS B1123      43.100   1.248  73.803  1.00 95.32           C  
ANISOU 5060  CG  LYS B1123    12486  12305  11427  -1246  -1055    447       C  
ATOM   5061  CD  LYS B1123      43.254   2.751  73.681  1.00 85.98           C  
ANISOU 5061  CD  LYS B1123    11236  11190  10244  -1153   -942    429       C  
ATOM   5062  CE  LYS B1123      44.705   3.169  73.529  1.00 87.73           C  
ANISOU 5062  CE  LYS B1123    11486  11328  10520  -1056   -935    338       C  
ATOM   5063  NZ  LYS B1123      45.000   4.505  74.117  1.00 86.86           N  
ANISOU 5063  NZ  LYS B1123    11336  11260  10407   -978   -842    334       N  
ATOM   5064  N   ARG B1124      38.440   0.293  75.158  1.00 94.06           N  
ANISOU 5064  N   ARG B1124    12223  12433  11081  -1559  -1042    766       N  
ATOM   5065  CA  ARG B1124      37.139  -0.293  74.886  1.00106.89           C  
ANISOU 5065  CA  ARG B1124    13820  14124  12670  -1651  -1064    839       C  
ATOM   5066  C   ARG B1124      36.087   0.817  74.851  1.00117.91           C  
ANISOU 5066  C   ARG B1124    15118  15654  14029  -1640   -956    888       C  
ATOM   5067  O   ARG B1124      35.458   1.090  75.870  1.00124.81           O  
ANISOU 5067  O   ARG B1124    15972  16589  14862  -1678   -918    947       O  
ATOM   5068  CB  ARG B1124      36.827  -1.404  75.895  1.00107.06           C  
ANISOU 5068  CB  ARG B1124    13901  14110  12665  -1753  -1145    897       C  
ATOM   5069  CG  ARG B1124      37.753  -2.610  75.798  1.00119.41           C  
ANISOU 5069  CG  ARG B1124    15558  15541  14269  -1773  -1264    851       C  
ATOM   5070  CD  ARG B1124      37.330  -3.792  76.655  1.00124.27           C  
ANISOU 5070  CD  ARG B1124    16231  16125  14860  -1885  -1355    915       C  
ATOM   5071  NE  ARG B1124      37.227  -3.419  78.058  1.00133.11           N  
ANISOU 5071  NE  ARG B1124    17358  17274  15942  -1905  -1318    959       N  
ATOM   5072  CZ  ARG B1124      36.831  -4.219  79.040  1.00136.22           C  
ANISOU 5072  CZ  ARG B1124    17796  17657  16304  -2001  -1377   1023       C  
ATOM   5073  NH1 ARG B1124      36.508  -5.475  78.784  1.00134.94           N  
ANISOU 5073  NH1 ARG B1124    17675  17450  16145  -2085  -1482   1050       N  
ATOM   5074  NH2 ARG B1124      36.763  -3.758  80.277  1.00146.65           N  
ANISOU 5074  NH2 ARG B1124    19120  19012  17590  -2012  -1333   1058       N  
ATOM   5075  N   TRP B1125      35.897   1.430  73.668  1.00119.41           N  
ANISOU 5075  N   TRP B1125    15249  15888  14234  -1591   -911    862       N  
ATOM   5076  CA  TRP B1125      35.094   2.635  73.483  1.00 99.28           C  
ANISOU 5076  CA  TRP B1125    12604  13455  11664  -1560   -806    891       C  
ATOM   5077  C   TRP B1125      33.608   2.319  73.557  1.00 97.11           C  
ANISOU 5077  C   TRP B1125    12283  13268  11345  -1653   -803    979       C  
ATOM   5078  O   TRP B1125      32.840   3.024  74.207  1.00101.10           O  
ANISOU 5078  O   TRP B1125    12732  13864  11819  -1664   -732   1029       O  
ATOM   5079  CB  TRP B1125      35.420   3.321  72.151  1.00 93.46           C  
ANISOU 5079  CB  TRP B1125    11823  12727  10959  -1482   -769    834       C  
ATOM   5080  CG  TRP B1125      36.886   3.420  71.874  1.00 90.80           C  
ANISOU 5080  CG  TRP B1125    11536  12294  10669  -1400   -788    744       C  
ATOM   5081  CD1 TRP B1125      37.550   2.905  70.804  1.00 97.38           C  
ANISOU 5081  CD1 TRP B1125    12403  13058  11538  -1378   -841    682       C  
ATOM   5082  CD2 TRP B1125      37.877   4.068  72.688  1.00 90.11           C  
ANISOU 5082  CD2 TRP B1125    11470  12168  10598  -1330   -753    703       C  
ATOM   5083  NE1 TRP B1125      38.885   3.192  70.892  1.00100.31           N  
ANISOU 5083  NE1 TRP B1125    12813  13352  11948  -1299   -841    606       N  
ATOM   5084  CE2 TRP B1125      39.115   3.901  72.039  1.00 94.79           C  
ANISOU 5084  CE2 TRP B1125    12108  12668  11239  -1267   -788    618       C  
ATOM   5085  CE3 TRP B1125      37.842   4.773  73.896  1.00 97.13           C  
ANISOU 5085  CE3 TRP B1125    12345  13093  11467  -1313   -695    729       C  
ATOM   5086  CZ2 TRP B1125      40.303   4.413  72.563  1.00103.14           C  
ANISOU 5086  CZ2 TRP B1125    13196  13666  12326  -1189   -769    561       C  
ATOM   5087  CZ3 TRP B1125      39.014   5.277  74.413  1.00 95.46           C  
ANISOU 5087  CZ3 TRP B1125    12166  12822  11284  -1236   -677    673       C  
ATOM   5088  CH2 TRP B1125      40.230   5.099  73.753  1.00 98.22           C  
ANISOU 5088  CH2 TRP B1125    12559  13077  11682  -1175   -714    591       C  
ATOM   5089  N   ASP B1126      33.214   1.262  72.845  1.00 96.55           N  
ANISOU 5089  N   ASP B1126    12238  13171  11276  -1718   -882    996       N  
ATOM   5090  CA  ASP B1126      31.812   0.934  72.675  1.00 98.58           C  
ANISOU 5090  CA  ASP B1126    12449  13508  11499  -1802   -884   1075       C  
ATOM   5091  C   ASP B1126      31.194   0.511  74.009  1.00 93.56           C  
ANISOU 5091  C   ASP B1126    11828  12900  10819  -1884   -894   1148       C  
ATOM   5092  O   ASP B1126      30.042   0.809  74.284  1.00100.02           O  
ANISOU 5092  O   ASP B1126    12585  13815  11602  -1930   -848   1215       O  
ATOM   5093  CB  ASP B1126      31.639  -0.075  71.542  1.00101.92           C  
ANISOU 5093  CB  ASP B1126    12899  13889  11939  -1844   -968   1068       C  
ATOM   5094  CG  ASP B1126      32.169   0.453  70.223  1.00115.94           C  
ANISOU 5094  CG  ASP B1126    14651  15652  13751  -1765   -946    999       C  
ATOM   5095  OD1 ASP B1126      33.405   0.350  69.985  1.00123.33           O  
ANISOU 5095  OD1 ASP B1126    15638  16499  14723  -1705   -974    922       O  
ATOM   5096  OD2 ASP B1126      31.345   0.984  69.457  1.00128.24           O1-
ANISOU 5096  OD2 ASP B1126    16138  17287  15300  -1764   -899   1024       O1-
ATOM   5097  N   GLU B1127      31.962  -0.182  74.846  1.00 88.85           N  
ANISOU 5097  N   GLU B1127    11313  12219  10226  -1903   -956   1134       N  
ATOM   5098  CA  GLU B1127      31.458  -0.652  76.119  1.00 90.15           C  
ANISOU 5098  CA  GLU B1127    11502  12404  10348  -1986   -974   1201       C  
ATOM   5099  C   GLU B1127      31.243   0.544  77.041  1.00 98.55           C  
ANISOU 5099  C   GLU B1127    12511  13548  11384  -1949   -867   1218       C  
ATOM   5100  O   GLU B1127      30.299   0.553  77.828  1.00112.77           O  
ANISOU 5100  O   GLU B1127    14282  15425  13139  -2015   -840   1289       O  
ATOM   5101  CB  GLU B1127      32.437  -1.685  76.680  1.00112.82           C  
ANISOU 5101  CB  GLU B1127    14477  15154  13237  -2010  -1075   1175       C  
ATOM   5102  CG  GLU B1127      31.999  -2.357  77.969  1.00134.00           C  
ANISOU 5102  CG  GLU B1127    17197  17841  15875  -2106  -1113   1245       C  
ATOM   5103  CD  GLU B1127      32.984  -3.396  78.502  1.00142.72           C  
ANISOU 5103  CD  GLU B1127    18407  18820  17001  -2133  -1220   1220       C  
ATOM   5104  OE1 GLU B1127      33.908  -3.796  77.744  1.00150.37           O  
ANISOU 5104  OE1 GLU B1127    19419  19694  18021  -2088  -1279   1150       O  
ATOM   5105  OE2 GLU B1127      32.825  -3.812  79.672  1.00139.03           O1-
ANISOU 5105  OE2 GLU B1127    17976  18350  16499  -2200  -1246   1269       O1-
ATOM   5106  N   ALA B1128      32.129   1.543  76.947  1.00106.41           N  
ANISOU 5106  N   ALA B1128    13494  14528  12408  -1843   -808   1152       N  
ATOM   5107  CA  ALA B1128      32.052   2.740  77.775  1.00111.76           C  
ANISOU 5107  CA  ALA B1128    14121  15275  13066  -1795   -707   1158       C  
ATOM   5108  C   ALA B1128      30.924   3.662  77.317  1.00107.80           C  
ANISOU 5108  C   ALA B1128    13512  14897  12549  -1787   -619   1193       C  
ATOM   5109  O   ALA B1128      30.345   4.398  78.121  1.00106.35           O  
ANISOU 5109  O   ALA B1128    13277  14797  12335  -1790   -543   1227       O  
ATOM   5110  CB  ALA B1128      33.384   3.446  77.767  1.00112.57           C  
ANISOU 5110  CB  ALA B1128    14248  15315  13209  -1687   -682   1076       C  
ATOM   5111  N   ALA B1129      30.622   3.617  76.018  1.00100.53           N  
ANISOU 5111  N   ALA B1129    12559  13986  11651  -1776   -629   1181       N  
ATOM   5112  CA  ALA B1129      29.581   4.462  75.458  1.00 97.41           C  
ANISOU 5112  CA  ALA B1129    12064  13700  11248  -1768   -553   1211       C  
ATOM   5113  C   ALA B1129      28.217   4.108  76.058  1.00 96.87           C  
ANISOU 5113  C   ALA B1129    11958  13715  11132  -1868   -546   1300       C  
ATOM   5114  O   ALA B1129      27.458   5.007  76.410  1.00 99.55           O  
ANISOU 5114  O   ALA B1129    12219  14152  11453  -1860   -461   1330       O  
ATOM   5115  CB  ALA B1129      29.601   4.365  73.953  1.00 81.22           C  
ANISOU 5115  CB  ALA B1129     9996  11632   9231  -1743   -578   1181       C  
ATOM   5116  N   VAL B1130      27.915   2.807  76.183  1.00 92.69           N  
ANISOU 5116  N   VAL B1130    11485  13147  10585  -1962   -634   1341       N  
ATOM   5117  CA  VAL B1130      26.636   2.353  76.711  1.00105.74           C  
ANISOU 5117  CA  VAL B1130    13109  14875  12194  -2065   -636   1427       C  
ATOM   5118  C   VAL B1130      26.599   2.550  78.226  1.00109.69           C  
ANISOU 5118  C   VAL B1130    13620  15405  12654  -2091   -601   1457       C  
ATOM   5119  O   VAL B1130      25.527   2.733  78.815  1.00107.77           O  
ANISOU 5119  O   VAL B1130    13322  15254  12370  -2148   -556   1520       O  
ATOM   5120  CB  VAL B1130      26.299   0.901  76.313  1.00103.87           C  
ANISOU 5120  CB  VAL B1130    12927  14588  11952  -2158   -746   1464       C  
ATOM   5121  CG1 VAL B1130      27.263  -0.117  76.908  1.00104.79           C  
ANISOU 5121  CG1 VAL B1130    13151  14594  12072  -2185   -838   1444       C  
ATOM   5122  CG2 VAL B1130      24.861   0.554  76.667  1.00100.30           C  
ANISOU 5122  CG2 VAL B1130    12428  14224  11456  -2259   -739   1555       C  
ATOM   5123  N   ASN B1131      27.784   2.504  78.844  1.00109.77           N  
ANISOU 5123  N   ASN B1131    13700  15334  12674  -2049   -622   1409       N  
ATOM   5124  CA  ASN B1131      27.896   2.646  80.284  1.00103.74           C  
ANISOU 5124  CA  ASN B1131    12957  14585  11873  -2072   -597   1431       C  
ATOM   5125  C   ASN B1131      27.634   4.095  80.696  1.00113.80           C  
ANISOU 5125  C   ASN B1131    14149  15953  13139  -2006   -475   1422       C  
ATOM   5126  O   ASN B1131      27.003   4.336  81.726  1.00118.41           O  
ANISOU 5126  O   ASN B1131    14705  16609  13678  -2049   -428   1468       O  
ATOM   5127  CB  ASN B1131      29.229   2.099  80.776  1.00100.96           C  
ANISOU 5127  CB  ASN B1131    12709  14113  11539  -2051   -665   1384       C  
ATOM   5128  CG  ASN B1131      29.232   1.979  82.278  1.00111.92           C  
ANISOU 5128  CG  ASN B1131    14131  15512  12882  -2100   -658   1420       C  
ATOM   5129  OD1 ASN B1131      28.675   1.028  82.809  1.00120.51           O  
ANISOU 5129  OD1 ASN B1131    15251  16603  13933  -2204   -714   1481       O  
ATOM   5130  ND2 ASN B1131      29.821   2.949  82.961  1.00124.91           N  
ANISOU 5130  ND2 ASN B1131    15766  17167  14526  -2028   -589   1385       N  
ATOM   5131  N   LEU B1132      28.125   5.050  79.887  1.00122.04           N  
ANISOU 5131  N   LEU B1132    15151  16994  14223  -1902   -426   1362       N  
ATOM   5132  CA  LEU B1132      27.952   6.476  80.148  1.00117.68           C  
ANISOU 5132  CA  LEU B1132    14517  16523  13672  -1829   -315   1347       C  
ATOM   5133  C   LEU B1132      26.493   6.912  79.987  1.00112.48           C  
ANISOU 5133  C   LEU B1132    13758  15988  12991  -1871   -254   1405       C  
ATOM   5134  O   LEU B1132      26.111   7.940  80.544  1.00 98.50           O  
ANISOU 5134  O   LEU B1132    11919  14298  11208  -1839   -165   1409       O  
ATOM   5135  CB  LEU B1132      28.855   7.310  79.231  1.00124.94           C  
ANISOU 5135  CB  LEU B1132    15422  17405  14646  -1713   -289   1270       C  
ATOM   5136  CG  LEU B1132      30.323   7.417  79.626  1.00122.93           C  
ANISOU 5136  CG  LEU B1132    15240  17052  14416  -1642   -308   1205       C  
ATOM   5137  CD1 LEU B1132      31.136   8.027  78.502  1.00122.68           C  
ANISOU 5137  CD1 LEU B1132    15196  16979  14438  -1541   -297   1134       C  
ATOM   5138  CD2 LEU B1132      30.498   8.218  80.902  1.00114.10           C  
ANISOU 5138  CD2 LEU B1132    14109  15970  13274  -1612   -240   1204       C  
ATOM   5139  N   ALA B1133      25.689   6.159  79.216  1.00103.94           N  
ANISOU 5139  N   ALA B1133    12665  14919  11907  -1940   -302   1446       N  
ATOM   5140  CA  ALA B1133      24.280   6.493  79.036  1.00 99.03           C  
ANISOU 5140  CA  ALA B1133    11950  14410  11267  -1986   -250   1503       C  
ATOM   5141  C   ALA B1133      23.470   6.131  80.285  1.00106.75           C  
ANISOU 5141  C   ALA B1133    12923  15450  12188  -2078   -237   1570       C  
ATOM   5142  O   ALA B1133      22.418   6.718  80.540  1.00114.18           O  
ANISOU 5142  O   ALA B1133    13777  16496  13109  -2100   -167   1609       O  
ATOM   5143  CB  ALA B1133      23.735   5.852  77.784  1.00 85.69           C  
ANISOU 5143  CB  ALA B1133    10251  12712   9597  -2024   -305   1523       C  
ATOM   5144  N   LYS B1134      23.981   5.193  81.091  1.00106.19           N  
ANISOU 5144  N   LYS B1134    12942  15313  12091  -2131   -303   1582       N  
ATOM   5145  CA  LYS B1134      23.278   4.803  82.304  1.00102.96           C  
ANISOU 5145  CA  LYS B1134    12537  14960  11625  -2223   -295   1646       C  
ATOM   5146  C   LYS B1134      23.664   5.732  83.456  1.00103.66           C  
ANISOU 5146  C   LYS B1134    12612  15081  11692  -2175   -216   1623       C  
ATOM   5147  O   LYS B1134      23.795   5.279  84.595  1.00111.52           O  
ANISOU 5147  O   LYS B1134    13658  16068  12645  -2230   -234   1648       O  
ATOM   5148  CB  LYS B1134      23.610   3.355  82.693  1.00102.40           C  
ANISOU 5148  CB  LYS B1134    12569  14804  11532  -2310   -405   1674       C  
ATOM   5149  CG  LYS B1134      23.467   2.266  81.634  1.00 92.30           C  
ANISOU 5149  CG  LYS B1134    11326  13467  10276  -2356   -502   1689       C  
ATOM   5150  CD  LYS B1134      24.140   0.985  82.111  1.00 84.68           C  
ANISOU 5150  CD  LYS B1134    10474  12400   9301  -2417   -613   1697       C  
ATOM   5151  CE  LYS B1134      24.471  -0.031  81.041  1.00 85.62           C  
ANISOU 5151  CE  LYS B1134    10646  12427   9457  -2433   -717   1682       C  
ATOM   5152  NZ  LYS B1134      23.261  -0.433  80.292  1.00112.46           N  
ANISOU 5152  NZ  LYS B1134    13994  15885  12850  -2498   -732   1738       N  
ATOM   5153  N   SER B1135      23.844   7.029  83.164  1.00112.64           N  
ANISOU 5153  N   SER B1135    13681  16258  12858  -2075   -132   1577       N  
ATOM   5154  CA  SER B1135      24.372   7.960  84.155  1.00115.79           C  
ANISOU 5154  CA  SER B1135    14073  16677  13247  -2014    -62   1544       C  
ATOM   5155  C   SER B1135      23.333   9.005  84.557  1.00105.31           C  
ANISOU 5155  C   SER B1135    12633  15479  11899  -2008     45   1567       C  
ATOM   5156  O   SER B1135      22.305   9.156  83.907  1.00 90.00           O  
ANISOU 5156  O   SER B1135    10618  13610   9968  -2033     69   1598       O  
ATOM   5157  CB  SER B1135      25.650   8.619  83.688  1.00114.42           C  
ANISOU 5157  CB  SER B1135    13924  16427  13124  -1895    -56   1463       C  
ATOM   5158  OG  SER B1135      26.643   7.651  83.416  1.00147.64           O  
ANISOU 5158  OG  SER B1135    18234  20513  17349  -1900   -153   1438       O  
ATOM   5159  N   ARG B1136      23.634   9.719  85.646  1.00101.80           N  
ANISOU 5159  N   ARG B1136    12182  15064  11433  -1975    107   1549       N  
ATOM   5160  CA  ARG B1136      22.881  10.893  86.062  1.00117.35           C  
ANISOU 5160  CA  ARG B1136    14047  17148  13393  -1945    214   1552       C  
ATOM   5161  C   ARG B1136      23.156  12.028  85.081  1.00119.58           C  
ANISOU 5161  C   ARG B1136    14262  17436  13735  -1832    262   1497       C  
ATOM   5162  O   ARG B1136      22.287  12.864  84.830  1.00122.88           O  
ANISOU 5162  O   ARG B1136    14577  17947  14164  -1814    332   1506       O  
ATOM   5163  CB  ARG B1136      23.239  11.315  87.496  1.00126.39           C  
ANISOU 5163  CB  ARG B1136    15211  18313  14497  -1937    261   1542       C  
ATOM   5164  CG  ARG B1136      24.632  11.911  87.675  1.00142.54           C  
ANISOU 5164  CG  ARG B1136    17305  20279  16573  -1832    266   1471       C  
ATOM   5165  CD  ARG B1136      25.726  10.874  87.885  1.00152.77           C  
ANISOU 5165  CD  ARG B1136    18728  21450  17866  -1853    169   1460       C  
ATOM   5166  NE  ARG B1136      27.054  11.386  88.222  1.00149.37           N  
ANISOU 5166  NE  ARG B1136    18350  20943  17461  -1760    173   1396       N  
ATOM   5167  CZ  ARG B1136      28.143  10.641  88.444  1.00136.88           C  
ANISOU 5167  CZ  ARG B1136    16876  19246  15885  -1762     94   1375       C  
ATOM   5168  NH1 ARG B1136      28.096   9.322  88.385  1.00133.89           N  
ANISOU 5168  NH1 ARG B1136    16569  18813  15489  -1852      2   1412       N  
ATOM   5169  NH2 ARG B1136      29.294  11.221  88.716  1.00129.19           N  
ANISOU 5169  NH2 ARG B1136    15939  18211  14938  -1672    106   1316       N  
ATOM   5170  N   TRP B1137      24.381  12.033  84.538  1.00115.64           N  
ANISOU 5170  N   TRP B1137    13825  16836  13278  -1757    220   1441       N  
ATOM   5171  CA  TRP B1137      24.844  13.010  83.568  1.00106.85           C  
ANISOU 5171  CA  TRP B1137    12666  15711  12223  -1649    253   1385       C  
ATOM   5172  C   TRP B1137      24.015  12.930  82.292  1.00109.66           C  
ANISOU 5172  C   TRP B1137    12961  16101  12605  -1667    242   1407       C  
ATOM   5173  O   TRP B1137      23.668  13.957  81.726  1.00117.87           O  
ANISOU 5173  O   TRP B1137    13913  17196  13677  -1608    302   1390       O  
ATOM   5174  CB  TRP B1137      26.333  12.805  83.276  1.00 92.59           C  
ANISOU 5174  CB  TRP B1137    10949  13782  10449  -1582    198   1325       C  
ATOM   5175  CG  TRP B1137      26.867  13.637  82.148  1.00 87.39           C  
ANISOU 5175  CG  TRP B1137    10254  13101   9850  -1479    217   1270       C  
ATOM   5176  CD1 TRP B1137      26.772  14.990  81.983  1.00 81.79           C  
ANISOU 5176  CD1 TRP B1137     9457  12450   9168  -1395    298   1241       C  
ATOM   5177  CD2 TRP B1137      27.611  13.150  81.019  1.00 77.65           C  
ANISOU 5177  CD2 TRP B1137     9070  11778   8655  -1451    150   1236       C  
ATOM   5178  NE1 TRP B1137      27.384  15.369  80.820  1.00 73.53           N  
ANISOU 5178  NE1 TRP B1137     8406  11359   8174  -1320    285   1196       N  
ATOM   5179  CE2 TRP B1137      27.938  14.266  80.226  1.00 74.93           C  
ANISOU 5179  CE2 TRP B1137     8667  11444   8357  -1351    197   1189       C  
ATOM   5180  CE3 TRP B1137      28.076  11.887  80.628  1.00 79.32           C  
ANISOU 5180  CE3 TRP B1137     9373  11898   8868  -1499     54   1237       C  
ATOM   5181  CZ2 TRP B1137      28.673  14.151  79.048  1.00 80.35           C  
ANISOU 5181  CZ2 TRP B1137     9381  12060   9087  -1302    155   1146       C  
ATOM   5182  CZ3 TRP B1137      28.788  11.763  79.460  1.00 79.34           C  
ANISOU 5182  CZ3 TRP B1137     9400  11830   8914  -1449     12   1192       C  
ATOM   5183  CH2 TRP B1137      29.079  12.885  78.683  1.00 86.34           C  
ANISOU 5183  CH2 TRP B1137    10227  12734   9843  -1353     64   1147       C  
ATOM   5184  N   TYR B1138      23.726  11.710  81.840  1.00107.92           N  
ANISOU 5184  N   TYR B1138    12788  15843  12372  -1750    163   1445       N  
ATOM   5185  CA  TYR B1138      23.051  11.496  80.573  1.00 96.82           C  
ANISOU 5185  CA  TYR B1138    11340  14453  10992  -1770    139   1464       C  
ATOM   5186  C   TYR B1138      21.584  11.885  80.679  1.00107.17           C  
ANISOU 5186  C   TYR B1138    12549  15885  12287  -1820    199   1518       C  
ATOM   5187  O   TYR B1138      21.032  12.416  79.720  1.00106.73           O  
ANISOU 5187  O   TYR B1138    12419  15870  12265  -1795    223   1517       O  
ATOM   5188  CB  TYR B1138      23.196  10.050  80.118  1.00 85.28           C  
ANISOU 5188  CB  TYR B1138     9965  12915   9523  -1844     34   1487       C  
ATOM   5189  CG  TYR B1138      22.554   9.778  78.785  1.00 93.01           C  
ANISOU 5189  CG  TYR B1138    10907  13904  10528  -1864      4   1505       C  
ATOM   5190  CD1 TYR B1138      23.240  10.001  77.607  1.00 95.64           C  
ANISOU 5190  CD1 TYR B1138    11250  14180  10909  -1794    -18   1454       C  
ATOM   5191  CD2 TYR B1138      21.266   9.283  78.699  1.00103.61           C  
ANISOU 5191  CD2 TYR B1138    12207  15313  11848  -1957     -3   1573       C  
ATOM   5192  CE1 TYR B1138      22.662   9.734  76.378  1.00103.73           C  
ANISOU 5192  CE1 TYR B1138    12245  15213  11955  -1816    -48   1470       C  
ATOM   5193  CE2 TYR B1138      20.664   9.027  77.476  1.00104.00           C  
ANISOU 5193  CE2 TYR B1138    12224  15370  11921  -1977    -33   1591       C  
ATOM   5194  CZ  TYR B1138      21.372   9.247  76.310  1.00108.32           C  
ANISOU 5194  CZ  TYR B1138    12784  15858  12513  -1907    -56   1539       C  
ATOM   5195  OH  TYR B1138      20.826   8.999  75.085  1.00123.09           O  
ANISOU 5195  OH  TYR B1138    14628  17733  14406  -1926    -87   1554       O  
ATOM   5196  N   ASN B1139      20.977  11.636  81.851  1.00116.88           N  
ANISOU 5196  N   ASN B1139    13773  17170  13465  -1891    222   1562       N  
ATOM   5197  CA  ASN B1139      19.552  11.860  82.040  1.00115.47           C  
ANISOU 5197  CA  ASN B1139    13502  17106  13267  -1951    273   1617       C  
ATOM   5198  C   ASN B1139      19.256  13.324  82.350  1.00116.97           C  
ANISOU 5198  C   ASN B1139    13591  17380  13474  -1878    378   1590       C  
ATOM   5199  O   ASN B1139      18.161  13.804  82.043  1.00125.52           O  
ANISOU 5199  O   ASN B1139    14576  18550  14566  -1895    425   1617       O  
ATOM   5200  CB  ASN B1139      18.912  10.896  83.043  1.00116.98           C  
ANISOU 5200  CB  ASN B1139    13725  17326  13396  -2068    250   1681       C  
ATOM   5201  CG  ASN B1139      18.921   9.460  82.556  1.00129.47           C  
ANISOU 5201  CG  ASN B1139    15386  18838  14967  -2149    144   1717       C  
ATOM   5202  OD1 ASN B1139      19.808   9.057  81.805  1.00141.11           O  
ANISOU 5202  OD1 ASN B1139    16926  20216  16473  -2112     80   1682       O  
ATOM   5203  ND2 ASN B1139      17.946   8.671  82.978  1.00117.39           N  
ANISOU 5203  ND2 ASN B1139    13852  17355  13396  -2259    124   1787       N  
ATOM   5204  N   GLN B1140      20.226  14.021  82.957  1.00110.20           N  
ANISOU 5204  N   GLN B1140    12755  16494  12620  -1798    412   1537       N  
ATOM   5205  CA  GLN B1140      20.005  15.408  83.343  1.00110.10           C  
ANISOU 5205  CA  GLN B1140    12651  16559  12624  -1727    509   1508       C  
ATOM   5206  C   GLN B1140      20.134  16.282  82.099  1.00116.01           C  
ANISOU 5206  C   GLN B1140    13338  17303  13436  -1640    526   1470       C  
ATOM   5207  O   GLN B1140      19.247  17.088  81.810  1.00137.72           O  
ANISOU 5207  O   GLN B1140    15983  20137  16209  -1626    584   1479       O  
ATOM   5208  CB  GLN B1140      20.943  15.823  84.484  1.00119.43           C  
ANISOU 5208  CB  GLN B1140    13877  17715  13785  -1678    539   1469       C  
ATOM   5209  CG  GLN B1140      20.680  17.226  85.045  1.00117.08           C  
ANISOU 5209  CG  GLN B1140    13486  17501  13498  -1610    640   1441       C  
ATOM   5210  CD  GLN B1140      19.569  17.314  86.072  1.00125.03           C  
ANISOU 5210  CD  GLN B1140    14433  18617  14457  -1681    699   1484       C  
ATOM   5211  OE1 GLN B1140      18.432  16.927  85.824  1.00129.64           O  
ANISOU 5211  OE1 GLN B1140    14967  19261  15028  -1758    699   1535       O  
ATOM   5212  NE2 GLN B1140      19.871  17.848  87.248  1.00124.39           N  
ANISOU 5212  NE2 GLN B1140    14353  18562  14347  -1656    751   1462       N  
ATOM   5213  N   THR B1141      21.226  16.087  81.346  1.00102.90           N  
ANISOU 5213  N   THR B1141    11745  15545  11808  -1585    473   1429       N  
ATOM   5214  CA  THR B1141      21.484  16.867  80.146  1.00 96.53           C  
ANISOU 5214  CA  THR B1141    10892  14725  11059  -1503    482   1390       C  
ATOM   5215  C   THR B1141      21.735  15.912  78.985  1.00 86.96           C  
ANISOU 5215  C   THR B1141     9739  13438   9863  -1531    396   1396       C  
ATOM   5216  O   THR B1141      22.867  15.534  78.703  1.00 90.32           O  
ANISOU 5216  O   THR B1141    10248  13769  10301  -1495    346   1357       O  
ATOM   5217  CB  THR B1141      22.619  17.876  80.366  1.00 99.45           C  
ANISOU 5217  CB  THR B1141    11269  15060  11459  -1388    518   1323       C  
ATOM   5218  OG1 THR B1141      23.784  17.161  80.790  1.00125.00           O  
ANISOU 5218  OG1 THR B1141    14619  18197  14678  -1383    464   1299       O  
ATOM   5219  CG2 THR B1141      22.278  18.961  81.365  1.00 93.24           C  
ANISOU 5219  CG2 THR B1141    10409  14355  10664  -1352    607   1314       C  
ATOM   5220  N   PRO B1142      20.676  15.478  78.282  1.00 88.94           N  
ANISOU 5220  N   PRO B1142     9949  13730  10115  -1598    377   1444       N  
ATOM   5221  CA  PRO B1142      20.801  14.378  77.321  1.00 97.75           C  
ANISOU 5221  CA  PRO B1142    11127  14777  11235  -1644    289   1457       C  
ATOM   5222  C   PRO B1142      21.449  14.755  75.986  1.00 91.48           C  
ANISOU 5222  C   PRO B1142    10334  13932  10492  -1570    268   1411       C  
ATOM   5223  O   PRO B1142      22.194  13.977  75.399  1.00 92.98           O  
ANISOU 5223  O   PRO B1142    10605  14036  10689  -1572    197   1390       O  
ATOM   5224  CB  PRO B1142      19.346  13.896  77.166  1.00 91.05           C  
ANISOU 5224  CB  PRO B1142    10224  14003  10368  -1741    286   1528       C  
ATOM   5225  CG  PRO B1142      18.511  15.144  77.449  1.00 89.31           C  
ANISOU 5225  CG  PRO B1142     9883  13887  10161  -1710    379   1534       C  
ATOM   5226  CD  PRO B1142      19.309  15.995  78.413  1.00 82.19           C  
ANISOU 5226  CD  PRO B1142     8986  12986   9257  -1635    436   1486       C  
ATOM   5227  N   ASN B1143      21.174  15.970  75.520  1.00 90.71           N  
ANISOU 5227  N   ASN B1143    10145  13889  10430  -1505    329   1392       N  
ATOM   5228  CA  ASN B1143      21.609  16.420  74.210  1.00 93.91           C  
ANISOU 5228  CA  ASN B1143    10536  14261  10882  -1442    315   1355       C  
ATOM   5229  C   ASN B1143      23.118  16.623  74.215  1.00 96.63           C  
ANISOU 5229  C   ASN B1143    10951  14521  11244  -1358    301   1288       C  
ATOM   5230  O   ASN B1143      23.772  16.351  73.218  1.00 97.56           O  
ANISOU 5230  O   ASN B1143    11110  14573  11384  -1332    254   1257       O  
ATOM   5231  CB  ASN B1143      20.898  17.716  73.810  1.00107.26           C  
ANISOU 5231  CB  ASN B1143    12108  16036  12609  -1397    384   1356       C  
ATOM   5232  CG  ASN B1143      19.396  17.552  73.814  1.00114.71           C  
ANISOU 5232  CG  ASN B1143    12979  17065  13541  -1478    399   1420       C  
ATOM   5233  OD1 ASN B1143      18.929  16.419  73.717  1.00117.93           O  
ANISOU 5233  OD1 ASN B1143    13427  17459  13921  -1565    346   1464       O  
ATOM   5234  ND2 ASN B1143      18.654  18.651  73.946  1.00142.39           N  
ANISOU 5234  ND2 ASN B1143    16377  20656  17069  -1450    469   1426       N  
ATOM   5235  N   ARG B1144      23.642  17.111  75.349  1.00 97.67           N  
ANISOU 5235  N   ARG B1144    11092  14654  11363  -1317    343   1265       N  
ATOM   5236  CA  ARG B1144      25.055  17.410  75.487  1.00 80.64           C  
ANISOU 5236  CA  ARG B1144     8995  12420   9223  -1234    338   1202       C  
ATOM   5237  C   ARG B1144      25.826  16.119  75.693  1.00 83.02           C  
ANISOU 5237  C   ARG B1144     9415  12626   9502  -1275    259   1195       C  
ATOM   5238  O   ARG B1144      26.928  15.983  75.183  1.00 91.71           O  
ANISOU 5238  O   ARG B1144    10575  13644  10627  -1224    223   1145       O  
ATOM   5239  CB  ARG B1144      25.304  18.360  76.655  1.00 75.12           C  
ANISOU 5239  CB  ARG B1144     8266  11757   8520  -1179    408   1182       C  
ATOM   5240  CG  ARG B1144      26.756  18.799  76.771  1.00 79.79           C  
ANISOU 5240  CG  ARG B1144     8911  12271   9135  -1085    407   1116       C  
ATOM   5241  CD  ARG B1144      27.027  19.475  78.100  1.00 87.97           C  
ANISOU 5241  CD  ARG B1144     9938  13332  10156  -1046    464   1102       C  
ATOM   5242  NE  ARG B1144      28.441  19.739  78.311  1.00 81.65           N  
ANISOU 5242  NE  ARG B1144     9200  12449   9374   -965    455   1043       N  
ATOM   5243  CZ  ARG B1144      28.972  20.948  78.307  1.00 84.01           C  
ANISOU 5243  CZ  ARG B1144     9455  12756   9707   -867    505   1000       C  
ATOM   5244  NH1 ARG B1144      28.217  22.017  78.095  1.00 85.14           N  
ANISOU 5244  NH1 ARG B1144     9492  12986   9871   -836    567   1008       N  
ATOM   5245  NH2 ARG B1144      30.268  21.083  78.509  1.00102.33           N  
ANISOU 5245  NH2 ARG B1144    11840  14997  12045   -799    491    949       N  
ATOM   5246  N   ALA B1145      25.247  15.189  76.461  1.00 90.36           N  
ANISOU 5246  N   ALA B1145    10377  13568  10388  -1367    234   1245       N  
ATOM   5247  CA  ALA B1145      25.935  13.958  76.818  1.00 82.61           C  
ANISOU 5247  CA  ALA B1145     9506  12497   9384  -1412    157   1243       C  
ATOM   5248  C   ALA B1145      26.114  13.093  75.580  1.00 79.07           C  
ANISOU 5248  C   ALA B1145     9102  11988   8955  -1437     80   1237       C  
ATOM   5249  O   ALA B1145      27.171  12.499  75.407  1.00 82.66           O  
ANISOU 5249  O   ALA B1145     9641  12346   9419  -1418     23   1197       O  
ATOM   5250  CB  ALA B1145      25.199  13.215  77.904  1.00 81.80           C  
ANISOU 5250  CB  ALA B1145     9421  12430   9229  -1510    148   1302       C  
ATOM   5251  N   LYS B1146      25.077  13.033  74.735  1.00 79.04           N  
ANISOU 5251  N   LYS B1146     9038  12037   8954  -1479     79   1275       N  
ATOM   5252  CA  LYS B1146      25.100  12.186  73.552  1.00 77.03           C  
ANISOU 5252  CA  LYS B1146     8820  11733   8714  -1510      6   1275       C  
ATOM   5253  C   LYS B1146      26.213  12.645  72.604  1.00 76.31           C  
ANISOU 5253  C   LYS B1146     8750  11579   8665  -1419     -2   1204       C  
ATOM   5254  O   LYS B1146      26.868  11.813  71.986  1.00 80.31           O  
ANISOU 5254  O   LYS B1146     9329  12005   9181  -1427    -72   1178       O  
ATOM   5255  CB  LYS B1146      23.697  12.026  72.949  1.00 64.74           C  
ANISOU 5255  CB  LYS B1146     7195  10251   7151  -1579      7   1335       C  
ATOM   5256  N   ARG B1147      26.468  13.958  72.533  1.00 71.15           N  
ANISOU 5256  N   ARG B1147     8034  10961   8037  -1332     68   1171       N  
ATOM   5257  CA  ARG B1147      27.538  14.492  71.706  1.00 69.70           C  
ANISOU 5257  CA  ARG B1147     7866  10725   7894  -1243     67   1105       C  
ATOM   5258  C   ARG B1147      28.907  14.096  72.271  1.00 76.62           C  
ANISOU 5258  C   ARG B1147     8836  11504   8772  -1205     34   1053       C  
ATOM   5259  O   ARG B1147      29.816  13.743  71.514  1.00 72.13           O  
ANISOU 5259  O   ARG B1147     8322  10858   8226  -1174    -12   1005       O  
ATOM   5260  CB  ARG B1147      27.456  16.016  71.653  1.00 68.89           C  
ANISOU 5260  CB  ARG B1147     7672  10685   7817  -1162    150   1086       C  
ATOM   5261  CG  ARG B1147      26.342  16.529  70.766  1.00 70.23           C  
ANISOU 5261  CG  ARG B1147     7749  10934   8001  -1179    175   1121       C  
ATOM   5262  CD  ARG B1147      26.462  18.014  70.515  1.00 78.28           C  
ANISOU 5262  CD  ARG B1147     8688  11999   9056  -1091    244   1092       C  
ATOM   5263  NE  ARG B1147      26.216  18.777  71.719  1.00 80.10           N  
ANISOU 5263  NE  ARG B1147     8872  12284   9278  -1068    309   1101       N  
ATOM   5264  CZ  ARG B1147      25.025  19.237  72.066  1.00 95.93           C  
ANISOU 5264  CZ  ARG B1147    10791  14381  11276  -1100    356   1147       C  
ATOM   5265  NH1 ARG B1147      23.963  19.012  71.304  1.00 97.98           N  
ANISOU 5265  NH1 ARG B1147    11002  14686  11538  -1158    343   1190       N  
ATOM   5266  NH2 ARG B1147      24.900  19.918  73.187  1.00108.62           N  
ANISOU 5266  NH2 ARG B1147    12362  16034  12875  -1075    416   1147       N  
ATOM   5267  N   VAL B1148      29.060  14.178  73.600  1.00 62.47           N  
ANISOU 5267  N   VAL B1148     7062   9716   6957  -1207     58   1061       N  
ATOM   5268  CA  VAL B1148      30.323  13.836  74.213  1.00 65.73           C  
ANISOU 5268  CA  VAL B1148     7564  10038   7374  -1173     28   1016       C  
ATOM   5269  C   VAL B1148      30.575  12.328  74.117  1.00 69.38           C  
ANISOU 5269  C   VAL B1148     8119  10420   7821  -1245    -67   1024       C  
ATOM   5270  O   VAL B1148      31.696  11.893  73.871  1.00 71.69           O  
ANISOU 5270  O   VAL B1148     8484  10618   8135  -1213   -116    972       O  
ATOM   5271  CB  VAL B1148      30.395  14.363  75.653  1.00 74.16           C  
ANISOU 5271  CB  VAL B1148     8624  11133   8419  -1157     79   1024       C  
ATOM   5272  CG1 VAL B1148      31.708  13.990  76.338  1.00 74.44           C  
ANISOU 5272  CG1 VAL B1148     8754  11070   8460  -1124     44    979       C  
ATOM   5273  CG2 VAL B1148      30.201  15.867  75.663  1.00 74.60           C  
ANISOU 5273  CG2 VAL B1148     8585  11262   8496  -1079    168   1010       C  
ATOM   5274  N   ILE B1149      29.531  11.528  74.307  1.00 75.89           N  
ANISOU 5274  N   ILE B1149     8940  11281   8612  -1344    -95   1087       N  
ATOM   5275  CA  ILE B1149      29.662  10.081  74.273  1.00 74.44           C  
ANISOU 5275  CA  ILE B1149     8841  11027   8415  -1420   -188   1101       C  
ATOM   5276  C   ILE B1149      30.046   9.628  72.869  1.00 69.16           C  
ANISOU 5276  C   ILE B1149     8197  10304   7778  -1407   -243   1066       C  
ATOM   5277  O   ILE B1149      30.852   8.710  72.745  1.00 71.42           O  
ANISOU 5277  O   ILE B1149     8567  10496   8073  -1417   -317   1035       O  
ATOM   5278  CB  ILE B1149      28.399   9.362  74.790  1.00 75.61           C  
ANISOU 5278  CB  ILE B1149     8975  11233   8520  -1530   -205   1182       C  
ATOM   5279  CG1 ILE B1149      28.126   9.666  76.259  1.00 86.04           C  
ANISOU 5279  CG1 ILE B1149    10286  12600   9805  -1550   -158   1213       C  
ATOM   5280  CG2 ILE B1149      28.577   7.877  74.627  1.00 72.68           C  
ANISOU 5280  CG2 ILE B1149     8691  10785   8141  -1604   -308   1194       C  
ATOM   5281  CD1 ILE B1149      26.783   9.179  76.712  1.00 94.93           C  
ANISOU 5281  CD1 ILE B1149    11378  13802  10889  -1653   -157   1293       C  
ATOM   5282  N   THR B1150      29.475  10.265  71.835  1.00 72.54           N  
ANISOU 5282  N   THR B1150     8551  10790   8222  -1385   -209   1070       N  
ATOM   5283  CA  THR B1150      29.801   9.942  70.447  1.00 79.64           C  
ANISOU 5283  CA  THR B1150     9466  11645   9147  -1371   -253   1035       C  
ATOM   5284  C   THR B1150      31.287  10.205  70.206  1.00 83.71           C  
ANISOU 5284  C   THR B1150    10032  12077   9697  -1283   -261    953       C  
ATOM   5285  O   THR B1150      31.967   9.414  69.554  1.00 86.47           O  
ANISOU 5285  O   THR B1150    10446  12348  10062  -1286   -328    914       O  
ATOM   5286  CB  THR B1150      28.946  10.728  69.434  1.00 79.19           C  
ANISOU 5286  CB  THR B1150     9317  11669   9102  -1359   -208   1054       C  
ATOM   5287  OG1 THR B1150      27.554  10.454  69.606  1.00 88.16           O  
ANISOU 5287  OG1 THR B1150    10406  12880  10211  -1442   -203   1130       O  
ATOM   5288  CG2 THR B1150      29.322  10.471  67.986  1.00 71.44           C  
ANISOU 5288  CG2 THR B1150     8353  10647   8146  -1341   -250   1015       C  
ATOM   5289  N   THR B1151      31.779  11.333  70.733  1.00 75.23           N  
ANISOU 5289  N   THR B1151     8926  11023   8635  -1204   -192    925       N  
ATOM   5290  CA  THR B1151      33.170  11.726  70.598  1.00 62.06           C  
ANISOU 5290  CA  THR B1151     7298   9283   7001  -1114   -190    850       C  
ATOM   5291  C   THR B1151      34.069  10.681  71.266  1.00 57.41           C  
ANISOU 5291  C   THR B1151     6812   8592   6410  -1134   -259    825       C  
ATOM   5292  O   THR B1151      35.135  10.378  70.759  1.00 54.68           O  
ANISOU 5292  O   THR B1151     6520   8162   6092  -1094   -298    763       O  
ATOM   5293  CB  THR B1151      33.351  13.170  71.092  1.00 65.74           C  
ANISOU 5293  CB  THR B1151     7701   9799   7478  -1032   -102    835       C  
ATOM   5294  OG1 THR B1151      32.448  13.987  70.344  1.00 67.33           O  
ANISOU 5294  OG1 THR B1151     7808  10089   7684  -1025    -52    861       O  
ATOM   5295  CG2 THR B1151      34.755  13.704  70.931  1.00 73.32           C  
ANISOU 5295  CG2 THR B1151     8692  10692   8475   -935    -93    759       C  
ATOM   5296  N   PHE B1152      33.663  10.139  72.418  1.00 63.98           N  
ANISOU 5296  N   PHE B1152     7671   9429   7209  -1197   -274    871       N  
ATOM   5297  CA  PHE B1152      34.396   9.049  73.058  1.00 76.59           C  
ANISOU 5297  CA  PHE B1152     9366  10930   8803  -1230   -349    856       C  
ATOM   5298  C   PHE B1152      34.359   7.770  72.217  1.00 77.79           C  
ANISOU 5298  C   PHE B1152     9571  11026   8961  -1291   -441    854       C  
ATOM   5299  O   PHE B1152      35.357   7.055  72.123  1.00 77.55           O  
ANISOU 5299  O   PHE B1152     9618  10894   8953  -1281   -505    805       O  
ATOM   5300  CB  PHE B1152      33.843   8.734  74.454  1.00 82.87           C  
ANISOU 5300  CB  PHE B1152    10175  11753   9557  -1295   -346    914       C  
ATOM   5301  CG  PHE B1152      34.319   9.658  75.544  1.00 79.33           C  
ANISOU 5301  CG  PHE B1152     9718  11318   9106  -1236   -283    899       C  
ATOM   5302  CD1 PHE B1152      35.664   9.732  75.873  1.00 79.84           C  
ANISOU 5302  CD1 PHE B1152     9844  11293   9199  -1171   -300    838       C  
ATOM   5303  CD2 PHE B1152      33.427  10.468  76.229  1.00 82.19           C  
ANISOU 5303  CD2 PHE B1152    10007  11781   9440  -1244   -207    945       C  
ATOM   5304  CE1 PHE B1152      36.107  10.589  76.869  1.00 80.67           C  
ANISOU 5304  CE1 PHE B1152     9941  11407   9302  -1116   -243    825       C  
ATOM   5305  CE2 PHE B1152      33.865  11.325  77.227  1.00 77.27           C  
ANISOU 5305  CE2 PHE B1152     9375  11171   8814  -1188   -149    930       C  
ATOM   5306  CZ  PHE B1152      35.205  11.386  77.537  1.00 81.31           C  
ANISOU 5306  CZ  PHE B1152     9951  11592   9353  -1124   -168    870       C  
ATOM   5307  N   ARG B1153      33.197   7.488  71.621  1.00 71.57           N  
ANISOU 5307  N   ARG B1153     8739  10301   8154  -1355   -447    906       N  
ATOM   5308  CA  ARG B1153      32.981   6.226  70.951  1.00 76.17           C  
ANISOU 5308  CA  ARG B1153     9368  10838   8736  -1425   -535    916       C  
ATOM   5309  C   ARG B1153      33.765   6.209  69.643  1.00 84.51           C  
ANISOU 5309  C   ARG B1153    10440  11840   9830  -1370   -560    846       C  
ATOM   5310  O   ARG B1153      34.361   5.187  69.307  1.00101.89           O  
ANISOU 5310  O   ARG B1153    12712  13954  12046  -1391   -641    814       O  
ATOM   5311  CB  ARG B1153      31.477   6.027  70.735  1.00 83.86           C  
ANISOU 5311  CB  ARG B1153    10284  11900   9678  -1506   -528    995       C  
ATOM   5312  CG  ARG B1153      31.069   4.665  70.190  1.00 74.20           C  
ANISOU 5312  CG  ARG B1153     9106  10639   8448  -1592   -622   1020       C  
ATOM   5313  CD  ARG B1153      29.556   4.605  70.007  1.00 69.87           C  
ANISOU 5313  CD  ARG B1153     8493  10184   7869  -1666   -606   1100       C  
ATOM   5314  NE  ARG B1153      29.053   5.475  68.959  1.00 74.26           N  
ANISOU 5314  NE  ARG B1153     8970  10806   8438  -1629   -552   1097       N  
ATOM   5315  CZ  ARG B1153      29.171   5.228  67.641  1.00 92.77           C  
ANISOU 5315  CZ  ARG B1153    11319  13127  10805  -1620   -586   1068       C  
ATOM   5316  NH1 ARG B1153      29.780   4.139  67.195  1.00 91.94           N  
ANISOU 5316  NH1 ARG B1153    11290  12932  10711  -1641   -674   1035       N  
ATOM   5317  NH2 ARG B1153      28.674   6.075  66.755  1.00 96.74           N  
ANISOU 5317  NH2 ARG B1153    11747  13694  11317  -1589   -535   1070       N  
ATOM   5318  N   THR B1154      33.752   7.331  68.909  1.00 86.33           N  
ANISOU 5318  N   THR B1154    10603  12122  10076  -1303   -492    824       N  
ATOM   5319  CA  THR B1154      34.275   7.372  67.546  1.00 92.33           C  
ANISOU 5319  CA  THR B1154    11366  12852  10866  -1261   -509    767       C  
ATOM   5320  C   THR B1154      35.650   8.041  67.464  1.00 89.15           C  
ANISOU 5320  C   THR B1154    10983  12393  10498  -1160   -483    686       C  
ATOM   5321  O   THR B1154      36.458   7.702  66.603  1.00 88.96           O  
ANISOU 5321  O   THR B1154    10996  12305  10500  -1131   -521    625       O  
ATOM   5322  CB  THR B1154      33.296   8.048  66.580  1.00 95.43           C  
ANISOU 5322  CB  THR B1154    11672  13335  11252  -1265   -463    798       C  
ATOM   5323  OG1 THR B1154      33.120   9.391  67.026  1.00 84.73           O  
ANISOU 5323  OG1 THR B1154    10245  12050   9897  -1208   -372    808       O  
ATOM   5324  CG2 THR B1154      31.968   7.329  66.515  1.00 95.83           C  
ANISOU 5324  CG2 THR B1154    11704  13434  11272  -1364   -495    875       C  
ATOM   5325  N   GLY B1155      35.912   9.002  68.350  1.00 84.04           N  
ANISOU 5325  N   GLY B1155    10310  11771   9852  -1106   -417    685       N  
ATOM   5326  CA  GLY B1155      37.155   9.750  68.286  1.00 78.12           C  
ANISOU 5326  CA  GLY B1155     9570  10976   9136  -1007   -387    613       C  
ATOM   5327  C   GLY B1155      37.115  10.822  67.193  1.00 74.51           C  
ANISOU 5327  C   GLY B1155     9043  10573   8696   -946   -330    591       C  
ATOM   5328  O   GLY B1155      38.166  11.254  66.718  1.00 69.43           O  
ANISOU 5328  O   GLY B1155     8412   9885   8084   -871   -320    524       O  
ATOM   5329  N   THR B1156      35.904  11.258  66.814  1.00 65.93           N  
ANISOU 5329  N   THR B1156     7879   9580   7589   -979   -293    647       N  
ATOM   5330  CA  THR B1156      35.739  12.259  65.774  1.00 62.13           C  
ANISOU 5330  CA  THR B1156     7328   9155   7123   -931   -244    634       C  
ATOM   5331  C   THR B1156      34.842  13.374  66.295  1.00 66.43           C  
ANISOU 5331  C   THR B1156     7785   9800   7657   -919   -166    685       C  
ATOM   5332  O   THR B1156      34.315  13.273  67.396  1.00 64.29           O  
ANISOU 5332  O   THR B1156     7509   9555   7364   -955   -153    730       O  
ATOM   5333  CB  THR B1156      35.154  11.641  64.504  1.00 55.61           C  
ANISOU 5333  CB  THR B1156     6497   8341   6291   -984   -287    645       C  
ATOM   5334  OG1 THR B1156      33.852  11.154  64.828  1.00 66.87           O  
ANISOU 5334  OG1 THR B1156     7899   9821   7686  -1071   -299    722       O  
ATOM   5335  CG2 THR B1156      35.991  10.509  63.956  1.00 53.95           C  
ANISOU 5335  CG2 THR B1156     6371   8034   6092   -998   -366    592       C  
ATOM   5336  N   TRP B1157      34.690  14.430  65.480  1.00 73.81           N  
ANISOU 5336  N   TRP B1157     8648  10788   8608   -871   -117    676       N  
ATOM   5337  CA  TRP B1157      33.861  15.587  65.802  1.00 73.88           C  
ANISOU 5337  CA  TRP B1157     8565  10893   8615   -852    -44    718       C  
ATOM   5338  C   TRP B1157      32.516  15.540  65.067  1.00 83.53           C  
ANISOU 5338  C   TRP B1157     9725  12189   9823   -916    -44    775       C  
ATOM   5339  O   TRP B1157      31.852  16.575  64.908  1.00 71.59           O  
ANISOU 5339  O   TRP B1157     8127  10756   8319   -895     12    801       O  
ATOM   5340  CB  TRP B1157      34.595  16.879  65.447  1.00 69.06           C  
ANISOU 5340  CB  TRP B1157     7912  10290   8036   -753     11    671       C  
ATOM   5341  CG  TRP B1157      35.943  17.017  66.070  1.00 69.66           C  
ANISOU 5341  CG  TRP B1157     8044  10293   8131   -684     13    613       C  
ATOM   5342  CD1 TRP B1157      37.150  16.976  65.440  1.00 65.12           C  
ANISOU 5342  CD1 TRP B1157     7514   9647   7582   -629     -8    544       C  
ATOM   5343  CD2 TRP B1157      36.215  17.236  67.464  1.00 69.34           C  
ANISOU 5343  CD2 TRP B1157     8019  10243   8085   -662     38    617       C  
ATOM   5344  NE1 TRP B1157      38.159  17.168  66.345  1.00 55.85           N  
ANISOU 5344  NE1 TRP B1157     6381   8418   6422   -573      2    507       N  
ATOM   5345  CE2 TRP B1157      37.622  17.329  67.592  1.00 57.55           C  
ANISOU 5345  CE2 TRP B1157     6581   8667   6618   -592     29    550       C  
ATOM   5346  CE3 TRP B1157      35.409  17.348  68.608  1.00 64.96           C  
ANISOU 5346  CE3 TRP B1157     7437   9739   7505   -697     67    670       C  
ATOM   5347  CZ2 TRP B1157      38.245  17.554  68.817  1.00 51.75           C  
ANISOU 5347  CZ2 TRP B1157     5876   7900   5886   -554     47    536       C  
ATOM   5348  CZ3 TRP B1157      36.026  17.579  69.817  1.00 65.74           C  
ANISOU 5348  CZ3 TRP B1157     7565   9809   7604   -661     87    655       C  
ATOM   5349  CH2 TRP B1157      37.424  17.686  69.912  1.00 57.42           C  
ANISOU 5349  CH2 TRP B1157     6567   8672   6577   -589     76    590       C  
ATOM   5350  N   ASP B1158      32.110  14.340  64.619  1.00 87.14           N  
ANISOU 5350  N   ASP B1158    10225  12622  10263   -994   -109    796       N  
ATOM   5351  CA  ASP B1158      30.885  14.162  63.854  1.00 76.74           C  
ANISOU 5351  CA  ASP B1158     8858  11365   8933  -1059   -119    849       C  
ATOM   5352  C   ASP B1158      29.673  14.649  64.649  1.00 79.36           C  
ANISOU 5352  C   ASP B1158     9118  11786   9250  -1093    -71    917       C  
ATOM   5353  O   ASP B1158      28.726  15.155  64.055  1.00 92.54           O  
ANISOU 5353  O   ASP B1158    10713  13525  10922  -1110    -46    954       O  
ATOM   5354  CB  ASP B1158      30.740  12.709  63.395  1.00 80.90           C  
ANISOU 5354  CB  ASP B1158     9454  11842   9444  -1136   -203    857       C  
ATOM   5355  CG  ASP B1158      31.691  12.354  62.273  1.00 91.48           C  
ANISOU 5355  CG  ASP B1158    10843  13113  10801  -1106   -245    792       C  
ATOM   5356  OD1 ASP B1158      32.643  13.135  62.076  1.00118.99           O  
ANISOU 5356  OD1 ASP B1158    14323  16577  14308  -1024   -212    736       O  
ATOM   5357  OD2 ASP B1158      31.480  11.303  61.607  1.00 91.36           O1-
ANISOU 5357  OD2 ASP B1158    10869  13067  10777  -1165   -311    797       O1-
ATOM   5358  N   ALA B1159      29.684  14.480  65.981  1.00 74.75           N  
ANISOU 5358  N   ALA B1159     8553  11199   8648  -1105    -58    934       N  
ATOM   5359  CA  ALA B1159      28.548  14.865  66.801  1.00 67.04           C  
ANISOU 5359  CA  ALA B1159     7512  10307   7655  -1141    -12    996       C  
ATOM   5360  C   ALA B1159      28.403  16.385  66.909  1.00 69.16           C  
ANISOU 5360  C   ALA B1159     7690  10642   7945  -1070     70    990       C  
ATOM   5361  O   ALA B1159      27.444  16.842  67.531  1.00 66.64           O  
ANISOU 5361  O   ALA B1159     7304  10399   7616  -1093    114   1037       O  
ATOM   5362  CB  ALA B1159      28.640  14.237  68.162  1.00 69.85           C  
ANISOU 5362  CB  ALA B1159     7917  10640   7982  -1177    -24   1014       C  
ATOM   5363  N   TYR B1160      29.335  17.154  66.306  1.00 60.78           N  
ANISOU 5363  N   TYR B1160     6624   9554   6914   -985     88    933       N  
ATOM   5364  CA  TYR B1160      29.287  18.604  66.341  1.00 55.11           C  
ANISOU 5364  CA  TYR B1160     5823   8893   6222   -913    159    924       C  
ATOM   5365  C   TYR B1160      29.179  19.179  64.936  1.00 61.09           C  
ANISOU 5365  C   TYR B1160     6534   9671   7006   -889    160    912       C  
ATOM   5366  O   TYR B1160      29.159  20.397  64.781  1.00 82.10           O  
ANISOU 5366  O   TYR B1160     9124  12376   9692   -829    212    903       O  
ATOM   5367  CB  TYR B1160      30.486  19.181  67.097  1.00 49.27           C  
ANISOU 5367  CB  TYR B1160     5114   8111   5497   -829    188    871       C  
ATOM   5368  CG  TYR B1160      30.417  18.950  68.581  1.00 50.94           C  
ANISOU 5368  CG  TYR B1160     5347   8324   5684   -847    204    889       C  
ATOM   5369  CD1 TYR B1160      30.767  17.724  69.124  1.00 54.45           C  
ANISOU 5369  CD1 TYR B1160     5881   8703   6102   -897    149    890       C  
ATOM   5370  CD2 TYR B1160      29.962  19.934  69.449  1.00 58.22           C  
ANISOU 5370  CD2 TYR B1160     6200   9314   6608   -818    271    907       C  
ATOM   5371  CE1 TYR B1160      30.666  17.464  70.481  1.00 60.15           C  
ANISOU 5371  CE1 TYR B1160     6628   9429   6799   -922    160    911       C  
ATOM   5372  CE2 TYR B1160      29.847  19.700  70.813  1.00 62.20           C  
ANISOU 5372  CE2 TYR B1160     6725   9825   7085   -841    287    926       C  
ATOM   5373  CZ  TYR B1160      30.217  18.465  71.334  1.00 67.72           C  
ANISOU 5373  CZ  TYR B1160     7517  10459   7756   -894    231    929       C  
ATOM   5374  OH  TYR B1160      30.094  18.213  72.676  1.00 69.84           O  
ANISOU 5374  OH  TYR B1160     7809  10735   7994   -922    244    950       O  
ATOM   5375  N   SER B 261      29.128  18.314  63.921  1.00 62.76           N  
ANISOU 5375  N   SER B 261     6786   9851   7211   -935    102    912       N  
ATOM   5376  CA  SER B 261      29.072  18.749  62.530  1.00 72.98           C  
ANISOU 5376  CA  SER B 261     8045  11159   8525   -919     96    899       C  
ATOM   5377  C   SER B 261      27.630  19.026  62.098  1.00 83.62           C  
ANISOU 5377  C   SER B 261     9310  12590   9872   -973    110    963       C  
ATOM   5378  O   SER B 261      26.703  18.374  62.568  1.00109.99           O  
ANISOU 5378  O   SER B 261    12646  15956  13190  -1046     96   1015       O  
ATOM   5379  CB  SER B 261      29.716  17.713  61.637  1.00 74.42           C  
ANISOU 5379  CB  SER B 261     8308  11267   8700   -942     29    865       C  
ATOM   5380  OG  SER B 261      29.763  18.136  60.284  1.00 92.45           O  
ANISOU 5380  OG  SER B 261    10565  13563  11000   -924     24    848       O  
ATOM   5381  N   GLU B 262      27.455  19.968  61.167  1.00 85.26           N  
ANISOU 5381  N   GLU B 262     9454  12836  10106   -939    133    959       N  
ATOM   5382  CA  GLU B 262      26.158  20.249  60.562  1.00 75.64           C  
ANISOU 5382  CA  GLU B 262     8158  11688   8893   -988    138   1014       C  
ATOM   5383  C   GLU B 262      25.966  19.365  59.329  1.00 64.71           C  
ANISOU 5383  C   GLU B 262     6812  10277   7497  -1045     75   1020       C  
ATOM   5384  O   GLU B 262      26.889  19.181  58.559  1.00 69.65           O  
ANISOU 5384  O   GLU B 262     7488  10849   8126  -1016     48    971       O  
ATOM   5385  CB  GLU B 262      26.102  21.725  60.169  1.00 76.29           C  
ANISOU 5385  CB  GLU B 262     8153  11821   9011   -923    189   1006       C  
ATOM   5386  CG  GLU B 262      26.030  22.676  61.355  1.00 92.18           C  
ANISOU 5386  CG  GLU B 262    10111  13875  11039   -873    253   1008       C  
ATOM   5387  CD  GLU B 262      25.428  24.058  61.090  1.00105.27           C  
ANISOU 5387  CD  GLU B 262    11659  15605  12734   -836    302   1024       C  
ATOM   5388  OE1 GLU B 262      26.179  24.955  60.668  1.00 98.59           O  
ANISOU 5388  OE1 GLU B 262    10796  14749  11914   -763    320    985       O  
ATOM   5389  OE2 GLU B 262      24.198  24.243  61.298  1.00120.03           O1-
ANISOU 5389  OE2 GLU B 262    13458  17540  14607   -881    319   1076       O1-
ATOM   5390  N   GLN B 263      24.762  18.840  59.118  1.00 73.66           N  
ANISOU 5390  N   GLN B 263     7920  11449   8619  -1125     53   1079       N  
ATOM   5391  CA  GLN B 263      24.534  17.836  58.078  1.00 72.32           C  
ANISOU 5391  CA  GLN B 263     7795  11249   8434  -1187    -12   1089       C  
ATOM   5392  C   GLN B 263      24.505  18.453  56.680  1.00 59.89           C  
ANISOU 5392  C   GLN B 263     6185   9691   6879  -1170    -17   1078       C  
ATOM   5393  O   GLN B 263      24.701  17.736  55.698  1.00 51.70           O  
ANISOU 5393  O   GLN B 263     5196   8617   5831  -1200    -69   1064       O  
ATOM   5394  CB  GLN B 263      23.259  17.028  58.321  1.00 93.05           C  
ANISOU 5394  CB  GLN B 263    10409  13907  11040  -1281    -38   1158       C  
ATOM   5395  N   TRP B 264      24.295  19.769  56.591  1.00 50.99           N  
ANISOU 5395  N   TRP B 264     4974   8617   5780  -1121     36   1082       N  
ATOM   5396  CA  TRP B 264      24.303  20.407  55.287  1.00 55.61           C  
ANISOU 5396  CA  TRP B 264     5526   9219   6385  -1104     31   1072       C  
ATOM   5397  C   TRP B 264      25.709  20.566  54.734  1.00 63.45           C  
ANISOU 5397  C   TRP B 264     6573  10155   7381  -1040     24   1000       C  
ATOM   5398  O   TRP B 264      25.850  20.786  53.539  1.00 72.08           O  
ANISOU 5398  O   TRP B 264     7661  11247   8479  -1038      6    986       O  
ATOM   5399  CB  TRP B 264      23.573  21.748  55.289  1.00 58.74           C  
ANISOU 5399  CB  TRP B 264     5813   9689   6815  -1078     81   1103       C  
ATOM   5400  CG  TRP B 264      24.195  22.808  56.130  1.00 59.13           C  
ANISOU 5400  CG  TRP B 264     5830   9751   6887   -994    140   1072       C  
ATOM   5401  CD1 TRP B 264      23.913  23.059  57.434  1.00 70.35           C  
ANISOU 5401  CD1 TRP B 264     7221  11198   8309   -982    181   1088       C  
ATOM   5402  CD2 TRP B 264      25.144  23.805  55.730  1.00 64.58           C  
ANISOU 5402  CD2 TRP B 264     6507  10431   7602   -913    164   1024       C  
ATOM   5403  NE1 TRP B 264      24.640  24.131  57.885  1.00 67.91           N  
ANISOU 5403  NE1 TRP B 264     6884  10893   8025   -896    228   1051       N  
ATOM   5404  CE2 TRP B 264      25.412  24.602  56.867  1.00 65.44           C  
ANISOU 5404  CE2 TRP B 264     6580  10556   7726   -852    218   1012       C  
ATOM   5405  CE3 TRP B 264      25.812  24.098  54.536  1.00 80.08           C  
ANISOU 5405  CE3 TRP B 264     8485  12371   9571   -886    145    989       C  
ATOM   5406  CZ2 TRP B 264      26.327  25.650  56.860  1.00 71.41           C  
ANISOU 5406  CZ2 TRP B 264     7318  11305   8509   -765    251    967       C  
ATOM   5407  CZ3 TRP B 264      26.716  25.141  54.526  1.00 87.57           C  
ANISOU 5407  CZ3 TRP B 264     9414  13314  10544   -802    179    946       C  
ATOM   5408  CH2 TRP B 264      26.974  25.900  55.672  1.00 82.24           C  
ANISOU 5408  CH2 TRP B 264     8706  12654   9888   -741    230    936       C  
ATOM   5409  N   ILE B 265      26.737  20.507  55.589  1.00 71.64           N  
ANISOU 5409  N   ILE B 265     7658  11148   8416   -988     40    955       N  
ATOM   5410  CA  ILE B 265      28.105  20.672  55.123  1.00 67.31           C  
ANISOU 5410  CA  ILE B 265     7159  10545   7873   -925     36    884       C  
ATOM   5411  C   ILE B 265      28.521  19.519  54.208  1.00 70.75           C  
ANISOU 5411  C   ILE B 265     7674  10922   8285   -965    -28    857       C  
ATOM   5412  O   ILE B 265      29.114  19.750  53.161  1.00 62.79           O  
ANISOU 5412  O   ILE B 265     6677   9898   7281   -941    -39    818       O  
ATOM   5413  CB  ILE B 265      29.070  20.853  56.295  1.00 73.39           C  
ANISOU 5413  CB  ILE B 265     7960  11277   8647   -861     65    845       C  
ATOM   5414  CG1 ILE B 265      28.683  22.076  57.125  1.00 77.64           C  
ANISOU 5414  CG1 ILE B 265     8416  11875   9209   -816    129    868       C  
ATOM   5415  CG2 ILE B 265      30.483  20.984  55.763  1.00 75.20           C  
ANISOU 5415  CG2 ILE B 265     8241  11448   8885   -798     59    771       C  
ATOM   5416  CD1 ILE B 265      29.024  23.386  56.462  1.00 67.95           C  
ANISOU 5416  CD1 ILE B 265     7129  10676   8014   -750    163    847       C  
ATOM   5417  N   PHE B 266      28.203  18.283  54.585  1.00 65.49           N  
ANISOU 5417  N   PHE B 266     7062  10226   7595  -1028    -71    875       N  
ATOM   5418  CA  PHE B 266      28.558  17.153  53.749  1.00 61.72           C  
ANISOU 5418  CA  PHE B 266     6659   9693   7098  -1068   -135    848       C  
ATOM   5419  C   PHE B 266      27.777  17.200  52.436  1.00 71.96           C  
ANISOU 5419  C   PHE B 266     7922  11027   8392  -1115   -158    877       C  
ATOM   5420  O   PHE B 266      28.239  16.693  51.422  1.00 76.34           O  
ANISOU 5420  O   PHE B 266     8523  11546   8936  -1126   -198    842       O  
ATOM   5421  CB  PHE B 266      28.209  15.879  54.508  1.00 63.81           C  
ANISOU 5421  CB  PHE B 266     6978   9925   7340  -1131   -178    873       C  
ATOM   5422  CG  PHE B 266      28.618  14.586  53.859  1.00 68.73           C  
ANISOU 5422  CG  PHE B 266     7686  10483   7946  -1173   -249    843       C  
ATOM   5423  CD1 PHE B 266      29.859  14.040  54.137  1.00 77.22           C  
ANISOU 5423  CD1 PHE B 266     8838  11481   9022  -1138   -271    777       C  
ATOM   5424  CD2 PHE B 266      27.763  13.901  53.006  1.00 69.36           C  
ANISOU 5424  CD2 PHE B 266     7767  10576   8011  -1247   -296    879       C  
ATOM   5425  CE1 PHE B 266      30.245  12.830  53.577  1.00 82.01           C  
ANISOU 5425  CE1 PHE B 266     9520  12023   9615  -1175   -339    746       C  
ATOM   5426  CE2 PHE B 266      28.162  12.714  52.412  1.00 76.47           C  
ANISOU 5426  CE2 PHE B 266     8745  11415   8897  -1282   -364    848       C  
ATOM   5427  CZ  PHE B 266      29.401  12.182  52.700  1.00 83.00           C  
ANISOU 5427  CZ  PHE B 266     9646  12165   9726  -1246   -385    780       C  
ATOM   5428  N   ARG B 267      26.567  17.779  52.442  1.00 79.33           N  
ANISOU 5428  N   ARG B 267     8776  12032   9335  -1145   -135    942       N  
ATOM   5429  CA  ARG B 267      25.803  17.942  51.207  1.00 79.16           C  
ANISOU 5429  CA  ARG B 267     8716  12048   9314  -1187   -156    972       C  
ATOM   5430  C   ARG B 267      26.437  19.010  50.318  1.00 76.21           C  
ANISOU 5430  C   ARG B 267     8313  11686   8957  -1127   -130    934       C  
ATOM   5431  O   ARG B 267      26.180  19.052  49.117  1.00 74.56           O  
ANISOU 5431  O   ARG B 267     8095  11490   8745  -1154   -155    939       O  
ATOM   5432  CB  ARG B 267      24.338  18.339  51.454  1.00 76.63           C  
ANISOU 5432  CB  ARG B 267     8313  11800   9004  -1232   -138   1051       C  
ATOM   5433  CG  ARG B 267      23.451  17.253  52.043  1.00 70.48           C  
ANISOU 5433  CG  ARG B 267     7554  11020   8206  -1310   -170   1102       C  
ATOM   5434  CD  ARG B 267      23.318  16.008  51.203  1.00 68.37           C  
ANISOU 5434  CD  ARG B 267     7351  10713   7914  -1376   -242   1104       C  
ATOM   5435  NE  ARG B 267      22.426  15.154  51.962  1.00 76.32           N  
ANISOU 5435  NE  ARG B 267     8364  11727   8906  -1444   -264   1159       N  
ATOM   5436  CZ  ARG B 267      21.103  15.135  51.855  1.00 79.22           C  
ANISOU 5436  CZ  ARG B 267     8676  12147   9277  -1505   -269   1229       C  
ATOM   5437  NH1 ARG B 267      20.484  15.918  50.983  1.00 77.34           N  
ANISOU 5437  NH1 ARG B 267     8372  11956   9058  -1509   -257   1253       N  
ATOM   5438  NH2 ARG B 267      20.410  14.315  52.627  1.00 74.90           N  
ANISOU 5438  NH2 ARG B 267     8140  11602   8715  -1564   -289   1274       N  
ATOM   5439  N   LEU B 268      27.252  19.892  50.908  1.00 67.56           N  
ANISOU 5439  N   LEU B 268     7202  10589   7881  -1048    -82    898       N  
ATOM   5440  CA  LEU B 268      27.901  20.925  50.116  1.00 62.33           C  
ANISOU 5440  CA  LEU B 268     6511   9936   7235   -990    -58    863       C  
ATOM   5441  C   LEU B 268      29.182  20.370  49.500  1.00 61.81           C  
ANISOU 5441  C   LEU B 268     6526   9803   7154   -965    -85    789       C  
ATOM   5442  O   LEU B 268      29.608  20.832  48.458  1.00 62.46           O  
ANISOU 5442  O   LEU B 268     6603   9890   7238   -946    -87    762       O  
ATOM   5443  CB  LEU B 268      28.184  22.143  50.992  1.00 65.02           C  
ANISOU 5443  CB  LEU B 268     6794  10304   7606   -915      4    857       C  
ATOM   5444  CG  LEU B 268      28.581  23.410  50.253  1.00 65.75           C  
ANISOU 5444  CG  LEU B 268     6836  10425   7723   -860     32    838       C  
ATOM   5445  CD1 LEU B 268      27.574  23.730  49.163  1.00 72.85           C  
ANISOU 5445  CD1 LEU B 268     7680  11375   8626   -911     14    885       C  
ATOM   5446  CD2 LEU B 268      28.681  24.559  51.233  1.00 70.91           C  
ANISOU 5446  CD2 LEU B 268     7427  11109   8408   -793     90    842       C  
ATOM   5447  N   TYR B 269      29.784  19.366  50.138  1.00 68.06           N  
ANISOU 5447  N   TYR B 269     7393  10534   7931   -968   -109    757       N  
ATOM   5448  CA  TYR B 269      30.893  18.643  49.538  1.00 64.78           C  
ANISOU 5448  CA  TYR B 269     7059  10052   7502   -956   -144    688       C  
ATOM   5449  C   TYR B 269      30.430  17.810  48.346  1.00 64.65           C  
ANISOU 5449  C   TYR B 269     7070  10031   7462  -1027   -199    696       C  
ATOM   5450  O   TYR B 269      31.116  17.778  47.333  1.00 74.12           O  
ANISOU 5450  O   TYR B 269     8298  11209   8654  -1014   -214    647       O  
ATOM   5451  CB  TYR B 269      31.629  17.788  50.571  1.00 65.94           C  
ANISOU 5451  CB  TYR B 269     7278  10132   7645   -942   -158    653       C  
ATOM   5452  CG  TYR B 269      32.223  18.548  51.736  1.00 62.18           C  
ANISOU 5452  CG  TYR B 269     6785   9651   7190   -870   -107    637       C  
ATOM   5453  CD1 TYR B 269      32.678  19.854  51.603  1.00 53.50           C  
ANISOU 5453  CD1 TYR B 269     5633   8580   6113   -800    -56    619       C  
ATOM   5454  CD2 TYR B 269      32.350  17.932  52.974  1.00 60.01           C  
ANISOU 5454  CD2 TYR B 269     6548   9341   6911   -874   -113    640       C  
ATOM   5455  CE1 TYR B 269      33.211  20.536  52.684  1.00 53.44           C  
ANISOU 5455  CE1 TYR B 269     5612   8568   6126   -734    -11    605       C  
ATOM   5456  CE2 TYR B 269      32.898  18.598  54.057  1.00 56.86           C  
ANISOU 5456  CE2 TYR B 269     6138   8936   6530   -810    -67    626       C  
ATOM   5457  CZ  TYR B 269      33.321  19.905  53.914  1.00 56.57           C  
ANISOU 5457  CZ  TYR B 269     6048   8929   6517   -739    -16    608       C  
ATOM   5458  OH  TYR B 269      33.845  20.545  55.004  1.00 67.74           O  
ANISOU 5458  OH  TYR B 269     7452  10337   7950   -675     26    594       O  
ATOM   5459  N   VAL B 270      29.278  17.146  48.451  1.00 66.43           N  
ANISOU 5459  N   VAL B 270     7287  10276   7675  -1101   -229    757       N  
ATOM   5460  CA  VAL B 270      28.807  16.294  47.365  1.00 79.56           C  
ANISOU 5460  CA  VAL B 270     8980  11933   9316  -1170   -286    767       C  
ATOM   5461  C   VAL B 270      28.384  17.174  46.194  1.00 73.52           C  
ANISOU 5461  C   VAL B 270     8158  11221   8556  -1175   -274    785       C  
ATOM   5462  O   VAL B 270      28.416  16.726  45.051  1.00 83.91           O  
ANISOU 5462  O   VAL B 270     9503  12527   9854  -1209   -313    769       O  
ATOM   5463  CB  VAL B 270      27.684  15.309  47.771  1.00 85.08           C  
ANISOU 5463  CB  VAL B 270     9688  12636  10002  -1251   -326    829       C  
ATOM   5464  CG1 VAL B 270      28.099  14.269  48.809  1.00 78.96           C  
ANISOU 5464  CG1 VAL B 270     8980  11803   9219  -1259   -352    812       C  
ATOM   5465  CG2 VAL B 270      26.458  16.044  48.251  1.00 98.74           C  
ANISOU 5465  CG2 VAL B 270    11332  14439  11747  -1271   -291    906       C  
ATOM   5466  N   ALA B 271      27.997  18.424  46.478  1.00 65.75           N  
ANISOU 5466  N   ALA B 271     7092  10293   7595  -1141   -223    818       N  
ATOM   5467  CA  ALA B 271      27.673  19.360  45.406  1.00 66.94           C  
ANISOU 5467  CA  ALA B 271     7186  10493   7754  -1141   -211    834       C  
ATOM   5468  C   ALA B 271      28.936  19.905  44.720  1.00 69.05           C  
ANISOU 5468  C   ALA B 271     7475  10739   8021  -1080   -196    763       C  
ATOM   5469  O   ALA B 271      28.853  20.369  43.574  1.00 64.19           O  
ANISOU 5469  O   ALA B 271     6838  10150   7402  -1091   -203    764       O  
ATOM   5470  CB  ALA B 271      26.768  20.453  45.927  1.00 60.32           C  
ANISOU 5470  CB  ALA B 271     6253   9720   6946  -1130   -169    894       C  
ATOM   5471  N   ILE B 272      30.095  19.821  45.406  1.00 69.82           N  
ANISOU 5471  N   ILE B 272     7616  10789   8123  -1019   -177    704       N  
ATOM   5472  CA  ILE B 272      31.378  20.264  44.872  1.00 57.25           C  
ANISOU 5472  CA  ILE B 272     6048   9171   6532   -959   -162    633       C  
ATOM   5473  C   ILE B 272      32.037  19.117  44.118  1.00 57.99           C  
ANISOU 5473  C   ILE B 272     6227   9208   6598   -986   -210    576       C  
ATOM   5474  O   ILE B 272      32.426  19.298  42.969  1.00 59.16           O  
ANISOU 5474  O   ILE B 272     6383   9362   6734   -987   -219    545       O  
ATOM   5475  CB  ILE B 272      32.303  20.819  45.968  1.00 53.00           C  
ANISOU 5475  CB  ILE B 272     5510   8609   6017   -877   -117    597       C  
ATOM   5476  CG1 ILE B 272      31.784  22.158  46.514  1.00 53.11           C  
ANISOU 5476  CG1 ILE B 272     5435   8684   6063   -840    -65    642       C  
ATOM   5477  CG2 ILE B 272      33.703  20.966  45.420  1.00 53.18           C  
ANISOU 5477  CG2 ILE B 272     5576   8592   6039   -822   -110    516       C  
ATOM   5478  CD1 ILE B 272      32.523  22.714  47.722  1.00 43.22           C  
ANISOU 5478  CD1 ILE B 272     4176   7412   4833   -763    -21    617       C  
ATOM   5479  N   GLY B 273      32.168  17.952  44.771  1.00 55.03           N  
ANISOU 5479  N   GLY B 273     5913   8781   6214  -1007   -242    562       N  
ATOM   5480  CA  GLY B 273      32.772  16.786  44.147  1.00 55.98           C  
ANISOU 5480  CA  GLY B 273     6115   8843   6312  -1033   -292    506       C  
ATOM   5481  C   GLY B 273      32.049  16.289  42.889  1.00 62.02           C  
ANISOU 5481  C   GLY B 273     6884   9629   7051  -1106   -337    528       C  
ATOM   5482  O   GLY B 273      32.701  15.982  41.911  1.00 72.16           O  
ANISOU 5482  O   GLY B 273     8208  10890   8318  -1108   -358    473       O  
ATOM   5483  N   TRP B 274      30.713  16.187  42.892  1.00 66.23           N  
ANISOU 5483  N   TRP B 274     7379  10205   7581  -1168   -353    606       N  
ATOM   5484  CA  TRP B 274      29.978  15.653  41.746  1.00 61.25           C  
ANISOU 5484  CA  TRP B 274     6755   9589   6926  -1240   -400    631       C  
ATOM   5485  C   TRP B 274      29.214  16.747  40.988  1.00 60.22           C  
ANISOU 5485  C   TRP B 274     6549   9531   6801  -1253   -378    681       C  
ATOM   5486  O   TRP B 274      28.872  16.582  39.817  1.00 46.70           O  
ANISOU 5486  O   TRP B 274     4841   7834   5069  -1299   -408    687       O  
ATOM   5487  CB  TRP B 274      29.001  14.576  42.209  1.00 62.58           C  
ANISOU 5487  CB  TRP B 274     6943   9746   7086  -1309   -445    683       C  
ATOM   5488  CG  TRP B 274      29.636  13.416  42.906  1.00 65.24           C  
ANISOU 5488  CG  TRP B 274     7356  10013   7419  -1308   -478    640       C  
ATOM   5489  CD1 TRP B 274      29.532  13.085  44.225  1.00 62.61           C  
ANISOU 5489  CD1 TRP B 274     7032   9660   7098  -1302   -473    661       C  
ATOM   5490  CD2 TRP B 274      30.454  12.403  42.305  1.00 63.63           C  
ANISOU 5490  CD2 TRP B 274     7232   9747   7198  -1317   -525    570       C  
ATOM   5491  NE1 TRP B 274      30.228  11.933  44.484  1.00 65.16           N  
ANISOU 5491  NE1 TRP B 274     7434   9910   7413  -1308   -517    611       N  
ATOM   5492  CE2 TRP B 274      30.796  11.487  43.326  1.00 61.98           C  
ANISOU 5492  CE2 TRP B 274     7075   9480   6995  -1316   -550    554       C  
ATOM   5493  CE3 TRP B 274      30.903  12.173  41.004  1.00 62.55           C  
ANISOU 5493  CE3 TRP B 274     7125   9599   7041  -1328   -550    520       C  
ATOM   5494  CZ2 TRP B 274      31.586  10.367  43.092  1.00 60.99           C  
ANISOU 5494  CZ2 TRP B 274     7029   9284   6862  -1322   -600    487       C  
ATOM   5495  CZ3 TRP B 274      31.683  11.062  40.764  1.00 67.75           C  
ANISOU 5495  CZ3 TRP B 274     7862  10190   7689  -1334   -596    452       C  
ATOM   5496  CH2 TRP B 274      32.020  10.175  41.795  1.00 68.36           C  
ANISOU 5496  CH2 TRP B 274     7989  10208   7778  -1330   -622    435       C  
ATOM   5497  N   GLY B 275      28.915  17.863  41.671  1.00 64.02           N  
ANISOU 5497  N   GLY B 275     6960  10055   7311  -1214   -327    718       N  
ATOM   5498  CA  GLY B 275      28.101  18.934  41.109  1.00 62.27           C  
ANISOU 5498  CA  GLY B 275     6658   9900   7102  -1227   -308    772       C  
ATOM   5499  C   GLY B 275      28.879  19.895  40.220  1.00 56.82           C  
ANISOU 5499  C   GLY B 275     5950   9225   6412  -1183   -284    732       C  
ATOM   5500  O   GLY B 275      28.497  20.153  39.084  1.00 54.47           O  
ANISOU 5500  O   GLY B 275     5635   8958   6102  -1220   -303    749       O  
ATOM   5501  N   VAL B 276      29.989  20.407  40.741  1.00 60.36           N  
ANISOU 5501  N   VAL B 276     6407   9653   6873  -1107   -245    679       N  
ATOM   5502  CA  VAL B 276      30.774  21.389  40.005  1.00 71.76           C  
ANISOU 5502  CA  VAL B 276     7832  11114   8321  -1061   -218    642       C  
ATOM   5503  C   VAL B 276      31.381  20.822  38.712  1.00 70.79           C  
ANISOU 5503  C   VAL B 276     7766  10968   8162  -1087   -252    589       C  
ATOM   5504  O   VAL B 276      31.349  21.511  37.697  1.00 69.90           O  
ANISOU 5504  O   VAL B 276     7625  10892   8042  -1095   -250    593       O  
ATOM   5505  CB  VAL B 276      31.828  22.056  40.899  1.00 70.31           C  
ANISOU 5505  CB  VAL B 276     7643  10910   8161   -971   -170    598       C  
ATOM   5506  CG1 VAL B 276      32.786  22.946  40.106  1.00 62.23           C  
ANISOU 5506  CG1 VAL B 276     6610   9896   7138   -924   -146    552       C  
ATOM   5507  CG2 VAL B 276      31.161  22.786  42.055  1.00 67.27           C  
ANISOU 5507  CG2 VAL B 276     7191  10558   7811   -946   -133    653       C  
ATOM   5508  N   PRO B 277      31.947  19.589  38.662  1.00 61.60           N  
ANISOU 5508  N   PRO B 277     9027   5832   8547    928   -375    403       N  
ATOM   5509  CA  PRO B 277      32.369  19.021  37.383  1.00 64.13           C  
ANISOU 5509  CA  PRO B 277     9296   6118   8952    888   -313    372       C  
ATOM   5510  C   PRO B 277      31.269  19.064  36.316  1.00 68.60           C  
ANISOU 5510  C   PRO B 277     9838   6710   9516    832   -271    404       C  
ATOM   5511  O   PRO B 277      31.530  19.363  35.140  1.00 67.83           O  
ANISOU 5511  O   PRO B 277     9765   6595   9413    806   -287    399       O  
ATOM   5512  CB  PRO B 277      32.668  17.556  37.733  1.00 59.09           C  
ANISOU 5512  CB  PRO B 277     8663   5413   8375    904   -264    297       C  
ATOM   5513  CG  PRO B 277      33.096  17.610  39.157  1.00 62.75           C  
ANISOU 5513  CG  PRO B 277     9172   5872   8797    961   -318    293       C  
ATOM   5514  CD  PRO B 277      32.243  18.691  39.794  1.00 64.17           C  
ANISOU 5514  CD  PRO B 277     9389   6113   8878    971   -376    357       C  
ATOM   5515  N   LEU B 278      30.038  18.750  36.733  1.00 58.84           N  
ANISOU 5515  N   LEU B 278     8634   5492   8231    830   -264    420       N  
ATOM   5516  CA  LEU B 278      28.935  18.740  35.791  1.00 65.11           C  
ANISOU 5516  CA  LEU B 278     9446   6303   8990    783   -243    446       C  
ATOM   5517  C   LEU B 278      28.733  20.130  35.185  1.00 70.04           C  
ANISOU 5517  C   LEU B 278    10076   6986   9548    762   -289    521       C  
ATOM   5518  O   LEU B 278      28.110  20.282  34.133  1.00 74.52           O  
ANISOU 5518  O   LEU B 278    10702   7552  10059    724   -293    543       O  
ATOM   5519  CB  LEU B 278      27.688  18.303  36.547  1.00 51.83           C  
ANISOU 5519  CB  LEU B 278     7782   4648   7264    787   -226    459       C  
ATOM   5520  CG  LEU B 278      26.700  17.401  35.817  1.00 47.75           C  
ANISOU 5520  CG  LEU B 278     7321   4105   6719    755   -181    433       C  
ATOM   5521  CD1 LEU B 278      27.321  16.398  34.843  1.00 43.57           C  
ANISOU 5521  CD1 LEU B 278     6842   3486   6227    741   -143    347       C  
ATOM   5522  CD2 LEU B 278      25.916  16.641  36.862  1.00 57.55           C  
ANISOU 5522  CD2 LEU B 278     8563   5355   7946    775   -160    418       C  
ATOM   5523  N   LEU B 279      29.253  21.145  35.864  1.00 69.17           N  
ANISOU 5523  N   LEU B 279     9918   6928   9434    785   -325    560       N  
ATOM   5524  CA  LEU B 279      28.895  22.499  35.491  1.00 67.84           C  
ANISOU 5524  CA  LEU B 279     9736   6835   9204    764   -362    635       C  
ATOM   5525  C   LEU B 279      29.798  23.021  34.380  1.00 57.23           C  
ANISOU 5525  C   LEU B 279     8409   5474   7863    749   -402    634       C  
ATOM   5526  O   LEU B 279      29.429  23.956  33.679  1.00 54.37           O  
ANISOU 5526  O   LEU B 279     8054   5162   7443    718   -437    692       O  
ATOM   5527  CB  LEU B 279      28.917  23.396  36.730  1.00 77.30           C  
ANISOU 5527  CB  LEU B 279    10973   8067  10331    808   -431    649       C  
ATOM   5528  CG  LEU B 279      27.910  24.536  36.644  1.00 75.76           C  
ANISOU 5528  CG  LEU B 279    10779   7952  10055    784   -455    718       C  
ATOM   5529  CD1 LEU B 279      27.363  24.851  38.017  1.00 64.50           C  
ANISOU 5529  CD1 LEU B 279     9409   6537   8562    822   -492    709       C  
ATOM   5530  CD2 LEU B 279      28.523  25.767  35.967  1.00 86.81           C  
ANISOU 5530  CD2 LEU B 279    12137   9400  11447    766   -491    760       C  
ATOM   5531  N   PHE B 280      30.982  22.422  34.216  1.00 52.40           N  
ANISOU 5531  N   PHE B 280     7804   4790   7314    766   -404    567       N  
ATOM   5532  CA  PHE B 280      31.845  22.844  33.121  1.00 45.54           C  
ANISOU 5532  CA  PHE B 280     6957   3895   6452    746   -460    553       C  
ATOM   5533  C   PHE B 280      32.100  21.731  32.113  1.00 43.01           C  
ANISOU 5533  C   PHE B 280     6693   3473   6175    716   -446    475       C  
ATOM   5534  O   PHE B 280      32.467  22.037  30.989  1.00 36.52           O  
ANISOU 5534  O   PHE B 280     5895   2624   5357    670   -498    469       O  
ATOM   5535  CB  PHE B 280      33.174  23.419  33.597  1.00 45.27           C  
ANISOU 5535  CB  PHE B 280     6875   3872   6451    779   -493    540       C  
ATOM   5536  CG  PHE B 280      34.039  22.524  34.450  1.00 56.60           C  
ANISOU 5536  CG  PHE B 280     8291   5261   7954    819   -451    476       C  
ATOM   5537  CD1 PHE B 280      34.992  21.673  33.892  1.00 57.15           C  
ANISOU 5537  CD1 PHE B 280     8379   5249   8086    819   -449    394       C  
ATOM   5538  CD2 PHE B 280      33.958  22.594  35.846  1.00 59.31           C  
ANISOU 5538  CD2 PHE B 280     8618   5632   8286    856   -442    489       C  
ATOM   5539  CE1 PHE B 280      35.811  20.903  34.723  1.00 57.89           C  
ANISOU 5539  CE1 PHE B 280     8449   5311   8235    854   -404    344       C  
ATOM   5540  CE2 PHE B 280      34.764  21.817  36.676  1.00 49.01           C  
ANISOU 5540  CE2 PHE B 280     7334   4273   7015    896   -446    429       C  
ATOM   5541  CZ  PHE B 280      35.694  20.968  36.109  1.00 50.37           C  
ANISOU 5541  CZ  PHE B 280     7484   4389   7265    890   -398    368       C  
ATOM   5542  N   VAL B 281      31.863  20.470  32.489  1.00 46.09           N  
ANISOU 5542  N   VAL B 281     7098   3810   6602    729   -377    414       N  
ATOM   5543  CA  VAL B 281      32.094  19.368  31.575  1.00 46.15           C  
ANISOU 5543  CA  VAL B 281     7156   3725   6655    694   -343    322       C  
ATOM   5544  C   VAL B 281      31.028  19.354  30.491  1.00 50.28           C  
ANISOU 5544  C   VAL B 281     7758   4235   7112    622   -332    345       C  
ATOM   5545  O   VAL B 281      31.387  19.156  29.324  1.00 64.83           O  
ANISOU 5545  O   VAL B 281     9633   6027   8971    551   -338    294       O  
ATOM   5546  CB  VAL B 281      32.205  18.010  32.290  1.00 51.71           C  
ANISOU 5546  CB  VAL B 281     7843   4385   7420    725   -267    245       C  
ATOM   5547  CG1 VAL B 281      32.096  16.842  31.313  1.00 48.42           C  
ANISOU 5547  CG1 VAL B 281     7482   3886   7031    676   -210    145       C  
ATOM   5548  CG2 VAL B 281      33.511  17.926  33.064  1.00 61.08           C  
ANISOU 5548  CG2 VAL B 281     8969   5565   8672    772   -270    214       C  
ATOM   5549  N   VAL B 282      29.750  19.563  30.860  1.00 43.87           N  
ANISOU 5549  N   VAL B 282     6964   3482   6222    621   -306    418       N  
ATOM   5550  CA  VAL B 282      28.704  19.404  29.866  1.00 46.13           C  
ANISOU 5550  CA  VAL B 282     7342   3758   6429    544   -262    442       C  
ATOM   5551  C   VAL B 282      28.767  20.506  28.827  1.00 43.27           C  
ANISOU 5551  C   VAL B 282     6914   3512   6014    447   -304    500       C  
ATOM   5552  O   VAL B 282      28.567  20.208  27.659  1.00 48.63           O  
ANISOU 5552  O   VAL B 282     7479   4340   6659    308   -219    449       O  
ATOM   5553  CB  VAL B 282      27.269  19.168  30.390  1.00 55.44           C  
ANISOU 5553  CB  VAL B 282     8540   4991   7533    550   -205    491       C  
ATOM   5554  CG1 VAL B 282      27.220  18.098  31.478  1.00 64.39           C  
ANISOU 5554  CG1 VAL B 282     9638   6104   8723    610   -164    425       C  
ATOM   5555  CG2 VAL B 282      26.533  20.439  30.792  1.00 51.96           C  
ANISOU 5555  CG2 VAL B 282     8055   4664   7022    557   -257    607       C  
ATOM   5556  N   PRO B 283      29.011  21.793  29.153  1.00 43.06           N  
ANISOU 5556  N   PRO B 283     6904   3482   5976    497   -417    597       N  
ATOM   5557  CA  PRO B 283      29.154  22.800  28.096  1.00 49.19           C  
ANISOU 5557  CA  PRO B 283     7561   4421   6708    386   -442    636       C  
ATOM   5558  C   PRO B 283      30.385  22.579  27.208  1.00 61.78           C  
ANISOU 5558  C   PRO B 283     9030   6074   8371    309   -434    535       C  
ATOM   5559  O   PRO B 283      30.343  22.950  26.039  1.00 71.96           O  
ANISOU 5559  O   PRO B 283    10195   7528   9618    178   -402    529       O  
ATOM   5560  CB  PRO B 283      29.125  24.160  28.792  1.00 41.53           C  
ANISOU 5560  CB  PRO B 283     6623   3444   5712    465   -550    752       C  
ATOM   5561  CG  PRO B 283      28.787  23.818  30.246  1.00 45.16           C  
ANISOU 5561  CG  PRO B 283     7046   3927   6184    559   -489    727       C  
ATOM   5562  CD  PRO B 283      29.176  22.366  30.492  1.00 43.49           C  
ANISOU 5562  CD  PRO B 283     6870   3610   6046    586   -433    623       C  
ATOM   5563  N   TRP B 284      31.455  21.947  27.736  1.00 74.01           N  
ANISOU 5563  N   TRP B 284    10609   7489  10023    388   -459    455       N  
ATOM   5564  CA  TRP B 284      32.602  21.525  26.935  1.00 58.37           C  
ANISOU 5564  CA  TRP B 284     8516   5551   8112    318   -437    346       C  
ATOM   5565  C   TRP B 284      32.174  20.465  25.930  1.00 58.21           C  
ANISOU 5565  C   TRP B 284     8410   5640   8068    188   -299    253       C  
ATOM   5566  O   TRP B 284      32.523  20.551  24.752  1.00 46.27           O  
ANISOU 5566  O   TRP B 284     6765   4268   6548     62   -263    207       O  
ATOM   5567  CB  TRP B 284      33.753  21.002  27.796  1.00 54.69           C  
ANISOU 5567  CB  TRP B 284     8112   4910   7759    437   -488    282       C  
ATOM   5568  CG  TRP B 284      34.791  20.292  26.981  1.00 56.79           C  
ANISOU 5568  CG  TRP B 284     8269   5213   8095    362   -442    157       C  
ATOM   5569  CD1 TRP B 284      35.795  20.850  26.243  1.00 60.24           C  
ANISOU 5569  CD1 TRP B 284     8598   5724   8567    303   -486    132       C  
ATOM   5570  CD2 TRP B 284      34.904  18.876  26.769  1.00 56.03           C  
ANISOU 5570  CD2 TRP B 284     8158   5091   8041    331   -337     38       C  
ATOM   5571  NE1 TRP B 284      36.524  19.888  25.597  1.00 56.94           N  
ANISOU 5571  NE1 TRP B 284     8099   5325   8209    239   -417      8       N  
ATOM   5572  CE2 TRP B 284      35.997  18.662  25.899  1.00 53.69           C  
ANISOU 5572  CE2 TRP B 284     7743   4854   7803    254   -324    -53       C  
ATOM   5573  CE3 TRP B 284      34.173  17.769  27.209  1.00 56.59           C  
ANISOU 5573  CE3 TRP B 284     8303   5096   8104    359   -251     -1       C  
ATOM   5574  CZ2 TRP B 284      36.392  17.388  25.496  1.00 46.80           C  
ANISOU 5574  CZ2 TRP B 284     6828   3973   6983    208   -230   -179       C  
ATOM   5575  CZ3 TRP B 284      34.588  16.504  26.838  1.00 52.15           C  
ANISOU 5575  CZ3 TRP B 284     7700   4521   7595    317   -160   -126       C  
ATOM   5576  CH2 TRP B 284      35.682  16.325  25.993  1.00 47.86           C  
ANISOU 5576  CH2 TRP B 284     7040   4035   7110    243   -150   -213       C  
ATOM   5577  N   GLY B 285      31.393  19.490  26.420  1.00 57.17           N  
ANISOU 5577  N   GLY B 285     8358   5442   7921    221   -223    228       N  
ATOM   5578  CA  GLY B 285      30.855  18.440  25.566  1.00 67.77           C  
ANISOU 5578  CA  GLY B 285     9633   6879   9235    105    -88    145       C  
ATOM   5579  C   GLY B 285      29.949  18.990  24.458  1.00 69.47           C  
ANISOU 5579  C   GLY B 285     9755   7294   9348    -37    -37    193       C  
ATOM   5580  O   GLY B 285      29.982  18.503  23.340  1.00 70.34           O  
ANISOU 5580  O   GLY B 285     9751   7530   9446   -167     49    119       O  
ATOM   5581  N   ILE B 286      29.146  20.010  24.781  1.00 65.11           N  
ANISOU 5581  N   ILE B 286     9251   6769   8721    -10    -91    317       N  
ATOM   5582  CA  ILE B 286      28.164  20.550  23.857  1.00 62.15           C  
ANISOU 5582  CA  ILE B 286     8802   6572   8241   -133    -45    374       C  
ATOM   5583  C   ILE B 286      28.868  21.354  22.752  1.00 71.44           C  
ANISOU 5583  C   ILE B 286     9837   7892   9416   -238    -76    369       C  
ATOM   5584  O   ILE B 286      28.523  21.201  21.570  1.00 61.16           O  
ANISOU 5584  O   ILE B 286     8421   6751   8066   -381      5    336       O  
ATOM   5585  CB  ILE B 286      27.069  21.336  24.612  1.00 55.11           C  
ANISOU 5585  CB  ILE B 286     8013   5655   7271    -65    -91    508       C  
ATOM   5586  CG1 ILE B 286      26.141  20.387  25.371  1.00 55.16           C  
ANISOU 5586  CG1 ILE B 286     8132   5567   7260     -4    -25    501       C  
ATOM   5587  CG2 ILE B 286      26.266  22.212  23.668  1.00 56.84           C  
ANISOU 5587  CG2 ILE B 286     8149   6061   7388   -184    -74    583       C  
ATOM   5588  CD1 ILE B 286      25.281  21.042  26.434  1.00 47.92           C  
ANISOU 5588  CD1 ILE B 286     7346   4570   6293    103    -86    625       C  
ATOM   5589  N   VAL B 287      29.874  22.173  23.113  1.00 62.15           N  
ANISOU 5589  N   VAL B 287     8665   6656   8295   -170   -190    398       N  
ATOM   5590  CA  VAL B 287      30.571  22.949  22.090  1.00 66.84           C  
ANISOU 5590  CA  VAL B 287     9126   7381   8890   -266   -222    394       C  
ATOM   5591  C   VAL B 287      31.417  22.017  21.241  1.00 66.20           C  
ANISOU 5591  C   VAL B 287     8941   7342   8872   -350   -152    259       C  
ATOM   5592  O   VAL B 287      31.550  22.261  20.052  1.00 59.79           O  
ANISOU 5592  O   VAL B 287     7999   6686   8034   -480   -117    234       O  
ATOM   5593  CB  VAL B 287      31.428  24.110  22.632  1.00 62.17           C  
ANISOU 5593  CB  VAL B 287     8559   6724   8338   -178   -362    462       C  
ATOM   5594  CG1 VAL B 287      30.552  25.158  23.276  1.00 65.89           C  
ANISOU 5594  CG1 VAL B 287     9113   7185   8736   -116   -428    602       C  
ATOM   5595  CG2 VAL B 287      32.438  23.614  23.649  1.00 70.80           C  
ANISOU 5595  CG2 VAL B 287     9735   7627   9539    -44   -418    410       C  
ATOM   5596  N   LYS B 288      31.990  20.971  21.854  1.00 70.10           N  
ANISOU 5596  N   LYS B 288     9491   7695   9448   -276   -132    172       N  
ATOM   5597  CA  LYS B 288      32.825  20.036  21.110  1.00 79.25           C  
ANISOU 5597  CA  LYS B 288    10558   8882  10672   -349    -65     41       C  
ATOM   5598  C   LYS B 288      31.953  19.066  20.319  1.00 79.13           C  
ANISOU 5598  C   LYS B 288    10491   8971  10604   -465     75    -20       C  
ATOM   5599  O   LYS B 288      32.463  18.116  19.748  1.00 90.59           O  
ANISOU 5599  O   LYS B 288    11877  10441  12103   -526    148   -133       O  
ATOM   5600  CB  LYS B 288      33.761  19.249  22.041  1.00 78.82           C  
ANISOU 5600  CB  LYS B 288    10581   8642  10725   -229    -92    -31       C  
ATOM   5601  CG  LYS B 288      34.948  20.000  22.630  1.00 69.17           C  
ANISOU 5601  CG  LYS B 288     9383   7322   9578   -131   -220     -8       C  
ATOM   5602  CD  LYS B 288      35.965  20.443  21.620  1.00 62.76           C  
ANISOU 5602  CD  LYS B 288     8434   6612   8799   -220   -244    -50       C  
ATOM   5603  CE  LYS B 288      36.735  19.242  21.112  1.00 71.78           C  
ANISOU 5603  CE  LYS B 288     9513   7746  10015   -270   -167   -190       C  
ATOM   5604  NZ  LYS B 288      37.728  19.547  20.053  1.00 85.87           N  
ANISOU 5604  NZ  LYS B 288    11159   9635  11834   -366   -178   -242       N  
ATOM   5605  N   TYR B 289      30.632  19.244  20.345  1.00 94.43           N  
ANISOU 5605  N   TYR B 289    12466  10967  12448   -489    114     53       N  
ATOM   5606  CA  TYR B 289      29.744  18.394  19.562  1.00 84.06           C  
ANISOU 5606  CA  TYR B 289    11100   9761  11077   -604    246      2       C  
ATOM   5607  C   TYR B 289      29.140  19.189  18.412  1.00 72.70           C  
ANISOU 5607  C   TYR B 289     9551   8524   9547   -742    270     54       C  
ATOM   5608  O   TYR B 289      28.978  18.657  17.320  1.00 67.89           O  
ANISOU 5608  O   TYR B 289     8836   8044   8914   -874    365    -14       O  
ATOM   5609  CB  TYR B 289      28.625  17.810  20.430  1.00 78.34           C  
ANISOU 5609  CB  TYR B 289    10502   8951  10314   -534    290     34       C  
ATOM   5610  CG  TYR B 289      27.670  16.889  19.717  1.00 79.21           C  
ANISOU 5610  CG  TYR B 289    10570   9160  10366   -643    426    -17       C  
ATOM   5611  CD1 TYR B 289      28.065  15.619  19.314  1.00 73.91           C  
ANISOU 5611  CD1 TYR B 289     9856   8479   9747   -690    519   -145       C  
ATOM   5612  CD2 TYR B 289      26.371  17.293  19.437  1.00 81.32           C  
ANISOU 5612  CD2 TYR B 289    10839   9532  10526   -700    463     63       C  
ATOM   5613  CE1 TYR B 289      27.190  14.762  18.667  1.00 72.19           C  
ANISOU 5613  CE1 TYR B 289     9602   8352   9477   -790    645   -193       C  
ATOM   5614  CE2 TYR B 289      25.477  16.447  18.796  1.00 71.75           C  
ANISOU 5614  CE2 TYR B 289     9592   8411   9260   -799    588     17       C  
ATOM   5615  CZ  TYR B 289      25.897  15.183  18.406  1.00 75.16           C  
ANISOU 5615  CZ  TYR B 289     9981   8830   9745   -845    679   -112       C  
ATOM   5616  OH  TYR B 289      25.046  14.341  17.760  1.00 76.19           O  
ANISOU 5616  OH  TYR B 289    10074   9051   9825   -944    803   -160       O  
ATOM   5617  N   LEU B 290      28.815  20.454  18.694  1.00 65.44           N  
ANISOU 5617  N   LEU B 290     8660   7627   8577   -707    182    175       N  
ATOM   5618  CA  LEU B 290      28.258  21.345  17.694  1.00 59.56           C  
ANISOU 5618  CA  LEU B 290     7817   7067   7745   -826    191    237       C  
ATOM   5619  C   LEU B 290      29.349  22.022  16.868  1.00 59.63           C  
ANISOU 5619  C   LEU B 290     7705   7162   7792   -890    140    214       C  
ATOM   5620  O   LEU B 290      29.127  22.262  15.695  1.00 63.44           O  
ANISOU 5620  O   LEU B 290     8067   7814   8223  -1026    189    206       O  
ATOM   5621  CB  LEU B 290      27.353  22.378  18.366  1.00 50.60           C  
ANISOU 5621  CB  LEU B 290     6769   5921   6537   -762    125    379       C  
ATOM   5622  CG  LEU B 290      26.176  21.820  19.163  1.00 49.57           C  
ANISOU 5622  CG  LEU B 290     6758   5715   6360   -702    172    414       C  
ATOM   5623  CD1 LEU B 290      25.407  22.940  19.873  1.00 42.06           C  
ANISOU 5623  CD1 LEU B 290     5894   4744   5343   -629     93    559       C  
ATOM   5624  CD2 LEU B 290      25.260  20.949  18.299  1.00 44.32           C  
ANISOU 5624  CD2 LEU B 290     6034   5171   5634   -827    310    361       C  
ATOM   5625  N   TYR B 291      30.528  22.311  17.450  1.00 71.50           N  
ANISOU 5625  N   TYR B 291     9235   8549   9382   -796     45    202       N  
ATOM   5626  CA  TYR B 291      31.496  23.208  16.813  1.00 73.48           C  
ANISOU 5626  CA  TYR B 291     9386   8874   9660   -840    -25    208       C  
ATOM   5627  C   TYR B 291      32.902  22.632  16.626  1.00 67.70           C  
ANISOU 5627  C   TYR B 291     8602   8086   9036   -834    -34     95       C  
ATOM   5628  O   TYR B 291      33.721  23.288  16.005  1.00 66.22           O  
ANISOU 5628  O   TYR B 291     8321   7966   8872   -881    -82     90       O  
ATOM   5629  CB  TYR B 291      31.570  24.560  17.525  1.00 73.85           C  
ANISOU 5629  CB  TYR B 291     9494   8874   9693   -747   -154    330       C  
ATOM   5630  CG  TYR B 291      30.250  25.287  17.606  1.00 80.92           C  
ANISOU 5630  CG  TYR B 291    10427   9841  10480   -761   -153    448       C  
ATOM   5631  CD1 TYR B 291      29.765  26.033  16.541  1.00 79.01           C  
ANISOU 5631  CD1 TYR B 291    10079   9784  10158   -886   -132    494       C  
ATOM   5632  CD2 TYR B 291      29.456  25.186  18.740  1.00 93.06           C  
ANISOU 5632  CD2 TYR B 291    12106  11260  11992   -652   -168    512       C  
ATOM   5633  CE1 TYR B 291      28.538  26.668  16.609  1.00 87.28           C  
ANISOU 5633  CE1 TYR B 291    11161  10898  11105   -900   -128    601       C  
ATOM   5634  CE2 TYR B 291      28.232  25.829  18.827  1.00 87.32           C  
ANISOU 5634  CE2 TYR B 291    11416  10597  11165   -664   -166    620       C  
ATOM   5635  CZ  TYR B 291      27.766  26.570  17.756  1.00 85.50           C  
ANISOU 5635  CZ  TYR B 291    11078  10552  10856   -789   -145    665       C  
ATOM   5636  OH  TYR B 291      26.566  27.219  17.837  1.00 72.67           O  
ANISOU 5636  OH  TYR B 291     9488   8990   9132   -802   -143    773       O  
ATOM   5637  N   GLU B 292      33.192  21.454  17.177  1.00 79.27           N  
ANISOU 5637  N   GLU B 292    10127   9425  10566   -775      9     10       N  
ATOM   5638  CA  GLU B 292      34.458  20.778  16.924  1.00 84.35           C  
ANISOU 5638  CA  GLU B 292    10717  10024  11309   -781     17   -105       C  
ATOM   5639  C   GLU B 292      34.279  19.270  17.116  1.00 93.59           C  
ANISOU 5639  C   GLU B 292    11925  11123  12512   -775    120   -206       C  
ATOM   5640  O   GLU B 292      34.632  18.718  18.161  1.00100.37           O  
ANISOU 5640  O   GLU B 292    12888  11814  13435   -654     95   -231       O  
ATOM   5641  CB  GLU B 292      35.536  21.252  17.904  1.00 81.43           C  
ANISOU 5641  CB  GLU B 292    10416   9499  11024   -643   -106    -85       C  
ATOM   5642  CG  GLU B 292      36.294  22.496  17.474  1.00101.01           C  
ANISOU 5642  CG  GLU B 292    12821  12046  13513   -665   -202    -37       C  
ATOM   5643  CD  GLU B 292      37.504  22.762  18.360  1.00111.43           C  
ANISOU 5643  CD  GLU B 292    14198  13210  14929   -537   -311    -42       C  
ATOM   5644  OE1 GLU B 292      38.152  21.763  18.736  1.00101.10           O  
ANISOU 5644  OE1 GLU B 292    12921  11792  13701   -488   -286   -134       O  
ATOM   5645  OE2 GLU B 292      37.810  23.970  18.658  1.00123.29           O1-
ANISOU 5645  OE2 GLU B 292    15713  14704  16427   -487   -421     45       O1-
ATOM   5646  N   ASP B 293      33.757  18.591  16.093  1.00 87.48           N  
ANISOU 5646  N   ASP B 293    11064  10478  11696   -908    237   -267       N  
ATOM   5647  CA  ASP B 293      33.490  17.161  16.213  1.00 96.16           C  
ANISOU 5647  CA  ASP B 293    12195  11523  12819   -912    342   -361       C  
ATOM   5648  C   ASP B 293      34.399  16.393  15.255  1.00113.11           C  
ANISOU 5648  C   ASP B 293    14225  13726  15025  -1007    405   -488       C  
ATOM   5649  O   ASP B 293      34.138  16.369  14.052  1.00152.50           O  
ANISOU 5649  O   ASP B 293    19096  18880  19968  -1149    474   -517       O  
ATOM   5650  CB  ASP B 293      32.007  16.878  15.941  1.00 98.14           C  
ANISOU 5650  CB  ASP B 293    12458  11861  12968   -978    434   -327       C  
ATOM   5651  CG  ASP B 293      31.559  15.444  16.168  1.00 96.62           C  
ANISOU 5651  CG  ASP B 293    12314  11608  12790   -974    542   -410       C  
ATOM   5652  OD1 ASP B 293      31.747  14.949  17.280  1.00 98.55           O  
ANISOU 5652  OD1 ASP B 293    12673  11683  13087   -847    517   -421       O  
ATOM   5653  OD2 ASP B 293      31.008  14.835  15.229  1.00116.38           O1-
ANISOU 5653  OD2 ASP B 293    14739  14234  15248  -1098    652   -463       O1-
ATOM   5654  N   GLU B 294      35.471  15.783  15.778  1.00 99.53           N  
ANISOU 5654  N   GLU B 294    12537  11872  13408   -929    381   -564       N  
ATOM   5655  CA  GLU B 294      36.401  15.082  14.904  1.00 95.84           C  
ANISOU 5655  CA  GLU B 294    11960  11451  13002  -1013    435   -684       C  
ATOM   5656  C   GLU B 294      37.249  14.091  15.702  1.00 99.77           C  
ANISOU 5656  C   GLU B 294    12527  11776  13603   -912    435   -770       C  
ATOM   5657  O   GLU B 294      38.190  14.479  16.403  1.00 83.84           O  
ANISOU 5657  O   GLU B 294    10555   9643  11657   -809    337   -758       O  
ATOM   5658  CB  GLU B 294      37.200  16.081  14.060  1.00 82.50           C  
ANISOU 5658  CB  GLU B 294    10154   9871  11321  -1083    372   -668       C  
ATOM   5659  N   GLY B 295      36.872  12.807  15.590  1.00121.87           N  
ANISOU 5659  N   GLY B 295    15336  14560  16409   -944    547   -855       N  
ATOM   5660  CA  GLY B 295      37.568  11.681  16.203  1.00123.90           C  
ANISOU 5660  CA  GLY B 295    15648  14670  16759   -868    572   -950       C  
ATOM   5661  C   GLY B 295      37.512  11.696  17.733  1.00123.58           C  
ANISOU 5661  C   GLY B 295    15767  14438  16751   -695    501   -899       C  
ATOM   5662  O   GLY B 295      38.538  11.855  18.383  1.00125.00           O  
ANISOU 5662  O   GLY B 295    15985  14498  17012   -597    419   -909       O  
ATOM   5663  N   CYS B 296      36.310  11.506  18.297  1.00118.21           N  
ANISOU 5663  N   CYS B 296    15177  13730  16008   -658    536   -845       N  
ATOM   5664  CA  CYS B 296      36.007  11.577  19.725  1.00 99.50           C  
ANISOU 5664  CA  CYS B 296    12962  11194  13650   -501    475   -783       C  
ATOM   5665  C   CYS B 296      36.616  12.820  20.347  1.00 90.21           C  
ANISOU 5665  C   CYS B 296    11823   9956  12496   -407    332   -695       C  
ATOM   5666  O   CYS B 296      36.965  12.800  21.525  1.00105.85           O  
ANISOU 5666  O   CYS B 296    13916  11772  14530   -265    264   -674       O  
ATOM   5667  CB  CYS B 296      36.493  10.382  20.534  1.00 86.67           C  
ANISOU 5667  CB  CYS B 296    11417   9404  12111   -406    505   -868       C  
ATOM   5668  SG  CYS B 296      36.118   8.807  19.734  1.00122.09           S  
ANISOU 5668  SG  CYS B 296    15843  13951  16594   -518    673   -997       S  
ATOM   5669  N   TRP B 297      36.698  13.886  19.548  1.00 92.46           N  
ANISOU 5669  N   TRP B 297    12015  10377  12738   -488    289   -642       N  
ATOM   5670  CA  TRP B 297      37.157  15.192  19.983  1.00108.26           C  
ANISOU 5670  CA  TRP B 297    14038  12350  14746   -419    157   -549       C  
ATOM   5671  C   TRP B 297      38.617  15.117  20.427  1.00121.07           C  
ANISOU 5671  C   TRP B 297    15668  13853  16481   -337     83   -603       C  
ATOM   5672  O   TRP B 297      39.015  15.802  21.364  1.00119.07           O  
ANISOU 5672  O   TRP B 297    15495  13488  16258   -217    -26   -539       O  
ATOM   5673  CB  TRP B 297      36.245  15.712  21.110  1.00117.63           C  
ANISOU 5673  CB  TRP B 297    15361  13449  15883   -307    103   -436       C  
ATOM   5674  CG  TRP B 297      34.768  15.555  20.873  1.00118.13           C  
ANISOU 5674  CG  TRP B 297    15440  13598  15844   -367    184   -393       C  
ATOM   5675  CD1 TRP B 297      34.102  15.762  19.699  1.00120.82           C  
ANISOU 5675  CD1 TRP B 297    15676  14124  16106   -513    251   -385       C  
ATOM   5676  CD2 TRP B 297      33.754  15.208  21.841  1.00113.36           C  
ANISOU 5676  CD2 TRP B 297    14967  12900  15205   -281    203   -345       C  
ATOM   5677  NE1 TRP B 297      32.758  15.561  19.867  1.00101.94           N  
ANISOU 5677  NE1 TRP B 297    13340  11761  13633   -525    311   -337       N  
ATOM   5678  CE2 TRP B 297      32.511  15.235  21.172  1.00103.09           C  
ANISOU 5678  CE2 TRP B 297    13630  11737  13802   -384    282   -310       C  
ATOM   5679  CE3 TRP B 297      33.761  14.869  23.201  1.00110.76           C  
ANISOU 5679  CE3 TRP B 297    14780  12384  14918   -127    162   -329       C  
ATOM   5680  CZ2 TRP B 297      31.310  14.932  21.813  1.00100.10           C  
ANISOU 5680  CZ2 TRP B 297    13352  11315  13366   -338    320   -261       C  
ATOM   5681  CZ3 TRP B 297      32.571  14.576  23.836  1.00105.62           C  
ANISOU 5681  CZ3 TRP B 297    14230  11690  14210    -82    200   -280       C  
ATOM   5682  CH2 TRP B 297      31.361  14.590  23.146  1.00 95.94           C  
ANISOU 5682  CH2 TRP B 297    12965  10603  12885   -187    279   -248       C  
ATOM   5683  N   THR B 298      39.416  14.267  19.770  1.00124.36           N  
ANISOU 5683  N   THR B 298    16003  14289  16959   -401    144   -720       N  
ATOM   5684  CA  THR B 298      40.815  14.095  20.132  1.00116.61           C  
ANISOU 5684  CA  THR B 298    15023  13198  16086   -331     84   -780       C  
ATOM   5685  C   THR B 298      41.624  15.259  19.566  1.00131.23           C  
ANISOU 5685  C   THR B 298    16786  15128  17948   -369     -5   -744       C  
ATOM   5686  O   THR B 298      42.635  15.656  20.150  1.00158.19           O  
ANISOU 5686  O   THR B 298    20231  18441  21435   -278   -101   -738       O  
ATOM   5687  CB  THR B 298      41.336  12.726  19.669  1.00101.64           C  
ANISOU 5687  CB  THR B 298    13078  11291  14252   -383    185   -918       C  
ATOM   5688  N   ARG B 299      41.176  15.778  18.412  1.00132.09           N  
ANISOU 5688  N   ARG B 299    16783  15419  17985   -505     30   -722       N  
ATOM   5689  CA  ARG B 299      41.805  16.909  17.743  1.00128.36           C  
ANISOU 5689  CA  ARG B 299    16215  15045  17510   -558    -44   -684       C  
ATOM   5690  C   ARG B 299      41.302  18.193  18.406  1.00119.46           C  
ANISOU 5690  C   ARG B 299    15159  13901  16330   -484   -147   -547       C  
ATOM   5691  O   ARG B 299      40.623  19.010  17.787  1.00114.25           O  
ANISOU 5691  O   ARG B 299    14446  13377  15587   -562   -148   -476       O  
ATOM   5692  CB  ARG B 299      41.535  16.857  16.232  1.00136.19           C  
ANISOU 5692  CB  ARG B 299    17058  16237  18449   -735     42   -724       C  
ATOM   5693  CG  ARG B 299      42.010  15.593  15.526  1.00130.94           C  
ANISOU 5693  CG  ARG B 299    16320  15596  17833   -814    146   -860       C  
ATOM   5694  CD  ARG B 299      43.494  15.644  15.304  1.00144.96           C  
ANISOU 5694  CD  ARG B 299    18034  17339  19704   -806     94   -923       C  
ATOM   5695  NE  ARG B 299      43.802  16.742  14.397  1.00156.36           N  
ANISOU 5695  NE  ARG B 299    19367  18923  21120   -892     46   -882       N  
ATOM   5696  CZ  ARG B 299      44.174  16.589  13.128  1.00148.10           C  
ANISOU 5696  CZ  ARG B 299    18182  18015  20074  -1027    102   -948       C  
ATOM   5697  NH1 ARG B 299      44.292  15.375  12.618  1.00140.28           N  
ANISOU 5697  NH1 ARG B 299    17147  17040  19111  -1092    209  -1059       N  
ATOM   5698  NH2 ARG B 299      44.450  17.643  12.381  1.00142.92           N  
ANISOU 5698  NH2 ARG B 299    17433  17479  19393  -1095     52   -903       N  
ATOM   5699  N   ASN B 300      41.652  18.354  19.684  1.00119.66           N  
ANISOU 5699  N   ASN B 300    15305  13755  16404   -331   -233   -510       N  
ATOM   5700  CA  ASN B 300      41.178  19.463  20.497  1.00134.11           C  
ANISOU 5700  CA  ASN B 300    17223  15541  18192   -241   -331   -382       C  
ATOM   5701  C   ASN B 300      42.126  20.645  20.335  1.00129.68           C  
ANISOU 5701  C   ASN B 300    16610  15003  17660   -230   -444   -338       C  
ATOM   5702  O   ASN B 300      42.657  21.160  21.320  1.00135.93           O  
ANISOU 5702  O   ASN B 300    17485  15666  18497   -104   -549   -292       O  
ATOM   5703  CB  ASN B 300      41.008  19.081  21.972  1.00132.05           C  
ANISOU 5703  CB  ASN B 300    17122  15087  17964    -82   -367   -357       C  
ATOM   5704  N   SER B 301      42.308  21.083  19.087  1.00107.07           N  
ANISOU 5704  N   SER B 301    13608  12304  14768   -363   -423   -351       N  
ATOM   5705  CA  SER B 301      43.285  22.114  18.801  1.00115.10           C  
ANISOU 5705  CA  SER B 301    14561  13353  15818   -365   -521   -324       C  
ATOM   5706  C   SER B 301      42.719  23.077  17.764  1.00107.78           C  
ANISOU 5706  C   SER B 301    13533  12615  14803   -486   -516   -260       C  
ATOM   5707  O   SER B 301      42.996  22.965  16.573  1.00113.47           O  
ANISOU 5707  O   SER B 301    14124  13471  15519   -614   -462   -317       O  
ATOM   5708  CB  SER B 301      44.620  21.521  18.401  1.00122.99           C  
ANISOU 5708  CB  SER B 301    15489  14326  16916   -386   -514   -437       C  
ATOM   5709  OG  SER B 301      44.485  20.680  17.272  1.00139.79           O  
ANISOU 5709  OG  SER B 301    17511  16572  19031   -521   -396   -528       O  
ATOM   5710  N   ASN B 302      41.938  24.033  18.263  1.00101.34           N  
ANISOU 5710  N   ASN B 302    12781  11803  13920   -440   -574   -140       N  
ATOM   5711  CA  ASN B 302      41.244  24.979  17.413  1.00125.02           C  
ANISOU 5711  CA  ASN B 302    15703  14973  16828   -543   -570    -66       C  
ATOM   5712  C   ASN B 302      40.995  26.279  18.173  1.00132.95           C  
ANISOU 5712  C   ASN B 302    16781  15937  17798   -453   -685     66       C  
ATOM   5713  O   ASN B 302      41.516  27.314  17.770  1.00150.02           O  
ANISOU 5713  O   ASN B 302    18877  18164  19959   -478   -757    108       O  
ATOM   5714  CB  ASN B 302      39.969  24.376  16.811  1.00150.00           C  
ANISOU 5714  CB  ASN B 302    18842  18245  19905   -643   -448    -75       C  
ATOM   5715  CG  ASN B 302      39.177  25.321  15.925  1.00167.77           C  
ANISOU 5715  CG  ASN B 302    21012  20676  22055   -752   -438      3       C  
ATOM   5716  OD1 ASN B 302      39.736  26.212  15.287  1.00212.39           O  
ANISOU 5716  OD1 ASN B 302    26574  26417  27708   -803   -491     26       O  
ATOM   5717  ND2 ASN B 302      37.865  25.134  15.890  1.00137.47           N  
ANISOU 5717  ND2 ASN B 302    17208  16893  18132   -786   -371     45       N  
ATOM   5718  N   MET B 303      40.198  26.239  19.253  1.00126.66           N  
ANISOU 5718  N   MET B 303    16119  15035  16972   -351   -701    130       N  
ATOM   5719  CA  MET B 303      39.640  27.481  19.757  1.00111.45           C  
ANISOU 5719  CA  MET B 303    14249  13111  14985   -297   -787    264       C  
ATOM   5720  C   MET B 303      39.552  27.427  21.276  1.00112.76           C  
ANISOU 5720  C   MET B 303    14577  13085  15182   -130   -852    310       C  
ATOM   5721  O   MET B 303      40.250  26.639  21.904  1.00131.18           O  
ANISOU 5721  O   MET B 303    16963  15282  17598    -51   -858    240       O  
ATOM   5722  CB  MET B 303      38.246  27.707  19.169  1.00113.29           C  
ANISOU 5722  CB  MET B 303    14456  13486  15103   -392   -717    324       C  
ATOM   5723  CG  MET B 303      37.894  29.140  18.767  1.00128.69           C  
ANISOU 5723  CG  MET B 303    16361  15553  16981   -433   -780    435       C  
ATOM   5724  SD  MET B 303      36.537  29.195  17.534  1.00151.63           S  
ANISOU 5724  SD  MET B 303    19172  18676  19763   -600   -668    461       S  
ATOM   5725  CE  MET B 303      36.997  30.655  16.592  1.00118.56           C  
ANISOU 5725  CE  MET B 303    14859  14641  15546   -682   -739    522       C  
ATOM   5726  N   ASN B 304      38.689  28.274  21.850  1.00108.48           N  
ANISOU 5726  N   ASN B 304    13449  12655  15111   1410   -688    750       N  
ATOM   5727  CA  ASN B 304      38.592  28.463  23.289  1.00109.12           C  
ANISOU 5727  CA  ASN B 304    13514  12658  15287   1320   -659    732       C  
ATOM   5728  C   ASN B 304      38.019  27.219  23.979  1.00109.32           C  
ANISOU 5728  C   ASN B 304    13656  12616  15266   1327   -678    718       C  
ATOM   5729  O   ASN B 304      37.971  27.157  25.210  1.00108.83           O  
ANISOU 5729  O   ASN B 304    13579  12465  15306   1255   -680    707       O  
ATOM   5730  CB  ASN B 304      37.787  29.723  23.607  1.00111.23           C  
ANISOU 5730  CB  ASN B 304    13646  12794  15823   1136   -600    720       C  
ATOM   5731  CG  ASN B 304      37.771  30.053  25.081  1.00143.30           C  
ANISOU 5731  CG  ASN B 304    17631  16749  20066   1020   -564    719       C  
ATOM   5732  OD1 ASN B 304      36.814  29.709  25.772  1.00167.26           O  
ANISOU 5732  OD1 ASN B 304    20700  19665  23185    930   -549    688       O  
ATOM   5733  ND2 ASN B 304      38.821  30.702  25.570  1.00171.21           N  
ANISOU 5733  ND2 ASN B 304    21063  20335  23653   1024   -543    749       N  
ATOM   5734  N   TYR B 305      37.614  26.218  23.184  1.00111.45           N  
ANISOU 5734  N   TYR B 305    13997  12897  15452   1394   -712    730       N  
ATOM   5735  CA  TYR B 305      36.883  25.066  23.694  1.00107.94           C  
ANISOU 5735  CA  TYR B 305    13640  12372  15001   1377   -730    716       C  
ATOM   5736  C   TYR B 305      37.770  24.162  24.554  1.00100.67           C  
ANISOU 5736  C   TYR B 305    12778  11522  13951   1458   -732    746       C  
ATOM   5737  O   TYR B 305      37.267  23.401  25.374  1.00111.86           O  
ANISOU 5737  O   TYR B 305    14258  12862  15380   1421   -734    727       O  
ATOM   5738  CB  TYR B 305      36.160  24.314  22.573  1.00103.30           C  
ANISOU 5738  CB  TYR B 305    13079  11763  14407   1404   -774    721       C  
ATOM   5739  CG  TYR B 305      35.435  25.197  21.590  1.00 97.04           C  
ANISOU 5739  CG  TYR B 305    12217  10926  13727   1341   -772    705       C  
ATOM   5740  CD1 TYR B 305      34.528  26.173  21.984  1.00 98.80           C  
ANISOU 5740  CD1 TYR B 305    12371  11043  14125   1194   -733    670       C  
ATOM   5741  CD2 TYR B 305      35.639  25.019  20.237  1.00101.65           C  
ANISOU 5741  CD2 TYR B 305    12793  11579  14250   1423   -803    733       C  
ATOM   5742  CE1 TYR B 305      33.876  26.972  21.055  1.00 88.96           C  
ANISOU 5742  CE1 TYR B 305    11043   9766  12991   1131   -725    667       C  
ATOM   5743  CE2 TYR B 305      34.997  25.806  19.292  1.00 96.68           C  
ANISOU 5743  CE2 TYR B 305    12100  10912  13720   1370   -801    723       C  
ATOM   5744  CZ  TYR B 305      34.135  26.807  19.701  1.00 94.24           C  
ANISOU 5744  CZ  TYR B 305    11715  10504  13588   1223   -761    692       C  
ATOM   5745  OH  TYR B 305      33.501  27.552  18.748  1.00 94.04           O  
ANISOU 5745  OH  TYR B 305    11613  10449  13667   1168   -754    691       O  
ATOM   5746  N   TRP B 306      39.087  24.253  24.366  1.00 89.02           N  
ANISOU 5746  N   TRP B 306    11267  10199  12357   1560   -729    796       N  
ATOM   5747  CA  TRP B 306      40.031  23.547  25.214  1.00 92.10           C  
ANISOU 5747  CA  TRP B 306    11670  10672  12652   1615   -727    842       C  
ATOM   5748  C   TRP B 306      40.112  24.182  26.607  1.00 89.63           C  
ANISOU 5748  C   TRP B 306    11339  10248  12468   1533   -768    790       C  
ATOM   5749  O   TRP B 306      40.324  23.514  27.622  1.00 65.86           O  
ANISOU 5749  O   TRP B 306     8368   7207   9448   1528   -798    790       O  
ATOM   5750  CB  TRP B 306      41.406  23.474  24.538  1.00102.43           C  
ANISOU 5750  CB  TRP B 306    12896  12170  13851   1701   -727    927       C  
ATOM   5751  CG  TRP B 306      42.416  22.683  25.309  1.00113.34           C  
ANISOU 5751  CG  TRP B 306    14244  13636  15186   1693   -754    983       C  
ATOM   5752  CD1 TRP B 306      43.536  23.191  25.889  1.00109.80           C  
ANISOU 5752  CD1 TRP B 306    13732  13267  14721   1703   -784   1001       C  
ATOM   5753  CD2 TRP B 306      42.401  21.266  25.616  1.00143.76           C  
ANISOU 5753  CD2 TRP B 306    18141  17458  19025   1684   -835    998       C  
ATOM   5754  NE1 TRP B 306      44.240  22.192  26.511  1.00135.14           N  
ANISOU 5754  NE1 TRP B 306    16943  16504  17899   1689   -872   1032       N  
ATOM   5755  CE2 TRP B 306      43.559  21.006  26.382  1.00143.78           C  
ANISOU 5755  CE2 TRP B 306    18113  17540  18976   1677   -894   1019       C  
ATOM   5756  CE3 TRP B 306      41.518  20.201  25.357  1.00160.51           C  
ANISOU 5756  CE3 TRP B 306    20352  19488  21148   1671   -891    949       C  
ATOM   5757  CZ2 TRP B 306      43.859  19.725  26.854  1.00146.30           C  
ANISOU 5757  CZ2 TRP B 306    18507  17871  19211   1666   -979    991       C  
ATOM   5758  CZ3 TRP B 306      41.806  18.942  25.837  1.00150.22           C  
ANISOU 5758  CZ3 TRP B 306    19114  18191  19771   1668   -977    924       C  
ATOM   5759  CH2 TRP B 306      42.972  18.708  26.567  1.00152.34           C  
ANISOU 5759  CH2 TRP B 306    19370  18553  19959   1672  -1017    940       C  
ATOM   5760  N   LEU B 307      39.913  25.498  26.648  1.00 88.31           N  
ANISOU 5760  N   LEU B 307    11082  10014  12457   1443   -757    757       N  
ATOM   5761  CA  LEU B 307      40.172  26.266  27.851  1.00 74.45           C  
ANISOU 5761  CA  LEU B 307     9239   8174  10873   1346   -755    744       C  
ATOM   5762  C   LEU B 307      39.055  26.088  28.879  1.00 80.77           C  
ANISOU 5762  C   LEU B 307    10073   8784  11833   1209   -731    702       C  
ATOM   5763  O   LEU B 307      39.292  26.262  30.068  1.00 82.50           O  
ANISOU 5763  O   LEU B 307    10259   8932  12155   1147   -723    695       O  
ATOM   5764  CB  LEU B 307      40.366  27.727  27.445  1.00 66.49           C  
ANISOU 5764  CB  LEU B 307     8076   7175  10010   1277   -708    754       C  
ATOM   5765  CG  LEU B 307      41.372  28.512  28.282  1.00 72.70           C  
ANISOU 5765  CG  LEU B 307     8731   7998  10895   1253   -688    781       C  
ATOM   5766  CD1 LEU B 307      42.726  27.813  28.364  1.00 61.92           C  
ANISOU 5766  CD1 LEU B 307     7413   6813   9300   1412   -762    808       C  
ATOM   5767  CD2 LEU B 307      41.514  29.921  27.720  1.00 83.58           C  
ANISOU 5767  CD2 LEU B 307     9947   9399  12410   1185   -616    800       C  
ATOM   5768  N   ILE B 308      37.852  25.709  28.430  1.00 84.16           N  
ANISOU 5768  N   ILE B 308    10567   9140  12270   1163   -713    672       N  
ATOM   5769  CA  ILE B 308      36.711  25.597  29.330  1.00 80.67           C  
ANISOU 5769  CA  ILE B 308    10153   8539  11960   1025   -677    626       C  
ATOM   5770  C   ILE B 308      36.768  24.302  30.138  1.00 74.60           C  
ANISOU 5770  C   ILE B 308     9513   7750  11083   1075   -717    617       C  
ATOM   5771  O   ILE B 308      35.998  24.125  31.075  1.00 63.36           O  
ANISOU 5771  O   ILE B 308     8125   6206   9745    969   -687    577       O  
ATOM   5772  CB  ILE B 308      35.376  25.748  28.575  1.00 85.41           C  
ANISOU 5772  CB  ILE B 308    10758   9088  12605    953   -642    598       C  
ATOM   5773  CG1 ILE B 308      35.208  24.713  27.468  1.00 75.75           C  
ANISOU 5773  CG1 ILE B 308     9639   7950  11193   1080   -676    612       C  
ATOM   5774  CG2 ILE B 308      35.235  27.157  28.024  1.00114.25           C  
ANISOU 5774  CG2 ILE B 308    14264  12740  16406    870   -592    604       C  
ATOM   5775  CD1 ILE B 308      33.976  24.934  26.628  1.00 62.42           C  
ANISOU 5775  CD1 ILE B 308     7942   6222   9554   1018   -651    589       C  
ATOM   5776  N   ILE B 309      37.691  23.400  29.789  1.00 78.83           N  
ANISOU 5776  N   ILE B 309    10109   8416  11427   1228   -771    656       N  
ATOM   5777  CA  ILE B 309      37.878  22.161  30.537  1.00 76.88           C  
ANISOU 5777  CA  ILE B 309     9961   8168  11080   1274   -808    657       C  
ATOM   5778  C   ILE B 309      39.197  22.171  31.329  1.00 75.03           C  
ANISOU 5778  C   ILE B 309     9710   8006  10794   1334   -860    681       C  
ATOM   5779  O   ILE B 309      39.378  21.354  32.230  1.00 73.84           O  
ANISOU 5779  O   ILE B 309     9634   7831  10590   1345   -899    671       O  
ATOM   5780  CB  ILE B 309      37.765  20.945  29.594  1.00 73.84           C  
ANISOU 5780  CB  ILE B 309     9634   7881  10543   1368   -815    690       C  
ATOM   5781  CG1 ILE B 309      37.466  19.647  30.340  1.00 61.64           C  
ANISOU 5781  CG1 ILE B 309     8178   6292   8950   1364   -843    676       C  
ATOM   5782  CG2 ILE B 309      39.018  20.804  28.745  1.00103.21           C  
ANISOU 5782  CG2 ILE B 309    13296  11792  14129   1486   -834    761       C  
ATOM   5783  CD1 ILE B 309      36.055  19.546  30.807  1.00 62.84           C  
ANISOU 5783  CD1 ILE B 309     8384   6289   9203   1255   -802    620       C  
ATOM   5784  N   ARG B 310      40.114  23.098  31.001  1.00 77.86           N  
ANISOU 5784  N   ARG B 310     9967   8458  11160   1372   -864    711       N  
ATOM   5785  CA  ARG B 310      41.435  23.156  31.619  1.00 70.29           C  
ANISOU 5785  CA  ARG B 310     8976   7604  10127   1441   -917    738       C  
ATOM   5786  C   ARG B 310      41.535  24.281  32.653  1.00 64.44           C  
ANISOU 5786  C   ARG B 310     8132   6751   9600   1332   -891    719       C  
ATOM   5787  O   ARG B 310      42.413  24.246  33.525  1.00 61.54           O  
ANISOU 5787  O   ARG B 310     7751   6425   9206   1363   -938    727       O  
ATOM   5788  CB  ARG B 310      42.530  23.321  30.561  1.00 73.05           C  
ANISOU 5788  CB  ARG B 310     9258   8171  10326   1557   -923    798       C  
ATOM   5789  CG  ARG B 310      42.696  22.131  29.621  1.00 78.81           C  
ANISOU 5789  CG  ARG B 310    10025   9022  10896   1625   -925    852       C  
ATOM   5790  CD  ARG B 310      43.630  21.031  30.091  1.00 72.98           C  
ANISOU 5790  CD  ARG B 310     9323   8389  10017   1660  -1004    870       C  
ATOM   5791  NE  ARG B 310      43.108  20.224  31.187  1.00 83.59           N  
ANISOU 5791  NE  ARG B 310    10786   9620  11354   1633  -1045    814       N  
ATOM   5792  CZ  ARG B 310      42.510  19.040  31.042  1.00 87.22           C  
ANISOU 5792  CZ  ARG B 310    11324  10044  11772   1621  -1058    799       C  
ATOM   5793  NH1 ARG B 310      42.098  18.365  32.102  1.00 87.22           N  
ANISOU 5793  NH1 ARG B 310    11430   9948  11763   1597  -1092    750       N  
ATOM   5794  NH2 ARG B 310      42.343  18.520  29.838  1.00 85.22           N  
ANISOU 5794  NH2 ARG B 310    11039   9851  11490   1629  -1040    834       N  
ATOM   5795  N   LEU B 311      40.647  25.283  32.560  1.00 58.94           N  
ANISOU 5795  N   LEU B 311     7347   5924   9126   1191   -800    699       N  
ATOM   5796  CA  LEU B 311      40.650  26.366  33.538  1.00 65.65           C  
ANISOU 5796  CA  LEU B 311     8066   6659  10219   1053   -711    692       C  
ATOM   5797  C   LEU B 311      40.008  25.970  34.867  1.00 57.88           C  
ANISOU 5797  C   LEU B 311     7170   5547   9277    917   -655    626       C  
ATOM   5798  O   LEU B 311      40.521  26.320  35.927  1.00 57.94           O  
ANISOU 5798  O   LEU B 311     7149   5640   9224    806   -567    577       O  
ATOM   5799  CB  LEU B 311      39.989  27.625  32.970  1.00 68.92           C  
ANISOU 5799  CB  LEU B 311     8347   7016  10823    929   -601    687       C  
ATOM   5800  CG  LEU B 311      40.887  28.465  32.068  1.00 67.48           C  
ANISOU 5800  CG  LEU B 311     8030   6988  10623   1002   -598    739       C  
ATOM   5801  CD1 LEU B 311      40.109  29.646  31.521  1.00 63.84           C  
ANISOU 5801  CD1 LEU B 311     7453   6457  10347    871   -493    729       C  
ATOM   5802  CD2 LEU B 311      42.128  28.925  32.819  1.00 60.15           C  
ANISOU 5802  CD2 LEU B 311     7021   6227   9608    980   -549    732       C  
ATOM   5803  N   PRO B 312      38.856  25.267  34.888  1.00 53.59           N  
ANISOU 5803  N   PRO B 312     6740   4872   8751    882   -667    595       N  
ATOM   5804  CA  PRO B 312      38.306  24.823  36.160  1.00 54.77           C  
ANISOU 5804  CA  PRO B 312     6976   4888   8946    774   -628    542       C  
ATOM   5805  C   PRO B 312      39.176  23.786  36.871  1.00 54.12           C  
ANISOU 5805  C   PRO B 312     7008   4900   8656    870   -710    537       C  
ATOM   5806  O   PRO B 312      39.193  23.774  38.099  1.00 54.99           O  
ANISOU 5806  O   PRO B 312     7147   5009   8738    748   -632    479       O  
ATOM   5807  CB  PRO B 312      36.904  24.328  35.806  1.00 49.91           C  
ANISOU 5807  CB  PRO B 312     6442   4223   8299    715   -603    502       C  
ATOM   5808  CG  PRO B 312      36.645  24.882  34.431  1.00 45.07           C  
ANISOU 5808  CG  PRO B 312     5751   3680   7693    747   -602    528       C  
ATOM   5809  CD  PRO B 312      37.995  24.895  33.757  1.00 53.06           C  
ANISOU 5809  CD  PRO B 312     6725   4835   8603    910   -682    588       C  
ATOM   5810  N   ILE B 313      39.916  22.954  36.118  1.00 49.91           N  
ANISOU 5810  N   ILE B 313     6536   4488   7938   1073   -850    587       N  
ATOM   5811  CA  ILE B 313      40.822  22.015  36.764  1.00 48.82           C  
ANISOU 5811  CA  ILE B 313     6501   4495   7553   1154   -913    574       C  
ATOM   5812  C   ILE B 313      42.030  22.759  37.320  1.00 51.67           C  
ANISOU 5812  C   ILE B 313     6764   5069   7799   1101   -835    554       C  
ATOM   5813  O   ILE B 313      42.508  22.396  38.398  1.00 52.08           O  
ANISOU 5813  O   ILE B 313     6872   5198   7719   1057   -809    510       O  
ATOM   5814  CB  ILE B 313      41.237  20.851  35.851  1.00 50.46           C  
ANISOU 5814  CB  ILE B 313     6802   4808   7562   1357  -1049    622       C  
ATOM   5815  CG1 ILE B 313      40.035  19.960  35.537  1.00 56.67           C  
ANISOU 5815  CG1 ILE B 313     7668   5517   8347   1314  -1010    602       C  
ATOM   5816  CG2 ILE B 313      42.382  20.067  36.489  1.00 50.68           C  
ANISOU 5816  CG2 ILE B 313     6921   4981   7355   1467  -1140    621       C  
ATOM   5817  CD1 ILE B 313      40.352  18.835  34.595  1.00 66.45           C  
ANISOU 5817  CD1 ILE B 313     8938   6915   9393   1424  -1053    637       C  
ATOM   5818  N   LEU B 314      42.509  23.786  36.585  1.00 52.57           N  
ANISOU 5818  N   LEU B 314     6732   5276   7965   1106   -799    586       N  
ATOM   5819  CA  LEU B 314      43.615  24.598  37.071  1.00 53.53           C  
ANISOU 5819  CA  LEU B 314     6747   5593   8000   1046   -718    567       C  
ATOM   5820  C   LEU B 314      43.198  25.363  38.336  1.00 51.51           C  
ANISOU 5820  C   LEU B 314     6441   5270   7863    819   -560    493       C  
ATOM   5821  O   LEU B 314      44.010  25.560  39.234  1.00 46.14           O  
ANISOU 5821  O   LEU B 314     5739   4728   7064    760   -503    453       O  
ATOM   5822  CB  LEU B 314      44.124  25.548  35.982  1.00 53.51           C  
ANISOU 5822  CB  LEU B 314     6597   5687   8045   1097   -710    619       C  
ATOM   5823  CG  LEU B 314      45.358  26.349  36.419  1.00 50.35           C  
ANISOU 5823  CG  LEU B 314     6086   5502   7544   1052   -635    603       C  
ATOM   5824  CD1 LEU B 314      46.521  25.387  36.619  1.00 53.19           C  
ANISOU 5824  CD1 LEU B 314     6535   6052   7622   1196   -736    613       C  
ATOM   5825  CD2 LEU B 314      45.713  27.472  35.443  1.00 42.38           C  
ANISOU 5825  CD2 LEU B 314     4914   4562   6625   1066   -598    648       C  
ATOM   5826  N   PHE B 315      41.929  25.790  38.394  1.00 50.52           N  
ANISOU 5826  N   PHE B 315     6295   4930   7970    693   -490    474       N  
ATOM   5827  CA  PHE B 315      41.388  26.482  39.553  1.00 52.11           C  
ANISOU 5827  CA  PHE B 315     6456   5042   8302    476   -342    404       C  
ATOM   5828  C   PHE B 315      41.401  25.553  40.763  1.00 60.25           C  
ANISOU 5828  C   PHE B 315     7621   6065   9205    448   -350    354       C  
ATOM   5829  O   PHE B 315      41.777  25.972  41.856  1.00 71.07           O  
ANISOU 5829  O   PHE B 315     8960   7502  10540    323   -252    298       O  
ATOM   5830  CB  PHE B 315      39.956  26.973  39.302  1.00 53.01           C  
ANISOU 5830  CB  PHE B 315     6539   4915   8686    365   -282    399       C  
ATOM   5831  CG  PHE B 315      39.318  27.649  40.488  1.00 51.13           C  
ANISOU 5831  CG  PHE B 315     6265   4570   8590    142   -132    329       C  
ATOM   5832  CD1 PHE B 315      39.592  28.983  40.753  1.00 48.22           C  
ANISOU 5832  CD1 PHE B 315     5743   4260   8320      3      0    305       C  
ATOM   5833  CD2 PHE B 315      38.487  26.960  41.357  1.00 50.13           C  
ANISOU 5833  CD2 PHE B 315     6258   4294   8496     72   -120    286       C  
ATOM   5834  CE1 PHE B 315      39.039  29.644  41.841  1.00 44.94           C  
ANISOU 5834  CE1 PHE B 315     5289   3753   8033   -203    140    240       C  
ATOM   5835  CE2 PHE B 315      37.974  27.618  42.468  1.00 56.24           C  
ANISOU 5835  CE2 PHE B 315     6993   4983   9391   -132     21    222       C  
ATOM   5836  CZ  PHE B 315      38.254  28.954  42.718  1.00 45.44           C  
ANISOU 5836  CZ  PHE B 315     5472   3675   8119   -269    150    198       C  
ATOM   5837  N   ALA B 316      40.987  24.292  40.570  1.00 63.39           N  
ANISOU 5837  N   ALA B 316     8169   6381   9534    564   -466    372       N  
ATOM   5838  CA  ALA B 316      40.990  23.321  41.661  1.00 66.10           C  
ANISOU 5838  CA  ALA B 316     8649   6714   9751    552   -482    330       C  
ATOM   5839  C   ALA B 316      42.414  22.995  42.127  1.00 62.99           C  
ANISOU 5839  C   ALA B 316     8272   6564   9098    627   -514    323       C  
ATOM   5840  O   ALA B 316      42.626  22.685  43.306  1.00 55.82           O  
ANISOU 5840  O   ALA B 316     7423   5689   8098    557   -470    271       O  
ATOM   5841  CB  ALA B 316      40.228  22.070  41.311  1.00 65.55           C  
ANISOU 5841  CB  ALA B 316     8731   6501   9673    660   -598    353       C  
ATOM   5842  N   CYS B 317      43.389  23.110  41.214  1.00 57.96           N  
ANISOU 5842  N   CYS B 317     7579   6097   8347    764   -584    374       N  
ATOM   5843  CA  CYS B 317      44.768  22.776  41.533  1.00 51.23           C  
ANISOU 5843  CA  CYS B 317     6741   5478   7244    852   -625    374       C  
ATOM   5844  C   CYS B 317      45.458  23.921  42.268  1.00 48.51           C  
ANISOU 5844  C   CYS B 317     6266   5262   6905    711   -493    330       C  
ATOM   5845  O   CYS B 317      46.259  23.677  43.159  1.00 47.80           O  
ANISOU 5845  O   CYS B 317     6205   5308   6648    699   -477    294       O  
ATOM   5846  CB  CYS B 317      45.511  22.336  40.291  1.00 48.51           C  
ANISOU 5846  CB  CYS B 317     6403   5259   6769   1062   -759    447       C  
ATOM   5847  SG  CYS B 317      45.060  20.636  39.882  1.00 72.11           S  
ANISOU 5847  SG  CYS B 317     9590   8157   9654   1239   -926    481       S  
ATOM   5848  N   ILE B 318      45.139  25.161  41.886  1.00 47.04           N  
ANISOU 5848  N   ILE B 318     5934   5031   6909    608   -399    333       N  
ATOM   5849  CA  ILE B 318      45.704  26.335  42.517  1.00 44.54           C  
ANISOU 5849  CA  ILE B 318     5480   4819   6623    467   -268    291       C  
ATOM   5850  C   ILE B 318      45.236  26.347  43.962  1.00 52.08           C  
ANISOU 5850  C   ILE B 318     6479   5695   7615    298   -167    213       C  
ATOM   5851  O   ILE B 318      46.048  26.578  44.852  1.00 56.88           O  
ANISOU 5851  O   ILE B 318     7060   6444   8107    241   -111    169       O  
ATOM   5852  CB  ILE B 318      45.332  27.640  41.777  1.00 44.73           C  
ANISOU 5852  CB  ILE B 318     5344   4788   6864    388   -188    312       C  
ATOM   5853  CG1 ILE B 318      46.086  27.845  40.465  1.00 46.70           C  
ANISOU 5853  CG1 ILE B 318     5521   5167   7054    544   -267    384       C  
ATOM   5854  CG2 ILE B 318      45.482  28.866  42.663  1.00 42.18           C  
ANISOU 5854  CG2 ILE B 318     4894   4499   6635    192    -28    252       C  
ATOM   5855  CD1 ILE B 318      45.426  28.899  39.583  1.00 55.08           C  
ANISOU 5855  CD1 ILE B 318     6455   6124   8350    488   -209    414       C  
ATOM   5856  N   VAL B 319      43.935  26.108  44.189  1.00 58.60           N  
ANISOU 5856  N   VAL B 319     7369   6296   8602    219   -144    195       N  
ATOM   5857  CA  VAL B 319      43.412  26.141  45.549  1.00 67.09           C  
ANISOU 5857  CA  VAL B 319     8485   7282   9725     55    -44    123       C  
ATOM   5858  C   VAL B 319      43.983  24.971  46.330  1.00 67.06           C  
ANISOU 5858  C   VAL B 319     8622   7369   9490    133   -111    102       C  
ATOM   5859  O   VAL B 319      44.267  25.122  47.504  1.00 80.12           O  
ANISOU 5859  O   VAL B 319    10279   9076  11089     27    -31     42       O  
ATOM   5860  CB  VAL B 319      41.874  26.150  45.671  1.00 67.21           C  
ANISOU 5860  CB  VAL B 319     8538   7032   9967    -52      1    107       C  
ATOM   5861  CG1 VAL B 319      41.217  27.415  45.144  1.00 73.95           C  
ANISOU 5861  CG1 VAL B 319     9247   7781  11067   -168     95    114       C  
ATOM   5862  CG2 VAL B 319      41.247  24.933  45.049  1.00 74.55           C  
ANISOU 5862  CG2 VAL B 319     9609   7843  10876     86   -130    149       C  
ATOM   5863  N   ASN B 320      44.134  23.812  45.678  1.00 66.19           N  
ANISOU 5863  N   ASN B 320     8626   7274   9248    316   -256    151       N  
ATOM   5864  CA  ASN B 320      44.699  22.643  46.344  1.00 67.56           C  
ANISOU 5864  CA  ASN B 320     8938   7537   9194    405   -329    137       C  
ATOM   5865  C   ASN B 320      46.115  22.907  46.853  1.00 63.63           C  
ANISOU 5865  C   ASN B 320     8389   7289   8500    419   -308    116       C  
ATOM   5866  O   ASN B 320      46.473  22.448  47.932  1.00 62.18           O  
ANISOU 5866  O   ASN B 320     8274   7166   8185    388   -288     71       O  
ATOM   5867  CB  ASN B 320      44.623  21.374  45.496  1.00 68.99           C  
ANISOU 5867  CB  ASN B 320     9248   7694   9273    603   -490    195       C  
ATOM   5868  CG  ASN B 320      43.302  20.663  45.686  1.00 72.26           C  
ANISOU 5868  CG  ASN B 320     9777   7871   9807    573   -508    186       C  
ATOM   5869  OD1 ASN B 320      42.673  20.780  46.741  1.00 84.17           O  
ANISOU 5869  OD1 ASN B 320    11311   9272  11397    426   -414    129       O  
ATOM   5870  ND2 ASN B 320      42.853  19.968  44.659  1.00 61.19           N  
ANISOU 5870  ND2 ASN B 320     8440   6383   8425    709   -623    240       N  
ATOM   5871  N   PHE B 321      46.905  23.661  46.081  1.00 65.04           N  
ANISOU 5871  N   PHE B 321     8443   7608   8663    466   -311    150       N  
ATOM   5872  CA  PHE B 321      48.244  24.025  46.515  1.00 63.09           C  
ANISOU 5872  CA  PHE B 321     8131   7596   8246    473   -285    131       C  
ATOM   5873  C   PHE B 321      48.209  25.132  47.565  1.00 67.18           C  
ANISOU 5873  C   PHE B 321     8544   8118   8865    265   -123     60       C  
ATOM   5874  O   PHE B 321      49.113  25.211  48.395  1.00 74.58           O  
ANISOU 5874  O   PHE B 321     9468   9214   9656    237    -88     20       O  
ATOM   5875  CB  PHE B 321      49.125  24.423  45.332  1.00 60.58           C  
ANISOU 5875  CB  PHE B 321     7717   7429   7871    598   -344    193       C  
ATOM   5876  CG  PHE B 321      49.796  23.235  44.700  1.00 61.84           C  
ANISOU 5876  CG  PHE B 321     7986   7695   7816    816   -503    246       C  
ATOM   5877  CD1 PHE B 321      50.758  22.502  45.390  1.00 60.04           C  
ANISOU 5877  CD1 PHE B 321     7836   7630   7347    883   -546    227       C  
ATOM   5878  CD2 PHE B 321      49.421  22.825  43.435  1.00 57.58           C  
ANISOU 5878  CD2 PHE B 321     7475   7086   7317    952   -608    315       C  
ATOM   5879  CE1 PHE B 321      51.340  21.386  44.810  1.00 58.70           C  
ANISOU 5879  CE1 PHE B 321     7770   7551   6981   1083   -693    277       C  
ATOM   5880  CE2 PHE B 321      49.988  21.701  42.864  1.00 59.76           C  
ANISOU 5880  CE2 PHE B 321     7856   7451   7399   1152   -755    363       C  
ATOM   5881  CZ  PHE B 321      50.962  20.999  43.541  1.00 64.72           C  
ANISOU 5881  CZ  PHE B 321     8559   8243   7788   1217   -796    345       C  
ATOM   5882  N   LEU B 322      47.181  25.988  47.521  1.00 58.26           N  
ANISOU 5882  N   LEU B 322     7338   6816   7982    121    -27     45       N  
ATOM   5883  CA  LEU B 322      47.076  27.012  48.546  1.00 56.48           C  
ANISOU 5883  CA  LEU B 322     7018   6582   7860    -81    127    -25       C  
ATOM   5884  C   LEU B 322      46.671  26.365  49.864  1.00 58.35           C  
ANISOU 5884  C   LEU B 322     7372   6750   8049   -161    162    -86       C  
ATOM   5885  O   LEU B 322      47.148  26.794  50.903  1.00 66.71           O  
ANISOU 5885  O   LEU B 322     8393   7898   9056   -266    250   -145       O  
ATOM   5886  CB  LEU B 322      46.125  28.125  48.103  1.00 59.50           C  
ANISOU 5886  CB  LEU B 322     7283   6806   8517   -209    220    -22       C  
ATOM   5887  CG  LEU B 322      46.591  28.933  46.883  1.00 62.13           C  
ANISOU 5887  CG  LEU B 322     7482   7221   8905   -147    206     34       C  
ATOM   5888  CD1 LEU B 322      45.585  30.016  46.519  1.00 59.68           C  
ANISOU 5888  CD1 LEU B 322     7060   6744   8871   -282    304     33       C  
ATOM   5889  CD2 LEU B 322      47.976  29.529  47.095  1.00 52.54           C  
ANISOU 5889  CD2 LEU B 322     6166   6248   7551   -140    237     20       C  
ATOM   5890  N   ILE B 323      45.859  25.300  49.820  1.00 59.83           N  
ANISOU 5890  N   ILE B 323     7703   6789   8240   -102     89    -71       N  
ATOM   5891  CA  ILE B 323      45.481  24.558  51.013  1.00 61.76           C  
ANISOU 5891  CA  ILE B 323     8071   6966   8427   -158    109   -121       C  
ATOM   5892  C   ILE B 323      46.697  23.783  51.488  1.00 68.07           C  
ANISOU 5892  C   ILE B 323     8943   7974   8947    -47     43   -129       C  
ATOM   5893  O   ILE B 323      46.983  23.758  52.682  1.00 80.85           O  
ANISOU 5893  O   ILE B 323    10586   9648  10487   -131    108   -188       O  
ATOM   5894  CB  ILE B 323      44.276  23.629  50.750  1.00 66.48           C  
ANISOU 5894  CB  ILE B 323     8800   7346   9111   -117     45    -98       C  
ATOM   5895  CG1 ILE B 323      43.015  24.416  50.376  1.00 73.88           C  
ANISOU 5895  CG1 ILE B 323     9668   8069  10333   -240    120    -97       C  
ATOM   5896  CG2 ILE B 323      44.021  22.683  51.914  1.00 69.66           C  
ANISOU 5896  CG2 ILE B 323     9347   7702   9420   -141     47   -142       C  
ATOM   5897  CD1 ILE B 323      42.710  25.620  51.260  1.00 76.28           C  
ANISOU 5897  CD1 ILE B 323     9861   8333  10789   -456    286   -160       C  
ATOM   5898  N   PHE B 324      47.409  23.174  50.539  1.00 65.74           N  
ANISOU 5898  N   PHE B 324     8679   7793   8504    141    -86    -68       N  
ATOM   5899  CA  PHE B 324      48.652  22.474  50.834  1.00 73.53           C  
ANISOU 5899  CA  PHE B 324     9724   8993   9221    261   -158    -67       C  
ATOM   5900  C   PHE B 324      49.599  23.323  51.698  1.00 78.68           C  
ANISOU 5900  C   PHE B 324    10274   9820   9802    160    -58   -122       C  
ATOM   5901  O   PHE B 324      50.106  22.840  52.707  1.00 79.50           O  
ANISOU 5901  O   PHE B 324    10446  10015   9748    152    -49   -164       O  
ATOM   5902  CB  PHE B 324      49.312  22.086  49.520  1.00 64.15           C  
ANISOU 5902  CB  PHE B 324     8535   7911   7928    457   -290     10       C  
ATOM   5903  CG  PHE B 324      50.672  21.463  49.633  1.00 60.70           C  
ANISOU 5903  CG  PHE B 324     8141   7707   7217    593   -370     21       C  
ATOM   5904  CD1 PHE B 324      51.819  22.247  49.625  1.00 54.41           C  
ANISOU 5904  CD1 PHE B 324     7224   7114   6337    587   -333     14       C  
ATOM   5905  CD2 PHE B 324      50.787  20.082  49.682  1.00 58.86           C  
ANISOU 5905  CD2 PHE B 324     8068   7484   6813    733   -485     41       C  
ATOM   5906  CE1 PHE B 324      53.062  21.639  49.657  1.00 56.41           C  
ANISOU 5906  CE1 PHE B 324     7517   7578   6336    722   -414     28       C  
ATOM   5907  CE2 PHE B 324      52.038  19.482  49.675  1.00 63.89           C  
ANISOU 5907  CE2 PHE B 324     8745   8335   7197    870   -567     57       C  
ATOM   5908  CZ  PHE B 324      53.174  20.265  49.690  1.00 57.88           C  
ANISOU 5908  CZ  PHE B 324     7864   7776   6352    862   -530     50       C  
ATOM   5909  N   VAL B 325      49.803  24.592  51.323  1.00 61.79           N  
ANISOU 5909  N   VAL B 325     7972   7723   7785     79     20   -122       N  
ATOM   5910  CA  VAL B 325      50.736  25.470  52.004  1.00 53.91           C  
ANISOU 5910  CA  VAL B 325     6861   6894   6728    -10    112   -170       C  
ATOM   5911  C   VAL B 325      50.171  25.875  53.353  1.00 54.13           C  
ANISOU 5911  C   VAL B 325     6888   6834   6846   -202    242   -251       C  
ATOM   5912  O   VAL B 325      50.893  25.878  54.351  1.00 53.46           O  
ANISOU 5912  O   VAL B 325     6806   6880   6625   -243    283   -304       O  
ATOM   5913  CB  VAL B 325      51.070  26.688  51.126  1.00 54.36           C  
ANISOU 5913  CB  VAL B 325     6744   7010   6899    -33    154   -142       C  
ATOM   5914  CG1 VAL B 325      51.573  27.897  51.910  1.00 46.74           C  
ANISOU 5914  CG1 VAL B 325     5640   6141   5977   -191    290   -204       C  
ATOM   5915  CG2 VAL B 325      51.979  26.289  49.958  1.00 48.05           C  
ANISOU 5915  CG2 VAL B 325     5943   6360   5956    167     27    -69       C  
ATOM   5916  N   ARG B 326      48.868  26.184  53.383  1.00 64.79           N  
ANISOU 5916  N   ARG B 326     8235   7960   8421   -316    304   -261       N  
ATOM   5917  CA  ARG B 326      48.247  26.675  54.606  1.00 67.75           C  
ANISOU 5917  CA  ARG B 326     8598   8238   8907   -508    436   -336       C  
ATOM   5918  C   ARG B 326      48.260  25.580  55.672  1.00 65.09           C  
ANISOU 5918  C   ARG B 326     8415   7903   8413   -488    409   -373       C  
ATOM   5919  O   ARG B 326      48.597  25.851  56.832  1.00 49.83           O  
ANISOU 5919  O   ARG B 326     6468   6038   6425   -591    493   -439       O  
ATOM   5920  CB  ARG B 326      46.862  27.273  54.339  1.00 74.11           C  
ANISOU 5920  CB  ARG B 326     9362   8805   9990   -631    507   -335       C  
ATOM   5921  CG  ARG B 326      46.181  27.908  55.546  1.00 88.91           C  
ANISOU 5921  CG  ARG B 326    11208  10572  12000   -839    651   -411       C  
ATOM   5922  CD  ARG B 326      46.986  28.891  56.376  1.00 98.39           C  
ANISOU 5922  CD  ARG B 326    12292  11924  13168   -957    761   -473       C  
ATOM   5923  NE  ARG B 326      47.841  29.784  55.597  1.00117.47           N  
ANISOU 5923  NE  ARG B 326    14561  14487  15584   -928    767   -446       N  
ATOM   5924  CZ  ARG B 326      48.837  30.517  56.096  1.00130.42           C  
ANISOU 5924  CZ  ARG B 326    16098  16306  17148   -982    831   -487       C  
ATOM   5925  NH1 ARG B 326      49.088  30.502  57.396  1.00140.61           N  
ANISOU 5925  NH1 ARG B 326    17415  17650  18361  -1074    899   -559       N  
ATOM   5926  NH2 ARG B 326      49.569  31.274  55.294  1.00115.95           N  
ANISOU 5926  NH2 ARG B 326    14136  14598  15322   -944    828   -456       N  
ATOM   5927  N   VAL B 327      47.901  24.358  55.239  1.00 62.98           N  
ANISOU 5927  N   VAL B 327     8289   7562   8076   -352    292   -328       N  
ATOM   5928  CA  VAL B 327      47.826  23.193  56.107  1.00 58.36           C  
ANISOU 5928  CA  VAL B 327     7864   6962   7349   -313    252   -352       C  
ATOM   5929  C   VAL B 327      49.195  22.954  56.721  1.00 56.45           C  
ANISOU 5929  C   VAL B 327     7630   6962   6856   -255    233   -377       C  
ATOM   5930  O   VAL B 327      49.267  22.700  57.919  1.00 60.83           O  
ANISOU 5930  O   VAL B 327     8241   7537   7335   -323    285   -434       O  
ATOM   5931  CB  VAL B 327      47.316  21.944  55.364  1.00 60.62           C  
ANISOU 5931  CB  VAL B 327     8290   7145   7597   -158    117   -292       C  
ATOM   5932  CG1 VAL B 327      47.718  20.638  56.056  1.00 54.79           C  
ANISOU 5932  CG1 VAL B 327     7711   6472   6636    -60     44   -302       C  
ATOM   5933  CG2 VAL B 327      45.808  22.014  55.113  1.00 54.81           C  
ANISOU 5933  CG2 VAL B 327     7578   6144   7105   -237    148   -284       C  
ATOM   5934  N   ILE B 328      50.256  23.042  55.905  1.00 51.77           N  
ANISOU 5934  N   ILE B 328     6980   6549   6140   -130    161   -335       N  
ATOM   5935  CA  ILE B 328      51.601  22.806  56.417  1.00 56.61           C  
ANISOU 5935  CA  ILE B 328     7598   7399   6510    -66    137   -355       C  
ATOM   5936  C   ILE B 328      51.988  23.807  57.506  1.00 58.12           C  
ANISOU 5936  C   ILE B 328     7687   7673   6723   -232    274   -433       C  
ATOM   5937  O   ILE B 328      52.587  23.385  58.506  1.00 58.66           O  
ANISOU 5937  O   ILE B 328     7813   7852   6623   -233    284   -477       O  
ATOM   5938  CB  ILE B 328      52.649  22.738  55.296  1.00 57.01           C  
ANISOU 5938  CB  ILE B 328     7604   7624   6433    100     34   -293       C  
ATOM   5939  CG1 ILE B 328      52.418  21.512  54.413  1.00 66.23           C  
ANISOU 5939  CG1 ILE B 328     8902   8738   7524    282   -114   -223       C  
ATOM   5940  CG2 ILE B 328      54.056  22.744  55.868  1.00 50.26           C  
ANISOU 5940  CG2 ILE B 328     6725   7019   5353    138     31   -321       C  
ATOM   5941  CD1 ILE B 328      53.379  21.414  53.244  1.00 70.42           C  
ANISOU 5941  CD1 ILE B 328     9393   9428   7936    451   -220   -157       C  
ATOM   5942  N   CYS B 329      51.644  25.100  57.329  1.00 56.56           N  
ANISOU 5942  N   CYS B 329     7341   7421   6728   -368    378   -449       N  
ATOM   5943  CA  CYS B 329      51.951  26.076  58.368  1.00 65.34           C  
ANISOU 5943  CA  CYS B 329     8353   8599   7872   -532    512   -525       C  
ATOM   5944  C   CYS B 329      51.200  25.748  59.659  1.00 78.95           C  
ANISOU 5944  C   CYS B 329    10167  10202   9627   -650    583   -588       C  
ATOM   5945  O   CYS B 329      51.732  25.999  60.737  1.00 90.09           O  
ANISOU 5945  O   CYS B 329    11560  11718  10954   -728    653   -652       O  
ATOM   5946  CB  CYS B 329      51.535  27.492  58.011  1.00 66.74           C  
ANISOU 5946  CB  CYS B 329     8366   8709   8285   -671    618   -534       C  
ATOM   5947  SG  CYS B 329      52.546  28.270  56.734  1.00 77.50           S  
ANISOU 5947  SG  CYS B 329     9577  10239   9630   -581    579   -478       S  
ATOM   5948  N   ILE B 330      49.971  25.213  59.545  1.00 77.31           N  
ANISOU 5948  N   ILE B 330    10054   9777   9545   -663    568   -570       N  
ATOM   5949  CA  ILE B 330      49.120  24.935  60.693  1.00 61.54           C  
ANISOU 5949  CA  ILE B 330     8140   7639   7605   -779    640   -625       C  
ATOM   5950  C   ILE B 330      49.658  23.716  61.425  1.00 58.29           C  
ANISOU 5950  C   ILE B 330     7874   7320   6953   -680    572   -638       C  
ATOM   5951  O   ILE B 330      49.749  23.744  62.650  1.00 66.97           O  
ANISOU 5951  O   ILE B 330     8998   8448   8001   -772    647   -703       O  
ATOM   5952  CB  ILE B 330      47.645  24.771  60.261  1.00 63.90           C  
ANISOU 5952  CB  ILE B 330     8485   7673   8119   -820    642   -597       C  
ATOM   5953  CG1 ILE B 330      47.039  26.071  59.710  1.00 61.82           C  
ANISOU 5953  CG1 ILE B 330     8072   7309   8109   -944    730   -594       C  
ATOM   5954  CG2 ILE B 330      46.782  24.131  61.345  1.00 60.21           C  
ANISOU 5954  CG2 ILE B 330     8141   7059   7675   -894    683   -639       C  
ATOM   5955  CD1 ILE B 330      47.423  27.341  60.479  1.00 74.88           C  
ANISOU 5955  CD1 ILE B 330     9585   9043   9822  -1110    869   -661       C  
ATOM   5956  N   VAL B 331      50.034  22.672  60.678  1.00 53.95           N  
ANISOU 5956  N   VAL B 331     7420   6824   6256   -493    433   -577       N  
ATOM   5957  CA  VAL B 331      50.469  21.428  61.294  1.00 62.51           C  
ANISOU 5957  CA  VAL B 331     8654   7981   7117   -389    360   -583       C  
ATOM   5958  C   VAL B 331      51.772  21.654  62.069  1.00 72.88           C  
ANISOU 5958  C   VAL B 331     9926   9533   8233   -391    389   -629       C  
ATOM   5959  O   VAL B 331      51.900  21.201  63.203  1.00 68.76           O  
ANISOU 5959  O   VAL B 331     9481   9042   7603   -424    420   -679       O  
ATOM   5960  CB  VAL B 331      50.617  20.285  60.271  1.00 64.54           C  
ANISOU 5960  CB  VAL B 331     9015   8246   7259   -184    202   -506       C  
ATOM   5961  CG1 VAL B 331      51.278  19.064  60.881  1.00 63.76           C  
ANISOU 5961  CG1 VAL B 331     9058   8261   6907    -68    126   -511       C  
ATOM   5962  CG2 VAL B 331      49.302  19.894  59.647  1.00 65.03           C  
ANISOU 5962  CG2 VAL B 331     9141   8068   7498   -177    169   -466       C  
ATOM   5963  N   VAL B 332      52.737  22.362  61.462  1.00 78.20           N  
ANISOU 5963  N   VAL B 332    10475  10374   8862   -355    379   -614       N  
ATOM   5964  CA  VAL B 332      54.026  22.617  62.093  1.00 74.59           C  
ANISOU 5964  CA  VAL B 332     9968  10151   8220   -350    400   -655       C  
ATOM   5965  C   VAL B 332      53.855  23.541  63.292  1.00 73.25           C  
ANISOU 5965  C   VAL B 332     9722   9970   8140   -546    550   -740       C  
ATOM   5966  O   VAL B 332      54.681  23.499  64.185  1.00 78.27           O  
ANISOU 5966  O   VAL B 332    10362  10760   8617   -559    576   -790       O  
ATOM   5967  CB  VAL B 332      55.093  23.167  61.122  1.00 74.67           C  
ANISOU 5967  CB  VAL B 332     9862  10341   8169   -264    354   -615       C  
ATOM   5968  CG1 VAL B 332      55.271  22.284  59.891  1.00 72.70           C  
ANISOU 5968  CG1 VAL B 332     9683  10106   7833    -67    204   -529       C  
ATOM   5969  CG2 VAL B 332      54.838  24.617  60.731  1.00 70.36           C  
ANISOU 5969  CG2 VAL B 332     9140   9753   7840   -396    453   -625       C  
ATOM   5970  N   SER B 333      52.800  24.365  63.304  1.00 73.49           N  
ANISOU 5970  N   SER B 333     9684   9820   8420   -696    646   -758       N  
ATOM   5971  CA  SER B 333      52.486  25.191  64.459  1.00 74.47           C  
ANISOU 5971  CA  SER B 333     9746   9905   8644   -887    790   -839       C  
ATOM   5972  C   SER B 333      52.000  24.310  65.596  1.00 79.46           C  
ANISOU 5972  C   SER B 333    10524  10460   9207   -913    804   -878       C  
ATOM   5973  O   SER B 333      52.470  24.436  66.723  1.00 88.81           O  
ANISOU 5973  O   SER B 333    11708  11741  10295   -979    868   -943       O  
ATOM   5974  CB  SER B 333      51.460  26.245  64.151  1.00 68.53           C  
ANISOU 5974  CB  SER B 333     8890   8975   8173  -1034    885   -843       C  
ATOM   5975  OG  SER B 333      52.046  27.232  63.338  1.00 96.10           O  
ANISOU 5975  OG  SER B 333    12227  12565  11720  -1036    897   -823       O  
ATOM   5976  N   LYS B 334      51.048  23.429  65.282  1.00 78.30           N  
ANISOU 5976  N   LYS B 334    10499  10137   9114   -859    746   -837       N  
ATOM   5977  CA  LYS B 334      50.413  22.614  66.303  1.00 84.84           C  
ANISOU 5977  CA  LYS B 334    11466  10860   9911   -891    765   -870       C  
ATOM   5978  C   LYS B 334      51.405  21.595  66.867  1.00 77.94           C  
ANISOU 5978  C   LYS B 334    10699  10161   8753   -766    692   -878       C  
ATOM   5979  O   LYS B 334      51.350  21.253  68.051  1.00 75.09           O  
ANISOU 5979  O   LYS B 334    10409   9803   8319   -820    742   -931       O  
ATOM   5980  CB  LYS B 334      49.100  22.029  65.772  1.00 79.64           C  
ANISOU 5980  CB  LYS B 334    10898   9959   9404   -874    727   -824       C  
ATOM   5981  CG  LYS B 334      48.012  23.054  65.472  1.00 73.87           C  
ANISOU 5981  CG  LYS B 334    10067   9038   8960  -1023    820   -830       C  
ATOM   5982  CD  LYS B 334      46.746  22.443  64.919  1.00 75.69           C  
ANISOU 5982  CD  LYS B 334    10388   9035   9335   -999    776   -784       C  
ATOM   5983  CE  LYS B 334      46.111  21.355  65.771  1.00 88.77           C  
ANISOU 5983  CE  LYS B 334    12208  10578  10941   -991    766   -800       C  
ATOM   5984  NZ  LYS B 334      45.391  21.864  66.966  1.00 96.56           N  
ANISOU 5984  NZ  LYS B 334    13184  11453  12050  -1174    903   -869       N  
ATOM   5985  N   LEU B 335      52.326  21.131  66.017  1.00 70.00           N  
ANISOU 5985  N   LEU B 335     9703   9306   7588   -600    576   -825       N  
ATOM   5986  CA  LEU B 335      53.328  20.177  66.462  1.00 71.67           C  
ANISOU 5986  CA  LEU B 335    10011   9694   7526   -473    501   -829       C  
ATOM   5987  C   LEU B 335      54.355  20.862  67.362  1.00 69.51           C  
ANISOU 5987  C   LEU B 335     9651   9618   7142   -544    577   -897       C  
ATOM   5988  O   LEU B 335      54.721  20.294  68.391  1.00 71.12           O  
ANISOU 5988  O   LEU B 335     9937   9897   7188   -537    586   -938       O  
ATOM   5989  CB  LEU B 335      53.976  19.495  65.255  1.00 65.56           C  
ANISOU 5989  CB  LEU B 335     9271   9016   6623   -275    355   -751       C  
ATOM   5990  CG  LEU B 335      53.101  18.465  64.554  1.00 64.15           C  
ANISOU 5990  CG  LEU B 335     9219   8667   6487   -173    259   -688       C  
ATOM   5991  CD1 LEU B 335      53.722  18.073  63.219  1.00 67.26           C  
ANISOU 5991  CD1 LEU B 335     9612   9154   6791      5    126   -611       C  
ATOM   5992  CD2 LEU B 335      52.881  17.251  65.441  1.00 56.98           C  
ANISOU 5992  CD2 LEU B 335     8481   7722   5448   -128    230   -704       C  
ATOM   5993  N   LYS B 336      54.787  22.078  66.985  1.00 65.32           N  
ANISOU 5993  N   LYS B 336     8955   9166   6698   -614    633   -908       N  
ATOM   5994  CA  LYS B 336      55.802  22.804  67.730  1.00 77.00           C  
ANISOU 5994  CA  LYS B 336    10338  10838   8082   -679    702   -971       C  
ATOM   5995  C   LYS B 336      55.248  23.209  69.084  1.00 76.81           C  
ANISOU 5995  C   LYS B 336    10314  10736   8135   -851    831  -1053       C  
ATOM   5996  O   LYS B 336      55.988  23.184  70.060  1.00104.12           O  
ANISOU 5996  O   LYS B 336    13779  14339  11444   -871    864  -1110       O  
ATOM   5997  CB  LYS B 336      56.339  24.040  66.997  1.00 81.76           C  
ANISOU 5997  CB  LYS B 336    10761  11531   8775   -719    736   -964       C  
ATOM   5998  CG  LYS B 336      57.444  24.787  67.731  1.00 78.28           C  
ANISOU 5998  CG  LYS B 336    10215  11296   8231   -780    802  -1029       C  
ATOM   5999  CD  LYS B 336      58.803  24.164  67.464  1.00 79.41           C  
ANISOU 5999  CD  LYS B 336    10388  11672   8113   -613    697  -1003       C  
ATOM   6000  CE  LYS B 336      60.014  24.985  67.878  1.00 78.44           C  
ANISOU 6000  CE  LYS B 336    10140  11770   7895   -652    747  -1054       C  
ATOM   6001  NZ  LYS B 336      60.112  26.319  67.225  1.00 71.34           N  
ANISOU 6001  NZ  LYS B 336     9060  10881   7164   -735    809  -1051       N  
ATOM   6002  N   ALA B 337      53.955  23.549  69.132  1.00 70.65           N  
ANISOU 6002  N   ALA B 337     8701   8514   9628   1282   -977   -583       N  
ATOM   6003  CA  ALA B 337      53.315  24.000  70.361  1.00 72.17           C  
ANISOU 6003  CA  ALA B 337     8901   8751   9769   1311   -986   -583       C  
ATOM   6004  C   ALA B 337      52.799  22.832  71.211  1.00 74.73           C  
ANISOU 6004  C   ALA B 337     9368   9062   9962   1311   -981   -541       C  
ATOM   6005  O   ALA B 337      52.094  23.059  72.192  1.00 74.74           O  
ANISOU 6005  O   ALA B 337     9393   9099   9905   1320   -974   -528       O  
ATOM   6006  CB  ALA B 337      52.224  24.985  70.022  1.00 69.37           C  
ANISOU 6006  CB  ALA B 337     8457   8457   9442   1241   -940   -554       C  
ATOM   6007  N   ASN B 338      53.150  21.591  70.837  1.00 79.34           N  
ANISOU 6007  N   ASN B 338    10050   9593  10501   1299   -982   -519       N  
ATOM   6008  CA  ASN B 338      52.681  20.366  71.477  1.00 76.14           C  
ANISOU 6008  CA  ASN B 338     9794   9164   9973   1289   -968   -473       C  
ATOM   6009  C   ASN B 338      51.154  20.322  71.581  1.00 77.76           C  
ANISOU 6009  C   ASN B 338    10015   9411  10119   1194   -896   -406       C  
ATOM   6010  O   ASN B 338      50.628  19.634  72.450  1.00 78.94           O  
ANISOU 6010  O   ASN B 338    10274   9553  10167   1194   -877   -376       O  
ATOM   6011  CB  ASN B 338      53.391  20.069  72.798  1.00 81.95           C  
ANISOU 6011  CB  ASN B 338    10617   9872  10647   1406  -1029   -518       C  
ATOM   6012  CG  ASN B 338      53.014  21.031  73.915  1.00118.12           C  
ANISOU 6012  CG  ASN B 338    15160  14503  15218   1455  -1041   -541       C  
ATOM   6013  OD1 ASN B 338      53.731  21.998  74.178  1.00130.85           O  
ANISOU 6013  OD1 ASN B 338    16680  16129  16907   1531  -1090   -610       O  
ATOM   6014  ND2 ASN B 338      51.894  20.794  74.588  1.00129.07           N  
ANISOU 6014  ND2 ASN B 338    16612  15915  16514   1413   -994   -488       N  
ATOM   6015  N   LEU B 339      50.444  20.997  70.663  1.00 78.94           N  
ANISOU 6015  N   LEU B 339    10062   9601  10329   1113   -852   -386       N  
ATOM   6016  CA  LEU B 339      48.987  20.888  70.553  1.00 76.95           C  
ANISOU 6016  CA  LEU B 339     9817   9388  10033   1014   -783   -331       C  
ATOM   6017  C   LEU B 339      48.576  19.613  69.810  1.00 87.17           C  
ANISOU 6017  C   LEU B 339    11193  10645  11283    938   -739   -279       C  
ATOM   6018  O   LEU B 339      47.410  19.224  69.820  1.00 87.47           O  
ANISOU 6018  O   LEU B 339    11263  10702  11272    859   -680   -238       O  
ATOM   6019  CB  LEU B 339      48.406  22.099  69.814  1.00 64.73           C  
ANISOU 6019  CB  LEU B 339     8131   7895   8568    965   -762   -339       C  
ATOM   6020  CG  LEU B 339      48.701  23.449  70.457  1.00 69.59           C  
ANISOU 6020  CG  LEU B 339     8652   8552   9236   1030   -801   -389       C  
ATOM   6021  CD1 LEU B 339      48.184  24.577  69.573  1.00 75.08           C  
ANISOU 6021  CD1 LEU B 339     9222   9293  10013    980   -781   -394       C  
ATOM   6022  CD2 LEU B 339      48.076  23.523  71.836  1.00 59.25           C  
ANISOU 6022  CD2 LEU B 339     7388   7275   7848   1053   -798   -386       C  
ATOM   6023  N   MET B 340      49.530  18.975  69.129  1.00 94.56           N  
ANISOU 6023  N   MET B 340    12156  11529  12243    960   -768   -286       N  
ATOM   6024  CA  MET B 340      49.208  17.820  68.311  1.00 85.44           C  
ANISOU 6024  CA  MET B 340    11065  10339  11058    890   -732   -240       C  
ATOM   6025  C   MET B 340      50.394  16.855  68.330  1.00 79.79           C  
ANISOU 6025  C   MET B 340    10437   9559  10321    951   -782   -254       C  
ATOM   6026  O   MET B 340      51.548  17.275  68.248  1.00 75.26           O  
ANISOU 6026  O   MET B 340     9821   8969   9805   1025   -839   -306       O  
ATOM   6027  CB  MET B 340      48.869  18.272  66.885  1.00 80.00           C  
ANISOU 6027  CB  MET B 340    10274   9672  10451    824   -705   -230       C  
ATOM   6028  CG  MET B 340      48.556  17.145  65.922  1.00 92.50           C  
ANISOU 6028  CG  MET B 340    11908  11223  12016    756   -672   -187       C  
ATOM   6029  SD  MET B 340      48.595  17.775  64.197  1.00 97.31           S  
ANISOU 6029  SD  MET B 340    12399  11846  12730    715   -662   -191       S  
ATOM   6030  CE  MET B 340      47.135  18.807  64.174  1.00 77.18           C  
ANISOU 6030  CE  MET B 340     9765   9367  10194    653   -613   -185       C  
ATOM   6031  N   CYS B 341      50.076  15.564  68.476  1.00 75.59           N  
ANISOU 6031  N   CYS B 341    10028   8988   9706    920   -758   -212       N  
ATOM   6032  CA  CYS B 341      51.040  14.485  68.367  1.00 71.75           C  
ANISOU 6032  CA  CYS B 341     9636   8438   9189    962   -801   -218       C  
ATOM   6033  C   CYS B 341      50.928  13.887  66.973  1.00 71.80           C  
ANISOU 6033  C   CYS B 341     9619   8428   9233    890   -777   -188       C  
ATOM   6034  O   CYS B 341      49.888  14.020  66.324  1.00 73.69           O  
ANISOU 6034  O   CYS B 341     9811   8699   9491    804   -718   -152       O  
ATOM   6035  CB  CYS B 341      50.802  13.400  69.411  1.00 67.31           C  
ANISOU 6035  CB  CYS B 341     9234   7835   8505    978   -791   -190       C  
ATOM   6036  SG  CYS B 341      51.226  13.916  71.098  1.00107.05           S  
ANISOU 6036  SG  CYS B 341    14321  12872  13481   1093   -837   -233       S  
ATOM   6037  N   LYS B 342      52.015  13.237  66.534  1.00 73.99           N  
ANISOU 6037  N   LYS B 342     9933   8658   9524    932   -827   -208       N  
ATOM   6038  CA  LYS B 342      52.067  12.606  65.224  1.00 74.86           C  
ANISOU 6038  CA  LYS B 342    10027   8748   9669    876   -815   -184       C  
ATOM   6039  C   LYS B 342      51.168  11.366  65.171  1.00 75.15           C  
ANISOU 6039  C   LYS B 342    10165   8762   9626    805   -765   -122       C  
ATOM   6040  O   LYS B 342      51.027  10.754  64.113  1.00 81.07           O  
ANISOU 6040  O   LYS B 342    10907   9498  10397    752   -749    -96       O  
ATOM   6041  CB  LYS B 342      53.515  12.348  64.787  1.00 69.88           C  
ANISOU 6041  CB  LYS B 342     9395   8077   9081    943   -884   -232       C  
ATOM   6042  CG  LYS B 342      54.252  13.587  64.291  1.00 65.30           C  
ANISOU 6042  CG  LYS B 342     8682   7519   8610    979   -909   -287       C  
ATOM   6043  CD  LYS B 342      55.557  13.339  63.563  1.00 64.29           C  
ANISOU 6043  CD  LYS B 342     8533   7354   8541   1021   -960   -335       C  
ATOM   6044  CE  LYS B 342      56.104  14.633  62.982  1.00 74.64           C  
ANISOU 6044  CE  LYS B 342     9708   8687   9966   1039   -961   -383       C  
ATOM   6045  NZ  LYS B 342      57.208  14.456  62.005  1.00 86.73           N  
ANISOU 6045  NZ  LYS B 342    11202  10185  11568   1056   -989   -423       N  
ATOM   6046  N   THR B 343      50.516  11.045  66.293  1.00 73.82           N  
ANISOU 6046  N   THR B 343    10088   8590   9371    801   -736   -100       N  
ATOM   6047  CA  THR B 343      49.674   9.868  66.460  1.00 81.35           C  
ANISOU 6047  CA  THR B 343    11151   9514  10244    737   -682    -46       C  
ATOM   6048  C   THR B 343      48.191  10.183  66.203  1.00 78.53           C  
ANISOU 6048  C   THR B 343    10738   9204   9898    637   -596    -14       C  
ATOM   6049  O   THR B 343      47.363   9.262  66.169  1.00 73.30           O  
ANISOU 6049  O   THR B 343    10145   8520   9186    568   -539     27       O  
ATOM   6050  CB  THR B 343      49.946   9.183  67.814  1.00 86.98           C  
ANISOU 6050  CB  THR B 343    12017  10182  10848    796   -698    -44       C  
ATOM   6051  OG1 THR B 343      49.110   8.028  67.852  1.00115.90           O  
ANISOU 6051  OG1 THR B 343    15785  13812  14441    724   -635     10       O  
ATOM   6052  CG2 THR B 343      49.627  10.036  69.023  1.00 76.12           C  
ANISOU 6052  CG2 THR B 343    10641   8840   9442    835   -689    -61       C  
ATOM   6053  N   ASP B 344      47.863  11.477  66.041  1.00 68.55           N  
ANISOU 6053  N   ASP B 344     9349   7999   8698    631   -590    -37       N  
ATOM   6054  CA  ASP B 344      46.491  11.955  65.925  1.00 76.85           C  
ANISOU 6054  CA  ASP B 344    10338   9100   9760    550   -519    -21       C  
ATOM   6055  C   ASP B 344      45.975  11.843  64.482  1.00 79.07           C  
ANISOU 6055  C   ASP B 344    10543   9394  10105    479   -492     -8       C  
ATOM   6056  O   ASP B 344      46.766  11.816  63.539  1.00 77.62           O  
ANISOU 6056  O   ASP B 344    10321   9195   9975    502   -533    -17       O  
ATOM   6057  CB  ASP B 344      46.383  13.359  66.530  1.00 92.89           C  
ANISOU 6057  CB  ASP B 344    12284  11188  11823    585   -531    -55       C  
ATOM   6058  CG  ASP B 344      46.600  13.398  68.040  1.00 99.47           C  
ANISOU 6058  CG  ASP B 344    13200  12012  12581    647   -545    -64       C  
ATOM   6059  OD1 ASP B 344      46.364  12.349  68.697  1.00101.86           O  
ANISOU 6059  OD1 ASP B 344    13633  12273  12795    636   -517    -34       O  
ATOM   6060  OD2 ASP B 344      47.002  14.480  68.550  1.00 89.78           O1-
ANISOU 6060  OD2 ASP B 344    11910  10818  11384    708   -584   -101       O1-
ATOM   6061  N   ILE B 345      44.640  11.790  64.303  1.00 73.26           N  
ANISOU 6061  N   ILE B 345     9784   8686   9366    395   -423      6       N  
ATOM   6062  CA  ILE B 345      44.053  11.642  62.974  1.00 79.46           C  
ANISOU 6062  CA  ILE B 345    10502   9483  10206    333   -398     12       C  
ATOM   6063  C   ILE B 345      44.416  12.840  62.120  1.00 74.31           C  
ANISOU 6063  C   ILE B 345     9726   8869   9640    362   -434    -16       C  
ATOM   6064  O   ILE B 345      44.709  12.653  60.937  1.00 78.94           O  
ANISOU 6064  O   ILE B 345    10277   9443  10273    356   -448    -12       O  
ATOM   6065  CB  ILE B 345      42.521  11.472  62.953  1.00 85.72           C  
ANISOU 6065  CB  ILE B 345    11279  10302  10987    243   -320     17       C  
ATOM   6066  CG1 ILE B 345      41.857  12.200  64.132  1.00 97.75           C  
ANISOU 6066  CG1 ILE B 345    12796  11866  12478    237   -289      2       C  
ATOM   6067  CG2 ILE B 345      42.165   9.993  62.857  1.00 84.19           C  
ANISOU 6067  CG2 ILE B 345    11183  10058  10749    191   -278     49       C  
ATOM   6068  CD1 ILE B 345      40.396  12.601  63.944  1.00 82.89           C  
ANISOU 6068  CD1 ILE B 345    10844  10033  10617    159   -227    -17       C  
ATOM   6069  N   ALA B 346      44.337  14.039  62.717  1.00 62.68           N  
ANISOU 6069  N   ALA B 346     8193   7441   8183    390   -443    -42       N  
ATOM   6070  CA  ALA B 346      44.569  15.248  61.939  1.00 64.02           C  
ANISOU 6070  CA  ALA B 346     8248   7645   8433    412   -468    -69       C  
ATOM   6071  C   ALA B 346      45.951  15.227  61.273  1.00 67.76           C  
ANISOU 6071  C   ALA B 346     8712   8082   8951    470   -522    -76       C  
ATOM   6072  O   ALA B 346      46.111  15.693  60.135  1.00 59.33           O  
ANISOU 6072  O   ALA B 346     7575   7021   7948    468   -528    -84       O  
ATOM   6073  CB  ALA B 346      44.344  16.480  62.766  1.00 54.75           C  
ANISOU 6073  CB  ALA B 346     7016   6519   7267    437   -474    -96       C  
ATOM   6074  N   PHE B 347      46.952  14.685  61.986  1.00 69.31           N  
ANISOU 6074  N   PHE B 347     8984   8238   9112    525   -561    -79       N  
ATOM   6075  CA  PHE B 347      48.306  14.630  61.463  1.00 62.44           C  
ANISOU 6075  CA  PHE B 347     8108   7333   8285    583   -613    -97       C  
ATOM   6076  C   PHE B 347      48.432  13.525  60.416  1.00 63.82           C  
ANISOU 6076  C   PHE B 347     8318   7469   8460    550   -610    -70       C  
ATOM   6077  O   PHE B 347      49.078  13.721  59.380  1.00 51.89           O  
ANISOU 6077  O   PHE B 347     6758   5948   7010    564   -630    -81       O  
ATOM   6078  CB  PHE B 347      49.342  14.505  62.580  1.00 58.67           C  
ANISOU 6078  CB  PHE B 347     7691   6828   7775    662   -664   -123       C  
ATOM   6079  CG  PHE B 347      50.733  14.397  62.015  1.00 62.39           C  
ANISOU 6079  CG  PHE B 347     8151   7261   8295    718   -718   -153       C  
ATOM   6080  CD1 PHE B 347      51.370  15.508  61.480  1.00 67.30           C  
ANISOU 6080  CD1 PHE B 347     8670   7897   9005    750   -736   -192       C  
ATOM   6081  CD2 PHE B 347      51.362  13.167  61.915  1.00 63.87           C  
ANISOU 6081  CD2 PHE B 347     8427   7396   8444    733   -746   -145       C  
ATOM   6082  CE1 PHE B 347      52.626  15.405  60.897  1.00 67.80           C  
ANISOU 6082  CE1 PHE B 347     8718   7924   9120    794   -776   -225       C  
ATOM   6083  CE2 PHE B 347      52.626  13.067  61.350  1.00 65.60           C  
ANISOU 6083  CE2 PHE B 347     8630   7583   8712    781   -795   -179       C  
ATOM   6084  CZ  PHE B 347      53.252  14.181  60.829  1.00 61.57           C  
ANISOU 6084  CZ  PHE B 347     8014   7088   8293    810   -808   -221       C  
ATOM   6085  N   ARG B 348      47.849  12.352  60.713  1.00 71.11           N  
ANISOU 6085  N   ARG B 348     9332   8370   9315    509   -583    -37       N  
ATOM   6086  CA  ARG B 348      47.962  11.226  59.794  1.00 73.44           C  
ANISOU 6086  CA  ARG B 348     9667   8628   9608    479   -583    -12       C  
ATOM   6087  C   ARG B 348      47.181  11.494  58.504  1.00 71.07           C  
ANISOU 6087  C   ARG B 348     9286   8356   9363    425   -549     -3       C  
ATOM   6088  O   ARG B 348      47.653  11.151  57.424  1.00 67.67           O  
ANISOU 6088  O   ARG B 348     8838   7905   8969    428   -567      1       O  
ATOM   6089  CB  ARG B 348      47.520   9.930  60.471  1.00 72.32           C  
ANISOU 6089  CB  ARG B 348     9645   8452   9382    448   -559     20       C  
ATOM   6090  CG  ARG B 348      48.417   9.479  61.612  1.00 74.85           C  
ANISOU 6090  CG  ARG B 348    10067   8733   9639    513   -601     11       C  
ATOM   6091  CD  ARG B 348      47.857   8.222  62.265  1.00 75.36           C  
ANISOU 6091  CD  ARG B 348    10260   8759   9615    477   -566     48       C  
ATOM   6092  NE  ARG B 348      46.556   8.547  62.829  1.00 77.86           N  
ANISOU 6092  NE  ARG B 348    10567   9110   9908    419   -495     60       N  
ATOM   6093  CZ  ARG B 348      45.878   7.762  63.638  1.00 78.47           C  
ANISOU 6093  CZ  ARG B 348    10745   9162   9907    383   -445     86       C  
ATOM   6094  NH1 ARG B 348      46.383   6.604  64.014  1.00105.81           N  
ANISOU 6094  NH1 ARG B 348    14335  12564  13304    403   -461    107       N  
ATOM   6095  NH2 ARG B 348      44.706   8.142  64.084  1.00 73.46           N  
ANISOU 6095  NH2 ARG B 348    10088   8562   9260    327   -378     89       N  
ATOM   6096  N   LEU B 349      45.991  12.103  58.619  1.00 64.09           N  
ANISOU 6096  N   LEU B 349     8353   7517   8483    380   -503     -5       N  
ATOM   6097  CA  LEU B 349      45.218  12.500  57.452  1.00 62.11           C  
ANISOU 6097  CA  LEU B 349     8022   7294   8282    341   -477     -8       C  
ATOM   6098  C   LEU B 349      45.968  13.568  56.641  1.00 62.93           C  
ANISOU 6098  C   LEU B 349     8044   7408   8457    387   -508    -30       C  
ATOM   6099  O   LEU B 349      45.905  13.568  55.412  1.00 60.31           O  
ANISOU 6099  O   LEU B 349     7674   7074   8167    378   -505    -27       O  
ATOM   6100  CB  LEU B 349      43.824  12.971  57.894  1.00 61.47           C  
ANISOU 6100  CB  LEU B 349     7909   7260   8188    290   -427    -18       C  
ATOM   6101  CG  LEU B 349      42.845  13.346  56.778  1.00 62.43           C  
ANISOU 6101  CG  LEU B 349     7954   7413   8355    250   -400    -32       C  
ATOM   6102  CD1 LEU B 349      42.514  12.130  55.932  1.00 69.32           C  
ANISOU 6102  CD1 LEU B 349     8859   8255   9224    212   -384    -13       C  
ATOM   6103  CD2 LEU B 349      41.566  13.946  57.348  1.00 68.66           C  
ANISOU 6103  CD2 LEU B 349     8704   8251   9132    208   -359    -55       C  
ATOM   6104  N   ALA B 350      46.661  14.492  57.325  1.00 58.45           N  
ANISOU 6104  N   ALA B 350     7451   6851   7904    438   -534    -54       N  
ATOM   6105  CA  ALA B 350      47.477  15.486  56.641  1.00 57.22           C  
ANISOU 6105  CA  ALA B 350     7225   6698   7820    482   -558    -77       C  
ATOM   6106  C   ALA B 350      48.689  14.824  55.991  1.00 58.45           C  
ANISOU 6106  C   ALA B 350     7408   6804   7996    514   -591    -76       C  
ATOM   6107  O   ALA B 350      49.195  15.279  54.957  1.00 48.00           O  
ANISOU 6107  O   ALA B 350     6034   5472   6730    530   -596    -85       O  
ATOM   6108  CB  ALA B 350      47.894  16.576  57.584  1.00 52.19           C  
ANISOU 6108  CB  ALA B 350     6552   6081   7197    527   -576   -108       C  
ATOM   6109  N   LYS B 351      49.140  13.722  56.592  1.00 60.05           N  
ANISOU 6109  N   LYS B 351     7696   6973   8148    523   -614    -66       N  
ATOM   6110  CA  LYS B 351      50.312  13.026  56.090  1.00 61.22           C  
ANISOU 6110  CA  LYS B 351     7875   7075   8311    555   -653    -71       C  
ATOM   6111  C   LYS B 351      50.018  12.403  54.729  1.00 55.61           C  
ANISOU 6111  C   LYS B 351     7157   6354   7620    518   -637    -45       C  
ATOM   6112  O   LYS B 351      50.921  12.247  53.919  1.00 58.50           O  
ANISOU 6112  O   LYS B 351     7511   6693   8024    543   -661    -54       O  
ATOM   6113  CB  LYS B 351      50.807  12.030  57.139  1.00 60.62           C  
ANISOU 6113  CB  LYS B 351     7899   6965   8168    580   -685    -70       C  
ATOM   6114  CG  LYS B 351      52.221  11.511  56.919  1.00 51.96           C  
ANISOU 6114  CG  LYS B 351     6831   5823   7088    632   -740    -96       C  
ATOM   6115  CD  LYS B 351      52.916  11.165  58.211  1.00 53.64           C  
ANISOU 6115  CD  LYS B 351     7120   6012   7251    689   -785   -121       C  
ATOM   6116  CE  LYS B 351      52.161  10.248  59.154  1.00 57.26           C  
ANISOU 6116  CE  LYS B 351     7683   6461   7614    664   -768    -86       C  
ATOM   6117  NZ  LYS B 351      52.055   8.864  58.627  1.00 61.20           N  
ANISOU 6117  NZ  LYS B 351     8255   6923   8074    629   -769    -51       N  
ATOM   6118  N   SER B 352      48.758  12.046  54.496  1.00 61.00           N  
ANISOU 6118  N   SER B 352     7844   7056   8276    461   -597    -18       N  
ATOM   6119  CA  SER B 352      48.321  11.406  53.261  1.00 71.80           C  
ANISOU 6119  CA  SER B 352     9205   8416   9658    427   -583      4       C  
ATOM   6120  C   SER B 352      47.827  12.447  52.263  1.00 69.50           C  
ANISOU 6120  C   SER B 352     8829   8156   9422    423   -560     -7       C  
ATOM   6121  O   SER B 352      48.064  12.295  51.072  1.00 71.12           O  
ANISOU 6121  O   SER B 352     9014   8347   9660    430   -564     -1       O  
ATOM   6122  CB  SER B 352      47.242  10.351  53.487  1.00 64.75           C  
ANISOU 6122  CB  SER B 352     8365   7522   8714    370   -553     29       C  
ATOM   6123  OG  SER B 352      47.771   9.258  54.212  1.00 63.70           O  
ANISOU 6123  OG  SER B 352     8324   7351   8529    376   -575     43       O  
ATOM   6124  N   THR B 353      47.070  13.440  52.746  1.00 65.05           N  
ANISOU 6124  N   THR B 353     8222   7633   8862    413   -536    -21       N  
ATOM   6125  CA  THR B 353      46.474  14.422  51.859  1.00 62.19           C  
ANISOU 6125  CA  THR B 353     7789   7299   8541    411   -515    -33       C  
ATOM   6126  C   THR B 353      47.550  15.351  51.304  1.00 66.96           C  
ANISOU 6126  C   THR B 353     8351   7889   9202    461   -531    -49       C  
ATOM   6127  O   THR B 353      47.476  15.711  50.131  1.00 70.43           O  
ANISOU 6127  O   THR B 353     8758   8325   9676    469   -521    -49       O  
ATOM   6128  CB  THR B 353      45.355  15.216  52.528  1.00 55.79           C  
ANISOU 6128  CB  THR B 353     6943   6536   7718    386   -489    -50       C  
ATOM   6129  OG1 THR B 353      44.420  14.272  53.028  1.00 54.50           O  
ANISOU 6129  OG1 THR B 353     6822   6378   7506    336   -466    -38       O  
ATOM   6130  CG2 THR B 353      44.671  16.136  51.551  1.00 51.71           C  
ANISOU 6130  CG2 THR B 353     6363   6047   7239    387   -473    -66       C  
ATOM   6131  N   LEU B 354      48.550  15.701  52.131  1.00 62.33           N  
ANISOU 6131  N   LEU B 354     7768   7290   8624    498   -555    -66       N  
ATOM   6132  CA  LEU B 354      49.663  16.540  51.699  1.00 61.76           C  
ANISOU 6132  CA  LEU B 354     7655   7199   8612    543   -566    -90       C  
ATOM   6133  C   LEU B 354      50.520  15.830  50.652  1.00 58.80           C  
ANISOU 6133  C   LEU B 354     7299   6781   8259    556   -578    -82       C  
ATOM   6134  O   LEU B 354      51.234  16.484  49.899  1.00 55.14           O  
ANISOU 6134  O   LEU B 354     6800   6300   7851    583   -571    -97       O  
ATOM   6135  CB  LEU B 354      50.497  16.951  52.910  1.00 60.67           C  
ANISOU 6135  CB  LEU B 354     7516   7057   8479    581   -591   -120       C  
ATOM   6136  CG  LEU B 354      49.888  18.064  53.749  1.00 64.71           C  
ANISOU 6136  CG  LEU B 354     7985   7611   8991    583   -580   -136       C  
ATOM   6137  CD1 LEU B 354      50.815  18.384  54.883  1.00 76.20           C  
ANISOU 6137  CD1 LEU B 354     9440   9057  10454    630   -611   -170       C  
ATOM   6138  CD2 LEU B 354      49.658  19.319  52.926  1.00 74.51           C  
ANISOU 6138  CD2 LEU B 354     9156   8867  10286    588   -554   -147       C  
ATOM   6139  N   THR B 355      50.393  14.500  50.583  1.00 62.73           N  
ANISOU 6139  N   THR B 355     7855   7264   8716    534   -592    -58       N  
ATOM   6140  CA  THR B 355      51.083  13.678  49.602  1.00 54.26           C  
ANISOU 6140  CA  THR B 355     6803   6154   7657    542   -607    -48       C  
ATOM   6141  C   THR B 355      50.317  13.691  48.281  1.00 60.53           C  
ANISOU 6141  C   THR B 355     7576   6958   8466    522   -580    -27       C  
ATOM   6142  O   THR B 355      50.935  13.888  47.240  1.00 68.29           O  
ANISOU 6142  O   THR B 355     8540   7919   9489    544   -577    -30       O  
ATOM   6143  CB  THR B 355      51.282  12.240  50.103  1.00 53.94           C  
ANISOU 6143  CB  THR B 355     6837   6091   7565    530   -638    -33       C  
ATOM   6144  OG1 THR B 355      52.041  12.292  51.310  1.00 51.66           O  
ANISOU 6144  OG1 THR B 355     6575   5792   7261    560   -668    -58       O  
ATOM   6145  CG2 THR B 355      51.938  11.335  49.083  1.00 52.46           C  
ANISOU 6145  CG2 THR B 355     6670   5871   7391    536   -659    -23       C  
ATOM   6146  N   LEU B 356      48.985  13.507  48.330  1.00 57.48           N  
ANISOU 6146  N   LEU B 356     7191   6601   8048    485   -559    -12       N  
ATOM   6147  CA  LEU B 356      48.177  13.358  47.131  1.00 54.38           C  
ANISOU 6147  CA  LEU B 356     6782   6216   7663    472   -541      0       C  
ATOM   6148  C   LEU B 356      48.089  14.670  46.354  1.00 54.76           C  
ANISOU 6148  C   LEU B 356     6778   6274   7752    499   -519    -15       C  
ATOM   6149  O   LEU B 356      48.037  14.644  45.126  1.00 61.05           O  
ANISOU 6149  O   LEU B 356     7569   7060   8568    514   -512     -8       O  
ATOM   6150  CB  LEU B 356      46.801  12.801  47.499  1.00 52.13           C  
ANISOU 6150  CB  LEU B 356     6509   5958   7338    425   -525      6       C  
ATOM   6151  CG  LEU B 356      46.853  11.324  47.901  1.00 59.10           C  
ANISOU 6151  CG  LEU B 356     7453   6819   8182    397   -539     26       C  
ATOM   6152  CD1 LEU B 356      45.604  10.848  48.605  1.00 47.74           C  
ANISOU 6152  CD1 LEU B 356     6031   5403   6705    346   -513     27       C  
ATOM   6153  CD2 LEU B 356      47.157  10.419  46.726  1.00 55.56           C  
ANISOU 6153  CD2 LEU B 356     7019   6344   7746    404   -555     42       C  
ATOM   6154  N   ILE B 357      48.093  15.807  47.054  1.00 50.14           N  
ANISOU 6154  N   ILE B 357     6162   5710   7181    509   -509    -35       N  
ATOM   6155  CA  ILE B 357      47.895  17.077  46.378  1.00 55.36           C  
ANISOU 6155  CA  ILE B 357     6780   6380   7876    533   -487    -48       C  
ATOM   6156  C   ILE B 357      49.012  17.341  45.367  1.00 66.44           C  
ANISOU 6156  C   ILE B 357     8181   7740   9322    569   -481    -47       C  
ATOM   6157  O   ILE B 357      48.721  17.581  44.193  1.00 63.77           O  
ANISOU 6157  O   ILE B 357     7840   7394   8996    585   -464    -40       O  
ATOM   6158  CB  ILE B 357      47.682  18.242  47.365  1.00 53.07           C  
ANISOU 6158  CB  ILE B 357     6454   6119   7592    536   -480    -71       C  
ATOM   6159  CG1 ILE B 357      46.352  18.065  48.108  1.00 49.18           C  
ANISOU 6159  CG1 ILE B 357     5959   5671   7056    497   -477    -75       C  
ATOM   6160  CG2 ILE B 357      47.788  19.581  46.632  1.00 49.78           C  
ANISOU 6160  CG2 ILE B 357     6000   5699   7217    567   -458    -85       C  
ATOM   6161  CD1 ILE B 357      46.102  19.042  49.207  1.00 49.64           C  
ANISOU 6161  CD1 ILE B 357     5985   5763   7114    497   -475    -96       C  
ATOM   6162  N   PRO B 358      50.317  17.334  45.748  1.00 74.13           N  
ANISOU 6162  N   PRO B 358     9156   8685  10324    588   -492    -58       N  
ATOM   6163  CA  PRO B 358      51.352  17.612  44.760  1.00 66.61           C  
ANISOU 6163  CA  PRO B 358     8198   7691   9418    618   -478    -63       C  
ATOM   6164  C   PRO B 358      51.544  16.430  43.818  1.00 71.37           C  
ANISOU 6164  C   PRO B 358     8836   8271  10009    615   -491    -41       C  
ATOM   6165  O   PRO B 358      52.164  16.571  42.768  1.00 76.27           O  
ANISOU 6165  O   PRO B 358     9458   8861  10661    637   -473    -39       O  
ATOM   6166  CB  PRO B 358      52.576  17.852  45.647  1.00 66.96           C  
ANISOU 6166  CB  PRO B 358     8229   7716   9495    634   -492    -95       C  
ATOM   6167  CG  PRO B 358      52.359  16.982  46.834  1.00 56.40           C  
ANISOU 6167  CG  PRO B 358     6920   6398   8112    616   -529    -92       C  
ATOM   6168  CD  PRO B 358      50.875  17.091  47.096  1.00 62.12           C  
ANISOU 6168  CD  PRO B 358     7644   7166   8793    586   -518    -74       C  
ATOM   6169  N   LEU B 359      51.000  15.270  44.195  1.00 68.32           N  
ANISOU 6169  N   LEU B 359     8482   7900   9578    587   -518    -24       N  
ATOM   6170  CA  LEU B 359      51.130  14.075  43.378  1.00 66.01           C  
ANISOU 6170  CA  LEU B 359     8221   7588   9273    584   -536     -3       C  
ATOM   6171  C   LEU B 359      50.167  14.153  42.195  1.00 68.52           C  
ANISOU 6171  C   LEU B 359     8534   7916   9586    588   -516     12       C  
ATOM   6172  O   LEU B 359      50.499  13.699  41.111  1.00 75.43           O  
ANISOU 6172  O   LEU B 359     9420   8768  10471    605   -518     24       O  
ATOM   6173  CB  LEU B 359      50.811  12.873  44.269  1.00 74.28           C  
ANISOU 6173  CB  LEU B 359     9306   8645  10274    552   -567      8       C  
ATOM   6174  CG  LEU B 359      51.230  11.490  43.783  1.00 68.90           C  
ANISOU 6174  CG  LEU B 359     8663   7939   9578    547   -597     25       C  
ATOM   6175  CD1 LEU B 359      52.753  11.373  43.772  1.00 69.80           C  
ANISOU 6175  CD1 LEU B 359     8782   8017   9720    575   -621      6       C  
ATOM   6176  CD2 LEU B 359      50.647  10.446  44.726  1.00 61.26           C  
ANISOU 6176  CD2 LEU B 359     7736   6981   8559    511   -617     38       C  
ATOM   6177  N   LEU B 360      48.976  14.728  42.407  1.00 71.79           N  
ANISOU 6177  N   LEU B 360     8930   8365   9983    576   -500      7       N  
ATOM   6178  CA  LEU B 360      47.927  14.748  41.399  1.00 62.87           C  
ANISOU 6178  CA  LEU B 360     7796   7248   8844    585   -489      9       C  
ATOM   6179  C   LEU B 360      47.791  16.124  40.752  1.00 62.48           C  
ANISOU 6179  C   LEU B 360     7726   7197   8817    621   -460     -3       C  
ATOM   6180  O   LEU B 360      47.262  16.197  39.653  1.00 77.53           O  
ANISOU 6180  O   LEU B 360     9639   9100  10720    647   -453     -2       O  
ATOM   6181  CB  LEU B 360      46.594  14.366  42.042  1.00 61.89           C  
ANISOU 6181  CB  LEU B 360     7667   7163   8687    547   -494      1       C  
ATOM   6182  CG  LEU B 360      46.243  12.883  42.117  1.00 72.10           C  
ANISOU 6182  CG  LEU B 360     8985   8454   9954    515   -513     15       C  
ATOM   6183  CD1 LEU B 360      47.187  12.107  43.027  1.00 74.73           C  
ANISOU 6183  CD1 LEU B 360     9351   8768  10276    496   -533     30       C  
ATOM   6184  CD2 LEU B 360      44.825  12.746  42.634  1.00 87.61           C  
ANISOU 6184  CD2 LEU B 360    10937  10456  11897    478   -502     -4       C  
ATOM   6185  N   CYS B 361      48.239  17.202  41.412  1.00 60.45           N  
ANISOU 6185  N   CYS B 361     7447   6941   8580    626   -444    -17       N  
ATOM   6186  CA  CYS B 361      47.950  18.546  40.923  1.00 69.82           C  
ANISOU 6186  CA  CYS B 361     8618   8128   9782    657   -416    -30       C  
ATOM   6187  C   CYS B 361      49.179  19.265  40.359  1.00 68.08           C  
ANISOU 6187  C   CYS B 361     8400   7862   9605    689   -386    -29       C  
ATOM   6188  O   CYS B 361      49.058  20.384  39.842  1.00 60.57           O  
ANISOU 6188  O   CYS B 361     7447   6901   8668    717   -356    -36       O  
ATOM   6189  CB  CYS B 361      47.256  19.422  41.971  1.00 84.28           C  
ANISOU 6189  CB  CYS B 361    10418   9999  11606    640   -414    -51       C  
ATOM   6190  SG  CYS B 361      45.462  19.566  41.718  1.00102.87           S  
ANISOU 6190  SG  CYS B 361    12763  12400  13924    635   -420    -71       S  
ATOM   6191  N   THR B 362      50.355  18.626  40.433  1.00 76.55           N  
ANISOU 6191  N   THR B 362     9482   8905  10700    685   -393    -24       N  
ATOM   6192  CA  THR B 362      51.589  19.278  40.004  1.00 66.85           C  
ANISOU 6192  CA  THR B 362     8249   7631   9521    709   -360    -33       C  
ATOM   6193  C   THR B 362      51.634  19.395  38.483  1.00 63.60           C  
ANISOU 6193  C   THR B 362     7867   7186   9112    742   -330    -17       C  
ATOM   6194  O   THR B 362      52.019  20.421  37.950  1.00 54.83           O  
ANISOU 6194  O   THR B 362     6758   6044   8029    767   -284    -23       O  
ATOM   6195  CB  THR B 362      52.832  18.632  40.635  1.00 67.68           C  
ANISOU 6195  CB  THR B 362     8348   7716   9652    697   -380    -47       C  
ATOM   6196  OG1 THR B 362      53.801  19.668  40.628  1.00 73.46           O  
ANISOU 6196  OG1 THR B 362     9056   8415  10440    715   -342    -73       O  
ATOM   6197  CG2 THR B 362      53.394  17.435  39.900  1.00 67.37           C  
ANISOU 6197  CG2 THR B 362     8337   7652   9607    699   -398    -33       C  
ATOM   6198  N   HIS B 363      51.258  18.318  37.797  1.00 74.73           N  
ANISOU 6198  N   HIS B 363     9302   8598  10492    744   -353      3       N  
ATOM   6199  CA  HIS B 363      51.239  18.268  36.346  1.00 76.33           C  
ANISOU 6199  CA  HIS B 363     9538   8773  10690    782   -333     19       C  
ATOM   6200  C   HIS B 363      50.395  19.392  35.737  1.00 77.01           C  
ANISOU 6200  C   HIS B 363     9638   8859  10762    817   -303     16       C  
ATOM   6201  O   HIS B 363      50.818  20.012  34.760  1.00 78.09           O  
ANISOU 6201  O   HIS B 363     9803   8955  10912    854   -260     22       O  
ATOM   6202  CB  HIS B 363      50.746  16.889  35.879  1.00 81.59           C  
ANISOU 6202  CB  HIS B 363    10223   9454  11325    778   -374     36       C  
ATOM   6203  CG  HIS B 363      50.793  16.752  34.394  1.00 85.72           C  
ANISOU 6203  CG  HIS B 363    10781   9948  11843    823   -358     51       C  
ATOM   6204  ND1 HIS B 363      49.685  16.990  33.602  1.00 88.55           N  
ANISOU 6204  ND1 HIS B 363    11157  10316  12170    860   -358     51       N  
ATOM   6205  CD2 HIS B 363      51.814  16.482  33.549  1.00 75.78           C  
ANISOU 6205  CD2 HIS B 363     9542   8647  10604    843   -340     61       C  
ATOM   6206  CE1 HIS B 363      50.005  16.830  32.336  1.00 83.50           C  
ANISOU 6206  CE1 HIS B 363    10553   9644  11528    904   -343     65       C  
ATOM   6207  NE2 HIS B 363      51.305  16.511  32.283  1.00 84.41           N  
ANISOU 6207  NE2 HIS B 363    10669   9727  11675    891   -329     73       N  
ATOM   6208  N   GLU B 364      49.182  19.605  36.267  1.00 71.62           N  
ANISOU 6208  N   GLU B 364     8940   8222  10050    807   -325      4       N  
ATOM   6209  CA  GLU B 364      48.259  20.566  35.692  1.00 65.96           C  
ANISOU 6209  CA  GLU B 364     8239   7511   9314    845   -309     -6       C  
ATOM   6210  C   GLU B 364      48.843  21.973  35.784  1.00 64.34           C  
ANISOU 6210  C   GLU B 364     8032   7276   9138    860   -262    -14       C  
ATOM   6211  O   GLU B 364      48.654  22.788  34.880  1.00 66.23           O  
ANISOU 6211  O   GLU B 364     8307   7488   9369    906   -231    -13       O  
ATOM   6212  CB  GLU B 364      46.925  20.512  36.432  1.00 88.92           C  
ANISOU 6212  CB  GLU B 364    11118  10474  12191    823   -344    -28       C  
ATOM   6213  CG  GLU B 364      45.825  21.358  35.790  1.00117.63           C  
ANISOU 6213  CG  GLU B 364    14770  14121  15801    867   -341    -50       C  
ATOM   6214  CD  GLU B 364      45.421  20.937  34.379  1.00122.47           C  
ANISOU 6214  CD  GLU B 364    15428  14714  16391    921   -347    -47       C  
ATOM   6215  OE1 GLU B 364      45.451  19.712  34.128  1.00116.34           O  
ANISOU 6215  OE1 GLU B 364    14652  13941  15610    910   -371    -36       O  
ATOM   6216  OE2 GLU B 364      45.133  21.841  33.520  1.00101.58           O1-
ANISOU 6216  OE2 GLU B 364    12820  12046  13731    979   -328    -56       O1-
ATOM   6217  N   VAL B 365      49.566  22.240  36.874  1.00 63.68           N  
ANISOU 6217  N   VAL B 365     7911   7197   9089    826   -257    -23       N  
ATOM   6218  CA  VAL B 365      50.116  23.565  37.134  1.00 68.40           C  
ANISOU 6218  CA  VAL B 365     8495   7770   9723    834   -214    -37       C  
ATOM   6219  C   VAL B 365      51.375  23.824  36.292  1.00 69.71           C  
ANISOU 6219  C   VAL B 365     8686   7869   9930    855   -159    -29       C  
ATOM   6220  O   VAL B 365      51.568  24.926  35.773  1.00 65.47           O  
ANISOU 6220  O   VAL B 365     8170   7295   9410    882   -108    -32       O  
ATOM   6221  CB  VAL B 365      50.381  23.784  38.635  1.00 63.09           C  
ANISOU 6221  CB  VAL B 365     7768   7127   9076    797   -232    -57       C  
ATOM   6222  CG1 VAL B 365      51.105  25.103  38.870  1.00 63.52           C  
ANISOU 6222  CG1 VAL B 365     7803   7152   9181    807   -186    -76       C  
ATOM   6223  CG2 VAL B 365      49.093  23.717  39.457  1.00 58.57           C  
ANISOU 6223  CG2 VAL B 365     7174   6618   8463    776   -274    -67       C  
ATOM   6224  N   ILE B 366      52.233  22.807  36.160  1.00 62.38           N  
ANISOU 6224  N   ILE B 366     7759   6924   9020    840   -168    -23       N  
ATOM   6225  CA  ILE B 366      53.496  22.961  35.463  1.00 65.43           C  
ANISOU 6225  CA  ILE B 366     8160   7250   9450    852   -116    -24       C  
ATOM   6226  C   ILE B 366      53.230  23.260  33.988  1.00 66.53           C  
ANISOU 6226  C   ILE B 366     8362   7351   9565    898    -75     -1       C  
ATOM   6227  O   ILE B 366      53.775  24.216  33.441  1.00 76.01           O  
ANISOU 6227  O   ILE B 366     9587   8501  10794    919     -9     -4       O  
ATOM   6228  CB  ILE B 366      54.404  21.734  35.695  1.00 67.07           C  
ANISOU 6228  CB  ILE B 366     8352   7453   9677    827   -146    -28       C  
ATOM   6229  CG1 ILE B 366      54.962  21.730  37.118  1.00 63.37           C  
ANISOU 6229  CG1 ILE B 366     7831   7004   9242    794   -171    -60       C  
ATOM   6230  CG2 ILE B 366      55.516  21.653  34.663  1.00 79.37           C  
ANISOU 6230  CG2 ILE B 366     9936   8952  11270    843    -96    -28       C  
ATOM   6231  CD1 ILE B 366      55.543  20.398  37.564  1.00 68.36           C  
ANISOU 6231  CD1 ILE B 366     8454   7645   9873    773   -222    -66       C  
ATOM   6232  N   PHE B 367      52.381  22.455  33.354  1.00 64.32           N  
ANISOU 6232  N   PHE B 367     8112   7093   9233    918   -113     19       N  
ATOM   6233  CA  PHE B 367      52.066  22.673  31.955  1.00 69.89           C  
ANISOU 6233  CA  PHE B 367     8881   7764   9908    972    -83     37       C  
ATOM   6234  C   PHE B 367      50.725  23.392  31.806  1.00 81.79           C  
ANISOU 6234  C   PHE B 367    10411   9297  11370   1007    -97     32       C  
ATOM   6235  O   PHE B 367      49.867  22.907  31.075  1.00109.52           O  
ANISOU 6235  O   PHE B 367    13954  12822  14836   1043   -127     38       O  
ATOM   6236  CB  PHE B 367      52.024  21.321  31.239  1.00 65.27           C  
ANISOU 6236  CB  PHE B 367     8315   7185   9299    983   -120     56       C  
ATOM   6237  CG  PHE B 367      53.283  20.501  31.368  1.00 61.66           C  
ANISOU 6237  CG  PHE B 367     7837   6709   8881    951   -119     56       C  
ATOM   6238  CD1 PHE B 367      54.404  20.780  30.593  1.00 56.94           C  
ANISOU 6238  CD1 PHE B 367     7266   6052   8318    966    -57     59       C  
ATOM   6239  CD2 PHE B 367      53.354  19.470  32.286  1.00 52.09           C  
ANISOU 6239  CD2 PHE B 367     6582   5536   7673    908   -177     50       C  
ATOM   6240  CE1 PHE B 367      55.566  20.041  30.719  1.00 48.58           C  
ANISOU 6240  CE1 PHE B 367     6183   4977   7299    937    -60     48       C  
ATOM   6241  CE2 PHE B 367      54.515  18.714  32.385  1.00 53.44           C  
ANISOU 6241  CE2 PHE B 367     6738   5689   7878    885   -183     44       C  
ATOM   6242  CZ  PHE B 367      55.609  18.989  31.599  1.00 51.93           C  
ANISOU 6242  CZ  PHE B 367     6565   5442   7722    900   -128     40       C  
ATOM   6243  N   ALA B 368      50.542  24.533  32.494  1.00 86.15           N  
ANISOU 6243  N   ALA B 368    10944   9855  11936    998    -78     15       N  
ATOM   6244  CA  ALA B 368      49.216  25.124  32.635  1.00 81.01           C  
ANISOU 6244  CA  ALA B 368    10297   9240  11242   1021   -107      0       C  
ATOM   6245  C   ALA B 368      48.581  25.459  31.286  1.00 91.74           C  
ANISOU 6245  C   ALA B 368    11733  10570  12554   1093    -94      6       C  
ATOM   6246  O   ALA B 368      47.436  25.046  31.050  1.00114.35           O  
ANISOU 6246  O   ALA B 368    14603  13471  15373   1118   -145     -8       O  
ATOM   6247  CB  ALA B 368      49.162  26.296  33.585  1.00 71.45           C  
ANISOU 6247  CB  ALA B 368     9052   8042  10055   1001    -93    -21       C  
ATOM   6248  N   PHE B 369      49.297  26.194  30.416  1.00 64.76           N  
ANISOU 6248  N   PHE B 369     8375   7085   9146   1130    -25     21       N  
ATOM   6249  CA  PHE B 369      48.641  26.613  29.181  1.00 63.02           C  
ANISOU 6249  CA  PHE B 369     8239   6834   8872   1209    -14     25       C  
ATOM   6250  C   PHE B 369      49.313  26.036  27.932  1.00 69.91           C  
ANISOU 6250  C   PHE B 369     9173   7653   9737   1246     21     53       C  
ATOM   6251  O   PHE B 369      49.471  26.732  26.932  1.00 89.45           O  
ANISOU 6251  O   PHE B 369    11730  10068  12189   1304     75     65       O  
ATOM   6252  CB  PHE B 369      48.523  28.135  29.117  1.00 58.88           C  
ANISOU 6252  CB  PHE B 369     7755   6275   8343   1238     33     16       C  
ATOM   6253  CG  PHE B 369      47.587  28.732  30.130  1.00 59.88           C  
ANISOU 6253  CG  PHE B 369     7832   6458   8461   1219    -13    -16       C  
ATOM   6254  CD1 PHE B 369      46.230  28.838  29.871  1.00 56.28           C  
ANISOU 6254  CD1 PHE B 369     7397   6038   7948   1266    -67    -43       C  
ATOM   6255  CD2 PHE B 369      48.062  29.155  31.363  1.00 64.63           C  
ANISOU 6255  CD2 PHE B 369     8362   7080   9115   1158     -4    -26       C  
ATOM   6256  CE1 PHE B 369      45.361  29.365  30.821  1.00 61.45           C  
ANISOU 6256  CE1 PHE B 369     8002   6748   8597   1245   -110    -78       C  
ATOM   6257  CE2 PHE B 369      47.188  29.680  32.309  1.00 71.98           C  
ANISOU 6257  CE2 PHE B 369     9246   8067  10037   1141    -48    -55       C  
ATOM   6258  CZ  PHE B 369      45.838  29.797  32.037  1.00 62.59           C  
ANISOU 6258  CZ  PHE B 369     8078   6913   8790   1182    -99    -81       C  
ATOM   6259  N   VAL B 370      49.691  24.757  27.981  1.00 70.15           N  
ANISOU 6259  N   VAL B 370     9168   7703   9781   1216    -10     63       N  
ATOM   6260  CA  VAL B 370      50.437  24.140  26.900  1.00 75.41           C  
ANISOU 6260  CA  VAL B 370     9881   8325  10447   1243     20     88       C  
ATOM   6261  C   VAL B 370      49.572  23.033  26.308  1.00 89.52           C  
ANISOU 6261  C   VAL B 370    11678  10147  12190   1280    -48     88       C  
ATOM   6262  O   VAL B 370      49.259  22.062  26.990  1.00102.00           O  
ANISOU 6262  O   VAL B 370    13195  11781  13778   1237   -109     79       O  
ATOM   6263  CB  VAL B 370      51.796  23.602  27.403  1.00 78.64           C  
ANISOU 6263  CB  VAL B 370    10240   8721  10920   1178     45     95       C  
ATOM   6264  CG1 VAL B 370      52.525  22.803  26.340  1.00 92.02           C  
ANISOU 6264  CG1 VAL B 370    11972  10378  12613   1201     65    116       C  
ATOM   6265  CG2 VAL B 370      52.693  24.705  27.949  1.00 71.89           C  
ANISOU 6265  CG2 VAL B 370     9371   7827  10119   1146    115     85       C  
ATOM   6266  N   MET B 371      49.176  23.173  25.033  1.00113.51           N  
ANISOU 6266  N   MET B 371    14797  13152  15181   1364    -38     95       N  
ATOM   6267  CA  MET B 371      48.489  22.072  24.361  1.00102.15           C  
ANISOU 6267  CA  MET B 371    13365  11739  13707   1406   -100     91       C  
ATOM   6268  C   MET B 371      49.567  21.166  23.753  1.00106.37           C  
ANISOU 6268  C   MET B 371    13908  12246  14263   1398    -80    120       C  
ATOM   6269  O   MET B 371      49.456  19.929  23.926  1.00114.14           O  
ANISOU 6269  O   MET B 371    14844  13270  15255   1373   -138    119       O  
ATOM   6270  CB  MET B 371      47.470  22.520  23.297  1.00 74.70           C  
ANISOU 6270  CB  MET B 371     9968   8247  10167   1510   -114     74       C  
ATOM   6271  N   ARG B 380      58.913  13.558  23.294  1.00126.35           N  
ANISOU 6271  N   ARG B 380    16206  14707  17095   1100   -117    145       N  
ATOM   6272  CA  ARG B 380      57.438  13.608  23.519  1.00112.64           C  
ANISOU 6272  CA  ARG B 380    14478  13011  15310   1124   -162    164       C  
ATOM   6273  C   ARG B 380      56.921  12.196  23.796  1.00105.77           C  
ANISOU 6273  C   ARG B 380    13575  12193  14421   1112   -261    169       C  
ATOM   6274  O   ARG B 380      55.991  12.010  24.588  1.00103.82           O  
ANISOU 6274  O   ARG B 380    13303  11988  14156   1093   -308    167       O  
ATOM   6275  CB  ARG B 380      56.711  14.271  22.340  1.00 91.10           C  
ANISOU 6275  CB  ARG B 380    11821  10257  12537   1202   -121    188       C  
ATOM   6276  N   PHE B 381      57.556  11.201  23.159  1.00114.04           N  
ANISOU 6276  N   PHE B 381    14620  13236  15473   1120   -288    173       N  
ATOM   6277  CA  PHE B 381      57.194   9.799  23.320  1.00115.08           C  
ANISOU 6277  CA  PHE B 381    14724  13410  15590   1109   -379    178       C  
ATOM   6278  C   PHE B 381      57.403   9.383  24.772  1.00127.60           C  
ANISOU 6278  C   PHE B 381    16261  15024  17197   1039   -424    157       C  
ATOM   6279  O   PHE B 381      56.446   8.963  25.426  1.00120.87           O  
ANISOU 6279  O   PHE B 381    15392  14210  16322   1023   -473    162       O  
ATOM   6280  CB  PHE B 381      57.974   8.908  22.352  1.00121.10           C  
ANISOU 6280  CB  PHE B 381    15494  14159  16358   1131   -397    183       C  
ATOM   6281  N   ILE B 382      58.639   9.561  25.273  1.00145.43           N  
ANISOU 6281  N   ILE B 382    18500  17260  19498   1000   -401    130       N  
ATOM   6282  CA  ILE B 382      59.044   9.146  26.614  1.00124.47           C  
ANISOU 6282  CA  ILE B 382    15806  14625  16863    943   -445    104       C  
ATOM   6283  C   ILE B 382      58.238   9.914  27.664  1.00115.56           C  
ANISOU 6283  C   ILE B 382    14666  13515  15724    922   -435    103       C  
ATOM   6284  O   ILE B 382      57.974   9.382  28.738  1.00 95.00           O  
ANISOU 6284  O   ILE B 382    12042  10941  13112    886   -486     95       O  
ATOM   6285  CB  ILE B 382      60.572   9.275  26.819  1.00119.55           C  
ANISOU 6285  CB  ILE B 382    15162  13968  16292    918   -420     62       C  
ATOM   6286  CG1 ILE B 382      61.353   8.908  25.554  1.00129.84           C  
ANISOU 6286  CG1 ILE B 382    16482  15244  17608    946   -401     62       C  
ATOM   6287  CG2 ILE B 382      61.055   8.478  28.028  1.00103.84           C  
ANISOU 6287  CG2 ILE B 382    13141  12000  14314    874   -489     31       C  
ATOM   6288  CD1 ILE B 382      61.138   7.481  25.067  1.00157.13           C  
ANISOU 6288  CD1 ILE B 382    19940  18727  21035    959   -481     81       C  
ATOM   6289  N   LYS B 383      57.811  11.145  27.337  1.00 99.00           N  
ANISOU 6289  N   LYS B 383    12588  11401  13625    947   -369    110       N  
ATOM   6290  CA  LYS B 383      56.946  11.921  28.212  1.00 95.80           C  
ANISOU 6290  CA  LYS B 383    12174  11018  13208    933   -360    109       C  
ATOM   6291  C   LYS B 383      55.588  11.244  28.400  1.00 83.50           C  
ANISOU 6291  C   LYS B 383    10615   9506  11606    936   -418    127       C  
ATOM   6292  O   LYS B 383      55.124  11.085  29.530  1.00 77.13           O  
ANISOU 6292  O   LYS B 383     9785   8729  10791    898   -450    120       O  
ATOM   6293  CB  LYS B 383      56.799  13.370  27.740  1.00 95.39           C  
ANISOU 6293  CB  LYS B 383    12148  10935  13162    964   -280    111       C  
ATOM   6294  CG  LYS B 383      55.995  14.251  28.685  1.00 80.95           C  
ANISOU 6294  CG  LYS B 383    10305   9129  11325    948   -273    105       C  
ATOM   6295  CD  LYS B 383      54.702  14.720  28.113  1.00 77.00           C  
ANISOU 6295  CD  LYS B 383     9836   8641  10782    992   -267    122       C  
ATOM   6296  CE  LYS B 383      54.445  16.151  28.555  1.00 74.10           C  
ANISOU 6296  CE  LYS B 383     9470   8263  10421    993   -216    112       C  
ATOM   6297  NZ  LYS B 383      53.139  16.701  28.093  1.00 69.41           N  
ANISOU 6297  NZ  LYS B 383     8906   7683   9783   1038   -216    119       N  
ATOM   6298  N   LEU B 384      54.979  10.804  27.300  1.00 85.33           N  
ANISOU 6298  N   LEU B 384    10872   9740  11810    982   -432    147       N  
ATOM   6299  CA  LEU B 384      53.762  10.004  27.372  1.00 93.18           C  
ANISOU 6299  CA  LEU B 384    11859  10774  12772    986   -489    155       C  
ATOM   6300  C   LEU B 384      54.008   8.641  28.033  1.00 87.98           C  
ANISOU 6300  C   LEU B 384    11176  10138  12115    941   -554    154       C  
ATOM   6301  O   LEU B 384      53.138   8.130  28.747  1.00 90.99           O  
ANISOU 6301  O   LEU B 384    11542  10551  12479    913   -591    153       O  
ATOM   6302  CB  LEU B 384      53.152   9.852  25.968  1.00103.30           C  
ANISOU 6302  CB  LEU B 384    13171  12050  14029   1055   -491    168       C  
ATOM   6303  CG  LEU B 384      51.762   9.204  25.877  1.00 95.23           C  
ANISOU 6303  CG  LEU B 384    12139  11066  12980   1072   -541    164       C  
ATOM   6304  CD1 LEU B 384      50.694  10.046  26.570  1.00102.60           C  
ANISOU 6304  CD1 LEU B 384    13062  12021  13899   1063   -527    147       C  
ATOM   6305  CD2 LEU B 384      51.386   8.906  24.436  1.00 78.23           C  
ANISOU 6305  CD2 LEU B 384    10014   8903  10807   1149   -552    171       C  
ATOM   6306  N   PHE B 385      55.199   8.068  27.817  1.00 79.55           N  
ANISOU 6306  N   PHE B 385    10107   9049  11068    932   -566    152       N  
ATOM   6307  CA  PHE B 385      55.513   6.755  28.362  1.00 91.40           C  
ANISOU 6307  CA  PHE B 385    11594  10565  12567    897   -632    149       C  
ATOM   6308  C   PHE B 385      55.574   6.811  29.890  1.00 97.58           C  
ANISOU 6308  C   PHE B 385    12363  11362  13352    842   -646    134       C  
ATOM   6309  O   PHE B 385      55.555   5.776  30.545  1.00113.89           O  
ANISOU 6309  O   PHE B 385    14426  13442  15405    811   -699    134       O  
ATOM   6310  CB  PHE B 385      56.831   6.223  27.791  1.00116.14           C  
ANISOU 6310  CB  PHE B 385    14730  13673  15723    903   -643    141       C  
ATOM   6311  CG  PHE B 385      56.911   6.054  26.285  1.00163.36           C  
ANISOU 6311  CG  PHE B 385    20728  19639  21701    958   -632    157       C  
ATOM   6312  CD1 PHE B 385      55.806   6.274  25.465  1.00171.51           C  
ANISOU 6312  CD1 PHE B 385    21778  20681  22708   1006   -622    176       C  
ATOM   6313  CD2 PHE B 385      58.096   5.653  25.671  1.00170.55           C  
ANISOU 6313  CD2 PHE B 385    21640  20526  22634    966   -635    147       C  
ATOM   6314  CE1 PHE B 385      55.887   6.128  24.082  1.00141.38           C  
ANISOU 6314  CE1 PHE B 385    17985  16849  18885   1065   -613    189       C  
ATOM   6315  CE2 PHE B 385      58.171   5.491  24.290  1.00148.51           C  
ANISOU 6315  CE2 PHE B 385    18869  17722  19837   1018   -623    163       C  
ATOM   6316  CZ  PHE B 385      57.067   5.730  23.495  1.00129.83           C  
ANISOU 6316  CZ  PHE B 385    16525  15364  17441   1071   -612    186       C  
ATOM   6317  N   THR B 386      55.677   8.021  30.458  1.00 97.56           N  
ANISOU 6317  N   THR B 386    12353  11352  13363    834   -597    120       N  
ATOM   6318  CA  THR B 386      55.815   8.178  31.903  1.00 95.21           C  
ANISOU 6318  CA  THR B 386    12042  11065  13069    791   -608    102       C  
ATOM   6319  C   THR B 386      54.505   8.671  32.517  1.00 95.06           C  
ANISOU 6319  C   THR B 386    12017  11076  13024    779   -597    110       C  
ATOM   6320  O   THR B 386      54.223   8.403  33.689  1.00 84.36           O  
ANISOU 6320  O   THR B 386    10658   9740  11656    742   -620    104       O  
ATOM   6321  CB  THR B 386      56.981   9.095  32.313  1.00 93.44           C  
ANISOU 6321  CB  THR B 386    11804  10813  12886    786   -569     71       C  
ATOM   6322  OG1 THR B 386      56.695  10.412  31.859  1.00 97.05           O  
ANISOU 6322  OG1 THR B 386    12262  11259  13356    809   -502     74       O  
ATOM   6323  CG2 THR B 386      58.309   8.693  31.713  1.00102.71           C  
ANISOU 6323  CG2 THR B 386    12977  11956  14091    796   -573     52       C  
ATOM   6324  N   GLU B 387      53.721   9.425  31.734  1.00 90.64           N  
ANISOU 6324  N   GLU B 387    11462  10518  12458    813   -561    119       N  
ATOM   6325  CA  GLU B 387      52.478   9.970  32.247  1.00 85.54           C  
ANISOU 6325  CA  GLU B 387    10808   9902  11792    805   -551    117       C  
ATOM   6326  C   GLU B 387      51.458   8.850  32.371  1.00 89.16           C  
ANISOU 6326  C   GLU B 387    11265  10390  12223    788   -597    124       C  
ATOM   6327  O   GLU B 387      50.649   8.863  33.293  1.00 98.32           O  
ANISOU 6327  O   GLU B 387    12414  11577  13368    755   -602    117       O  
ATOM   6328  CB  GLU B 387      51.925  11.072  31.348  1.00 94.01           C  
ANISOU 6328  CB  GLU B 387    11892  10967  12862    853   -506    117       C  
ATOM   6329  CG  GLU B 387      51.850  12.406  32.053  1.00113.59           C  
ANISOU 6329  CG  GLU B 387    14361  13447  15351    844   -465    103       C  
ATOM   6330  CD  GLU B 387      53.110  13.236  31.898  1.00128.00           C  
ANISOU 6330  CD  GLU B 387    16189  15232  17212    852   -418     96       C  
ATOM   6331  OE1 GLU B 387      53.878  12.949  30.954  1.00119.65           O  
ANISOU 6331  OE1 GLU B 387    15150  14143  16168    877   -406    104       O  
ATOM   6332  OE2 GLU B 387      53.321  14.163  32.717  1.00152.58           O1-
ANISOU 6332  OE2 GLU B 387    19286  18344  20345    835   -391     80       O1-
ATOM   6333  N   LEU B 388      51.468   7.910  31.419  1.00 90.22           N  
ANISOU 6333  N   LEU B 388    11408  10518  12353    812   -625    136       N  
ATOM   6334  CA  LEU B 388      50.460   6.862  31.397  1.00 88.59           C  
ANISOU 6334  CA  LEU B 388    11195  10336  12128    800   -664    138       C  
ATOM   6335  C   LEU B 388      50.643   5.910  32.576  1.00 80.60           C  
ANISOU 6335  C   LEU B 388    10185   9332  11107    742   -697    140       C  
ATOM   6336  O   LEU B 388      49.674   5.327  33.052  1.00 74.68           O  
ANISOU 6336  O   LEU B 388     9429   8603  10342    713   -711    137       O  
ATOM   6337  CB  LEU B 388      50.560   6.100  30.075  1.00108.14           C  
ANISOU 6337  CB  LEU B 388    13679  12801  14606    845   -689    148       C  
ATOM   6338  CG  LEU B 388      50.284   6.908  28.812  1.00120.46           C  
ANISOU 6338  CG  LEU B 388    15251  14351  16167    914   -659    146       C  
ATOM   6339  CD1 LEU B 388      50.572   6.037  27.592  1.00128.03           C  
ANISOU 6339  CD1 LEU B 388    16220  15299  17127    958   -689    157       C  
ATOM   6340  CD2 LEU B 388      48.849   7.432  28.802  1.00106.62           C  
ANISOU 6340  CD2 LEU B 388    13488  12622  14399    932   -650    125       C  
ATOM   6341  N   SER B 389      51.881   5.768  33.054  1.00 84.75           N  
ANISOU 6341  N   SER B 389    10721   9838  11642    726   -708    141       N  
ATOM   6342  CA  SER B 389      52.162   4.885  34.174  1.00 97.81           C  
ANISOU 6342  CA  SER B 389    12389  11493  13280    680   -743    142       C  
ATOM   6343  C   SER B 389      51.645   5.464  35.497  1.00105.51           C  
ANISOU 6343  C   SER B 389    13363  12485  14242    643   -722    133       C  
ATOM   6344  O   SER B 389      51.064   4.740  36.313  1.00110.87           O  
ANISOU 6344  O   SER B 389    14056  13175  14896    605   -739    137       O  
ATOM   6345  CB  SER B 389      53.628   4.551  34.221  1.00 95.07           C  
ANISOU 6345  CB  SER B 389    12054  11120  12948    683   -768    135       C  
ATOM   6346  OG  SER B 389      54.382   5.707  34.536  1.00122.59           O  
ANISOU 6346  OG  SER B 389    15529  14593  16457    692   -733    116       O  
ATOM   6347  N   PHE B 390      51.842   6.771  35.710  1.00 99.61           N  
ANISOU 6347  N   PHE B 390    12601  11738  13510    655   -683    120       N  
ATOM   6348  CA  PHE B 390      51.466   7.380  36.975  1.00100.29           C  
ANISOU 6348  CA  PHE B 390    12682  11840  13585    625   -666    110       C  
ATOM   6349  C   PHE B 390      49.951   7.545  37.064  1.00103.83           C  
ANISOU 6349  C   PHE B 390    13117  12320  14015    611   -648    109       C  
ATOM   6350  O   PHE B 390      49.370   7.385  38.138  1.00138.94           O  
ANISOU 6350  O   PHE B 390    17568  16783  18440    572   -647    105       O  
ATOM   6351  CB  PHE B 390      52.160   8.726  37.177  1.00 90.21           C  
ANISOU 6351  CB  PHE B 390    11388  10554  12335    643   -631     93       C  
ATOM   6352  CG  PHE B 390      53.418   8.679  37.998  1.00 91.19           C  
ANISOU 6352  CG  PHE B 390    11519  10658  12472    636   -648     75       C  
ATOM   6353  CD1 PHE B 390      54.593   8.171  37.462  1.00 91.63           C  
ANISOU 6353  CD1 PHE B 390    11582  10685  12548    653   -670     67       C  
ATOM   6354  CD2 PHE B 390      53.434   9.187  39.292  1.00 90.51           C  
ANISOU 6354  CD2 PHE B 390    11429  10582  12379    618   -644     59       C  
ATOM   6355  CE1 PHE B 390      55.758   8.155  38.218  1.00 98.11           C  
ANISOU 6355  CE1 PHE B 390    12405  11487  13385    652   -690     37       C  
ATOM   6356  CE2 PHE B 390      54.597   9.172  40.047  1.00 89.22           C  
ANISOU 6356  CE2 PHE B 390    11270  10398  12229    621   -665     33       C  
ATOM   6357  CZ  PHE B 390      55.755   8.653  39.508  1.00100.60           C  
ANISOU 6357  CZ  PHE B 390    12719  11811  13694    639   -688     19       C  
ATOM   6358  N   THR B 391      49.326   7.902  35.937  1.00 77.89           N  
ANISOU 6358  N   THR B 391     9817   9039  10738    646   -633    107       N  
ATOM   6359  CA  THR B 391      47.900   8.162  35.934  1.00 76.69           C  
ANISOU 6359  CA  THR B 391     9647   8917  10575    641   -619     93       C  
ATOM   6360  C   THR B 391      47.136   6.860  36.136  1.00 73.22           C  
ANISOU 6360  C   THR B 391     9212   8488  10121    607   -643     94       C  
ATOM   6361  O   THR B 391      45.993   6.886  36.596  1.00 85.05           O  
ANISOU 6361  O   THR B 391    10695  10010  11609    580   -630     76       O  
ATOM   6362  CB  THR B 391      47.443   8.912  34.674  1.00 76.55           C  
ANISOU 6362  CB  THR B 391     9620   8899  10568    697   -602     83       C  
ATOM   6363  OG1 THR B 391      47.909   8.164  33.553  1.00112.50           O  
ANISOU 6363  OG1 THR B 391    14186  13432  15128    731   -624     97       O  
ATOM   6364  CG2 THR B 391      47.942  10.334  34.595  1.00 72.37           C  
ANISOU 6364  CG2 THR B 391     9089   8359  10050    725   -566     79       C  
ATOM   6365  N   SER B 392      47.770   5.732  35.792  1.00 70.42           N  
ANISOU 6365  N   SER B 392     8877   8114   9767    606   -677    112       N  
ATOM   6366  CA  SER B 392      47.111   4.435  35.887  1.00 67.60           C  
ANISOU 6366  CA  SER B 392     8525   7760   9399    575   -699    114       C  
ATOM   6367  C   SER B 392      47.161   3.920  37.319  1.00 67.87           C  
ANISOU 6367  C   SER B 392     8587   7792   9408    517   -700    121       C  
ATOM   6368  O   SER B 392      46.149   3.464  37.843  1.00 77.31           O  
ANISOU 6368  O   SER B 392     9781   9000  10592    477   -687    112       O  
ATOM   6369  CB  SER B 392      47.672   3.446  34.912  1.00 62.50           C  
ANISOU 6369  CB  SER B 392     7890   7096   8763    601   -737    129       C  
ATOM   6370  OG  SER B 392      49.055   3.236  35.132  1.00 72.35           O  
ANISOU 6370  OG  SER B 392     9162   8319  10008    602   -759    145       O  
ATOM   6371  N   PHE B 393      48.339   4.038  37.945  1.00 74.59           N  
ANISOU 6371  N   PHE B 393     9464   8626  10252    514   -712    132       N  
ATOM   6372  CA  PHE B 393      48.574   3.673  39.338  1.00 72.36           C  
ANISOU 6372  CA  PHE B 393     9218   8336   9939    473   -717    137       C  
ATOM   6373  C   PHE B 393      47.945   4.679  40.321  1.00 71.62           C  
ANISOU 6373  C   PHE B 393     9112   8266   9836    452   -678    123       C  
ATOM   6374  O   PHE B 393      47.968   4.479  41.528  1.00 59.76           O  
ANISOU 6374  O   PHE B 393     7641   6761   8304    420   -675    125       O  
ATOM   6375  CB  PHE B 393      50.081   3.455  39.533  1.00 60.04           C  
ANISOU 6375  CB  PHE B 393     7686   6748   8377    491   -753    142       C  
ATOM   6376  CG  PHE B 393      50.530   2.128  38.986  1.00 72.57           C  
ANISOU 6376  CG  PHE B 393     9298   8314   9959    494   -797    156       C  
ATOM   6377  CD1 PHE B 393      50.401   0.963  39.742  1.00 79.03           C  
ANISOU 6377  CD1 PHE B 393    10165   9118  10743    458   -820    167       C  
ATOM   6378  CD2 PHE B 393      51.002   2.024  37.684  1.00 75.09           C  
ANISOU 6378  CD2 PHE B 393     9596   8627  10307    532   -815    158       C  
ATOM   6379  CE1 PHE B 393      50.769  -0.266  39.207  1.00 82.93           C  
ANISOU 6379  CE1 PHE B 393    10683   9594  11234    461   -864    179       C  
ATOM   6380  CE2 PHE B 393      51.376   0.795  37.157  1.00 80.36           C  
ANISOU 6380  CE2 PHE B 393    10283   9279  10971    535   -860    169       C  
ATOM   6381  CZ  PHE B 393      51.263  -0.347  37.920  1.00 83.63           C  
ANISOU 6381  CZ  PHE B 393    10742   9681  11354    499   -887    179       C  
ATOM   6382  N   GLN B 394      47.384   5.774  39.804  1.00 69.20           N  
ANISOU 6382  N   GLN B 394     8762   7981   9549    474   -650    107       N  
ATOM   6383  CA  GLN B 394      46.937   6.886  40.615  1.00 67.66           C  
ANISOU 6383  CA  GLN B 394     8549   7809   9350    463   -618     91       C  
ATOM   6384  C   GLN B 394      45.904   6.377  41.617  1.00 78.26           C  
ANISOU 6384  C   GLN B 394     9904   9167  10665    408   -601     86       C  
ATOM   6385  O   GLN B 394      45.974   6.727  42.791  1.00 81.78           O  
ANISOU 6385  O   GLN B 394    10364   9619  11090    386   -589     84       O  
ATOM   6386  CB  GLN B 394      46.370   7.962  39.693  1.00 71.65           C  
ANISOU 6386  CB  GLN B 394     9012   8331   9879    498   -596     73       C  
ATOM   6387  CG  GLN B 394      46.910   9.364  39.899  1.00 67.96           C  
ANISOU 6387  CG  GLN B 394     8529   7868   9427    524   -577     65       C  
ATOM   6388  CD  GLN B 394      46.249  10.340  38.956  1.00 68.44           C  
ANISOU 6388  CD  GLN B 394     8560   7942   9503    561   -557     47       C  
ATOM   6389  OE1 GLN B 394      45.393  10.001  38.156  1.00 74.77           O  
ANISOU 6389  OE1 GLN B 394     9353   8752  10304    573   -560     37       O  
ATOM   6390  NE2 GLN B 394      46.592  11.605  39.084  1.00 90.31           N  
ANISOU 6390  NE2 GLN B 394    11316  10713  12286    582   -536     39       N  
ATOM   6391  N   GLY B 395      44.942   5.571  41.146  1.00 82.01           N  
ANISOU 6391  N   GLY B 395    10372   9647  11142    389   -597     79       N  
ATOM   6392  CA  GLY B 395      43.876   5.053  41.995  1.00 83.83           C  
ANISOU 6392  CA  GLY B 395    10611   9888  11351    332   -570     68       C  
ATOM   6393  C   GLY B 395      44.392   4.103  43.079  1.00 83.70           C  
ANISOU 6393  C   GLY B 395    10659   9846  11298    295   -577     94       C  
ATOM   6394  O   GLY B 395      43.888   4.094  44.204  1.00 85.65           O  
ANISOU 6394  O   GLY B 395    10927  10098  11517    254   -548     90       O  
ATOM   6395  N   LEU B 396      45.415   3.313  42.732  1.00 81.28           N  
ANISOU 6395  N   LEU B 396    10387   9508  10987    314   -617    118       N  
ATOM   6396  CA  LEU B 396      46.017   2.377  43.670  1.00 73.23           C  
ANISOU 6396  CA  LEU B 396     9438   8458   9928    291   -635    139       C  
ATOM   6397  C   LEU B 396      46.585   3.139  44.868  1.00 78.49           C  
ANISOU 6397  C   LEU B 396    10129   9127  10569    296   -630    138       C  
ATOM   6398  O   LEU B 396      46.361   2.737  46.006  1.00 85.03           O  
ANISOU 6398  O   LEU B 396    11009   9945  11356    263   -615    145       O  
ATOM   6399  CB  LEU B 396      47.112   1.559  42.980  1.00 65.40           C  
ANISOU 6399  CB  LEU B 396     8471   7437   8941    321   -687    157       C  
ATOM   6400  CG  LEU B 396      48.034   0.803  43.941  1.00 62.86           C  
ANISOU 6400  CG  LEU B 396     8226   7081   8575    315   -719    172       C  
ATOM   6401  CD1 LEU B 396      47.259  -0.312  44.647  1.00 62.20           C  
ANISOU 6401  CD1 LEU B 396     8200   6980   8454    262   -699    186       C  
ATOM   6402  CD2 LEU B 396      49.312   0.315  43.248  1.00 59.09           C  
ANISOU 6402  CD2 LEU B 396     7761   6580   8109    356   -778    177       C  
ATOM   6403  N   MET B 397      47.300   4.246  44.601  1.00 75.46           N  
ANISOU 6403  N   MET B 397     9708   8753  10209    339   -641    127       N  
ATOM   6404  CA  MET B 397      47.978   4.987  45.649  1.00 75.18           C  
ANISOU 6404  CA  MET B 397     9688   8718  10160    353   -644    119       C  
ATOM   6405  C   MET B 397      46.961   5.684  46.558  1.00 76.88           C  
ANISOU 6405  C   MET B 397     9890   8963  10359    323   -600    108       C  
ATOM   6406  O   MET B 397      47.182   5.848  47.765  1.00 80.61           O  
ANISOU 6406  O   MET B 397    10397   9432  10798    318   -598    107       O  
ATOM   6407  CB  MET B 397      48.997   5.977  45.071  1.00 73.84           C  
ANISOU 6407  CB  MET B 397     9478   8547  10030    404   -661    105       C  
ATOM   6408  CG  MET B 397      49.838   6.634  46.152  1.00 97.00           C  
ANISOU 6408  CG  MET B 397    12425  11476  12955    424   -672     89       C  
ATOM   6409  SD  MET B 397      51.617   6.853  45.942  1.00125.93           S  
ANISOU 6409  SD  MET B 397    16088  15110  16650    478   -715     68       S  
ATOM   6410  CE  MET B 397      52.187   5.377  46.792  1.00105.89           C  
ANISOU 6410  CE  MET B 397    13640  12537  14057    472   -765     75       C  
ATOM   6411  N   VAL B 398      45.825   6.083  45.981  1.00 70.73           N  
ANISOU 6411  N   VAL B 398     9059   8212   9600    306   -568     95       N  
ATOM   6412  CA  VAL B 398      44.780   6.675  46.795  1.00 67.65           C  
ANISOU 6412  CA  VAL B 398     8653   7854   9197    273   -527     78       C  
ATOM   6413  C   VAL B 398      44.247   5.629  47.777  1.00 76.66           C  
ANISOU 6413  C   VAL B 398     9854   8979  10293    220   -505     90       C  
ATOM   6414  O   VAL B 398      44.000   5.953  48.947  1.00 67.07           O  
ANISOU 6414  O   VAL B 398     8662   7775   9047    200   -482     87       O  
ATOM   6415  CB  VAL B 398      43.677   7.286  45.914  1.00 53.23           C  
ANISOU 6415  CB  VAL B 398     6759   6060   7405    270   -502     52       C  
ATOM   6416  CG1 VAL B 398      42.472   7.700  46.746  1.00 54.53           C  
ANISOU 6416  CG1 VAL B 398     6906   6257   7555    228   -460     27       C  
ATOM   6417  CG2 VAL B 398      44.221   8.457  45.118  1.00 42.04           C  
ANISOU 6417  CG2 VAL B 398     5298   4654   6024    324   -516     43       C  
ATOM   6418  N   ALA B 399      44.077   4.383  47.288  1.00 79.78           N  
ANISOU 6418  N   ALA B 399    10279   9349  10685    199   -510    104       N  
ATOM   6419  CA  ALA B 399      43.614   3.276  48.118  1.00 78.41           C  
ANISOU 6419  CA  ALA B 399    10172   9151  10468    148   -485    117       C  
ATOM   6420  C   ALA B 399      44.613   2.961  49.228  1.00 70.83           C  
ANISOU 6420  C   ALA B 399     9296   8160   9457    162   -508    140       C  
ATOM   6421  O   ALA B 399      44.211   2.726  50.367  1.00 62.09           O  
ANISOU 6421  O   ALA B 399     8242   7044   8304    129   -476    145       O  
ATOM   6422  CB  ALA B 399      43.304   2.058  47.284  1.00 84.68           C  
ANISOU 6422  CB  ALA B 399    10976   9923  11277    128   -489    125       C  
ATOM   6423  N   ILE B 400      45.906   2.993  48.893  1.00 72.71           N  
ANISOU 6423  N   ILE B 400     9544   8381   9701    214   -564    147       N  
ATOM   6424  CA  ILE B 400      46.959   2.765  49.876  1.00 77.81           C  
ANISOU 6424  CA  ILE B 400    10264   8998  10303    241   -598    156       C  
ATOM   6425  C   ILE B 400      46.928   3.841  50.969  1.00 76.62           C  
ANISOU 6425  C   ILE B 400    10107   8869  10135    252   -581    141       C  
ATOM   6426  O   ILE B 400      46.748   3.510  52.139  1.00 63.32           O  
ANISOU 6426  O   ILE B 400     8492   7170   8396    236   -564    148       O  
ATOM   6427  CB  ILE B 400      48.338   2.675  49.197  1.00 90.97           C  
ANISOU 6427  CB  ILE B 400    11927  10645  11993    296   -662    152       C  
ATOM   6428  CG1 ILE B 400      48.410   1.504  48.216  1.00109.77           C  
ANISOU 6428  CG1 ILE B 400    14322  13002  14382    286   -685    169       C  
ATOM   6429  CG2 ILE B 400      49.456   2.615  50.228  1.00 97.64           C  
ANISOU 6429  CG2 ILE B 400    12838  11463  12798    335   -703    145       C  
ATOM   6430  CD1 ILE B 400      48.171   0.143  48.834  1.00128.03           C  
ANISOU 6430  CD1 ILE B 400    16727  15277  16640    252   -684    191       C  
ATOM   6431  N   LEU B 401      47.088   5.120  50.579  1.00 71.47           N  
ANISOU 6431  N   LEU B 401     9376   8251   9529    281   -583    119       N  
ATOM   6432  CA  LEU B 401      47.272   6.199  51.540  1.00 67.24           C  
ANISOU 6432  CA  LEU B 401     8827   7735   8986    303   -578    102       C  
ATOM   6433  C   LEU B 401      46.019   6.448  52.376  1.00 67.34           C  
ANISOU 6433  C   LEU B 401     8842   7775   8971    256   -523    100       C  
ATOM   6434  O   LEU B 401      46.137   6.888  53.509  1.00 91.49           O  
ANISOU 6434  O   LEU B 401    11926  10839  11998    267   -519     94       O  
ATOM   6435  CB  LEU B 401      47.721   7.472  50.824  1.00 68.13           C  
ANISOU 6435  CB  LEU B 401     8855   7873   9159    342   -589     80       C  
ATOM   6436  CG  LEU B 401      49.056   7.368  50.083  1.00 70.14           C  
ANISOU 6436  CG  LEU B 401     9103   8100   9445    390   -637     74       C  
ATOM   6437  CD1 LEU B 401      49.407   8.688  49.419  1.00 63.71           C  
ANISOU 6437  CD1 LEU B 401     8210   7307   8691    422   -633     52       C  
ATOM   6438  CD2 LEU B 401      50.175   6.953  51.027  1.00 81.87           C  
ANISOU 6438  CD2 LEU B 401    10654   9554  10898    424   -680     64       C  
ATOM   6439  N   TYR B 402      44.830   6.158  51.842  1.00 71.29           N  
ANISOU 6439  N   TYR B 402     9313   8290   9483    206   -481    100       N  
ATOM   6440  CA  TYR B 402      43.592   6.449  52.555  1.00 64.11           C  
ANISOU 6440  CA  TYR B 402     8394   7408   8555    157   -425     88       C  
ATOM   6441  C   TYR B 402      42.914   5.183  53.088  1.00 70.53           C  
ANISOU 6441  C   TYR B 402     9282   8192   9324    100   -384    105       C  
ATOM   6442  O   TYR B 402      41.768   5.243  53.533  1.00 64.85           O  
ANISOU 6442  O   TYR B 402     8553   7492   8596     48   -328     91       O  
ATOM   6443  CB  TYR B 402      42.610   7.195  51.648  1.00 57.09           C  
ANISOU 6443  CB  TYR B 402     7411   6563   7718    141   -401     60       C  
ATOM   6444  CG  TYR B 402      42.828   8.677  51.545  1.00 52.99           C  
ANISOU 6444  CG  TYR B 402     6823   6080   7231    181   -415     38       C  
ATOM   6445  CD1 TYR B 402      43.394   9.370  52.593  1.00 62.44           C  
ANISOU 6445  CD1 TYR B 402     8034   7285   8407    206   -426     37       C  
ATOM   6446  CD2 TYR B 402      42.467   9.392  50.411  1.00 54.79           C  
ANISOU 6446  CD2 TYR B 402     6975   6333   7508    196   -418     17       C  
ATOM   6447  CE1 TYR B 402      43.612  10.736  52.513  1.00 64.17           C  
ANISOU 6447  CE1 TYR B 402     8188   7535   8660    242   -438     16       C  
ATOM   6448  CE2 TYR B 402      42.678  10.759  50.311  1.00 53.68           C  
ANISOU 6448  CE2 TYR B 402     6779   6221   7395    233   -428     -2       C  
ATOM   6449  CZ  TYR B 402      43.260  11.431  51.372  1.00 57.95           C  
ANISOU 6449  CZ  TYR B 402     7330   6769   7920    253   -437     -2       C  
ATOM   6450  OH  TYR B 402      43.512  12.774  51.321  1.00 58.95           O  
ANISOU 6450  OH  TYR B 402     7401   6921   8077    288   -446    -21       O  
ATOM   6451  N   CYS B 403      43.578   4.023  53.004  1.00 74.67           N  
ANISOU 6451  N   CYS B 403     9880   8668   9822    106   -410    131       N  
ATOM   6452  CA  CYS B 403      42.948   2.836  53.562  1.00 81.92           C  
ANISOU 6452  CA  CYS B 403    10878   9552  10696     51   -367    149       C  
ATOM   6453  C   CYS B 403      43.973   1.854  54.121  1.00 83.87           C  
ANISOU 6453  C   CYS B 403    11238   9743  10885     77   -404    179       C  
ATOM   6454  O   CYS B 403      44.020   1.616  55.321  1.00 75.93           O  
ANISOU 6454  O   CYS B 403    10318   8714   9816     74   -386    190       O  
ATOM   6455  CB  CYS B 403      42.048   2.128  52.556  1.00 83.50           C  
ANISOU 6455  CB  CYS B 403    11041   9751  10935      4   -337    142       C  
ATOM   6456  SG  CYS B 403      41.088   0.778  53.294  1.00 86.43           S  
ANISOU 6456  SG  CYS B 403    11499  10078  11261    -76   -263    155       S  
ATOM   6457  N   PHE B 404      44.785   1.275  53.239  1.00 85.57           N  
ANISOU 6457  N   PHE B 404    11456   9936  11120    107   -458    188       N  
ATOM   6458  CA  PHE B 404      45.593   0.122  53.606  1.00 91.67           C  
ANISOU 6458  CA  PHE B 404    12337  10653  11841    124   -495    212       C  
ATOM   6459  C   PHE B 404      46.614   0.446  54.700  1.00 91.62           C  
ANISOU 6459  C   PHE B 404    12399  10630  11782    181   -535    210       C  
ATOM   6460  O   PHE B 404      46.970  -0.440  55.462  1.00 97.61           O  
ANISOU 6460  O   PHE B 404    13272  11341  12475    189   -546    227       O  
ATOM   6461  CB  PHE B 404      46.220  -0.501  52.357  1.00 98.23           C  
ANISOU 6461  CB  PHE B 404    13143  11469  12709    144   -547    217       C  
ATOM   6462  CG  PHE B 404      45.199  -1.006  51.369  1.00106.15           C  
ANISOU 6462  CG  PHE B 404    14095  12482  13757     93   -511    218       C  
ATOM   6463  CD1 PHE B 404      44.376  -2.078  51.689  1.00112.25           C  
ANISOU 6463  CD1 PHE B 404    14926  13222  14501     33   -461    233       C  
ATOM   6464  CD2 PHE B 404      45.054  -0.408  50.128  1.00108.76           C  
ANISOU 6464  CD2 PHE B 404    14319  12849  14156    107   -523    200       C  
ATOM   6465  CE1 PHE B 404      43.438  -2.550  50.788  1.00108.71           C  
ANISOU 6465  CE1 PHE B 404    14424  12782  14101    -10   -428    224       C  
ATOM   6466  CE2 PHE B 404      44.106  -0.874  49.230  1.00107.51           C  
ANISOU 6466  CE2 PHE B 404    14112  12698  14038     70   -494    193       C  
ATOM   6467  CZ  PHE B 404      43.311  -1.949  49.558  1.00108.57           C  
ANISOU 6467  CZ  PHE B 404    14297  12803  14151     11   -449    202       C  
ATOM   6468  N   VAL B 405      47.091   1.696  54.775  1.00 84.41           N  
ANISOU 6468  N   VAL B 405    11419   9753  10900    226   -559    185       N  
ATOM   6469  CA  VAL B 405      48.074   2.083  55.775  1.00 71.72           C  
ANISOU 6469  CA  VAL B 405     9863   8133   9255    288   -602    171       C  
ATOM   6470  C   VAL B 405      47.411   2.860  56.903  1.00 72.70           C  
ANISOU 6470  C   VAL B 405     9992   8282   9349    278   -555    165       C  
ATOM   6471  O   VAL B 405      48.090   3.266  57.842  1.00 81.94           O  
ANISOU 6471  O   VAL B 405    11202   9446  10486    331   -585    150       O  
ATOM   6472  CB  VAL B 405      49.246   2.893  55.194  1.00 67.53           C  
ANISOU 6472  CB  VAL B 405     9263   7618   8779    353   -665    140       C  
ATOM   6473  CG1 VAL B 405      50.056   2.077  54.207  1.00 66.95           C  
ANISOU 6473  CG1 VAL B 405     9196   7516   8727    371   -717    142       C  
ATOM   6474  CG2 VAL B 405      48.794   4.212  54.586  1.00 69.38           C  
ANISOU 6474  CG2 VAL B 405     9372   7905   9082    346   -639    123       C  
ATOM   6475  N   ASN B 406      46.097   3.073  56.808  1.00 78.18           N  
ANISOU 6475  N   ASN B 406    10643   9006  10057    212   -484    170       N  
ATOM   6476  CA  ASN B 406      45.358   3.710  57.891  1.00 89.57           C  
ANISOU 6476  CA  ASN B 406    12093  10472  11468    193   -434    164       C  
ATOM   6477  C   ASN B 406      45.405   2.831  59.145  1.00 97.84           C  
ANISOU 6477  C   ASN B 406    13282  11470  12422    192   -416    186       C  
ATOM   6478  O   ASN B 406      45.200   1.618  59.082  1.00113.42           O  
ANISOU 6478  O   ASN B 406    15336  13397  14361    158   -396    211       O  
ATOM   6479  CB  ASN B 406      43.911   4.018  57.484  1.00 93.06           C  
ANISOU 6479  CB  ASN B 406    12459  10954  11946    119   -363    156       C  
ATOM   6480  CG  ASN B 406      43.104   4.666  58.591  1.00 91.47           C  
ANISOU 6480  CG  ASN B 406    12261  10779  11714     95   -309    146       C  
ATOM   6481  OD1 ASN B 406      42.005   4.213  58.927  1.00 90.57           O  
ANISOU 6481  OD1 ASN B 406    12172  10662  11579     27   -237    149       O  
ATOM   6482  ND2 ASN B 406      43.646   5.733  59.157  1.00 92.29           N  
ANISOU 6482  ND2 ASN B 406    12337  10911  11819    149   -341    129       N  
ATOM   6483  N   ASN B 407      45.644   3.458  60.299  1.00 95.23           N  
ANISOU 6483  N   ASN B 407    12986  11147  12050    232   -421    176       N  
ATOM   6484  CA  ASN B 407      45.770   2.729  61.553  1.00 86.59           C  
ANISOU 6484  CA  ASN B 407    12037  10004  10860    247   -408    194       C  
ATOM   6485  C   ASN B 407      44.413   2.208  62.033  1.00 85.24           C  
ANISOU 6485  C   ASN B 407    11914   9823  10651    161   -308    216       C  
ATOM   6486  O   ASN B 407      44.336   1.157  62.670  1.00 84.72           O  
ANISOU 6486  O   ASN B 407    11980   9699  10510    147   -280    243       O  
ATOM   6487  CB  ASN B 407      46.424   3.582  62.637  1.00 94.51           C  
ANISOU 6487  CB  ASN B 407    13061  11019  11831    323   -446    172       C  
ATOM   6488  CG  ASN B 407      47.780   4.122  62.239  1.00109.39           C  
ANISOU 6488  CG  ASN B 407    14895  12909  13759    407   -539    139       C  
ATOM   6489  OD1 ASN B 407      48.093   4.279  61.054  1.00127.17           O  
ANISOU 6489  OD1 ASN B 407    17060  15177  16084    403   -567    130       O  
ATOM   6490  ND2 ASN B 407      48.596   4.401  63.236  1.00107.41           N  
ANISOU 6490  ND2 ASN B 407    14702  12644  13466    487   -587    117       N  
ATOM   6491  N   GLU B 408      43.331   2.946  61.757  1.00 82.52           N  
ANISOU 6491  N   GLU B 408    11465   9532  10356    104   -252    201       N  
ATOM   6492  CA  GLU B 408      42.021   2.545  62.246  1.00 78.17           C  
ANISOU 6492  CA  GLU B 408    10948   8976   9777     20   -152    209       C  
ATOM   6493  C   GLU B 408      41.574   1.239  61.583  1.00 89.75           C  
ANISOU 6493  C   GLU B 408    12455  10397  11248    -43   -114    229       C  
ATOM   6494  O   GLU B 408      40.993   0.386  62.258  1.00 92.30           O  
ANISOU 6494  O   GLU B 408    12881  10675  11515    -92    -44    249       O  
ATOM   6495  CB  GLU B 408      40.999   3.660  62.056  1.00 72.66           C  
ANISOU 6495  CB  GLU B 408    10122   8349   9137    -22   -110    176       C  
ATOM   6496  CG  GLU B 408      41.181   4.789  63.039  1.00 80.95           C  
ANISOU 6496  CG  GLU B 408    11157   9435  10163     24   -124    160       C  
ATOM   6497  CD  GLU B 408      42.317   5.757  62.746  1.00 83.74           C  
ANISOU 6497  CD  GLU B 408    11444   9818  10556    111   -216    143       C  
ATOM   6498  OE1 GLU B 408      42.887   5.666  61.651  1.00 93.81           O  
ANISOU 6498  OE1 GLU B 408    12669  11090  11884    130   -265    140       O  
ATOM   6499  OE2 GLU B 408      42.618   6.612  63.599  1.00 72.61           O1-
ANISOU 6499  OE2 GLU B 408    10030   8431   9126    159   -236    129       O1-
ATOM   6500  N   VAL B 409      41.845   1.075  60.275  1.00 78.28           N  
ANISOU 6500  N   VAL B 409    10926   8953   9863    -40   -157    223       N  
ATOM   6501  CA  VAL B 409      41.404  -0.128  59.592  1.00 86.28           C  
ANISOU 6501  CA  VAL B 409    11966   9928  10889    -96   -125    238       C  
ATOM   6502  C   VAL B 409      42.216  -1.334  60.064  1.00 88.24           C  
ANISOU 6502  C   VAL B 409    12365  10100  11062    -69   -152    274       C  
ATOM   6503  O   VAL B 409      41.707  -2.452  60.161  1.00 90.25           O  
ANISOU 6503  O   VAL B 409    12697  10304  11288   -124    -97    294       O  
ATOM   6504  CB  VAL B 409      41.359   0.008  58.059  1.00 82.17           C  
ANISOU 6504  CB  VAL B 409    11324   9438  10459   -100   -160    219       C  
ATOM   6505  CG1 VAL B 409      40.677   1.302  57.638  1.00 84.82           C  
ANISOU 6505  CG1 VAL B 409    11522   9847  10860   -110   -146    180       C  
ATOM   6506  CG2 VAL B 409      42.723  -0.150  57.422  1.00 78.41           C  
ANISOU 6506  CG2 VAL B 409    10853   8948   9992    -27   -258    230       C  
ATOM   6507  N   GLN B 410      43.481  -1.088  60.384  1.00 84.45           N  
ANISOU 6507  N   GLN B 410    11926   9611  10550     18   -235    277       N  
ATOM   6508  CA  GLN B 410      44.330  -2.159  60.865  1.00 92.49           C  
ANISOU 6508  CA  GLN B 410    13091  10558  11492     57   -274    303       C  
ATOM   6509  C   GLN B 410      43.847  -2.638  62.232  1.00 96.47           C  
ANISOU 6509  C   GLN B 410    13737  11017  11901     35   -204    325       C  
ATOM   6510  O   GLN B 410      44.068  -3.792  62.576  1.00108.53           O  
ANISOU 6510  O   GLN B 410    15400  12475  13363     33   -198    353       O  
ATOM   6511  CB  GLN B 410      45.791  -1.714  60.862  1.00106.87           C  
ANISOU 6511  CB  GLN B 410    14911  12383  13310    158   -383    286       C  
ATOM   6512  CG  GLN B 410      46.340  -1.453  59.461  1.00115.94           C  
ANISOU 6512  CG  GLN B 410    15940  13564  14547    176   -446    269       C  
ATOM   6513  CD  GLN B 410      47.802  -1.070  59.442  1.00116.52           C  
ANISOU 6513  CD  GLN B 410    16012  13635  14624    271   -547    244       C  
ATOM   6514  OE1 GLN B 410      48.475  -1.011  60.469  1.00130.61           O  
ANISOU 6514  OE1 GLN B 410    17884  15396  16347    333   -581    235       O  
ATOM   6515  NE2 GLN B 410      48.324  -0.828  58.252  1.00 97.59           N  
ANISOU 6515  NE2 GLN B 410    13516  11262  12301    287   -596    228       N  
ATOM   6516  N   LEU B 411      43.207  -1.761  63.018  1.00 93.25           N  
ANISOU 6516  N   LEU B 411    13305  10645  11482     21   -151    313       N  
ATOM   6517  CA  LEU B 411      42.602  -2.167  64.280  1.00104.62           C  
ANISOU 6517  CA  LEU B 411    14874  12043  12834     -9    -69    334       C  
ATOM   6518  C   LEU B 411      41.443  -3.113  64.013  1.00 98.92           C  
ANISOU 6518  C   LEU B 411    14176  11289  12121   -115     35    349       C  
ATOM   6519  O   LEU B 411      41.225  -4.048  64.770  1.00109.05           O  
ANISOU 6519  O   LEU B 411    15606  12504  13325   -140     93    378       O  
ATOM   6520  CB  LEU B 411      42.072  -0.955  65.055  1.00114.03           C  
ANISOU 6520  CB  LEU B 411    16012  13290  14025     -8    -32    312       C  
ATOM   6521  CG  LEU B 411      43.116  -0.102  65.761  1.00113.41           C  
ANISOU 6521  CG  LEU B 411    15947  13229  13913     99   -114    298       C  
ATOM   6522  CD1 LEU B 411      42.488   1.195  66.245  1.00111.93           C  
ANISOU 6522  CD1 LEU B 411    15667  13110  13751     90    -82    272       C  
ATOM   6523  CD2 LEU B 411      43.683  -0.896  66.921  1.00107.37           C  
ANISOU 6523  CD2 LEU B 411    15375  12390  13030    152   -121    323       C  
ATOM   6524  N   GLU B 412      40.684  -2.829  62.953  1.00 98.30           N  
ANISOU 6524  N   GLU B 412    13953  11258  12140   -176     60    325       N  
ATOM   6525  CA  GLU B 412      39.493  -3.605  62.642  1.00103.57           C  
ANISOU 6525  CA  GLU B 412    14615  11902  12833   -278    160    323       C  
ATOM   6526  C   GLU B 412      39.878  -5.014  62.177  1.00108.26           C  
ANISOU 6526  C   GLU B 412    15298  12425  13409   -287    146    353       C  
ATOM   6527  O   GLU B 412      39.174  -5.967  62.478  1.00109.69           O  
ANISOU 6527  O   GLU B 412    15562  12552  13565   -357    234    368       O  
ATOM   6528  CB  GLU B 412      38.616  -2.859  61.641  1.00 98.64           C  
ANISOU 6528  CB  GLU B 412    13811  11350  12318   -326    180    278       C  
ATOM   6529  CG  GLU B 412      38.159  -1.507  62.152  1.00109.03           C  
ANISOU 6529  CG  GLU B 412    15046  12732  13647   -322    198    247       C  
ATOM   6530  CD  GLU B 412      37.413  -1.498  63.480  1.00118.21           C  
ANISOU 6530  CD  GLU B 412    16293  13878  14744   -366    295    250       C  
ATOM   6531  OE1 GLU B 412      36.493  -2.320  63.635  1.00129.74           O  
ANISOU 6531  OE1 GLU B 412    17799  15299  16199   -450    394    250       O  
ATOM   6532  OE2 GLU B 412      37.737  -0.655  64.346  1.00110.16           O1-
ANISOU 6532  OE2 GLU B 412    15290  12884  13682   -317    275    251       O1-
ATOM   6533  N   PHE B 413      41.010  -5.158  61.482  1.00103.51           N  
ANISOU 6533  N   PHE B 413    14685  11823  12822   -218     37    361       N  
ATOM   6534  CA  PHE B 413      41.476  -6.470  61.059  1.00103.53           C  
ANISOU 6534  CA  PHE B 413    14773  11760  12804   -218     10    388       C  
ATOM   6535  C   PHE B 413      41.970  -7.304  62.235  1.00108.49           C  
ANISOU 6535  C   PHE B 413    15602  12307  13312   -189     18    424       C  
ATOM   6536  O   PHE B 413      41.665  -8.485  62.282  1.00110.41           O  
ANISOU 6536  O   PHE B 413    15942  12484  13525   -235     67    449       O  
ATOM   6537  CB  PHE B 413      42.508  -6.369  59.937  1.00111.76           C  
ANISOU 6537  CB  PHE B 413    15737  12828  13898   -155   -107    379       C  
ATOM   6538  CG  PHE B 413      41.901  -6.036  58.598  1.00119.27           C  
ANISOU 6538  CG  PHE B 413    16523  13834  14961   -194   -103    352       C  
ATOM   6539  CD1 PHE B 413      41.255  -7.008  57.841  1.00110.45           C  
ANISOU 6539  CD1 PHE B 413    15390  12691  13884   -257    -64    354       C  
ATOM   6540  CD2 PHE B 413      41.955  -4.737  58.111  1.00121.20           C  
ANISOU 6540  CD2 PHE B 413    16630  14153  15268   -165   -138    320       C  
ATOM   6541  CE1 PHE B 413      40.683  -6.684  56.625  1.00104.96           C  
ANISOU 6541  CE1 PHE B 413    14545  12045  13288   -284    -64    322       C  
ATOM   6542  CE2 PHE B 413      41.379  -4.417  56.895  1.00117.11           C  
ANISOU 6542  CE2 PHE B 413    15971  13682  14844   -194   -135    293       C  
ATOM   6543  CZ  PHE B 413      40.753  -5.394  56.154  1.00108.48           C  
ANISOU 6543  CZ  PHE B 413    14865  12564  13788   -249   -101    293       C  
ATOM   6544  N   ARG B 414      42.711  -6.703  63.176  1.00105.14           N  
ANISOU 6544  N   ARG B 414    15242  11885  12821   -111    -27    425       N  
ATOM   6545  CA  ARG B 414      43.177  -7.398  64.385  1.00105.54           C  
ANISOU 6545  CA  ARG B 414    15493  11858  12747    -69    -22    455       C  
ATOM   6546  C   ARG B 414      41.968  -7.710  65.278  1.00106.03           C  
ANISOU 6546  C   ARG B 414    15639  11885  12763   -152    119    473       C  
ATOM   6547  O   ARG B 414      41.895  -8.788  65.862  1.00106.01           O  
ANISOU 6547  O   ARG B 414    15801  11798  12678   -169    167    506       O  
ATOM   6548  CB  ARG B 414      44.305  -6.589  65.035  1.00114.00           C  
ANISOU 6548  CB  ARG B 414    16590  12949  13774     46   -119    438       C  
ATOM   6549  CG  ARG B 414      44.451  -6.649  66.555  1.00160.22           C  
ANISOU 6549  CG  ARG B 414    22614  18756  19508     93    -93    454       C  
ATOM   6550  CD  ARG B 414      44.775  -7.950  67.264  1.00181.06           C  
ANISOU 6550  CD  ARG B 414    25471  21292  22031    114    -83    489       C  
ATOM   6551  NE  ARG B 414      45.805  -8.826  66.712  1.00182.74           N  
ANISOU 6551  NE  ARG B 414    25742  21461  22229    167   -182    492       N  
ATOM   6552  CZ  ARG B 414      46.645  -9.565  67.465  1.00175.30           C  
ANISOU 6552  CZ  ARG B 414    24985  20444  21176    247   -235    503       C  
ATOM   6553  NH1 ARG B 414      46.608  -9.483  68.787  1.00154.14           N  
ANISOU 6553  NH1 ARG B 414    22450  17724  18390    290   -201    513       N  
ATOM   6554  NH2 ARG B 414      47.530 -10.363  66.890  1.00187.73           N  
ANISOU 6554  NH2 ARG B 414    26601  21984  22745    289   -327    500       N  
ATOM   6555  N   LYS B 415      41.010  -6.773  65.372  1.00113.33           N  
ANISOU 6555  N   LYS B 415    16451  12870  13737   -205    189    448       N  
ATOM   6556  CA  LYS B 415      39.850  -6.960  66.225  1.00116.64           C  
ANISOU 6556  CA  LYS B 415    16935  13262  14119   -286    326    456       C  
ATOM   6557  C   LYS B 415      38.970  -8.074  65.653  1.00125.51           C  
ANISOU 6557  C   LYS B 415    18069  14340  15280   -389    417    464       C  
ATOM   6558  O   LYS B 415      38.383  -8.862  66.397  1.00129.89           O  
ANISOU 6558  O   LYS B 415    18757  14824  15772   -445    522    487       O  
ATOM   6559  CB  LYS B 415      39.108  -5.632  66.409  1.00113.20           C  
ANISOU 6559  CB  LYS B 415    16366  12912  13735   -311    365    419       C  
ATOM   6560  CG  LYS B 415      37.976  -5.653  67.428  1.00129.60           C  
ANISOU 6560  CG  LYS B 415    18506  14968  15768   -385    503    420       C  
ATOM   6561  CD  LYS B 415      37.417  -4.279  67.768  1.00123.07           C  
ANISOU 6561  CD  LYS B 415    17560  14224  14975   -391    523    383       C  
ATOM   6562  CE  LYS B 415      36.537  -3.719  66.668  1.00130.95           C  
ANISOU 6562  CE  LYS B 415    18359  15295  16100   -460    543    334       C  
ATOM   6563  NZ  LYS B 415      36.144  -2.305  66.895  1.00137.37           N  
ANISOU 6563  NZ  LYS B 415    19050  16196  16949   -451    538    295       N  
ATOM   6564  N   SER B 416      38.894  -8.138  64.319  1.00134.12           N  
ANISOU 6564  N   SER B 416    19020  15467  16473   -413    376    442       N  
ATOM   6565  CA  SER B 416      38.113  -9.158  63.635  1.00128.18           C  
ANISOU 6565  CA  SER B 416    18255  14676  15772   -502    447    440       C  
ATOM   6566  C   SER B 416      38.800 -10.516  63.737  1.00123.92           C  
ANISOU 6566  C   SER B 416    17878  14044  15162   -481    422    485       C  
ATOM   6567  O   SER B 416      38.123 -11.516  63.917  1.00115.13           O  
ANISOU 6567  O   SER B 416    16847  12863  14034   -557    520    499       O  
ATOM   6568  CB  SER B 416      37.864  -8.785  62.204  1.00126.50           C  
ANISOU 6568  CB  SER B 416    17849  14531  15684   -520    403    401       C  
ATOM   6569  OG  SER B 416      36.954  -9.691  61.605  1.00137.55           O  
ANISOU 6569  OG  SER B 416    19223  15898  17141   -609    482    387       O  
ATOM   6570  N   TRP B 417      40.134 -10.544  63.602  1.00124.14           N  
ANISOU 6570  N   TRP B 417    17948  14067  15151   -380    292    501       N  
ATOM   6571  CA  TRP B 417      40.917 -11.771  63.709  1.00117.50           C  
ANISOU 6571  CA  TRP B 417    17264  13142  14238   -345    248    538       C  
ATOM   6572  C   TRP B 417      40.855 -12.318  65.128  1.00125.76           C  
ANISOU 6572  C   TRP B 417    18524  14104  15155   -342    320    574       C  
ATOM   6573  O   TRP B 417      40.940 -13.528  65.300  1.00152.52           O  
ANISOU 6573  O   TRP B 417    22057  17407  18487   -358    345    606       O  
ATOM   6574  CB  TRP B 417      42.368 -11.610  63.237  1.00 95.85           C  
ANISOU 6574  CB  TRP B 417    14509  10420  11489   -235     89    535       C  
ATOM   6575  N   GLU B 418      40.698 -11.436  66.127  1.00129.89           N  
ANISOU 6575  N   GLU B 418    19072  14651  15630   -319    353    568       N  
ATOM   6576  CA  GLU B 418      40.574 -11.870  67.510  1.00132.69           C  
ANISOU 6576  CA  GLU B 418    19632  14927  15858   -312    428    601       C  
ATOM   6577  C   GLU B 418      39.233 -12.568  67.737  1.00117.98           C  
ANISOU 6577  C   GLU B 418    17813  13012  14001   -439    596    612       C  
ATOM   6578  O   GLU B 418      39.177 -13.566  68.451  1.00114.28           O  
ANISOU 6578  O   GLU B 418    17537  12445  13438   -454    661    650       O  
ATOM   6579  CB  GLU B 418      40.796 -10.715  68.486  1.00146.75           C  
ANISOU 6579  CB  GLU B 418    21419  16751  17588   -246    411    589       C  
ATOM   6580  CG  GLU B 418      41.001 -11.172  69.924  1.00166.16           C  
ANISOU 6580  CG  GLU B 418    24111  19124  19896   -202    454    624       C  
ATOM   6581  CD  GLU B 418      42.249 -11.999  70.191  1.00176.55           C  
ANISOU 6581  CD  GLU B 418    25601  20367  21114    -99    351    647       C  
ATOM   6582  OE1 GLU B 418      43.224 -11.847  69.432  1.00178.24           O  
ANISOU 6582  OE1 GLU B 418    25736  20615  21371    -30    216    627       O  
ATOM   6583  OE2 GLU B 418      42.208 -12.836  71.116  1.00175.00           O1-
ANISOU 6583  OE2 GLU B 418    25618  20074  20800    -91    410    684       O1-
ATOM   6584  N   ARG B 419      38.165 -12.025  67.140  1.00118.87           N  
ANISOU 6584  N   ARG B 419    17750  13189  14226   -529    667    574       N  
ATOM   6585  CA  ARG B 419      36.834 -12.595  67.273  1.00131.31           C  
ANISOU 6585  CA  ARG B 419    19339  14725  15830   -655    829    567       C  
ATOM   6586  C   ARG B 419      36.786 -13.979  66.623  1.00152.31           C  
ANISOU 6586  C   ARG B 419    22054  17310  18509   -702    849    586       C  
ATOM   6587  O   ARG B 419      36.022 -14.847  67.046  1.00159.53           O  
ANISOU 6587  O   ARG B 419    23071  18144  19397   -786    981    600       O  
ATOM   6588  CB  ARG B 419      35.781 -11.699  66.613  1.00142.49           C  
ANISOU 6588  CB  ARG B 419    20534  16231  17373   -729    878    508       C  
ATOM   6589  CG  ARG B 419      35.745 -10.271  67.128  1.00152.53           C  
ANISOU 6589  CG  ARG B 419    21726  17585  18642   -689    856    483       C  
ATOM   6590  CD  ARG B 419      35.129 -10.182  68.503  1.00164.89           C  
ANISOU 6590  CD  ARG B 419    23416  19113  20122   -724    978    496       C  
ATOM   6591  NE  ARG B 419      35.115  -8.813  69.009  1.00182.96           N  
ANISOU 6591  NE  ARG B 419    25626  21483  22407   -682    951    472       N  
ATOM   6592  CZ  ARG B 419      34.249  -7.853  68.672  1.00197.77           C  
ANISOU 6592  CZ  ARG B 419    27325  23443  24375   -734    984    417       C  
ATOM   6593  NH1 ARG B 419      33.284  -8.079  67.793  1.00194.97           N  
ANISOU 6593  NH1 ARG B 419    26844  23106  24127   -829   1047    373       N  
ATOM   6594  NH2 ARG B 419      34.363  -6.655  69.223  1.00206.29           N  
ANISOU 6594  NH2 ARG B 419    28354  24589  25438   -685    951    402       N  
ATOM   6595  N   TRP B 420      37.584 -14.162  65.564  1.00159.08           N  
ANISOU 6595  N   TRP B 420    22836  18193  19416   -650    721    583       N  
ATOM   6596  CA  TRP B 420      37.600 -15.399  64.797  1.00151.83           C  
ANISOU 6596  CA  TRP B 420    21943  17218  18529   -687    719    596       C  
ATOM   6597  C   TRP B 420      38.093 -16.547  65.666  1.00149.59           C  
ANISOU 6597  C   TRP B 420    21908  16816  18114   -664    741    651       C  
ATOM   6598  O   TRP B 420      37.541 -17.646  65.617  1.00175.24           O  
ANISOU 6598  O   TRP B 420    25234  19987  21364   -739    831    666       O  
ATOM   6599  CB  TRP B 420      38.556 -15.273  63.626  1.00154.97           C  
ANISOU 6599  CB  TRP B 420    22228  17668  18984   -615    562    586       C  
ATOM   6600  CG  TRP B 420      38.263 -16.274  62.559  1.00151.96           C  
ANISOU 6600  CG  TRP B 420    21796  17260  18680   -669    568    580       C  
ATOM   6601  CD1 TRP B 420      38.556 -17.606  62.530  1.00143.25           C  
ANISOU 6601  CD1 TRP B 420    20828  16068  17534   -678    568    615       C  
ATOM   6602  CD2 TRP B 420      37.635 -15.960  61.309  1.00154.41           C  
ANISOU 6602  CD2 TRP B 420    21896  17641  19130   -715    564    533       C  
ATOM   6603  NE1 TRP B 420      38.134 -18.144  61.341  1.00145.20           N  
ANISOU 6603  NE1 TRP B 420    20954  16327  17889   -730    568    591       N  
ATOM   6604  CE2 TRP B 420      37.573 -17.158  60.567  1.00149.84           C  
ANISOU 6604  CE2 TRP B 420    21331  17012  18590   -750    563    540       C  
ATOM   6605  CE3 TRP B 420      37.132 -14.778  60.746  1.00157.16           C  
ANISOU 6605  CE3 TRP B 420    22052  18089  19573   -724    557    483       C  
ATOM   6606  CZ2 TRP B 420      37.017 -17.202  59.288  1.00157.38           C  
ANISOU 6606  CZ2 TRP B 420    22109  18014  19675   -790    556    497       C  
ATOM   6607  CZ3 TRP B 420      36.587 -14.822  59.479  1.00156.13           C  
ANISOU 6607  CZ3 TRP B 420    21754  18002  19566   -762    549    440       C  
ATOM   6608  CH2 TRP B 420      36.529 -16.022  58.763  1.00158.57           C  
ANISOU 6608  CH2 TRP B 420    22077  18261  19912   -793    549    446       C  
ATOM   6609  N   ARG B 421      39.178 -16.283  66.401  1.00131.60           N  
ANISOU 6609  N   ARG B 421    19749  14525  15727   -553    648    676       N  
ATOM   6610  CA  ARG B 421      39.774 -17.248  67.315  1.00138.23           C  
ANISOU 6610  CA  ARG B 421    20840  15256  16427   -507    649    724       C  
ATOM   6611  C   ARG B 421      38.851 -17.491  68.514  1.00153.56           C  
ANISOU 6611  C   ARG B 421    22929  17127  18291   -574    819    746       C  
ATOM   6612  O   ARG B 421      38.518 -18.640  68.807  1.00188.88           O  
ANISOU 6612  O   ARG B 421    27554  21498  22714   -627    908    778       O  
ATOM   6613  CB  ARG B 421      41.192 -16.834  67.726  1.00122.95           C  
ANISOU 6613  CB  ARG B 421    18978  13333  14405   -361    495    730       C  
ATOM   6614  N   LEU B 422      38.447 -16.416  69.211  1.00140.29           N  
ANISOU 6614  N   LEU B 422    21208  15498  16600   -572    865    730       N  
ATOM   6615  CA  LEU B 422      37.627 -16.538  70.410  1.00126.50           C  
ANISOU 6615  CA  LEU B 422    19602  13690  14774   -628   1023    749       C  
ATOM   6616  C   LEU B 422      36.149 -16.450  70.023  1.00141.51           C  
ANISOU 6616  C   LEU B 422    21365  15615  16788   -774   1175    713       C  
ATOM   6617  O   LEU B 422      35.698 -17.357  69.282  1.00175.94           O  
ANISOU 6617  O   LEU B 422    25697  19936  21215   -852   1223    709       O  
ATOM   6618  CB  LEU B 422      38.003 -15.457  71.432  1.00107.90           C  
ANISOU 6618  CB  LEU B 422    17284  11373  12338   -542    989    747       C  
TER    6619      LEU B 422                                                      
HETATM 6620  C13 97Y A2001      22.153  32.541  29.697  1.00 62.69           C  
HETATM 6621  C15 97Y A2001      22.902  32.945  32.159  1.00 66.53           C  
HETATM 6622  C17 97Y A2001      21.132  33.117  28.815  1.00 59.20           C  
HETATM 6623  C20 97Y A2001      21.985  30.248  28.884  1.00 61.26           C  
HETATM 6624  C21 97Y A2001      22.152  24.101  24.593  1.00 73.76           C  
HETATM 6625  C22 97Y A2001      22.082  26.222  25.980  1.00 59.28           C  
HETATM 6626  C24 97Y A2001      22.716  29.818  26.568  1.00 53.37           C  
HETATM 6627  C26 97Y A2001      19.773  33.086  29.154  1.00 66.53           C  
HETATM 6628  C28 97Y A2001      22.526  30.687  27.654  1.00 55.96           C  
HETATM 6629  F01 97Y A2001      22.028  23.807  23.315  1.00 78.50           F  
HETATM 6630  F02 97Y A2001      23.219  23.412  24.986  1.00 78.39           F  
HETATM 6631  F03 97Y A2001      21.129  23.668  25.328  1.00 80.46           F  
HETATM 6632  O04 97Y A2001      18.602  35.424  25.150  1.00100.65           O  
HETATM 6633  O05 97Y A2001      13.322  34.026  26.428  1.00201.77           O  
HETATM 6634  O06 97Y A2001      12.780  34.427  24.335  1.00212.73           O  
HETATM 6635  N07 97Y A2001      22.511  27.482  25.757  1.00 58.98           N  
HETATM 6636  N08 97Y A2001      21.789  31.127  29.912  1.00 65.02           N  
HETATM 6637  N09 97Y A2001      22.962  26.445  23.908  1.00 58.74           N  
HETATM 6638  N10 97Y A2001      21.898  28.083  27.950  1.00 58.84           N  
HETATM 6639  N11 97Y A2001      16.877  34.818  26.430  1.00 99.09           N  
HETATM 6640  C12 97Y A2001      21.953  33.249  31.008  1.00 67.65           C  
HETATM 6641  C14 97Y A2001      22.903  34.433  32.466  1.00 69.49           C  
HETATM 6642  C16 97Y A2001      22.382  34.714  31.031  1.00 63.34           C  
HETATM 6643  C18 97Y A2001      22.386  25.592  24.794  1.00 62.56           C  
HETATM 6644  C19 97Y A2001      22.392  28.463  26.707  1.00 57.31           C  
HETATM 6645  C23 97Y A2001      23.028  27.665  24.521  1.00 55.97           C  
HETATM 6646  C25 97Y A2001      21.538  33.738  27.649  1.00 66.60           C  
HETATM 6647  C27 97Y A2001      21.672  28.899  29.029  1.00 58.01           C  
HETATM 6648  C29 97Y A2001      21.869  34.821  33.557  1.00 64.69           C  
HETATM 6649  C30 97Y A2001      24.284  34.894  32.915  1.00 63.39           C  
HETATM 6650  C31 97Y A2001      19.220  34.231  27.084  1.00 82.60           C  
HETATM 6651  C32 97Y A2001      20.593  34.300  26.784  1.00 74.53           C  
HETATM 6652  C33 97Y A2001      18.815  33.634  28.285  1.00 75.17           C  
HETATM 6653  C34 97Y A2001      18.192  34.860  26.159  1.00 94.66           C  
HETATM 6654  C35 97Y A2001      15.806  35.447  25.679  1.00107.09           C  
HETATM 6655  C36 97Y A2001      15.090  34.411  24.850  1.00147.37           C  
HETATM 6656  C37 97Y A2001      13.632  34.287  25.242  1.00182.03           C  
HETATM 6657  C13 97Y B2001      54.565   9.632  53.194  1.00 62.86           C  
HETATM 6658  C15 97Y B2001      55.236   9.504  50.700  1.00 58.47           C  
HETATM 6659  C17 97Y B2001      53.541   9.010  54.086  1.00 67.11           C  
HETATM 6660  C20 97Y B2001      54.546  11.977  54.024  1.00 60.65           C  
HETATM 6661  C21 97Y B2001      54.553  18.312  58.238  1.00 76.96           C  
HETATM 6662  C22 97Y B2001      54.506  16.270  56.659  1.00 54.12           C  
HETATM 6663  C24 97Y B2001      55.160  12.604  56.290  1.00 58.57           C  
HETATM 6664  C26 97Y B2001      52.179   8.980  53.785  1.00 76.42           C  
HETATM 6665  C28 97Y B2001      55.002  11.614  55.309  1.00 59.72           C  
HETATM 6666  F01 97Y B2001      54.495  18.476  59.573  1.00 93.34           F  
HETATM 6667  F02 97Y B2001      55.496  19.087  57.717  1.00 71.57           F  
HETATM 6668  F03 97Y B2001      53.388  18.699  57.755  1.00 83.72           F  
HETATM 6669  O04 97Y B2001      51.087   6.612  57.738  1.00113.01           O  
HETATM 6670  O05 97Y B2001      45.811   7.714  56.813  1.00145.17           O  
HETATM 6671  O06 97Y B2001      45.423   7.450  58.972  1.00126.10           O  
HETATM 6672  N07 97Y B2001      54.953  15.006  56.895  1.00 57.50           N  
HETATM 6673  N08 97Y B2001      54.320  11.062  53.027  1.00 54.85           N  
HETATM 6674  N09 97Y B2001      55.336  15.966  58.753  1.00 63.12           N  
HETATM 6675  N10 97Y B2001      54.439  14.254  54.730  1.00 54.97           N  
HETATM 6676  N11 97Y B2001      49.321   7.122  56.430  1.00100.68           N  
HETATM 6677  C12 97Y B2001      54.310   9.055  51.824  1.00 62.28           C  
HETATM 6678  C14 97Y B2001      55.229   8.049  50.263  1.00 70.54           C  
HETATM 6679  C16 97Y B2001      54.643   7.582  51.607  1.00 63.19           C  
HETATM 6680  C18 97Y B2001      54.797  16.851  57.875  1.00 63.27           C  
HETATM 6681  C19 97Y B2001      54.873  13.964  56.007  1.00 58.37           C  
HETATM 6682  C23 97Y B2001      55.413  14.761  58.138  1.00 57.37           C  
HETATM 6683  C25 97Y B2001      53.943   8.383  55.253  1.00 77.51           C  
HETATM 6684  C27 97Y B2001      54.267  13.328  53.766  1.00 57.30           C  
HETATM 6685  C29 97Y B2001      54.258   7.776  49.117  1.00 79.64           C  
HETATM 6686  C30 97Y B2001      56.604   7.582  49.838  1.00 81.74           C  
HETATM 6687  C31 97Y B2001      51.639   7.815  55.823  1.00 85.92           C  
HETATM 6688  C32 97Y B2001      53.004   7.789  56.104  1.00 83.33           C  
HETATM 6689  C33 97Y B2001      51.238   8.402  54.639  1.00 85.12           C  
HETATM 6690  C34 97Y B2001      50.636   7.152  56.733  1.00 98.21           C  
HETATM 6691  C35 97Y B2001      48.257   6.461  57.172  1.00 99.86           C  
HETATM 6692  C36 97Y B2001      47.690   7.432  58.188  1.00116.11           C  
HETATM 6693  C37 97Y B2001      46.199   7.535  57.988  1.00130.92           C  
HETATM 6694  O   HOH A3001       3.339  13.041  11.487  1.00 71.10           O  
HETATM 6695  O   HOH A3002     -15.556  23.624  -2.020  1.00 58.42           O  
HETATM 6696  O   HOH A3003      -6.740  15.512   2.239  1.00 73.20           O  
HETATM 6697  O   HOH A3004      -5.999  12.810   2.347  1.00 67.16           O  
HETATM 6698  O   HOH B3001      17.300  19.293  84.164  1.00 63.74           O  
HETATM 6699  O   HOH B3002      24.061  12.276  51.511  1.00 38.64           O  
HETATM 6700  O   HOH B3003      36.380   7.412  63.115  1.00 57.30           O  
CONECT  585 2366                                                                
CONECT 2366  585                                                                
CONECT 2538 2881                                                                
CONECT 2881 2538                                                                
CONECT 3887 5668                                                                
CONECT 5668 3887                                                                
CONECT 5847 6190                                                                
CONECT 6190 5847                                                                
CONECT 6620 6622 6636 6640                                                      
CONECT 6621 6640 6641                                                           
CONECT 6622 6620 6627 6646                                                      
CONECT 6623 6628 6636 6647                                                      
CONECT 6624 6629 6630 6631 6643                                                 
CONECT 6625 6635 6643                                                           
CONECT 6626 6628 6644                                                           
CONECT 6627 6622 6652                                                           
CONECT 6628 6623 6626                                                           
CONECT 6629 6624                                                                
CONECT 6630 6624                                                                
CONECT 6631 6624                                                                
CONECT 6632 6653                                                                
CONECT 6633 6656                                                                
CONECT 6634 6656                                                                
CONECT 6635 6625 6644 6645                                                      
CONECT 6636 6620 6623                                                           
CONECT 6637 6643 6645                                                           
CONECT 6638 6644 6647                                                           
CONECT 6639 6653 6654                                                           
CONECT 6640 6620 6621 6642                                                      
CONECT 6641 6621 6642 6648 6649                                                 
CONECT 6642 6640 6641                                                           
CONECT 6643 6624 6625 6637                                                      
CONECT 6644 6626 6635 6638                                                      
CONECT 6645 6635 6637                                                           
CONECT 6646 6622 6651                                                           
CONECT 6647 6623 6638                                                           
CONECT 6648 6641                                                                
CONECT 6649 6641                                                                
CONECT 6650 6651 6652 6653                                                      
CONECT 6651 6646 6650                                                           
CONECT 6652 6627 6650                                                           
CONECT 6653 6632 6639 6650                                                      
CONECT 6654 6639 6655                                                           
CONECT 6655 6654 6656                                                           
CONECT 6656 6633 6634 6655                                                      
CONECT 6657 6659 6673 6677                                                      
CONECT 6658 6677 6678                                                           
CONECT 6659 6657 6664 6683                                                      
CONECT 6660 6665 6673 6684                                                      
CONECT 6661 6666 6667 6668 6680                                                 
CONECT 6662 6672 6680                                                           
CONECT 6663 6665 6681                                                           
CONECT 6664 6659 6689                                                           
CONECT 6665 6660 6663                                                           
CONECT 6666 6661                                                                
CONECT 6667 6661                                                                
CONECT 6668 6661                                                                
CONECT 6669 6690                                                                
CONECT 6670 6693                                                                
CONECT 6671 6693                                                                
CONECT 6672 6662 6681 6682                                                      
CONECT 6673 6657 6660                                                           
CONECT 6674 6680 6682                                                           
CONECT 6675 6681 6684                                                           
CONECT 6676 6690 6691                                                           
CONECT 6677 6657 6658 6679                                                      
CONECT 6678 6658 6679 6685 6686                                                 
CONECT 6679 6677 6678                                                           
CONECT 6680 6661 6662 6674                                                      
CONECT 6681 6663 6672 6675                                                      
CONECT 6682 6672 6674                                                           
CONECT 6683 6659 6688                                                           
CONECT 6684 6660 6675                                                           
CONECT 6685 6678                                                                
CONECT 6686 6678                                                                
CONECT 6687 6688 6689 6690                                                      
CONECT 6688 6683 6687                                                           
CONECT 6689 6664 6687                                                           
CONECT 6690 6669 6676 6687                                                      
CONECT 6691 6676 6692                                                           
CONECT 6692 6691 6693                                                           
CONECT 6693 6670 6671 6692                                                      
MASTER      547    0    2   45    6    0    6    6 6698    2   82   70          
END