HEADER    MEMBRANE PROTEIN                        11-JUL-18   6A93              
TITLE     CRYSTAL STRUCTURE OF 5-HT2AR IN COMPLEX WITH RISPERIDONE              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 5-HYDROXYTRYPTAMINE RECEPTOR 2A,SOLUBLE CYTOCHROME B562;   
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: 5-HT-2A,SEROTONIN RECEPTOR 2A,CYTOCHROME B-562;             
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ESCHERICHIA COLI;                 
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606, 562;                                           
SOURCE   5 GENE: HTR2A, HTR2, CYBC;                                             
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    MEMBRANE PROTEIN                                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.K.KIMURA,H.ASADA,A.INOUE,F.M.N.KADJI,D.IM,C.MORI,T.ARAKAWA,         
AUTHOR   2 K.HIRATA,Y.NOMURA,N.NOMURA,J.AOKI,S.IWATA,T.SHIMAMURA                
REVDAT   2   20-NOV-19 6A93    1       JRNL                                     
REVDAT   1   13-FEB-19 6A93    0                                                
JRNL        AUTH   K.T.KIMURA,H.ASADA,A.INOUE,F.M.N.KADJI,D.IM,C.MORI,          
JRNL        AUTH 2 T.ARAKAWA,K.HIRATA,Y.NOMURA,N.NOMURA,J.AOKI,S.IWATA,         
JRNL        AUTH 3 T.SHIMAMURA                                                  
JRNL        TITL   STRUCTURES OF THE 5-HT2ARECEPTOR IN COMPLEX WITH THE         
JRNL        TITL 2 ANTIPSYCHOTICS RISPERIDONE AND ZOTEPINE.                     
JRNL        REF    NAT.STRUCT.MOL.BIOL.          V.  26   121 2019              
JRNL        REFN                   ESSN 1545-9985                               
JRNL        PMID   30723326                                                     
JRNL        DOI    10.1038/S41594-018-0180-Z                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (DEV_3150)                                    
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) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.24                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 2.030                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 84.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 18429                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.245                           
REMARK   3   R VALUE            (WORKING SET) : 0.244                           
REMARK   3   FREE R VALUE                     : 0.275                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.490                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1011                            
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 46.2463 -  5.7357    1.00     3093   182  0.2372 0.2434        
REMARK   3     2  5.7357 -  4.5539    1.00     2976   168  0.2315 0.2448        
REMARK   3     3  4.5539 -  3.9786    1.00     2965   168  0.2252 0.2575        
REMARK   3     4  3.9786 -  3.6150    1.00     2927   180  0.2448 0.2883        
REMARK   3     5  3.6150 -  3.3560    0.86     2511   137  0.2565 0.3151        
REMARK   3     6  3.3560 -  3.1581    0.63     1851   114  0.2747 0.3254        
REMARK   3     7  3.1581 -  3.0000    0.38     1095    62  0.2907 0.3390        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
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)     : 0.390            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.960           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 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      :  0.003           6018                                  
REMARK   3   ANGLE     :  0.651           8173                                  
REMARK   3   CHIRALITY :  0.040            969                                  
REMARK   3   PLANARITY :  0.004            974                                  
REMARK   3   DIHEDRAL  : 12.015           3602                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 9                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 69 THROUGH 144 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  20.6808   4.5076  70.7583              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5154 T22:   1.3779                                     
REMARK   3      T33:   0.9780 T12:  -0.0869                                     
REMARK   3      T13:   0.1916 T23:  -0.5543                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1936 L22:   1.8780                                     
REMARK   3      L33:   1.1415 L12:  -1.1697                                     
REMARK   3      L13:   0.5905 L23:   0.0648                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1091 S12:  -1.3421 S13:   0.4284                       
REMARK   3      S21:   0.4594 S22:   0.3077 S23:   0.1081                       
REMARK   3      S31:   0.1091 S32:  -0.2851 S33:  -0.1325                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND ((RESID 145 THROUGH 265 ) OR (RESID      
REMARK   3               1001 THROUGH 1106 ) OR (RESID 313 THROUGH 348 ))       
REMARK   3    ORIGIN FOR THE GROUP (A):  41.8946  -1.3750  53.2675              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2109 T22:  -0.2713                                     
REMARK   3      T33:   0.4002 T12:   0.0872                                     
REMARK   3      T13:   0.1726 T23:   0.0672                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4497 L22:   0.8651                                     
REMARK   3      L33:   1.2257 L12:   0.0088                                     
REMARK   3      L13:   0.0743 L23:   0.0815                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0286 S12:  -0.2235 S13:   0.0584                       
REMARK   3      S21:   0.2888 S22:  -0.0692 S23:   0.4928                       
REMARK   3      S31:  -0.0268 S32:  -0.8647 S33:   0.0687                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 349 THROUGH 399 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  24.5504  -3.4610  69.6949              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3981 T22:   1.3501                                     
REMARK   3      T33:   0.7981 T12:  -0.1396                                     
REMARK   3      T13:   0.2018 T23:  -0.0012                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7848 L22:   3.7405                                     
REMARK   3      L33:   2.9094 L12:  -0.7023                                     
REMARK   3      L13:  -2.1347 L23:  -0.2719                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0123 S12:  -0.7017 S13:  -0.1977                       
REMARK   3      S21:   0.2884 S22:   0.1719 S23:   0.3255                       
REMARK   3      S31:   0.0462 S32:   0.1452 S33:  -0.0980                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 72 THROUGH 101 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  24.6030  -7.5122  29.8674              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4906 T22:   0.7173                                     
REMARK   3      T33:   0.3070 T12:  -0.1053                                     
REMARK   3      T13:   0.1253 T23:  -0.1053                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.5460 L22:   3.7576                                     
REMARK   3      L33:   3.8312 L12:  -1.8029                                     
REMARK   3      L13:  -0.9027 L23:  -0.3779                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3680 S12:   0.3353 S13:  -0.0467                       
REMARK   3      S21:   0.3171 S22:  -0.0203 S23:   0.4878                       
REMARK   3      S31:   0.7016 S32:  -0.5326 S33:  -0.3384                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 102 THROUGH 243 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  23.0975   7.8988  20.9241              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4610 T22:   1.2319                                     
REMARK   3      T33:   1.2478 T12:   0.1031                                     
REMARK   3      T13:   0.3598 T23:   0.3562                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1642 L22:   1.0563                                     
REMARK   3      L33:   0.9191 L12:   0.5428                                     
REMARK   3      L13:  -0.7527 L23:   0.2282                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0603 S12:   0.3386 S13:   0.7029                       
REMARK   3      S21:   0.0412 S22:  -0.1023 S23:  -0.1685                       
REMARK   3      S31:  -0.1471 S32:  -0.0962 S33:   0.0883                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'B' AND ((RESID 244 THROUGH 265 ) OR (RESID      
REMARK   3               1001 THROUGH 1083 ))                                   
REMARK   3    ORIGIN FOR THE GROUP (A):  64.2343   6.0349   1.4453              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5466 T22:   1.6344                                     
REMARK   3      T33:   0.7550 T12:   0.0040                                     
REMARK   3      T13:   0.2513 T23:   0.2405                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2142 L22:   0.8259                                     
REMARK   3      L33:   0.4975 L12:  -0.0810                                     
REMARK   3      L13:  -0.9690 L23:   0.1838                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2516 S12:  -0.0489 S13:   0.4006                       
REMARK   3      S21:  -0.1374 S22:   0.2494 S23:  -0.1415                       
REMARK   3      S31:  -0.2423 S32:  -0.0994 S33:  -0.2776                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'B' AND ((RESID 1084 THROUGH 1106 ) OR (RESID    
REMARK   3               313 THROUGH 348 ))                                     
REMARK   3    ORIGIN FOR THE GROUP (A):  47.5158  -0.4583   9.8685              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4854 T22:   1.4383                                     
REMARK   3      T33:   0.5718 T12:   0.0782                                     
REMARK   3      T13:   0.2365 T23:   0.0808                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3432 L22:   0.8175                                     
REMARK   3      L33:   1.1661 L12:  -0.2925                                     
REMARK   3      L13:  -1.9635 L23:   0.0975                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0383 S12:  -0.0152 S13:   0.2078                       
REMARK   3      S21:  -0.1792 S22:  -0.0915 S23:  -0.2437                       
REMARK   3      S31:   0.0368 S32:  -0.1680 S33:  -0.0178                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 349 THROUGH 382 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  18.1288  -6.5547  15.5680              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4964 T22:   1.7777                                     
REMARK   3      T33:   0.6755 T12:  -0.0876                                     
REMARK   3      T13:   0.0459 T23:  -0.1810                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1001 L22:   5.6639                                     
REMARK   3      L33:   0.2381 L12:  -0.1916                                     
REMARK   3      L13:   0.1251 L23:  -0.6633                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2558 S12:   1.1927 S13:   0.4267                       
REMARK   3      S21:  -0.6346 S22:  -0.2187 S23:   1.0325                       
REMARK   3      S31:   0.0815 S32:  -0.5561 S33:   0.0072                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 383 THROUGH 401 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  44.3721  -7.1268  32.1730              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3547 T22:   0.7142                                     
REMARK   3      T33:   0.3790 T12:  -0.0720                                     
REMARK   3      T13:  -0.1393 T23:  -0.0795                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8963 L22:   4.4756                                     
REMARK   3      L33:   2.8269 L12:  -1.7879                                     
REMARK   3      L13:   0.8765 L23:  -2.1879                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2853 S12:   0.9082 S13:   0.0584                       
REMARK   3      S21:   0.1828 S22:  -0.0835 S23:  -0.4092                       
REMARK   3      S31:   0.7284 S32:   0.5860 S33:  -0.2248                       
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 6A93 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 20-JUL-18.                  
REMARK 100 THE DEPOSITION ID IS D_1300008335.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-DEC-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0-6.5                            
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL32XU                             
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 MX225-HS                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 29971                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.707                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 46.241                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 84.0                               
REMARK 200  DATA REDUNDANCY                : 22.40                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.6300                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.71                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.80                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 2RH1                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.62                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.21                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM MES, PH 6.0-6.5, 28-31% (V/V)     
REMARK 280  PEG 400, 120-200 MM AM-FORMATE, 1-2% (V/V) DMSO, LIPIDIC CUBIC      
REMARK 280  PHASE, TEMPERATURE 293K                                             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000      138.86000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       21.07500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000      138.86000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       21.07500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 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     GLY A    67                                                      
REMARK 465     GLY A    68                                                      
REMARK 465     LYS A   400                                                      
REMARK 465     GLU A   401                                                      
REMARK 465     ASN A   402                                                      
REMARK 465     LYS A   403                                                      
REMARK 465     GLY B    67                                                      
REMARK 465     GLY B    68                                                      
REMARK 465     THR B    69                                                      
REMARK 465     HIS B    70                                                      
REMARK 465     LEU B    71                                                      
REMARK 465     ILE B   181                                                      
REMARK 465     HIS B   182                                                      
REMARK 465     HIS B   183                                                      
REMARK 465     SER B   184                                                      
REMARK 465     ARG B   185                                                      
REMARK 465     PHE B   186                                                      
REMARK 465     ASN B   187                                                      
REMARK 465     SER B  1042                                                      
REMARK 465     GLY B  1043                                                      
REMARK 465     SER B  1044                                                      
REMARK 465     ASN B   402                                                      
REMARK 465     LYS B   403                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OD2  ASP A  1066     OH   TYR A  1105              2.10            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PHE A 243      -50.45   -122.01                                   
REMARK 500    PHE B 243      -50.17   -122.41                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     1PE A 3004                                                       
REMARK 610     1PE A 3006                                                       
REMARK 610     PLM B 3002                                                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A3003  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 182   NE2                                                    
REMARK 620 2 HIS A 183   NE2 108.7                                              
REMARK 620 3 GLU A 264   OE2 101.5  99.7                                        
REMARK 620 4 GLU A 318   OE1 146.5  93.5  99.0                                  
REMARK 620 5 GLU A 318   OE2  91.5 109.8 141.9  56.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 8NU A 3001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLR A 3002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 3003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE A 3004                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE A 3005                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 1PE A 3006                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 8NU B 3001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PLM B 3002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLR B 3003                
DBREF  6A93 A   70   265  UNP    P28223   5HT2A_HUMAN     70    265             
DBREF  6A93 A 1001  1040  UNP    P0ABE7   C562_ECOLX      23     62             
DBREF  6A93 A 1066  1106  UNP    P0ABE7   C562_ECOLX      88    128             
DBREF  6A93 A  313   403  UNP    P28223   5HT2A_HUMAN    313    403             
DBREF  6A93 B   70   265  UNP    P28223   5HT2A_HUMAN     70    265             
DBREF  6A93 B 1001  1040  UNP    P0ABE7   C562_ECOLX      23     62             
DBREF  6A93 B 1066  1106  UNP    P0ABE7   C562_ECOLX      88    128             
DBREF  6A93 B  313   403  UNP    P28223   5HT2A_HUMAN    313    403             
SEQADV 6A93 GLY A   67  UNP  P28223              EXPRESSION TAG                 
SEQADV 6A93 GLY A   68  UNP  P28223              EXPRESSION TAG                 
SEQADV 6A93 THR A   69  UNP  P28223              EXPRESSION TAG                 
SEQADV 6A93 LYS A  162  UNP  P28223    SER   162 ENGINEERED MUTATION            
SEQADV 6A93 TRP A  164  UNP  P28223    MET   164 ENGINEERED MUTATION            
SEQADV 6A93 TRP A 1007  UNP  P0ABE7    MET    29 ENGINEERED MUTATION            
SEQADV 6A93 GLY A 1041  UNP  P0ABE7              LINKER                         
SEQADV 6A93 SER A 1042  UNP  P0ABE7              LINKER                         
SEQADV 6A93 GLY A 1043  UNP  P0ABE7              LINKER                         
SEQADV 6A93 SER A 1044  UNP  P0ABE7              LINKER                         
SEQADV 6A93 GLY A 1045  UNP  P0ABE7              LINKER                         
SEQADV 6A93 ILE A 1098  UNP  P0ABE7    ARG   120 ENGINEERED MUTATION            
SEQADV 6A93 ILE A 1102  UNP  P0ABE7    HIS   124 ENGINEERED MUTATION            
SEQADV 6A93 GLY A 1106  UNP  P0ABE7    ARG   128 ENGINEERED MUTATION            
SEQADV 6A93 GLY B   67  UNP  P28223              EXPRESSION TAG                 
SEQADV 6A93 GLY B   68  UNP  P28223              EXPRESSION TAG                 
SEQADV 6A93 THR B   69  UNP  P28223              EXPRESSION TAG                 
SEQADV 6A93 LYS B  162  UNP  P28223    SER   162 ENGINEERED MUTATION            
SEQADV 6A93 TRP B  164  UNP  P28223    MET   164 ENGINEERED MUTATION            
SEQADV 6A93 TRP B 1007  UNP  P0ABE7    MET    29 ENGINEERED MUTATION            
SEQADV 6A93 GLY B 1041  UNP  P0ABE7              LINKER                         
SEQADV 6A93 SER B 1042  UNP  P0ABE7              LINKER                         
SEQADV 6A93 GLY B 1043  UNP  P0ABE7              LINKER                         
SEQADV 6A93 SER B 1044  UNP  P0ABE7              LINKER                         
SEQADV 6A93 GLY B 1045  UNP  P0ABE7              LINKER                         
SEQADV 6A93 ILE B 1098  UNP  P0ABE7    ARG   120 ENGINEERED MUTATION            
SEQADV 6A93 ILE B 1102  UNP  P0ABE7    HIS   124 ENGINEERED MUTATION            
SEQADV 6A93 GLY B 1106  UNP  P0ABE7    ARG   128 ENGINEERED MUTATION            
SEQRES   1 A  376  GLY GLY THR HIS LEU GLN GLU LYS ASN TRP SER ALA LEU          
SEQRES   2 A  376  LEU THR ALA VAL VAL ILE ILE LEU THR ILE ALA GLY ASN          
SEQRES   3 A  376  ILE LEU VAL ILE MET ALA VAL SER LEU GLU LYS LYS LEU          
SEQRES   4 A  376  GLN ASN ALA THR ASN TYR PHE LEU MET SER LEU ALA ILE          
SEQRES   5 A  376  ALA ASP MET LEU LEU GLY PHE LEU VAL MET PRO VAL SER          
SEQRES   6 A  376  MET LEU THR ILE LEU TYR GLY TYR ARG TRP PRO LEU PRO          
SEQRES   7 A  376  SER LYS LEU CYS ALA VAL TRP ILE TYR LEU ASP VAL LEU          
SEQRES   8 A  376  PHE SER THR ALA LYS ILE TRP HIS LEU CYS ALA ILE SER          
SEQRES   9 A  376  LEU ASP ARG TYR VAL ALA ILE GLN ASN PRO ILE HIS HIS          
SEQRES  10 A  376  SER ARG PHE ASN SER ARG THR LYS ALA PHE LEU LYS ILE          
SEQRES  11 A  376  ILE ALA VAL TRP THR ILE SER VAL GLY ILE SER MET PRO          
SEQRES  12 A  376  ILE PRO VAL PHE GLY LEU GLN ASP ASP SER LYS VAL PHE          
SEQRES  13 A  376  LYS GLU GLY SER CYS LEU LEU ALA ASP ASP ASN PHE VAL          
SEQRES  14 A  376  LEU ILE GLY SER PHE VAL SER PHE PHE ILE PRO LEU THR          
SEQRES  15 A  376  ILE MET VAL ILE THR TYR PHE LEU THR ILE LYS SER LEU          
SEQRES  16 A  376  GLN LYS GLU ALA ALA ASP LEU GLU ASP ASN TRP GLU THR          
SEQRES  17 A  376  LEU ASN ASP ASN LEU LYS VAL ILE GLU LYS ALA ASP ASN          
SEQRES  18 A  376  ALA ALA GLN VAL LYS ASP ALA LEU THR LYS MET ARG ALA          
SEQRES  19 A  376  ALA ALA LEU ASP ALA GLY SER GLY SER GLY ASP ILE LEU          
SEQRES  20 A  376  VAL GLY GLN ILE ASP ASP ALA LEU LYS LEU ALA ASN GLU          
SEQRES  21 A  376  GLY LYS VAL LYS GLU ALA GLN ALA ALA ALA GLU GLN LEU          
SEQRES  22 A  376  LYS THR THR ILE ASN ALA TYR ILE GLN LYS TYR GLY GLN          
SEQRES  23 A  376  SER ILE SER ASN GLU GLN LYS ALA CYS LYS VAL LEU GLY          
SEQRES  24 A  376  ILE VAL PHE PHE LEU PHE VAL VAL MET TRP CYS PRO PHE          
SEQRES  25 A  376  PHE ILE THR ASN ILE MET ALA VAL ILE CYS LYS GLU SER          
SEQRES  26 A  376  CYS ASN GLU ASP VAL ILE GLY ALA LEU LEU ASN VAL PHE          
SEQRES  27 A  376  VAL TRP ILE GLY TYR LEU SER SER ALA VAL ASN PRO LEU          
SEQRES  28 A  376  VAL TYR THR LEU PHE ASN LYS THR TYR ARG SER ALA PHE          
SEQRES  29 A  376  SER ARG TYR ILE GLN CYS GLN TYR LYS GLU ASN LYS              
SEQRES   1 B  376  GLY GLY THR HIS LEU GLN GLU LYS ASN TRP SER ALA LEU          
SEQRES   2 B  376  LEU THR ALA VAL VAL ILE ILE LEU THR ILE ALA GLY ASN          
SEQRES   3 B  376  ILE LEU VAL ILE MET ALA VAL SER LEU GLU LYS LYS LEU          
SEQRES   4 B  376  GLN ASN ALA THR ASN TYR PHE LEU MET SER LEU ALA ILE          
SEQRES   5 B  376  ALA ASP MET LEU LEU GLY PHE LEU VAL MET PRO VAL SER          
SEQRES   6 B  376  MET LEU THR ILE LEU TYR GLY TYR ARG TRP PRO LEU PRO          
SEQRES   7 B  376  SER LYS LEU CYS ALA VAL TRP ILE TYR LEU ASP VAL LEU          
SEQRES   8 B  376  PHE SER THR ALA LYS ILE TRP HIS LEU CYS ALA ILE SER          
SEQRES   9 B  376  LEU ASP ARG TYR VAL ALA ILE GLN ASN PRO ILE HIS HIS          
SEQRES  10 B  376  SER ARG PHE ASN SER ARG THR LYS ALA PHE LEU LYS ILE          
SEQRES  11 B  376  ILE ALA VAL TRP THR ILE SER VAL GLY ILE SER MET PRO          
SEQRES  12 B  376  ILE PRO VAL PHE GLY LEU GLN ASP ASP SER LYS VAL PHE          
SEQRES  13 B  376  LYS GLU GLY SER CYS LEU LEU ALA ASP ASP ASN PHE VAL          
SEQRES  14 B  376  LEU ILE GLY SER PHE VAL SER PHE PHE ILE PRO LEU THR          
SEQRES  15 B  376  ILE MET VAL ILE THR TYR PHE LEU THR ILE LYS SER LEU          
SEQRES  16 B  376  GLN LYS GLU ALA ALA ASP LEU GLU ASP ASN TRP GLU THR          
SEQRES  17 B  376  LEU ASN ASP ASN LEU LYS VAL ILE GLU LYS ALA ASP ASN          
SEQRES  18 B  376  ALA ALA GLN VAL LYS ASP ALA LEU THR LYS MET ARG ALA          
SEQRES  19 B  376  ALA ALA LEU ASP ALA GLY SER GLY SER GLY ASP ILE LEU          
SEQRES  20 B  376  VAL GLY GLN ILE ASP ASP ALA LEU LYS LEU ALA ASN GLU          
SEQRES  21 B  376  GLY LYS VAL LYS GLU ALA GLN ALA ALA ALA GLU GLN LEU          
SEQRES  22 B  376  LYS THR THR ILE ASN ALA TYR ILE GLN LYS TYR GLY GLN          
SEQRES  23 B  376  SER ILE SER ASN GLU GLN LYS ALA CYS LYS VAL LEU GLY          
SEQRES  24 B  376  ILE VAL PHE PHE LEU PHE VAL VAL MET TRP CYS PRO PHE          
SEQRES  25 B  376  PHE ILE THR ASN ILE MET ALA VAL ILE CYS LYS GLU SER          
SEQRES  26 B  376  CYS ASN GLU ASP VAL ILE GLY ALA LEU LEU ASN VAL PHE          
SEQRES  27 B  376  VAL TRP ILE GLY TYR LEU SER SER ALA VAL ASN PRO LEU          
SEQRES  28 B  376  VAL TYR THR LEU PHE ASN LYS THR TYR ARG SER ALA PHE          
SEQRES  29 B  376  SER ARG TYR ILE GLN CYS GLN TYR LYS GLU ASN LYS              
HET    8NU  A3001      30                                                       
HET    CLR  A3002      28                                                       
HET     ZN  A3003       1                                                       
HET    1PE  A3004      13                                                       
HET    1PE  A3005      16                                                       
HET    1PE  A3006      10                                                       
HET    8NU  B3001      30                                                       
HET    PLM  B3002      10                                                       
HET    CLR  B3003      28                                                       
HETNAM     8NU 3-[2-[4-(6-FLUORANYL-1,2-BENZOXAZOL-3-YL)PIPERIDIN-1-            
HETNAM   2 8NU  YL]ETHYL]-2-METHYL-6,7,8,9-TETRAHYDROPYRIDO[1,2-                
HETNAM   3 8NU  A]PYRIMIDIN-4-ONE                                               
HETNAM     CLR CHOLESTEROL                                                      
HETNAM      ZN ZINC ION                                                         
HETNAM     1PE PENTAETHYLENE GLYCOL                                             
HETNAM     PLM PALMITIC ACID                                                    
HETSYN     1PE PEG400                                                           
FORMUL   3  8NU    2(C23 H27 F N4 O2)                                           
FORMUL   4  CLR    2(C27 H46 O)                                                 
FORMUL   5   ZN    ZN 2+                                                        
FORMUL   6  1PE    3(C10 H22 O6)                                                
FORMUL  10  PLM    C16 H32 O2                                                   
HELIX    1 AA1 THR A   69  GLU A  102  1                                  34    
HELIX    2 AA2 LYS A  103  GLN A  106  5                                   4    
HELIX    3 AA3 ASN A  107  VAL A  127  1                                  21    
HELIX    4 AA4 VAL A  127  TYR A  137  1                                  11    
HELIX    5 AA5 PRO A  144  ASN A  179  1                                  36    
HELIX    6 AA6 SER A  188  MET A  208  1                                  21    
HELIX    7 AA7 MET A  208  ASP A  217  1                                  10    
HELIX    8 AA8 ASP A  231  PHE A  243  1                                  13    
HELIX    9 AA9 PHE A  243  LYS A 1019  1                                  42    
HELIX   10 AB1 ASN A 1022  GLY A 1041  1                                  20    
HELIX   11 AB2 ILE A 1067  GLU A 1081  1                                  15    
HELIX   12 AB3 LYS A 1083  CYS A  349  1                                  61    
HELIX   13 AB4 ASN A  354  PHE A  383  1                                  30    
HELIX   14 AB5 ASN A  384  GLN A  396  1                                  13    
HELIX   15 AB6 GLU B   73  GLU B  102  1                                  30    
HELIX   16 AB7 ASN B  107  VAL B  127  1                                  21    
HELIX   17 AB8 VAL B  127  TYR B  137  1                                  11    
HELIX   18 AB9 PRO B  144  ASN B  179  1                                  36    
HELIX   19 AC1 ARG B  189  MET B  208  1                                  20    
HELIX   20 AC2 MET B  208  ASP B  217  1                                  10    
HELIX   21 AC3 ASP B  218  VAL B  221  5                                   4    
HELIX   22 AC4 ASP B  231  PHE B  243  1                                  13    
HELIX   23 AC5 PHE B  243  LYS B 1019  1                                  42    
HELIX   24 AC6 ASN B 1022  GLY B 1041  1                                  20    
HELIX   25 AC7 ASP B 1066  GLU B 1081  1                                  16    
HELIX   26 AC8 LYS B 1083  CYS B  349  1                                  61    
HELIX   27 AC9 GLU B  355  PHE B  383  1                                  29    
HELIX   28 AD1 ASN B  384  GLN B  396  1                                  13    
SSBOND   1 CYS A  148    CYS A  227                          1555   1555  2.03  
SSBOND   2 CYS A  349    CYS A  353                          1555   1555  2.04  
SSBOND   3 CYS B  148    CYS B  227                          1555   1555  2.03  
SSBOND   4 CYS B  349    CYS B  353                          1555   1555  2.03  
LINK         NE2 HIS A 182                ZN    ZN A3003     1555   1555  2.10  
LINK         NE2 HIS A 183                ZN    ZN A3003     1555   1555  2.16  
LINK         OE2 GLU A 264                ZN    ZN A3003     1555   1555  1.97  
LINK         OE1 GLU A 318                ZN    ZN A3003     1555   1555  1.97  
LINK         OE2 GLU A 318                ZN    ZN A3003     1555   1555  2.53  
LINK         SG  CYS B 397                 C1  PLM B3002     1555   1555  1.75  
SITE     1 AC1 16 SER A 131  TRP A 151  ASP A 155  SER A 159                    
SITE     2 AC1 16 THR A 160  ILE A 163  LEU A 228  SER A 242                    
SITE     3 AC1 16 PHE A 243  PHE A 332  TRP A 336  PHE A 339                    
SITE     4 AC1 16 PHE A 340  LEU A 362  ASN A 363  TYR A 370                    
SITE     1 AC2  7 MET A 114  ILE A 118  TYR A 153  PHE A 193                    
SITE     2 AC2  7 ILE A 196  TRP A 200  VAL A 204                               
SITE     1 AC3  4 HIS A 182  HIS A 183  GLU A 264  GLU A 318                    
SITE     1 AC4  1 SER A 226                                                     
SITE     1 AC5  7 LEU A 261  GLN A 262  ALA A 265  ILE A 315                    
SITE     2 AC5  7 GLN A 319  GLU A1004  ASN A1080                               
SITE     1 AC6  3 GLU A1004  TRP A1007  LYS A1027                               
SITE     1 AC7 15 SER B 131  TRP B 151  ASP B 155  VAL B 156                    
SITE     2 AC7 15 SER B 159  THR B 160  ILE B 163  LEU B 228                    
SITE     3 AC7 15 SER B 242  PHE B 332  TRP B 336  PHE B 339                    
SITE     4 AC7 15 PHE B 340  ASN B 363  TYR B 370                               
SITE     1 AC8  4 ILE B 395  GLN B 396  CYS B 397  CLR B3003                    
SITE     1 AC9  4 LEU B  94  TYR B 394  TYR B 399  PLM B3002                    
CRYST1  277.720   42.150   91.940  90.00  92.55  90.00 C 1 2 1       8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.003601  0.000000  0.000160        0.00000                         
SCALE2      0.000000  0.023725  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010887        0.00000                         
ATOM      1  N   THR A  69       1.151 -10.899  83.708  1.00142.39           N  
ANISOU    1  N   THR A  69    12071  26368  15661  -1839   5088    880       N  
ATOM      2  CA  THR A  69       0.217  -9.964  83.096  1.00144.15           C  
ANISOU    2  CA  THR A  69    12113  26428  16228  -1832   5091    698       C  
ATOM      3  C   THR A  69       0.713  -9.561  81.708  1.00144.29           C  
ANISOU    3  C   THR A  69    12156  26122  16547  -1930   4823    451       C  
ATOM      4  O   THR A  69       1.917  -9.499  81.462  1.00142.86           O  
ANISOU    4  O   THR A  69    12138  25919  16225  -1897   4663    257       O  
ATOM      5  CB  THR A  69       0.020  -8.710  83.974  1.00145.57           C  
ANISOU    5  CB  THR A  69    12273  26842  16194  -1536   5226    387       C  
ATOM      6  OG1 THR A  69      -0.215  -9.108  85.331  1.00150.60           O  
ANISOU    6  OG1 THR A  69    12937  27800  16486  -1414   5461    593       O  
ATOM      7  CG2 THR A  69      -1.162  -7.881  83.490  1.00145.43           C  
ANISOU    7  CG2 THR A  69    12052  26686  16519  -1533   5273    284       C  
ATOM      8  N   HIS A  70      -0.223  -9.299  80.794  1.00145.10           N  
ANISOU    8  N   HIS A  70    12097  25966  17067  -2046   4776    459       N  
ATOM      9  CA  HIS A  70       0.127  -8.924  79.430  1.00141.93           C  
ANISOU    9  CA  HIS A  70    11721  25232  16974  -2136   4527    244       C  
ATOM     10  C   HIS A  70       0.554  -7.465  79.312  1.00135.56           C  
ANISOU   10  C   HIS A  70    10963  24419  16123  -1917   4461   -233       C  
ATOM     11  O   HIS A  70       1.203  -7.100  78.325  1.00128.34           O  
ANISOU   11  O   HIS A  70    10131  23264  15367  -1949   4252   -460       O  
ATOM     12  CB  HIS A  70      -1.046  -9.217  78.495  1.00147.33           C  
ANISOU   12  CB  HIS A  70    12229  25629  18120  -2330   4484    435       C  
ATOM     13  CG  HIS A  70      -1.462 -10.656  78.483  1.00152.89           C  
ANISOU   13  CG  HIS A  70    12891  26272  18928  -2568   4505    900       C  
ATOM     14  ND1 HIS A  70      -0.749 -11.631  77.819  1.00152.01           N  
ANISOU   14  ND1 HIS A  70    12902  25979  18875  -2758   4309   1066       N  
ATOM     15  CD2 HIS A  70      -2.511 -11.288  79.062  1.00158.07           C  
ANISOU   15  CD2 HIS A  70    13403  27010  19646  -2647   4693   1238       C  
ATOM     16  CE1 HIS A  70      -1.342 -12.799  77.985  1.00154.58           C  
ANISOU   16  CE1 HIS A  70    13170  26264  19299  -2944   4360   1491       C  
ATOM     17  NE2 HIS A  70      -2.414 -12.619  78.735  1.00158.32           N  
ANISOU   17  NE2 HIS A  70    13480  26893  19783  -2884   4597   1600       N  
ATOM     18  N   LEU A  71       0.206  -6.626  80.291  1.00138.67           N  
ANISOU   18  N   LEU A  71    11316  25059  16311  -1695   4628   -385       N  
ATOM     19  CA  LEU A  71       0.760  -5.274  80.344  1.00135.29           C  
ANISOU   19  CA  LEU A  71    10967  24647  15788  -1475   4551   -833       C  
ATOM     20  C   LEU A  71       2.208  -5.288  80.825  1.00137.89           C  
ANISOU   20  C   LEU A  71    11498  25116  15776  -1366   4469  -1015       C  
ATOM     21  O   LEU A  71       3.015  -4.433  80.426  1.00136.65           O  
ANISOU   21  O   LEU A  71    11442  24846  15631  -1270   4310  -1373       O  
ATOM     22  CB  LEU A  71      -0.106  -4.392  81.242  1.00129.69           C  
ANISOU   22  CB  LEU A  71    10153  24150  14973  -1272   4740   -927       C  
ATOM     23  CG  LEU A  71       0.583  -3.404  82.188  1.00123.17           C  
ANISOU   23  CG  LEU A  71     9445  23554  13800   -994   4756  -1264       C  
ATOM     24  CD1 LEU A  71       0.210  -1.969  81.840  1.00118.07           C  
ANISOU   24  CD1 LEU A  71     8754  22793  13313   -856   4692  -1607       C  
ATOM     25  CD2 LEU A  71       0.228  -3.720  83.634  1.00123.09           C  
ANISOU   25  CD2 LEU A  71     9418  23909  13443   -859   4997  -1087       C  
ATOM     26  N   GLN A  72       2.553  -6.252  81.683  1.00140.99           N  
ANISOU   26  N   GLN A  72    11957  25745  15870  -1378   4571   -768       N  
ATOM     27  CA  GLN A  72       3.949  -6.473  82.033  1.00140.95           C  
ANISOU   27  CA  GLN A  72    12143  25851  15560  -1304   4472   -897       C  
ATOM     28  C   GLN A  72       4.797  -6.713  80.793  1.00139.45           C  
ANISOU   28  C   GLN A  72    12033  25367  15583  -1461   4238   -989       C  
ATOM     29  O   GLN A  72       5.993  -6.402  80.791  1.00139.77           O  
ANISOU   29  O   GLN A  72    12216  25416  15473  -1367   4109  -1254       O  
ATOM     30  CB  GLN A  72       4.078  -7.637  83.011  1.00141.19           C  
ANISOU   30  CB  GLN A  72    12235  26145  15268  -1324   4611   -551       C  
ATOM     31  CG  GLN A  72       3.303  -7.446  84.301  1.00142.05           C  
ANISOU   31  CG  GLN A  72    12286  26552  15136  -1152   4856   -450       C  
ATOM     32  CD  GLN A  72       3.692  -6.179  85.040  1.00139.81           C  
ANISOU   32  CD  GLN A  72    12066  26434  14621   -853   4854   -857       C  
ATOM     33  OE1 GLN A  72       4.865  -5.810  85.089  1.00139.83           O  
ANISOU   33  OE1 GLN A  72    12219  26449  14461   -743   4699  -1143       O  
ATOM     34  NE2 GLN A  72       2.705  -5.505  85.621  1.00137.98           N  
ANISOU   34  NE2 GLN A  72    11720  26322  14386   -722   5018   -886       N  
ATOM     35  N   GLU A  73       4.209  -7.282  79.736  1.00137.16           N  
ANISOU   35  N   GLU A  73    11656  24810  15650  -1695   4173   -775       N  
ATOM     36  CA  GLU A  73       4.959  -7.457  78.496  1.00132.74           C  
ANISOU   36  CA  GLU A  73    11182  23938  15313  -1832   3941   -870       C  
ATOM     37  C   GLU A  73       5.349  -6.112  77.895  1.00127.14           C  
ANISOU   37  C   GLU A  73    10503  23056  14748  -1702   3817  -1314       C  
ATOM     38  O   GLU A  73       6.484  -5.938  77.434  1.00127.84           O  
ANISOU   38  O   GLU A  73    10754  22992  14829  -1674   3640  -1523       O  
ATOM     39  CB  GLU A  73       4.142  -8.270  77.489  1.00136.58           C  
ANISOU   39  CB  GLU A  73    11602  24115  16178  -2080   3860   -556       C  
ATOM     40  CG  GLU A  73       3.862  -9.701  77.907  1.00143.84           C  
ANISOU   40  CG  GLU A  73    12553  25080  17021  -2231   3911    -91       C  
ATOM     41  CD  GLU A  73       3.209 -10.510  76.799  1.00146.08           C  
ANISOU   41  CD  GLU A  73    12800  24999  17706  -2476   3769    185       C  
ATOM     42  OE1 GLU A  73       2.421  -9.932  76.021  1.00146.08           O  
ANISOU   42  OE1 GLU A  73    12636  24842  18028  -2526   3751     86       O  
ATOM     43  OE2 GLU A  73       3.491 -11.722  76.699  1.00147.16           O  
ANISOU   43  OE2 GLU A  73    13080  24995  17837  -2609   3661    491       O  
ATOM     44  N   LYS A  74       4.429  -5.143  77.899  1.00121.73           N  
ANISOU   44  N   LYS A  74     9710  22335  14208  -1606   3881  -1445       N  
ATOM     45  CA  LYS A  74       4.780  -3.823  77.389  1.00117.10           C  
ANISOU   45  CA  LYS A  74     9173  21575  13745  -1475   3759  -1850       C  
ATOM     46  C   LYS A  74       5.837  -3.185  78.273  1.00115.26           C  
ANISOU   46  C   LYS A  74     9063  21547  13184  -1263   3747  -2144       C  
ATOM     47  O   LYS A  74       6.770  -2.535  77.779  1.00113.49           O  
ANISOU   47  O   LYS A  74     8946  21161  13014  -1208   3589  -2444       O  
ATOM     48  CB  LYS A  74       3.540  -2.935  77.302  1.00120.99           C  
ANISOU   48  CB  LYS A  74     9528  22015  14428  -1407   3834  -1911       C  
ATOM     49  CG  LYS A  74       2.595  -3.300  76.177  1.00124.61           C  
ANISOU   49  CG  LYS A  74     9877  22189  15280  -1594   3782  -1719       C  
ATOM     50  CD  LYS A  74       3.359  -3.540  74.883  1.00123.66           C  
ANISOU   50  CD  LYS A  74     9870  21732  15382  -1723   3560  -1788       C  
ATOM     51  CE  LYS A  74       2.501  -3.260  73.661  1.00122.97           C  
ANISOU   51  CE  LYS A  74     9712  21313  15699  -1812   3460  -1778       C  
ATOM     52  NZ  LYS A  74       2.231  -1.804  73.480  1.00122.64           N  
ANISOU   52  NZ  LYS A  74     9670  21189  15738  -1642   3438  -2101       N  
ATOM     53  N   ASN A  75       5.715  -3.379  79.589  1.00115.92           N  
ANISOU   53  N   ASN A  75     9137  21977  12928  -1140   3908  -2055       N  
ATOM     54  CA  ASN A  75       6.689  -2.778  80.496  1.00115.97           C  
ANISOU   54  CA  ASN A  75     9264  22183  12615   -922   3880  -2339       C  
ATOM     55  C   ASN A  75       8.081  -3.365  80.272  1.00115.54           C  
ANISOU   55  C   ASN A  75     9357  22094  12448   -967   3739  -2393       C  
ATOM     56  O   ASN A  75       9.075  -2.631  80.232  1.00115.03           O  
ANISOU   56  O   ASN A  75     9393  21970  12342   -850   3602  -2729       O  
ATOM     57  CB  ASN A  75       6.246  -2.959  81.949  1.00119.32           C  
ANISOU   57  CB  ASN A  75     9665  22983  12689   -772   4080  -2206       C  
ATOM     58  CG  ASN A  75       5.109  -2.026  82.331  1.00116.50           C  
ANISOU   58  CG  ASN A  75     9185  22688  12392   -649   4201  -2279       C  
ATOM     59  OD1 ASN A  75       4.490  -2.183  83.382  1.00122.26           O  
ANISOU   59  OD1 ASN A  75     9865  23690  12900   -546   4389  -2129       O  
ATOM     60  ND2 ASN A  75       4.823  -1.056  81.469  1.00110.21           N  
ANISOU   60  ND2 ASN A  75     8344  21636  11895   -655   4096  -2502       N  
ATOM     61  N   TRP A  76       8.163  -4.683  80.067  1.00119.76           N  
ANISOU   61  N   TRP A  76     9902  22645  12957  -1147   3761  -2062       N  
ATOM     62  CA  TRP A  76       9.448  -5.320  79.799  1.00120.40           C  
ANISOU   62  CA  TRP A  76    10184  22601  12961  -1186   3579  -2066       C  
ATOM     63  C   TRP A  76      10.022  -4.894  78.457  1.00108.87           C  
ANISOU   63  C   TRP A  76     8799  20729  11839  -1263   3357  -2261       C  
ATOM     64  O   TRP A  76      11.231  -4.649  78.344  1.00104.08           O  
ANISOU   64  O   TRP A  76     8343  20027  11175  -1187   3197  -2484       O  
ATOM     65  CB  TRP A  76       9.316  -6.845  79.829  1.00130.37           C  
ANISOU   65  CB  TRP A  76    11540  23817  14177  -1351   3571  -1609       C  
ATOM     66  CG  TRP A  76       9.316  -7.572  81.176  1.00142.70           C  
ANISOU   66  CG  TRP A  76    13145  25742  15332  -1269   3725  -1387       C  
ATOM     67  CD1 TRP A  76       9.454  -8.924  81.351  1.00147.90           C  
ANISOU   67  CD1 TRP A  76    13932  26375  15889  -1384   3698  -1009       C  
ATOM     68  CD2 TRP A  76       9.213  -7.014  82.504  1.00148.80           C  
ANISOU   68  CD2 TRP A  76    13856  26941  15741  -1044   3917  -1525       C  
ATOM     69  NE1 TRP A  76       9.429  -9.241  82.684  1.00153.34           N  
ANISOU   69  NE1 TRP A  76    14642  27442  16179  -1252   3870   -892       N  
ATOM     70  CE2 TRP A  76       9.283  -8.092  83.414  1.00152.89           C  
ANISOU   70  CE2 TRP A  76    14472  27672  15947  -1036   4008  -1204       C  
ATOM     71  CE3 TRP A  76       9.059  -5.718  83.011  1.00148.26           C  
ANISOU   71  CE3 TRP A  76    13704  27032  15597   -834   3984  -1874       C  
ATOM     72  CZ2 TRP A  76       9.206  -7.913  84.794  1.00152.70           C  
ANISOU   72  CZ2 TRP A  76    14435  28074  15510   -823   4200  -1231       C  
ATOM     73  CZ3 TRP A  76       8.985  -5.546  84.382  1.00148.96           C  
ANISOU   73  CZ3 TRP A  76    13838  27437  15323   -616   4107  -1888       C  
ATOM     74  CH2 TRP A  76       9.058  -6.636  85.256  1.00150.73           C  
ANISOU   74  CH2 TRP A  76    14138  27912  15220   -607   4224  -1574       C  
ATOM     75  N   SER A  77       9.184  -4.826  77.421  1.00104.36           N  
ANISOU   75  N   SER A  77     8125  19907  11621  -1409   3342  -2173       N  
ATOM     76  CA  SER A  77       9.679  -4.399  76.118  1.00 97.92           C  
ANISOU   76  CA  SER A  77     7388  18698  11118  -1467   3144  -2349       C  
ATOM     77  C   SER A  77      10.243  -2.988  76.183  1.00 97.22           C  
ANISOU   77  C   SER A  77     7277  18636  11025  -1297   3121  -2802       C  
ATOM     78  O   SER A  77      11.346  -2.724  75.689  1.00100.69           O  
ANISOU   78  O   SER A  77     7858  18877  11523  -1269   2954  -2995       O  
ATOM     79  CB  SER A  77       8.562  -4.493  75.076  1.00 94.93           C  
ANISOU   79  CB  SER A  77     6893  18075  11103  -1626   3142  -2192       C  
ATOM     80  OG  SER A  77       8.164  -5.839  74.872  1.00 93.49           O  
ANISOU   80  OG  SER A  77     6751  17800  10970  -1799   3114  -1781       O  
ATOM     81  N   ALA A  78       9.520  -2.075  76.839  1.00 94.67           N  
ANISOU   81  N   ALA A  78     6846  18484  10641  -1163   3240  -2941       N  
ATOM     82  CA  ALA A  78      10.015  -0.709  76.974  1.00 94.10           C  
ANISOU   82  CA  ALA A  78     6827  18351  10575   -987   3156  -3331       C  
ATOM     83  C   ALA A  78      11.293  -0.656  77.804  1.00102.85           C  
ANISOU   83  C   ALA A  78     8043  19646  11390   -851   3100  -3524       C  
ATOM     84  O   ALA A  78      12.215   0.105  77.484  1.00103.78           O  
ANISOU   84  O   ALA A  78     8240  19604  11587   -785   2956  -3821       O  
ATOM     85  CB  ALA A  78       8.936   0.182  77.588  1.00 97.95           C  
ANISOU   85  CB  ALA A  78     7219  18959  11039   -862   3265  -3396       C  
ATOM     86  N   LEU A  79      11.377  -1.465  78.866  1.00107.73           N  
ANISOU   86  N   LEU A  79     8670  20591  11670   -807   3207  -3353       N  
ATOM     87  CA  LEU A  79      12.562  -1.453  79.719  1.00113.36           C  
ANISOU   87  CA  LEU A  79     9495  21496  12081   -658   3144  -3534       C  
ATOM     88  C   LEU A  79      13.796  -1.947  78.970  1.00111.30           C  
ANISOU   88  C   LEU A  79     9363  21019  11908   -744   2968  -3572       C  
ATOM     89  O   LEU A  79      14.863  -1.321  79.028  1.00110.81           O  
ANISOU   89  O   LEU A  79     9369  20910  11824   -638   2840  -3881       O  
ATOM     90  CB  LEU A  79      12.313  -2.290  80.973  1.00114.29           C  
ANISOU   90  CB  LEU A  79     9621  21992  11812   -589   3296  -3300       C  
ATOM     91  CG  LEU A  79      13.293  -2.026  82.115  1.00113.35           C  
ANISOU   91  CG  LEU A  79     9616  22108  11343   -367   3239  -3521       C  
ATOM     92  CD1 LEU A  79      13.220  -0.561  82.535  1.00108.11           C  
ANISOU   92  CD1 LEU A  79     8935  21430  10712   -178   3182  -3869       C  
ATOM     93  CD2 LEU A  79      12.991  -2.933  83.295  1.00118.85           C  
ANISOU   93  CD2 LEU A  79    10343  23161  11655   -300   3395  -3249       C  
ATOM     94  N   LEU A  80      13.682  -3.090  78.289  1.00111.11           N  
ANISOU   94  N   LEU A  80     9422  20793  12000   -928   2912  -3226       N  
ATOM     95  CA  LEU A  80      14.808  -3.602  77.512  1.00 91.00           C  
ANISOU   95  CA  LEU A  80     7057  17956   9564  -1002   2700  -3210       C  
ATOM     96  C   LEU A  80      15.185  -2.637  76.394  1.00 91.50           C  
ANISOU   96  C   LEU A  80     7107  17700   9958  -1021   2588  -3484       C  
ATOM     97  O   LEU A  80      16.372  -2.476  76.071  1.00 90.97           O  
ANISOU   97  O   LEU A  80     7152  17480   9930   -987   2434  -3657       O  
ATOM     98  CB  LEU A  80      14.479  -4.987  76.952  1.00 90.37           C  
ANISOU   98  CB  LEU A  80     7065  17709   9561  -1190   2660  -2785       C  
ATOM     99  CG  LEU A  80      14.346  -6.099  78.000  1.00 92.88           C  
ANISOU   99  CG  LEU A  80     7441  18297   9550  -1184   2742  -2485       C  
ATOM    100  CD1 LEU A  80      14.131  -7.467  77.357  1.00 92.10           C  
ANISOU  100  CD1 LEU A  80     7447  17985   9562  -1377   2665  -2079       C  
ATOM    101  CD2 LEU A  80      15.563  -6.116  78.914  1.00 98.17           C  
ANISOU  101  CD2 LEU A  80     8241  19159   9899  -1018   2669  -2656       C  
ATOM    102  N   THR A  81      14.186  -1.994  75.783  1.00 92.75           N  
ANISOU  102  N   THR A  81     7128  17751  10364  -1072   2665  -3519       N  
ATOM    103  CA  THR A  81      14.467  -0.950  74.807  1.00 95.34           C  
ANISOU  103  CA  THR A  81     7437  17798  10988  -1068   2581  -3795       C  
ATOM    104  C   THR A  81      15.307   0.163  75.419  1.00 89.89           C  
ANISOU  104  C   THR A  81     6728  17230  10196   -893   2553  -4200       C  
ATOM    105  O   THR A  81      16.286   0.613  74.814  1.00 84.39           O  
ANISOU  105  O   THR A  81     6106  16307   9651   -884   2418  -4398       O  
ATOM    106  CB  THR A  81      13.154  -0.395  74.261  1.00105.83           C  
ANISOU  106  CB  THR A  81     8610  19050  12551  -1121   2684  -3779       C  
ATOM    107  OG1 THR A  81      12.636  -1.274  73.253  1.00106.67           O  
ANISOU  107  OG1 THR A  81     8762  18898  12872  -1297   2633  -3469       O  
ATOM    108  CG2 THR A  81      13.352   0.994  73.700  1.00108.54           C  
ANISOU  108  CG2 THR A  81     8994  19132  13112  -1042   2583  -4084       C  
ATOM    109  N   ALA A  82      14.942   0.612  76.622  1.00 89.68           N  
ANISOU  109  N   ALA A  82     6660  17486   9928   -747   2630  -4283       N  
ATOM    110  CA  ALA A  82      15.712   1.659  77.286  1.00 94.90           C  
ANISOU  110  CA  ALA A  82     7363  18197  10497   -573   2533  -4625       C  
ATOM    111  C   ALA A  82      17.133   1.193  77.588  1.00 94.52           C  
ANISOU  111  C   ALA A  82     7405  18220  10290   -529   2430  -4729       C  
ATOM    112  O   ALA A  82      18.087   1.977  77.499  1.00 88.63           O  
ANISOU  112  O   ALA A  82     6702  17340   9632   -459   2287  -5013       O  
ATOM    113  CB  ALA A  82      15.006   2.099  78.568  1.00 92.92           C  
ANISOU  113  CB  ALA A  82     7062  18252   9993   -416   2631  -4660       C  
ATOM    114  N   VAL A  83      17.288  -0.076  77.967  1.00 96.60           N  
ANISOU  114  N   VAL A  83     7718  18660  10325   -570   2475  -4476       N  
ATOM    115  CA  VAL A  83      18.623  -0.630  78.190  1.00 96.62           C  
ANISOU  115  CA  VAL A  83     7873  18645  10193   -534   2319  -4502       C  
ATOM    116  C   VAL A  83      19.463  -0.512  76.922  1.00 93.02           C  
ANISOU  116  C   VAL A  83     7490  17797  10057   -636   2160  -4571       C  
ATOM    117  O   VAL A  83      20.611  -0.042  76.952  1.00 85.88           O  
ANISOU  117  O   VAL A  83     6623  16828   9180   -561   2033  -4830       O  
ATOM    118  CB  VAL A  83      18.527  -2.092  78.666  1.00 90.45           C  
ANISOU  118  CB  VAL A  83     7203  18002   9160   -587   2342  -4123       C  
ATOM    119  CG1 VAL A  83      19.890  -2.763  78.603  1.00 89.45           C  
ANISOU  119  CG1 VAL A  83     7248  17781   8959   -579   2158  -4117       C  
ATOM    120  CG2 VAL A  83      17.962  -2.160  80.076  1.00 96.99           C  
ANISOU  120  CG2 VAL A  83     7980  19250   9621   -445   2495  -4090       C  
ATOM    121  N   VAL A  84      18.898  -0.937  75.787  1.00 90.27           N  
ANISOU  121  N   VAL A  84     7159  17180   9961   -802   2166  -4338       N  
ATOM    122  CA  VAL A  84      19.628  -0.871  74.521  1.00 86.27           C  
ANISOU  122  CA  VAL A  84     6734  16298   9749   -889   2031  -4374       C  
ATOM    123  C   VAL A  84      19.955   0.574  74.161  1.00 89.36           C  
ANISOU  123  C   VAL A  84     7035  16558  10359   -824   2011  -4749       C  
ATOM    124  O   VAL A  84      21.047   0.873  73.662  1.00 91.70           O  
ANISOU  124  O   VAL A  84     7387  16661  10792   -815   1892  -4909       O  
ATOM    125  CB  VAL A  84      18.831  -1.570  73.403  1.00 80.05           C  
ANISOU  125  CB  VAL A  84     5985  15257   9175  -1058   2040  -4058       C  
ATOM    126  CG1 VAL A  84      19.613  -1.550  72.098  1.00 77.30           C  
ANISOU  126  CG1 VAL A  84     5741  14528   9100  -1124   1904  -4084       C  
ATOM    127  CG2 VAL A  84      18.509  -3.000  73.798  1.00 80.97           C  
ANISOU  127  CG2 VAL A  84     6185  15493   9087  -1129   2051  -3685       C  
ATOM    128  N   ILE A  85      19.014   1.491  74.405  1.00 82.05           N  
ANISOU  128  N   ILE A  85     5966  15733   9476   -776   2130  -4892       N  
ATOM    129  CA  ILE A  85      19.231   2.904  74.093  1.00 85.43           C  
ANISOU  129  CA  ILE A  85     6386  15952  10122   -720   2050  -5181       C  
ATOM    130  C   ILE A  85      20.407   3.453  74.892  1.00 87.06           C  
ANISOU  130  C   ILE A  85     6613  16256  10208   -590   1934  -5463       C  
ATOM    131  O   ILE A  85      21.311   4.101  74.343  1.00 85.23           O  
ANISOU  131  O   ILE A  85     6411  15785  10186   -594   1815  -5652       O  
ATOM    132  CB  ILE A  85      17.948   3.714  74.354  1.00 87.04           C  
ANISOU  132  CB  ILE A  85     6525  16192  10357   -683   2124  -5194       C  
ATOM    133  CG1 ILE A  85      16.873   3.366  73.322  1.00 85.91           C  
ANISOU  133  CG1 ILE A  85     6362  15859  10421   -816   2197  -4956       C  
ATOM    134  CG2 ILE A  85      18.240   5.206  74.351  1.00 83.12           C  
ANISOU  134  CG2 ILE A  85     6030  15540  10013   -602   2021  -5502       C  
ATOM    135  CD1 ILE A  85      15.538   4.028  73.587  1.00 82.99           C  
ANISOU  135  CD1 ILE A  85     5918  15546  10070   -779   2280  -4943       C  
ATOM    136  N   ILE A  86      20.396   3.221  76.208  1.00 90.72           N  
ANISOU  136  N   ILE A  86     7061  17069  10341   -468   1964  -5490       N  
ATOM    137  CA  ILE A  86      21.456   3.743  77.066  1.00 91.94           C  
ANISOU  137  CA  ILE A  86     7233  17330  10371   -328   1834  -5762       C  
ATOM    138  C   ILE A  86      22.800   3.149  76.669  1.00 85.03           C  
ANISOU  138  C   ILE A  86     6419  16358   9529   -360   1730  -5800       C  
ATOM    139  O   ILE A  86      23.813   3.860  76.596  1.00 84.79           O  
ANISOU  139  O   ILE A  86     6390  16185   9639   -319   1586  -6043       O  
ATOM    140  CB  ILE A  86      21.134   3.472  78.548  1.00 96.25           C  
ANISOU  140  CB  ILE A  86     7773  18274  10524   -177   1889  -5746       C  
ATOM    141  CG1 ILE A  86      19.848   4.191  78.968  1.00 91.11           C  
ANISOU  141  CG1 ILE A  86     7054  17713   9853   -123   1988  -5736       C  
ATOM    142  CG2 ILE A  86      22.297   3.902  79.437  1.00 98.96           C  
ANISOU  142  CG2 ILE A  86     8145  18722  10734    -22   1728  -6018       C  
ATOM    143  CD1 ILE A  86      19.991   5.694  79.074  1.00 91.70           C  
ANISOU  143  CD1 ILE A  86     7090  17654  10097    -40   1873  -6042       C  
ATOM    144  N   LEU A  87      22.833   1.840  76.397  1.00 84.16           N  
ANISOU  144  N   LEU A  87     6373  16294   9311   -441   1778  -5530       N  
ATOM    145  CA  LEU A  87      24.084   1.207  75.988  1.00 87.96           C  
ANISOU  145  CA  LEU A  87     6970  16616   9833   -479   1628  -5485       C  
ATOM    146  C   LEU A  87      24.605   1.810  74.689  1.00 87.19           C  
ANISOU  146  C   LEU A  87     6862  16141  10124   -566   1567  -5590       C  
ATOM    147  O   LEU A  87      25.794   2.134  74.577  1.00 91.15           O  
ANISOU  147  O   LEU A  87     7371  16540  10723   -530   1449  -5788       O  
ATOM    148  CB  LEU A  87      23.888  -0.302  75.844  1.00 86.03           C  
ANISOU  148  CB  LEU A  87     6862  16384   9443   -572   1629  -5079       C  
ATOM    149  CG  LEU A  87      23.711  -1.096  77.139  1.00 86.94           C  
ANISOU  149  CG  LEU A  87     7026  16856   9152   -482   1663  -4947       C  
ATOM    150  CD1 LEU A  87      23.512  -2.574  76.838  1.00 84.08           C  
ANISOU  150  CD1 LEU A  87     6802  16446   8699   -597   1654  -4532       C  
ATOM    151  CD2 LEU A  87      24.903  -0.887  78.061  1.00 86.16           C  
ANISOU  151  CD2 LEU A  87     6953  16925   8859   -321   1538  -5210       C  
ATOM    152  N   THR A  88      23.725   1.971  73.696  1.00 86.36           N  
ANISOU  152  N   THR A  88     6738  15825  10248   -677   1650  -5458       N  
ATOM    153  CA  THR A  88      24.121   2.571  72.426  1.00 83.78           C  
ANISOU  153  CA  THR A  88     6413  15136  10282   -750   1612  -5541       C  
ATOM    154  C   THR A  88      24.732   3.947  72.639  1.00 84.64           C  
ANISOU  154  C   THR A  88     6456  15166  10537   -674   1536  -5889       C  
ATOM    155  O   THR A  88      25.858   4.220  72.198  1.00 86.46           O  
ANISOU  155  O   THR A  88     6702  15213  10934   -680   1439  -6017       O  
ATOM    156  CB  THR A  88      22.911   2.672  71.493  1.00 83.30           C  
ANISOU  156  CB  THR A  88     6339  14896  10414   -850   1711  -5374       C  
ATOM    157  OG1 THR A  88      22.479   1.360  71.112  1.00 74.74           O  
ANISOU  157  OG1 THR A  88     5366  13775   9255   -947   1711  -5000       O  
ATOM    158  CG2 THR A  88      23.261   3.468  70.245  1.00 82.90           C  
ANISOU  158  CG2 THR A  88     6311  14467  10721   -900   1671  -5475       C  
ATOM    159  N   ILE A  89      23.997   4.830  73.321  1.00 85.70           N  
ANISOU  159  N   ILE A  89     6537  15403  10621   -610   1549  -6002       N  
ATOM    160  CA  ILE A  89      24.455   6.206  73.486  1.00 86.49           C  
ANISOU  160  CA  ILE A  89     6594  15379  10890   -560   1440  -6281       C  
ATOM    161  C   ILE A  89      25.791   6.240  74.219  1.00 91.81           C  
ANISOU  161  C   ILE A  89     7244  16162  11477   -473   1307  -6481       C  
ATOM    162  O   ILE A  89      26.746   6.886  73.771  1.00 97.08           O  
ANISOU  162  O   ILE A  89     7888  16611  12386   -496   1203  -6638       O  
ATOM    163  CB  ILE A  89      23.385   7.047  74.206  1.00 83.92           C  
ANISOU  163  CB  ILE A  89     6211  15191  10484   -488   1477  -6359       C  
ATOM    164  CG1 ILE A  89      22.085   7.059  73.399  1.00 80.55           C  
ANISOU  164  CG1 ILE A  89     5801  14626  10177   -574   1594  -6170       C  
ATOM    165  CG2 ILE A  89      23.882   8.468  74.421  1.00 84.94           C  
ANISOU  165  CG2 ILE A  89     6281  15204  10788   -434   1351  -6648       C  
ATOM    166  CD1 ILE A  89      20.967   7.847  74.048  1.00 82.36           C  
ANISOU  166  CD1 ILE A  89     5972  14990  10332   -501   1640  -6232       C  
ATOM    167  N   ALA A  90      25.890   5.518  75.340  1.00 90.29           N  
ANISOU  167  N   ALA A  90     7058  16305  10941   -371   1309  -6466       N  
ATOM    168  CA  ALA A  90      27.101   5.578  76.152  1.00 88.07           C  
ANISOU  168  CA  ALA A  90     6761  16145  10555   -264   1163  -6667       C  
ATOM    169  C   ALA A  90      28.305   5.016  75.404  1.00 85.67           C  
ANISOU  169  C   ALA A  90     6494  15667  10391   -327   1096  -6655       C  
ATOM    170  O   ALA A  90      29.374   5.641  75.370  1.00 82.57           O  
ANISOU  170  O   ALA A  90     6049  15145  10179   -307    962  -6855       O  
ATOM    171  CB  ALA A  90      26.886   4.831  77.468  1.00 87.99           C  
ANISOU  171  CB  ALA A  90     6785  16527  10119   -133   1185  -6619       C  
ATOM    172  N   GLY A  91      28.157   3.833  74.801  1.00 80.75           N  
ANISOU  172  N   GLY A  91     5947  15039   9693   -401   1187  -6416       N  
ATOM    173  CA  GLY A  91      29.274   3.236  74.090  1.00 87.33           C  
ANISOU  173  CA  GLY A  91     6834  15705  10642   -450   1116  -6375       C  
ATOM    174  C   GLY A  91      29.740   4.074  72.916  1.00 84.35           C  
ANISOU  174  C   GLY A  91     6414  14959  10676   -535   1097  -6465       C  
ATOM    175  O   GLY A  91      30.946   4.245  72.698  1.00 91.11           O  
ANISOU  175  O   GLY A  91     7248  15691  11679   -528    993  -6592       O  
ATOM    176  N   ASN A  92      28.797   4.611  72.136  1.00 79.97           N  
ANISOU  176  N   ASN A  92     5861  14209  10317   -620   1185  -6372       N  
ATOM    177  CA  ASN A  92      29.217   5.387  70.978  1.00 75.01           C  
ANISOU  177  CA  ASN A  92     5230  13208  10062   -703   1162  -6412       C  
ATOM    178  C   ASN A  92      29.799   6.732  71.389  1.00 76.74           C  
ANISOU  178  C   ASN A  92     5346  13358  10454   -668   1051  -6688       C  
ATOM    179  O   ASN A  92      30.692   7.244  70.708  1.00 77.35           O  
ANISOU  179  O   ASN A  92     5393  13189  10808   -715    999  -6765       O  
ATOM    180  CB  ASN A  92      28.050   5.560  70.007  1.00 81.67           C  
ANISOU  180  CB  ASN A  92     6131  13851  11051   -791   1271  -6232       C  
ATOM    181  CG  ASN A  92      27.722   4.277  69.265  1.00 82.63           C  
ANISOU  181  CG  ASN A  92     6333  13945  11118   -849   1356  -5948       C  
ATOM    182  OD1 ASN A  92      28.438   3.878  68.346  1.00 70.28           O  
ANISOU  182  OD1 ASN A  92     4825  12174   9704   -891   1338  -5860       O  
ATOM    183  ND2 ASN A  92      26.638   3.622  69.663  1.00 90.28           N  
ANISOU  183  ND2 ASN A  92     7310  15113  11879   -856   1435  -5777       N  
ATOM    184  N   ILE A  93      29.360   7.294  72.520  1.00 78.52           N  
ANISOU  184  N   ILE A  93     5504  13807  10522   -579   1014  -6833       N  
ATOM    185  CA  ILE A  93      30.012   8.495  73.036  1.00 87.44           C  
ANISOU  185  CA  ILE A  93     6512  14905  11805   -527    889  -7100       C  
ATOM    186  C   ILE A  93      31.434   8.179  73.487  1.00 85.94           C  
ANISOU  186  C   ILE A  93     6269  14786  11599   -467    766  -7228       C  
ATOM    187  O   ILE A  93      32.356   8.981  73.291  1.00 81.38           O  
ANISOU  187  O   ILE A  93     5583  14044  11292   -478    678  -7388       O  
ATOM    188  CB  ILE A  93      29.173   9.115  74.168  1.00 82.37           C  
ANISOU  188  CB  ILE A  93     5821  14498  10978   -422    876  -7215       C  
ATOM    189  CG1 ILE A  93      27.927   9.790  73.592  1.00 81.69           C  
ANISOU  189  CG1 ILE A  93     5754  14271  11013   -485    971  -7143       C  
ATOM    190  CG2 ILE A  93      29.992  10.116  74.967  1.00 84.52           C  
ANISOU  190  CG2 ILE A  93     5963  14813  11340   -326    724  -7495       C  
ATOM    191  CD1 ILE A  93      27.046  10.444  74.631  1.00 88.38           C  
ANISOU  191  CD1 ILE A  93     6553  15337  11692   -376    968  -7251       C  
ATOM    192  N   LEU A  94      31.639   7.005  74.092  1.00 82.74           N  
ANISOU  192  N   LEU A  94     5932  14625  10881   -400    758  -7151       N  
ATOM    193  CA  LEU A  94      32.996   6.588  74.441  1.00 82.81           C  
ANISOU  193  CA  LEU A  94     5912  14688  10865   -341    633  -7252       C  
ATOM    194  C   LEU A  94      33.877   6.475  73.201  1.00 86.71           C  
ANISOU  194  C   LEU A  94     6402  14881  11663   -446    640  -7201       C  
ATOM    195  O   LEU A  94      35.034   6.911  73.209  1.00 88.44           O  
ANISOU  195  O   LEU A  94     6517  15007  12080   -426    537  -7352       O  
ATOM    196  CB  LEU A  94      32.968   5.261  75.198  1.00 84.38           C  
ANISOU  196  CB  LEU A  94     6221  15187  10654   -259    630  -7143       C  
ATOM    197  CG  LEU A  94      32.599   5.322  76.680  1.00 89.90           C  
ANISOU  197  CG  LEU A  94     6915  16220  11024   -106    576  -7235       C  
ATOM    198  CD1 LEU A  94      32.753   3.952  77.322  1.00 91.05           C  
ANISOU  198  CD1 LEU A  94     7184  16633  10778    -33    566  -7105       C  
ATOM    199  CD2 LEU A  94      33.457   6.352  77.399  1.00 87.21           C  
ANISOU  199  CD2 LEU A  94     6445  15878  10813     -3    408  -7514       C  
ATOM    200  N   VAL A  95      33.346   5.885  72.127  1.00 87.60           N  
ANISOU  200  N   VAL A  95     6622  14840  11823   -546    767  -6977       N  
ATOM    201  CA  VAL A  95      34.118   5.770  70.888  1.00 76.00           C  
ANISOU  201  CA  VAL A  95     5169  13075  10633   -632    788  -6905       C  
ATOM    202  C   VAL A  95      34.431   7.152  70.321  1.00 76.11           C  
ANISOU  202  C   VAL A  95     5071  12813  11033   -696    771  -7033       C  
ATOM    203  O   VAL A  95      35.545   7.409  69.836  1.00 82.31           O  
ANISOU  203  O   VAL A  95     5782  13427  12064   -721    730  -7099       O  
ATOM    204  CB  VAL A  95      33.367   4.895  69.868  1.00 73.74           C  
ANISOU  204  CB  VAL A  95     5023  12680  10316   -703    927  -6620       C  
ATOM    205  CG1 VAL A  95      34.086   4.902  68.526  1.00 72.01           C  
ANISOU  205  CG1 VAL A  95     4833  12130  10395   -776    956  -6529       C  
ATOM    206  CG2 VAL A  95      33.233   3.480  70.392  1.00 73.77           C  
ANISOU  206  CG2 VAL A  95     5139  12923   9966   -662    907  -6424       C  
ATOM    207  N   ILE A  96      33.448   8.056  70.361  1.00 76.42           N  
ANISOU  207  N   ILE A  96     5094  12808  11136   -722    810  -7060       N  
ATOM    208  CA  ILE A  96      33.656   9.425  69.896  1.00 76.75           C  
ANISOU  208  CA  ILE A  96     5027  12607  11528   -778    795  -7181       C  
ATOM    209  C   ILE A  96      34.795  10.076  70.667  1.00102.89           C  
ANISOU  209  C   ILE A  96     8143  15993  14959   -698    675  -7422       C  
ATOM    210  O   ILE A  96      35.693  10.691  70.082  1.00105.73           O  
ANISOU  210  O   ILE A  96     8459  16105  15606   -712    682  -7441       O  
ATOM    211  CB  ILE A  96      32.356  10.239  70.029  1.00 77.09           C  
ANISOU  211  CB  ILE A  96     5083  12648  11561   -788    839  -7188       C  
ATOM    212  CG1 ILE A  96      31.301   9.734  69.047  1.00 78.98           C  
ANISOU  212  CG1 ILE A  96     5495  12744  11770   -865    966  -6940       C  
ATOM    213  CG2 ILE A  96      32.625  11.719  69.806  1.00 77.97           C  
ANISOU  213  CG2 ILE A  96     5052  12567  12007   -816    806  -7344       C  
ATOM    214  CD1 ILE A  96      29.892  10.166  69.400  1.00 75.46           C  
ANISOU  214  CD1 ILE A  96     5070  12389  11210   -847   1014  -6924       C  
ATOM    215  N   MET A  97      34.770   9.951  71.996  1.00 93.93           N  
ANISOU  215  N   MET A  97     6967  15159  13563   -571    583  -7555       N  
ATOM    216  CA  MET A  97      35.818  10.543  72.823  1.00 92.10           C  
ANISOU  216  CA  MET A  97     6570  15003  13421   -461    455  -7788       C  
ATOM    217  C   MET A  97      37.178   9.930  72.513  1.00 94.42           C  
ANISOU  217  C   MET A  97     6831  15232  13812   -449    421  -7786       C  
ATOM    218  O   MET A  97      38.189  10.642  72.442  1.00 94.75           O  
ANISOU  218  O   MET A  97     6727  15143  14132   -412    386  -7926       O  
ATOM    219  CB  MET A  97      35.477  10.362  74.302  1.00 95.70           C  
ANISOU  219  CB  MET A  97     7039  15799  13524   -314    356  -7903       C  
ATOM    220  CG  MET A  97      34.331  11.229  74.793  1.00100.30           C  
ANISOU  220  CG  MET A  97     7609  16453  14046   -282    371  -7969       C  
ATOM    221  SD  MET A  97      33.994  10.988  76.548  1.00108.10           S  
ANISOU  221  SD  MET A  97     8623  17849  14603    -82    266  -8094       S  
ATOM    222  CE  MET A  97      35.588  11.391  77.260  1.00112.41           C  
ANISOU  222  CE  MET A  97     9022  18409  15281     45     75  -8343       C  
ATOM    223  N   ALA A  98      37.218   8.611  72.307  1.00 96.18           N  
ANISOU  223  N   ALA A  98     7196  15539  13811   -468    442  -7624       N  
ATOM    224  CA  ALA A  98      38.484   7.942  72.029  1.00100.77           C  
ANISOU  224  CA  ALA A  98     7765  16071  14451   -446    401  -7615       C  
ATOM    225  C   ALA A  98      39.091   8.433  70.723  1.00102.64           C  
ANISOU  225  C   ALA A  98     7976  15950  15072   -531    502  -7549       C  
ATOM    226  O   ALA A  98      40.299   8.692  70.650  1.00107.54           O  
ANISOU  226  O   ALA A  98     8535  16450  15875   -479    468  -7636       O  
ATOM    227  CB  ALA A  98      38.282   6.428  71.993  1.00104.17           C  
ANISOU  227  CB  ALA A  98     8380  16648  14551   -451    407  -7433       C  
ATOM    228  N   VAL A  99      38.272   8.566  69.678  1.00101.04           N  
ANISOU  228  N   VAL A  99     7910  15526  14955   -648    622  -7355       N  
ATOM    229  CA  VAL A  99      38.811   9.034  68.403  1.00 93.85           C  
ANISOU  229  CA  VAL A  99     7079  14233  14347   -708    720  -7226       C  
ATOM    230  C   VAL A  99      39.143  10.522  68.469  1.00 85.73           C  
ANISOU  230  C   VAL A  99     5951  13029  13593   -675    729  -7359       C  
ATOM    231  O   VAL A  99      40.108  10.978  67.844  1.00 78.67           O  
ANISOU  231  O   VAL A  99     5063  11882  12945   -668    773  -7368       O  
ATOM    232  CB  VAL A  99      37.835   8.723  67.253  1.00 74.51           C  
ANISOU  232  CB  VAL A  99     4823  11590  11896   -836    819  -6995       C  
ATOM    233  CG1 VAL A  99      38.366   9.277  65.935  1.00 73.58           C  
ANISOU  233  CG1 VAL A  99     4825  11066  12066   -883    916  -6891       C  
ATOM    234  CG2 VAL A  99      37.606   7.225  67.147  1.00 73.12           C  
ANISOU  234  CG2 VAL A  99     4739  11575  11468   -846    825  -6885       C  
ATOM    235  N   SER A 100      38.377  11.299  69.240  1.00 84.37           N  
ANISOU  235  N   SER A 100     5690  12987  13382   -654    681  -7487       N  
ATOM    236  CA  SER A 100      38.579  12.741  69.287  1.00 86.07           C  
ANISOU  236  CA  SER A 100     5805  13038  13860   -627    682  -7615       C  
ATOM    237  C   SER A 100      39.797  13.136  70.111  1.00 92.59           C  
ANISOU  237  C   SER A 100     6466  13927  14788   -514    572  -7860       C  
ATOM    238  O   SER A 100      40.393  14.189  69.855  1.00 94.50           O  
ANISOU  238  O   SER A 100     6638  13950  15317   -501    587  -7946       O  
ATOM    239  CB  SER A 100      37.331  13.425  69.848  1.00 82.45           C  
ANISOU  239  CB  SER A 100     5304  12705  13320   -629    658  -7688       C  
ATOM    240  OG  SER A 100      36.179  13.087  69.096  1.00 79.75           O  
ANISOU  240  OG  SER A 100     5113  12293  12895   -732    750  -7482       O  
ATOM    241  N   LEU A 101      40.184  12.326  71.095  1.00 94.41           N  
ANISOU  241  N   LEU A 101     6625  14450  14795   -427    456  -7981       N  
ATOM    242  CA  LEU A 101      41.265  12.710  71.995  1.00 97.17           C  
ANISOU  242  CA  LEU A 101     6804  14885  15231   -302    324  -8238       C  
ATOM    243  C   LEU A 101      42.594  12.041  71.670  1.00105.59           C  
ANISOU  243  C   LEU A 101     7877  15868  16374   -282    309  -8233       C  
ATOM    244  O   LEU A 101      43.638  12.699  71.714  1.00111.10           O  
ANISOU  244  O   LEU A 101     8470  16418  17324   -236    268  -8383       O  
ATOM    245  CB  LEU A 101      40.880  12.388  73.442  1.00 90.99           C  
ANISOU  245  CB  LEU A 101     5911  14506  14155   -181    178  -8418       C  
ATOM    246  CG  LEU A 101      39.669  13.140  73.998  1.00 89.45           C  
ANISOU  246  CG  LEU A 101     5685  14428  13873   -170    160  -8485       C  
ATOM    247  CD1 LEU A 101      39.265  12.585  75.356  1.00 90.90           C  
ANISOU  247  CD1 LEU A 101     5931  14962  13647    -54     18  -8555       C  
ATOM    248  CD2 LEU A 101      39.960  14.629  74.087  1.00 91.29           C  
ANISOU  248  CD2 LEU A 101     5782  14483  14420   -129    130  -8667       C  
ATOM    249  N   GLU A 102      42.585  10.752  71.344  1.00105.01           N  
ANISOU  249  N   GLU A 102     7916  15886  16098   -315    334  -8075       N  
ATOM    250  CA  GLU A 102      43.820  10.012  71.112  1.00107.87           C  
ANISOU  250  CA  GLU A 102     8277  16209  16501   -287    301  -8083       C  
ATOM    251  C   GLU A 102      44.373  10.298  69.720  1.00112.47           C  
ANISOU  251  C   GLU A 102     8952  16406  17375   -388    432  -7944       C  
ATOM    252  O   GLU A 102      43.675  10.104  68.718  1.00109.63           O  
ANISOU  252  O   GLU A 102     8750  15893  17013   -493    558  -7721       O  
ATOM    253  CB  GLU A 102      43.576   8.513  71.280  1.00104.48           C  
ANISOU  253  CB  GLU A 102     7934  16028  15735   -281    267  -7961       C  
ATOM    254  CG  GLU A 102      43.102   8.099  72.661  1.00104.64           C  
ANISOU  254  CG  GLU A 102     7951  16409  15400   -193    108  -8035       C  
ATOM    255  CD  GLU A 102      44.084   8.473  73.753  1.00109.10           C  
ANISOU  255  CD  GLU A 102     8391  17080  15981    -54    -71  -8270       C  
ATOM    256  OE1 GLU A 102      45.307   8.407  73.506  1.00110.57           O  
ANISOU  256  OE1 GLU A 102     8525  17140  16347    -29   -111  -8325       O  
ATOM    257  OE2 GLU A 102      43.632   8.833  74.861  1.00111.99           O  
ANISOU  257  OE2 GLU A 102     8721  17651  16178     37   -176  -8399       O  
ATOM    258  N   LYS A 103      45.626  10.756  69.654  1.00120.86           N  
ANISOU  258  N   LYS A 103     9913  17315  18695   -353    399  -8082       N  
ATOM    259  CA  LYS A 103      46.289  10.934  68.367  1.00115.21           C  
ANISOU  259  CA  LYS A 103     9265  16256  18253   -444    517  -7962       C  
ATOM    260  C   LYS A 103      46.810   9.619  67.805  1.00 98.02           C  
ANISOU  260  C   LYS A 103     7175  14101  15965   -468    527  -7834       C  
ATOM    261  O   LYS A 103      47.156   9.561  66.621  1.00 97.54           O  
ANISOU  261  O   LYS A 103     7202  13779  16079   -559    631  -7666       O  
ATOM    262  CB  LYS A 103      47.433  11.949  68.452  1.00120.60           C  
ANISOU  262  CB  LYS A 103     9790  16750  19285   -411    488  -8158       C  
ATOM    263  CG  LYS A 103      47.020  13.335  68.919  1.00123.12           C  
ANISOU  263  CG  LYS A 103    10005  17013  19761   -385    474  -8297       C  
ATOM    264  CD  LYS A 103      48.198  14.295  68.857  1.00124.24           C  
ANISOU  264  CD  LYS A 103     9991  16931  20285   -365    455  -8476       C  
ATOM    265  CE  LYS A 103      47.809  15.690  69.319  1.00125.41           C  
ANISOU  265  CE  LYS A 103    10023  17021  20605   -333    427  -8626       C  
ATOM    266  NZ  LYS A 103      48.958  16.635  69.246  1.00128.48           N  
ANISOU  266  NZ  LYS A 103    10248  17178  21392   -315    406  -8805       N  
ATOM    267  N   LYS A 104      46.870   8.572  68.629  1.00 92.70           N  
ANISOU  267  N   LYS A 104     6491  13737  14993   -400    394  -7846       N  
ATOM    268  CA  LYS A 104      47.237   7.241  68.171  1.00 81.89           C  
ANISOU  268  CA  LYS A 104     5217  12428  13469   -429    366  -7657       C  
ATOM    269  C   LYS A 104      46.138   6.603  67.333  1.00 94.29           C  
ANISOU  269  C   LYS A 104     6960  13968  14895   -519    478  -7406       C  
ATOM    270  O   LYS A 104      46.372   5.558  66.717  1.00 80.46           O  
ANISOU  270  O   LYS A 104     5290  12221  13061   -551    478  -7207       O  
ATOM    271  CB  LYS A 104      47.544   6.371  69.392  1.00 83.02           C  
ANISOU  271  CB  LYS A 104     5302  12923  13319   -317    176  -7750       C  
ATOM    272  CG  LYS A 104      48.369   5.120  69.148  1.00 98.07           C  
ANISOU  272  CG  LYS A 104     7245  14902  15115   -304     94  -7628       C  
ATOM    273  CD  LYS A 104      48.580   4.391  70.467  1.00102.02           C  
ANISOU  273  CD  LYS A 104     7712  15747  15303   -180   -107  -7736       C  
ATOM    274  CE  LYS A 104      49.447   3.156  70.314  1.00105.41           C  
ANISOU  274  CE  LYS A 104     8175  16262  15612   -146   -211  -7634       C  
ATOM    275  NZ  LYS A 104      49.627   2.461  71.619  1.00109.76           N  
ANISOU  275  NZ  LYS A 104     8737  17134  15834    -13   -415  -7728       N  
ATOM    276  N   LEU A 105      44.953   7.212  67.302  1.00 99.01           N  
ANISOU  276  N   LEU A 105     7605  14540  15473   -551    569  -7410       N  
ATOM    277  CA  LEU A 105      43.795   6.691  66.587  1.00 97.85           C  
ANISOU  277  CA  LEU A 105     7620  14364  15195   -636    663  -7188       C  
ATOM    278  C   LEU A 105      43.302   7.704  65.558  1.00102.45           C  
ANISOU  278  C   LEU A 105     8287  14613  16027   -725    804  -7089       C  
ATOM    279  O   LEU A 105      42.101   7.980  65.491  1.00104.82           O  
ANISOU  279  O   LEU A 105     8662  14917  16247   -767    851  -7004       O  
ATOM    280  CB  LEU A 105      42.673   6.343  67.567  1.00 97.85           C  
ANISOU  280  CB  LEU A 105     7612  14681  14885   -602    613  -7223       C  
ATOM    281  CG  LEU A 105      42.908   5.186  68.542  1.00 97.86           C  
ANISOU  281  CG  LEU A 105     7580  15033  14569   -534    457  -7237       C  
ATOM    282  CD1 LEU A 105      41.745   5.049  69.516  1.00 96.30           C  
ANISOU  282  CD1 LEU A 105     7393  15119  14077   -515    413  -7268       C  
ATOM    283  CD2 LEU A 105      43.134   3.885  67.790  1.00 96.98           C  
ANISOU  283  CD2 LEU A 105     7581  14909  14357   -585    444  -6997       C  
ATOM    284  N   GLN A 106      44.203   8.284  64.768  1.00101.53           N  
ANISOU  284  N   GLN A 106     8153  14213  16211   -753    868  -7086       N  
ATOM    285  CA  GLN A 106      43.846   9.393  63.884  1.00 94.26           C  
ANISOU  285  CA  GLN A 106     7288  12986  15539   -821    990  -6995       C  
ATOM    286  C   GLN A 106      44.239   9.105  62.440  1.00 82.75           C  
ANISOU  286  C   GLN A 106     5934  11250  14258   -890   1109  -6802       C  
ATOM    287  O   GLN A 106      44.847   9.931  61.756  1.00 80.26           O  
ANISOU  287  O   GLN A 106     5594  10669  14233   -919   1192  -6792       O  
ATOM    288  CB  GLN A 106      44.484  10.689  64.371  1.00 98.49           C  
ANISOU  288  CB  GLN A 106     7674  13434  16315   -781    969  -7192       C  
ATOM    289  CG  GLN A 106      43.962  11.155  65.716  1.00108.68           C  
ANISOU  289  CG  GLN A 106     8855  14976  17464   -704    865  -7377       C  
ATOM    290  CD  GLN A 106      44.287  12.605  66.001  1.00126.26           C  
ANISOU  290  CD  GLN A 106    10944  17071  19958   -676    862  -7542       C  
ATOM    291  OE1 GLN A 106      45.281  13.134  65.508  1.00136.10           O  
ANISOU  291  OE1 GLN A 106    12130  18092  21490   -690    900  -7586       O  
ATOM    292  NE2 GLN A 106      43.463  13.250  66.820  1.00130.37           N  
ANISOU  292  NE2 GLN A 106    11398  17739  20396   -634    814  -7641       N  
ATOM    293  N   ASN A 107      43.900   7.916  61.958  1.00 72.24           N  
ANISOU  293  N   ASN A 107     4710   9997  12741   -906   1114  -6568       N  
ATOM    294  CA  ASN A 107      43.999   7.612  60.543  1.00 70.71           C  
ANISOU  294  CA  ASN A 107     4630   9571  12665   -947   1234  -6289       C  
ATOM    295  C   ASN A 107      42.604   7.679  59.919  1.00 73.06           C  
ANISOU  295  C   ASN A 107     5077   9782  12900   -993   1315  -6134       C  
ATOM    296  O   ASN A 107      41.626   8.066  60.566  1.00 81.59           O  
ANISOU  296  O   ASN A 107     6160  10965  13876  -1008   1282  -6251       O  
ATOM    297  CB  ASN A 107      44.677   6.256  60.335  1.00 70.01           C  
ANISOU  297  CB  ASN A 107     4549   9608  12443   -896   1195  -6126       C  
ATOM    298  CG  ASN A 107      44.084   5.163  61.198  1.00 74.70           C  
ANISOU  298  CG  ASN A 107     5152  10529  12700   -851   1086  -6128       C  
ATOM    299  OD1 ASN A 107      42.917   5.220  61.585  1.00 84.03           O  
ANISOU  299  OD1 ASN A 107     6384  11811  13733   -870   1082  -6144       O  
ATOM    300  ND2 ASN A 107      44.892   4.157  61.509  1.00 80.42           N  
ANISOU  300  ND2 ASN A 107     5821  11429  13307   -788    999  -6109       N  
ATOM    301  N   ALA A 108      42.505   7.294  58.644  1.00 67.42           N  
ANISOU  301  N   ALA A 108     4485   8883  12249  -1004   1423  -5867       N  
ATOM    302  CA  ALA A 108      41.232   7.392  57.935  1.00 65.84           C  
ANISOU  302  CA  ALA A 108     4427   8571  12019  -1037   1501  -5710       C  
ATOM    303  C   ALA A 108      40.198   6.429  58.508  1.00 64.78           C  
ANISOU  303  C   ALA A 108     4346   8690  11580  -1009   1437  -5656       C  
ATOM    304  O   ALA A 108      39.029   6.798  58.691  1.00 64.39           O  
ANISOU  304  O   ALA A 108     4337   8659  11468  -1043   1442  -5676       O  
ATOM    305  CB  ALA A 108      41.442   7.132  56.445  1.00 64.63           C  
ANISOU  305  CB  ALA A 108     4395   8174  11989  -1022   1629  -5440       C  
ATOM    306  N   THR A 109      40.609   5.189  58.788  1.00 65.95           N  
ANISOU  306  N   THR A 109     4485   9034  11541   -946   1380  -5584       N  
ATOM    307  CA  THR A 109      39.670   4.187  59.282  1.00 63.54           C  
ANISOU  307  CA  THR A 109     4226   8965  10952   -918   1334  -5513       C  
ATOM    308  C   THR A 109      39.052   4.616  60.607  1.00 69.10           C  
ANISOU  308  C   THR A 109     4837   9898  11518   -942   1252  -5727       C  
ATOM    309  O   THR A 109      37.857   4.403  60.840  1.00 70.00           O  
ANISOU  309  O   THR A 109     5003  10114  11479   -954   1263  -5675       O  
ATOM    310  CB  THR A 109      40.373   2.835  59.426  1.00 65.66           C  
ANISOU  310  CB  THR A 109     4477   9411  11060   -843   1277  -5429       C  
ATOM    311  OG1 THR A 109      40.854   2.407  58.146  1.00 65.15           O  
ANISOU  311  OG1 THR A 109     4515   9133  11106   -797   1363  -5225       O  
ATOM    312  CG2 THR A 109      39.413   1.786  59.971  1.00 68.79           C  
ANISOU  312  CG2 THR A 109     4995  10017  11124   -827   1196  -5302       C  
ATOM    313  N   ASN A 110      39.842   5.241  61.482  1.00 66.48           N  
ANISOU  313  N   ASN A 110     4365   9650  11244   -939   1174  -5973       N  
ATOM    314  CA  ASN A 110      39.301   5.682  62.763  1.00 67.78           C  
ANISOU  314  CA  ASN A 110     4437  10042  11273   -937   1096  -6198       C  
ATOM    315  C   ASN A 110      38.365   6.874  62.604  1.00 75.26           C  
ANISOU  315  C   ASN A 110     5412  10838  12345   -998   1150  -6268       C  
ATOM    316  O   ASN A 110      37.386   6.989  63.350  1.00 75.16           O  
ANISOU  316  O   ASN A 110     5376  11007  12173  -1004   1119  -6337       O  
ATOM    317  CB  ASN A 110      40.433   6.008  63.734  1.00 74.98           C  
ANISOU  317  CB  ASN A 110     5194  11080  12215   -889    990  -6463       C  
ATOM    318  CG  ASN A 110      40.917   4.785  64.488  1.00 78.75           C  
ANISOU  318  CG  ASN A 110     5611  11862  12447   -822    882  -6459       C  
ATOM    319  OD1 ASN A 110      40.117   4.015  65.021  1.00 80.13           O  
ANISOU  319  OD1 ASN A 110     5803  12283  12359   -805    856  -6397       O  
ATOM    320  ND2 ASN A 110      42.230   4.597  64.534  1.00 86.20           N  
ANISOU  320  ND2 ASN A 110     6480  12794  13479   -780    820  -6521       N  
ATOM    321  N   TYR A 111      38.645   7.773  61.657  1.00 73.54           N  
ANISOU  321  N   TYR A 111     5233  10303  12406  -1040   1229  -6240       N  
ATOM    322  CA  TYR A 111      37.686   8.832  61.355  1.00 73.16           C  
ANISOU  322  CA  TYR A 111     5225  10113  12458  -1075   1285  -6192       C  
ATOM    323  C   TYR A 111      36.364   8.242  60.881  1.00 66.27           C  
ANISOU  323  C   TYR A 111     4470   9251  11459  -1111   1330  -6033       C  
ATOM    324  O   TYR A 111      35.285   8.685  61.302  1.00 66.05           O  
ANISOU  324  O   TYR A 111     4435   9305  11357  -1124   1322  -6061       O  
ATOM    325  CB  TYR A 111      38.256   9.782  60.300  1.00 82.93           C  
ANISOU  325  CB  TYR A 111     6493  11018  13999  -1097   1375  -6115       C  
ATOM    326  CG  TYR A 111      39.524  10.494  60.715  1.00 93.57           C  
ANISOU  326  CG  TYR A 111     7715  12322  15515  -1062   1348  -6284       C  
ATOM    327  CD1 TYR A 111      39.754  10.831  62.043  1.00 95.90           C  
ANISOU  327  CD1 TYR A 111     7876  12835  15728  -1006   1245  -6511       C  
ATOM    328  CD2 TYR A 111      40.489  10.836  59.776  1.00 96.27           C  
ANISOU  328  CD2 TYR A 111     8065  12404  16111  -1077   1431  -6221       C  
ATOM    329  CE1 TYR A 111      40.913  11.484  62.424  1.00 94.97           C  
ANISOU  329  CE1 TYR A 111     7626  12672  15787   -959   1221  -6679       C  
ATOM    330  CE2 TYR A 111      41.649  11.487  60.146  1.00 94.78           C  
ANISOU  330  CE2 TYR A 111     7744  12166  16102  -1046   1413  -6386       C  
ATOM    331  CZ  TYR A 111      41.857  11.809  61.470  1.00 90.68           C  
ANISOU  331  CZ  TYR A 111     7085  11860  15509   -985   1304  -6619       C  
ATOM    332  OH  TYR A 111      43.012  12.459  61.840  1.00 83.40           O  
ANISOU  332  OH  TYR A 111     6013  10884  14790   -946   1281  -6794       O  
ATOM    333  N   PHE A 112      36.432   7.237  60.004  1.00 66.68           N  
ANISOU  333  N   PHE A 112     4635   9232  11470  -1089   1383  -5803       N  
ATOM    334  CA  PHE A 112      35.217   6.566  59.552  1.00 62.79           C  
ANISOU  334  CA  PHE A 112     4265   8753  10840  -1081   1430  -5602       C  
ATOM    335  C   PHE A 112      34.486   5.906  60.714  1.00 63.19           C  
ANISOU  335  C   PHE A 112     4270   9137  10604  -1058   1370  -5651       C  
ATOM    336  O   PHE A 112      33.256   5.970  60.799  1.00 62.83           O  
ANISOU  336  O   PHE A 112     4264   9134  10474  -1074   1395  -5606       O  
ATOM    337  CB  PHE A 112      35.554   5.524  58.488  1.00 61.29           C  
ANISOU  337  CB  PHE A 112     4192   8449  10647  -1035   1484  -5359       C  
ATOM    338  CG  PHE A 112      35.622   6.068  57.090  1.00 60.45           C  
ANISOU  338  CG  PHE A 112     4189   8004  10776  -1047   1580  -5220       C  
ATOM    339  CD1 PHE A 112      34.473   6.197  56.328  1.00 59.33           C  
ANISOU  339  CD1 PHE A 112     4164   7722  10658  -1054   1636  -5084       C  
ATOM    340  CD2 PHE A 112      36.836   6.425  56.528  1.00 82.58           C  
ANISOU  340  CD2 PHE A 112     6967  10637  13771  -1045   1617  -5217       C  
ATOM    341  CE1 PHE A 112      34.531   6.687  55.038  1.00 58.67           C  
ANISOU  341  CE1 PHE A 112     4177   7343  10771  -1051   1722  -4941       C  
ATOM    342  CE2 PHE A 112      36.901   6.915  55.238  1.00 82.99           C  
ANISOU  342  CE2 PHE A 112     7113  10396  14025  -1050   1720  -5067       C  
ATOM    343  CZ  PHE A 112      35.747   7.046  54.492  1.00 79.67           C  
ANISOU  343  CZ  PHE A 112     6815   9848  13609  -1049   1770  -4925       C  
ATOM    344  N   LEU A 113      35.229   5.270  61.623  1.00 64.08           N  
ANISOU  344  N   LEU A 113     4290   9495  10563  -1018   1294  -5741       N  
ATOM    345  CA  LEU A 113      34.603   4.610  62.765  1.00 64.69           C  
ANISOU  345  CA  LEU A 113     4314   9912  10352   -991   1246  -5778       C  
ATOM    346  C   LEU A 113      33.969   5.611  63.722  1.00 78.00           C  
ANISOU  346  C   LEU A 113     5914  11718  12004  -1006   1215  -5986       C  
ATOM    347  O   LEU A 113      32.926   5.321  64.316  1.00 74.10           O  
ANISOU  347  O   LEU A 113     5423  11421  11311   -997   1228  -5955       O  
ATOM    348  CB  LEU A 113      35.626   3.750  63.507  1.00 75.30           C  
ANISOU  348  CB  LEU A 113     5572  11495  11545   -935   1163  -5839       C  
ATOM    349  CG  LEU A 113      36.158   2.500  62.800  1.00 69.90           C  
ANISOU  349  CG  LEU A 113     5044  10736  10779   -914   1128  -5568       C  
ATOM    350  CD1 LEU A 113      37.056   1.701  63.731  1.00 65.26           C  
ANISOU  350  CD1 LEU A 113     4436  10383   9977   -859    991  -5605       C  
ATOM    351  CD2 LEU A 113      35.013   1.639  62.295  1.00 62.79           C  
ANISOU  351  CD2 LEU A 113     4335   9798   9722   -936   1147  -5275       C  
ATOM    352  N   MET A 114      34.564   6.795  63.878  1.00 77.44           N  
ANISOU  352  N   MET A 114     5756  11534  12134  -1028   1175  -6193       N  
ATOM    353  CA  MET A 114      33.949   7.801  64.737  1.00 78.76           C  
ANISOU  353  CA  MET A 114     5820  11810  12294  -1041   1132  -6389       C  
ATOM    354  C   MET A 114      32.694   8.378  64.097  1.00 81.07           C  
ANISOU  354  C   MET A 114     6196  11942  12666  -1087   1209  -6285       C  
ATOM    355  O   MET A 114      31.700   8.629  64.787  1.00 84.95           O  
ANISOU  355  O   MET A 114     6653  12600  13022  -1074   1204  -6334       O  
ATOM    356  CB  MET A 114      34.939   8.914  65.067  1.00 86.31           C  
ANISOU  356  CB  MET A 114     6652  12686  13455  -1025   1072  -6578       C  
ATOM    357  CG  MET A 114      34.388   9.914  66.078  1.00 91.95           C  
ANISOU  357  CG  MET A 114     7237  13553  14147   -996   1019  -6752       C  
ATOM    358  SD  MET A 114      35.429  11.360  66.344  1.00 98.58           S  
ANISOU  358  SD  MET A 114     7931  14260  15265   -947    974  -6912       S  
ATOM    359  CE  MET A 114      35.486  12.044  64.694  1.00 92.04           C  
ANISOU  359  CE  MET A 114     7237  12993  14740  -1020   1095  -6711       C  
ATOM    360  N   SER A 115      32.724   8.617  62.783  1.00 83.29           N  
ANISOU  360  N   SER A 115     6581  11904  13160  -1131   1282  -6142       N  
ATOM    361  CA  SER A 115      31.500   9.008  62.089  1.00 65.54           C  
ANISOU  361  CA  SER A 115     4422   9507  10972  -1162   1350  -6021       C  
ATOM    362  C   SER A 115      30.429   7.934  62.242  1.00 72.16           C  
ANISOU  362  C   SER A 115     5342  10515  11560  -1130   1386  -5859       C  
ATOM    363  O   SER A 115      29.245   8.238  62.438  1.00 64.85           O  
ANISOU  363  O   SER A 115     4421   9641  10577  -1136   1408  -5853       O  
ATOM    364  CB  SER A 115      31.798   9.273  60.614  1.00 64.22           C  
ANISOU  364  CB  SER A 115     4357   8991  11054  -1195   1423  -5865       C  
ATOM    365  OG  SER A 115      30.623   9.636  59.912  1.00 71.24           O  
ANISOU  365  OG  SER A 115     5325   9740  12004  -1216   1479  -5750       O  
ATOM    366  N   LEU A 116      30.840   6.668  62.180  1.00 66.91           N  
ANISOU  366  N   LEU A 116     4719   9948  10754  -1098   1390  -5727       N  
ATOM    367  CA  LEU A 116      29.929   5.555  62.415  1.00 65.79           C  
ANISOU  367  CA  LEU A 116     4613   9998  10385  -1083   1419  -5567       C  
ATOM    368  C   LEU A 116      29.328   5.622  63.814  1.00 66.32           C  
ANISOU  368  C   LEU A 116     4577  10396  10226  -1062   1390  -5692       C  
ATOM    369  O   LEU A 116      28.125   5.397  64.002  1.00 65.05           O  
ANISOU  369  O   LEU A 116     4426  10338   9950  -1071   1434  -5604       O  
ATOM    370  CB  LEU A 116      30.694   4.245  62.222  1.00 67.20           C  
ANISOU  370  CB  LEU A 116     4815  10250  10468  -1059   1406  -5430       C  
ATOM    371  CG  LEU A 116      29.954   2.916  62.255  1.00 69.56           C  
ANISOU  371  CG  LEU A 116     5220  10669  10539  -1072   1382  -5166       C  
ATOM    372  CD1 LEU A 116      29.090   2.836  61.032  1.00 76.67           C  
ANISOU  372  CD1 LEU A 116     6246  11313  11571  -1100   1434  -4974       C  
ATOM    373  CD2 LEU A 116      30.935   1.758  62.296  1.00 66.20           C  
ANISOU  373  CD2 LEU A 116     4889  10292   9970  -1048   1285  -5019       C  
ATOM    374  N   ALA A 117      30.161   5.929  64.810  1.00 69.19           N  
ANISOU  374  N   ALA A 117     4832  10931  10525  -1028   1315  -5899       N  
ATOM    375  CA  ALA A 117      29.692   5.986  66.189  1.00 71.17           C  
ANISOU  375  CA  ALA A 117     4989  11513  10541   -982   1285  -6027       C  
ATOM    376  C   ALA A 117      28.729   7.145  66.404  1.00 75.14           C  
ANISOU  376  C   ALA A 117     5459  11980  11111   -994   1297  -6130       C  
ATOM    377  O   ALA A 117      27.742   7.006  67.132  1.00 75.10           O  
ANISOU  377  O   ALA A 117     5428  12196  10910   -965   1327  -6115       O  
ATOM    378  CB  ALA A 117      30.881   6.093  67.142  1.00 69.91           C  
ANISOU  378  CB  ALA A 117     4721  11526  10316   -926   1183  -6242       C  
ATOM    379  N   ILE A 118      28.988   8.294  65.776  1.00 76.06           N  
ANISOU  379  N   ILE A 118     5567  11828  11504  -1034   1279  -6226       N  
ATOM    380  CA  ILE A 118      28.046   9.405  65.904  1.00 78.93           C  
ANISOU  380  CA  ILE A 118     5895  12150  11946  -1043   1286  -6314       C  
ATOM    381  C   ILE A 118      26.737   9.074  65.191  1.00 81.70           C  
ANISOU  381  C   ILE A 118     6354  12412  12277  -1066   1378  -6112       C  
ATOM    382  O   ILE A 118      25.657   9.482  65.633  1.00 81.62           O  
ANISOU  382  O   ILE A 118     6314  12507  12190  -1049   1399  -6141       O  
ATOM    383  CB  ILE A 118      28.655  10.737  65.409  1.00 76.64           C  
ANISOU  383  CB  ILE A 118     5543  11606  11973  -1088   1246  -6453       C  
ATOM    384  CG1 ILE A 118      28.584  10.878  63.887  1.00 71.88           C  
ANISOU  384  CG1 ILE A 118     5060  10646  11605  -1152   1315  -6284       C  
ATOM    385  CG2 ILE A 118      30.064  10.928  65.919  1.00 75.63           C  
ANISOU  385  CG2 ILE A 118     5291  11529  11915  -1075   1160  -6624       C  
ATOM    386  CD1 ILE A 118      27.372  11.640  63.396  1.00 67.85           C  
ANISOU  386  CD1 ILE A 118     4583  10006  11189  -1173   1358  -6242       C  
ATOM    387  N   ALA A 119      26.809   8.349  64.069  1.00 84.66           N  
ANISOU  387  N   ALA A 119     6847  12591  12728  -1098   1429  -5908       N  
ATOM    388  CA  ALA A 119      25.589   7.915  63.393  1.00 76.20           C  
ANISOU  388  CA  ALA A 119     5862  11446  11645  -1113   1502  -5715       C  
ATOM    389  C   ALA A 119      24.765   7.007  64.298  1.00 77.88           C  
ANISOU  389  C   ALA A 119     6027  11982  11580  -1092   1533  -5630       C  
ATOM    390  O   ALA A 119      23.544   7.167  64.418  1.00 83.18           O  
ANISOU  390  O   ALA A 119     6686  12711  12209  -1093   1576  -5586       O  
ATOM    391  CB  ALA A 119      25.935   7.207  62.083  1.00 66.68           C  
ANISOU  391  CB  ALA A 119     4779   9994  10564  -1134   1536  -5518       C  
ATOM    392  N   ASP A 120      25.426   6.050  64.951  1.00 73.02           N  
ANISOU  392  N   ASP A 120     5375  11592  10778  -1073   1514  -5602       N  
ATOM    393  CA  ASP A 120      24.720   5.161  65.869  1.00 75.31           C  
ANISOU  393  CA  ASP A 120     5608  12213  10795  -1060   1552  -5506       C  
ATOM    394  C   ASP A 120      24.168   5.927  67.066  1.00 69.50           C  
ANISOU  394  C   ASP A 120     4778  11709   9921  -1006   1549  -5679       C  
ATOM    395  O   ASP A 120      23.086   5.609  67.571  1.00 70.29           O  
ANISOU  395  O   ASP A 120     4841  12001   9864  -1001   1612  -5586       O  
ATOM    396  CB  ASP A 120      25.641   4.029  66.320  1.00 84.72           C  
ANISOU  396  CB  ASP A 120     6779  13597  11812  -1045   1525  -5453       C  
ATOM    397  CG  ASP A 120      25.794   2.958  65.263  1.00 89.26           C  
ANISOU  397  CG  ASP A 120     7494  13981  12441  -1103   1502  -5171       C  
ATOM    398  OD1 ASP A 120      24.822   2.732  64.513  1.00 91.62           O  
ANISOU  398  OD1 ASP A 120     7853  14139  12818  -1153   1540  -4991       O  
ATOM    399  OD2 ASP A 120      26.879   2.345  65.181  1.00 89.27           O  
ANISOU  399  OD2 ASP A 120     7566  13954  12398  -1091   1424  -5120       O  
ATOM    400  N   MET A 121      24.902   6.937  67.539  1.00 73.80           N  
ANISOU  400  N   MET A 121     5272  12241  10529   -965   1472  -5925       N  
ATOM    401  CA  MET A 121      24.413   7.761  68.639  1.00 79.84           C  
ANISOU  401  CA  MET A 121     5945  13209  11182   -901   1452  -6104       C  
ATOM    402  C   MET A 121      23.175   8.551  68.230  1.00 84.58           C  
ANISOU  402  C   MET A 121     6555  13685  11897   -919   1500  -6085       C  
ATOM    403  O   MET A 121      22.219   8.663  69.006  1.00 87.75           O  
ANISOU  403  O   MET A 121     6902  14304  12135   -872   1542  -6092       O  
ATOM    404  CB  MET A 121      25.517   8.707  69.111  1.00 80.81           C  
ANISOU  404  CB  MET A 121     5994  13309  11401   -863   1339  -6368       C  
ATOM    405  CG  MET A 121      25.097   9.641  70.230  1.00 84.07           C  
ANISOU  405  CG  MET A 121     6305  13918  11719   -782   1297  -6569       C  
ATOM    406  SD  MET A 121      26.350  10.883  70.593  1.00 85.11           S  
ANISOU  406  SD  MET A 121     6321  13966  12052   -752   1150  -6870       S  
ATOM    407  CE  MET A 121      26.364  11.809  69.060  1.00 81.87           C  
ANISOU  407  CE  MET A 121     5951  13108  12046   -868   1168  -6834       C  
ATOM    408  N   LEU A 122      23.175   9.107  67.017  1.00 82.85           N  
ANISOU  408  N   LEU A 122     6405  13122  11951   -978   1498  -6058       N  
ATOM    409  CA  LEU A 122      21.994   9.806  66.521  1.00 80.11           C  
ANISOU  409  CA  LEU A 122     6077  12641  11719   -991   1538  -6034       C  
ATOM    410  C   LEU A 122      20.820   8.850  66.370  1.00 80.77           C  
ANISOU  410  C   LEU A 122     6186  12823  11680  -1005   1630  -5807       C  
ATOM    411  O   LEU A 122      19.670   9.217  66.643  1.00 85.66           O  
ANISOU  411  O   LEU A 122     6764  13523  12259   -982   1672  -5804       O  
ATOM    412  CB  LEU A 122      22.305  10.482  65.186  1.00 74.16           C  
ANISOU  412  CB  LEU A 122     5405  11500  11274  -1047   1521  -6028       C  
ATOM    413  CG  LEU A 122      23.285  11.656  65.178  1.00 73.89           C  
ANISOU  413  CG  LEU A 122     5314  11325  11435  -1057   1441  -6230       C  
ATOM    414  CD1 LEU A 122      23.483  12.175  63.762  1.00 68.37           C  
ANISOU  414  CD1 LEU A 122     4696  10252  11028  -1118   1453  -6158       C  
ATOM    415  CD2 LEU A 122      22.802  12.767  66.097  1.00 75.76           C  
ANISOU  415  CD2 LEU A 122     5436  11705  11646  -1009   1399  -6430       C  
ATOM    416  N   LEU A 123      21.094   7.613  65.952  1.00 80.43           N  
ANISOU  416  N   LEU A 123     6193  12779  11587  -1044   1659  -5611       N  
ATOM    417  CA  LEU A 123      20.039   6.609  65.858  1.00 76.89           C  
ANISOU  417  CA  LEU A 123     5738  12438  11038  -1076   1734  -5376       C  
ATOM    418  C   LEU A 123      19.454   6.298  67.232  1.00 73.76           C  
ANISOU  418  C   LEU A 123     5233  12428  10365  -1034   1782  -5375       C  
ATOM    419  O   LEU A 123      18.231   6.238  67.403  1.00 71.73           O  
ANISOU  419  O   LEU A 123     4928  12265  10062  -1038   1849  -5278       O  
ATOM    420  CB  LEU A 123      20.587   5.341  65.202  1.00 73.43           C  
ANISOU  420  CB  LEU A 123     5359  11935  10607  -1132   1733  -5173       C  
ATOM    421  CG  LEU A 123      19.583   4.234  64.875  1.00 66.97           C  
ANISOU  421  CG  LEU A 123     4529  11167   9751  -1198   1785  -4902       C  
ATOM    422  CD1 LEU A 123      18.672   4.661  63.735  1.00 65.89           C  
ANISOU  422  CD1 LEU A 123     4448  10744   9843  -1221   1794  -4838       C  
ATOM    423  CD2 LEU A 123      20.302   2.937  64.537  1.00 65.93           C  
ANISOU  423  CD2 LEU A 123     4443  11035   9573  -1253   1752  -4719       C  
ATOM    424  N   GLY A 124      20.318   6.101  68.227  1.00 76.92           N  
ANISOU  424  N   GLY A 124     5590  13058  10577   -985   1751  -5481       N  
ATOM    425  CA  GLY A 124      19.876   5.791  69.576  1.00 86.11           C  
ANISOU  425  CA  GLY A 124     6665  14603  11451   -923   1801  -5483       C  
ATOM    426  C   GLY A 124      19.320   6.958  70.360  1.00 91.49           C  
ANISOU  426  C   GLY A 124     7280  15393  12088   -837   1797  -5678       C  
ATOM    427  O   GLY A 124      18.726   6.738  71.419  1.00 98.04           O  
ANISOU  427  O   GLY A 124     8041  16532  12679   -774   1860  -5653       O  
ATOM    428  N   PHE A 125      19.507   8.188  69.880  1.00 90.96           N  
ANISOU  428  N   PHE A 125     7233  15086  12243   -829   1728  -5863       N  
ATOM    429  CA  PHE A 125      19.010   9.364  70.581  1.00 97.05           C  
ANISOU  429  CA  PHE A 125     7935  15945  12993   -747   1708  -6058       C  
ATOM    430  C   PHE A 125      17.797  10.009  69.927  1.00 98.58           C  
ANISOU  430  C   PHE A 125     8134  15977  13344   -768   1752  -6019       C  
ATOM    431  O   PHE A 125      16.991  10.621  70.631  1.00111.19           O  
ANISOU  431  O   PHE A 125     9661  17733  14851   -694   1778  -6099       O  
ATOM    432  CB  PHE A 125      20.121  10.417  70.711  1.00102.54           C  
ANISOU  432  CB  PHE A 125     8615  16525  13820   -716   1580  -6324       C  
ATOM    433  CG  PHE A 125      19.704  11.651  71.462  1.00109.19           C  
ANISOU  433  CG  PHE A 125     9378  17459  14649   -626   1538  -6537       C  
ATOM    434  CD1 PHE A 125      19.541  11.619  72.837  1.00113.15           C  
ANISOU  434  CD1 PHE A 125     9808  18307  14877   -506   1542  -6622       C  
ATOM    435  CD2 PHE A 125      19.477  12.842  70.794  1.00109.14           C  
ANISOU  435  CD2 PHE A 125     9372  17196  14899   -652   1494  -6647       C  
ATOM    436  CE1 PHE A 125      19.157  12.750  73.533  1.00114.38           C  
ANISOU  436  CE1 PHE A 125     9893  18549  15016   -407   1498  -6819       C  
ATOM    437  CE2 PHE A 125      19.093  13.980  71.484  1.00110.44           C  
ANISOU  437  CE2 PHE A 125     9458  17448  15056   -564   1448  -6842       C  
ATOM    438  CZ  PHE A 125      18.933  13.933  72.855  1.00112.73           C  
ANISOU  438  CZ  PHE A 125     9677  18082  15073   -438   1448  -6931       C  
ATOM    439  N   LEU A 126      17.642   9.896  68.605  1.00 93.08           N  
ANISOU  439  N   LEU A 126     7520  14973  12875   -853   1758  -5901       N  
ATOM    440  CA  LEU A 126      16.518  10.508  67.911  1.00 74.85           C  
ANISOU  440  CA  LEU A 126     5221  12495  10724   -866   1788  -5873       C  
ATOM    441  C   LEU A 126      15.490   9.515  67.392  1.00 85.26           C  
ANISOU  441  C   LEU A 126     6547  13816  12034   -917   1877  -5610       C  
ATOM    442  O   LEU A 126      14.333   9.900  67.200  1.00 87.43           O  
ANISOU  442  O   LEU A 126     6788  14066  12366   -904   1918  -5582       O  
ATOM    443  CB  LEU A 126      17.012  11.356  66.729  1.00 73.26           C  
ANISOU  443  CB  LEU A 126     5104  11911  10818   -910   1718  -5960       C  
ATOM    444  CG  LEU A 126      17.980  12.505  67.011  1.00 73.94           C  
ANISOU  444  CG  LEU A 126     5163  11926  11004   -887   1620  -6206       C  
ATOM    445  CD1 LEU A 126      18.374  13.189  65.713  1.00 79.50           C  
ANISOU  445  CD1 LEU A 126     5946  12247  12012   -949   1578  -6220       C  
ATOM    446  CD2 LEU A 126      17.364  13.502  67.977  1.00 76.15           C  
ANISOU  446  CD2 LEU A 126     5343  12388  11204   -802   1602  -6384       C  
ATOM    447  N   VAL A 127      15.871   8.263  67.157  1.00 73.10           N  
ANISOU  447  N   VAL A 127     5037  12303  10436   -977   1900  -5417       N  
ATOM    448  CA  VAL A 127      15.007   7.280  66.514  1.00 72.26           C  
ANISOU  448  CA  VAL A 127     4932  12153  10372  -1047   1958  -5155       C  
ATOM    449  C   VAL A 127      14.545   6.210  67.497  1.00 73.74           C  
ANISOU  449  C   VAL A 127     5020  12686  10311  -1061   2040  -4978       C  
ATOM    450  O   VAL A 127      13.348   5.948  67.625  1.00 86.99           O  
ANISOU  450  O   VAL A 127     6621  14462  11969  -1078   2112  -4838       O  
ATOM    451  CB  VAL A 127      15.712   6.644  65.295  1.00 69.92           C  
ANISOU  451  CB  VAL A 127     4747  11578  10242  -1118   1911  -5038       C  
ATOM    452  CG1 VAL A 127      14.882   5.500  64.742  1.00 69.29           C  
ANISOU  452  CG1 VAL A 127     4652  11479  10196  -1198   1947  -4759       C  
ATOM    453  CG2 VAL A 127      15.969   7.695  64.223  1.00 68.62           C  
ANISOU  453  CG2 VAL A 127     4680  11058  10333  -1104   1855  -5175       C  
ATOM    454  N   MET A 128      15.486   5.573  68.192  1.00 74.12           N  
ANISOU  454  N   MET A 128     5065  12924  10174  -1055   2033  -4977       N  
ATOM    455  CA  MET A 128      15.128   4.499  69.115  1.00 83.25           C  
ANISOU  455  CA  MET A 128     6136  14412  11081  -1072   2117  -4795       C  
ATOM    456  C   MET A 128      14.213   4.944  70.256  1.00 88.76           C  
ANISOU  456  C   MET A 128     6729  15398  11599   -988   2203  -4838       C  
ATOM    457  O   MET A 128      13.268   4.198  70.573  1.00 89.70           O  
ANISOU  457  O   MET A 128     6766  15689  11626  -1030   2303  -4616       O  
ATOM    458  CB  MET A 128      16.411   3.846  69.647  1.00 83.02           C  
ANISOU  458  CB  MET A 128     6135  14529  10879  -1061   2081  -4823       C  
ATOM    459  CG  MET A 128      17.226   3.146  68.563  1.00 84.74           C  
ANISOU  459  CG  MET A 128     6443  14505  11250  -1148   2014  -4723       C  
ATOM    460  SD  MET A 128      18.768   2.410  69.145  1.00 89.57           S  
ANISOU  460  SD  MET A 128     7080  15284  11669  -1124   1964  -4773       S  
ATOM    461  CE  MET A 128      18.181   1.415  70.510  1.00 94.87           C  
ANISOU  461  CE  MET A 128     7704  16369  11975  -1113   2041  -4572       C  
ATOM    462  N   PRO A 129      14.415   6.098  70.908  1.00 93.22           N  
ANISOU  462  N   PRO A 129     7281  16028  12111   -874   2171  -5099       N  
ATOM    463  CA  PRO A 129      13.435   6.526  71.923  1.00 93.19           C  
ANISOU  463  CA  PRO A 129     7177  16286  11944   -783   2258  -5127       C  
ATOM    464  C   PRO A 129      12.053   6.793  71.354  1.00 81.93           C  
ANISOU  464  C   PRO A 129     5700  14753  10676   -815   2318  -5021       C  
ATOM    465  O   PRO A 129      11.051   6.536  72.034  1.00 83.86           O  
ANISOU  465  O   PRO A 129     5844  15233  10788   -786   2431  -4896       O  
ATOM    466  CB  PRO A 129      14.065   7.799  72.507  1.00 92.65           C  
ANISOU  466  CB  PRO A 129     7120  16234  11847   -662   2169  -5451       C  
ATOM    467  CG  PRO A 129      15.036   8.256  71.480  1.00 80.59           C  
ANISOU  467  CG  PRO A 129     5689  14365  10565   -718   2047  -5576       C  
ATOM    468  CD  PRO A 129      15.573   7.008  70.866  1.00 78.84           C  
ANISOU  468  CD  PRO A 129     5522  14072  10362   -821   2054  -5372       C  
ATOM    469  N   VAL A 130      11.964   7.305  70.125  1.00 79.98           N  
ANISOU  469  N   VAL A 130     5519  14160  10710   -866   2248  -5064       N  
ATOM    470  CA  VAL A 130      10.655   7.474  69.505  1.00 82.13           C  
ANISOU  470  CA  VAL A 130     5745  14320  11141   -895   2293  -4958       C  
ATOM    471  C   VAL A 130      10.021   6.116  69.235  1.00 84.41           C  
ANISOU  471  C   VAL A 130     5980  14660  11431  -1005   2363  -4634       C  
ATOM    472  O   VAL A 130       8.801   5.956  69.353  1.00 89.85           O  
ANISOU  472  O   VAL A 130     6566  15438  12136  -1016   2445  -4496       O  
ATOM    473  CB  VAL A 130      10.769   8.320  68.224  1.00 80.81           C  
ANISOU  473  CB  VAL A 130     5675  13765  11263   -913   2196  -5083       C  
ATOM    474  CG1 VAL A 130       9.398   8.537  67.606  1.00 78.06           C  
ANISOU  474  CG1 VAL A 130     5277  13310  11074   -927   2232  -4997       C  
ATOM    475  CG2 VAL A 130      11.426   9.653  68.536  1.00 78.36           C  
ANISOU  475  CG2 VAL A 130     5402  13405  10965   -825   2120  -5388       C  
ATOM    476  N   SER A 131      10.831   5.112  68.890  1.00 79.73           N  
ANISOU  476  N   SER A 131     5448  14016  10831  -1092   2329  -4505       N  
ATOM    477  CA  SER A 131      10.301   3.760  68.742  1.00 79.40           C  
ANISOU  477  CA  SER A 131     5348  14042  10778  -1210   2381  -4189       C  
ATOM    478  C   SER A 131       9.793   3.222  70.075  1.00 81.10           C  
ANISOU  478  C   SER A 131     5439  14651  10723  -1188   2513  -4061       C  
ATOM    479  O   SER A 131       8.790   2.500  70.119  1.00 82.10           O  
ANISOU  479  O   SER A 131     5465  14863  10867  -1265   2591  -3812       O  
ATOM    480  CB  SER A 131      11.372   2.838  68.160  1.00 77.13           C  
ANISOU  480  CB  SER A 131     5155  13631  10521  -1299   2305  -4096       C  
ATOM    481  OG  SER A 131      10.844   1.552  67.885  1.00 77.05           O  
ANISOU  481  OG  SER A 131     5095  13642  10540  -1434   2327  -3789       O  
ATOM    482  N   MET A 132      10.468   3.567  71.175  1.00 82.44           N  
ANISOU  482  N   MET A 132     5614  15063  10646  -1078   2536  -4223       N  
ATOM    483  CA  MET A 132       9.968   3.182  72.493  1.00 85.25           C  
ANISOU  483  CA  MET A 132     5866  15803  10722  -1024   2672  -4119       C  
ATOM    484  C   MET A 132       8.638   3.860  72.796  1.00 87.10           C  
ANISOU  484  C   MET A 132     5992  16114  10989   -960   2762  -4120       C  
ATOM    485  O   MET A 132       7.710   3.231  73.321  1.00 89.01           O  
ANISOU  485  O   MET A 132     6119  16561  11141   -988   2893  -3891       O  
ATOM    486  CB  MET A 132      10.991   3.530  73.571  1.00 95.48           C  
ANISOU  486  CB  MET A 132     7206  17320  11751   -892   2654  -4329       C  
ATOM    487  CG  MET A 132      10.573   3.098  74.966  1.00105.85           C  
ANISOU  487  CG  MET A 132     8438  19039  12741   -813   2795  -4221       C  
ATOM    488  SD  MET A 132      11.841   3.400  76.210  1.00115.77           S  
ANISOU  488  SD  MET A 132     9763  20550  13674   -645   2746  -4466       S  
ATOM    489  CE  MET A 132      11.717   5.176  76.391  1.00118.57           C  
ANISOU  489  CE  MET A 132    10116  20815  14118   -491   2668  -4827       C  
ATOM    490  N   LEU A 133       8.536   5.153  72.487  1.00 86.71           N  
ANISOU  490  N   LEU A 133     5971  15905  11069   -874   2696  -4372       N  
ATOM    491  CA  LEU A 133       7.266   5.854  72.646  1.00 88.31           C  
ANISOU  491  CA  LEU A 133     6073  16153  11328   -811   2768  -4388       C  
ATOM    492  C   LEU A 133       6.172   5.188  71.820  1.00 99.89           C  
ANISOU  492  C   LEU A 133     7461  17488  13003   -937   2809  -4124       C  
ATOM    493  O   LEU A 133       5.018   5.096  72.257  1.00 89.93           O  
ANISOU  493  O   LEU A 133     6065  16388  11716   -921   2927  -3989       O  
ATOM    494  CB  LEU A 133       7.428   7.321  72.249  1.00 87.59           C  
ANISOU  494  CB  LEU A 133     6044  15860  11375   -722   2663  -4700       C  
ATOM    495  CG  LEU A 133       6.191   8.210  72.372  1.00 89.17           C  
ANISOU  495  CG  LEU A 133     6151  16092  11638   -640   2717  -4764       C  
ATOM    496  CD1 LEU A 133       5.833   8.417  73.834  1.00 98.61           C  
ANISOU  496  CD1 LEU A 133     7255  17664  12550   -503   2832  -4796       C  
ATOM    497  CD2 LEU A 133       6.418   9.541  71.674  1.00 87.91           C  
ANISOU  497  CD2 LEU A 133     6073  15659  11667   -593   2590  -5042       C  
ATOM    498  N   THR A 134       6.519   4.720  70.620  1.00 91.20           N  
ANISOU  498  N   THR A 134     6441  16092  12120  -1059   2708  -4048       N  
ATOM    499  CA  THR A 134       5.554   4.025  69.774  1.00 90.71           C  
ANISOU  499  CA  THR A 134     6312  15881  12275  -1183   2713  -3801       C  
ATOM    500  C   THR A 134       5.099   2.716  70.413  1.00 93.61           C  
ANISOU  500  C   THR A 134     6562  16489  12515  -1280   2827  -3479       C  
ATOM    501  O   THR A 134       3.897   2.433  70.484  1.00106.74           O  
ANISOU  501  O   THR A 134     8086  18216  14255  -1321   2910  -3293       O  
ATOM    502  CB  THR A 134       6.159   3.772  68.391  1.00 81.81           C  
ANISOU  502  CB  THR A 134     5314  14387  11381  -1276   2567  -3798       C  
ATOM    503  OG1 THR A 134       6.309   5.018  67.699  1.00 80.53           O  
ANISOU  503  OG1 THR A 134     5243  13981  11374  -1194   2481  -4060       O  
ATOM    504  CG2 THR A 134       5.268   2.852  67.575  1.00 81.44           C  
ANISOU  504  CG2 THR A 134     5203  14197  11545  -1414   2547  -3522       C  
ATOM    505  N   ILE A 135       6.048   1.904  70.891  1.00 86.35           N  
ANISOU  505  N   ILE A 135     5696  15707  11408  -1320   2833  -3405       N  
ATOM    506  CA  ILE A 135       5.676   0.635  71.513  1.00 90.52           C  
ANISOU  506  CA  ILE A 135     6126  16465  11803  -1421   2942  -3087       C  
ATOM    507  C   ILE A 135       4.928   0.849  72.823  1.00 99.35           C  
ANISOU  507  C   ILE A 135     7118  17935  12697  -1317   3121  -3046       C  
ATOM    508  O   ILE A 135       4.242  -0.065  73.295  1.00104.24           O  
ANISOU  508  O   ILE A 135     7623  18729  13254  -1399   3241  -2754       O  
ATOM    509  CB  ILE A 135       6.898  -0.279  71.745  1.00 87.20           C  
ANISOU  509  CB  ILE A 135     5799  16125  11207  -1481   2906  -3024       C  
ATOM    510  CG1 ILE A 135       7.731   0.199  72.935  1.00 88.43           C  
ANISOU  510  CG1 ILE A 135     6001  16558  11041  -1322   2955  -3228       C  
ATOM    511  CG2 ILE A 135       7.743  -0.390  70.485  1.00 86.76           C  
ANISOU  511  CG2 ILE A 135     5879  15725  11362  -1556   2732  -3094       C  
ATOM    512  CD1 ILE A 135       8.963  -0.641  73.197  1.00 87.71           C  
ANISOU  512  CD1 ILE A 135     6000  16562  10763  -1361   2914  -3191       C  
ATOM    513  N   LEU A 136       5.038   2.035  73.427  1.00102.40           N  
ANISOU  513  N   LEU A 136     7522  18424  12963  -1139   3140  -3324       N  
ATOM    514  CA  LEU A 136       4.238   2.331  74.612  1.00105.56           C  
ANISOU  514  CA  LEU A 136     7805  19139  13165  -1020   3307  -3296       C  
ATOM    515  C   LEU A 136       2.795   2.675  74.260  1.00106.24           C  
ANISOU  515  C   LEU A 136     7747  19157  13461  -1032   3370  -3207       C  
ATOM    516  O   LEU A 136       1.888   2.412  75.058  1.00109.41           O  
ANISOU  516  O   LEU A 136     8010  19800  13760  -1004   3537  -3033       O  
ATOM    517  CB  LEU A 136       4.860   3.483  75.404  1.00 96.29           C  
ANISOU  517  CB  LEU A 136     6700  18095  11789   -820   3284  -3631       C  
ATOM    518  CG  LEU A 136       5.952   3.134  76.415  1.00 97.10           C  
ANISOU  518  CG  LEU A 136     6883  18445  11566   -744   3297  -3687       C  
ATOM    519  CD1 LEU A 136       6.331   4.363  77.226  1.00 98.35           C  
ANISOU  519  CD1 LEU A 136     7083  18727  11558   -536   3266  -4016       C  
ATOM    520  CD2 LEU A 136       5.495   2.008  77.328  1.00 99.63           C  
ANISOU  520  CD2 LEU A 136     7119  19075  11661   -775   3474  -3372       C  
ATOM    521  N   TYR A 137       2.563   3.253  73.080  1.00104.23           N  
ANISOU  521  N   TYR A 137     7525  18580  13498  -1067   3243  -3319       N  
ATOM    522  CA  TYR A 137       1.230   3.648  72.640  1.00103.69           C  
ANISOU  522  CA  TYR A 137     7328  18423  13646  -1069   3277  -3265       C  
ATOM    523  C   TYR A 137       0.522   2.559  71.845  1.00 94.96           C  
ANISOU  523  C   TYR A 137     6133  17169  12780  -1257   3264  -2949       C  
ATOM    524  O   TYR A 137      -0.353   2.868  71.025  1.00 94.59           O  
ANISOU  524  O   TYR A 137     6022  16925  12993  -1285   3214  -2939       O  
ATOM    525  CB  TYR A 137       1.315   4.932  71.813  1.00 96.50           C  
ANISOU  525  CB  TYR A 137     6507  17249  12911   -990   3141  -3569       C  
ATOM    526  CG  TYR A 137       1.263   6.198  72.634  1.00105.14           C  
ANISOU  526  CG  TYR A 137     7600  18504  13844   -799   3181  -3841       C  
ATOM    527  CD1 TYR A 137       0.086   6.925  72.752  1.00113.23           C  
ANISOU  527  CD1 TYR A 137     8504  19577  14940   -716   3247  -3882       C  
ATOM    528  CD2 TYR A 137       2.391   6.666  73.294  1.00108.44           C  
ANISOU  528  CD2 TYR A 137     8133  19023  14047   -700   3142  -4061       C  
ATOM    529  CE1 TYR A 137       0.035   8.085  73.502  1.00116.82           C  
ANISOU  529  CE1 TYR A 137     8961  20176  15248   -539   3271  -4133       C  
ATOM    530  CE2 TYR A 137       2.350   7.823  74.046  1.00112.36           C  
ANISOU  530  CE2 TYR A 137     8629  19656  14407   -526   3155  -4313       C  
ATOM    531  CZ  TYR A 137       1.171   8.529  74.147  1.00115.52           C  
ANISOU  531  CZ  TYR A 137     8916  20101  14874   -446   3220  -4347       C  
ATOM    532  OH  TYR A 137       1.127   9.682  74.896  1.00116.52           O  
ANISOU  532  OH  TYR A 137     9045  20361  14865   -270   3224  -4600       O  
ATOM    533  N   GLY A 138       0.870   1.295  72.066  1.00 95.13           N  
ANISOU  533  N   GLY A 138     6148  17273  12722  -1386   3297  -2694       N  
ATOM    534  CA  GLY A 138       0.268   0.223  71.292  1.00103.31           C  
ANISOU  534  CA  GLY A 138     7108  18144  14002  -1579   3255  -2394       C  
ATOM    535  C   GLY A 138       0.575   0.306  69.816  1.00104.34           C  
ANISOU  535  C   GLY A 138     7352  17877  14413  -1654   3045  -2477       C  
ATOM    536  O   GLY A 138      -0.270  -0.055  68.989  1.00108.77           O  
ANISOU  536  O   GLY A 138     7835  18243  15248  -1758   2980  -2325       O  
ATOM    537  N   TYR A 139       1.767   0.792  69.464  1.00102.42           N  
ANISOU  537  N   TYR A 139     7295  17507  14115  -1596   2935  -2719       N  
ATOM    538  CA  TYR A 139       2.220   0.952  68.083  1.00 98.22           C  
ANISOU  538  CA  TYR A 139     6901  16596  13822  -1640   2748  -2821       C  
ATOM    539  C   TYR A 139       1.362   1.934  67.291  1.00 95.57           C  
ANISOU  539  C   TYR A 139     6542  16050  13721  -1574   2691  -2964       C  
ATOM    540  O   TYR A 139       1.361   1.904  66.059  1.00 97.69           O  
ANISOU  540  O   TYR A 139     6891  15995  14231  -1625   2546  -2979       O  
ATOM    541  CB  TYR A 139       2.293  -0.398  67.359  1.00101.49           C  
ANISOU  541  CB  TYR A 139     7329  16845  14388  -1831   2653  -2547       C  
ATOM    542  CG  TYR A 139       3.159  -1.412  68.070  1.00105.26           C  
ANISOU  542  CG  TYR A 139     7839  17519  14635  -1908   2698  -2400       C  
ATOM    543  CD1 TYR A 139       4.543  -1.299  68.058  1.00102.72           C  
ANISOU  543  CD1 TYR A 139     7680  17175  14176  -1865   2636  -2568       C  
ATOM    544  CD2 TYR A 139       2.594  -2.477  68.759  1.00112.19           C  
ANISOU  544  CD2 TYR A 139     8584  18609  15436  -2023   2804  -2089       C  
ATOM    545  CE1 TYR A 139       5.339  -2.220  68.708  1.00106.54           C  
ANISOU  545  CE1 TYR A 139     8193  17851  14437  -1928   2670  -2443       C  
ATOM    546  CE2 TYR A 139       3.384  -3.404  69.413  1.00116.17           C  
ANISOU  546  CE2 TYR A 139     9128  19302  15709  -2093   2844  -1951       C  
ATOM    547  CZ  TYR A 139       4.756  -3.269  69.385  1.00114.70           C  
ANISOU  547  CZ  TYR A 139     9105  19100  15375  -2041   2774  -2135       C  
ATOM    548  OH  TYR A 139       5.547  -4.189  70.034  1.00119.78           O  
ANISOU  548  OH  TYR A 139     9832  19904  15773  -2084   2784  -1985       O  
ATOM    549  N   ARG A 140       0.629   2.812  67.971  1.00 92.93           N  
ANISOU  549  N   ARG A 140     6105  15894  13313  -1453   2799  -3075       N  
ATOM    550  CA  ARG A 140      -0.114   3.879  67.315  1.00 87.53           C  
ANISOU  550  CA  ARG A 140     5406  15036  12815  -1370   2747  -3251       C  
ATOM    551  C   ARG A 140       0.713   5.157  67.374  1.00 88.93           C  
ANISOU  551  C   ARG A 140     5730  15162  12898  -1226   2705  -3600       C  
ATOM    552  O   ARG A 140       1.217   5.526  68.439  1.00 96.55           O  
ANISOU  552  O   ARG A 140     6702  16368  13613  -1136   2785  -3714       O  
ATOM    553  CB  ARG A 140      -1.477   4.100  67.971  1.00101.01           C  
ANISOU  553  CB  ARG A 140     6902  16955  14521  -1325   2883  -3162       C  
ATOM    554  CG  ARG A 140      -2.201   5.336  67.458  1.00 97.85           C  
ANISOU  554  CG  ARG A 140     6488  16421  14268  -1214   2840  -3382       C  
ATOM    555  CD  ARG A 140      -3.378   5.721  68.338  1.00 97.13           C  
ANISOU  555  CD  ARG A 140     6196  16595  14112  -1131   2995  -3343       C  
ATOM    556  NE  ARG A 140      -3.082   6.906  69.137  1.00 96.43           N  
ANISOU  556  NE  ARG A 140     6153  16668  13818   -956   3050  -3619       N  
ATOM    557  CZ  ARG A 140      -3.228   8.154  68.702  1.00 95.45           C  
ANISOU  557  CZ  ARG A 140     6090  16402  13773   -847   2975  -3894       C  
ATOM    558  NH1 ARG A 140      -3.667   8.382  67.471  1.00 92.44           N  
ANISOU  558  NH1 ARG A 140     5738  15722  13664   -886   2853  -3933       N  
ATOM    559  NH2 ARG A 140      -2.933   9.174  69.496  1.00 94.98           N  
ANISOU  559  NH2 ARG A 140     6069  16495  13525   -699   3013  -4132       N  
ATOM    560  N   TRP A 141       0.851   5.822  66.237  1.00 87.24           N  
ANISOU  560  N   TRP A 141     5631  14628  12887  -1206   2574  -3767       N  
ATOM    561  CA  TRP A 141       1.675   7.019  66.142  1.00 88.93           C  
ANISOU  561  CA  TRP A 141     5992  14740  13059  -1093   2517  -4085       C  
ATOM    562  C   TRP A 141       1.034   8.177  66.897  1.00 92.24           C  
ANISOU  562  C   TRP A 141     6329  15331  13385   -955   2589  -4271       C  
ATOM    563  O   TRP A 141      -0.032   8.654  66.484  1.00 93.04           O  
ANISOU  563  O   TRP A 141     6353  15360  13640   -924   2586  -4293       O  
ATOM    564  CB  TRP A 141       1.902   7.385  64.679  1.00 80.66           C  
ANISOU  564  CB  TRP A 141     5084  13295  12268  -1111   2373  -4186       C  
ATOM    565  CG  TRP A 141       2.870   8.508  64.489  1.00 92.86           C  
ANISOU  565  CG  TRP A 141     6785  14701  13797  -1023   2311  -4480       C  
ATOM    566  CD1 TRP A 141       2.597   9.756  64.011  1.00 95.51           C  
ANISOU  566  CD1 TRP A 141     7168  14869  14252   -936   2262  -4709       C  
ATOM    567  CD2 TRP A 141       4.270   8.491  64.791  1.00 88.70           C  
ANISOU  567  CD2 TRP A 141     6378  14187  13137  -1021   2285  -4571       C  
ATOM    568  NE1 TRP A 141       3.743  10.515  63.987  1.00 96.50           N  
ANISOU  568  NE1 TRP A 141     7433  14893  14339   -892   2207  -4925       N  
ATOM    569  CE2 TRP A 141       4.784   9.761  64.462  1.00 90.85           C  
ANISOU  569  CE2 TRP A 141     6760  14285  13473   -940   2219  -4848       C  
ATOM    570  CE3 TRP A 141       5.140   7.524  65.305  1.00 85.24           C  
ANISOU  570  CE3 TRP A 141     5959  13889  12540  -1082   2307  -4446       C  
ATOM    571  CZ2 TRP A 141       6.127  10.089  64.629  1.00 84.89           C  
ANISOU  571  CZ2 TRP A 141     6122  13488  12644   -925   2173  -4994       C  
ATOM    572  CZ3 TRP A 141       6.473   7.852  65.469  1.00 81.91           C  
ANISOU  572  CZ3 TRP A 141     5658  13434  12032  -1053   2261  -4606       C  
ATOM    573  CH2 TRP A 141       6.953   9.123  65.132  1.00 80.77           C  
ANISOU  573  CH2 TRP A 141     5611  13110  11969   -978   2194  -4875       C  
ATOM    574  N   PRO A 142       1.628   8.655  67.996  1.00 95.03           N  
ANISOU  574  N   PRO A 142     6696  15915  13497   -863   2644  -4414       N  
ATOM    575  CA  PRO A 142       1.007   9.730  68.778  1.00101.06           C  
ANISOU  575  CA  PRO A 142     7381  16857  14161   -722   2706  -4588       C  
ATOM    576  C   PRO A 142       1.373  11.143  68.347  1.00105.24           C  
ANISOU  576  C   PRO A 142     8025  17187  14775   -632   2596  -4908       C  
ATOM    577  O   PRO A 142       0.712  12.094  68.789  1.00112.98           O  
ANISOU  577  O   PRO A 142     8939  18266  15723   -521   2625  -5054       O  
ATOM    578  CB  PRO A 142       1.523   9.446  70.196  1.00101.44           C  
ANISOU  578  CB  PRO A 142     7393  17252  13898   -665   2807  -4572       C  
ATOM    579  CG  PRO A 142       2.804   8.635  70.012  1.00 88.56           C  
ANISOU  579  CG  PRO A 142     5882  15552  12216   -756   2747  -4512       C  
ATOM    580  CD  PRO A 142       2.930   8.261  68.555  1.00 89.92           C  
ANISOU  580  CD  PRO A 142     6140  15366  12658   -874   2636  -4439       C  
ATOM    581  N   LEU A 143       2.390  11.311  67.518  1.00 98.42           N  
ANISOU  581  N   LEU A 143     7324  16049  14021   -677   2476  -5013       N  
ATOM    582  CA  LEU A 143       2.887  12.624  67.133  1.00 96.24           C  
ANISOU  582  CA  LEU A 143     7161  15575  13832   -610   2371  -5301       C  
ATOM    583  C   LEU A 143       2.212  13.082  65.848  1.00 92.31           C  
ANISOU  583  C   LEU A 143     6699  14768  13607   -626   2301  -5336       C  
ATOM    584  O   LEU A 143       1.440  12.338  65.238  1.00 83.02           O  
ANISOU  584  O   LEU A 143     5465  13524  12556   -688   2320  -5144       O  
ATOM    585  CB  LEU A 143       4.406  12.564  66.991  1.00 92.11           C  
ANISOU  585  CB  LEU A 143     6784  14933  13282   -648   2290  -5386       C  
ATOM    586  CG  LEU A 143       5.152  12.275  68.296  1.00 89.29           C  
ANISOU  586  CG  LEU A 143     6397  14878  12651   -610   2338  -5405       C  
ATOM    587  CD1 LEU A 143       6.620  11.974  68.037  1.00 82.04           C  
ANISOU  587  CD1 LEU A 143     5607  13832  11731   -668   2259  -5445       C  
ATOM    588  CD2 LEU A 143       5.002  13.439  69.271  1.00 94.38           C  
ANISOU  588  CD2 LEU A 143     6992  15700  13168   -475   2339  -5635       C  
ATOM    589  N   PRO A 144       2.460  14.323  65.415  1.00 92.13           N  
ANISOU  589  N   PRO A 144     6765  14550  13692   -569   2211  -5578       N  
ATOM    590  CA  PRO A 144       1.883  14.788  64.147  1.00 92.74           C  
ANISOU  590  CA  PRO A 144     6892  14318  14027   -577   2139  -5622       C  
ATOM    591  C   PRO A 144       2.246  13.894  62.968  1.00 98.99           C  
ANISOU  591  C   PRO A 144     7779  14846  14985   -676   2093  -5469       C  
ATOM    592  O   PRO A 144       3.177  13.086  63.017  1.00110.89           O  
ANISOU  592  O   PRO A 144     9348  16360  16425   -743   2094  -5366       O  
ATOM    593  CB  PRO A 144       2.478  16.190  63.984  1.00 92.21           C  
ANISOU  593  CB  PRO A 144     6924  14091  14021   -521   2045  -5891       C  
ATOM    594  CG  PRO A 144       2.659  16.666  65.376  1.00 93.15           C  
ANISOU  594  CG  PRO A 144     6967  14514  13911   -441   2085  -6005       C  
ATOM    595  CD  PRO A 144       3.000  15.449  66.204  1.00 91.89           C  
ANISOU  595  CD  PRO A 144     6753  14614  13546   -480   2177  -5822       C  
ATOM    596  N   SER A 145       1.485  14.063  61.882  1.00114.40           N  
ANISOU  596  N   SER A 145     8952  16680  17836   3050   3392  -1943       N  
ATOM    597  CA  SER A 145       1.573  13.144  60.750  1.00109.47           C  
ANISOU  597  CA  SER A 145     8272  16077  17243   2923   3258  -1878       C  
ATOM    598  C   SER A 145       2.890  13.298  59.996  1.00113.35           C  
ANISOU  598  C   SER A 145     9015  16557  17494   2955   2952  -1938       C  
ATOM    599  O   SER A 145       3.485  12.300  59.571  1.00117.34           O  
ANISOU  599  O   SER A 145     9574  17279  17730   2853   2798  -1933       O  
ATOM    600  CB  SER A 145       0.387  13.362  59.810  1.00104.54           C  
ANISOU  600  CB  SER A 145     7423  15329  16967   3019   3348  -1650       C  
ATOM    601  OG  SER A 145      -0.830  12.981  60.429  1.00104.87           O  
ANISOU  601  OG  SER A 145     7218  15497  17131   3014   3607  -1529       O  
ATOM    602  N   LYS A 146       3.358  14.535  59.809  1.00111.26           N  
ANISOU  602  N   LYS A 146     8920  16079  17276   3123   2866  -1940       N  
ATOM    603  CA  LYS A 146       4.605  14.749  59.080  1.00107.13           C  
ANISOU  603  CA  LYS A 146     8655  15486  16564   3162   2606  -1938       C  
ATOM    604  C   LYS A 146       5.792  14.137  59.813  1.00 92.35           C  
ANISOU  604  C   LYS A 146     7005  13793  14289   3124   2550  -1919       C  
ATOM    605  O   LYS A 146       6.734  13.637  59.178  1.00 86.20           O  
ANISOU  605  O   LYS A 146     6397  13038  13318   3104   2394  -1815       O  
ATOM    606  CB  LYS A 146       4.843  16.245  58.870  1.00108.24           C  
ANISOU  606  CB  LYS A 146     8918  15364  16843   3371   2584  -1897       C  
ATOM    607  CG  LYS A 146       3.689  17.000  58.220  1.00111.85           C  
ANISOU  607  CG  LYS A 146     9180  15692  17627   3502   2676  -1792       C  
ATOM    608  CD  LYS A 146       3.967  18.497  58.219  1.00114.18           C  
ANISOU  608  CD  LYS A 146     9614  15821  17949   3731   2650  -1767       C  
ATOM    609  CE  LYS A 146       2.790  19.289  57.674  1.00121.34           C  
ANISOU  609  CE  LYS A 146    10325  16707  19074   3919   2725  -1662       C  
ATOM    610  NZ  LYS A 146       3.051  20.755  57.703  1.00125.52           N  
ANISOU  610  NZ  LYS A 146    10992  17108  19594   4147   2690  -1664       N  
ATOM    611  N   LEU A 147       5.760  14.167  61.147  1.00 86.38           N  
ANISOU  611  N   LEU A 147     6262  13120  13439   3121   2714  -1952       N  
ATOM    612  CA  LEU A 147       6.853  13.618  61.936  1.00 93.45           C  
ANISOU  612  CA  LEU A 147     7373  14093  14043   3084   2729  -1853       C  
ATOM    613  C   LEU A 147       7.028  12.122  61.727  1.00106.16           C  
ANISOU  613  C   LEU A 147     8938  15912  15484   2935   2745  -1698       C  
ATOM    614  O   LEU A 147       8.134  11.616  61.923  1.00113.91           O  
ANISOU  614  O   LEU A 147    10130  16822  16330   2883   2737  -1557       O  
ATOM    615  CB  LEU A 147       6.624  13.913  63.419  1.00 93.09           C  
ANISOU  615  CB  LEU A 147     7318  14095  13958   3099   2923  -1921       C  
ATOM    616  CG  LEU A 147       6.609  15.395  63.799  1.00 93.09           C  
ANISOU  616  CG  LEU A 147     7400  13871  14099   3251   2940  -2026       C  
ATOM    617  CD1 LEU A 147       6.640  15.565  65.310  1.00 97.97           C  
ANISOU  617  CD1 LEU A 147     8063  14551  14611   3262   3116  -2071       C  
ATOM    618  CD2 LEU A 147       7.768  16.136  63.148  1.00 87.23           C  
ANISOU  618  CD2 LEU A 147     6919  12882  13341   3360   2769  -1957       C  
ATOM    619  N   CYS A 148       5.987  11.410  61.290  1.00105.96           N  
ANISOU  619  N   CYS A 148     8647  16094  15517   2847   2779  -1710       N  
ATOM    620  CA  CYS A 148       6.146   9.993  60.976  1.00101.55           C  
ANISOU  620  CA  CYS A 148     8046  15718  14821   2693   2793  -1524       C  
ATOM    621  C   CYS A 148       7.097   9.795  59.801  1.00 99.51           C  
ANISOU  621  C   CYS A 148     7962  15302  14546   2700   2618  -1395       C  
ATOM    622  O   CYS A 148       8.049   9.005  59.878  1.00 96.10           O  
ANISOU  622  O   CYS A 148     7683  14789  14041   2591   2642  -1237       O  
ATOM    623  CB  CYS A 148       4.785   9.364  60.680  1.00 97.71           C  
ANISOU  623  CB  CYS A 148     7232  15490  14403   2597   2845  -1573       C  
ATOM    624  SG  CYS A 148       4.884   7.717  59.949  1.00 88.76           S  
ANISOU  624  SG  CYS A 148     6030  14550  13147   2408   2825  -1309       S  
ATOM    625  N   ALA A 149       6.849  10.505  58.698  1.00 98.26           N  
ANISOU  625  N   ALA A 149     7779  15058  14498   2805   2450  -1480       N  
ATOM    626  CA  ALA A 149       7.748  10.430  57.552  1.00 89.04           C  
ANISOU  626  CA  ALA A 149     6790  13735  13307   2823   2277  -1369       C  
ATOM    627  C   ALA A 149       9.135  10.948  57.904  1.00 85.26           C  
ANISOU  627  C   ALA A 149     6635  12988  12773   2870   2238  -1329       C  
ATOM    628  O   ALA A 149      10.144  10.371  57.480  1.00 84.50           O  
ANISOU  628  O   ALA A 149     6707  12765  12634   2795   2190  -1192       O  
ATOM    629  CB  ALA A 149       7.164  11.208  56.374  1.00 86.03           C  
ANISOU  629  CB  ALA A 149     6324  13297  13066   2928   2108  -1488       C  
ATOM    630  N   VAL A 150       9.209  12.029  58.687  1.00 74.12           N  
ANISOU  630  N   VAL A 150     5307  11466  11389   2975   2262  -1453       N  
ATOM    631  CA  VAL A 150      10.513  12.561  59.087  1.00 71.56           C  
ANISOU  631  CA  VAL A 150     5287  10897  11006   3010   2221  -1420       C  
ATOM    632  C   VAL A 150      11.293  11.522  59.887  1.00 79.29           C  
ANISOU  632  C   VAL A 150     6367  11873  11885   2873   2355  -1287       C  
ATOM    633  O   VAL A 150      12.501  11.333  59.688  1.00 73.05           O  
ANISOU  633  O   VAL A 150     5806  10886  11063   2829   2295  -1196       O  
ATOM    634  CB  VAL A 150      10.333  13.870  59.878  1.00 73.32           C  
ANISOU  634  CB  VAL A 150     5541  11012  11305   3146   2271  -1553       C  
ATOM    635  CG1 VAL A 150      11.657  14.326  60.470  1.00 71.09           C  
ANISOU  635  CG1 VAL A 150     5553  10503  10956   3176   2270  -1497       C  
ATOM    636  CG2 VAL A 150       9.742  14.952  58.985  1.00 85.55           C  
ANISOU  636  CG2 VAL A 150     7008  12453  13045   3275   2168  -1646       C  
ATOM    637  N   TRP A 151      10.607  10.813  60.784  1.00 79.86           N  
ANISOU  637  N   TRP A 151     6265  12151  11926   2786   2541  -1282       N  
ATOM    638  CA  TRP A 151      11.259   9.838  61.647  1.00 76.17           C  
ANISOU  638  CA  TRP A 151     5880  11670  11389   2636   2688  -1173       C  
ATOM    639  C   TRP A 151      11.701   8.611  60.859  1.00 75.51           C  
ANISOU  639  C   TRP A 151     5796  11564  11330   2473   2664  -1026       C  
ATOM    640  O   TRP A 151      12.800   8.088  61.083  1.00 65.90           O  
ANISOU  640  O   TRP A 151     4795  10146  10097   2356   2678   -921       O  
ATOM    641  CB  TRP A 151      10.304   9.466  62.782  1.00 73.20           C  
ANISOU  641  CB  TRP A 151     5311  11531  10972   2578   2887  -1212       C  
ATOM    642  CG  TRP A 151      10.699   8.284  63.601  1.00 72.46           C  
ANISOU  642  CG  TRP A 151     5244  11471  10815   2387   3051  -1098       C  
ATOM    643  CD1 TRP A 151      11.757   8.192  64.456  1.00 73.34           C  
ANISOU  643  CD1 TRP A 151     5596  11399  10872   2336   3114  -1049       C  
ATOM    644  CD2 TRP A 151      10.014   7.029  63.671  1.00 75.90           C  
ANISOU  644  CD2 TRP A 151     5479  12117  11243   2198   3165  -1013       C  
ATOM    645  NE1 TRP A 151      11.783   6.950  65.043  1.00 75.91           N  
ANISOU  645  NE1 TRP A 151     5903  11778  11163   2118   3255   -936       N  
ATOM    646  CE2 TRP A 151      10.722   6.217  64.578  1.00 72.49           C  
ANISOU  646  CE2 TRP A 151     5183  11604  10756   2032   3294   -919       C  
ATOM    647  CE3 TRP A 151       8.875   6.511  63.049  1.00 80.82           C  
ANISOU  647  CE3 TRP A 151     5835  12973  11902   2136   3158   -999       C  
ATOM    648  CZ2 TRP A 151      10.329   4.916  64.876  1.00 76.04           C  
ANISOU  648  CZ2 TRP A 151     5511  12193  11187   1803   3416   -817       C  
ATOM    649  CZ3 TRP A 151       8.486   5.220  63.346  1.00 82.25           C  
ANISOU  649  CZ3 TRP A 151     5882  13309  12058   1914   3280   -891       C  
ATOM    650  CH2 TRP A 151       9.210   4.437  64.252  1.00 80.83           C  
ANISOU  650  CH2 TRP A 151     5836  13050  11826   1749   3411   -807       C  
ATOM    651  N   ILE A 152      10.865   8.141  59.928  1.00 78.68           N  
ANISOU  651  N   ILE A 152     5989  12125  11782   2434   2614  -1003       N  
ATOM    652  CA  ILE A 152      11.275   7.030  59.069  1.00 79.72           C  
ANISOU  652  CA  ILE A 152     6116  12217  11957   2276   2576   -873       C  
ATOM    653  C   ILE A 152      12.478   7.427  58.221  1.00 80.37           C  
ANISOU  653  C   ILE A 152     6466  12006  12063   2324   2405   -830       C  
ATOM    654  O   ILE A 152      13.410   6.633  58.022  1.00 77.70           O  
ANISOU  654  O   ILE A 152     6299  11475  11748   2160   2393   -708       O  
ATOM    655  CB  ILE A 152      10.096   6.565  58.193  1.00 77.74           C  
ANISOU  655  CB  ILE A 152     5592  12194  11752   2235   2537   -860       C  
ATOM    656  CG1 ILE A 152       8.950   6.044  59.062  1.00 77.49           C  
ANISOU  656  CG1 ILE A 152     5316  12440  11686   2143   2705   -876       C  
ATOM    657  CG2 ILE A 152      10.549   5.497  57.206  1.00 76.39           C  
ANISOU  657  CG2 ILE A 152     5423  11959  11641   2073   2476   -737       C  
ATOM    658  CD1 ILE A 152       7.805   5.449  58.269  1.00 74.91           C  
ANISOU  658  CD1 ILE A 152     4716  12350  11396   2072   2674   -845       C  
ATOM    659  N   TYR A 153      12.489   8.670  57.727  1.00 80.53           N  
ANISOU  659  N   TYR A 153     6555  11961  12080   2523   2263   -926       N  
ATOM    660  CA  TYR A 153      13.626   9.150  56.950  1.00 81.49           C  
ANISOU  660  CA  TYR A 153     6932  11825  12205   2575   2097   -896       C  
ATOM    661  C   TYR A 153      14.898   9.155  57.781  1.00 73.90           C  
ANISOU  661  C   TYR A 153     6264  10615  11200   2497   2133   -835       C  
ATOM    662  O   TYR A 153      15.946   8.694  57.324  1.00 72.48           O  
ANISOU  662  O   TYR A 153     6284  10224  11032   2386   2068   -729       O  
ATOM    663  CB  TYR A 153      13.343  10.547  56.403  1.00 91.68           C  
ANISOU  663  CB  TYR A 153     8269  13070  13494   2763   1937  -1008       C  
ATOM    664  CG  TYR A 153      14.581  11.285  55.929  1.00 93.48           C  
ANISOU  664  CG  TYR A 153     8781  13010  13727   2826   1805   -980       C  
ATOM    665  CD1 TYR A 153      15.245  10.898  54.773  1.00 91.84           C  
ANISOU  665  CD1 TYR A 153     8676  12682  13536   2777   1686   -887       C  
ATOM    666  CD2 TYR A 153      15.068  12.385  56.623  1.00 94.59           C  
ANISOU  666  CD2 TYR A 153     9077  12996  13866   2930   1811  -1040       C  
ATOM    667  CE1 TYR A 153      16.362  11.576  54.327  1.00 89.88           C  
ANISOU  667  CE1 TYR A 153     8686  12170  13293   2815   1576   -849       C  
ATOM    668  CE2 TYR A 153      16.190  13.069  56.185  1.00 91.34           C  
ANISOU  668  CE2 TYR A 153     8915  12328  13463   2972   1699  -1002       C  
ATOM    669  CZ  TYR A 153      16.832  12.657  55.036  1.00 89.57           C  
ANISOU  669  CZ  TYR A 153     8796  11992  13245   2907   1582   -903       C  
ATOM    670  OH  TYR A 153      17.947  13.328  54.590  1.00 87.97           O  
ANISOU  670  OH  TYR A 153     8848  11539  13038   2915   1473   -852       O  
ATOM    671  N   LEU A 154      14.824   9.673  59.009  1.00 67.45           N  
ANISOU  671  N   LEU A 154     5473   9821  10334   2552   2238   -907       N  
ATOM    672  CA  LEU A 154      16.013   9.717  59.856  1.00 58.68           C  
ANISOU  672  CA  LEU A 154     4636   8485   9174   2483   2271   -852       C  
ATOM    673  C   LEU A 154      16.500   8.313  60.205  1.00 57.38           C  
ANISOU  673  C   LEU A 154     4520   8257   9022   2252   2385   -713       C  
ATOM    674  O   LEU A 154      17.710   8.050  60.217  1.00 61.07           O  
ANISOU  674  O   LEU A 154     5233   8486   9486   2156   2344   -627       O  
ATOM    675  CB  LEU A 154      15.723  10.522  61.122  1.00 70.82           C  
ANISOU  675  CB  LEU A 154     6170  10081  10659   2586   2369   -961       C  
ATOM    676  CG  LEU A 154      15.543  12.026  60.898  1.00 76.49           C  
ANISOU  676  CG  LEU A 154     6907  10754  11403   2799   2265  -1091       C  
ATOM    677  CD1 LEU A 154      15.280  12.750  62.213  1.00 79.83           C  
ANISOU  677  CD1 LEU A 154     7328  11212  11793   2882   2385  -1191       C  
ATOM    678  CD2 LEU A 154      16.753  12.613  60.184  1.00 75.58           C  
ANISOU  678  CD2 LEU A 154     7060  10347  11309   2819   2113  -1021       C  
ATOM    679  N   ASP A 155      15.569   7.399  60.487  1.00 59.24           N  
ANISOU  679  N   ASP A 155     4523   8707   9278   2150   2524   -695       N  
ATOM    680  CA  ASP A 155      15.925   6.017  60.796  1.00 58.28           C  
ANISOU  680  CA  ASP A 155     4429   8534   9180   1912   2629   -576       C  
ATOM    681  C   ASP A 155      16.675   5.368  59.636  1.00 57.54           C  
ANISOU  681  C   ASP A 155     4441   8260   9162   1801   2508   -477       C  
ATOM    682  O   ASP A 155      17.795   4.853  59.801  1.00 53.43           O  
ANISOU  682  O   ASP A 155     4140   7508   8651   1676   2507   -394       O  
ATOM    683  CB  ASP A 155      14.649   5.239  61.126  1.00 61.04           C  
ANISOU  683  CB  ASP A 155     4479   9180   9532   1820   2771   -586       C  
ATOM    684  CG  ASP A 155      14.923   3.859  61.681  1.00 66.40           C  
ANISOU  684  CG  ASP A 155     5187   9825  10217   1563   2896   -481       C  
ATOM    685  OD1 ASP A 155      16.103   3.516  61.899  1.00 66.22           O  
ANISOU  685  OD1 ASP A 155     5416   9545  10198   1470   2885   -410       O  
ATOM    686  OD2 ASP A 155      13.944   3.118  61.906  1.00 62.63           O  
ANISOU  686  OD2 ASP A 155     4478   9584   9734   1451   3000   -473       O  
ATOM    687  N   VAL A 156      16.058   5.376  58.450  1.00 64.29           N  
ANISOU  687  N   VAL A 156     5135   9221  10069   1846   2405   -490       N  
ATOM    688  CA  VAL A 156      16.686   4.775  57.277  1.00 54.19           C  
ANISOU  688  CA  VAL A 156     3940   7787   8863   1746   2287   -404       C  
ATOM    689  C   VAL A 156      18.001   5.474  56.964  1.00 59.83           C  
ANISOU  689  C   VAL A 156     4957   8221   9553   1811   2155   -386       C  
ATOM    690  O   VAL A 156      18.988   4.830  56.589  1.00 49.08           O  
ANISOU  690  O   VAL A 156     3764   6652   8230   1677   2114   -296       O  
ATOM    691  CB  VAL A 156      15.721   4.807  56.077  1.00 55.56           C  
ANISOU  691  CB  VAL A 156     3885   8143   9084   1807   2193   -432       C  
ATOM    692  CG1 VAL A 156      16.413   4.306  54.819  1.00 59.32           C  
ANISOU  692  CG1 VAL A 156     4465   8445   9629   1722   2059   -352       C  
ATOM    693  CG2 VAL A 156      14.486   3.972  56.374  1.00 58.19           C  
ANISOU  693  CG2 VAL A 156     3915   8758   9436   1699   2319   -436       C  
ATOM    694  N   LEU A 157      18.043   6.797  57.141  1.00 62.28           N  
ANISOU  694  N   LEU A 157     5342   8526   9795   2005   2085   -474       N  
ATOM    695  CA  LEU A 157      19.255   7.562  56.878  1.00 62.78           C  
ANISOU  695  CA  LEU A 157     5687   8353   9814   2057   1947   -466       C  
ATOM    696  C   LEU A 157      20.407   7.079  57.743  1.00 66.27           C  
ANISOU  696  C   LEU A 157     6351   8593  10236   1916   2016   -389       C  
ATOM    697  O   LEU A 157      21.492   6.780  57.236  1.00 70.69           O  
ANISOU  697  O   LEU A 157     7101   8951  10807   1821   1932   -313       O  
ATOM    698  CB  LEU A 157      18.990   9.049  57.119  1.00 60.14           C  
ANISOU  698  CB  LEU A 157     5371   8061   9418   2271   1882   -587       C  
ATOM    699  CG  LEU A 157      20.220   9.949  57.242  1.00 58.41           C  
ANISOU  699  CG  LEU A 157     5434   7579   9179   2308   1810   -560       C  
ATOM    700  CD1 LEU A 157      20.946  10.055  55.910  1.00 58.69           C  
ANISOU  700  CD1 LEU A 157     5597   7456   9246   2285   1656   -494       C  
ATOM    701  CD2 LEU A 157      19.831  11.325  57.763  1.00 60.53           C  
ANISOU  701  CD2 LEU A 157     5690   7880   9428   2498   1812   -670       C  
ATOM    702  N   PHE A 158      20.189   6.998  59.056  1.00 62.17           N  
ANISOU  702  N   PHE A 158     5809   8132   9681   1901   2170   -411       N  
ATOM    703  CA  PHE A 158      21.280   6.623  59.950  1.00 58.08           C  
ANISOU  703  CA  PHE A 158     5509   7424   9134   1783   2234   -345       C  
ATOM    704  C   PHE A 158      21.714   5.178  59.729  1.00 53.02           C  
ANISOU  704  C   PHE A 158     4892   6685   8568   1568   2291   -233       C  
ATOM    705  O   PHE A 158      22.916   4.882  59.720  1.00 55.66           O  
ANISOU  705  O   PHE A 158     5446   6799   8903   1473   2250   -162       O  
ATOM    706  CB  PHE A 158      20.871   6.863  61.403  1.00 68.07           C  
ANISOU  706  CB  PHE A 158     6740   8788  10337   1820   2390   -398       C  
ATOM    707  CG  PHE A 158      20.638   8.313  61.729  1.00 80.61           C  
ANISOU  707  CG  PHE A 158     8344  10427  11856   2021   2330   -513       C  
ATOM    708  CD1 PHE A 158      21.309   9.306  61.032  1.00 83.08           C  
ANISOU  708  CD1 PHE A 158     8808  10603  12157   2116   2154   -534       C  
ATOM    709  CD2 PHE A 158      19.752   8.683  62.726  1.00 89.22           C  
ANISOU  709  CD2 PHE A 158     9299  11695  12906   2106   2459   -600       C  
ATOM    710  CE1 PHE A 158      21.101  10.641  61.322  1.00 88.57           C  
ANISOU  710  CE1 PHE A 158     9519  11299  12834   2291   2133   -620       C  
ATOM    711  CE2 PHE A 158      19.539  10.018  63.022  1.00 94.63           C  
ANISOU  711  CE2 PHE A 158     9998  12412  13545   2288   2403   -717       C  
ATOM    712  CZ  PHE A 158      20.215  10.998  62.319  1.00 93.59           C  
ANISOU  712  CZ  PHE A 158    10019  12104  13435   2380   2251   -719       C  
ATOM    713  N   SER A 159      20.761   4.264  59.509  1.00 47.96           N  
ANISOU  713  N   SER A 159     4024   6210   7989   1482   2376   -221       N  
ATOM    714  CA  SER A 159      21.154   2.869  59.309  1.00 53.84           C  
ANISOU  714  CA  SER A 159     4791   6858   8806   1266   2423   -126       C  
ATOM    715  C   SER A 159      21.905   2.678  57.990  1.00 57.35           C  
ANISOU  715  C   SER A 159     5340   7132   9317   1230   2266    -70       C  
ATOM    716  O   SER A 159      22.927   1.970  57.938  1.00 59.99           O  
ANISOU  716  O   SER A 159     5848   7260   9686   1095   2259      7       O  
ATOM    717  CB  SER A 159      19.923   1.968  59.368  1.00 55.15           C  
ANISOU  717  CB  SER A 159     4684   7266   9006   1162   2532   -131       C  
ATOM    718  OG  SER A 159      19.303   2.035  60.641  1.00 50.50           O  
ANISOU  718  OG  SER A 159     4011   6833   8343   1168   2687   -174       O  
ATOM    719  N   THR A 160      21.419   3.309  56.917  1.00 56.56           N  
ANISOU  719  N   THR A 160     5142   7116   9230   1351   2139   -110       N  
ATOM    720  CA  THR A 160      22.100   3.234  55.631  1.00 55.76           C  
ANISOU  720  CA  THR A 160     5144   6868   9173   1327   1983    -64       C  
ATOM    721  C   THR A 160      23.474   3.884  55.705  1.00 53.98           C  
ANISOU  721  C   THR A 160     5210   6422   8879   1348   1887    -41       C  
ATOM    722  O   THR A 160      24.442   3.379  55.123  1.00 54.55           O  
ANISOU  722  O   THR A 160     5429   6317   8980   1237   1819     30       O  
ATOM    723  CB  THR A 160      21.240   3.900  54.555  1.00 50.81           C  
ANISOU  723  CB  THR A 160     4360   6396   8549   1470   1867   -123       C  
ATOM    724  OG1 THR A 160      19.945   3.289  54.535  1.00 56.42           O  
ANISOU  724  OG1 THR A 160     4782   7343   9312   1435   1954   -144       O  
ATOM    725  CG2 THR A 160      21.873   3.751  53.188  1.00 47.32           C  
ANISOU  725  CG2 THR A 160     4015   5819   8144   1434   1712    -75       C  
ATOM    726  N   ALA A 161      23.580   5.007  56.421  1.00 52.16           N  
ANISOU  726  N   ALA A 161     5059   6213   8548   1481   1874   -105       N  
ATOM    727  CA  ALA A 161      24.875   5.643  56.620  1.00 49.95           C  
ANISOU  727  CA  ALA A 161     5041   5757   8180   1478   1779    -89       C  
ATOM    728  C   ALA A 161      25.834   4.718  57.350  1.00 47.67           C  
ANISOU  728  C   ALA A 161     4898   5305   7909   1305   1870     -2       C  
ATOM    729  O   ALA A 161      27.021   4.665  57.018  1.00 50.71           O  
ANISOU  729  O   ALA A 161     5470   5539   8258   1222   1775     51       O  
ATOM    730  CB  ALA A 161      24.704   6.953  57.388  1.00 39.38           C  
ANISOU  730  CB  ALA A 161     3733   4458   6772   1639   1791   -165       C  
ATOM    731  N   LYS A 162      25.339   3.967  58.335  1.00 43.33           N  
ANISOU  731  N   LYS A 162     4261   4804   7400   1242   2051      9       N  
ATOM    732  CA  LYS A 162      26.208   3.030  59.041  1.00 41.70           C  
ANISOU  732  CA  LYS A 162     4196   4437   7211   1081   2143     87       C  
ATOM    733  C   LYS A 162      26.732   1.943  58.105  1.00 43.70           C  
ANISOU  733  C   LYS A 162     4482   4563   7560    929   2103    168       C  
ATOM    734  O   LYS A 162      27.945   1.681  58.044  1.00 43.23           O  
ANISOU  734  O   LYS A 162     4613   4329   7482    832   2055    232       O  
ATOM    735  CB  LYS A 162      25.470   2.412  60.230  1.00 38.34           C  
ANISOU  735  CB  LYS A 162     3662   4113   6792   1036   2341     72       C  
ATOM    736  CG  LYS A 162      26.117   1.134  60.736  1.00 53.59           C  
ANISOU  736  CG  LYS A 162     5700   5899   8764    848   2442    150       C  
ATOM    737  CD  LYS A 162      25.786   0.862  62.189  1.00 64.51           C  
ANISOU  737  CD  LYS A 162     7076   7350  10086    815   2613    130       C  
ATOM    738  CE  LYS A 162      26.869   0.008  62.837  1.00 72.63           C  
ANISOU  738  CE  LYS A 162     8317   8170  11109    672   2670    199       C  
ATOM    739  NZ  LYS A 162      26.589  -0.274  64.273  1.00 79.20           N  
ANISOU  739  NZ  LYS A 162     9164   9068  11861    630   2828    180       N  
ATOM    740  N   ILE A 163      25.829   1.290  57.368  1.00 49.62           N  
ANISOU  740  N   ILE A 163     5034   5415   8403    899   2118    164       N  
ATOM    741  CA  ILE A 163      26.280   0.176  56.535  1.00 34.37           C  
ANISOU  741  CA  ILE A 163     3128   3358   6573    749   2087    235       C  
ATOM    742  C   ILE A 163      27.190   0.672  55.414  1.00 37.08           C  
ANISOU  742  C   ILE A 163     3608   3589   6893    765   1908    262       C  
ATOM    743  O   ILE A 163      28.170   0.005  55.052  1.00 30.25           O  
ANISOU  743  O   ILE A 163     2872   2566   6058    636   1876    331       O  
ATOM    744  CB  ILE A 163      25.090  -0.634  55.991  1.00 36.12           C  
ANISOU  744  CB  ILE A 163     3097   3744   6881    695   2125    221       C  
ATOM    745  CG1 ILE A 163      25.602  -1.907  55.307  1.00 34.72           C  
ANISOU  745  CG1 ILE A 163     2965   3424   6803    525   2102    288       C  
ATOM    746  CG2 ILE A 163      24.250   0.201  55.043  1.00 37.23           C  
ANISOU  746  CG2 ILE A 163     3080   4048   7019    838   2018    165       C  
ATOM    747  CD1 ILE A 163      24.528  -2.899  54.935  1.00 36.42           C  
ANISOU  747  CD1 ILE A 163     2953   3815   7070    414   2135    281       C  
ATOM    748  N   TRP A 164      26.915   1.858  54.867  1.00 37.18           N  
ANISOU  748  N   TRP A 164     3598   3701   6828    916   1785    203       N  
ATOM    749  CA  TRP A 164      27.789   2.369  53.821  1.00 39.40           C  
ANISOU  749  CA  TRP A 164     4013   3918   7037    917   1604    215       C  
ATOM    750  C   TRP A 164      29.090   2.926  54.379  1.00 39.71           C  
ANISOU  750  C   TRP A 164     4267   3867   6953    882   1561    235       C  
ATOM    751  O   TRP A 164      30.086   2.955  53.655  1.00 43.00           O  
ANISOU  751  O   TRP A 164     4781   4206   7349    803   1486    283       O  
ATOM    752  CB  TRP A 164      27.065   3.416  52.974  1.00 42.69           C  
ANISOU  752  CB  TRP A 164     4345   4470   7407   1085   1481    139       C  
ATOM    753  CG  TRP A 164      26.139   2.786  51.975  1.00 51.74           C  
ANISOU  753  CG  TRP A 164     5298   5688   8673   1078   1476    145       C  
ATOM    754  CD1 TRP A 164      24.796   2.600  52.108  1.00 57.15           C  
ANISOU  754  CD1 TRP A 164     5742   6543   9429   1138   1560    105       C  
ATOM    755  CD2 TRP A 164      26.498   2.212  50.711  1.00 54.53           C  
ANISOU  755  CD2 TRP A 164     5671   5971   9078    991   1379    191       C  
ATOM    756  NE1 TRP A 164      24.289   1.972  50.996  1.00 57.99           N  
ANISOU  756  NE1 TRP A 164     5713   6691   9628   1094   1511    124       N  
ATOM    757  CE2 TRP A 164      25.315   1.719  50.124  1.00 57.51           C  
ANISOU  757  CE2 TRP A 164     5816   6466   9568   1009   1403    177       C  
ATOM    758  CE3 TRP A 164      27.703   2.077  50.014  1.00 52.85           C  
ANISOU  758  CE3 TRP A 164     5637   5639   8806    892   1269    234       C  
ATOM    759  CZ2 TRP A 164      25.302   1.102  48.875  1.00 57.38           C  
ANISOU  759  CZ2 TRP A 164     5756   6416   9630    941   1320    211       C  
ATOM    760  CZ3 TRP A 164      27.688   1.464  48.774  1.00 52.91           C  
ANISOU  760  CZ3 TRP A 164     5601   5618   8883    826   1197    264       C  
ATOM    761  CH2 TRP A 164      26.496   0.984  48.217  1.00 54.78           C  
ANISOU  761  CH2 TRP A 164     5620   5935   9258    854   1222    256       C  
ATOM    762  N   HIS A 165      29.118   3.334  55.650  1.00 35.73           N  
ANISOU  762  N   HIS A 165     3809   3371   6396    926   1647    212       N  
ATOM    763  CA  HIS A 165      30.390   3.610  56.305  1.00 41.11           C  
ANISOU  763  CA  HIS A 165     4668   3950   7000    857   1660    258       C  
ATOM    764  C   HIS A 165      31.242   2.351  56.357  1.00 45.44           C  
ANISOU  764  C   HIS A 165     5282   4424   7558    669   1692    331       C  
ATOM    765  O   HIS A 165      32.440   2.386  56.060  1.00 48.74           O  
ANISOU  765  O   HIS A 165     5789   4813   7916    586   1651    374       O  
ATOM    766  CB  HIS A 165      30.156   4.153  57.716  1.00 44.84           C  
ANISOU  766  CB  HIS A 165     5170   4447   7419    936   1754    218       C  
ATOM    767  CG  HIS A 165      30.065   5.645  57.788  1.00 51.51           C  
ANISOU  767  CG  HIS A 165     6037   5322   8212   1091   1709    165       C  
ATOM    768  ND1 HIS A 165      30.218   6.456  56.685  1.00 52.91           N  
ANISOU  768  ND1 HIS A 165     6218   5499   8385   1154   1591    155       N  
ATOM    769  CD2 HIS A 165      29.847   6.475  58.836  1.00 55.91           C  
ANISOU  769  CD2 HIS A 165     6618   5907   8716   1197   1765    115       C  
ATOM    770  CE1 HIS A 165      30.091   7.720  57.047  1.00 51.95           C  
ANISOU  770  CE1 HIS A 165     6124   5398   8217   1291   1576    101       C  
ATOM    771  NE2 HIS A 165      29.866   7.759  58.348  1.00 50.27           N  
ANISOU  771  NE2 HIS A 165     5922   5204   7975   1320   1679     76       N  
ATOM    772  N   LEU A 166      30.634   1.225  56.741  1.00 45.33           N  
ANISOU  772  N   LEU A 166     5194   4374   7654    602   1820    357       N  
ATOM    773  CA  LEU A 166      31.372  -0.040  56.744  1.00 43.72           C  
ANISOU  773  CA  LEU A 166     5035   4079   7497    422   1888    435       C  
ATOM    774  C   LEU A 166      31.886  -0.382  55.345  1.00 44.06           C  
ANISOU  774  C   LEU A 166     5051   4166   7523    355   1749    446       C  
ATOM    775  O   LEU A 166      33.051  -0.772  55.167  1.00 46.57           O  
ANISOU  775  O   LEU A 166     5416   4546   7733    275   1703    454       O  
ATOM    776  CB  LEU A 166      30.488  -1.166  57.279  1.00 43.90           C  
ANISOU  776  CB  LEU A 166     4982   3997   7702    370   2076    461       C  
ATOM    777  CG  LEU A 166      30.024  -1.067  58.733  1.00 48.02           C  
ANISOU  777  CG  LEU A 166     5521   4523   8200    424   2220    426       C  
ATOM    778  CD1 LEU A 166      29.274  -2.329  59.135  1.00 49.10           C  
ANISOU  778  CD1 LEU A 166     5573   4648   8436    360   2350    410       C  
ATOM    779  CD2 LEU A 166      31.204  -0.823  59.660  1.00 50.63           C  
ANISOU  779  CD2 LEU A 166     6037   4797   8403    369   2242    466       C  
ATOM    780  N   CYS A 167      31.020  -0.237  54.338  1.00 43.45           N  
ANISOU  780  N   CYS A 167     4868   4098   7543    417   1690    427       N  
ATOM    781  CA  CYS A 167      31.414  -0.532  52.962  1.00 40.56           C  
ANISOU  781  CA  CYS A 167     4481   3769   7162    364   1556    433       C  
ATOM    782  C   CYS A 167      32.554   0.372  52.503  1.00 37.10           C  
ANISOU  782  C   CYS A 167     4128   3373   6597    384   1459    425       C  
ATOM    783  O   CYS A 167      33.505  -0.089  51.854  1.00 30.26           O  
ANISOU  783  O   CYS A 167     3264   2543   5690    309   1417    437       O  
ATOM    784  CB  CYS A 167      30.205  -0.388  52.036  1.00 42.38           C  
ANISOU  784  CB  CYS A 167     4574   4004   7524    449   1522    412       C  
ATOM    785  SG  CYS A 167      30.540  -0.741  50.297  1.00 45.62           S  
ANISOU  785  SG  CYS A 167     4961   4439   7932    390   1364    421       S  
ATOM    786  N   ALA A 168      32.469   1.666  52.821  1.00 37.97           N  
ANISOU  786  N   ALA A 168     4288   3484   6656    504   1438    395       N  
ATOM    787  CA  ALA A 168      33.520   2.603  52.448  1.00 34.20           C  
ANISOU  787  CA  ALA A 168     3893   3020   6082    527   1366    391       C  
ATOM    788  C   ALA A 168      34.824   2.274  53.158  1.00 26.22           C  
ANISOU  788  C   ALA A 168     2961   2026   4976    442   1414    411       C  
ATOM    789  O   ALA A 168      35.900   2.405  52.572  1.00 26.30           O  
ANISOU  789  O   ALA A 168     3005   2071   4917    413   1351    409       O  
ATOM    790  CB  ALA A 168      33.085   4.035  52.757  1.00 24.65           C  
ANISOU  790  CB  ALA A 168     2717   1808   4842    682   1343    348       C  
ATOM    791  N   ILE A 169      34.750   1.837  54.417  1.00 23.38           N  
ANISOU  791  N   ILE A 169     2627   1652   4606    415   1522    422       N  
ATOM    792  CA  ILE A 169      35.957   1.425  55.129  1.00 21.31           C  
ANISOU  792  CA  ILE A 169     2429   1423   4244    353   1569    429       C  
ATOM    793  C   ILE A 169      36.626   0.272  54.398  1.00 20.15           C  
ANISOU  793  C   ILE A 169     2229   1337   4089    278   1539    425       C  
ATOM    794  O   ILE A 169      37.833   0.300  54.121  1.00 19.34           O  
ANISOU  794  O   ILE A 169     2170   1280   3897    270   1484    409       O  
ATOM    795  CB  ILE A 169      35.623   1.037  56.581  1.00 21.77           C  
ANISOU  795  CB  ILE A 169     2521   1454   4297    339   1696    439       C  
ATOM    796  CG1 ILE A 169      35.215   2.266  57.386  1.00 29.33           C  
ANISOU  796  CG1 ILE A 169     3547   2365   5234    439   1713    426       C  
ATOM    797  CG2 ILE A 169      36.806   0.336  57.230  1.00 20.83           C  
ANISOU  797  CG2 ILE A 169     2453   1386   4076    286   1741    431       C  
ATOM    798  CD1 ILE A 169      34.687   1.939  58.758  1.00 30.20           C  
ANISOU  798  CD1 ILE A 169     3688   2437   5351    437   1834    430       C  
ATOM    799  N   SER A 170      35.841  -0.756  54.065  1.00 21.79           N  
ANISOU  799  N   SER A 170     2343   1545   4391    239   1565    430       N  
ATOM    800  CA  SER A 170      36.396  -1.918  53.377  1.00 21.20           C  
ANISOU  800  CA  SER A 170     2244   1528   4283    207   1486    399       C  
ATOM    801  C   SER A 170      37.042  -1.518  52.052  1.00 21.56           C  
ANISOU  801  C   SER A 170     2263   1601   4328    207   1396    402       C  
ATOM    802  O   SER A 170      38.212  -1.840  51.792  1.00 24.02           O  
ANISOU  802  O   SER A 170     2615   1957   4554    200   1344    381       O  
ATOM    803  CB  SER A 170      35.298  -2.961  53.156  1.00 28.06           C  
ANISOU  803  CB  SER A 170     3048   2385   5230    190   1472    387       C  
ATOM    804  OG  SER A 170      35.844  -4.218  52.797  1.00 40.54           O  
ANISOU  804  OG  SER A 170     4630   3996   6777    176   1423    355       O  
ATOM    805  N   LEU A 171      36.297  -0.794  51.210  1.00 20.19           N  
ANISOU  805  N   LEU A 171     2055   1394   4223    228   1339    416       N  
ATOM    806  CA  LEU A 171      36.814  -0.417  49.897  1.00 18.78           C  
ANISOU  806  CA  LEU A 171     1877   1237   4023    236   1221    407       C  
ATOM    807  C   LEU A 171      38.030   0.497  50.004  1.00 24.46           C  
ANISOU  807  C   LEU A 171     2695   1974   4624    263   1181    393       C  
ATOM    808  O   LEU A 171      39.000   0.338  49.254  1.00 19.28           O  
ANISOU  808  O   LEU A 171     2055   1358   3912    246   1109    379       O  
ATOM    809  CB  LEU A 171      35.717   0.250  49.067  1.00 19.61           C  
ANISOU  809  CB  LEU A 171     1942   1296   4213    277   1165    414       C  
ATOM    810  CG  LEU A 171      34.842  -0.704  48.255  1.00 31.58           C  
ANISOU  810  CG  LEU A 171     3350   2808   5839    238   1143    422       C  
ATOM    811  CD1 LEU A 171      33.814   0.065  47.443  1.00 40.84           C  
ANISOU  811  CD1 LEU A 171     4498   3939   7081    306   1075    418       C  
ATOM    812  CD2 LEU A 171      35.707  -1.567  47.349  1.00 34.48           C  
ANISOU  812  CD2 LEU A 171     3694   3233   6174    191   1077    409       C  
ATOM    813  N   ASP A 172      37.994   1.467  50.921  1.00 27.47           N  
ANISOU  813  N   ASP A 172     3146   2323   4968    309   1223    396       N  
ATOM    814  CA  ASP A 172      39.098   2.407  51.057  1.00 18.72           C  
ANISOU  814  CA  ASP A 172     2132   1226   3756    338   1184    382       C  
ATOM    815  C   ASP A 172      40.362   1.706  51.530  1.00 17.80           C  
ANISOU  815  C   ASP A 172     2052   1160   3551    294   1201    371       C  
ATOM    816  O   ASP A 172      41.449   1.966  51.005  1.00 17.19           O  
ANISOU  816  O   ASP A 172     2015   1113   3404    291   1132    356       O  
ATOM    817  CB  ASP A 172      38.707   3.529  52.018  1.00 39.30           C  
ANISOU  817  CB  ASP A 172     4804   3784   6344    408   1226    382       C  
ATOM    818  CG  ASP A 172      39.689   4.682  52.003  1.00 51.55           C  
ANISOU  818  CG  ASP A 172     6447   5335   7802    450   1171    364       C  
ATOM    819  OD1 ASP A 172      39.812   5.347  50.952  1.00 57.81           O  
ANISOU  819  OD1 ASP A 172     7246   6125   8593    483   1082    351       O  
ATOM    820  OD2 ASP A 172      40.334   4.928  53.044  1.00 57.64           O  
ANISOU  820  OD2 ASP A 172     7289   6109   8503    452   1217    363       O  
ATOM    821  N   ARG A 173      40.242   0.801  52.504  1.00 22.49           N  
ANISOU  821  N   ARG A 173     2637   1762   4145    267   1288    374       N  
ATOM    822  CA  ARG A 173      41.417   0.068  52.962  1.00 18.49           C  
ANISOU  822  CA  ARG A 173     2176   1299   3551    244   1292    354       C  
ATOM    823  C   ARG A 173      41.969  -0.833  51.864  1.00 19.38           C  
ANISOU  823  C   ARG A 173     2248   1454   3663    217   1211    338       C  
ATOM    824  O   ARG A 173      43.191  -0.958  51.713  1.00 15.67           O  
ANISOU  824  O   ARG A 173     1827   1015   3110    211   1160    320       O  
ATOM    825  CB  ARG A 173      41.076  -0.740  54.211  1.00 17.30           C  
ANISOU  825  CB  ARG A 173     2034   1140   3400    233   1398    353       C  
ATOM    826  CG  ARG A 173      40.780   0.123  55.422  1.00 24.08           C  
ANISOU  826  CG  ARG A 173     2956   1959   4235    259   1479    367       C  
ATOM    827  CD  ARG A 173      40.503  -0.724  56.643  1.00 35.81           C  
ANISOU  827  CD  ARG A 173     4459   3436   5711    246   1586    362       C  
ATOM    828  NE  ARG A 173      41.619  -1.606  56.972  1.00 38.41           N  
ANISOU  828  NE  ARG A 173     4846   3800   5947    233   1555    329       N  
ATOM    829  CZ  ARG A 173      42.634  -1.263  57.757  1.00 38.79           C  
ANISOU  829  CZ  ARG A 173     4987   3856   5895    241   1569    321       C  
ATOM    830  NH1 ARG A 173      42.675  -0.054  58.299  1.00 37.60           N  
ANISOU  830  NH1 ARG A 173     4891   3683   5714    266   1591    338       N  
ATOM    831  NH2 ARG A 173      43.608  -2.128  58.000  1.00 42.54           N  
ANISOU  831  NH2 ARG A 173     5512   4354   6297    229   1540    294       N  
ATOM    832  N   TYR A 174      41.087  -1.461  51.081  1.00 16.41           N  
ANISOU  832  N   TYR A 174     1786   1073   3378    202   1195    344       N  
ATOM    833  CA  TYR A 174      41.551  -2.297  49.977  1.00 15.82           C  
ANISOU  833  CA  TYR A 174     1680   1029   3301    182   1111    330       C  
ATOM    834  C   TYR A 174      42.321  -1.472  48.949  1.00 15.40           C  
ANISOU  834  C   TYR A 174     1652    994   3207    188   1018    325       C  
ATOM    835  O   TYR A 174      43.468  -1.794  48.601  1.00 16.82           O  
ANISOU  835  O   TYR A 174     1870   1206   3314    179    963    308       O  
ATOM    836  CB  TYR A 174      40.355  -2.998  49.334  1.00 21.06           C  
ANISOU  836  CB  TYR A 174     2248   1677   4078    169   1108    339       C  
ATOM    837  CG  TYR A 174      40.702  -3.887  48.167  1.00 21.17           C  
ANISOU  837  CG  TYR A 174     2236   1715   4095    151   1017    327       C  
ATOM    838  CD1 TYR A 174      41.325  -5.111  48.363  1.00 27.55           C  
ANISOU  838  CD1 TYR A 174     3081   2534   4853    139   1002    308       C  
ATOM    839  CD2 TYR A 174      40.389  -3.510  46.868  1.00 18.72           C  
ANISOU  839  CD2 TYR A 174     1878   1405   3831    147    941    334       C  
ATOM    840  CE1 TYR A 174      41.640  -5.928  47.297  1.00 30.44           C  
ANISOU  840  CE1 TYR A 174     3439   2912   5216    124    915    300       C  
ATOM    841  CE2 TYR A 174      40.697  -4.322  45.795  1.00 28.76           C  
ANISOU  841  CE2 TYR A 174     3131   2694   5101    132    859    324       C  
ATOM    842  CZ  TYR A 174      41.321  -5.531  46.015  1.00 30.67           C  
ANISOU  842  CZ  TYR A 174     3413   2948   5293    120    847    309       C  
ATOM    843  OH  TYR A 174      41.631  -6.346  44.951  1.00 28.05           O  
ANISOU  843  OH  TYR A 174     3079   2625   4952    105    762    302       O  
ATOM    844  N   VAL A 175      41.706  -0.391  48.463  1.00 25.90           N  
ANISOU  844  N   VAL A 175     2969   2293   4577    209    997    339       N  
ATOM    845  CA  VAL A 175      42.370   0.485  47.500  1.00 20.88           C  
ANISOU  845  CA  VAL A 175     2371   1664   3900    224    910    330       C  
ATOM    846  C   VAL A 175      43.681   1.014  48.071  1.00 21.95           C  
ANISOU  846  C   VAL A 175     2594   1817   3928    233    906    316       C  
ATOM    847  O   VAL A 175      44.671   1.173  47.345  1.00 14.70           O  
ANISOU  847  O   VAL A 175     1705    924   2956    229    837    302       O  
ATOM    848  CB  VAL A 175      41.423   1.627  47.082  1.00 22.76           C  
ANISOU  848  CB  VAL A 175     2604   1853   4191    264    890    341       C  
ATOM    849  CG1 VAL A 175      42.144   2.625  46.191  1.00 20.82           C  
ANISOU  849  CG1 VAL A 175     2414   1606   3890    291    805    327       C  
ATOM    850  CG2 VAL A 175      40.200   1.066  46.372  1.00 16.77           C  
ANISOU  850  CG2 VAL A 175     1755   1077   3540    253    879    353       C  
ATOM    851  N   ALA A 176      43.717   1.276  49.381  1.00 27.29           N  
ANISOU  851  N   ALA A 176     3315   2481   4574    246    980    320       N  
ATOM    852  CA  ALA A 176      44.942   1.757  50.010  1.00 15.21           C  
ANISOU  852  CA  ALA A 176     1868    964   2945    254    976    307       C  
ATOM    853  C   ALA A 176      46.046   0.713  49.924  1.00 26.60           C  
ANISOU  853  C   ALA A 176     3321   2454   4333    224    949    290       C  
ATOM    854  O   ALA A 176      47.140   0.993  49.422  1.00 29.50           O  
ANISOU  854  O   ALA A 176     3724   2843   4641    222    886    276       O  
ATOM    855  CB  ALA A 176      44.670   2.138  51.465  1.00 15.74           C  
ANISOU  855  CB  ALA A 176     1983   1005   2993    274   1064    315       C  
ATOM    856  N   ILE A 177      45.767  -0.512  50.380  1.00 20.52           N  
ANISOU  856  N   ILE A 177     2523   1694   3581    204    991    288       N  
ATOM    857  CA  ILE A 177      46.781  -1.563  50.352  1.00 13.76           C  
ANISOU  857  CA  ILE A 177     1691    870   2669    185    958    270       C  
ATOM    858  C   ILE A 177      47.169  -1.941  48.932  1.00 23.26           C  
ANISOU  858  C   ILE A 177     2860   2096   3881    171    868    263       C  
ATOM    859  O   ILE A 177      48.180  -2.623  48.736  1.00 57.88           O  
ANISOU  859  O   ILE A 177     7275   6506   8212    158    824    248       O  
ATOM    860  CB  ILE A 177      46.345  -2.818  51.136  1.00 13.96           C  
ANISOU  860  CB  ILE A 177     1709    885   2707    174   1014    266       C  
ATOM    861  CG1 ILE A 177      45.327  -3.640  50.346  1.00 20.60           C  
ANISOU  861  CG1 ILE A 177     2472   1718   3638    161   1002    272       C  
ATOM    862  CG2 ILE A 177      45.824  -2.437  52.515  1.00 14.52           C  
ANISOU  862  CG2 ILE A 177     1812    929   2775    188   1113    274       C  
ATOM    863  CD1 ILE A 177      45.064  -4.998  50.946  1.00 15.60           C  
ANISOU  863  CD1 ILE A 177     1850   1069   3009    149   1034    264       C  
ATOM    864  N   GLN A 178      46.391  -1.509  47.936  1.00 28.95           N  
ANISOU  864  N   GLN A 178     3527   2806   4668    173    838    273       N  
ATOM    865  CA  GLN A 178      46.822  -1.680  46.552  1.00 13.04           C  
ANISOU  865  CA  GLN A 178     1493    811   2651    162    751    266       C  
ATOM    866  C   GLN A 178      48.004  -0.771  46.221  1.00 19.14           C  
ANISOU  866  C   GLN A 178     2324   1598   3352    171    703    255       C  
ATOM    867  O   GLN A 178      48.872  -1.150  45.425  1.00 19.38           O  
ANISOU  867  O   GLN A 178     2364   1653   3347    159    642    243       O  
ATOM    868  CB  GLN A 178      45.664  -1.422  45.591  1.00 28.22           C  
ANISOU  868  CB  GLN A 178     3349   2712   4660    164    728    279       C  
ATOM    869  CG  GLN A 178      44.514  -2.401  45.734  1.00 30.65           C  
ANISOU  869  CG  GLN A 178     3589   3006   5049    152    765    289       C  
ATOM    870  CD  GLN A 178      44.931  -3.829  45.461  1.00 33.93           C  
ANISOU  870  CD  GLN A 178     4003   3441   5448    132    734    278       C  
ATOM    871  OE1 GLN A 178      44.493  -4.755  46.142  1.00 46.75           O  
ANISOU  871  OE1 GLN A 178     5618   5053   7093    126    778    278       O  
ATOM    872  NE2 GLN A 178      45.777  -4.017  44.456  1.00 12.89           N  
ANISOU  872  NE2 GLN A 178     1357    800   2742    123    657    267       N  
ATOM    873  N   ASN A 179      48.053   0.419  46.809  1.00 20.91           N  
ANISOU  873  N   ASN A 179     2590   1801   3554    194    728    259       N  
ATOM    874  CA  ASN A 179      49.085   1.410  46.499  1.00 16.45           C  
ANISOU  874  CA  ASN A 179     2082   1240   2928    206    681    249       C  
ATOM    875  C   ASN A 179      50.442   0.945  47.018  1.00 12.26           C  
ANISOU  875  C   ASN A 179     1597    740   2321    193    673    234       C  
ATOM    876  O   ASN A 179      50.576   0.676  48.218  1.00 12.35           O  
ANISOU  876  O   ASN A 179     1637    751   2307    194    726    234       O  
ATOM    877  CB  ASN A 179      48.695   2.744  47.141  1.00 26.99           C  
ANISOU  877  CB  ASN A 179     3459   2536   4261    240    711    256       C  
ATOM    878  CG  ASN A 179      49.604   3.891  46.743  1.00 25.98           C  
ANISOU  878  CG  ASN A 179     3391   2401   4080    259    658    245       C  
ATOM    879  OD1 ASN A 179      50.448   3.762  45.861  1.00 27.87           O  
ANISOU  879  OD1 ASN A 179     3634   2664   4292    245    599    233       O  
ATOM    880  ND2 ASN A 179      49.434   5.029  47.408  1.00 24.72           N  
ANISOU  880  ND2 ASN A 179     3282   2204   3908    294    679    247       N  
ATOM    881  N   PRO A 180      51.466   0.835  46.163  1.00 18.01           N  
ANISOU  881  N   PRO A 180     2338   1493   3013    183    609    221       N  
ATOM    882  CA  PRO A 180      52.747   0.251  46.597  1.00 11.28           C  
ANISOU  882  CA  PRO A 180     1524    668   2096    171    595    208       C  
ATOM    883  C   PRO A 180      53.517   1.077  47.616  1.00 11.37           C  
ANISOU  883  C   PRO A 180     1598    672   2051    184    615    203       C  
ATOM    884  O   PRO A 180      54.562   0.614  48.087  1.00 11.05           O  
ANISOU  884  O   PRO A 180     1590    649   1959    175    604    193       O  
ATOM    885  CB  PRO A 180      53.539   0.138  45.284  1.00 10.83           C  
ANISOU  885  CB  PRO A 180     1461    632   2022    160    522    199       C  
ATOM    886  CG  PRO A 180      52.922   1.148  44.382  1.00 11.11           C  
ANISOU  886  CG  PRO A 180     1483    646   2092    174    498    205       C  
ATOM    887  CD  PRO A 180      51.462   1.131  44.721  1.00 32.71           C  
ANISOU  887  CD  PRO A 180     4180   3357   4892    182    545    219       C  
ATOM    888  N   ILE A 181      53.062   2.277  47.969  1.00 29.83           N  
ANISOU  888  N   ILE A 181     3958   2979   4396    206    637    210       N  
ATOM    889  CA  ILE A 181      53.740   3.068  48.990  1.00 12.02           C  
ANISOU  889  CA  ILE A 181     1768    711   2088    221    655    205       C  
ATOM    890  C   ILE A 181      52.772   3.356  50.129  1.00 12.63           C  
ANISOU  890  C   ILE A 181     1859    758   2181    238    729    217       C  
ATOM    891  O   ILE A 181      52.870   4.394  50.794  1.00 61.18           O  
ANISOU  891  O   ILE A 181     8061   6880   8306    262    745    218       O  
ATOM    892  CB  ILE A 181      54.316   4.372  48.408  1.00 12.12           C  
ANISOU  892  CB  ILE A 181     1816    708   2081    238    606    200       C  
ATOM    893  CG1 ILE A 181      53.231   5.158  47.670  1.00 19.13           C  
ANISOU  893  CG1 ILE A 181     2685   1563   3020    260    597    209       C  
ATOM    894  CG2 ILE A 181      55.486   4.078  47.484  1.00 11.52           C  
ANISOU  894  CG2 ILE A 181     1737    663   1978    219    541    187       C  
ATOM    895  CD1 ILE A 181      53.717   6.475  47.113  1.00 14.79           C  
ANISOU  895  CD1 ILE A 181     2180    988   2452    284    547    201       C  
ATOM    896  N   HIS A 182      51.837   2.436  50.371  1.00 12.74           N  
ANISOU  896  N   HIS A 182     1829    773   2238    229    776    226       N  
ATOM    897  CA  HIS A 182      50.796   2.641  51.371  1.00 29.16           C  
ANISOU  897  CA  HIS A 182     3914   2822   4344    244    854    240       C  
ATOM    898  C   HIS A 182      51.284   2.426  52.798  1.00 16.62           C  
ANISOU  898  C   HIS A 182     2387   1232   2697    245    905    235       C  
ATOM    899  O   HIS A 182      50.471   2.472  53.727  1.00 13.97           O  
ANISOU  899  O   HIS A 182     2062    871   2376    257    979    246       O  
ATOM    900  CB  HIS A 182      49.599   1.730  51.090  1.00 13.50           C  
ANISOU  900  CB  HIS A 182     1858    837   2434    232    888    251       C  
ATOM    901  CG  HIS A 182      49.872   0.276  51.315  1.00 26.01           C  
ANISOU  901  CG  HIS A 182     3428   2447   4008    207    897    243       C  
ATOM    902  ND1 HIS A 182      50.257  -0.574  50.301  1.00 29.07           N  
ANISOU  902  ND1 HIS A 182     3780   2861   4404    187    837    235       N  
ATOM    903  CD2 HIS A 182      49.797  -0.483  52.434  1.00 26.23           C  
ANISOU  903  CD2 HIS A 182     3480   2470   4015    202    956    241       C  
ATOM    904  CE1 HIS A 182      50.417  -1.792  50.787  1.00 12.51           C  
ANISOU  904  CE1 HIS A 182     1689    771   2291    173    853    228       C  
ATOM    905  NE2 HIS A 182      50.144  -1.763  52.079  1.00 21.61           N  
ANISOU  905  NE2 HIS A 182     2879   1905   3426    182    925    231       N  
ATOM    906  N   HIS A 183      52.577   2.188  53.000  1.00 13.01           N  
ANISOU  906  N   HIS A 183     1971    797   2174    234    868    220       N  
ATOM    907  CA  HIS A 183      53.151   2.146  54.336  1.00 19.78           C  
ANISOU  907  CA  HIS A 183     2898   1648   2968    238    904    214       C  
ATOM    908  C   HIS A 183      53.901   3.427  54.681  1.00 28.25           C  
ANISOU  908  C   HIS A 183     4035   2704   3993    257    880    210       C  
ATOM    909  O   HIS A 183      54.601   3.474  55.700  1.00 29.05           O  
ANISOU  909  O   HIS A 183     4202   2802   4035    259    893    202       O  
ATOM    910  CB  HIS A 183      54.066   0.929  54.482  1.00 20.72           C  
ANISOU  910  CB  HIS A 183     3029   1796   3049    215    877    201       C  
ATOM    911  CG  HIS A 183      53.330  -0.338  54.790  1.00 30.89           C  
ANISOU  911  CG  HIS A 183     4291   3083   4363    203    922    203       C  
ATOM    912  ND1 HIS A 183      53.007  -0.718  56.075  1.00 29.02           N  
ANISOU  912  ND1 HIS A 183     4099   2825   4100    206    991    203       N  
ATOM    913  CD2 HIS A 183      52.849  -1.310  53.979  1.00 28.83           C  
ANISOU  913  CD2 HIS A 183     3970   2833   4150    188    905    204       C  
ATOM    914  CE1 HIS A 183      52.360  -1.869  56.043  1.00 25.27           C  
ANISOU  914  CE1 HIS A 183     3594   2348   3660    193   1016    204       C  
ATOM    915  NE2 HIS A 183      52.253  -2.251  54.783  1.00 22.81           N  
ANISOU  915  NE2 HIS A 183     3218   2055   3395    182    963    204       N  
ATOM    916  N   SER A 184      53.758   4.467  53.862  1.00 13.46           N  
ANISOU  916  N   SER A 184     2152    817   2146    273    843    212       N  
ATOM    917  CA  SER A 184      54.363   5.755  54.153  1.00 32.99           C  
ANISOU  917  CA  SER A 184     4688   3265   4580    296    820    206       C  
ATOM    918  C   SER A 184      53.580   6.474  55.242  1.00 35.61           C  
ANISOU  918  C   SER A 184     5068   3554   4908    327    885    216       C  
ATOM    919  O   SER A 184      52.368   6.292  55.399  1.00 34.15           O  
ANISOU  919  O   SER A 184     4853   3351   4770    337    940    231       O  
ATOM    920  CB  SER A 184      54.422   6.631  52.899  1.00 39.85           C  
ANISOU  920  CB  SER A 184     5538   4126   5477    308    758    204       C  
ATOM    921  OG  SER A 184      53.139   7.113  52.542  1.00 47.70           O  
ANISOU  921  OG  SER A 184     6506   5089   6529    332    779    216       O  
ATOM    922  N   ARG A 185      54.293   7.305  55.999  1.00 37.70           N  
ANISOU  922  N   ARG A 185     5410   3798   5117    344    879    209       N  
ATOM    923  CA  ARG A 185      53.695   8.031  57.111  1.00 36.66           C  
ANISOU  923  CA  ARG A 185     5338   3621   4970    378    938    216       C  
ATOM    924  C   ARG A 185      52.767   9.154  56.658  1.00 29.56           C  
ANISOU  924  C   ARG A 185     4437   2677   4118    420    935    222       C  
ATOM    925  O   ARG A 185      52.031   9.694  57.488  1.00 39.65           O  
ANISOU  925  O   ARG A 185     5755   3912   5397    456    989    230       O  
ATOM    926  CB  ARG A 185      54.805   8.594  57.998  1.00 51.73           C  
ANISOU  926  CB  ARG A 185     7334   5519   6803    384    921    203       C  
ATOM    927  CG  ARG A 185      55.922   9.270  57.216  1.00 59.03           C  
ANISOU  927  CG  ARG A 185     8267   6450   7712    381    837    189       C  
ATOM    928  CD  ARG A 185      57.252   9.196  57.958  1.00 68.61           C  
ANISOU  928  CD  ARG A 185     9539   7674   8856    366    812    175       C  
ATOM    929  NE  ARG A 185      58.224  10.159  57.447  1.00 75.69           N  
ANISOU  929  NE  ARG A 185    10459   8560   9738    372    744    163       N  
ATOM    930  CZ  ARG A 185      58.279  11.430  57.831  1.00 81.58           C  
ANISOU  930  CZ  ARG A 185    11270   9259  10466    405    739    159       C  
ATOM    931  NH1 ARG A 185      57.417  11.888  58.729  1.00 82.21           N  
ANISOU  931  NH1 ARG A 185    11399   9300  10539    438    797    166       N  
ATOM    932  NH2 ARG A 185      59.191  12.245  57.319  1.00 87.03           N  
ANISOU  932  NH2 ARG A 185    11980   9940  11148    407    678    147       N  
ATOM    933  N   PHE A 186      52.782   9.517  55.377  1.00 38.48           N  
ANISOU  933  N   PHE A 186     5525   3810   5284    423    873    218       N  
ATOM    934  CA  PHE A 186      52.042  10.676  54.888  1.00 42.84           C  
ANISOU  934  CA  PHE A 186     6087   4314   5875    472    854    219       C  
ATOM    935  C   PHE A 186      50.616  10.267  54.528  1.00 46.30           C  
ANISOU  935  C   PHE A 186     6462   4743   6388    483    889    234       C  
ATOM    936  O   PHE A 186      50.358   9.752  53.438  1.00 42.15           O  
ANISOU  936  O   PHE A 186     5870   4240   5906    463    856    237       O  
ATOM    937  CB  PHE A 186      52.764  11.297  53.700  1.00 41.76           C  
ANISOU  937  CB  PHE A 186     5946   4180   5739    472    770    206       C  
ATOM    938  CG  PHE A 186      54.201  11.642  53.977  1.00 32.77           C  
ANISOU  938  CG  PHE A 186     4860   3053   4538    457    734    192       C  
ATOM    939  CD1 PHE A 186      54.536  12.836  54.592  1.00 23.23           C  
ANISOU  939  CD1 PHE A 186     3730   1800   3296    493    728    183       C  
ATOM    940  CD2 PHE A 186      55.217  10.767  53.634  1.00 42.07           C  
ANISOU  940  CD2 PHE A 186     6010   4283   5693    409    704    187       C  
ATOM    941  CE1 PHE A 186      55.862  13.152  54.853  1.00 27.73           C  
ANISOU  941  CE1 PHE A 186     4346   2377   3812    477    694    171       C  
ATOM    942  CE2 PHE A 186      56.539  11.079  53.891  1.00 37.39           C  
ANISOU  942  CE2 PHE A 186     5461   3698   5048    397    669    174       C  
ATOM    943  CZ  PHE A 186      56.862  12.270  54.500  1.00 15.90           C  
ANISOU  943  CZ  PHE A 186     2814    931   2295    429    664    167       C  
ATOM    944  N   ASN A 187      49.680  10.510  55.446  1.00 65.51           N  
ANISOU  944  N   ASN A 187     8918   7138   8837    518    955    243       N  
ATOM    945  CA  ASN A 187      48.256  10.303  55.210  1.00 75.59           C  
ANISOU  945  CA  ASN A 187    10138   8393  10188    541    990    257       C  
ATOM    946  C   ASN A 187      47.537  11.631  55.402  1.00 78.78           C  
ANISOU  946  C   ASN A 187    10588   8733  10613    622    985    249       C  
ATOM    947  O   ASN A 187      47.840  12.374  56.341  1.00 81.07           O  
ANISOU  947  O   ASN A 187    10954   8992  10856    655   1006    241       O  
ATOM    948  CB  ASN A 187      47.675   9.251  56.163  1.00 79.59           C  
ANISOU  948  CB  ASN A 187    10621   8911  10706    514   1081    274       C  
ATOM    949  CG  ASN A 187      48.447   7.943  56.134  1.00 84.22           C  
ANISOU  949  CG  ASN A 187    11177   9558  11265    447   1086    274       C  
ATOM    950  OD1 ASN A 187      48.930   7.517  55.086  1.00 86.05           O  
ANISOU  950  OD1 ASN A 187    11363   9826  11507    417   1026    268       O  
ATOM    951  ND2 ASN A 187      48.566   7.301  57.291  1.00 88.50           N  
ANISOU  951  ND2 ASN A 187    11748  10107  11770    428   1154    279       N  
ATOM    952  N   SER A 188      46.592  11.936  54.516  1.00 76.22           N  
ANISOU  952  N   SER A 188    10218   8386  10356    662    954    247       N  
ATOM    953  CA  SER A 188      45.891  13.210  54.580  1.00 70.54           C  
ANISOU  953  CA  SER A 188     9537   7605   9659    755    938    230       C  
ATOM    954  C   SER A 188      44.586  13.059  55.352  1.00 68.33           C  
ANISOU  954  C   SER A 188     9237   7297   9428    802   1011    236       C  
ATOM    955  O   SER A 188      43.779  12.170  55.064  1.00 69.54           O  
ANISOU  955  O   SER A 188     9314   7467   9641    780   1039    252       O  
ATOM    956  CB  SER A 188      45.608  13.747  53.178  1.00 66.61           C  
ANISOU  956  CB  SER A 188     9011   7095   9204    790    853    217       C  
ATOM    957  OG  SER A 188      44.849  14.943  53.231  1.00 65.25           O  
ANISOU  957  OG  SER A 188     8870   6863   9059    894    835    194       O  
ATOM    958  N   ARG A 189      44.395  13.939  56.336  1.00 68.01           N  
ANISOU  958  N   ARG A 189     9263   7212   9365    870   1042    222       N  
ATOM    959  CA  ARG A 189      43.161  13.991  57.115  1.00 69.47           C  
ANISOU  959  CA  ARG A 189     9436   7366   9595    936   1110    219       C  
ATOM    960  C   ARG A 189      41.995  14.514  56.279  1.00 70.26           C  
ANISOU  960  C   ARG A 189     9481   7441   9773   1027   1067    196       C  
ATOM    961  O   ARG A 189      40.871  13.993  56.361  1.00 68.71           O  
ANISOU  961  O   ARG A 189     9217   7246   9642   1053   1109    198       O  
ATOM    962  CB  ARG A 189      43.416  14.845  58.356  1.00 72.86           C  
ANISOU  962  CB  ARG A 189     9960   7756   9969    988   1148    204       C  
ATOM    963  CG  ARG A 189      42.267  15.080  59.304  1.00 82.46           C  
ANISOU  963  CG  ARG A 189    11177   8937  11218   1072   1219    190       C  
ATOM    964  CD  ARG A 189      42.739  16.067  60.371  1.00 92.99           C  
ANISOU  964  CD  ARG A 189    12618  10231  12485   1123   1239    170       C  
ATOM    965  NE  ARG A 189      41.735  16.379  61.381  1.00104.87           N  
ANISOU  965  NE  ARG A 189    14133  11702  14010   1213   1310    148       N  
ATOM    966  CZ  ARG A 189      41.997  17.057  62.494  1.00114.32           C  
ANISOU  966  CZ  ARG A 189    15422  12864  15150   1256   1347    131       C  
ATOM    967  NH1 ARG A 189      43.227  17.492  62.733  1.00116.96           N  
ANISOU  967  NH1 ARG A 189    15843  13190  15405   1216   1317    137       N  
ATOM    968  NH2 ARG A 189      41.034  17.298  63.371  1.00118.62           N  
ANISOU  968  NH2 ARG A 189    15969  13385  15718   1344   1415    104       N  
ATOM    969  N   THR A 190      42.252  15.543  55.466  1.00 72.67           N  
ANISOU  969  N   THR A 190     9812   7723  10075   1079    983    171       N  
ATOM    970  CA  THR A 190      41.191  16.190  54.699  1.00 77.51           C  
ANISOU  970  CA  THR A 190    10383   8312  10756   1184    934    140       C  
ATOM    971  C   THR A 190      40.557  15.241  53.690  1.00 72.03           C  
ANISOU  971  C   THR A 190     9594   7651  10124   1149    913    155       C  
ATOM    972  O   THR A 190      39.342  15.286  53.469  1.00 72.38           O  
ANISOU  972  O   THR A 190     9576   7689  10235   1231    912    135       O  
ATOM    973  CB  THR A 190      41.749  17.426  53.987  1.00 88.83           C  
ANISOU  973  CB  THR A 190    11870   9712  12169   1232    848    114       C  
ATOM    974  OG1 THR A 190      42.285  18.333  54.956  1.00 95.92           O  
ANISOU  974  OG1 THR A 190    12857  10574  13013   1266    871    100       O  
ATOM    975  CG2 THR A 190      40.664  18.140  53.194  1.00 93.08           C  
ANISOU  975  CG2 THR A 190    12367  10224  12777   1351    792     77       C  
ATOM    976  N   LYS A 191      41.357  14.373  53.071  1.00 70.59           N  
ANISOU  976  N   LYS A 191     9392   7507   9920   1036    894    185       N  
ATOM    977  CA  LYS A 191      40.806  13.418  52.113  1.00 68.22           C  
ANISOU  977  CA  LYS A 191     9006   7238   9678    995    876    201       C  
ATOM    978  C   LYS A 191      39.839  12.451  52.789  1.00 62.74           C  
ANISOU  978  C   LYS A 191     8246   6556   9038    982    962    219       C  
ATOM    979  O   LYS A 191      38.757  12.167  52.258  1.00 59.50           O  
ANISOU  979  O   LYS A 191     7760   6147   8700   1023    953    213       O  
ATOM    980  CB  LYS A 191      41.946  12.681  51.411  1.00 68.41           C  
ANISOU  980  CB  LYS A 191     9025   7305   9663    881    844    223       C  
ATOM    981  CG  LYS A 191      42.803  13.627  50.584  1.00 73.61           C  
ANISOU  981  CG  LYS A 191     9738   7952  10280    899    756    204       C  
ATOM    982  CD  LYS A 191      43.947  12.937  49.870  1.00 77.31           C  
ANISOU  982  CD  LYS A 191    10197   8468  10710    800    723    218       C  
ATOM    983  CE  LYS A 191      44.816  13.971  49.168  1.00 82.92           C  
ANISOU  983  CE  LYS A 191    10967   9160  11380    822    643    198       C  
ATOM    984  NZ  LYS A 191      44.003  15.054  48.543  1.00 87.97           N  
ANISOU  984  NZ  LYS A 191    11620   9746  12059    926    585    173       N  
ATOM    985  N   ALA A 192      40.219  11.925  53.956  1.00 64.24           N  
ANISOU  985  N   ALA A 192     8462   6754   9194    926   1045    239       N  
ATOM    986  CA  ALA A 192      39.322  11.046  54.699  1.00 62.85           C  
ANISOU  986  CA  ALA A 192     8230   6582   9068    912   1135    255       C  
ATOM    987  C   ALA A 192      38.044  11.775  55.092  1.00 65.05           C  
ANISOU  987  C   ALA A 192     8488   6831   9399   1047   1154    220       C  
ATOM    988  O   ALA A 192      36.945  11.206  55.019  1.00 60.59           O  
ANISOU  988  O   ALA A 192     7838   6276   8909   1071   1186    217       O  
ATOM    989  CB  ALA A 192      40.030  10.498  55.936  1.00 60.28           C  
ANISOU  989  CB  ALA A 192     7956   6266   8684    841   1219    278       C  
ATOM    990  N   PHE A 193      38.166  13.038  55.514  1.00 71.50           N  
ANISOU  990  N   PHE A 193     9372   7616  10177   1143   1134    184       N  
ATOM    991  CA  PHE A 193      36.973  13.805  55.868  1.00 63.72           C  
ANISOU  991  CA  PHE A 193     8357   6617   9238   1291   1147    134       C  
ATOM    992  C   PHE A 193      36.055  13.983  54.662  1.00 47.81           C  
ANISOU  992  C   PHE A 193     6256   4617   7291   1370   1074    105       C  
ATOM    993  O   PHE A 193      34.827  13.877  54.782  1.00 46.89           O  
ANISOU  993  O   PHE A 193     6052   4526   7238   1461   1102     73       O  
ATOM    994  CB  PHE A 193      37.370  15.160  56.452  1.00 61.16           C  
ANISOU  994  CB  PHE A 193     8123   6254   8859   1377   1131     98       C  
ATOM    995  CG  PHE A 193      37.863  15.089  57.870  1.00 73.30           C  
ANISOU  995  CG  PHE A 193     9735   7777  10339   1344   1216    112       C  
ATOM    996  CD1 PHE A 193      37.727  13.923  58.607  1.00 75.69           C  
ANISOU  996  CD1 PHE A 193    10013   8098  10646   1264   1306    147       C  
ATOM    997  CD2 PHE A 193      38.453  16.189  58.469  1.00 83.18           C  
ANISOU  997  CD2 PHE A 193    11083   8992  11531   1394   1207     89       C  
ATOM    998  CE1 PHE A 193      38.178  13.854  59.912  1.00 80.54           C  
ANISOU  998  CE1 PHE A 193    10703   8697  11202   1236   1383    158       C  
ATOM    999  CE2 PHE A 193      38.904  16.127  59.774  1.00 87.71           C  
ANISOU  999  CE2 PHE A 193    11729   9551  12044   1366   1282    101       C  
ATOM   1000  CZ  PHE A 193      38.766  14.957  60.496  1.00 86.13           C  
ANISOU 1000  CZ  PHE A 193    11509   9371  11845   1289   1370    135       C  
ATOM   1001  N   LEU A 194      36.635  14.262  53.493  1.00 35.78           N  
ANISOU 1001  N   LEU A 194     4752   3090   5754   1344    981    111       N  
ATOM   1002  CA  LEU A 194      35.833  14.402  52.282  1.00 44.69           C  
ANISOU 1002  CA  LEU A 194     5809   4232   6940   1416    905     87       C  
ATOM   1003  C   LEU A 194      35.131  13.094  51.933  1.00 50.25           C  
ANISOU 1003  C   LEU A 194     6412   4975   7708   1357    938    114       C  
ATOM   1004  O   LEU A 194      33.969  13.101  51.508  1.00 53.82           O  
ANISOU 1004  O   LEU A 194     6773   5455   8223   1454    921     81       O  
ATOM   1005  CB  LEU A 194      36.705  14.881  51.122  1.00 55.37           C  
ANISOU 1005  CB  LEU A 194     7213   5567   8257   1384    805     92       C  
ATOM   1006  CG  LEU A 194      37.299  16.283  51.284  1.00 62.59           C  
ANISOU 1006  CG  LEU A 194     8217   6438   9125   1452    761     60       C  
ATOM   1007  CD1 LEU A 194      38.237  16.618  50.134  1.00 64.80           C  
ANISOU 1007  CD1 LEU A 194     8544   6706   9373   1404    670     70       C  
ATOM   1008  CD2 LEU A 194      36.199  17.324  51.411  1.00 68.00           C  
ANISOU 1008  CD2 LEU A 194     8873   7106   9859   1626    742     -3       C  
ATOM   1009  N   LYS A 195      35.819  11.961  52.103  1.00 51.01           N  
ANISOU 1009  N   LYS A 195     6512   5079   7789   1205    983    168       N  
ATOM   1010  CA  LYS A 195      35.171  10.673  51.856  1.00 48.68           C  
ANISOU 1010  CA  LYS A 195     6121   4811   7564   1138   1021    196       C  
ATOM   1011  C   LYS A 195      33.996  10.458  52.804  1.00 46.87           C  
ANISOU 1011  C   LYS A 195     5823   4597   7389   1212   1106    173       C  
ATOM   1012  O   LYS A 195      32.935   9.966  52.396  1.00 47.47           O  
ANISOU 1012  O   LYS A 195     5791   4707   7540   1250   1109    160       O  
ATOM   1013  CB  LYS A 195      36.171   9.523  51.996  1.00 25.33           C  
ANISOU 1013  CB  LYS A 195     3181   1863   4580    968   1061    250       C  
ATOM   1014  CG  LYS A 195      37.370   9.576  51.069  1.00 30.83           C  
ANISOU 1014  CG  LYS A 195     3923   2571   5221    895    986    263       C  
ATOM   1015  CD  LYS A 195      38.433   8.583  51.523  1.00 27.58           C  
ANISOU 1015  CD  LYS A 195     3527   2187   4764    760   1036    297       C  
ATOM   1016  CE  LYS A 195      39.764   8.820  50.831  1.00 30.13           C  
ANISOU 1016  CE  LYS A 195     3901   2533   5014    713    967    295       C  
ATOM   1017  NZ  LYS A 195      40.858   8.030  51.466  1.00 35.73           N  
ANISOU 1017  NZ  LYS A 195     4631   3280   5664    618   1014    312       N  
ATOM   1018  N   ILE A 196      34.173  10.809  54.080  1.00 45.89           N  
ANISOU 1018  N   ILE A 196     5753   4457   7224   1234   1177    164       N  
ATOM   1019  CA  ILE A 196      33.090  10.658  55.052  1.00 43.38           C  
ANISOU 1019  CA  ILE A 196     5369   4165   6949   1312   1265    132       C  
ATOM   1020  C   ILE A 196      31.894  11.520  54.660  1.00 41.31           C  
ANISOU 1020  C   ILE A 196     5018   3950   6729   1495   1224     57       C  
ATOM   1021  O   ILE A 196      30.734  11.084  54.740  1.00 45.13           O  
ANISOU 1021  O   ILE A 196     5373   4501   7275   1557   1266     24       O  
ATOM   1022  CB  ILE A 196      33.597  10.998  56.466  1.00 45.76           C  
ANISOU 1022  CB  ILE A 196     5762   4438   7187   1309   1343    132       C  
ATOM   1023  CG1 ILE A 196      34.647   9.979  56.910  1.00 49.84           C  
ANISOU 1023  CG1 ILE A 196     6342   4931   7665   1136   1393    201       C  
ATOM   1024  CG2 ILE A 196      32.440  11.041  57.455  1.00 43.05           C  
ANISOU 1024  CG2 ILE A 196     5346   4134   6878   1415   1432     81       C  
ATOM   1025  CD1 ILE A 196      35.316  10.327  58.216  1.00 54.35           C  
ANISOU 1025  CD1 ILE A 196     7018   5474   8158   1126   1457    205       C  
ATOM   1026  N   ILE A 197      32.155  12.758  54.234  1.00 33.53           N  
ANISOU 1026  N   ILE A 197     4087   2944   5709   1588   1143     22       N  
ATOM   1027  CA  ILE A 197      31.066  13.640  53.820  1.00 47.87           C  
ANISOU 1027  CA  ILE A 197     5818   4808   7563   1770   1097    -57       C  
ATOM   1028  C   ILE A 197      30.365  13.075  52.589  1.00 53.48           C  
ANISOU 1028  C   ILE A 197     6419   5570   8333   1781   1039    -56       C  
ATOM   1029  O   ILE A 197      29.134  13.150  52.463  1.00 60.06           O  
ANISOU 1029  O   ILE A 197     7116   6489   9217   1907   1044   -115       O  
ATOM   1030  CB  ILE A 197      31.599  15.063  53.568  1.00 51.72           C  
ANISOU 1030  CB  ILE A 197     6400   5245   8007   1852   1017    -90       C  
ATOM   1031  CG1 ILE A 197      32.147  15.665  54.863  1.00 61.36           C  
ANISOU 1031  CG1 ILE A 197     7716   6424   9173   1858   1081    -98       C  
ATOM   1032  CG2 ILE A 197      30.508  15.956  52.996  1.00 53.66           C  
ANISOU 1032  CG2 ILE A 197     6554   5536   8301   2038    956   -173       C  
ATOM   1033  CD1 ILE A 197      32.861  16.986  54.664  1.00 67.37           C  
ANISOU 1033  CD1 ILE A 197     8581   7123   9892   1906   1010   -118       C  
ATOM   1034  N   ALA A 198      31.134  12.481  51.674  1.00 46.57           N  
ANISOU 1034  N   ALA A 198     5590   4656   7449   1650    986      6       N  
ATOM   1035  CA  ALA A 198      30.536  11.852  50.501  1.00 51.78           C  
ANISOU 1035  CA  ALA A 198     6153   5356   8163   1644    934     14       C  
ATOM   1036  C   ALA A 198      29.626  10.697  50.896  1.00 56.87           C  
ANISOU 1036  C   ALA A 198     6666   6065   8876   1615   1017     19       C  
ATOM   1037  O   ALA A 198      28.550  10.517  50.314  1.00 66.48           O  
ANISOU 1037  O   ALA A 198     7747   7365  10147   1699    995    -15       O  
ATOM   1038  CB  ALA A 198      31.630  11.372  49.547  1.00 48.32           C  
ANISOU 1038  CB  ALA A 198     5793   4866   7700   1495    874     76       C  
ATOM   1039  N   VAL A 199      30.035   9.908  51.892  1.00 50.44           N  
ANISOU 1039  N   VAL A 199     5882   5224   8058   1498   1113     59       N  
ATOM   1040  CA  VAL A 199      29.202   8.785  52.316  1.00 59.00           C  
ANISOU 1040  CA  VAL A 199     6843   6368   9208   1461   1198     63       C  
ATOM   1041  C   VAL A 199      27.912   9.287  52.958  1.00 62.68           C  
ANISOU 1041  C   VAL A 199     7175   6950   9692   1632   1251    -22       C  
ATOM   1042  O   VAL A 199      26.825   8.742  52.714  1.00 66.47           O  
ANISOU 1042  O   VAL A 199     7485   7544  10228   1673   1275    -52       O  
ATOM   1043  CB  VAL A 199      29.979   7.853  53.262  1.00 63.90           C  
ANISOU 1043  CB  VAL A 199     7540   6926   9815   1299   1289    122       C  
ATOM   1044  CG1 VAL A 199      29.077   6.724  53.733  1.00 60.24           C  
ANISOU 1044  CG1 VAL A 199     6948   6523   9419   1265   1381    119       C  
ATOM   1045  CG2 VAL A 199      31.204   7.292  52.563  1.00 69.13           C  
ANISOU 1045  CG2 VAL A 199     8296   7515  10456   1136   1239    194       C  
ATOM   1046  N   TRP A 200      28.007  10.325  53.795  1.00 56.88           N  
ANISOU 1046  N   TRP A 200     6498   6207   8906   1731   1275    -67       N  
ATOM   1047  CA  TRP A 200      26.796  10.888  54.390  1.00 50.45           C  
ANISOU 1047  CA  TRP A 200     5545   5520   8104   1901   1326   -161       C  
ATOM   1048  C   TRP A 200      25.857  11.435  53.318  1.00 57.65           C  
ANISOU 1048  C   TRP A 200     6327   6528   9049   2047   1239   -221       C  
ATOM   1049  O   TRP A 200      24.630  11.283  53.413  1.00 65.72           O  
ANISOU 1049  O   TRP A 200     7155   7708  10106   2143   1280   -285       O  
ATOM   1050  CB  TRP A 200      27.153  11.974  55.404  1.00 38.68           C  
ANISOU 1050  CB  TRP A 200     4156   3986   6556   1979   1356   -200       C  
ATOM   1051  CG  TRP A 200      27.341  11.444  56.793  1.00 42.04           C  
ANISOU 1051  CG  TRP A 200     4613   4404   6956   1908   1483   -185       C  
ATOM   1052  CD1 TRP A 200      28.518  11.313  57.470  1.00 43.09           C  
ANISOU 1052  CD1 TRP A 200     4916   4419   7036   1790   1512   -123       C  
ATOM   1053  CD2 TRP A 200      26.317  10.958  57.670  1.00 47.51           C  
ANISOU 1053  CD2 TRP A 200     5158   5227   7666   1949   1603   -237       C  
ATOM   1054  NE1 TRP A 200      28.290  10.784  58.718  1.00 49.77           N  
ANISOU 1054  NE1 TRP A 200     5745   5296   7870   1760   1637   -130       N  
ATOM   1055  CE2 TRP A 200      26.947  10.556  58.865  1.00 54.82           C  
ANISOU 1055  CE2 TRP A 200     6190   6089   8549   1853   1699   -201       C  
ATOM   1056  CE3 TRP A 200      24.929  10.827  57.563  1.00 50.76           C  
ANISOU 1056  CE3 TRP A 200     5346   5824   8117   2053   1642   -314       C  
ATOM   1057  CZ2 TRP A 200      26.237  10.033  59.944  1.00 61.67           C  
ANISOU 1057  CZ2 TRP A 200     6959   7063   9411   1857   1833   -239       C  
ATOM   1058  CZ3 TRP A 200      24.226  10.307  58.636  1.00 55.95           C  
ANISOU 1058  CZ3 TRP A 200     5888   6607   8765   2049   1780   -353       C  
ATOM   1059  CH2 TRP A 200      24.881   9.916  59.810  1.00 62.89           C  
ANISOU 1059  CH2 TRP A 200     6887   7410   9599   1951   1875   -316       C  
ATOM   1060  N   THR A 201      26.416  12.070  52.283  1.00 55.74           N  
ANISOU 1060  N   THR A 201     6180   6208   8793   2063   1119   -204       N  
ATOM   1061  CA  THR A 201      25.588  12.564  51.187  1.00 62.99           C  
ANISOU 1061  CA  THR A 201     6989   7205   9739   2199   1026   -256       C  
ATOM   1062  C   THR A 201      24.920  11.414  50.439  1.00 65.90           C  
ANISOU 1062  C   THR A 201     7212   7666  10162   2144   1026   -229       C  
ATOM   1063  O   THR A 201      23.751  11.514  50.046  1.00 71.49           O  
ANISOU 1063  O   THR A 201     7739   8522  10901   2269   1011   -290       O  
ATOM   1064  CB  THR A 201      26.432  13.409  50.233  1.00 65.25           C  
ANISOU 1064  CB  THR A 201     7422   7379   9991   2207    903   -238       C  
ATOM   1065  OG1 THR A 201      26.996  14.515  50.949  1.00 74.21           O  
ANISOU 1065  OG1 THR A 201     8673   8439  11084   2257    904   -268       O  
ATOM   1066  CG2 THR A 201      25.582  13.939  49.088  1.00 61.54           C  
ANISOU 1066  CG2 THR A 201     6851   6983   9548   2354    802   -292       C  
ATOM   1067  N   ILE A 202      25.652  10.317  50.226  1.00 59.28           N  
ANISOU 1067  N   ILE A 202     6440   6747   9337   1956   1040   -142       N  
ATOM   1068  CA  ILE A 202      25.066   9.131  49.603  1.00 61.27           C  
ANISOU 1068  CA  ILE A 202     6554   7074   9650   1882   1047   -114       C  
ATOM   1069  C   ILE A 202      23.890   8.626  50.428  1.00 62.27           C  
ANISOU 1069  C   ILE A 202     6476   7374   9808   1925   1156   -165       C  
ATOM   1070  O   ILE A 202      22.841   8.252  49.886  1.00 70.06           O  
ANISOU 1070  O   ILE A 202     7267   8517  10834   1973   1147   -194       O  
ATOM   1071  CB  ILE A 202      26.137   8.038  49.422  1.00 63.67           C  
ANISOU 1071  CB  ILE A 202     6975   7246   9970   1663   1054    -19       C  
ATOM   1072  CG1 ILE A 202      27.148   8.446  48.349  1.00 68.12           C  
ANISOU 1072  CG1 ILE A 202     7689   7695  10500   1616    943     22       C  
ATOM   1073  CG2 ILE A 202      25.495   6.701  49.076  1.00 63.25           C  
ANISOU 1073  CG2 ILE A 202     6774   7267   9991   1573   1085      3       C  
ATOM   1074  CD1 ILE A 202      28.282   7.458  48.178  1.00 70.18           C  
ANISOU 1074  CD1 ILE A 202     8055   7845  10764   1404    950    104       C  
ATOM   1075  N   SER A 203      24.047   8.612  51.753  1.00 55.47           N  
ANISOU 1075  N   SER A 203     5648   6506   8922   1903   1263   -177       N  
ATOM   1076  CA  SER A 203      22.970   8.142  52.619  1.00 56.61           C  
ANISOU 1076  CA  SER A 203     5595   6833   9080   1931   1382   -229       C  
ATOM   1077  C   SER A 203      21.745   9.042  52.510  1.00 59.77           C  
ANISOU 1077  C   SER A 203     5813   7422   9477   2135   1368   -333       C  
ATOM   1078  O   SER A 203      20.608   8.556  52.417  1.00 63.16           O  
ANISOU 1078  O   SER A 203     6008   8059   9931   2160   1411   -373       O  
ATOM   1079  CB  SER A 203      23.460   8.071  54.063  1.00 56.62           C  
ANISOU 1079  CB  SER A 203     5692   6778   9042   1876   1497   -224       C  
ATOM   1080  OG  SER A 203      24.761   7.516  54.122  1.00 53.92           O  
ANISOU 1080  OG  SER A 203     5552   6241   8694   1711   1487   -132       O  
ATOM   1081  N   VAL A 204      21.960  10.361  52.521  1.00 57.26           N  
ANISOU 1081  N   VAL A 204     5590   7040   9126   2276   1308   -382       N  
ATOM   1082  CA  VAL A 204      20.845  11.297  52.381  1.00 56.54           C  
ANISOU 1082  CA  VAL A 204     5335   7106   9040   2480   1282   -492       C  
ATOM   1083  C   VAL A 204      20.138  11.089  51.046  1.00 56.48           C  
ANISOU 1083  C   VAL A 204     5185   7206   9068   2529   1189   -496       C  
ATOM   1084  O   VAL A 204      18.901  11.115  50.966  1.00 57.63           O  
ANISOU 1084  O   VAL A 204     5094   7570   9233   2632   1209   -571       O  
ATOM   1085  CB  VAL A 204      21.343  12.746  52.536  1.00 54.59           C  
ANISOU 1085  CB  VAL A 204     5240   6734   8766   2603   1219   -540       C  
ATOM   1086  CG1 VAL A 204      20.241  13.734  52.176  1.00 52.39           C  
ANISOU 1086  CG1 VAL A 204     4799   6588   8520   2813   1166   -661       C  
ATOM   1087  CG2 VAL A 204      21.841  12.989  53.951  1.00 58.98           C  
ANISOU 1087  CG2 VAL A 204     5901   7224   9286   2573   1322   -548       C  
ATOM   1088  N   GLY A 205      20.911  10.875  49.979  1.00 56.03           N  
ANISOU 1088  N   GLY A 205     5263   7009   9016   2451   1088   -417       N  
ATOM   1089  CA  GLY A 205      20.308  10.657  48.674  1.00 61.95           C  
ANISOU 1089  CA  GLY A 205     5895   7848   9793   2492    996   -411       C  
ATOM   1090  C   GLY A 205      19.493   9.380  48.610  1.00 67.70           C  
ANISOU 1090  C   GLY A 205     6406   8753  10563   2397   1062   -391       C  
ATOM   1091  O   GLY A 205      18.424   9.345  47.996  1.00 68.98           O  
ANISOU 1091  O   GLY A 205     6360   9107  10743   2483   1031   -430       O  
ATOM   1092  N   ILE A 206      19.988   8.313  49.239  1.00 72.76           N  
ANISOU 1092  N   ILE A 206     7088   9339  11219   2210   1151   -330       N  
ATOM   1093  CA  ILE A 206      19.238   7.060  49.267  1.00 73.91           C  
ANISOU 1093  CA  ILE A 206     7024   9654  11404   2093   1220   -313       C  
ATOM   1094  C   ILE A 206      17.955   7.216  50.077  1.00 68.13           C  
ANISOU 1094  C   ILE A 206     6039   9182  10666   2184   1326   -396       C  
ATOM   1095  O   ILE A 206      16.917   6.634  49.738  1.00 76.87           O  
ANISOU 1095  O   ILE A 206     6889  10481  11836   2161   1365   -394       O  
ATOM   1096  CB  ILE A 206      20.117   5.918  49.812  1.00 68.96           C  
ANISOU 1096  CB  ILE A 206     6509   8875  10820   1871   1305   -224       C  
ATOM   1097  CG1 ILE A 206      21.326   5.688  48.904  1.00 72.45           C  
ANISOU 1097  CG1 ILE A 206     7176   9093  11258   1774   1190   -152       C  
ATOM   1098  CG2 ILE A 206      19.311   4.631  49.952  1.00 61.24           C  
ANISOU 1098  CG2 ILE A 206     5288   8023   9957   1726   1426   -184       C  
ATOM   1099  CD1 ILE A 206      22.282   4.636  49.422  1.00 75.63           C  
ANISOU 1099  CD1 ILE A 206     7703   9322  11712   1568   1268    -68       C  
ATOM   1100  N   SER A 207      17.995   8.013  51.144  1.00 67.69           N  
ANISOU 1100  N   SER A 207     6036   9124  10560   2279   1386   -462       N  
ATOM   1101  CA  SER A 207      16.837   8.141  52.022  1.00 52.13           C  
ANISOU 1101  CA  SER A 207     3831   7395   8580   2353   1503   -546       C  
ATOM   1102  C   SER A 207      15.833   9.209  51.588  1.00 78.68           C  
ANISOU 1102  C   SER A 207     7037  10924  11933   2578   1433   -661       C  
ATOM   1103  O   SER A 207      14.730   9.253  52.142  1.00 73.97           O  
ANISOU 1103  O   SER A 207     6217  10559  11332   2628   1515   -738       O  
ATOM   1104  CB  SER A 207      17.303   8.425  53.453  1.00 60.21           C  
ANISOU 1104  CB  SER A 207     4974   8347   9558   2342   1613   -571       C  
ATOM   1105  OG  SER A 207      18.248   7.459  53.873  1.00 49.88           O  
ANISOU 1105  OG  SER A 207     3811   6866   8275   2142   1686   -462       O  
ATOM   1106  N   MET A 208      16.178  10.054  50.616  1.00 77.68           N  
ANISOU 1106  N   MET A 208     7028  10671  11816   2696   1290   -666       N  
ATOM   1107  CA  MET A 208      15.266  11.119  50.192  1.00 86.40           C  
ANISOU 1107  CA  MET A 208     8032  11869  12927   2870   1215   -755       C  
ATOM   1108  C   MET A 208      13.887  10.666  49.689  1.00 89.35           C  
ANISOU 1108  C   MET A 208     8120  12514  13314   2878   1215   -779       C  
ATOM   1109  O   MET A 208      12.924  11.437  49.871  1.00 94.49           O  
ANISOU 1109  O   MET A 208     8635  13287  13980   3001   1210   -887       O  
ATOM   1110  CB  MET A 208      15.961  11.959  49.109  1.00 90.44           C  
ANISOU 1110  CB  MET A 208     8743  12182  13439   2949   1056   -731       C  
ATOM   1111  CG  MET A 208      15.267  13.270  48.775  1.00 96.88           C  
ANISOU 1111  CG  MET A 208     9515  13017  14279   3121    969   -836       C  
ATOM   1112  SD  MET A 208      15.409  14.475  50.105  1.00105.45           S  
ANISOU 1112  SD  MET A 208    10671  13996  15398   3207   1033   -950       S  
ATOM   1113  CE  MET A 208      17.162  14.836  50.036  1.00105.24           C  
ANISOU 1113  CE  MET A 208    10992  13666  15329   3150    976   -860       C  
ATOM   1114  N   PRO A 209      13.718   9.505  49.037  1.00 84.99           N  
ANISOU 1114  N   PRO A 209     7461  12057  12772   2748   1213   -694       N  
ATOM   1115  CA  PRO A 209      12.366   9.122  48.590  1.00 83.05           C  
ANISOU 1115  CA  PRO A 209     6927  12080  12546   2752   1219   -707       C  
ATOM   1116  C   PRO A 209      11.321   9.075  49.693  1.00 79.11           C  
ANISOU 1116  C   PRO A 209     6200  11798  12061   2758   1364   -782       C  
ATOM   1117  O   PRO A 209      10.129   9.225  49.397  1.00 80.50           O  
ANISOU 1117  O   PRO A 209     6153  12186  12248   2821   1350   -833       O  
ATOM   1118  CB  PRO A 209      12.587   7.738  47.970  1.00 85.76           C  
ANISOU 1118  CB  PRO A 209     7187  12430  12966   2568   1242   -586       C  
ATOM   1119  CG  PRO A 209      13.963   7.800  47.444  1.00 84.90           C  
ANISOU 1119  CG  PRO A 209     7365  12051  12841   2542   1150   -533       C  
ATOM   1120  CD  PRO A 209      14.745   8.644  48.418  1.00 83.20           C  
ANISOU 1120  CD  PRO A 209     7371  11675  12565   2610   1175   -587       C  
ATOM   1121  N   ILE A 210      11.712   8.865  50.946  1.00 76.88           N  
ANISOU 1121  N   ILE A 210     5963  11476  11772   2693   1504   -792       N  
ATOM   1122  CA  ILE A 210      10.729   8.769  52.024  1.00 78.67           C  
ANISOU 1122  CA  ILE A 210     5977  11914  12001   2684   1655   -860       C  
ATOM   1123  C   ILE A 210      10.177  10.160  52.329  1.00 82.39           C  
ANISOU 1123  C   ILE A 210     6445  12398  12460   2872   1603  -1027       C  
ATOM   1124  O   ILE A 210       8.950  10.313  52.407  1.00 80.64           O  
ANISOU 1124  O   ILE A 210     5981  12379  12278   2915   1632  -1123       O  
ATOM   1125  CB  ILE A 210      11.314   8.085  53.271  1.00 73.32           C  
ANISOU 1125  CB  ILE A 210     5353  11191  11313   2548   1828   -816       C  
ATOM   1126  CG1 ILE A 210      11.745   6.657  52.933  1.00 71.75           C  
ANISOU 1126  CG1 ILE A 210     5121  10973  11169   2332   1876   -685       C  
ATOM   1127  CG2 ILE A 210      10.296   8.080  54.402  1.00 71.40           C  
ANISOU 1127  CG2 ILE A 210     4908  11168  11054   2545   1985   -890       C  
ATOM   1128  CD1 ILE A 210      12.560   5.993  54.015  1.00 72.26           C  
ANISOU 1128  CD1 ILE A 210     5326  10903  11225   2171   2013   -625       C  
ATOM   1129  N   PRO A 211      11.005  11.199  52.518  1.00 87.64           N  
ANISOU 1129  N   PRO A 211     7352  12833  13116   2971   1531  -1083       N  
ATOM   1130  CA  PRO A 211      10.423  12.544  52.661  1.00 88.46           C  
ANISOU 1130  CA  PRO A 211     7406  12883  13320   3129   1492  -1248       C  
ATOM   1131  C   PRO A 211       9.686  13.009  51.422  1.00 88.88           C  
ANISOU 1131  C   PRO A 211     7338  12952  13481   3207   1349  -1317       C  
ATOM   1132  O   PRO A 211       8.655  13.682  51.547  1.00 89.77           O  
ANISOU 1132  O   PRO A 211     7250  13046  13814   3248   1371  -1481       O  
ATOM   1133  CB  PRO A 211      11.639  13.431  52.953  1.00 91.74           C  
ANISOU 1133  CB  PRO A 211     8110  13010  13736   3192   1456  -1232       C  
ATOM   1134  CG  PRO A 211      12.612  12.538  53.533  1.00 93.39           C  
ANISOU 1134  CG  PRO A 211     8465  13174  13845   3066   1539  -1112       C  
ATOM   1135  CD  PRO A 211      12.439  11.216  52.853  1.00 90.08           C  
ANISOU 1135  CD  PRO A 211     7941  12892  13392   2931   1536  -1004       C  
ATOM   1136  N   VAL A 212      10.189  12.689  50.226  1.00 88.05           N  
ANISOU 1136  N   VAL A 212     7340  12808  13309   3203   1222  -1199       N  
ATOM   1137  CA  VAL A 212       9.537  13.185  49.013  1.00 89.61           C  
ANISOU 1137  CA  VAL A 212     7439  13003  13608   3282   1076  -1268       C  
ATOM   1138  C   VAL A 212       8.116  12.637  48.914  1.00 91.45           C  
ANISOU 1138  C   VAL A 212     7341  13487  13919   3234   1112  -1359       C  
ATOM   1139  O   VAL A 212       7.137  13.393  48.915  1.00 95.55           O  
ANISOU 1139  O   VAL A 212     7638  13768  14897   3201   1142  -1549       O  
ATOM   1140  CB  VAL A 212      10.365  12.832  47.765  1.00 82.46           C  
ANISOU 1140  CB  VAL A 212     6718  12035  12576   3282    955  -1096       C  
ATOM   1141  CG1 VAL A 212       9.609  13.224  46.506  1.00 82.71           C  
ANISOU 1141  CG1 VAL A 212     6638  12117  12670   3366    808  -1153       C  
ATOM   1142  CG2 VAL A 212      11.709  13.536  47.810  1.00 80.03           C  
ANISOU 1142  CG2 VAL A 212     6719  11429  12261   3308    906  -1059       C  
ATOM   1143  N   PHE A 213       7.985  11.314  48.827  1.00 88.27           N  
ANISOU 1143  N   PHE A 213     6865  13357  13318   3136   1174  -1185       N  
ATOM   1144  CA  PHE A 213       6.676  10.692  48.666  1.00 94.02           C  
ANISOU 1144  CA  PHE A 213     7269  14368  14086   3093   1223  -1207       C  
ATOM   1145  C   PHE A 213       5.908  10.544  49.977  1.00 96.71           C  
ANISOU 1145  C   PHE A 213     7399  14802  14543   3015   1396  -1352       C  
ATOM   1146  O   PHE A 213       4.676  10.440  49.946  1.00101.22           O  
ANISOU 1146  O   PHE A 213     7663  15364  15431   2915   1440  -1552       O  
ATOM   1147  CB  PHE A 213       6.830   9.323  47.999  1.00 98.14           C  
ANISOU 1147  CB  PHE A 213     7740  15036  14511   2968   1263   -919       C  
ATOM   1148  CG  PHE A 213       7.269   9.394  46.562  1.00 98.11           C  
ANISOU 1148  CG  PHE A 213     7863  14938  14474   3016   1110   -801       C  
ATOM   1149  CD1 PHE A 213       6.351   9.244  45.534  1.00100.32           C  
ANISOU 1149  CD1 PHE A 213     7967  15419  14730   3071   1055   -685       C  
ATOM   1150  CD2 PHE A 213       8.597   9.621  46.238  1.00 91.07           C  
ANISOU 1150  CD2 PHE A 213     7273  13765  13567   3010   1035   -766       C  
ATOM   1151  CE1 PHE A 213       6.751   9.311  44.211  1.00 94.97           C  
ANISOU 1151  CE1 PHE A 213     7409  14643  14032   3109    935   -550       C  
ATOM   1152  CE2 PHE A 213       9.003   9.691  44.917  1.00 85.69           C  
ANISOU 1152  CE2 PHE A 213     6710  12989  12857   3042    901   -670       C  
ATOM   1153  CZ  PHE A 213       8.078   9.536  43.903  1.00 87.66           C  
ANISOU 1153  CZ  PHE A 213     6781  13426  13099   3090    851   -576       C  
ATOM   1154  N   GLY A 214       6.597  10.534  51.120  1.00 94.81           N  
ANISOU 1154  N   GLY A 214     7299  14494  14231   2989   1519  -1310       N  
ATOM   1155  CA  GLY A 214       5.909  10.334  52.388  1.00 94.68           C  
ANISOU 1155  CA  GLY A 214     7104  14597  14275   2919   1704  -1406       C  
ATOM   1156  C   GLY A 214       5.110  11.538  52.849  1.00 96.36           C  
ANISOU 1156  C   GLY A 214     7183  14489  14942   2930   1773  -1682       C  
ATOM   1157  O   GLY A 214       4.006  11.393  53.380  1.00102.08           O  
ANISOU 1157  O   GLY A 214     7645  15102  16041   2815   1986  -1731       O  
ATOM   1158  N   LEU A 215       5.657  12.741  52.677  1.00 94.81           N  
ANISOU 1158  N   LEU A 215     7171  13954  14898   3028   1705  -1712       N  
ATOM   1159  CA  LEU A 215       4.901  13.932  53.047  1.00 98.47           C  
ANISOU 1159  CA  LEU A 215     7523  14036  15853   3089   1907  -1659       C  
ATOM   1160  C   LEU A 215       3.824  14.248  52.019  1.00 99.87           C  
ANISOU 1160  C   LEU A 215     7500  13987  16460   3133   2007  -1393       C  
ATOM   1161  O   LEU A 215       2.761  14.768  52.378  1.00 88.54           O  
ANISOU 1161  O   LEU A 215     5886  12557  15198   3257   2199  -1248       O  
ATOM   1162  CB  LEU A 215       5.840  15.125  53.230  1.00 92.04           C  
ANISOU 1162  CB  LEU A 215     6965  13060  14947   3251   1839  -1653       C  
ATOM   1163  CG  LEU A 215       6.883  14.981  54.340  1.00 79.21           C  
ANISOU 1163  CG  LEU A 215     5563  11586  12946   3267   1827  -1716       C  
ATOM   1164  CD1 LEU A 215       7.705  16.252  54.481  1.00 78.40           C  
ANISOU 1164  CD1 LEU A 215     5694  11231  12863   3406   1793  -1683       C  
ATOM   1165  CD2 LEU A 215       6.207  14.633  55.657  1.00 83.57           C  
ANISOU 1165  CD2 LEU A 215     5963  12296  13493   3208   2035  -1783       C  
ATOM   1166  N   GLN A 216       4.083  13.945  50.745  1.00103.96           N  
ANISOU 1166  N   GLN A 216     8052  14430  17018   3092   1847  -1315       N  
ATOM   1167  CA  GLN A 216       3.064  14.109  49.715  1.00104.63           C  
ANISOU 1167  CA  GLN A 216     7951  14455  17350   3185   1915   -982       C  
ATOM   1168  C   GLN A 216       1.902  13.144  49.923  1.00105.81           C  
ANISOU 1168  C   GLN A 216     7816  14789  17600   3112   2080   -832       C  
ATOM   1169  O   GLN A 216       0.742  13.499  49.683  1.00112.28           O  
ANISOU 1169  O   GLN A 216     8406  15746  18511   3259   2142   -700       O  
ATOM   1170  CB  GLN A 216       3.681  13.897  48.333  1.00101.71           C  
ANISOU 1170  CB  GLN A 216     7698  13969  16979   3142   1722   -890       C  
ATOM   1171  CG  GLN A 216       4.469  15.078  47.797  1.00 97.69           C  
ANISOU 1171  CG  GLN A 216     7408  13300  16410   3291   1584   -903       C  
ATOM   1172  CD  GLN A 216       4.637  15.017  46.292  1.00 94.71           C  
ANISOU 1172  CD  GLN A 216     7074  12835  16076   3301   1455   -696       C  
ATOM   1173  OE1 GLN A 216       3.870  14.349  45.598  1.00 94.86           O  
ANISOU 1173  OE1 GLN A 216     6914  12964  16164   3275   1482   -485       O  
ATOM   1174  NE2 GLN A 216       5.649  15.707  45.779  1.00 94.08           N  
ANISOU 1174  NE2 GLN A 216     7236  12594  15918   3346   1311   -738       N  
ATOM   1175  N   ASP A 217       2.192  11.924  50.372  1.00 99.93           N  
ANISOU 1175  N   ASP A 217     7055  14121  16792   2901   2115   -922       N  
ATOM   1176  CA  ASP A 217       1.197  10.860  50.465  1.00 99.42           C  
ANISOU 1176  CA  ASP A 217     6729  14251  16795   2825   2274   -695       C  
ATOM   1177  C   ASP A 217       1.224  10.269  51.865  1.00103.90           C  
ANISOU 1177  C   ASP A 217     7272  14909  17297   2687   2437   -866       C  
ATOM   1178  O   ASP A 217       2.233   9.687  52.276  1.00106.78           O  
ANISOU 1178  O   ASP A 217     7776  15444  17353   2508   2248  -1367       O  
ATOM   1179  CB  ASP A 217       1.469   9.774  49.420  1.00 96.82           C  
ANISOU 1179  CB  ASP A 217     6405  13929  16452   2693   2182   -478       C  
ATOM   1180  CG  ASP A 217       0.381   8.718  49.370  1.00103.23           C  
ANISOU 1180  CG  ASP A 217     6927  15041  17254   2639   2287   -223       C  
ATOM   1181  OD1 ASP A 217      -0.662   8.894  50.034  1.00109.12           O  
ANISOU 1181  OD1 ASP A 217     7441  15952  18069   2692   2412   -292       O  
ATOM   1182  OD2 ASP A 217       0.572   7.705  48.665  1.00103.95           O  
ANISOU 1182  OD2 ASP A 217     7017  15267  17213   2548   2225     42       O  
ATOM   1183  N   ASP A 218       0.106  10.394  52.585  1.00104.73           N  
ANISOU 1183  N   ASP A 218     7157  15178  17459   2774   2637   -757       N  
ATOM   1184  CA  ASP A 218       0.022   9.864  53.941  1.00 96.93           C  
ANISOU 1184  CA  ASP A 218     6140  14276  16413   2656   2830   -850       C  
ATOM   1185  C   ASP A 218      -0.006   8.341  53.976  1.00 93.08           C  
ANISOU 1185  C   ASP A 218     5587  13880  15901   2438   2906   -669       C  
ATOM   1186  O   ASP A 218       0.315   7.754  55.015  1.00 92.59           O  
ANISOU 1186  O   ASP A 218     5581  13835  15764   2278   3022   -807       O  
ATOM   1187  CB  ASP A 218      -1.222  10.412  54.643  1.00103.87           C  
ANISOU 1187  CB  ASP A 218     6784  15326  17356   2811   3011   -804       C  
ATOM   1188  CG  ASP A 218      -1.202  11.921  54.779  1.00104.73           C  
ANISOU 1188  CG  ASP A 218     6973  15340  17481   3036   2972   -935       C  
ATOM   1189  OD1 ASP A 218      -0.102  12.512  54.726  1.00100.31           O  
ANISOU 1189  OD1 ASP A 218     6681  14591  16843   3047   2842  -1081       O  
ATOM   1190  OD2 ASP A 218      -2.288  12.517  54.940  1.00106.43           O  
ANISOU 1190  OD2 ASP A 218     6974  15689  17774   3199   3058   -909       O  
ATOM   1191  N   SER A 219      -0.379   7.688  52.874  1.00 93.29           N  
ANISOU 1191  N   SER A 219     5492  14012  15942   2427   2823   -385       N  
ATOM   1192  CA  SER A 219      -0.574   6.243  52.904  1.00106.60           C  
ANISOU 1192  CA  SER A 219     7082  15920  17500   2272   2885    -87       C  
ATOM   1193  C   SER A 219       0.734   5.467  52.804  1.00102.54           C  
ANISOU 1193  C   SER A 219     6875  16029  16058   2407   2727    460       C  
ATOM   1194  O   SER A 219       0.818   4.345  53.314  1.00106.70           O  
ANISOU 1194  O   SER A 219     7314  17331  15897   2275   2580    263       O  
ATOM   1195  CB  SER A 219      -1.517   5.820  51.777  1.00108.06           C  
ANISOU 1195  CB  SER A 219     6989  16305  17762   2254   2763    -15       C  
ATOM   1196  OG  SER A 219      -0.900   5.974  50.511  1.00109.06           O  
ANISOU 1196  OG  SER A 219     7249  16342  17846   2301   2556     74       O  
ATOM   1197  N   LYS A 220       1.758   6.034  52.164  1.00 94.74           N  
ANISOU 1197  N   LYS A 220     6039  15968  13990   2552   2138   -419       N  
ATOM   1198  CA  LYS A 220       3.019   5.319  52.000  1.00 88.75           C  
ANISOU 1198  CA  LYS A 220     5453  14973  13297   2317   2058   -648       C  
ATOM   1199  C   LYS A 220       3.850   5.268  53.275  1.00 83.93           C  
ANISOU 1199  C   LYS A 220     5005  14205  12679   2234   2179   -763       C  
ATOM   1200  O   LYS A 220       4.827   4.513  53.324  1.00 80.98           O  
ANISOU 1200  O   LYS A 220     4778  13654  12338   2071   2203   -684       O  
ATOM   1201  CB  LYS A 220       3.847   5.938  50.872  1.00 90.27           C  
ANISOU 1201  CB  LYS A 220     5848  14926  13525   2429   1866   -712       C  
ATOM   1202  CG  LYS A 220       3.186   5.865  49.506  1.00 99.13           C  
ANISOU 1202  CG  LYS A 220     6844  16167  14654   2497   1759   -514       C  
ATOM   1203  CD  LYS A 220       4.117   6.365  48.413  1.00104.77           C  
ANISOU 1203  CD  LYS A 220     7783  16637  15389   2578   1574   -579       C  
ATOM   1204  CE  LYS A 220       3.450   6.296  47.048  1.00111.48           C  
ANISOU 1204  CE  LYS A 220     8512  17580  16266   2644   1494   -317       C  
ATOM   1205  NZ  LYS A 220       4.376   6.700  45.954  1.00111.27           N  
ANISOU 1205  NZ  LYS A 220     8709  17329  16239   2705   1313   -389       N  
ATOM   1206  N   VAL A 221       3.493   6.040  54.300  1.00 83.45           N  
ANISOU 1206  N   VAL A 221     4923  14192  12593   2336   2259   -940       N  
ATOM   1207  CA  VAL A 221       4.215   6.045  55.565  1.00 82.31           C  
ANISOU 1207  CA  VAL A 221     4935  13918  12423   2285   2395   -973       C  
ATOM   1208  C   VAL A 221       3.346   5.632  56.741  1.00 85.07           C  
ANISOU 1208  C   VAL A 221     5097  14511  12714   2199   2582   -975       C  
ATOM   1209  O   VAL A 221       3.842   5.575  57.870  1.00 84.46           O  
ANISOU 1209  O   VAL A 221     5134  14360  12598   2151   2712   -987       O  
ATOM   1210  CB  VAL A 221       4.861   7.419  55.839  1.00 81.26           C  
ANISOU 1210  CB  VAL A 221     5012  13534  12328   2476   2331  -1159       C  
ATOM   1211  CG1 VAL A 221       5.951   7.700  54.820  1.00 78.09           C  
ANISOU 1211  CG1 VAL A 221     4850  12883  11939   2541   2166  -1088       C  
ATOM   1212  CG2 VAL A 221       3.807   8.514  55.815  1.00 84.26           C  
ANISOU 1212  CG2 VAL A 221     5218  13882  12913   2579   2300  -1477       C  
ATOM   1213  N   PHE A 222       2.070   5.334  56.517  1.00 94.95           N  
ANISOU 1213  N   PHE A 222     6077  16070  13930   2198   2605   -897       N  
ATOM   1214  CA  PHE A 222       1.171   4.894  57.573  1.00 97.14           C  
ANISOU 1214  CA  PHE A 222     6185  16615  14108   2176   2808   -677       C  
ATOM   1215  C   PHE A 222       0.601   3.532  57.208  1.00 91.95           C  
ANISOU 1215  C   PHE A 222     5396  15870  13671   2049   2991     16       C  
ATOM   1216  O   PHE A 222       0.292   3.267  56.042  1.00 92.03           O  
ANISOU 1216  O   PHE A 222     5335  15617  14015   2034   2983    299       O  
ATOM   1217  CB  PHE A 222       0.048   5.905  57.815  1.00 94.35           C  
ANISOU 1217  CB  PHE A 222     5797  14256  15797   2023   3554   -460       C  
ATOM   1218  CG  PHE A 222       0.468   7.082  58.647  1.00 94.09           C  
ANISOU 1218  CG  PHE A 222     5772  14555  15425   1963   3287  -1581       C  
ATOM   1219  CD1 PHE A 222       0.593   6.962  60.021  1.00 94.60           C  
ANISOU 1219  CD1 PHE A 222     5834  15195  14915   1950   3259  -1839       C  
ATOM   1220  CD2 PHE A 222       0.744   8.305  58.059  1.00 93.39           C  
ANISOU 1220  CD2 PHE A 222     5780  14310  15396   2191   3156  -1583       C  
ATOM   1221  CE1 PHE A 222       0.983   8.040  60.794  1.00 94.42           C  
ANISOU 1221  CE1 PHE A 222     5952  15129  14794   2137   3281  -1893       C  
ATOM   1222  CE2 PHE A 222       1.135   9.387  58.826  1.00 93.22           C  
ANISOU 1222  CE2 PHE A 222     5885  14352  15182   2358   3123  -1748       C  
ATOM   1223  CZ  PHE A 222       1.254   9.254  60.195  1.00 93.73           C  
ANISOU 1223  CZ  PHE A 222     5978  14683  14954   2327   3216  -1874       C  
ATOM   1224  N   LYS A 223       0.467   2.671  58.216  1.00 92.75           N  
ANISOU 1224  N   LYS A 223     5448  16013  13779   1857   3159     76       N  
ATOM   1225  CA  LYS A 223       0.038   1.285  58.023  1.00 93.53           C  
ANISOU 1225  CA  LYS A 223     5406  16004  14128   1584   3262    310       C  
ATOM   1226  C   LYS A 223      -0.926   0.942  59.159  1.00 96.77           C  
ANISOU 1226  C   LYS A 223     5671  16212  14886   1514   3597    478       C  
ATOM   1227  O   LYS A 223      -0.503   0.486  60.225  1.00 96.28           O  
ANISOU 1227  O   LYS A 223     5689  16381  14510   1405   3634    403       O  
ATOM   1228  CB  LYS A 223       1.257   0.371  57.990  1.00103.51           C  
ANISOU 1228  CB  LYS A 223     6837  17360  15132   1299   3112     22       C  
ATOM   1229  CG  LYS A 223       1.020  -1.071  57.592  1.00102.76           C  
ANISOU 1229  CG  LYS A 223     6641  17231  15171   1004   3130    200       C  
ATOM   1230  CD  LYS A 223       2.369  -1.777  57.488  1.00 98.04           C  
ANISOU 1230  CD  LYS A 223     6277  16501  14473    781   3042     31       C  
ATOM   1231  CE  LYS A 223       2.250  -3.199  56.974  1.00 93.08           C  
ANISOU 1231  CE  LYS A 223     5586  15847  13934    483   3016    173       C  
ATOM   1232  NZ  LYS A 223       3.596  -3.828  56.844  1.00 83.16           N  
ANISOU 1232  NZ  LYS A 223     4580  14382  12636    299   2956     82       N  
ATOM   1233  N   GLU A 224      -2.220   1.169  58.917  1.00110.53           N  
ANISOU 1233  N   GLU A 224     7159  17605  17231   1498   3788    424       N  
ATOM   1234  CA  GLU A 224      -3.278   0.927  59.902  1.00103.68           C  
ANISOU 1234  CA  GLU A 224     6080  16772  16540   1407   4033    341       C  
ATOM   1235  C   GLU A 224      -3.043   1.738  61.176  1.00104.01           C  
ANISOU 1235  C   GLU A 224     6272  16751  16495   1562   4207    303       C  
ATOM   1236  O   GLU A 224      -3.052   1.208  62.289  1.00104.73           O  
ANISOU 1236  O   GLU A 224     6386  16989  16417   1477   4345    369       O  
ATOM   1237  CB  GLU A 224      -3.402  -0.563  60.227  1.00104.06           C  
ANISOU 1237  CB  GLU A 224     6052  17017  16470   1119   4062    446       C  
ATOM   1238  CG  GLU A 224      -3.712  -1.457  59.043  1.00104.07           C  
ANISOU 1238  CG  GLU A 224     5899  17052  16590    929   3912    467       C  
ATOM   1239  CD  GLU A 224      -4.074  -2.865  59.472  1.00105.28           C  
ANISOU 1239  CD  GLU A 224     5947  17335  16719    624   3988    526       C  
ATOM   1240  OE1 GLU A 224      -4.196  -3.101  60.693  1.00106.43           O  
ANISOU 1240  OE1 GLU A 224     6112  17551  16776    570   4170    543       O  
ATOM   1241  OE2 GLU A 224      -4.229  -3.737  58.592  1.00115.77           O  
ANISOU 1241  OE2 GLU A 224     7184  18683  18121    435   3866    553       O  
ATOM   1242  N   GLY A 225      -2.834   3.041  61.006  1.00103.54           N  
ANISOU 1242  N   GLY A 225     6318  16447  16576   1770   4198    159       N  
ATOM   1243  CA  GLY A 225      -2.635   3.916  62.145  1.00104.61           C  
ANISOU 1243  CA  GLY A 225     6598  16437  16713   1891   4367     43       C  
ATOM   1244  C   GLY A 225      -1.205   3.922  62.646  1.00101.47           C  
ANISOU 1244  C   GLY A 225     6550  16332  15672   2064   4215    357       C  
ATOM   1245  O   GLY A 225      -0.749   4.906  63.237  1.00 99.83           O  
ANISOU 1245  O   GLY A 225     6531  16073  15328   2271   4240    342       O  
ATOM   1246  N   SER A 226      -0.491   2.823  62.416  1.00101.66           N  
ANISOU 1246  N   SER A 226     6556  17169  14901   1910   3842    258       N  
ATOM   1247  CA  SER A 226       0.893   2.704  62.846  1.00 94.72           C  
ANISOU 1247  CA  SER A 226     5868  16529  13591   1706   3611   -334       C  
ATOM   1248  C   SER A 226       1.826   3.351  61.832  1.00 91.69           C  
ANISOU 1248  C   SER A 226     5644  15955  13238   1759   3384   -622       C  
ATOM   1249  O   SER A 226       1.580   3.310  60.623  1.00 91.88           O  
ANISOU 1249  O   SER A 226     5591  15988  13329   1799   3253   -539       O  
ATOM   1250  CB  SER A 226       1.268   1.233  63.033  1.00 93.63           C  
ANISOU 1250  CB  SER A 226     5762  16314  13500   1390   3686   -187       C  
ATOM   1251  OG  SER A 226       0.981   0.479  61.870  1.00 94.79           O  
ANISOU 1251  OG  SER A 226     5800  16418  13798   1280   3607     -3       O  
ATOM   1252  N   CYS A 227       2.902   3.955  62.334  1.00 89.38           N  
ANISOU 1252  N   CYS A 227     5595  15421  12945   1797   3374   -821       N  
ATOM   1253  CA  CYS A 227       3.869   4.654  61.490  1.00 86.49           C  
ANISOU 1253  CA  CYS A 227     5427  14777  12658   1909   3207   -924       C  
ATOM   1254  C   CYS A 227       4.884   3.640  60.982  1.00 83.37           C  
ANISOU 1254  C   CYS A 227     5179  14197  12300   1724   3171   -767       C  
ATOM   1255  O   CYS A 227       5.916   3.391  61.607  1.00 81.18           O  
ANISOU 1255  O   CYS A 227     5112  13730  12002   1648   3233   -738       O  
ATOM   1256  CB  CYS A 227       4.545   5.780  62.262  1.00 85.60           C  
ANISOU 1256  CB  CYS A 227     5516  14469  12538   2067   3226  -1086       C  
ATOM   1257  SG  CYS A 227       5.861   6.618  61.348  1.00 81.97           S  
ANISOU 1257  SG  CYS A 227     5342  13652  12149   2213   3032  -1118       S  
ATOM   1258  N   LEU A 228       4.588   3.049  59.826  1.00 86.44           N  
ANISOU 1258  N   LEU A 228     5456  14637  12750   1646   3067   -676       N  
ATOM   1259  CA  LEU A 228       5.464   2.074  59.197  1.00 85.70           C  
ANISOU 1259  CA  LEU A 228     5477  14367  12716   1454   3013   -567       C  
ATOM   1260  C   LEU A 228       5.608   2.397  57.718  1.00 84.86           C  
ANISOU 1260  C   LEU A 228     5376  14177  12688   1547   2817   -578       C  
ATOM   1261  O   LEU A 228       4.694   2.940  57.092  1.00 82.01           O  
ANISOU 1261  O   LEU A 228     4850  13975  12335   1684   2737   -616       O  
ATOM   1262  CB  LEU A 228       4.930   0.641  59.358  1.00 81.68           C  
ANISOU 1262  CB  LEU A 228     4818  14008  12210   1174   3104   -414       C  
ATOM   1263  CG  LEU A 228       4.709   0.116  60.777  1.00 83.10           C  
ANISOU 1263  CG  LEU A 228     4983  14283  12309   1045   3302   -364       C  
ATOM   1264  CD1 LEU A 228       4.171  -1.306  60.740  1.00 84.29           C  
ANISOU 1264  CD1 LEU A 228     4996  14547  12484    766   3360   -191       C  
ATOM   1265  CD2 LEU A 228       5.994   0.184  61.584  1.00 80.47           C  
ANISOU 1265  CD2 LEU A 228     4927  13709  11938   1018   3364   -406       C  
ATOM   1266  N   LEU A 229       6.764   2.044  57.161  1.00 76.03           N  
ANISOU 1266  N   LEU A 229     4452  12811  11623   1473   2740   -537       N  
ATOM   1267  CA  LEU A 229       6.992   2.162  55.723  1.00 75.02           C  
ANISOU 1267  CA  LEU A 229     4343  12591  11569   1525   2557   -524       C  
ATOM   1268  C   LEU A 229       6.168   1.084  55.030  1.00 89.74           C  
ANISOU 1268  C   LEU A 229     5984  14635  13476   1333   2536   -428       C  
ATOM   1269  O   LEU A 229       6.573  -0.078  54.959  1.00 94.66           O  
ANISOU 1269  O   LEU A 229     6636  15198  14132   1087   2562   -342       O  
ATOM   1270  CB  LEU A 229       8.477   2.028  55.404  1.00 70.91           C  
ANISOU 1270  CB  LEU A 229     4093  11762  11088   1491   2496   -493       C  
ATOM   1271  CG  LEU A 229       8.899   2.235  53.948  1.00 69.17           C  
ANISOU 1271  CG  LEU A 229     3937  11409  10935   1561   2306   -478       C  
ATOM   1272  CD1 LEU A 229       8.595   3.655  53.497  1.00 69.94           C  
ANISOU 1272  CD1 LEU A 229     4058  11507  11008   1847   2189   -573       C  
ATOM   1273  CD2 LEU A 229      10.374   1.920  53.774  1.00 65.59           C  
ANISOU 1273  CD2 LEU A 229     3790  10611  10518   1474   2258   -417       C  
ATOM   1274  N   ALA A 230       5.000   1.467  54.515  1.00 98.28           N  
ANISOU 1274  N   ALA A 230     6849  15936  14555   1441   2483   -434       N  
ATOM   1275  CA  ALA A 230       4.027   0.507  54.011  1.00105.67           C  
ANISOU 1275  CA  ALA A 230     7547  17077  15527   1273   2482   -306       C  
ATOM   1276  C   ALA A 230       4.155   0.230  52.520  1.00109.20           C  
ANISOU 1276  C   ALA A 230     7978  17460  16053   1241   2306   -271       C  
ATOM   1277  O   ALA A 230       3.538  -0.723  52.031  1.00117.73           O  
ANISOU 1277  O   ALA A 230     8894  18657  17183   1058   2290   -154       O  
ATOM   1278  CB  ALA A 230       2.606   0.995  54.312  1.00110.36           C  
ANISOU 1278  CB  ALA A 230     7895  17945  16091   1419   2551   -220       C  
ATOM   1279  N   ASP A 231       4.924   1.028  51.784  1.00100.06           N  
ANISOU 1279  N   ASP A 231     6993  16111  14914   1410   2171   -351       N  
ATOM   1280  CA  ASP A 231       5.071   0.805  50.351  1.00 90.70           C  
ANISOU 1280  CA  ASP A 231     5805  14861  13798   1391   2003   -316       C  
ATOM   1281  C   ASP A 231       5.951  -0.415  50.098  1.00 82.87           C  
ANISOU 1281  C   ASP A 231     4918  13705  12865   1123   1994   -261       C  
ATOM   1282  O   ASP A 231       7.096  -0.469  50.557  1.00 83.60           O  
ANISOU 1282  O   ASP A 231     5230  13578  12956   1092   2034   -275       O  
ATOM   1283  CB  ASP A 231       5.666   2.040  49.680  1.00 84.47           C  
ANISOU 1283  CB  ASP A 231     5192  13901  13000   1654   1866   -392       C  
ATOM   1284  CG  ASP A 231       5.417   2.069  48.185  1.00 74.87           C  
ANISOU 1284  CG  ASP A 231     3920  12698  11831   1698   1694   -350       C  
ATOM   1285  OD1 ASP A 231       4.300   2.444  47.772  1.00 80.19           O  
ANISOU 1285  OD1 ASP A 231     4401  13581  12489   1808   1660   -308       O  
ATOM   1286  OD2 ASP A 231       6.338   1.711  47.423  1.00 73.61           O  
ANISOU 1286  OD2 ASP A 231     3908  12337  11724   1627   1598   -332       O  
ATOM   1287  N   ASP A 232       5.415  -1.393  49.363  1.00 78.30           N  
ANISOU 1287  N   ASP A 232     4186  13230  12334    930   1939   -187       N  
ATOM   1288  CA  ASP A 232       6.156  -2.628  49.122  1.00 72.89           C  
ANISOU 1288  CA  ASP A 232     3597  12404  11694    655   1927   -137       C  
ATOM   1289  C   ASP A 232       7.357  -2.372  48.222  1.00 80.69           C  
ANISOU 1289  C   ASP A 232     4799  13126  12733    726   1797   -157       C  
ATOM   1290  O   ASP A 232       8.450  -2.903  48.463  1.00 70.54           O  
ANISOU 1290  O   ASP A 232     3747  11589  11467    595   1817   -130       O  
ATOM   1291  CB  ASP A 232       5.236  -3.679  48.502  1.00 75.55           C  
ANISOU 1291  CB  ASP A 232     3727  12916  12064    436   1881    -58       C  
ATOM   1292  CG  ASP A 232       3.766  -3.396  48.760  1.00 91.37           C  
ANISOU 1292  CG  ASP A 232     5461  15206  14051    512   1933      3       C  
ATOM   1293  OD1 ASP A 232       3.456  -2.668  49.725  1.00 99.50           O  
ANISOU 1293  OD1 ASP A 232     6465  16313  15028    666   2049    -13       O  
ATOM   1294  OD2 ASP A 232       2.920  -3.908  47.996  1.00 98.64           O  
ANISOU 1294  OD2 ASP A 232     6196  16254  15028    421   1861    101       O  
ATOM   1295  N   ASN A 233       7.170  -1.555  47.181  1.00 84.08           N  
ANISOU 1295  N   ASN A 233     5210  13556  13182    928   1653   -186       N  
ATOM   1296  CA  ASN A 233       8.274  -1.227  46.287  1.00 89.32           C  
ANISOU 1296  CA  ASN A 233     6098  13952  13886   1012   1521   -188       C  
ATOM   1297  C   ASN A 233       9.385  -0.518  47.045  1.00 85.78           C  
ANISOU 1297  C   ASN A 233     5938  13248  13407   1133   1572   -213       C  
ATOM   1298  O   ASN A 233      10.570  -0.822  46.855  1.00 88.01           O  
ANISOU 1298  O   ASN A 233     6480  13236  13726   1055   1534   -174       O  
ATOM   1299  CB  ASN A 233       7.774  -0.358  45.134  1.00 97.73           C  
ANISOU 1299  CB  ASN A 233     7091  15090  14952   1230   1367   -210       C  
ATOM   1300  CG  ASN A 233       6.803  -1.089  44.230  1.00103.12           C  
ANISOU 1300  CG  ASN A 233     7547  15960  15675   1095   1286   -168       C  
ATOM   1301  OD1 ASN A 233       6.914  -2.298  44.027  1.00100.88           O  
ANISOU 1301  OD1 ASN A 233     7227  15669  15435    831   1286   -126       O  
ATOM   1302  ND2 ASN A 233       5.840  -0.356  43.681  1.00107.38           N  
ANISOU 1302  ND2 ASN A 233     7943  16666  16191   1271   1215   -169       N  
ATOM   1303  N   PHE A 234       9.021   0.435  47.907  1.00 80.33           N  
ANISOU 1303  N   PHE A 234     5205  12668  12647   1325   1656   -276       N  
ATOM   1304  CA  PHE A 234      10.022   1.109  48.725  1.00 75.55           C  
ANISOU 1304  CA  PHE A 234     4868  11836  12002   1427   1708   -302       C  
ATOM   1305  C   PHE A 234      10.753   0.115  49.613  1.00 62.49           C  
ANISOU 1305  C   PHE A 234     3352  10028  10362   1189   1827   -246       C  
ATOM   1306  O   PHE A 234      11.979   0.173  49.737  1.00 59.77           O  
ANISOU 1306  O   PHE A 234     3289   9392  10028   1177   1810   -217       O  
ATOM   1307  CB  PHE A 234       9.371   2.204  49.571  1.00 77.81           C  
ANISOU 1307  CB  PHE A 234     5065  12293  12207   1648   1782   -391       C  
ATOM   1308  CG  PHE A 234       9.169   3.498  48.838  1.00 87.89           C  
ANISOU 1308  CG  PHE A 234     6396  13550  13448   1915   1642   -448       C  
ATOM   1309  CD1 PHE A 234       9.878   3.774  47.680  1.00 89.38           C  
ANISOU 1309  CD1 PHE A 234     6742  13559  13659   1982   1485   -422       C  
ATOM   1310  CD2 PHE A 234       8.276   4.445  49.312  1.00 98.11           C  
ANISOU 1310  CD2 PHE A 234     7596  15005  14679   2093   1668   -528       C  
ATOM   1311  CE1 PHE A 234       9.695   4.967  47.007  1.00 92.15           C  
ANISOU 1311  CE1 PHE A 234     7165  13889  13957   2214   1356   -467       C  
ATOM   1312  CE2 PHE A 234       8.088   5.640  48.643  1.00101.45           C  
ANISOU 1312  CE2 PHE A 234     8082  15404  15059   2327   1535   -586       C  
ATOM   1313  CZ  PHE A 234       8.799   5.902  47.489  1.00 97.74           C  
ANISOU 1313  CZ  PHE A 234     7782  14755  14601   2384   1380   -549       C  
ATOM   1314  N   VAL A 235      10.018  -0.819  50.222  1.00 64.33           N  
ANISOU 1314  N   VAL A 235     3397  10459  10588    993   1944   -222       N  
ATOM   1315  CA  VAL A 235      10.635  -1.795  51.117  1.00 63.23           C  
ANISOU 1315  CA  VAL A 235     3390  10193  10443    761   2060   -167       C  
ATOM   1316  C   VAL A 235      11.667  -2.629  50.367  1.00 79.02           C  
ANISOU 1316  C   VAL A 235     5591  11922  12511    595   1968    -99       C  
ATOM   1317  O   VAL A 235      12.801  -2.803  50.826  1.00 80.07           O  
ANISOU 1317  O   VAL A 235     5983  11796  12645    545   1999    -65       O  
ATOM   1318  CB  VAL A 235       9.560  -2.681  51.773  1.00 65.97           C  
ANISOU 1318  CB  VAL A 235     3490  10823  10753    568   2185   -144       C  
ATOM   1319  CG1 VAL A 235      10.190  -3.934  52.361  1.00 64.76           C  
ANISOU 1319  CG1 VAL A 235     3482  10529  10593    284   2262    -70       C  
ATOM   1320  CG2 VAL A 235       8.828  -1.906  52.855  1.00 68.26           C  
ANISOU 1320  CG2 VAL A 235     3647  11326  10965    719   2316   -202       C  
ATOM   1321  N   LEU A 236      11.297  -3.141  49.191  1.00 64.79           N  
ANISOU 1321  N   LEU A 236     3676  10178  10763    514   1849    -77       N  
ATOM   1322  CA  LEU A 236      12.200  -4.034  48.468  1.00 65.98           C  
ANISOU 1322  CA  LEU A 236     4005  10091  10975    341   1763    -15       C  
ATOM   1323  C   LEU A 236      13.399  -3.275  47.904  1.00 69.17           C  
ANISOU 1323  C   LEU A 236     4672  10198  11412    506   1661    -12       C  
ATOM   1324  O   LEU A 236      14.550  -3.725  48.027  1.00 69.13           O  
ANISOU 1324  O   LEU A 236     4910   9927  11430    413   1662     37       O  
ATOM   1325  CB  LEU A 236      11.440  -4.753  47.353  1.00 73.06           C  
ANISOU 1325  CB  LEU A 236     4708  11139  11911    211   1658      0       C  
ATOM   1326  CG  LEU A 236      10.201  -5.539  47.789  1.00 80.32           C  
ANISOU 1326  CG  LEU A 236     5357  12370  12792     29   1742      9       C  
ATOM   1327  CD1 LEU A 236       9.449  -6.084  46.583  1.00 82.15           C  
ANISOU 1327  CD1 LEU A 236     5400  12753  13062    -71   1616     20       C  
ATOM   1328  CD2 LEU A 236      10.582  -6.662  48.742  1.00 82.57           C  
ANISOU 1328  CD2 LEU A 236     5754  12585  13035   -232   1857     63       C  
ATOM   1329  N   ILE A 237      13.154  -2.113  47.291  1.00 71.45           N  
ANISOU 1329  N   ILE A 237     4924  10532  11693    754   1569    -59       N  
ATOM   1330  CA  ILE A 237      14.252  -1.330  46.734  1.00 68.43           C  
ANISOU 1330  CA  ILE A 237     4799   9883  11318    908   1464    -52       C  
ATOM   1331  C   ILE A 237      15.182  -0.842  47.837  1.00 51.86           C  
ANISOU 1331  C   ILE A 237     2930   7601   9172    968   1556    -53       C  
ATOM   1332  O   ILE A 237      16.398  -0.761  47.637  1.00 51.24           O  
ANISOU 1332  O   ILE A 237     3113   7248   9109    968   1506    -14       O  
ATOM   1333  CB  ILE A 237      13.699  -0.164  45.890  1.00 68.02           C  
ANISOU 1333  CB  ILE A 237     4666   9943  11236   1158   1345   -105       C  
ATOM   1334  CG1 ILE A 237      12.917  -0.705  44.690  1.00 67.79           C  
ANISOU 1334  CG1 ILE A 237     4435  10064  11258   1089   1238    -93       C  
ATOM   1335  CG2 ILE A 237      14.822   0.745  45.412  1.00 51.95           C  
ANISOU 1335  CG2 ILE A 237     2918   7648   9173   1315   1242   -100       C  
ATOM   1336  CD1 ILE A 237      12.311   0.372  43.817  1.00 68.75           C  
ANISOU 1336  CD1 ILE A 237     4469  10309  11342   1330   1118   -137       C  
ATOM   1337  N   GLY A 238      14.646  -0.550  49.024  1.00 53.51           N  
ANISOU 1337  N   GLY A 238     3049   7961   9322   1008   1691    -94       N  
ATOM   1338  CA  GLY A 238      15.500  -0.140  50.124  1.00 52.19           C  
ANISOU 1338  CA  GLY A 238     3097   7629   9106   1050   1780    -95       C  
ATOM   1339  C   GLY A 238      16.280  -1.296  50.715  1.00 50.69           C  
ANISOU 1339  C   GLY A 238     3043   7272   8943    816   1865    -25       C  
ATOM   1340  O   GLY A 238      17.435  -1.132  51.113  1.00 48.47           O  
ANISOU 1340  O   GLY A 238     3018   6747   8653    825   1875      4       O  
ATOM   1341  N   SER A 239      15.667  -2.480  50.777  1.00 51.92           N  
ANISOU 1341  N   SER A 239     3042   7565   9122    597   1920      4       N  
ATOM   1342  CA  SER A 239      16.405  -3.664  51.199  1.00 59.01           C  
ANISOU 1342  CA  SER A 239     4087   8302  10032    363   1976     72       C  
ATOM   1343  C   SER A 239      17.580  -3.930  50.270  1.00 58.97           C  
ANISOU 1343  C   SER A 239     4301   8011  10094    332   1855    123       C  
ATOM   1344  O   SER A 239      18.665  -4.313  50.721  1.00 57.43           O  
ANISOU 1344  O   SER A 239     4335   7587   9899    257   1887    167       O  
ATOM   1345  CB  SER A 239      15.475  -4.876  51.250  1.00 60.21           C  
ANISOU 1345  CB  SER A 239     4039   8665  10174    125   2023     93       C  
ATOM   1346  OG  SER A 239      14.475  -4.712  52.241  1.00 63.54           O  
ANISOU 1346  OG  SER A 239     4274   9344  10526    133   2154     56       O  
ATOM   1347  N   PHE A 240      17.388  -3.717  48.968  1.00 58.94           N  
ANISOU 1347  N   PHE A 240     4233   8019  10144    396   1713    117       N  
ATOM   1348  CA  PHE A 240      18.482  -3.962  48.032  1.00 44.87           C  
ANISOU 1348  CA  PHE A 240     2653   5973   8424    368   1595    166       C  
ATOM   1349  C   PHE A 240      19.539  -2.860  48.085  1.00 42.81           C  
ANISOU 1349  C   PHE A 240     2627   5495   8143    556   1555    163       C  
ATOM   1350  O   PHE A 240      20.731  -3.146  48.245  1.00 55.76           O  
ANISOU 1350  O   PHE A 240     4500   6887   9801    498   1557    211       O  
ATOM   1351  CB  PHE A 240      17.940  -4.133  46.614  1.00 45.44           C  
ANISOU 1351  CB  PHE A 240     2588   6128   8548    363   1454    163       C  
ATOM   1352  CG  PHE A 240      17.798  -5.569  46.200  1.00 55.47           C  
ANISOU 1352  CG  PHE A 240     3810   7413   9852    107   1433    204       C  
ATOM   1353  CD1 PHE A 240      16.704  -6.316  46.606  1.00 65.91           C  
ANISOU 1353  CD1 PHE A 240     4920   8986  11137    -52   1502    193       C  
ATOM   1354  CD2 PHE A 240      18.769  -6.179  45.423  1.00 50.41           C  
ANISOU 1354  CD2 PHE A 240     3353   6540   9262     19   1340    254       C  
ATOM   1355  CE1 PHE A 240      16.576  -7.644  46.233  1.00 70.82           C  
ANISOU 1355  CE1 PHE A 240     5526   9625  11756   -302   1470    229       C  
ATOM   1356  CE2 PHE A 240      18.647  -7.504  45.047  1.00 53.36           C  
ANISOU 1356  CE2 PHE A 240     3711   6929   9636   -216   1308    286       C  
ATOM   1357  CZ  PHE A 240      17.550  -8.238  45.452  1.00 65.94           C  
ANISOU 1357  CZ  PHE A 240     5108   8772  11176   -381   1369    273       C  
ATOM   1358  N   VAL A 241      19.127  -1.598  47.954  1.00 43.66           N  
ANISOU 1358  N   VAL A 241     2690   5701   8199    775   1512    107       N  
ATOM   1359  CA  VAL A 241      20.090  -0.508  47.827  1.00 49.51           C  
ANISOU 1359  CA  VAL A 241     3670   6257   8886    936   1438    101       C  
ATOM   1360  C   VAL A 241      20.784  -0.234  49.157  1.00 48.07           C  
ANISOU 1360  C   VAL A 241     3653   5966   8644    943   1549    103       C  
ATOM   1361  O   VAL A 241      21.983   0.071  49.194  1.00 49.59           O  
ANISOU 1361  O   VAL A 241     4098   5936   8809    953   1508    134       O  
ATOM   1362  CB  VAL A 241      19.390   0.752  47.284  1.00 43.15           C  
ANISOU 1362  CB  VAL A 241     2780   5605   8012   1162   1346     32       C  
ATOM   1363  CG1 VAL A 241      20.338   1.942  47.280  1.00 41.47           C  
ANISOU 1363  CG1 VAL A 241     2826   5233   7697   1311   1268     16       C  
ATOM   1364  CG2 VAL A 241      18.850   0.495  45.885  1.00 49.65           C  
ANISOU 1364  CG2 VAL A 241     3471   6506   8887   1157   1222     38       C  
ATOM   1365  N   SER A 242      20.056  -0.346  50.267  1.00 48.88           N  
ANISOU 1365  N   SER A 242     3621   6234   8718    927   1688     72       N  
ATOM   1366  CA  SER A 242      20.597   0.015  51.568  1.00 42.44           C  
ANISOU 1366  CA  SER A 242     2950   5340   7836    953   1794     65       C  
ATOM   1367  C   SER A 242      21.190  -1.157  52.336  1.00 41.52           C  
ANISOU 1367  C   SER A 242     2924   5100   7751    748   1906    126       C  
ATOM   1368  O   SER A 242      21.973  -0.928  53.262  1.00 51.63           O  
ANISOU 1368  O   SER A 242     4387   6245   8983    756   1969    137       O  
ATOM   1369  CB  SER A 242      19.507   0.669  52.428  1.00 50.91           C  
ANISOU 1369  CB  SER A 242     3844   6660   8841   1071   1886    -12       C  
ATOM   1370  OG  SER A 242      18.894   1.749  51.747  1.00 55.01           O  
ANISOU 1370  OG  SER A 242     4274   7304   9324   1271   1782    -77       O  
ATOM   1371  N   PHE A 243      20.838  -2.398  52.002  1.00 41.96           N  
ANISOU 1371  N   PHE A 243     2869   5206   7867    560   1925    162       N  
ATOM   1372  CA  PHE A 243      21.372  -3.534  52.747  1.00 60.02           C  
ANISOU 1372  CA  PHE A 243     5263   7389  10154    361   2019    213       C  
ATOM   1373  C   PHE A 243      22.129  -4.532  51.885  1.00 68.77           C  
ANISOU 1373  C   PHE A 243     6485   8314  11331    215   1933    274       C  
ATOM   1374  O   PHE A 243      23.260  -4.897  52.226  1.00 69.31           O  
ANISOU 1374  O   PHE A 243     6779   8156  11399    160   1946    316       O  
ATOM   1375  CB  PHE A 243      20.240  -4.252  53.495  1.00 43.80           C  
ANISOU 1375  CB  PHE A 243     3004   5589   8051    225   2137    196       C  
ATOM   1376  CG  PHE A 243      20.722  -5.283  54.472  1.00 43.37           C  
ANISOU 1376  CG  PHE A 243     3080   5454   7945     34   2235    240       C  
ATOM   1377  CD1 PHE A 243      21.437  -4.905  55.596  1.00 42.58           C  
ANISOU 1377  CD1 PHE A 243     3158   5229   7790     86   2323    241       C  
ATOM   1378  CD2 PHE A 243      20.461  -6.627  54.269  1.00 43.84           C  
ANISOU 1378  CD2 PHE A 243     3100   5565   7990   -198   2224    278       C  
ATOM   1379  CE1 PHE A 243      21.885  -5.851  56.500  1.00 42.25           C  
ANISOU 1379  CE1 PHE A 243     3249   5118   7684    -81   2400    278       C  
ATOM   1380  CE2 PHE A 243      20.905  -7.577  55.169  1.00 50.89           C  
ANISOU 1380  CE2 PHE A 243     4140   6393   8805   -368   2290    317       C  
ATOM   1381  CZ  PHE A 243      21.618  -7.188  56.286  1.00 42.72           C  
ANISOU 1381  CZ  PHE A 243     3278   5235   7719   -306   2378    316       C  
ATOM   1382  N   PHE A 244      21.546  -4.988  50.775  1.00 67.63           N  
ANISOU 1382  N   PHE A 244     6196   8263  11238    156   1840    277       N  
ATOM   1383  CA  PHE A 244      22.117  -6.128  50.061  1.00 59.19           C  
ANISOU 1383  CA  PHE A 244     5223   7057  10210    -12   1765    328       C  
ATOM   1384  C   PHE A 244      23.356  -5.736  49.265  1.00 52.03           C  
ANISOU 1384  C   PHE A 244     4525   5878   9367     80   1659    360       C  
ATOM   1385  O   PHE A 244      24.381  -6.430  49.310  1.00 55.02           O  
ANISOU 1385  O   PHE A 244     5102   6055   9749     -5   1644    401       O  
ATOM   1386  CB  PHE A 244      21.068  -6.750  49.137  1.00 61.26           C  
ANISOU 1386  CB  PHE A 244     5266   7515  10494   -116   1694    320       C  
ATOM   1387  CG  PHE A 244      20.000  -7.520  49.862  1.00 52.55           C  
ANISOU 1387  CG  PHE A 244     3991   6659   9319   -283   1789    309       C  
ATOM   1388  CD1 PHE A 244      20.330  -8.594  50.672  1.00 50.03           C  
ANISOU 1388  CD1 PHE A 244     3795   6296   8919   -477   1853    345       C  
ATOM   1389  CD2 PHE A 244      18.664  -7.181  49.719  1.00 45.28           C  
ANISOU 1389  CD2 PHE A 244     2790   6020   8394   -245   1805    265       C  
ATOM   1390  CE1 PHE A 244      19.349  -9.305  51.335  1.00 45.56           C  
ANISOU 1390  CE1 PHE A 244     3081   5958   8273   -643   1935    343       C  
ATOM   1391  CE2 PHE A 244      17.682  -7.886  50.378  1.00 47.63           C  
ANISOU 1391  CE2 PHE A 244     2923   6550   8623   -407   1894    261       C  
ATOM   1392  CZ  PHE A 244      18.023  -8.951  51.187  1.00 47.41           C  
ANISOU 1392  CZ  PHE A 244     3025   6471   8517   -613   1961    304       C  
ATOM   1393  N   ILE A 245      23.272  -4.632  48.519  1.00 47.89           N  
ANISOU 1393  N   ILE A 245     3970   5360   8868    254   1572    336       N  
ATOM   1394  CA  ILE A 245      24.405  -4.203  47.697  1.00 49.30           C  
ANISOU 1394  CA  ILE A 245     4347   5304   9079    321   1461    369       C  
ATOM   1395  C   ILE A 245      25.641  -3.900  48.537  1.00 58.38           C  
ANISOU 1395  C   ILE A 245     5746   6245  10191    334   1514    399       C  
ATOM   1396  O   ILE A 245      26.718  -4.439  48.228  1.00 69.18           O  
ANISOU 1396  O   ILE A 245     7289   7394  11602    255   1479    452       O  
ATOM   1397  CB  ILE A 245      23.986  -3.020  46.801  1.00 50.05           C  
ANISOU 1397  CB  ILE A 245     4383   5495   9141    492   1343    328       C  
ATOM   1398  CG1 ILE A 245      22.903  -3.456  45.812  1.00 35.45           C  
ANISOU 1398  CG1 ILE A 245     2303   3823   7345    462   1274    310       C  
ATOM   1399  CG2 ILE A 245      25.190  -2.451  46.068  1.00 31.39           C  
ANISOU 1399  CG2 ILE A 245     2253   2936   6738    531   1226    357       C  
ATOM   1400  CD1 ILE A 245      22.400  -2.337  44.925  1.00 36.17           C  
ANISOU 1400  CD1 ILE A 245     2330   4023   7389    642   1157    265       C  
ATOM   1401  N   PRO A 246      25.575  -3.067  49.586  1.00 49.12           N  
ANISOU 1401  N   PRO A 246     4604   5129   8932    426   1591    368       N  
ATOM   1402  CA  PRO A 246      26.783  -2.853  50.399  1.00 42.17           C  
ANISOU 1402  CA  PRO A 246     3959   4065   7997    407   1635    402       C  
ATOM   1403  C   PRO A 246      27.267  -4.112  51.092  1.00 45.01           C  
ANISOU 1403  C   PRO A 246     4403   4289   8410    267   1735    442       C  
ATOM   1404  O   PRO A 246      28.477  -4.275  51.271  1.00 57.23           O  
ANISOU 1404  O   PRO A 246     6160   5628   9959    214   1733    492       O  
ATOM   1405  CB  PRO A 246      26.346  -1.779  51.406  1.00 39.30           C  
ANISOU 1405  CB  PRO A 246     3572   3836   7524    540   1694    346       C  
ATOM   1406  CG  PRO A 246      24.873  -1.909  51.478  1.00 40.99           C  
ANISOU 1406  CG  PRO A 246     3520   4293   7762    575   1749    294       C  
ATOM   1407  CD  PRO A 246      24.439  -2.276  50.096  1.00 43.56           C  
ANISOU 1407  CD  PRO A 246     3725   4665   8163    550   1638    300       C  
ATOM   1408  N   LEU A 247      26.363  -5.020  51.465  1.00 43.03           N  
ANISOU 1408  N   LEU A 247     3998   4195   8156    179   1804    418       N  
ATOM   1409  CA  LEU A 247      26.779  -6.285  52.064  1.00 44.34           C  
ANISOU 1409  CA  LEU A 247     4266   4308   8272     38   1845    431       C  
ATOM   1410  C   LEU A 247      27.625  -7.103  51.094  1.00 43.55           C  
ANISOU 1410  C   LEU A 247     4287   4077   8183      6   1715    447       C  
ATOM   1411  O   LEU A 247      28.699  -7.607  51.455  1.00 37.97           O  
ANISOU 1411  O   LEU A 247     3758   3294   7377     22   1687    432       O  
ATOM   1412  CB  LEU A 247      25.551  -7.078  52.514  1.00 49.41           C  
ANISOU 1412  CB  LEU A 247     4722   5208   8843   -113   1907    413       C  
ATOM   1413  CG  LEU A 247      25.737  -8.577  52.757  1.00 49.30           C  
ANISOU 1413  CG  LEU A 247     4799   5215   8718   -314   1877    431       C  
ATOM   1414  CD1 LEU A 247      26.718  -8.828  53.889  1.00 53.36           C  
ANISOU 1414  CD1 LEU A 247     5536   5609   9128   -317   1922    433       C  
ATOM   1415  CD2 LEU A 247      24.397  -9.237  53.049  1.00 49.77           C  
ANISOU 1415  CD2 LEU A 247     4653   5536   8721   -478   1932    427       C  
ATOM   1416  N   THR A 248      27.145  -7.264  49.858  1.00 50.79           N  
ANISOU 1416  N   THR A 248     5088   5047   9165    -20   1616    455       N  
ATOM   1417  CA  THR A 248      27.902  -8.032  48.874  1.00 54.16           C  
ANISOU 1417  CA  THR A 248     5616   5406   9559    -36   1477    458       C  
ATOM   1418  C   THR A 248      29.234  -7.361  48.558  1.00 50.87           C  
ANISOU 1418  C   THR A 248     5315   4885   9127    149   1425    438       C  
ATOM   1419  O   THR A 248      30.268  -8.039  48.441  1.00 59.37           O  
ANISOU 1419  O   THR A 248     6485   6067  10006    127   1341    407       O  
ATOM   1420  CB  THR A 248      27.076  -8.219  47.600  1.00 42.47           C  
ANISOU 1420  CB  THR A 248     3977   4007   8154    -94   1385    470       C  
ATOM   1421  OG1 THR A 248      26.736  -6.938  47.054  1.00 51.21           O  
ANISOU 1421  OG1 THR A 248     4984   5081   9394     35   1377    476       O  
ATOM   1422  CG2 THR A 248      25.801  -8.994  47.901  1.00 38.95           C  
ANISOU 1422  CG2 THR A 248     3359   3794   7646   -277   1427    462       C  
ATOM   1423  N   ILE A 249      29.231  -6.031  48.416  1.00 25.21           N  
ANISOU 1423  N   ILE A 249     2101   1646   5831    177   1384    455       N  
ATOM   1424  CA  ILE A 249      30.482  -5.317  48.173  1.00 23.04           C  
ANISOU 1424  CA  ILE A 249     1883   1577   5292    133   1295    440       C  
ATOM   1425  C   ILE A 249      31.453  -5.545  49.324  1.00 42.30           C  
ANISOU 1425  C   ILE A 249     4446   4073   7552    152   1327    404       C  
ATOM   1426  O   ILE A 249      32.651  -5.766  49.113  1.00 41.99           O  
ANISOU 1426  O   ILE A 249     4505   4128   7320    142   1225    374       O  
ATOM   1427  CB  ILE A 249      30.213  -3.816  47.950  1.00 25.92           C  
ANISOU 1427  CB  ILE A 249     2244   1877   5728    145   1308    484       C  
ATOM   1428  CG1 ILE A 249      29.298  -3.602  46.743  1.00 26.93           C  
ANISOU 1428  CG1 ILE A 249     2243   1924   6064    155   1267    514       C  
ATOM   1429  CG2 ILE A 249      31.519  -3.063  47.751  1.00 21.24           C  
ANISOU 1429  CG2 ILE A 249     1760   1406   4904    154   1215    457       C  
ATOM   1430  CD1 ILE A 249      28.909  -2.153  46.525  1.00 25.11           C  
ANISOU 1430  CD1 ILE A 249     2045   1806   5689    338   1168    448       C  
ATOM   1431  N   MET A 250      30.944  -5.515  50.558  1.00 38.16           N  
ANISOU 1431  N   MET A 250     3923   3478   7099    174   1470    407       N  
ATOM   1432  CA  MET A 250      31.771  -5.742  51.737  1.00 30.92           C  
ANISOU 1432  CA  MET A 250     3126   2590   6031    178   1509    378       C  
ATOM   1433  C   MET A 250      32.405  -7.127  51.714  1.00 38.66           C  
ANISOU 1433  C   MET A 250     4164   3581   6943    156   1469    346       C  
ATOM   1434  O   MET A 250      33.607  -7.275  51.962  1.00 65.23           O  
ANISOU 1434  O   MET A 250     7611   7006  10168    151   1439    329       O  
ATOM   1435  CB  MET A 250      30.915  -5.560  52.990  1.00 31.75           C  
ANISOU 1435  CB  MET A 250     3233   2566   6266    215   1680    385       C  
ATOM   1436  CG  MET A 250      31.188  -4.292  53.773  1.00 42.66           C  
ANISOU 1436  CG  MET A 250     4672   3978   7560    162   1732    436       C  
ATOM   1437  SD  MET A 250      29.891  -3.985  54.986  1.00 49.75           S  
ANISOU 1437  SD  MET A 250     5559   4635   8709    216   1968    469       S  
ATOM   1438  CE  MET A 250      29.601  -5.641  55.600  1.00 47.61           C  
ANISOU 1438  CE  MET A 250     5274   4316   8498    196   2073    413       C  
ATOM   1439  N   VAL A 251      31.605  -8.156  51.428  1.00 25.30           N  
ANISOU 1439  N   VAL A 251     2436   1807   5370    103   1485    358       N  
ATOM   1440  CA  VAL A 251      32.124  -9.525  51.408  1.00 34.98           C  
ANISOU 1440  CA  VAL A 251     3800   3080   6410    -32   1364    358       C  
ATOM   1441  C   VAL A 251      33.223  -9.666  50.358  1.00 37.15           C  
ANISOU 1441  C   VAL A 251     4087   3397   6632      7   1262    347       C  
ATOM   1442  O   VAL A 251      34.326 -10.175  50.636  1.00 41.28           O  
ANISOU 1442  O   VAL A 251     4707   3938   7041     -7   1238    335       O  
ATOM   1443  CB  VAL A 251      30.980 -10.525  51.163  1.00 36.57           C  
ANISOU 1443  CB  VAL A 251     3969   3293   6632   -204   1339    393       C  
ATOM   1444  CG1 VAL A 251      31.531 -11.926  50.954  1.00 42.19           C  
ANISOU 1444  CG1 VAL A 251     4779   4011   7241   -316   1265    401       C  
ATOM   1445  CG2 VAL A 251      29.992 -10.500  52.320  1.00 37.14           C  
ANISOU 1445  CG2 VAL A 251     3974   3361   6776   -282   1500    413       C  
ATOM   1446  N   ILE A 252      32.928  -9.228  49.130  1.00 35.13           N  
ANISOU 1446  N   ILE A 252     3733   3160   6453     44   1198    355       N  
ATOM   1447  CA  ILE A 252      33.900  -9.332  48.044  1.00 38.43           C  
ANISOU 1447  CA  ILE A 252     4158   3628   6815     55   1097    351       C  
ATOM   1448  C   ILE A 252      35.187  -8.602  48.411  1.00 36.12           C  
ANISOU 1448  C   ILE A 252     3903   3397   6425     96   1118    338       C  
ATOM   1449  O   ILE A 252      36.294  -9.136  48.251  1.00 37.64           O  
ANISOU 1449  O   ILE A 252     4179   3612   6512     76   1062    328       O  
ATOM   1450  CB  ILE A 252      33.296  -8.803  46.731  1.00 35.62           C  
ANISOU 1450  CB  ILE A 252     3685   3288   6561     80   1032    365       C  
ATOM   1451  CG1 ILE A 252      32.074  -9.637  46.338  1.00 20.89           C  
ANISOU 1451  CG1 ILE A 252     1803   1362   4773     10    998    384       C  
ATOM   1452  CG2 ILE A 252      34.335  -8.821  45.619  1.00 35.54           C  
ANISOU 1452  CG2 ILE A 252     3691   3331   6481     79    929    362       C  
ATOM   1453  CD1 ILE A 252      31.304  -9.081  45.162  1.00 20.92           C  
ANISOU 1453  CD1 ILE A 252     1688   1368   4895     42    939    397       C  
ATOM   1454  N   THR A 253      35.059  -7.369  48.913  1.00 32.54           N  
ANISOU 1454  N   THR A 253     3399   2969   5996    133   1195    343       N  
ATOM   1455  CA  THR A 253      36.234  -6.566  49.230  1.00 18.10           C  
ANISOU 1455  CA  THR A 253     1637   1189   4053    140   1194    340       C  
ATOM   1456  C   THR A 253      37.045  -7.199  50.353  1.00 23.20           C  
ANISOU 1456  C   THR A 253     2386   1826   4602    137   1242    320       C  
ATOM   1457  O   THR A 253      38.277  -7.158  50.332  1.00 17.39           O  
ANISOU 1457  O   THR A 253     1721   1124   3761    134   1201    310       O  
ATOM   1458  CB  THR A 253      35.809  -5.146  49.604  1.00 18.33           C  
ANISOU 1458  CB  THR A 253     1668   1219   4077    150   1220    358       C  
ATOM   1459  OG1 THR A 253      35.058  -4.577  48.526  1.00 27.93           O  
ANISOU 1459  OG1 THR A 253     2809   2426   5377    145   1164    379       O  
ATOM   1460  CG2 THR A 253      37.023  -4.276  49.854  1.00 34.63           C  
ANISOU 1460  CG2 THR A 253     3797   3313   6046    158   1226    360       C  
ATOM   1461  N   TYR A 254      36.371  -7.805  51.335  1.00 18.79           N  
ANISOU 1461  N   TYR A 254     1856   1214   4068    130   1316    312       N  
ATOM   1462  CA  TYR A 254      37.074  -8.453  52.438  1.00 18.89           C  
ANISOU 1462  CA  TYR A 254     1990   1208   3978    111   1347    295       C  
ATOM   1463  C   TYR A 254      37.929  -9.614  51.942  1.00 40.49           C  
ANISOU 1463  C   TYR A 254     4806   3944   6633     64   1247    289       C  
ATOM   1464  O   TYR A 254      39.111  -9.738  52.303  1.00 39.49           O  
ANISOU 1464  O   TYR A 254     4761   3843   6401     63   1228    278       O  
ATOM   1465  CB  TYR A 254      36.060  -8.936  53.477  1.00 19.98           C  
ANISOU 1465  CB  TYR A 254     2155   1277   4161     86   1432    293       C  
ATOM   1466  CG  TYR A 254      36.662  -9.642  54.672  1.00 20.29           C  
ANISOU 1466  CG  TYR A 254     2325   1290   4095     46   1464    280       C  
ATOM   1467  CD1 TYR A 254      37.140  -8.927  55.762  1.00 29.96           C  
ANISOU 1467  CD1 TYR A 254     3593   2527   5263     88   1548    266       C  
ATOM   1468  CD2 TYR A 254      36.743 -11.028  54.711  1.00 20.86           C  
ANISOU 1468  CD2 TYR A 254     2481   1328   4118    -47   1407    289       C  
ATOM   1469  CE1 TYR A 254      37.687  -9.575  56.857  1.00 29.59           C  
ANISOU 1469  CE1 TYR A 254     3668   2454   5121     52   1573    255       C  
ATOM   1470  CE2 TYR A 254      37.289 -11.683  55.797  1.00 21.23           C  
ANISOU 1470  CE2 TYR A 254     2645   1352   4068    -93   1432    283       C  
ATOM   1471  CZ  TYR A 254      37.760 -10.952  56.867  1.00 34.17           C  
ANISOU 1471  CZ  TYR A 254     4324   2999   5659    -37   1514    263       C  
ATOM   1472  OH  TYR A 254      38.304 -11.603  57.951  1.00 41.38           O  
ANISOU 1472  OH  TYR A 254     5357   3888   6477    -82   1534    258       O  
ATOM   1473  N   PHE A 255      37.350 -10.477  51.105  1.00 19.02           N  
ANISOU 1473  N   PHE A 255     2069   1196   3960     18   1179    301       N  
ATOM   1474  CA  PHE A 255      38.130 -11.623  50.638  1.00 34.66           C  
ANISOU 1474  CA  PHE A 255     4136   3175   5860    -36   1088    302       C  
ATOM   1475  C   PHE A 255      39.250 -11.181  49.696  1.00 32.46           C  
ANISOU 1475  C   PHE A 255     3843   2958   5532      2   1013    295       C  
ATOM   1476  O   PHE A 255      40.372 -11.716  49.744  1.00 38.26           O  
ANISOU 1476  O   PHE A 255     4662   3706   6168    -14    967    286       O  
ATOM   1477  CB  PHE A 255      37.207 -12.656  49.995  1.00 29.93           C  
ANISOU 1477  CB  PHE A 255     3533   2531   5308   -118   1036    324       C  
ATOM   1478  CG  PHE A 255      36.436 -13.469  51.003  1.00 28.94           C  
ANISOU 1478  CG  PHE A 255     3465   2353   5179   -213   1089    339       C  
ATOM   1479  CD1 PHE A 255      37.035 -14.532  51.659  1.00 24.19           C  
ANISOU 1479  CD1 PHE A 255     2984   1731   4476   -288   1074    344       C  
ATOM   1480  CD2 PHE A 255      35.124 -13.151  51.315  1.00 21.90           C  
ANISOU 1480  CD2 PHE A 255     2503   1438   4380   -241   1154    354       C  
ATOM   1481  CE1 PHE A 255      36.337 -15.273  52.595  1.00 22.67           C  
ANISOU 1481  CE1 PHE A 255     2841   1503   4270   -398   1122    366       C  
ATOM   1482  CE2 PHE A 255      34.419 -13.889  52.249  1.00 23.26           C  
ANISOU 1482  CE2 PHE A 255     2719   1584   4533   -362   1206    375       C  
ATOM   1483  CZ  PHE A 255      35.027 -14.951  52.891  1.00 23.65           C  
ANISOU 1483  CZ  PHE A 255     2889   1620   4477   -443   1190    383       C  
ATOM   1484  N   LEU A 256      38.983 -10.173  48.862  1.00 28.97           N  
ANISOU 1484  N   LEU A 256     3300   2553   5155     44   1000    300       N  
ATOM   1485  CA  LEU A 256      40.046  -9.611  48.038  1.00 24.68           C  
ANISOU 1485  CA  LEU A 256     2752   2066   4557     64    934    295       C  
ATOM   1486  C   LEU A 256      41.153  -9.012  48.897  1.00 28.04           C  
ANISOU 1486  C   LEU A 256     3241   2524   4890     82    971    282       C  
ATOM   1487  O   LEU A 256      42.331  -9.070  48.525  1.00 15.36           O  
ANISOU 1487  O   LEU A 256     1683    950   3202     79    912    274       O  
ATOM   1488  CB  LEU A 256      39.467  -8.563  47.091  1.00 27.07           C  
ANISOU 1488  CB  LEU A 256     2948   2394   4943     87    915    307       C  
ATOM   1489  CG  LEU A 256      38.525  -9.086  46.007  1.00 16.67           C  
ANISOU 1489  CG  LEU A 256     1566   1053   3716     71    856    319       C  
ATOM   1490  CD1 LEU A 256      38.105  -7.963  45.075  1.00 16.50           C  
ANISOU 1490  CD1 LEU A 256     1449   1057   3764     90    828    331       C  
ATOM   1491  CD2 LEU A 256      39.175 -10.219  45.231  1.00 16.47           C  
ANISOU 1491  CD2 LEU A 256     1607   1024   3628     37    763    315       C  
ATOM   1492  N   THR A 257      40.796  -8.447  50.054  1.00 28.20           N  
ANISOU 1492  N   THR A 257     3264   2532   4918    100   1068    282       N  
ATOM   1493  CA  THR A 257      41.794  -7.881  50.954  1.00 27.51           C  
ANISOU 1493  CA  THR A 257     3245   2469   4739    114   1104    272       C  
ATOM   1494  C   THR A 257      42.681  -8.968  51.543  1.00 26.37           C  
ANISOU 1494  C   THR A 257     3207   2310   4501     90   1082    258       C  
ATOM   1495  O   THR A 257      43.902  -8.791  51.649  1.00 31.23           O  
ANISOU 1495  O   THR A 257     3879   2956   5029     93   1049    248       O  
ATOM   1496  CB  THR A 257      41.104  -7.088  52.067  1.00 23.06           C  
ANISOU 1496  CB  THR A 257     2668   1888   4206    136   1217    278       C  
ATOM   1497  OG1 THR A 257      40.464  -5.932  51.511  1.00 22.86           O  
ANISOU 1497  OG1 THR A 257     2559   1876   4251    152   1227    298       O  
ATOM   1498  CG2 THR A 257      42.106  -6.648  53.122  1.00 16.22           C  
ANISOU 1498  CG2 THR A 257     1891   1037   3236    145   1254    268       C  
ATOM   1499  N   ILE A 258      42.089 -10.100  51.937  1.00 24.71           N  
ANISOU 1499  N   ILE A 258     3032   2048   4307     57   1094    258       N  
ATOM   1500  CA  ILE A 258      42.925 -11.174  52.476  1.00 23.52           C  
ANISOU 1500  CA  ILE A 258     2993   1877   4065     21   1063    250       C  
ATOM   1501  C   ILE A 258      43.872 -11.692  51.395  1.00 20.04           C  
ANISOU 1501  C   ILE A 258     2573   1463   3579      6    955    250       C  
ATOM   1502  O   ILE A 258      45.056 -11.961  51.661  1.00 20.59           O  
ANISOU 1502  O   ILE A 258     2715   1549   3561      2    921    241       O  
ATOM   1503  CB  ILE A 258      42.071 -12.302  53.097  1.00 33.32           C  
ANISOU 1503  CB  ILE A 258     4284   3050   5326    -36   1089    258       C  
ATOM   1504  CG1 ILE A 258      41.572 -13.300  52.048  1.00 44.53           C  
ANISOU 1504  CG1 ILE A 258     5692   4443   6782    -89   1011    275       C  
ATOM   1505  CG2 ILE A 258      40.913 -11.729  53.899  1.00 38.16           C  
ANISOU 1505  CG2 ILE A 258     4855   3634   6010    -22   1195    260       C  
ATOM   1506  CD1 ILE A 258      40.751 -14.438  52.620  1.00 50.46           C  
ANISOU 1506  CD1 ILE A 258     6502   5128   7541   -176   1027    293       C  
ATOM   1507  N   LYS A 259      43.395 -11.766  50.145  1.00 17.48           N  
ANISOU 1507  N   LYS A 259     2183   1145   3315      2    899    259       N  
ATOM   1508  CA  LYS A 259      44.284 -12.209  49.069  1.00 15.44           C  
ANISOU 1508  CA  LYS A 259     1944    910   3011     -9    801    258       C  
ATOM   1509  C   LYS A 259      45.407 -11.205  48.815  1.00 16.61           C  
ANISOU 1509  C   LYS A 259     2082   1118   3110     27    783    247       C  
ATOM   1510  O   LYS A 259      46.565 -11.595  48.610  1.00 21.72           O  
ANISOU 1510  O   LYS A 259     2788   1782   3682     18    727    239       O  
ATOM   1511  CB  LYS A 259      43.493 -12.456  47.784  1.00 21.68           C  
ANISOU 1511  CB  LYS A 259     2671   1692   3874    -22    747    270       C  
ATOM   1512  CG  LYS A 259      42.668 -13.730  47.792  1.00 40.80           C  
ANISOU 1512  CG  LYS A 259     5132   4051   6318    -82    731    285       C  
ATOM   1513  CD  LYS A 259      42.439 -14.234  46.375  1.00 58.01           C  
ANISOU 1513  CD  LYS A 259     7290   6227   8524   -105    646    294       C  
ATOM   1514  CE  LYS A 259      41.895 -15.653  46.370  1.00 71.78           C  
ANISOU 1514  CE  LYS A 259     9107   7908  10258   -190    615    313       C  
ATOM   1515  NZ  LYS A 259      41.796 -16.204  44.990  1.00 79.28           N  
ANISOU 1515  NZ  LYS A 259    10055   8852  11215   -217    529    322       N  
ATOM   1516  N   SER A 260      45.090  -9.908  48.839  1.00 28.89           N  
ANISOU 1516  N   SER A 260     3572   2701   4705     60    826    248       N  
ATOM   1517  CA  SER A 260      46.113  -8.893  48.605  1.00 19.06           C  
ANISOU 1517  CA  SER A 260     2329   1503   3409     80    805    242       C  
ATOM   1518  C   SER A 260      47.159  -8.888  49.714  1.00 16.01           C  
ANISOU 1518  C   SER A 260     2026   1123   2934     83    829    230       C  
ATOM   1519  O   SER A 260      48.354  -8.712  49.446  1.00 27.69           O  
ANISOU 1519  O   SER A 260     3541   2631   4348     84    780    222       O  
ATOM   1520  CB  SER A 260      45.465  -7.518  48.466  1.00 18.28           C  
ANISOU 1520  CB  SER A 260     2159   1418   3368    103    844    252       C  
ATOM   1521  OG  SER A 260      44.477  -7.519  47.450  1.00 34.23           O  
ANISOU 1521  OG  SER A 260     4100   3431   5476    100    817    263       O  
ATOM   1522  N   LEU A 261      46.737  -9.084  50.965  1.00 14.08           N  
ANISOU 1522  N   LEU A 261     1817    849   2685     83    904    229       N  
ATOM   1523  CA  LEU A 261      47.707  -9.137  52.056  1.00 14.88           C  
ANISOU 1523  CA  LEU A 261     2004    952   2700     84    924    218       C  
ATOM   1524  C   LEU A 261      48.589 -10.378  51.953  1.00 25.55           C  
ANISOU 1524  C   LEU A 261     3425   2291   3990     56    857    212       C  
ATOM   1525  O   LEU A 261      49.788 -10.325  52.267  1.00 39.75           O  
ANISOU 1525  O   LEU A 261     5279   4109   5715     58    829    203       O  
ATOM   1526  CB  LEU A 261      46.991  -9.081  53.406  1.00 19.49           C  
ANISOU 1526  CB  LEU A 261     2615   1500   3291     88   1021    218       C  
ATOM   1527  CG  LEU A 261      46.337  -7.736  53.735  1.00 14.77           C  
ANISOU 1527  CG  LEU A 261     1965    912   2734    118   1096    226       C  
ATOM   1528  CD1 LEU A 261      45.763  -7.729  55.146  1.00 15.42           C  
ANISOU 1528  CD1 LEU A 261     2088    958   2811    123   1197    223       C  
ATOM   1529  CD2 LEU A 261      47.331  -6.599  53.553  1.00 14.20           C  
ANISOU 1529  CD2 LEU A 261     1904    881   2610    134   1067    225       C  
ATOM   1530  N   GLN A 262      48.017 -11.506  51.518  1.00 20.16           N  
ANISOU 1530  N   GLN A 262     2748   1575   3338     26    826    219       N  
ATOM   1531  CA  GLN A 262      48.840 -12.685  51.259  1.00 14.26           C  
ANISOU 1531  CA  GLN A 262     2069    813   2536     -5    753    219       C  
ATOM   1532  C   GLN A 262      49.887 -12.399  50.186  1.00 35.17           C  
ANISOU 1532  C   GLN A 262     4700   3506   5156      7    678    214       C  
ATOM   1533  O   GLN A 262      51.058 -12.785  50.322  1.00 26.76           O  
ANISOU 1533  O   GLN A 262     3692   2449   4024      1    636    207       O  
ATOM   1534  CB  GLN A 262      47.948 -13.855  50.849  1.00 14.89           C  
ANISOU 1534  CB  GLN A 262     2158    844   2657    -47    728    233       C  
ATOM   1535  CG  GLN A 262      47.201 -14.486  52.009  1.00 39.25           C  
ANISOU 1535  CG  GLN A 262     5294   3873   5747    -79    788    240       C  
ATOM   1536  CD  GLN A 262      46.274 -15.597  51.567  1.00 41.03           C  
ANISOU 1536  CD  GLN A 262     5531   4046   6012   -137    759    259       C  
ATOM   1537  OE1 GLN A 262      46.207 -15.933  50.384  1.00 46.53           O  
ANISOU 1537  OE1 GLN A 262     6202   4747   6730   -149    692    266       O  
ATOM   1538  NE2 GLN A 262      45.551 -16.176  52.518  1.00 42.78           N  
ANISOU 1538  NE2 GLN A 262     5798   4215   6241   -181    808    270       N  
ATOM   1539  N   LYS A 263      49.478 -11.720  49.110  1.00 28.74           N  
ANISOU 1539  N   LYS A 263     3808   2718   4393     22    660    216       N  
ATOM   1540  CA  LYS A 263      50.425 -11.312  48.074  1.00 27.54           C  
ANISOU 1540  CA  LYS A 263     3641   2608   4215     31    596    210       C  
ATOM   1541  C   LYS A 263      51.527 -10.428  48.649  1.00 19.99           C  
ANISOU 1541  C   LYS A 263     2709   1685   3202     50    608    200       C  
ATOM   1542  O   LYS A 263      52.705 -10.570  48.292  1.00 11.67           O  
ANISOU 1542  O   LYS A 263     1687    651   2096     47    554    193       O  
ATOM   1543  CB  LYS A 263      49.678 -10.580  46.957  1.00 34.12           C  
ANISOU 1543  CB  LYS A 263     4388   3459   5115     43    585    216       C  
ATOM   1544  CG  LYS A 263      50.565  -9.867  45.950  1.00 36.71           C  
ANISOU 1544  CG  LYS A 263     4700   3830   5420     53    532    210       C  
ATOM   1545  CD  LYS A 263      51.237 -10.837  44.998  1.00 42.12           C  
ANISOU 1545  CD  LYS A 263     5418   4514   6073     35    455    207       C  
ATOM   1546  CE  LYS A 263      51.900 -10.101  43.843  1.00 48.88           C  
ANISOU 1546  CE  LYS A 263     6248   5407   6917     44    408    201       C  
ATOM   1547  NZ  LYS A 263      50.925  -9.261  43.087  1.00 48.95           N  
ANISOU 1547  NZ  LYS A 263     6183   5422   6993     53    413    208       N  
ATOM   1548  N   GLU A 264      51.153  -9.497  49.527  1.00 25.74           N  
ANISOU 1548  N   GLU A 264     3424   2415   3938     68    677    200       N  
ATOM   1549  CA  GLU A 264      52.126  -8.615  50.167  1.00 12.33           C  
ANISOU 1549  CA  GLU A 264     1759    741   2184     83    689    193       C  
ATOM   1550  C   GLU A 264      53.167  -9.415  50.944  1.00 11.94           C  
ANISOU 1550  C   GLU A 264     1791    682   2063     72    670    184       C  
ATOM   1551  O   GLU A 264      54.376  -9.175  50.824  1.00 11.52           O  
ANISOU 1551  O   GLU A 264     1764    653   1961     74    628    177       O  
ATOM   1552  CB  GLU A 264      51.389  -7.640  51.086  1.00 12.26           C  
ANISOU 1552  CB  GLU A 264     1738    725   2197    101    772    197       C  
ATOM   1553  CG  GLU A 264      52.046  -6.291  51.265  1.00 19.56           C  
ANISOU 1553  CG  GLU A 264     2669   1673   3088    118    777    195       C  
ATOM   1554  CD  GLU A 264      51.079  -5.265  51.813  1.00 14.33           C  
ANISOU 1554  CD  GLU A 264     1982    999   2464    136    851    205       C  
ATOM   1555  OE1 GLU A 264      49.939  -5.191  51.302  1.00 12.62           O  
ANISOU 1555  OE1 GLU A 264     1702    772   2322    137    871    216       O  
ATOM   1556  OE2 GLU A 264      51.455  -4.546  52.760  1.00 12.48           O  
ANISOU 1556  OE2 GLU A 264     1795    762   2187    147    888    203       O  
ATOM   1557  N   ALA A 265      52.708 -10.371  51.756  1.00 31.54           N  
ANISOU 1557  N   ALA A 265     4317   3126   4542     57    700    187       N  
ATOM   1558  CA  ALA A 265      53.638 -11.177  52.544  1.00 12.58           C  
ANISOU 1558  CA  ALA A 265     1999    708   2074     43    680    181       C  
ATOM   1559  C   ALA A 265      54.556 -12.000  51.644  1.00 27.31           C  
ANISOU 1559  C   ALA A 265     3879   2581   3918     27    594    181       C  
ATOM   1560  O   ALA A 265      55.758 -12.137  51.921  1.00 31.03           O  
ANISOU 1560  O   ALA A 265     4393   3062   4334     27    560    175       O  
ATOM   1561  CB  ALA A 265      52.868 -12.083  53.502  1.00 13.33           C  
ANISOU 1561  CB  ALA A 265     2142    752   2171     23    726    186       C  
ATOM   1562  N   ALA A1001      54.010 -12.546  50.554  1.00 13.69           N  
ANISOU 1562  N   ALA A1001     2118    848   2235     15    557    188       N  
ATOM   1563  CA  ALA A1001      54.829 -13.319  49.624  1.00 12.04           C  
ANISOU 1563  CA  ALA A1001     1925    643   2005      0    477    188       C  
ATOM   1564  C   ALA A1001      55.918 -12.451  49.004  1.00 23.80           C  
ANISOU 1564  C   ALA A1001     3390   2180   3472     19    443    178       C  
ATOM   1565  O   ALA A1001      57.084 -12.863  48.907  1.00 11.14           O  
ANISOU 1565  O   ALA A1001     1821    583   1828     14    397    174       O  
ATOM   1566  CB  ALA A1001      53.945 -13.931  48.537  1.00 12.22           C  
ANISOU 1566  CB  ALA A1001     1918    647   2077    -17    447    198       C  
ATOM   1567  N   ASP A1002      55.552 -11.240  48.575  1.00 14.82           N  
ANISOU 1567  N   ASP A1002     2195   1073   2364     38    466    176       N  
ATOM   1568  CA  ASP A1002      56.534 -10.337  47.984  1.00 14.01           C  
ANISOU 1568  CA  ASP A1002     2073   1009   2240     50    435    168       C  
ATOM   1569  C   ASP A1002      57.609  -9.958  48.994  1.00 10.40           C  
ANISOU 1569  C   ASP A1002     1661    561   1729     57    443    161       C  
ATOM   1570  O   ASP A1002      58.790  -9.840  48.643  1.00 21.60           O  
ANISOU 1570  O   ASP A1002     3091   1999   3117     57    399    155       O  
ATOM   1571  CB  ASP A1002      55.842  -9.092  47.434  1.00 28.37           C  
ANISOU 1571  CB  ASP A1002     3829   2849   4102     65    459    171       C  
ATOM   1572  CG  ASP A1002      54.914  -9.407  46.281  1.00 40.56           C  
ANISOU 1572  CG  ASP A1002     5324   4387   5698     59    439    178       C  
ATOM   1573  OD1 ASP A1002      54.758 -10.602  45.954  1.00 45.78           O  
ANISOU 1573  OD1 ASP A1002     6007   5027   6362     42    409    181       O  
ATOM   1574  OD2 ASP A1002      54.341  -8.462  45.700  1.00 43.50           O  
ANISOU 1574  OD2 ASP A1002     5644   4772   6110     69    449    181       O  
ATOM   1575  N   LEU A1003      57.219  -9.748  50.255  1.00 10.74           N  
ANISOU 1575  N   LEU A1003     1732    588   1762     63    501    162       N  
ATOM   1576  CA  LEU A1003      58.214  -9.434  51.276  1.00 10.71           C  
ANISOU 1576  CA  LEU A1003     1780    587   1704     68    507    155       C  
ATOM   1577  C   LEU A1003      59.195 -10.587  51.465  1.00 16.38           C  
ANISOU 1577  C   LEU A1003     2550   1292   2383     54    459    153       C  
ATOM   1578  O   LEU A1003      60.410 -10.367  51.590  1.00 38.07           O  
ANISOU 1578  O   LEU A1003     5317   4054   5094     57    426    147       O  
ATOM   1579  CB  LEU A1003      57.532  -9.091  52.599  1.00 20.72           C  
ANISOU 1579  CB  LEU A1003     3077   1834   2963     76    580    157       C  
ATOM   1580  CG  LEU A1003      58.498  -8.818  53.754  1.00 11.22           C  
ANISOU 1580  CG  LEU A1003     1939    628   1697     81    586    150       C  
ATOM   1581  CD1 LEU A1003      59.411  -7.646  53.428  1.00 33.36           C  
ANISOU 1581  CD1 LEU A1003     4727   3462   4485     93    558    145       C  
ATOM   1582  CD2 LEU A1003      57.741  -8.565  55.044  1.00 31.09           C  
ANISOU 1582  CD2 LEU A1003     4492   3119   4200     88    664    151       C  
ATOM   1583  N   GLU A1004      58.690 -11.824  51.499  1.00 11.14           N  
ANISOU 1583  N   GLU A1004     1909    596   1729     36    454    160       N  
ATOM   1584  CA  GLU A1004      59.596 -12.966  51.616  1.00 11.27           C  
ANISOU 1584  CA  GLU A1004     1975    593   1713     21    407    161       C  
ATOM   1585  C   GLU A1004      60.533 -13.046  50.415  1.00 10.78           C  
ANISOU 1585  C   GLU A1004     1885    558   1655     21    342    158       C  
ATOM   1586  O   GLU A1004      61.717 -13.379  50.560  1.00 10.69           O  
ANISOU 1586  O   GLU A1004     1901    548   1611     19    308    155       O  
ATOM   1587  CB  GLU A1004      58.812 -14.268  51.772  1.00 23.20           C  
ANISOU 1587  CB  GLU A1004     3519   2058   3238     -3    411    171       C  
ATOM   1588  CG  GLU A1004      59.710 -15.496  51.875  1.00 36.98           C  
ANISOU 1588  CG  GLU A1004     5318   3779   4952    -20    365    175       C  
ATOM   1589  CD  GLU A1004      58.945 -16.771  52.171  1.00 48.33           C  
ANISOU 1589  CD  GLU A1004     6801   5163   6398    -49    372    188       C  
ATOM   1590  OE1 GLU A1004      58.281 -16.840  53.227  1.00 46.14           O  
ANISOU 1590  OE1 GLU A1004     6563   4858   6110    -57    424    190       O  
ATOM   1591  OE2 GLU A1004      59.010 -17.706  51.346  1.00 52.52           O  
ANISOU 1591  OE2 GLU A1004     7333   5676   6946    -66    327    196       O  
ATOM   1592  N   ASP A1005      60.022 -12.740  49.219  1.00 15.55           N  
ANISOU 1592  N   ASP A1005     2434   1178   2296     23    327    159       N  
ATOM   1593  CA  ASP A1005      60.878 -12.723  48.034  1.00 10.08           C  
ANISOU 1593  CA  ASP A1005     1717    508   1604     23    271    155       C  
ATOM   1594  C   ASP A1005      61.983 -11.679  48.167  1.00 25.59           C  
ANISOU 1594  C   ASP A1005     3673   2506   3544     37    265    146       C  
ATOM   1595  O   ASP A1005      63.143 -11.933  47.807  1.00 38.53           O  
ANISOU 1595  O   ASP A1005     5319   4153   5166     35    223    143       O  
ATOM   1596  CB  ASP A1005      60.040 -12.459  46.785  1.00 29.74           C  
ANISOU 1596  CB  ASP A1005     4157   3009   4133     23    262    158       C  
ATOM   1597  CG  ASP A1005      60.852 -12.550  45.509  1.00 39.74           C  
ANISOU 1597  CG  ASP A1005     5410   4295   5396     22    206    154       C  
ATOM   1598  OD1 ASP A1005      60.957 -13.660  44.947  1.00 53.75           O  
ANISOU 1598  OD1 ASP A1005     7203   6048   7173      8    167    158       O  
ATOM   1599  OD2 ASP A1005      61.392 -11.512  45.072  1.00 43.99           O  
ANISOU 1599  OD2 ASP A1005     5920   4865   5928     33    203    147       O  
ATOM   1600  N   ASN A1006      61.635 -10.491  48.668  1.00 14.12           N  
ANISOU 1600  N   ASN A1006     2206   1068   2093     50    307    144       N  
ATOM   1601  CA  ASN A1006      62.639  -9.450  48.870  1.00 12.44           C  
ANISOU 1601  CA  ASN A1006     1992    878   1856     60    299    137       C  
ATOM   1602  C   ASN A1006      63.706  -9.907  49.854  1.00 17.15           C  
ANISOU 1602  C   ASN A1006     2641   1463   2413     57    286    134       C  
ATOM   1603  O   ASN A1006      64.902  -9.660  49.648  1.00 20.49           O  
ANISOU 1603  O   ASN A1006     3063   1900   2821     59    250    129       O  
ATOM   1604  CB  ASN A1006      61.976  -8.164  49.366  1.00 13.83           C  
ANISOU 1604  CB  ASN A1006     2154   1060   2039     73    349    136       C  
ATOM   1605  CG  ASN A1006      61.096  -7.514  48.314  1.00 21.75           C  
ANISOU 1605  CG  ASN A1006     3102   2077   3084     78    357    140       C  
ATOM   1606  OD1 ASN A1006      61.384  -7.578  47.119  1.00 20.93           O  
ANISOU 1606  OD1 ASN A1006     2972   1988   2993     73    318    138       O  
ATOM   1607  ND2 ASN A1006      60.012  -6.884  48.756  1.00 26.14           N  
ANISOU 1607  ND2 ASN A1006     3644   2625   3663     86    410    144       N  
ATOM   1608  N   TRP A1007      63.292 -10.588  50.926  1.00 15.40           N  
ANISOU 1608  N   TRP A1007     2465   1213   2174     53    314    137       N  
ATOM   1609  CA  TRP A1007      64.263 -11.085  51.896  1.00 10.08           C  
ANISOU 1609  CA  TRP A1007     1847    524   1458     50    300    135       C  
ATOM   1610  C   TRP A1007      65.184 -12.121  51.261  1.00 13.56           C  
ANISOU 1610  C   TRP A1007     2293    960   1898     41    247    137       C  
ATOM   1611  O   TRP A1007      66.391 -12.152  51.540  1.00 24.26           O  
ANISOU 1611  O   TRP A1007     3668   2319   3229     42    219    133       O  
ATOM   1612  CB  TRP A1007      63.544 -11.695  53.097  1.00 12.30           C  
ANISOU 1612  CB  TRP A1007     2185    771   1718     45    343    139       C  
ATOM   1613  CG  TRP A1007      64.480 -12.289  54.108  1.00 33.60           C  
ANISOU 1613  CG  TRP A1007     4952   3449   4367     41    328    137       C  
ATOM   1614  CD1 TRP A1007      65.033 -11.653  55.182  1.00 24.17           C  
ANISOU 1614  CD1 TRP A1007     3800   2252   3130     49    340    131       C  
ATOM   1615  CD2 TRP A1007      65.025 -13.615  54.105  1.00 52.56           C  
ANISOU 1615  CD2 TRP A1007     7393   5826   6753     27    294    141       C  
ATOM   1616  NE1 TRP A1007      65.855 -12.512  55.870  1.00 27.79           N  
ANISOU 1616  NE1 TRP A1007     4323   2689   3549     42    314    131       N  
ATOM   1617  CE2 TRP A1007      65.872 -13.720  55.225  1.00 44.86           C  
ANISOU 1617  CE2 TRP A1007     6483   4836   5726     29    287    137       C  
ATOM   1618  CE3 TRP A1007      64.869 -14.727  53.271  1.00 53.58           C  
ANISOU 1618  CE3 TRP A1007     7512   5940   6905     14    268    148       C  
ATOM   1619  CZ2 TRP A1007      66.558 -14.894  55.535  1.00 50.44           C  
ANISOU 1619  CZ2 TRP A1007     7247   5516   6403     18    257    140       C  
ATOM   1620  CZ3 TRP A1007      65.560 -15.889  53.576  1.00 52.28           C  
ANISOU 1620  CZ3 TRP A1007     7405   5749   6712      4    241    151       C  
ATOM   1621  CH2 TRP A1007      66.388 -15.964  54.701  1.00 51.86           C  
ANISOU 1621  CH2 TRP A1007     7416   5681   6606      6    236    147       C  
ATOM   1622  N   GLU A1008      64.620 -12.999  50.426  1.00 16.26           N  
ANISOU 1622  N   GLU A1008     2619   1292   2268     30    234    143       N  
ATOM   1623  CA  GLU A1008      65.426 -13.997  49.728  1.00 17.46           C  
ANISOU 1623  CA  GLU A1008     2775   1437   2421     22    189    145       C  
ATOM   1624  C   GLU A1008      66.483 -13.330  48.858  1.00 12.34           C  
ANISOU 1624  C   GLU A1008     2086    822   1782     30    156    139       C  
ATOM   1625  O   GLU A1008      67.655 -13.730  48.862  1.00 14.67           O  
ANISOU 1625  O   GLU A1008     2396   1116   2063     30    130    137       O  
ATOM   1626  CB  GLU A1008      64.526 -14.898  48.881  1.00 23.46           C  
ANISOU 1626  CB  GLU A1008     3523   2178   3213     10    180    153       C  
ATOM   1627  CG  GLU A1008      63.713 -15.903  49.676  1.00 31.99           C  
ANISOU 1627  CG  GLU A1008     4655   3215   4286     -5    203    162       C  
ATOM   1628  CD  GLU A1008      64.527 -17.112  50.083  1.00 48.36           C  
ANISOU 1628  CD  GLU A1008     6788   5259   6329    -14    183    165       C  
ATOM   1629  OE1 GLU A1008      65.572 -17.367  49.447  1.00 53.79           O  
ANISOU 1629  OE1 GLU A1008     7468   5959   7014    -10    149    162       O  
ATOM   1630  OE2 GLU A1008      64.123 -17.808  51.037  1.00 58.36           O  
ANISOU 1630  OE2 GLU A1008     8114   6487   7572    -26    205    171       O  
ATOM   1631  N   THR A1009      66.076 -12.317  48.089  1.00 16.21           N  
ANISOU 1631  N   THR A1009     2528   1339   2294     36    159    135       N  
ATOM   1632  CA  THR A1009      67.032 -11.581  47.265  1.00 16.27           C  
ANISOU 1632  CA  THR A1009     2502   1375   2307     41    132    130       C  
ATOM   1633  C   THR A1009      68.122 -10.948  48.123  1.00 16.04           C  
ANISOU 1633  C   THR A1009     2490   1352   2255     48    130    125       C  
ATOM   1634  O   THR A1009      69.315 -11.009  47.781  1.00 15.32           O  
ANISOU 1634  O   THR A1009     2390   1267   2163     48    101    123       O  
ATOM   1635  CB  THR A1009      66.306 -10.515  46.445  1.00  8.49           C  
ANISOU 1635  CB  THR A1009     1475    412   1340     46    143    127       C  
ATOM   1636  OG1 THR A1009      65.388 -11.146  45.543  1.00  8.55           O  
ANISOU 1636  OG1 THR A1009     1468    412   1370     40    136    131       O  
ATOM   1637  CG2 THR A1009      67.293  -9.681  45.648  1.00  8.12           C  
ANISOU 1637  CG2 THR A1009     1402    389   1295     50    118    121       C  
ATOM   1638  N   LEU A1010      67.729 -10.340  49.247  1.00  8.90           N  
ANISOU 1638  N   LEU A1010     1609    441   1330     53    162    124       N  
ATOM   1639  CA  LEU A1010      68.701  -9.697  50.125  1.00 27.16           C  
ANISOU 1639  CA  LEU A1010     3946   2755   3618     58    158    120       C  
ATOM   1640  C   LEU A1010      69.724 -10.696  50.651  1.00  9.14           C  
ANISOU 1640  C   LEU A1010     1702    455   1315     54    132    121       C  
ATOM   1641  O   LEU A1010      70.928 -10.416  50.655  1.00  9.02           O  
ANISOU 1641  O   LEU A1010     1685    447   1297     56    105    118       O  
ATOM   1642  CB  LEU A1010      67.981  -8.999  51.280  1.00 21.92           C  
ANISOU 1642  CB  LEU A1010     3313   2083   2933     65    200    119       C  
ATOM   1643  CG  LEU A1010      67.240  -7.712  50.907  1.00  8.97           C  
ANISOU 1643  CG  LEU A1010     1638    459   1310     73    227    117       C  
ATOM   1644  CD1 LEU A1010      66.213  -7.336  51.965  1.00  9.30           C  
ANISOU 1644  CD1 LEU A1010     1710    486   1337     79    282    119       C  
ATOM   1645  CD2 LEU A1010      68.234  -6.582  50.701  1.00  8.73           C  
ANISOU 1645  CD2 LEU A1010     1595    444   1279     77    204    113       C  
ATOM   1646  N   ASN A1011      69.269 -11.872  51.090  1.00 18.61           N  
ANISOU 1646  N   ASN A1011     2941   1629   2500     48    140    125       N  
ATOM   1647  CA  ASN A1011      70.212 -12.868  51.598  1.00 25.82           C  
ANISOU 1647  CA  ASN A1011     3902   2521   3387     44    116    127       C  
ATOM   1648  C   ASN A1011      71.117 -13.402  50.495  1.00  9.63           C  
ANISOU 1648  C   ASN A1011     1822    479   1359     42     81    128       C  
ATOM   1649  O   ASN A1011      72.326 -13.565  50.706  1.00  9.69           O  
ANISOU 1649  O   ASN A1011     1845    482   1353     45     56    126       O  
ATOM   1650  CB  ASN A1011      69.483 -14.020  52.287  1.00 39.76           C  
ANISOU 1650  CB  ASN A1011     5726   4251   5129     35    133    132       C  
ATOM   1651  CG  ASN A1011      69.545 -13.926  53.798  1.00 56.96           C  
ANISOU 1651  CG  ASN A1011     7973   6409   7259     37    149    130       C  
ATOM   1652  OD1 ASN A1011      69.755 -12.851  54.357  1.00 58.57           O  
ANISOU 1652  OD1 ASN A1011     8177   6626   7452     45    158    125       O  
ATOM   1653  ND2 ASN A1011      69.417 -15.066  54.465  1.00 68.00           N  
ANISOU 1653  ND2 ASN A1011     9439   7771   8626     28    150    134       N  
ATOM   1654  N   ASP A1012      70.553 -13.700  49.320  1.00  9.45           N  
ANISOU 1654  N   ASP A1012     1760    464   1368     39     81    130       N  
ATOM   1655  CA  ASP A1012      71.378 -14.176  48.214  1.00  9.29           C  
ANISOU 1655  CA  ASP A1012     1714    450   1367     38     55    131       C  
ATOM   1656  C   ASP A1012      72.499 -13.193  47.909  1.00 40.54           C  
ANISOU 1656  C   ASP A1012     5636   4432   5337     45     39    126       C  
ATOM   1657  O   ASP A1012      73.669 -13.580  47.782  1.00 29.63           O  
ANISOU 1657  O   ASP A1012     4260   3045   3952     46     20    126       O  
ATOM   1658  CB  ASP A1012      70.524 -14.408  46.966  1.00 26.00           C  
ANISOU 1658  CB  ASP A1012     3792   2572   3514     34     56    133       C  
ATOM   1659  CG  ASP A1012      69.669 -15.650  47.067  1.00 24.57           C  
ANISOU 1659  CG  ASP A1012     3647   2359   3327     25     63    140       C  
ATOM   1660  OD1 ASP A1012      69.833 -16.410  48.044  1.00 37.82           O  
ANISOU 1660  OD1 ASP A1012     5385   4011   4975     21     66    143       O  
ATOM   1661  OD2 ASP A1012      68.841 -15.872  46.159  1.00 34.94           O  
ANISOU 1661  OD2 ASP A1012     4936   3673   4668     20     62    143       O  
ATOM   1662  N   ASN A1013      72.168 -11.904  47.824  1.00 41.57           N  
ANISOU 1662  N   ASN A1013     5734   4584   5479     48     49    122       N  
ATOM   1663  CA  ASN A1013      73.191 -10.944  47.434  1.00 23.42           C  
ANISOU 1663  CA  ASN A1013     3401   2302   3195     52     34    119       C  
ATOM   1664  C   ASN A1013      74.143 -10.607  48.578  1.00  8.51           C  
ANISOU 1664  C   ASN A1013     1544    405   1287     55     27    117       C  
ATOM   1665  O   ASN A1013      75.311 -10.302  48.322  1.00  8.42           O  
ANISOU 1665  O   ASN A1013     1514    397   1288     57     10    116       O  
ATOM   1666  CB  ASN A1013      72.531  -9.692  46.867  1.00 32.70           C  
ANISOU 1666  CB  ASN A1013     4541   3499   4384     53     42    115       C  
ATOM   1667  CG  ASN A1013      71.834  -9.963  45.550  1.00 28.76           C  
ANISOU 1667  CG  ASN A1013     4014   3010   3903     50     39    116       C  
ATOM   1668  OD1 ASN A1013      72.478 -10.073  44.505  1.00 10.33           O  
ANISOU 1668  OD1 ASN A1013     1656    684   1585     49     20    116       O  
ATOM   1669  ND2 ASN A1013      70.515 -10.090  45.595  1.00  7.94           N  
ANISOU 1669  ND2 ASN A1013     1384    371   1263     49     57    117       N  
ATOM   1670  N   LEU A1014      73.691 -10.686  49.834  1.00  8.81           N  
ANISOU 1670  N   LEU A1014     1630    427   1290     56     39    116       N  
ATOM   1671  CA  LEU A1014      74.624 -10.580  50.955  1.00  9.06           C  
ANISOU 1671  CA  LEU A1014     1704    445   1294     59     24    114       C  
ATOM   1672  C   LEU A1014      75.650 -11.707  50.922  1.00 16.44           C  
ANISOU 1672  C   LEU A1014     2661   1363   2222     57     -4    117       C  
ATOM   1673  O   LEU A1014      76.848 -11.480  51.146  1.00  9.34           O  
ANISOU 1673  O   LEU A1014     1765    460   1323     60    -29    115       O  
ATOM   1674  CB  LEU A1014      73.862 -10.581  52.281  1.00  9.40           C  
ANISOU 1674  CB  LEU A1014     1805    471   1296     60     44    114       C  
ATOM   1675  CG  LEU A1014      73.259  -9.254  52.752  1.00 26.53           C  
ANISOU 1675  CG  LEU A1014     3971   2649   3460     65     69    110       C  
ATOM   1676  CD1 LEU A1014      72.452  -9.455  54.023  1.00 29.22           C  
ANISOU 1676  CD1 LEU A1014     4375   2969   3757     66     98    110       C  
ATOM   1677  CD2 LEU A1014      74.347  -8.211  52.976  1.00  9.22           C  
ANISOU 1677  CD2 LEU A1014     1771    462   1270     68     47    106       C  
ATOM   1678  N   LYS A1015      75.202 -12.928  50.620  1.00 25.50           N  
ANISOU 1678  N   LYS A1015     3829   2498   3364     53     -2    120       N  
ATOM   1679  CA  LYS A1015      76.138 -14.043  50.527  1.00 21.68           C  
ANISOU 1679  CA  LYS A1015     3374   1994   2871     53    -29    123       C  
ATOM   1680  C   LYS A1015      77.083 -13.868  49.345  1.00  9.48           C  
ANISOU 1680  C   LYS A1015     1775    464   1364     56    -41    123       C  
ATOM   1681  O   LYS A1015      78.271 -14.202  49.439  1.00  9.66           O  
ANISOU 1681  O   LYS A1015     1810    475   1386     59    -66    123       O  
ATOM   1682  CB  LYS A1015      75.374 -15.360  50.412  1.00 40.00           C  
ANISOU 1682  CB  LYS A1015     5732   4292   5176     48    -23    127       C  
ATOM   1683  CG  LYS A1015      74.526 -15.689  51.630  1.00 56.62           C  
ANISOU 1683  CG  LYS A1015     7899   6372   7240     43     -8    129       C  
ATOM   1684  CD  LYS A1015      75.371 -15.788  52.885  1.00 72.18           C  
ANISOU 1684  CD  LYS A1015     9932   8322   9170     46    -33    127       C  
ATOM   1685  CE  LYS A1015      74.525 -16.124  54.102  1.00 86.31           C  
ANISOU 1685  CE  LYS A1015    11793  10085  10915     41    -15    128       C  
ATOM   1686  NZ  LYS A1015      75.342 -16.143  55.346  1.00 92.50           N  
ANISOU 1686  NZ  LYS A1015    12645  10848  11655     43    -43    125       N  
ATOM   1687  N   VAL A1016      76.571 -13.362  48.220  1.00 47.60           N  
ANISOU 1687  N   VAL A1016     6546   5316   6226     55    -23    123       N  
ATOM   1688  CA  VAL A1016      77.437 -13.061  47.080  1.00  8.81           C  
ANISOU 1688  CA  VAL A1016     1583    416   1347     57    -27    123       C  
ATOM   1689  C   VAL A1016      78.512 -12.052  47.472  1.00 18.42           C  
ANISOU 1689  C   VAL A1016     2786   1640   2575     61    -35    121       C  
ATOM   1690  O   VAL A1016      79.695 -12.224  47.155  1.00 17.43           O  
ANISOU 1690  O   VAL A1016     2653   1508   2462     64    -47    122       O  
ATOM   1691  CB  VAL A1016      76.607 -12.565  45.883  1.00  8.43           C  
ANISOU 1691  CB  VAL A1016     1484    390   1327     55    -10    123       C  
ATOM   1692  CG1 VAL A1016      77.525 -11.985  44.815  1.00  8.16           C  
ANISOU 1692  CG1 VAL A1016     1402    370   1327     57    -11    122       C  
ATOM   1693  CG2 VAL A1016      75.783 -13.702  45.307  1.00  9.87           C  
ANISOU 1693  CG2 VAL A1016     1683    564   1505     51     -7    125       C  
ATOM   1694  N   ILE A1017      78.117 -10.988  48.178  1.00 23.69           N  
ANISOU 1694  N   ILE A1017     3452   2315   3235     61    -29    118       N  
ATOM   1695  CA  ILE A1017      79.076  -9.965  48.595  1.00 22.81           C  
ANISOU 1695  CA  ILE A1017     3332   2204   3131     63    -38    116       C  
ATOM   1696  C   ILE A1017      80.131 -10.560  49.517  1.00 29.82           C  
ANISOU 1696  C   ILE A1017     4266   3070   3996     65    -70    115       C  
ATOM   1697  O   ILE A1017      81.320 -10.226  49.421  1.00 25.78           O  
ANISOU 1697  O   ILE A1017     3742   2555   3500     67    -86    115       O  
ATOM   1698  CB  ILE A1017      78.350  -8.780  49.261  1.00 19.35           C  
ANISOU 1698  CB  ILE A1017     2897   1773   2683     63    -28    112       C  
ATOM   1699  CG1 ILE A1017      77.519  -8.017  48.232  1.00  8.16           C  
ANISOU 1699  CG1 ILE A1017     1430    376   1293     62     -9    112       C  
ATOM   1700  CG2 ILE A1017      79.345  -7.840  49.922  1.00  8.61           C  
ANISOU 1700  CG2 ILE A1017     1544    406   1321     66    -43    110       C  
ATOM   1701  CD1 ILE A1017      76.540  -7.045  48.843  1.00 20.91           C  
ANISOU 1701  CD1 ILE A1017     3058   1994   2891     63      3    109       C  
ATOM   1702  N   GLU A1018      79.717 -11.448  50.427  1.00 32.38           N  
ANISOU 1702  N   GLU A1018     4647   3375   4281     65    -82    115       N  
ATOM   1703  CA  GLU A1018      80.666 -12.031  51.373  1.00 28.98           C  
ANISOU 1703  CA  GLU A1018     4268   2918   3824     66   -120    115       C  
ATOM   1704  C   GLU A1018      81.826 -12.726  50.665  1.00 25.41           C  
ANISOU 1704  C   GLU A1018     3802   2456   3396     69   -141    118       C  
ATOM   1705  O   GLU A1018      82.957 -12.706  51.164  1.00 10.14           O  
ANISOU 1705  O   GLU A1018     1883    508   1462     72   -177    117       O  
ATOM   1706  CB  GLU A1018      79.943 -13.011  52.299  1.00 31.88           C  
ANISOU 1706  CB  GLU A1018     4705   3262   4144     65   -125    116       C  
ATOM   1707  CG  GLU A1018      80.849 -13.714  53.300  1.00 55.22           C  
ANISOU 1707  CG  GLU A1018     7726   6187   7068     67   -170    116       C  
ATOM   1708  CD  GLU A1018      80.077 -14.561  54.290  1.00 79.82           C  
ANISOU 1708  CD  GLU A1018    10920   9277  10132     64   -170    117       C  
ATOM   1709  OE1 GLU A1018      78.865 -14.316  54.466  1.00 86.75           O  
ANISOU 1709  OE1 GLU A1018    11803  10163  10996     61   -132    116       O  
ATOM   1710  OE2 GLU A1018      80.682 -15.477  54.887  1.00 90.74           O  
ANISOU 1710  OE2 GLU A1018    12362  10627  11487     66   -206    118       O  
ATOM   1711  N   LYS A1019      81.577 -13.321  49.496  1.00 18.88           N  
ANISOU 1711  N   LYS A1019     2947   1637   2591     70   -122    121       N  
ATOM   1712  CA  LYS A1019      82.597 -14.054  48.756  1.00 11.87           C  
ANISOU 1712  CA  LYS A1019     2050    737   1725     74   -135    124       C  
ATOM   1713  C   LYS A1019      83.055 -13.320  47.498  1.00 13.31           C  
ANISOU 1713  C   LYS A1019     2168    940   1950     75   -109    125       C  
ATOM   1714  O   LYS A1019      83.579 -13.952  46.575  1.00  9.52           O  
ANISOU 1714  O   LYS A1019     1675    453   1488     79   -104    128       O  
ATOM   1715  CB  LYS A1019      82.078 -15.443  48.383  1.00 11.71           C  
ANISOU 1715  CB  LYS A1019     2062    699   1690     74   -134    127       C  
ATOM   1716  CG  LYS A1019      81.759 -16.343  49.564  1.00 25.26           C  
ANISOU 1716  CG  LYS A1019     3855   2385   3359     73   -159    128       C  
ATOM   1717  CD  LYS A1019      83.019 -16.923  50.178  1.00 40.66           C  
ANISOU 1717  CD  LYS A1019     5845   4303   5302     80   -204    129       C  
ATOM   1718  CE  LYS A1019      82.678 -17.945  51.248  1.00 46.12           C  
ANISOU 1718  CE  LYS A1019     6622   4958   5942     79   -228    131       C  
ATOM   1719  NZ  LYS A1019      83.896 -18.600  51.797  1.00 46.58           N  
ANISOU 1719  NZ  LYS A1019     6724   4980   5995     88   -277    132       N  
ATOM   1720  N   ALA A1020      82.883 -12.003  47.443  1.00 22.79           N  
ANISOU 1720  N   ALA A1020     3333   2162   3162     73    -90    122       N  
ATOM   1721  CA  ALA A1020      83.208 -11.277  46.226  1.00 28.58           C  
ANISOU 1721  CA  ALA A1020     4017   2913   3928     74    -59    123       C  
ATOM   1722  C   ALA A1020      84.714 -11.072  46.087  1.00 29.31           C  
ANISOU 1722  C   ALA A1020     4106   2996   4035     79    -74    124       C  
ATOM   1723  O   ALA A1020      85.474 -11.124  47.059  1.00 40.94           O  
ANISOU 1723  O   ALA A1020     5602   4452   5500     79   -114    122       O  
ATOM   1724  CB  ALA A1020      82.493  -9.929  46.201  1.00 30.33           C  
ANISOU 1724  CB  ALA A1020     4211   3156   4156     72    -35    121       C  
ATOM   1725  N   ASP A1021      85.137 -10.825  44.847  1.00 20.34           N  
ANISOU 1725  N   ASP A1021     2945   1869   2916     82    -46    125       N  
ATOM   1726  CA  ASP A1021      86.538 -10.622  44.499  1.00 27.85           C  
ANISOU 1726  CA  ASP A1021     3891   2811   3879     85    -60    125       C  
ATOM   1727  C   ASP A1021      86.827  -9.205  44.027  1.00 36.68           C  
ANISOU 1727  C   ASP A1021     4990   3947   4998     82    -48    121       C  
ATOM   1728  O   ASP A1021      87.779  -8.577  44.499  1.00 36.10           O  
ANISOU 1728  O   ASP A1021     4908   3867   4941     80    -80    119       O  
ATOM   1729  CB  ASP A1021      86.966 -11.625  43.417  1.00 39.74           C  
ANISOU 1729  CB  ASP A1021     5399   4306   5394     92    -45    129       C  
ATOM   1730  CG  ASP A1021      87.974 -12.635  43.927  1.00 55.72           C  
ANISOU 1730  CG  ASP A1021     7441   6298   7433     97    -83    132       C  
ATOM   1731  OD1 ASP A1021      88.758 -12.285  44.834  1.00 63.29           O  
ANISOU 1731  OD1 ASP A1021     8401   7246   8400     96   -124    131       O  
ATOM   1732  OD2 ASP A1021      87.983 -13.778  43.422  1.00 62.18           O  
ANISOU 1732  OD2 ASP A1021     8273   7097   8256    104    -76    137       O  
ATOM   1733  N   ASN A1022      86.021  -8.684  43.107  1.00 42.67           N  
ANISOU 1733  N   ASN A1022     5746   4725   5740     83    -10    118       N  
ATOM   1734  CA  ASN A1022      86.218  -7.362  42.535  1.00 41.28           C  
ANISOU 1734  CA  ASN A1022     5564   4564   5558     80     -9    114       C  
ATOM   1735  C   ASN A1022      85.002  -6.486  42.810  1.00 32.04           C  
ANISOU 1735  C   ASN A1022     4394   3417   4364     77     11    109       C  
ATOM   1736  O   ASN A1022      83.974  -6.942  43.314  1.00 29.63           O  
ANISOU 1736  O   ASN A1022     4082   3120   4058     76     29    111       O  
ATOM   1737  CB  ASN A1022      86.485  -7.451  41.027  1.00 48.33           C  
ANISOU 1737  CB  ASN A1022     6452   5466   6444     80     -8    111       C  
ATOM   1738  CG  ASN A1022      85.469  -8.315  40.305  1.00 41.82           C  
ANISOU 1738  CG  ASN A1022     5642   4661   5587     81      7    108       C  
ATOM   1739  OD1 ASN A1022      85.047  -9.353  40.815  1.00 36.34           O  
ANISOU 1739  OD1 ASN A1022     4953   3962   4894     84     25    112       O  
ATOM   1740  ND2 ASN A1022      85.077  -7.895  39.107  1.00 47.51           N  
ANISOU 1740  ND2 ASN A1022     6358   5398   6297     77     -3    103       N  
ATOM   1741  N   ALA A1023      85.134  -5.205  42.454  1.00 29.39           N  
ANISOU 1741  N   ALA A1023     4057   3087   4024     75      6    106       N  
ATOM   1742  CA  ALA A1023      84.098  -4.228  42.772  1.00 24.32           C  
ANISOU 1742  CA  ALA A1023     3422   2460   3360     74     23    102       C  
ATOM   1743  C   ALA A1023      82.858  -4.384  41.901  1.00 22.01           C  
ANISOU 1743  C   ALA A1023     3145   2192   3024     73     22     95       C  
ATOM   1744  O   ALA A1023      81.764  -3.987  42.317  1.00 24.00           O  
ANISOU 1744  O   ALA A1023     3416   2455   3248     73     25     91       O  
ATOM   1745  CB  ALA A1023      84.657  -2.813  42.642  1.00 18.85           C  
ANISOU 1745  CB  ALA A1023     2729   1756   2677     72     11    101       C  
ATOM   1746  N   ALA A1024      83.002  -4.938  40.695  1.00 18.36           N  
ANISOU 1746  N   ALA A1024     2675   1735   2565     70     -2     94       N  
ATOM   1747  CA  ALA A1024      81.866  -5.031  39.780  1.00 23.11           C  
ANISOU 1747  CA  ALA A1024     3264   2353   3163     65    -26     90       C  
ATOM   1748  C   ALA A1024      80.745  -5.887  40.361  1.00 42.05           C  
ANISOU 1748  C   ALA A1024     5670   4759   5548     60    -53     87       C  
ATOM   1749  O   ALA A1024      79.584  -5.462  40.412  1.00 48.26           O  
ANISOU 1749  O   ALA A1024     6422   5552   6362     55    -66     88       O  
ATOM   1750  CB  ALA A1024      82.328  -5.585  38.432  1.00 21.23           C  
ANISOU 1750  CB  ALA A1024     3008   2114   2946     65    -21     93       C  
ATOM   1751  N   GLN A1025      81.070  -7.104  40.806  1.00 46.79           N  
ANISOU 1751  N   GLN A1025     6308   5353   6117     66    -29     87       N  
ATOM   1752  CA  GLN A1025      80.029  -7.963  41.360  1.00 42.85           C  
ANISOU 1752  CA  GLN A1025     5628   4853   5801     51    -36    110       C  
ATOM   1753  C   GLN A1025      79.548  -7.462  42.716  1.00 35.52           C  
ANISOU 1753  C   GLN A1025     4718   3914   4863     55     -8    112       C  
ATOM   1754  O   GLN A1025      78.389  -7.693  43.079  1.00 53.06           O  
ANISOU 1754  O   GLN A1025     6964   6133   7066     53    -23    110       O  
ATOM   1755  CB  GLN A1025      80.518  -9.408  41.464  1.00 58.54           C  
ANISOU 1755  CB  GLN A1025     7643   6821   7780     62     29    118       C  
ATOM   1756  CG  GLN A1025      81.709  -9.627  42.372  1.00 65.59           C  
ANISOU 1756  CG  GLN A1025     8585   7688   8648     70     43    119       C  
ATOM   1757  CD  GLN A1025      81.991 -11.101  42.588  1.00 72.60           C  
ANISOU 1757  CD  GLN A1025     9499   8547   9540     72     21    123       C  
ATOM   1758  OE1 GLN A1025      83.141 -11.513  42.728  1.00 75.42           O  
ANISOU 1758  OE1 GLN A1025     9879   8882   9895     78     14    126       O  
ATOM   1759  NE2 GLN A1025      80.934 -11.905  42.611  1.00 72.44           N  
ANISOU 1759  NE2 GLN A1025     9486   8519   9519     68      6    125       N  
ATOM   1760  N   VAL A1026      80.411  -6.777  43.471  1.00 24.64           N  
ANISOU 1760  N   VAL A1026     3356   2528   3480     62     29    114       N  
ATOM   1761  CA  VAL A1026      79.959  -6.107  44.689  1.00 20.82           C  
ANISOU 1761  CA  VAL A1026     2891   2030   2989     61     11    112       C  
ATOM   1762  C   VAL A1026      78.850  -5.117  44.361  1.00 20.00           C  
ANISOU 1762  C   VAL A1026     2776   1940   2884     55    -21    107       C  
ATOM   1763  O   VAL A1026      77.791  -5.104  45.001  1.00 10.26           O  
ANISOU 1763  O   VAL A1026     1571    698   1629     57    -20    106       O  
ATOM   1764  CB  VAL A1026      81.138  -5.411  45.394  1.00 17.61           C  
ANISOU 1764  CB  VAL A1026     2512   1607   2573     66     24    113       C  
ATOM   1765  CG1 VAL A1026      80.624  -4.472  46.476  1.00 15.01           C  
ANISOU 1765  CG1 VAL A1026     2197   1264   2241     66      8    111       C  
ATOM   1766  CG2 VAL A1026      82.083  -6.435  45.988  1.00 18.71           C  
ANISOU 1766  CG2 VAL A1026     2689   1720   2702     70      6    115       C  
ATOM   1767  N   LYS A1027      79.079  -4.276  43.349  1.00 23.44           N  
ANISOU 1767  N   LYS A1027     3205   2389   3312     52    -56    100       N  
ATOM   1768  CA  LYS A1027      78.067  -3.311  42.935  1.00 22.33           C  
ANISOU 1768  CA  LYS A1027     3097   2252   3136     55    -56     95       C  
ATOM   1769  C   LYS A1027      76.814  -4.003  42.419  1.00 26.37           C  
ANISOU 1769  C   LYS A1027     3618   2770   3633     56    -39     95       C  
ATOM   1770  O   LYS A1027      75.698  -3.540  42.667  1.00 25.94           O  
ANISOU 1770  O   LYS A1027     3572   2709   3574     60    -19     96       O  
ATOM   1771  CB  LYS A1027      78.629  -2.375  41.866  1.00  7.10           C  
ANISOU 1771  CB  LYS A1027     1188    325   1182     57    -60     90       C  
ATOM   1772  CG  LYS A1027      77.598  -1.391  41.345  1.00 36.01           C  
ANISOU 1772  CG  LYS A1027     4852   3985   4846     61    -36     91       C  
ATOM   1773  CD  LYS A1027      78.166  -0.473  40.287  1.00 43.34           C  
ANISOU 1773  CD  LYS A1027     5786   4911   5772     64    -30     91       C  
ATOM   1774  CE  LYS A1027      77.104   0.500  39.808  1.00 49.35           C  
ANISOU 1774  CE  LYS A1027     6546   5664   6540     69    -12     93       C  
ATOM   1775  NZ  LYS A1027      77.624   1.468  38.805  1.00 51.07           N  
ANISOU 1775  NZ  LYS A1027     6769   5873   6764     71     -8     95       N  
ATOM   1776  N   ASP A1028      76.976  -5.114  41.698  1.00 21.82           N  
ANISOU 1776  N   ASP A1028     3039   2200   3051     53    -45     95       N  
ATOM   1777  CA  ASP A1028      75.813  -5.818  41.160  1.00 23.89           C  
ANISOU 1777  CA  ASP A1028     3305   2466   3308     54    -31     96       C  
ATOM   1778  C   ASP A1028      74.939  -6.376  42.281  1.00 22.10           C  
ANISOU 1778  C   ASP A1028     3084   2226   3088     54    -20    101       C  
ATOM   1779  O   ASP A1028      73.711  -6.190  42.291  1.00 18.16           O  
ANISOU 1779  O   ASP A1028     2593   1725   2581     56     -2    101       O  
ATOM   1780  CB  ASP A1028      76.276  -6.935  40.222  1.00 30.45           C  
ANISOU 1780  CB  ASP A1028     4132   3300   4136     51    -41     96       C  
ATOM   1781  CG  ASP A1028      75.123  -7.649  39.546  1.00 43.52           C  
ANISOU 1781  CG  ASP A1028     5790   4957   5790     50    -32     98       C  
ATOM   1782  OD1 ASP A1028      74.276  -6.967  38.932  1.00 53.60           O  
ANISOU 1782  OD1 ASP A1028     7067   6238   7059     53    -17     97       O  
ATOM   1783  OD2 ASP A1028      75.068  -8.894  39.625  1.00 49.68           O  
ANISOU 1783  OD2 ASP A1028     6567   5728   6581     47    -37    101       O  
ATOM   1784  N   ALA A1029      75.564  -7.061  43.242  1.00 28.07           N  
ANISOU 1784  N   ALA A1029     3838   2969   3856     53    -22    105       N  
ATOM   1785  CA  ALA A1029      74.820  -7.601  44.373  1.00 30.41           C  
ANISOU 1785  CA  ALA A1029     4160   3246   4148     54     -6    109       C  
ATOM   1786  C   ALA A1029      74.202  -6.488  45.210  1.00 29.60           C  
ANISOU 1786  C   ALA A1029     4073   3145   4030     58     10    106       C  
ATOM   1787  O   ALA A1029      73.065  -6.616  45.678  1.00 29.23           O  
ANISOU 1787  O   ALA A1029     4043   3096   3966     59     32    107       O  
ATOM   1788  CB  ALA A1029      75.729  -8.481  45.227  1.00  7.60           C  
ANISOU 1788  CB  ALA A1029     1285    339   1262     55     -4    113       C  
ATOM   1789  N   LEU A1030      74.927  -5.380  45.400  1.00 12.48           N  
ANISOU 1789  N   LEU A1030     1898    976   1869     60      3    105       N  
ATOM   1790  CA  LEU A1030      74.369  -4.255  46.143  1.00  7.50           C  
ANISOU 1790  CA  LEU A1030     1285    341   1223     65     21    102       C  
ATOM   1791  C   LEU A1030      73.211  -3.601  45.400  1.00 13.38           C  
ANISOU 1791  C   LEU A1030     2025   1098   1961     68     40    100       C  
ATOM   1792  O   LEU A1030      72.275  -3.110  46.034  1.00 12.15           O  
ANISOU 1792  O   LEU A1030     1884    938   1793     73     67    101       O  
ATOM   1793  CB  LEU A1030      75.457  -3.224  46.438  1.00 10.83           C  
ANISOU 1793  CB  LEU A1030     1702    753   1658     66      8    102       C  
ATOM   1794  CG  LEU A1030      76.365  -3.496  47.638  1.00 17.97           C  
ANISOU 1794  CG  LEU A1030     2626   1641   2561     67      5    104       C  
ATOM   1795  CD1 LEU A1030      77.487  -2.474  47.702  1.00 17.36           C  
ANISOU 1795  CD1 LEU A1030     2538   1553   2505     68     -4    104       C  
ATOM   1796  CD2 LEU A1030      75.557  -3.489  48.925  1.00  8.02           C  
ANISOU 1796  CD2 LEU A1030     1413    372   1263     71     24    102       C  
ATOM   1797  N   THR A1031      73.246  -3.595  44.067  1.00  7.20           N  
ANISOU 1797  N   THR A1031     1223    329   1186     66     30     99       N  
ATOM   1798  CA  THR A1031      72.135  -3.051  43.294  1.00 21.70           C  
ANISOU 1798  CA  THR A1031     3052   2174   3019     70     52     99       C  
ATOM   1799  C   THR A1031      70.891  -3.914  43.455  1.00 39.86           C  
ANISOU 1799  C   THR A1031     5353   4475   5317     69     72    101       C  
ATOM   1800  O   THR A1031      69.782  -3.401  43.672  1.00 60.21           O  
ANISOU 1800  O   THR A1031     7932   7050   7896     74     99    103       O  
ATOM   1801  CB  THR A1031      72.528  -2.945  41.819  1.00  6.98           C  
ANISOU 1801  CB  THR A1031     1172    321   1158     68     39     97       C  
ATOM   1802  OG1 THR A1031      73.758  -2.220  41.699  1.00 20.47           O  
ANISOU 1802  OG1 THR A1031     2882   2024   2870     68     21     96       O  
ATOM   1803  CG2 THR A1031      71.447  -2.232  41.026  1.00  9.56           C  
ANISOU 1803  CG2 THR A1031     1491    652   1489     72     59     98       C  
ATOM   1804  N   LYS A1032      71.059  -5.234  43.345  1.00 25.20           N  
ANISOU 1804  N   LYS A1032     3497   2616   3460     64     58    103       N  
ATOM   1805  CA  LYS A1032      69.933  -6.135  43.578  1.00  7.28           C  
ANISOU 1805  CA  LYS A1032     1234    342   1191     62     74    106       C  
ATOM   1806  C   LYS A1032      69.398  -5.983  44.999  1.00  8.21           C  
ANISOU 1806  C   LYS A1032     1373    447   1299     66    101    108       C  
ATOM   1807  O   LYS A1032      68.178  -5.965  45.218  1.00  7.64           O  
ANISOU 1807  O   LYS A1032     1301    371   1231     68    131    110       O  
ATOM   1808  CB  LYS A1032      70.358  -7.577  43.302  1.00  7.31           C  
ANISOU 1808  CB  LYS A1032     1242    338   1197     55     51    108       C  
ATOM   1809  CG  LYS A1032      70.812  -7.813  41.869  1.00  7.13           C  
ANISOU 1809  CG  LYS A1032     1204    324   1180     53     28    106       C  
ATOM   1810  CD  LYS A1032      71.229  -9.255  41.632  1.00  7.23           C  
ANISOU 1810  CD  LYS A1032     1222    324   1201     47      8    109       C  
ATOM   1811  CE  LYS A1032      71.612  -9.479  40.178  1.00  7.09           C  
ANISOU 1811  CE  LYS A1032     1194    316   1186     45     -9    107       C  
ATOM   1812  NZ  LYS A1032      71.887 -10.913  39.885  1.00 75.31           N  
ANISOU 1812  NZ  LYS A1032     9834   8944   9837     41    -19    111       N  
ATOM   1813  N   MET A1033      70.302  -5.848  45.975  1.00 11.65           N  
ANISOU 1813  N   MET A1033     1828    874   1724     67     94    107       N  
ATOM   1814  CA  MET A1033      69.900  -5.627  47.360  1.00 13.09           C  
ANISOU 1814  CA  MET A1033     2042   1043   1889     71    121    108       C  
ATOM   1815  C   MET A1033      69.121  -4.330  47.518  1.00 11.70           C  
ANISOU 1815  C   MET A1033     1864    868   1713     79    151    107       C  
ATOM   1816  O   MET A1033      68.131  -4.281  48.255  1.00 22.38           O  
ANISOU 1816  O   MET A1033     3233   2212   3059     84    188    109       O  
ATOM   1817  CB  MET A1033      71.134  -5.609  48.259  1.00 16.26           C  
ANISOU 1817  CB  MET A1033     2467   1434   2278     71    102    106       C  
ATOM   1818  CG  MET A1033      71.538  -6.957  48.805  1.00 15.30           C  
ANISOU 1818  CG  MET A1033     2369   1299   2146     66     91    109       C  
ATOM   1819  SD  MET A1033      73.053  -6.838  49.770  1.00  8.30           S  
ANISOU 1819  SD  MET A1033     1509    400   1246     67     67    107       S  
ATOM   1820  CE  MET A1033      72.569  -5.640  51.006  1.00 17.83           C  
ANISOU 1820  CE  MET A1033     2754   1598   2424     75     94    104       C  
ATOM   1821  N   ARG A1034      69.571  -3.262  46.858  1.00 12.40           N  
ANISOU 1821  N   ARG A1034     1936    965   1811     82    138    105       N  
ATOM   1822  CA  ARG A1034      68.884  -1.981  46.959  1.00 13.33           C  
ANISOU 1822  CA  ARG A1034     2057   1078   1931     91    164    105       C  
ATOM   1823  C   ARG A1034      67.482  -2.066  46.376  1.00  7.95           C  
ANISOU 1823  C   ARG A1034     1355    400   1266     93    192    109       C  
ATOM   1824  O   ARG A1034      66.529  -1.534  46.957  1.00  8.19           O  
ANISOU 1824  O   ARG A1034     1394    419   1298    102    229    112       O  
ATOM   1825  CB  ARG A1034      69.691  -0.898  46.246  1.00  7.85           C  
ANISOU 1825  CB  ARG A1034     1353    384   1244     92    141    103       C  
ATOM   1826  CG  ARG A1034      69.145   0.501  46.444  1.00 25.71           C  
ANISOU 1826  CG  ARG A1034     3629   2633   3509    103    162    104       C  
ATOM   1827  CD  ARG A1034      69.832   1.500  45.533  1.00 25.48           C  
ANISOU 1827  CD  ARG A1034     3590   2601   3489    103    138    102       C  
ATOM   1828  NE  ARG A1034      69.510   2.874  45.904  1.00 24.73           N  
ANISOU 1828  NE  ARG A1034     3520   2483   3394    115    153    103       N  
ATOM   1829  CZ  ARG A1034      68.451   3.541  45.458  1.00 20.55           C  
ANISOU 1829  CZ  ARG A1034     2989   1945   2876    124    173    106       C  
ATOM   1830  NH1 ARG A1034      67.604   2.960  44.619  1.00 16.41           N  
ANISOU 1830  NH1 ARG A1034     2436   1434   2364    122    180    109       N  
ATOM   1831  NH2 ARG A1034      68.237   4.788  45.853  1.00 31.15           N  
ANISOU 1831  NH2 ARG A1034     4359   3259   4216    136    183    107       N  
ATOM   1832  N   ALA A1035      67.337  -2.740  45.232  1.00  8.87           N  
ANISOU 1832  N   ALA A1035     1445    529   1396     87    176    110       N  
ATOM   1833  CA  ALA A1035      66.008  -2.930  44.655  1.00  7.80           C  
ANISOU 1833  CA  ALA A1035     1287    394   1282     89    197    114       C  
ATOM   1834  C   ALA A1035      65.106  -3.709  45.606  1.00  8.01           C  
ANISOU 1834  C   ALA A1035     1325    410   1310     89    229    118       C  
ATOM   1835  O   ALA A1035      63.957  -3.318  45.859  1.00  8.23           O  
ANISOU 1835  O   ALA A1035     1343    429   1354     95    265    123       O  
ATOM   1836  CB  ALA A1035      66.118  -3.641  43.306  1.00  7.58           C  
ANISOU 1836  CB  ALA A1035     1237    378   1263     81    169    114       C  
ATOM   1837  N   ALA A1036      65.621  -4.813  46.156  1.00 32.53           N  
ANISOU 1837  N   ALA A1036     4449   3511   4399     82    216    117       N  
ATOM   1838  CA  ALA A1036      64.834  -5.624  47.082  1.00 18.11           C  
ANISOU 1838  CA  ALA A1036     2642   1668   2571     81    246    121       C  
ATOM   1839  C   ALA A1036      64.416  -4.820  48.308  1.00  8.57           C  
ANISOU 1839  C   ALA A1036     1457    448   1350     91    290    122       C  
ATOM   1840  O   ALA A1036      63.256  -4.871  48.733  1.00  8.82           O  
ANISOU 1840  O   ALA A1036     1487    469   1395     95    333    127       O  
ATOM   1841  CB  ALA A1036      65.626  -6.864  47.494  1.00  8.33           C  
ANISOU 1841  CB  ALA A1036     1431    422   1314     73    220    120       C  
ATOM   1842  N   ALA A1037      65.355  -4.073  48.897  1.00 17.36           N  
ANISOU 1842  N   ALA A1037     2596   1561   2440     95    280    118       N  
ATOM   1843  CA  ALA A1037      65.059  -3.310  50.105  1.00  8.87           C  
ANISOU 1843  CA  ALA A1037     1554    470   1346    105    318    118       C  
ATOM   1844  C   ALA A1037      64.075  -2.183  49.825  1.00 11.64           C  
ANISOU 1844  C   ALA A1037     1886    819   1719    115    351    123       C  
ATOM   1845  O   ALA A1037      63.215  -1.884  50.662  1.00  9.33           O  
ANISOU 1845  O   ALA A1037     1611    510   1424    124    400    127       O  
ATOM   1846  CB  ALA A1037      66.348  -2.759  50.711  1.00  8.87           C  
ANISOU 1846  CB  ALA A1037     1587    466   1317    106    291    113       C  
ATOM   1847  N   LEU A1038      64.187  -1.537  48.659  1.00  8.80           N  
ANISOU 1847  N   LEU A1038     1494    469   1380    116    327    122       N  
ATOM   1848  CA  LEU A1038      63.229  -0.496  48.309  1.00 41.10           C  
ANISOU 1848  CA  LEU A1038     5569   4551   5495    126    352    127       C  
ATOM   1849  C   LEU A1038      61.834  -1.083  48.146  1.00 42.02           C  
ANISOU 1849  C   LEU A1038     5655   4664   5644    126    387    135       C  
ATOM   1850  O   LEU A1038      60.843  -0.478  48.572  1.00 49.94           O  
ANISOU 1850  O   LEU A1038     6658   5651   6664    137    430    142       O  
ATOM   1851  CB  LEU A1038      63.671   0.215  47.030  1.00 14.33           C  
ANISOU 1851  CB  LEU A1038     2157   1170   2119    126    314    125       C  
ATOM   1852  CG  LEU A1038      62.898   1.472  46.625  1.00  9.06           C  
ANISOU 1852  CG  LEU A1038     1484    485   1472    139    328    130       C  
ATOM   1853  CD1 LEU A1038      63.137   2.586  47.630  1.00  9.40           C  
ANISOU 1853  CD1 LEU A1038     1572    505   1495    152    344    129       C  
ATOM   1854  CD2 LEU A1038      63.293   1.919  45.225  1.00 42.98           C  
ANISOU 1854  CD2 LEU A1038     5763   4789   5780    136    287    128       C  
ATOM   1855  N   ASP A1039      61.737  -2.264  47.529  1.00 27.38           N  
ANISOU 1855  N   ASP A1039     3778   2823   3804    115    369    135       N  
ATOM   1856  CA  ASP A1039      60.440  -2.920  47.394  1.00  9.10           C  
ANISOU 1856  CA  ASP A1039     1434    500   1523    113    399    142       C  
ATOM   1857  C   ASP A1039      59.872  -3.327  48.750  1.00  9.44           C  
ANISOU 1857  C   ASP A1039     1504    525   1558    117    451    146       C  
ATOM   1858  O   ASP A1039      58.661  -3.213  48.982  1.00 16.68           O  
ANISOU 1858  O   ASP A1039     2402   1429   2508    123    497    154       O  
ATOM   1859  CB  ASP A1039      60.555  -4.140  46.485  1.00 22.19           C  
ANISOU 1859  CB  ASP A1039     3073   2168   3192    100    362    141       C  
ATOM   1860  CG  ASP A1039      59.209  -4.604  45.966  1.00 49.13           C  
ANISOU 1860  CG  ASP A1039     6446   5571   6650     98    380    149       C  
ATOM   1861  OD1 ASP A1039      58.219  -3.858  46.130  1.00 66.27           O  
ANISOU 1861  OD1 ASP A1039     8595   7732   8851    107    417    156       O  
ATOM   1862  OD2 ASP A1039      59.137  -5.717  45.403  1.00 54.21           O  
ANISOU 1862  OD2 ASP A1039     7082   6215   7301     88    354    149       O  
ATOM   1863  N   ALA A1040      60.731  -3.793  49.661  1.00  9.45           N  
ANISOU 1863  N   ALA A1040     1550    523   1516    114    445    140       N  
ATOM   1864  CA  ALA A1040      60.251  -4.356  50.920  1.00  9.81           C  
ANISOU 1864  CA  ALA A1040     1631    548   1547    115    491    142       C  
ATOM   1865  C   ALA A1040      59.665  -3.300  51.846  1.00 10.16           C  
ANISOU 1865  C   ALA A1040     1696    578   1587    130    548    146       C  
ATOM   1866  O   ALA A1040      58.807  -3.621  52.676  1.00 14.74           O  
ANISOU 1866  O   ALA A1040     2290   1139   2172    133    603    150       O  
ATOM   1867  CB  ALA A1040      61.385  -5.101  51.625  1.00 13.17           C  
ANISOU 1867  CB  ALA A1040     2108    971   1926    107    463    135       C  
ATOM   1868  N   GLY A1041      60.098  -2.045  51.721  1.00 22.08           N  
ANISOU 1868  N   GLY A1041     3211   2090   3087    139    537    144       N  
ATOM   1869  CA  GLY A1041      59.586  -1.009  52.598  1.00 25.04           C  
ANISOU 1869  CA  GLY A1041     3615   2446   3455    155    586    149       C  
ATOM   1870  C   GLY A1041      58.144  -0.637  52.336  1.00 28.54           C  
ANISOU 1870  C   GLY A1041     4019   2876   3949    164    634    160       C  
ATOM   1871  O   GLY A1041      57.515  -0.014  53.198  1.00 11.25           O  
ANISOU 1871  O   GLY A1041     1855    664   1756    178    689    166       O  
ATOM   1872  N   SER A1042      57.605  -1.016  51.174  1.00 28.38           N  
ANISOU 1872  N   SER A1042     3940   2867   3976    157    614    164       N  
ATOM   1873  CA  SER A1042      56.253  -0.631  50.763  1.00 30.39           C  
ANISOU 1873  CA  SER A1042     4150   3109   4288    165    649    176       C  
ATOM   1874  C   SER A1042      56.040   0.871  50.925  1.00 11.24           C  
ANISOU 1874  C   SER A1042     1744    663   1864    185    663    181       C  
ATOM   1875  O   SER A1042      54.974   1.332  51.338  1.00 16.52           O  
ANISOU 1875  O   SER A1042     2407   1308   2563    198    716    192       O  
ATOM   1876  CB  SER A1042      55.192  -1.422  51.529  1.00 28.82           C  
ANISOU 1876  CB  SER A1042     3942   2893   4114    164    713    183       C  
ATOM   1877  OG  SER A1042      54.860  -2.620  50.849  1.00 28.18           O  
ANISOU 1877  OG  SER A1042     3820   2821   4064    149    694    183       O  
ATOM   1878  N   GLY A1043      57.079   1.639  50.606  1.00 12.60           N  
ANISOU 1878  N   GLY A1043     1943    840   2004    188    616    173       N  
ATOM   1879  CA  GLY A1043      57.011   3.081  50.658  1.00 17.68           C  
ANISOU 1879  CA  GLY A1043     2615   1459   2645    208    615    176       C  
ATOM   1880  C   GLY A1043      57.118   3.690  52.036  1.00 11.83           C  
ANISOU 1880  C   GLY A1043     1937    693   1865    224    657    176       C  
ATOM   1881  O   GLY A1043      56.918   4.902  52.169  1.00 18.24           O  
ANISOU 1881  O   GLY A1043     2778   1476   2676    246    661    178       O  
ATOM   1882  N   SER A1044      57.425   2.895  53.065  1.00 11.79           N  
ANISOU 1882  N   SER A1044     1960    695   1825    215    685    172       N  
ATOM   1883  CA  SER A1044      57.529   3.434  54.418  1.00 12.23           C  
ANISOU 1883  CA  SER A1044     2085    726   1838    230    725    172       C  
ATOM   1884  C   SER A1044      58.518   4.592  54.465  1.00 39.78           C  
ANISOU 1884  C   SER A1044     5621   4203   5292    241    682    164       C  
ATOM   1885  O   SER A1044      58.195   5.694  54.920  1.00 40.86           O  
ANISOU 1885  O   SER A1044     5797   4305   5421    264    703    168       O  
ATOM   1886  CB  SER A1044      57.945   2.332  55.398  1.00 12.14           C  
ANISOU 1886  CB  SER A1044     2104    723   1785    217    745    166       C  
ATOM   1887  OG  SER A1044      59.337   2.070  55.315  1.00 11.74           O  
ANISOU 1887  OG  SER A1044     2075    691   1695    205    684    154       O  
ATOM   1888  N   GLY A1045      59.738   4.343  54.006  1.00 25.64           N  
ANISOU 1888  N   GLY A1045     3828   2435   3481    225    622    153       N  
ATOM   1889  CA  GLY A1045      60.764   5.361  53.920  1.00 35.43           C  
ANISOU 1889  CA  GLY A1045     5103   3665   4695    231    576    145       C  
ATOM   1890  C   GLY A1045      61.671   5.260  55.123  1.00 48.82           C  
ANISOU 1890  C   GLY A1045     6861   5354   6334    229    574    137       C  
ATOM   1891  O   GLY A1045      61.355   5.796  56.190  1.00 55.41           O  
ANISOU 1891  O   GLY A1045     7752   6160   7140    246    614    139       O  
ATOM   1892  N   ASP A1066      62.799   4.573  54.974  1.00 61.21           N  
ANISOU 1892  N   ASP A1066     8424   6948   7886    210    527    129       N  
ATOM   1893  CA  ASP A1066      63.701   4.362  56.091  1.00 66.65           C  
ANISOU 1893  CA  ASP A1066     9172   7630   8523    207    518    121       C  
ATOM   1894  C   ASP A1066      65.138   4.627  55.662  1.00 60.86           C  
ANISOU 1894  C   ASP A1066     8437   6905   7783    197    449    113       C  
ATOM   1895  O   ASP A1066      65.423   4.999  54.519  1.00 42.74           O  
ANISOU 1895  O   ASP A1066     6100   4621   5520    193    414    112       O  
ATOM   1896  CB  ASP A1066      63.536   2.952  56.669  1.00 70.27           C  
ANISOU 1896  CB  ASP A1066     9633   8102   8966    195    540    122       C  
ATOM   1897  CG  ASP A1066      63.500   1.887  55.601  1.00 84.31           C  
ANISOU 1897  CG  ASP A1066    11344   9910  10781    178    516    123       C  
ATOM   1898  OD1 ASP A1066      63.610   2.232  54.405  1.00 96.82           O  
ANISOU 1898  OD1 ASP A1066    12880  11508  12400    175    484    123       O  
ATOM   1899  OD2 ASP A1066      63.360   0.702  55.960  1.00 78.57           O  
ANISOU 1899  OD2 ASP A1066    10619   9189  10044    169    528    123       O  
ATOM   1900  N   ILE A1067      66.043   4.416  56.620  1.00 56.54           N  
ANISOU 1900  N   ILE A1067     7940   6351   7192    192    430    106       N  
ATOM   1901  CA  ILE A1067      67.476   4.563  56.428  1.00 51.57           C  
ANISOU 1901  CA  ILE A1067     7313   5726   6556    182    367     99       C  
ATOM   1902  C   ILE A1067      68.097   3.415  55.641  1.00 46.12           C  
ANISOU 1902  C   ILE A1067     6568   5067   5888    163    330     98       C  
ATOM   1903  O   ILE A1067      69.217   3.561  55.145  1.00 49.65           O  
ANISOU 1903  O   ILE A1067     6998   5520   6347    155    279     94       O  
ATOM   1904  CB  ILE A1067      68.162   4.713  57.795  1.00 49.42           C  
ANISOU 1904  CB  ILE A1067     7117   5431   6229    185    360     93       C  
ATOM   1905  CG1 ILE A1067      68.068   3.405  58.581  1.00 60.16           C  
ANISOU 1905  CG1 ILE A1067     8499   6799   7560    177    375     93       C  
ATOM   1906  CG2 ILE A1067      67.521   5.842  58.584  1.00 28.78           C  
ANISOU 1906  CG2 ILE A1067     4565   2782   3590    206    399     94       C  
ATOM   1907  CD1 ILE A1067      68.546   3.516  60.010  1.00 71.17           C  
ANISOU 1907  CD1 ILE A1067     9981   8168   8894    181    374     88       C  
ATOM   1908  N   LEU A1068      67.422   2.265  55.546  1.00 36.76           N  
ANISOU 1908  N   LEU A1068     5359   3898   4710    157    354    102       N  
ATOM   1909  CA  LEU A1068      68.048   1.062  54.995  1.00 26.84           C  
ANISOU 1909  CA  LEU A1068     4067   2664   3466    141    318    100       C  
ATOM   1910  C   LEU A1068      68.527   1.260  53.559  1.00 32.92           C  
ANISOU 1910  C   LEU A1068     4777   3453   4277    134    279    100       C  
ATOM   1911  O   LEU A1068      69.658   0.888  53.216  1.00 43.27           O  
ANISOU 1911  O   LEU A1068     6073   4774   5594    125    233     97       O  
ATOM   1912  CB  LEU A1068      67.065  -0.107  55.069  1.00 15.10           C  
ANISOU 1912  CB  LEU A1068     2570   1185   1984    138    354    105       C  
ATOM   1913  CG  LEU A1068      67.545  -1.429  54.474  1.00  9.76           C  
ANISOU 1913  CG  LEU A1068     1862    526   1320    123    320    105       C  
ATOM   1914  CD1 LEU A1068      68.786  -1.901  55.201  1.00 11.92           C  
ANISOU 1914  CD1 LEU A1068     2174    791   1562    118    281    100       C  
ATOM   1915  CD2 LEU A1068      66.448  -2.483  54.524  1.00 11.66           C  
ANISOU 1915  CD2 LEU A1068     2095    767   1569    121    358    109       C  
ATOM   1916  N   VAL A1069      67.679   1.825  52.696  1.00  9.68           N  
ANISOU 1916  N   VAL A1069     1801    514   1363    140    297    104       N  
ATOM   1917  CA  VAL A1069      68.111   2.082  51.324  1.00  9.36           C  
ANISOU 1917  CA  VAL A1069     1713    489   1355    134    262    104       C  
ATOM   1918  C   VAL A1069      69.261   3.082  51.308  1.00 27.76           C  
ANISOU 1918  C   VAL A1069     4059   2807   3682    135    227     99       C  
ATOM   1919  O   VAL A1069      70.166   2.987  50.471  1.00  9.18           O  
ANISOU 1919  O   VAL A1069     1675    465   1347    126    188     97       O  
ATOM   1920  CB  VAL A1069      66.926   2.557  50.462  1.00  9.39           C  
ANISOU 1920  CB  VAL A1069     1687    494   1386    141    287    109       C  
ATOM   1921  CG1 VAL A1069      67.376   2.798  49.027  1.00  9.10           C  
ANISOU 1921  CG1 VAL A1069     1611    471   1376    135    251    108       C  
ATOM   1922  CG2 VAL A1069      65.799   1.537  50.504  1.00  9.35           C  
ANISOU 1922  CG2 VAL A1069     1663    498   1391    139    322    114       C  
ATOM   1923  N   GLY A1070      69.262   4.038  52.240  1.00 23.93           N  
ANISOU 1923  N   GLY A1070     3623   2295   3174    146    240     97       N  
ATOM   1924  CA  GLY A1070      70.379   4.967  52.340  1.00 11.57           C  
ANISOU 1924  CA  GLY A1070     2079    712   1607    147    206     93       C  
ATOM   1925  C   GLY A1070      71.686   4.284  52.699  1.00 12.61           C  
ANISOU 1925  C   GLY A1070     2210    850   1731    134    168     90       C  
ATOM   1926  O   GLY A1070      72.741   4.614  52.154  1.00 31.26           O  
ANISOU 1926  O   GLY A1070     4552   3210   4113    128    132     88       O  
ATOM   1927  N   GLN A1071      71.639   3.340  53.641  1.00  9.90           N  
ANISOU 1927  N   GLN A1071     1892    509   1359    132    176     89       N  
ATOM   1928  CA  GLN A1071      72.841   2.596  54.007  1.00  9.80           C  
ANISOU 1928  CA  GLN A1071     1884    500   1341    121    138     87       C  
ATOM   1929  C   GLN A1071      73.325   1.735  52.846  1.00 55.10           C  
ANISOU 1929  C   GLN A1071     7559   6262   7115    110    113     89       C  
ATOM   1930  O   GLN A1071      74.536   1.612  52.608  1.00 37.61           O  
ANISOU 1930  O   GLN A1071     5326   4047   4917    103     77     89       O  
ATOM   1931  CB  GLN A1071      72.565   1.724  55.231  1.00 10.00           C  
ANISOU 1931  CB  GLN A1071     1957    518   1323    122    153     86       C  
ATOM   1932  CG  GLN A1071      72.056   2.470  56.450  1.00 15.07           C  
ANISOU 1932  CG  GLN A1071     2670   1134   1921    134    183     84       C  
ATOM   1933  CD  GLN A1071      71.886   1.556  57.646  1.00 28.54           C  
ANISOU 1933  CD  GLN A1071     4430   2832   3580    134    196     83       C  
ATOM   1934  OE1 GLN A1071      72.434   0.454  57.679  1.00 47.85           O  
ANISOU 1934  OE1 GLN A1071     6869   5286   6024    124    171     83       O  
ATOM   1935  NE2 GLN A1071      71.124   2.007  58.634  1.00 40.98           N  
ANISOU 1935  NE2 GLN A1071     6066   4387   5117    145    238     82       N  
ATOM   1936  N   ILE A1072      72.387   1.133  52.111  1.00 61.05           N  
ANISOU 1936  N   ILE A1072     8280   7034   7882    109    134     92       N  
ATOM   1937  CA  ILE A1072      72.767   0.366  50.929  1.00  8.73           C  
ANISOU 1937  CA  ILE A1072     1601    429   1287     99    111     94       C  
ATOM   1938  C   ILE A1072      73.399   1.283  49.889  1.00  8.61           C  
ANISOU 1938  C   ILE A1072     1555    416   1302     98     89     94       C  
ATOM   1939  O   ILE A1072      74.340   0.896  49.192  1.00  8.40           O  
ANISOU 1939  O   ILE A1072     1496    397   1300     90     61     95       O  
ATOM   1940  CB  ILE A1072      71.556  -0.400  50.367  1.00  8.56           C  
ANISOU 1940  CB  ILE A1072     1559    424   1270     99    137     97       C  
ATOM   1941  CG1 ILE A1072      71.046  -1.411  51.395  1.00  8.73           C  
ANISOU 1941  CG1 ILE A1072     1612    439   1264     99    159     98       C  
ATOM   1942  CG2 ILE A1072      71.931  -1.122  49.083  1.00  8.21           C  
ANISOU 1942  CG2 ILE A1072     1469    399   1253     90    112     98       C  
ATOM   1943  CD1 ILE A1072      69.870  -2.223  50.915  1.00  8.63           C  
ANISOU 1943  CD1 ILE A1072     1580    437   1262     97    185    102       C  
ATOM   1944  N   ASP A1073      72.911   2.522  49.786  1.00  8.81           N  
ANISOU 1944  N   ASP A1073     1593    428   1327    106    104     93       N  
ATOM   1945  CA  ASP A1073      73.520   3.481  48.868  1.00 14.05           C  
ANISOU 1945  CA  ASP A1073     2238   1086   2016    106     85     93       C  
ATOM   1946  C   ASP A1073      74.904   3.914  49.333  1.00 15.94           C  
ANISOU 1946  C   ASP A1073     2486   1307   2262    102     58     92       C  
ATOM   1947  O   ASP A1073      75.773   4.189  48.503  1.00  8.87           O  
ANISOU 1947  O   ASP A1073     1562    411   1397     97     36     93       O  
ATOM   1948  CB  ASP A1073      72.613   4.698  48.689  1.00 19.17           C  
ANISOU 1948  CB  ASP A1073     2905   1719   2661    118    108     94       C  
ATOM   1949  CG  ASP A1073      71.577   4.496  47.602  1.00 22.99           C  
ANISOU 1949  CG  ASP A1073     3360   2219   3156    119    123     97       C  
ATOM   1950  OD1 ASP A1073      71.832   3.688  46.685  1.00 20.70           O  
ANISOU 1950  OD1 ASP A1073     3035   1952   2879    110    108     97       O  
ATOM   1951  OD2 ASP A1073      70.515   5.151  47.654  1.00 26.20           O  
ANISOU 1951  OD2 ASP A1073     3781   2612   3559    130    151     99       O  
ATOM   1952  N   ASP A1074      75.122   4.011  50.644  1.00 10.55           N  
ANISOU 1952  N   ASP A1074     1848    608   1553    106     59     89       N  
ATOM   1953  CA  ASP A1074      76.468   4.279  51.150  1.00 14.48           C  
ANISOU 1953  CA  ASP A1074     2357   1088   2056    101     32     88       C  
ATOM   1954  C   ASP A1074      77.424   3.160  50.750  1.00 16.54           C  
ANISOU 1954  C   ASP A1074     2578   1364   2341     91     11     91       C  
ATOM   1955  O   ASP A1074      78.526   3.409  50.235  1.00 33.06           O  
ANISOU 1955  O   ASP A1074     4643   3451   4465     87     -5     93       O  
ATOM   1956  CB  ASP A1074      76.434   4.445  52.670  1.00 24.65           C  
ANISOU 1956  CB  ASP A1074     3711   2356   3300    107     34     84       C  
ATOM   1957  CG  ASP A1074      75.632   5.654  53.108  1.00 35.45           C  
ANISOU 1957  CG  ASP A1074     5125   3699   4644    119     56     81       C  
ATOM   1958  OD1 ASP A1074      75.653   6.676  52.391  1.00 41.14           O  
ANISOU 1958  OD1 ASP A1074     5836   4409   5388    123     56     82       O  
ATOM   1959  OD2 ASP A1074      74.984   5.582  54.173  1.00 37.17           O  
ANISOU 1959  OD2 ASP A1074     5394   3908   4821    127     76     79       O  
ATOM   1960  N   ALA A1075      77.012   1.911  50.986  1.00  9.19           N  
ANISOU 1960  N   ALA A1075     1645    450   1395     89     16     92       N  
ATOM   1961  CA  ALA A1075      77.815   0.771  50.553  1.00 16.81           C  
ANISOU 1961  CA  ALA A1075     2577   1428   2381     82      1     95       C  
ATOM   1962  C   ALA A1075      78.020   0.788  49.043  1.00  8.43           C  
ANISOU 1962  C   ALA A1075     1458    381   1363     77     -1     98       C  
ATOM   1963  O   ALA A1075      79.095   0.433  48.546  1.00 10.21           O  
ANISOU 1963  O   ALA A1075     1654    608   1618     73     -8    102       O  
ATOM   1964  CB  ALA A1075      77.155  -0.535  50.992  1.00 23.03           C  
ANISOU 1964  CB  ALA A1075     3381   2227   3144     81      9     95       C  
ATOM   1965  N   LEU A1076      76.997   1.212  48.299  1.00  8.31           N  
ANISOU 1965  N   LEU A1076     1433    376   1347     80      8     97       N  
ATOM   1966  CA  LEU A1076      77.077   1.252  46.845  1.00  8.06           C  
ANISOU 1966  CA  LEU A1076     1364    358   1341     76     -2     99       C  
ATOM   1967  C   LEU A1076      78.039   2.332  46.369  1.00 21.78           C  
ANISOU 1967  C   LEU A1076     3088   2085   3104     75    -12     99       C  
ATOM   1968  O   LEU A1076      78.708   2.154  45.347  1.00 53.49           O  
ANISOU 1968  O   LEU A1076     7072   6120   7134     69    -26     99       O  
ATOM   1969  CB  LEU A1076      75.679   1.472  46.264  1.00  7.97           C  
ANISOU 1969  CB  LEU A1076     1361    360   1309     80     15     97       C  
ATOM   1970  CG  LEU A1076      75.416   1.052  44.819  1.00 25.45           C  
ANISOU 1970  CG  LEU A1076     3552   2594   3525     77     10     96       C  
ATOM   1971  CD1 LEU A1076      76.106  -0.263  44.518  1.00 14.58           C  
ANISOU 1971  CD1 LEU A1076     2155   1229   2154     69    -10     97       C  
ATOM   1972  CD2 LEU A1076      73.918   0.930  44.580  1.00 33.64           C  
ANISOU 1972  CD2 LEU A1076     4595   3642   4544     82     39     96       C  
ATOM   1973  N   LYS A1077      78.111   3.456  47.084  1.00 22.70           N  
ANISOU 1973  N   LYS A1077     3234   2172   3219     80     -5     99       N  
ATOM   1974  CA  LYS A1077      79.117   4.467  46.779  1.00 18.87           C  
ANISOU 1974  CA  LYS A1077     2742   1670   2759     79     -9    100       C  
ATOM   1975  C   LYS A1077      80.511   3.917  47.033  1.00 20.87           C  
ANISOU 1975  C   LYS A1077     2978   1926   3027     75     -3    103       C  
ATOM   1976  O   LYS A1077      81.420   4.093  46.213  1.00  8.73           O  
ANISOU 1976  O   LYS A1077     1412    395   1509     72     10    106       O  
ATOM   1977  CB  LYS A1077      78.889   5.730  47.613  1.00 16.94           C  
ANISOU 1977  CB  LYS A1077     2547   1391   2499     87     -4     98       C  
ATOM   1978  CG  LYS A1077      78.568   6.972  46.794  1.00 19.31           C  
ANISOU 1978  CG  LYS A1077     2854   1674   2808     92     -1     98       C  
ATOM   1979  CD  LYS A1077      78.373   8.202  47.680  1.00 21.15           C  
ANISOU 1979  CD  LYS A1077     3144   1872   3019    100      5     95       C  
ATOM   1980  CE  LYS A1077      77.592   7.889  48.946  1.00 34.94           C  
ANISOU 1980  CE  LYS A1077     4932   3621   4723    107     16     90       C  
ATOM   1981  NZ  LYS A1077      76.155   7.612  48.679  1.00 48.02           N  
ANISOU 1981  NZ  LYS A1077     6588   5296   6360    114     39     90       N  
ATOM   1982  N   LEU A1078      80.697   3.250  48.177  1.00 32.28           N  
ANISOU 1982  N   LEU A1078     4452   3358   4453     76     -6    103       N  
ATOM   1983  CA  LEU A1078      81.977   2.598  48.448  1.00 13.97           C  
ANISOU 1983  CA  LEU A1078     2139   1036   2134     74     -7    104       C  
ATOM   1984  C   LEU A1078      82.354   1.634  47.330  1.00 14.51           C  
ANISOU 1984  C   LEU A1078     2170   1137   2205     72     13    106       C  
ATOM   1985  O   LEU A1078      83.522   1.554  46.932  1.00 22.78           O  
ANISOU 1985  O   LEU A1078     3229   2180   3245     72     17    107       O  
ATOM   1986  CB  LEU A1078      81.925   1.859  49.786  1.00  9.00           C  
ANISOU 1986  CB  LEU A1078     1549    405   1465     74    -33    100       C  
ATOM   1987  CG  LEU A1078      82.001   2.709  51.052  1.00  9.41           C  
ANISOU 1987  CG  LEU A1078     1657    433   1487     76    -57     94       C  
ATOM   1988  CD1 LEU A1078      81.749   1.855  52.286  1.00 14.20           C  
ANISOU 1988  CD1 LEU A1078     2307   1039   2049     76    -78     91       C  
ATOM   1989  CD2 LEU A1078      83.357   3.387  51.140  1.00 19.65           C  
ANISOU 1989  CD2 LEU A1078     2962   1707   2796     72    -81     94       C  
ATOM   1990  N   ALA A1079      81.372   0.892  46.812  1.00 21.55           N  
ANISOU 1990  N   ALA A1079     3031   2057   3100     70     15    106       N  
ATOM   1991  CA  ALA A1079      81.635  -0.031  45.710  1.00 20.45           C  
ANISOU 1991  CA  ALA A1079     2866   1946   2959     69     39    108       C  
ATOM   1992  C   ALA A1079      81.989   0.713  44.427  1.00 21.09           C  
ANISOU 1992  C   ALA A1079     2954   2038   3021     73     82    107       C  
ATOM   1993  O   ALA A1079      82.899   0.302  43.698  1.00 13.13           O  
ANISOU 1993  O   ALA A1079     2027   1030   1930     76     63     98       O  
ATOM   1994  CB  ALA A1079      80.426  -0.938  45.483  1.00 22.51           C  
ANISOU 1994  CB  ALA A1079     3100   2226   3228     63      7    107       C  
ATOM   1995  N   ASN A1080      81.278   1.807  44.136  1.00 27.17           N  
ANISOU 1995  N   ASN A1080     3659   2804   3860     61     -6    106       N  
ATOM   1996  CA  ASN A1080      81.533   2.575  42.919  1.00 16.18           C  
ANISOU 1996  CA  ASN A1080     2389   1410   2349     59   -111     87       C  
ATOM   1997  C   ASN A1080      82.923   3.193  42.921  1.00 20.51           C  
ANISOU 1997  C   ASN A1080     3026   1937   2829     77     32     91       C  
ATOM   1998  O   ASN A1080      83.552   3.311  41.864  1.00 42.96           O  
ANISOU 1998  O   ASN A1080     5855   4776   5692     72     -7     91       O  
ATOM   1999  CB  ASN A1080      80.477   3.669  42.757  1.00 12.04           C  
ANISOU 1999  CB  ASN A1080     1821    872   1883     62    -81     94       C  
ATOM   2000  CG  ASN A1080      79.180   3.146  42.185  1.00 17.37           C  
ANISOU 2000  CG  ASN A1080     2506   1561   2531     67    -57     93       C  
ATOM   2001  OD1 ASN A1080      79.186   2.309  41.286  1.00 20.66           O  
ANISOU 2001  OD1 ASN A1080     2929   1997   2924     66    -52     92       O  
ATOM   2002  ND2 ASN A1080      78.058   3.639  42.701  1.00 13.76           N  
ANISOU 2002  ND2 ASN A1080     2056   1092   2081     73    -35     96       N  
ATOM   2003  N   GLU A1081      83.414   3.601  44.091  1.00  9.63           N  
ANISOU 2003  N   GLU A1081     1575    535   1547     77     85    104       N  
ATOM   2004  CA  GLU A1081      84.765   4.132  44.201  1.00 17.80           C  
ANISOU 2004  CA  GLU A1081     2639   1539   2587     74     55    104       C  
ATOM   2005  C   GLU A1081      85.832   3.058  44.037  1.00 31.79           C  
ANISOU 2005  C   GLU A1081     4405   3311   4364     70     19    104       C  
ATOM   2006  O   GLU A1081      87.009   3.399  43.877  1.00 39.17           O  
ANISOU 2006  O   GLU A1081     5337   4219   5327     66     -4    107       O  
ATOM   2007  CB  GLU A1081      84.927   4.848  45.543  1.00 17.25           C  
ANISOU 2007  CB  GLU A1081     2560   1434   2561     73     40    107       C  
ATOM   2008  CG  GLU A1081      83.994   6.044  45.705  1.00 24.71           C  
ANISOU 2008  CG  GLU A1081     3486   2364   3540     74     45    109       C  
ATOM   2009  CD  GLU A1081      83.975   6.595  47.118  1.00 33.06           C  
ANISOU 2009  CD  GLU A1081     4578   3383   4602     74     11    107       C  
ATOM   2010  OE1 GLU A1081      82.929   7.140  47.532  1.00 30.79           O  
ANISOU 2010  OE1 GLU A1081     4301   3082   4314     77     -1    105       O  
ATOM   2011  OE2 GLU A1081      85.000   6.471  47.819  1.00 39.20           O  
ANISOU 2011  OE2 GLU A1081     5384   4138   5372     71    -12    106       O  
ATOM   2012  N   GLY A1082      85.454   1.781  44.069  1.00 34.87           N  
ANISOU 2012  N   GLY A1082     4783   3723   4743     71     18    103       N  
ATOM   2013  CA  GLY A1082      86.394   0.692  43.915  1.00 30.40           C  
ANISOU 2013  CA  GLY A1082     4200   3153   4196     69     -8    106       C  
ATOM   2014  C   GLY A1082      86.835   0.033  45.204  1.00 26.11           C  
ANISOU 2014  C   GLY A1082     3647   2602   3670     66    -36    107       C  
ATOM   2015  O   GLY A1082      87.582  -0.951  45.150  1.00 33.17           O  
ANISOU 2015  O   GLY A1082     4523   3501   4579     64    -63    107       O  
ATOM   2016  N   LYS A1083      86.395   0.538  46.354  1.00 21.61           N  
ANISOU 2016  N   LYS A1083     3093   2020   3100     67    -39    106       N  
ATOM   2017  CA  LYS A1083      86.804   0.015  47.655  1.00 22.45           C  
ANISOU 2017  CA  LYS A1083     3205   2115   3208     63    -85    105       C  
ATOM   2018  C   LYS A1083      85.999  -1.244  47.951  1.00 25.96           C  
ANISOU 2018  C   LYS A1083     3653   2574   3636     66    -77    105       C  
ATOM   2019  O   LYS A1083      84.828  -1.173  48.330  1.00 39.55           O  
ANISOU 2019  O   LYS A1083     5382   4300   5347     68    -55    105       O  
ATOM   2020  CB  LYS A1083      86.600   1.067  48.738  1.00 24.68           C  
ANISOU 2020  CB  LYS A1083     3514   2377   3487     63   -101    102       C  
ATOM   2021  CG  LYS A1083      87.173   2.432  48.395  1.00 16.33           C  
ANISOU 2021  CG  LYS A1083     2459   1300   2447     61    -99    103       C  
ATOM   2022  CD  LYS A1083      86.809   3.455  49.455  1.00 29.97           C  
ANISOU 2022  CD  LYS A1083     4219   3003   4166     61   -113    100       C  
ATOM   2023  CE  LYS A1083      87.404   4.815  49.137  1.00 40.35           C  
ANISOU 2023  CE  LYS A1083     5540   4289   5500     58   -113    101       C  
ATOM   2024  NZ  LYS A1083      86.925   5.863  50.080  1.00 46.17           N  
ANISOU 2024  NZ  LYS A1083     6317   5000   6228     60   -123     97       N  
ATOM   2025  N   VAL A1084      86.628  -2.408  47.783  1.00 30.09           N  
ANISOU 2025  N   VAL A1084     4169   3101   4163     65    -98    106       N  
ATOM   2026  CA  VAL A1084      85.902  -3.670  47.892  1.00 36.77           C  
ANISOU 2026  CA  VAL A1084     5020   3955   4995     67    -88    108       C  
ATOM   2027  C   VAL A1084      85.794  -4.113  49.348  1.00 29.88           C  
ANISOU 2027  C   VAL A1084     4182   3070   4103     66   -128    106       C  
ATOM   2028  O   VAL A1084      84.722  -4.524  49.809  1.00 32.04           O  
ANISOU 2028  O   VAL A1084     4472   3346   4355     67   -116    105       O  
ATOM   2029  CB  VAL A1084      86.576  -4.746  47.019  1.00  8.68           C  
ANISOU 2029  CB  VAL A1084     1448    402   1448     68    -91    110       C  
ATOM   2030  CG1 VAL A1084      85.836  -6.070  47.137  1.00  8.64           C  
ANISOU 2030  CG1 VAL A1084     1454    399   1430     71    -83    112       C  
ATOM   2031  CG2 VAL A1084      86.635  -4.291  45.566  1.00  8.43           C  
ANISOU 2031  CG2 VAL A1084     1399    385   1420     70    -58    110       C  
ATOM   2032  N   LYS A1085      86.903  -4.043  50.091  1.00 13.37           N  
ANISOU 2032  N   LYS A1085     2105    961   2015     63   -181    104       N  
ATOM   2033  CA  LYS A1085      86.904  -4.485  51.484  1.00 23.79           C  
ANISOU 2033  CA  LYS A1085     3470   2263   3305     63   -225    101       C  
ATOM   2034  C   LYS A1085      85.931  -3.664  52.326  1.00 32.31           C  
ANISOU 2034  C   LYS A1085     4582   3340   4354     63   -214     97       C  
ATOM   2035  O   LYS A1085      85.148  -4.212  53.118  1.00 41.99           O  
ANISOU 2035  O   LYS A1085     5848   4563   5545     65   -215     96       O  
ATOM   2036  CB  LYS A1085      88.320  -4.388  52.055  1.00 31.92           C  
ANISOU 2036  CB  LYS A1085     4505   3273   4351     59   -289     99       C  
ATOM   2037  CG  LYS A1085      89.373  -5.200  51.305  1.00 35.92           C  
ANISOU 2037  CG  LYS A1085     4978   3777   4893     59   -306    103       C  
ATOM   2038  CD  LYS A1085      89.398  -6.658  51.741  1.00 44.80           C  
ANISOU 2038  CD  LYS A1085     6131   4890   6001     63   -330    104       C  
ATOM   2039  CE  LYS A1085      90.570  -7.399  51.108  1.00 52.08           C  
ANISOU 2039  CE  LYS A1085     7024   5802   6963     65   -353    107       C  
ATOM   2040  NZ  LYS A1085      90.684  -8.798  51.605  1.00 50.89           N  
ANISOU 2040  NZ  LYS A1085     6911   5631   6796     70   -382    109       N  
ATOM   2041  N   GLU A1086      85.975  -2.338  52.173  1.00 26.14           N  
ANISOU 2041  N   GLU A1086     3790   2556   3586     62   -202     96       N  
ATOM   2042  CA  GLU A1086      85.082  -1.470  52.933  1.00 39.24           C  
ANISOU 2042  CA  GLU A1086     5482   4208   5218     64   -191     92       C  
ATOM   2043  C   GLU A1086      83.625  -1.700  52.550  1.00 38.62           C  
ANISOU 2043  C   GLU A1086     5395   4147   5131     68   -141     94       C  
ATOM   2044  O   GLU A1086      82.737  -1.660  53.410  1.00 43.44           O  
ANISOU 2044  O   GLU A1086     6045   4754   5707     70   -137     91       O  
ATOM   2045  CB  GLU A1086      85.479  -0.008  52.733  1.00 51.73           C  
ANISOU 2045  CB  GLU A1086     7057   5779   6820     63   -190     91       C  
ATOM   2046  CG  GLU A1086      86.914   0.301  53.141  1.00 59.80           C  
ANISOU 2046  CG  GLU A1086     8085   6780   7854     58   -246     90       C  
ATOM   2047  CD  GLU A1086      87.289   1.755  52.924  1.00 67.45           C  
ANISOU 2047  CD  GLU A1086     9051   7732   8844     56   -244     89       C  
ATOM   2048  OE1 GLU A1086      88.290   2.015  52.224  1.00 69.90           O  
ANISOU 2048  OE1 GLU A1086     9329   8039   9191     52   -255     92       O  
ATOM   2049  OE2 GLU A1086      86.576   2.640  53.444  1.00 71.82           O  
ANISOU 2049  OE2 GLU A1086     9638   8273   9377     59   -232     86       O  
ATOM   2050  N   ALA A1087      83.359  -1.939  51.262  1.00 33.47           N  
ANISOU 2050  N   ALA A1087     4693   3514   4510     68   -104     99       N  
ATOM   2051  CA  ALA A1087      81.998  -2.252  50.838  1.00 36.29           C  
ANISOU 2051  CA  ALA A1087     5036   3887   4867     70    -69    101       C  
ATOM   2052  C   ALA A1087      81.514  -3.550  51.471  1.00 32.21           C  
ANISOU 2052  C   ALA A1087     4548   3370   4318     70    -79    100       C  
ATOM   2053  O   ALA A1087      80.348  -3.659  51.873  1.00 38.73           O  
ANISOU 2053  O   ALA A1087     5394   4200   5122     71    -63     99       O  
ATOM   2054  CB  ALA A1087      81.927  -2.335  49.315  1.00  8.51           C  
ANISOU 2054  CB  ALA A1087     1462    385   1385     70    -36    105       C  
ATOM   2055  N   GLN A1088      82.400  -4.542  51.581  1.00 25.41           N  
ANISOU 2055  N   GLN A1088     3697   2503   3454     68   -105    101       N  
ATOM   2056  CA  GLN A1088      82.020  -5.800  52.214  1.00 14.12           C  
ANISOU 2056  CA  GLN A1088     2306   1068   1993     68   -118    101       C  
ATOM   2057  C   GLN A1088      81.711  -5.603  53.696  1.00 22.53           C  
ANISOU 2057  C   GLN A1088     3436   2115   3009     69   -137     97       C  
ATOM   2058  O   GLN A1088      80.752  -6.184  54.218  1.00 29.33           O  
ANISOU 2058  O   GLN A1088     4332   2974   3838     70   -122     96       O  
ATOM   2059  CB  GLN A1088      83.127  -6.839  52.020  1.00 19.32           C  
ANISOU 2059  CB  GLN A1088     2965   1717   2659     68   -149    103       C  
ATOM   2060  CG  GLN A1088      83.302  -7.303  50.576  1.00 23.61           C  
ANISOU 2060  CG  GLN A1088     3457   2274   3239     68   -123    108       C  
ATOM   2061  CD  GLN A1088      84.571  -8.112  50.365  1.00 14.95           C  
ANISOU 2061  CD  GLN A1088     2361   1164   2154     69   -155    110       C  
ATOM   2062  OE1 GLN A1088      85.617  -7.811  50.940  1.00 18.30           O  
ANISOU 2062  OE1 GLN A1088     2797   1575   2581     69   -195    108       O  
ATOM   2063  NE2 GLN A1088      84.482  -9.146  49.534  1.00 19.36           N  
ANISOU 2063  NE2 GLN A1088     2908   1725   2723     71   -140    113       N  
ATOM   2064  N   ALA A1089      82.507  -4.783  54.389  1.00 18.82           N  
ANISOU 2064  N   ALA A1089     2988   1631   2531     69   -168     93       N  
ATOM   2065  CA  ALA A1089      82.207  -4.480  55.790  1.00 17.83           C  
ANISOU 2065  CA  ALA A1089     2932   1488   2355     71   -185     88       C  
ATOM   2066  C   ALA A1089      80.867  -3.756  55.938  1.00 25.60           C  
ANISOU 2066  C   ALA A1089     3926   2479   3323     75   -139     87       C  
ATOM   2067  O   ALA A1089      80.075  -4.055  56.853  1.00 40.08           O  
ANISOU 2067  O   ALA A1089     5814   4303   5109     77   -127     85       O  
ATOM   2068  CB  ALA A1089      83.336  -3.649  56.398  1.00 16.76           C  
ANISOU 2068  CB  ALA A1089     2815   1335   2219     70   -232     84       C  
ATOM   2069  N   ALA A1090      80.606  -2.784  55.059  1.00 23.53           N  
ANISOU 2069  N   ALA A1090     3614   2229   3097     75   -112     88       N  
ATOM   2070  CA  ALA A1090      79.317  -2.100  55.077  1.00 25.98           C  
ANISOU 2070  CA  ALA A1090     3929   2544   3397     80    -71     87       C  
ATOM   2071  C   ALA A1090      78.173  -3.084  54.880  1.00 21.80           C  
ANISOU 2071  C   ALA A1090     3397   2027   2858     80    -40     90       C  
ATOM   2072  O   ALA A1090      77.144  -2.997  55.561  1.00 24.31           O  
ANISOU 2072  O   ALA A1090     3755   2341   3142     84    -13     88       O  
ATOM   2073  CB  ALA A1090      79.286  -1.012  54.005  1.00 25.06           C  
ANISOU 2073  CB  ALA A1090     3759   2437   3326     80    -55     88       C  
ATOM   2074  N   ALA A1091      78.343  -4.043  53.965  1.00 19.20           N  
ANISOU 2074  N   ALA A1091     3027   1712   2557     76    -42     94       N  
ATOM   2075  CA  ALA A1091      77.319  -5.065  53.767  1.00 19.08           C  
ANISOU 2075  CA  ALA A1091     3013   1704   2533     75    -18     96       C  
ATOM   2076  C   ALA A1091      77.167  -5.945  55.000  1.00 23.01           C  
ANISOU 2076  C   ALA A1091     3581   2182   2979     75    -24     95       C  
ATOM   2077  O   ALA A1091      76.061  -6.413  55.302  1.00 40.98           O  
ANISOU 2077  O   ALA A1091     5881   4456   5233     76      6     96       O  
ATOM   2078  CB  ALA A1091      77.651  -5.915  52.541  1.00  8.98           C  
ANISOU 2078  CB  ALA A1091     1682    438   1291     71    -23    101       C  
ATOM   2079  N   GLU A1092      78.263  -6.182  55.723  1.00 10.28           N  
ANISOU 2079  N   GLU A1092     2006    553   1346     75    -65     93       N  
ATOM   2080  CA  GLU A1092      78.181  -6.961  56.955  1.00 15.96           C  
ANISOU 2080  CA  GLU A1092     2803   1249   2010     75    -77     92       C  
ATOM   2081  C   GLU A1092      77.270  -6.283  57.974  1.00 18.54           C  
ANISOU 2081  C   GLU A1092     3184   1566   2294     79    -47     88       C  
ATOM   2082  O   GLU A1092      76.403  -6.930  58.573  1.00 13.97           O  
ANISOU 2082  O   GLU A1092     2651    977   1680     79    -20     89       O  
ATOM   2083  CB  GLU A1092      79.581  -7.171  57.533  1.00 31.69           C  
ANISOU 2083  CB  GLU A1092     4827   3224   3991     73   -136     90       C  
ATOM   2084  CG  GLU A1092      79.622  -8.036  58.783  1.00 56.31           C  
ANISOU 2084  CG  GLU A1092     8033   6314   7049     73   -159     88       C  
ATOM   2085  CD  GLU A1092      79.275  -9.486  58.510  1.00 78.12           C  
ANISOU 2085  CD  GLU A1092    10807   9070   9806     70   -152     93       C  
ATOM   2086  OE1 GLU A1092      79.429  -9.933  57.354  1.00 90.33           O  
ANISOU 2086  OE1 GLU A1092    12294  10631  11397     69   -147     97       O  
ATOM   2087  OE2 GLU A1092      78.843 -10.179  59.456  1.00 87.12           O  
ANISOU 2087  OE2 GLU A1092    12021  10186  10894     69   -150     93       O  
ATOM   2088  N   GLN A1093      77.459  -4.979  58.191  1.00 24.45           N  
ANISOU 2088  N   GLN A1093     3931   2314   3044     83    -48     84       N  
ATOM   2089  CA  GLN A1093      76.538  -4.248  59.073  1.00 34.16           C  
ANISOU 2089  CA  GLN A1093     5211   3533   4234     89    -13     81       C  
ATOM   2090  C   GLN A1093      75.111  -4.241  58.513  1.00 36.69           C  
ANISOU 2090  C   GLN A1093     5501   3869   4570     92     47     84       C  
ATOM   2091  O   GLN A1093      74.117  -4.386  59.257  1.00 45.11           O  
ANISOU 2091  O   GLN A1093     6614   4924   5600     96     88     84       O  
ATOM   2092  CB  GLN A1093      77.044  -2.823  59.293  1.00 57.05           C  
ANISOU 2092  CB  GLN A1093     8115   6426   7135     93    -28     77       C  
ATOM   2093  CG  GLN A1093      78.429  -2.744  59.919  1.00 74.00           C  
ANISOU 2093  CG  GLN A1093    10295   8555   9266     90    -90     73       C  
ATOM   2094  CD  GLN A1093      78.477  -3.360  61.307  1.00 86.68           C  
ANISOU 2094  CD  GLN A1093    11994  10136  10805     91   -108     70       C  
ATOM   2095  OE1 GLN A1093      77.486  -3.352  62.039  1.00 92.75           O  
ANISOU 2095  OE1 GLN A1093    12816  10894  11529     96    -67     69       O  
ATOM   2096  NE2 GLN A1093      79.634  -3.897  61.677  1.00 89.88           N  
ANISOU 2096  NE2 GLN A1093    12421  10528  11200     86   -170     69       N  
ATOM   2097  N   LEU A1094      74.997  -4.070  57.195  1.00 31.54           N  
ANISOU 2097  N   LEU A1094     4771   3239   3973     90     52     88       N  
ATOM   2098  CA  LEU A1094      73.701  -4.105  56.533  1.00 30.69           C  
ANISOU 2098  CA  LEU A1094     4630   3147   3886     92     98     91       C  
ATOM   2099  C   LEU A1094      72.962  -5.406  56.794  1.00 22.73           C  
ANISOU 2099  C   LEU A1094     3645   2132   2859     89    120     94       C  
ATOM   2100  O   LEU A1094      71.735  -5.424  56.768  1.00 26.85           O  
ANISOU 2100  O   LEU A1094     4164   2655   3381     91    166     96       O  
ATOM   2101  CB  LEU A1094      73.873  -3.883  55.033  1.00 38.00           C  
ANISOU 2101  CB  LEU A1094     5475   4095   4867     89     88     93       C  
ATOM   2102  CG  LEU A1094      73.871  -2.413  54.626  1.00 43.90           C  
ANISOU 2102  CG  LEU A1094     6199   4846   5635     94     93     92       C  
ATOM   2103  CD1 LEU A1094      74.115  -2.271  53.138  1.00 49.33           C  
ANISOU 2103  CD1 LEU A1094     6816   5554   6373     89     79     94       C  
ATOM   2104  CD2 LEU A1094      72.542  -1.793  55.015  1.00 44.52           C  
ANISOU 2104  CD2 LEU A1094     6300   4921   5696    102    141     92       C  
ATOM   2105  N   LYS A1095      73.682  -6.508  56.999  1.00 26.54           N  
ANISOU 2105  N   LYS A1095     4149   2605   3329     83     88     95       N  
ATOM   2106  CA  LYS A1095      73.018  -7.784  57.266  1.00 33.47           C  
ANISOU 2106  CA  LYS A1095     5058   3470   4188     78    106     99       C  
ATOM   2107  C   LYS A1095      72.100  -7.692  58.487  1.00 40.53           C  
ANISOU 2107  C   LYS A1095     6022   4344   5035     82    149     97       C  
ATOM   2108  O   LYS A1095      70.905  -8.025  58.416  1.00 42.95           O  
ANISOU 2108  O   LYS A1095     6326   4648   5346     81    196    100       O  
ATOM   2109  CB  LYS A1095      74.080  -8.867  57.458  1.00 25.88           C  
ANISOU 2109  CB  LYS A1095     4127   2495   3213     72     59    100       C  
ATOM   2110  CG  LYS A1095      73.578 -10.296  57.438  1.00 30.02           C  
ANISOU 2110  CG  LYS A1095     4676   3003   3725     66     67    104       C  
ATOM   2111  CD  LYS A1095      74.756 -11.252  57.561  1.00 32.78           C  
ANISOU 2111  CD  LYS A1095     5055   3336   4062     62     16    105       C  
ATOM   2112  CE  LYS A1095      75.839 -10.911  56.541  1.00 36.77           C  
ANISOU 2112  CE  LYS A1095     5495   3863   4614     64    -19    105       C  
ATOM   2113  NZ  LYS A1095      77.085 -11.700  56.744  1.00 43.28           N  
ANISOU 2113  NZ  LYS A1095     6348   4670   5427     63    -70    106       N  
ATOM   2114  N   THR A1096      72.641  -7.223  59.615  1.00 51.63           N  
ANISOU 2114  N   THR A1096     7491   5732   6394     85    135     92       N  
ATOM   2115  CA  THR A1096      71.832  -7.039  60.818  1.00 63.40           C  
ANISOU 2115  CA  THR A1096     9055   7201   7834     90    180     90       C  
ATOM   2116  C   THR A1096      70.723  -6.022  60.579  1.00 59.42           C  
ANISOU 2116  C   THR A1096     8519   6708   7349     99    237     91       C  
ATOM   2117  O   THR A1096      69.557  -6.248  60.951  1.00 61.09           O  
ANISOU 2117  O   THR A1096     8752   6909   7549    101    295     93       O  
ATOM   2118  CB  THR A1096      72.718  -6.606  61.989  1.00 72.88           C  
ANISOU 2118  CB  THR A1096    10330   8380   8979     93    147     84       C  
ATOM   2119  OG1 THR A1096      73.664  -7.640  62.286  1.00 80.12           O  
ANISOU 2119  OG1 THR A1096    11284   9283   9876     85     93     84       O  
ATOM   2120  CG2 THR A1096      71.873  -6.328  63.226  1.00 74.34           C  
ANISOU 2120  CG2 THR A1096    10597   8542   9108     99    198     81       C  
ATOM   2121  N   THR A1097      71.074  -4.877  59.977  1.00 49.59           N  
ANISOU 2121  N   THR A1097     7227   5480   6134    104    223     89       N  
ATOM   2122  CA  THR A1097      70.053  -3.853  59.743  1.00 41.77           C  
ANISOU 2122  CA  THR A1097     6212   4496   5161    114    274     90       C  
ATOM   2123  C   THR A1097      68.901  -4.403  58.900  1.00 31.84           C  
ANISOU 2123  C   THR A1097     4902   3253   3944    112    313     96       C  
ATOM   2124  O   THR A1097      67.725  -4.105  59.157  1.00 22.78           O  
ANISOU 2124  O   THR A1097     3760   2099   2796    119    373     99       O  
ATOM   2125  CB  THR A1097      70.681  -2.630  59.074  1.00 47.43           C  
ANISOU 2125  CB  THR A1097     6888   5226   5908    118    245     89       C  
ATOM   2126  OG1 THR A1097      71.678  -2.074  59.940  1.00 53.19           O  
ANISOU 2126  OG1 THR A1097     7672   5939   6601    120    210     83       O  
ATOM   2127  CG2 THR A1097      69.630  -1.570  58.793  1.00 46.52           C  
ANISOU 2127  CG2 THR A1097     6752   5113   5810    129    294     91       C  
ATOM   2128  N   ILE A1098      69.224  -5.241  57.914  1.00 35.24           N  
ANISOU 2128  N   ILE A1098     5282   3699   4409    102    281     99       N  
ATOM   2129  CA  ILE A1098      68.229  -5.796  57.006  1.00 26.96           C  
ANISOU 2129  CA  ILE A1098     4182   2661   3400     99    306    104       C  
ATOM   2130  C   ILE A1098      67.331  -6.779  57.735  1.00 37.93           C  
ANISOU 2130  C   ILE A1098     5616   4029   4768     95    347    107       C  
ATOM   2131  O   ILE A1098      66.111  -6.780  57.540  1.00 51.12           O  
ANISOU 2131  O   ILE A1098     7264   5698   6460     97    396    111       O  
ATOM   2132  CB  ILE A1098      68.922  -6.458  55.801  1.00 10.05           C  
ANISOU 2132  CB  ILE A1098     1986    537   1294     89    256    106       C  
ATOM   2133  CG1 ILE A1098      69.362  -5.410  54.782  1.00 13.22           C  
ANISOU 2133  CG1 ILE A1098     2330    961   1730     92    234    104       C  
ATOM   2134  CG2 ILE A1098      68.008  -7.479  55.141  1.00 10.01           C  
ANISOU 2134  CG2 ILE A1098     1955    533   1316     83    273    111       C  
ATOM   2135  CD1 ILE A1098      70.414  -5.918  53.830  1.00  9.75           C  
ANISOU 2135  CD1 ILE A1098     1852    534   1316     85    182    104       C  
ATOM   2136  N   ASN A1099      67.916  -7.660  58.551  1.00 34.87           N  
ANISOU 2136  N   ASN A1099     5290   3620   4340     89    327    106       N  
ATOM   2137  CA  ASN A1099      67.087  -8.570  59.338  1.00 34.31           C  
ANISOU 2137  CA  ASN A1099     5274   3521   4243     83    368    108       C  
ATOM   2138  C   ASN A1099      66.076  -7.790  60.173  1.00 29.21           C  
ANISOU 2138  C   ASN A1099     4658   2863   3578     93    438    107       C  
ATOM   2139  O   ASN A1099      64.873  -8.104  60.180  1.00 17.63           O  
ANISOU 2139  O   ASN A1099     3183   1386   2129     92    492    111       O  
ATOM   2140  CB  ASN A1099      67.965  -9.452  60.225  1.00 48.56           C  
ANISOU 2140  CB  ASN A1099     7155   5300   5995     75    333    106       C  
ATOM   2141  CG  ASN A1099      68.635 -10.571  59.449  1.00 53.93           C  
ANISOU 2141  CG  ASN A1099     7815   5983   6696     65    282    110       C  
ATOM   2142  OD1 ASN A1099      68.203 -10.925  58.352  1.00 55.29           O  
ANISOU 2142  OD1 ASN A1099     7925   6168   6915     61    282    115       O  
ATOM   2143  ND2 ASN A1099      69.693 -11.136  60.019  1.00 60.50           N  
ANISOU 2143  ND2 ASN A1099     8701   6797   7489     60    236    108       N  
ATOM   2144  N   ALA A1100      66.547  -6.741  60.857  1.00 33.44           N  
ANISOU 2144  N   ALA A1100     5227   3397   4080    104    437    102       N  
ATOM   2145  CA  ALA A1100      65.653  -5.940  61.692  1.00 25.88           C  
ANISOU 2145  CA  ALA A1100     4307   2426   3101    116    505    102       C  
ATOM   2146  C   ALA A1100      64.521  -5.328  60.869  1.00 29.64           C  
ANISOU 2146  C   ALA A1100     4710   2918   3634    123    552    107       C  
ATOM   2147  O   ALA A1100      63.338  -5.447  61.222  1.00 26.68           O  
ANISOU 2147  O   ALA A1100     4343   2529   3267    127    620    111       O  
ATOM   2148  CB  ALA A1100      66.447  -4.852  62.415  1.00 28.75           C  
ANISOU 2148  CB  ALA A1100     4718   2784   3423    125    486     96       C  
ATOM   2149  N   TYR A1101      64.868  -4.660  59.764  1.00 36.62           N  
ANISOU 2149  N   TYR A1101     5525   3828   4560    126    516    108       N  
ATOM   2150  CA  TYR A1101      63.850  -3.964  58.980  1.00 36.41           C  
ANISOU 2150  CA  TYR A1101     5435   3814   4584    134    554    114       C  
ATOM   2151  C   TYR A1101      62.869  -4.938  58.332  1.00 34.36           C  
ANISOU 2151  C   TYR A1101     5130   3557   4367    126    577    120       C  
ATOM   2152  O   TYR A1101      61.675  -4.634  58.208  1.00 29.98           O  
ANISOU 2152  O   TYR A1101     4548   3000   3846    133    633    125       O  
ATOM   2153  CB  TYR A1101      64.510  -3.063  57.938  1.00 29.78           C  
ANISOU 2153  CB  TYR A1101     4543   2999   3774    136    506    113       C  
ATOM   2154  CG  TYR A1101      64.784  -1.677  58.473  1.00 25.64           C  
ANISOU 2154  CG  TYR A1101     4052   2464   3226    150    512    111       C  
ATOM   2155  CD1 TYR A1101      63.746  -0.777  58.672  1.00 28.13           C  
ANISOU 2155  CD1 TYR A1101     4368   2767   3551    164    570    116       C  
ATOM   2156  CD2 TYR A1101      66.072  -1.274  58.797  1.00 25.28           C  
ANISOU 2156  CD2 TYR A1101     4040   2416   3150    148    460    104       C  
ATOM   2157  CE1 TYR A1101      63.982   0.489  59.168  1.00 32.95           C  
ANISOU 2157  CE1 TYR A1101     5018   3363   4139    178    574    114       C  
ATOM   2158  CE2 TYR A1101      66.319  -0.006  59.294  1.00 26.77           C  
ANISOU 2158  CE2 TYR A1101     4265   2590   3317    160    462    102       C  
ATOM   2159  CZ  TYR A1101      65.269   0.870  59.477  1.00 29.01           C  
ANISOU 2159  CZ  TYR A1101     4555   2860   3607    175    519    107       C  
ATOM   2160  OH  TYR A1101      65.501   2.133  59.972  1.00 28.12           O  
ANISOU 2160  OH  TYR A1101     4486   2727   3471    189    520    105       O  
ATOM   2161  N   ILE A1102      63.352  -6.102  57.893  1.00 17.97           N  
ANISOU 2161  N   ILE A1102     3046   1485   2296    112    533    119       N  
ATOM   2162  CA  ILE A1102      62.463  -7.107  57.318  1.00 11.35           C  
ANISOU 2162  CA  ILE A1102     2174    641   1496    102    548    124       C  
ATOM   2163  C   ILE A1102      61.449  -7.567  58.355  1.00 21.89           C  
ANISOU 2163  C   ILE A1102     3557   1944   2816    101    617    127       C  
ATOM   2164  O   ILE A1102      60.252  -7.707  58.059  1.00 31.46           O  
ANISOU 2164  O   ILE A1102     4733   3150   4071    101    662    132       O  
ATOM   2165  CB  ILE A1102      63.279  -8.288  56.759  1.00 15.51           C  
ANISOU 2165  CB  ILE A1102     2700   1170   2023     87    485    124       C  
ATOM   2166  CG1 ILE A1102      63.975  -7.889  55.455  1.00 22.98           C  
ANISOU 2166  CG1 ILE A1102     3582   2148   3000     87    430    123       C  
ATOM   2167  CG2 ILE A1102      62.391  -9.502  56.546  1.00 11.44           C  
ANISOU 2167  CG2 ILE A1102     2181    634   1530     74    501    130       C  
ATOM   2168  CD1 ILE A1102      63.034  -7.355  54.397  1.00 25.50           C  
ANISOU 2168  CD1 ILE A1102     3832   2485   3372     91    448    127       C  
ATOM   2169  N   GLN A1103      61.907  -7.813  59.589  1.00 26.83           N  
ANISOU 2169  N   GLN A1103     4266   2547   3381    100    625    122       N  
ATOM   2170  CA  GLN A1103      60.961  -8.188  60.637  1.00 19.85           C  
ANISOU 2170  CA  GLN A1103     3436   1628   2477     98    696    123       C  
ATOM   2171  C   GLN A1103      59.948  -7.073  60.879  1.00 13.06           C  
ANISOU 2171  C   GLN A1103     2555    769   1638    116    770    125       C  
ATOM   2172  O   GLN A1103      58.759  -7.340  61.098  1.00 20.48           O  
ANISOU 2172  O   GLN A1103     3489   1690   2605    115    836    129       O  
ATOM   2173  CB  GLN A1103      61.697  -8.540  61.928  1.00 17.18           C  
ANISOU 2173  CB  GLN A1103     3201   1264   2063     93    689    117       C  
ATOM   2174  CG  GLN A1103      60.766  -9.050  63.019  1.00 32.99           C  
ANISOU 2174  CG  GLN A1103     5271   3226   4039     87    762    116       C  
ATOM   2175  CD  GLN A1103      61.487  -9.841  64.089  1.00 51.78           C  
ANISOU 2175  CD  GLN A1103     7755   5573   6345     74    741    111       C  
ATOM   2176  OE1 GLN A1103      62.706  -9.755  64.228  1.00 59.66           O  
ANISOU 2176  OE1 GLN A1103     8781   6581   7306     76    678    107       O  
ATOM   2177  NE2 GLN A1103      60.733 -10.627  64.851  1.00 58.63           N  
ANISOU 2177  NE2 GLN A1103     8683   6400   7194     60    792    111       N  
ATOM   2178  N   LYS A1104      60.402  -5.816  60.839  1.00 25.36           N  
ANISOU 2178  N   LYS A1104     4105   2345   3186    131    760    124       N  
ATOM   2179  CA  LYS A1104      59.480  -4.694  61.018  1.00 17.97           C  
ANISOU 2179  CA  LYS A1104     3152   1406   2271    149    827    130       C  
ATOM   2180  C   LYS A1104      58.403  -4.682  59.935  1.00 21.52           C  
ANISOU 2180  C   LYS A1104     3510   1868   2799    150    849    138       C  
ATOM   2181  O   LYS A1104      57.216  -4.467  60.224  1.00 16.27           O  
ANISOU 2181  O   LYS A1104     2832   1187   2163    158    923    145       O  
ATOM   2182  CB  LYS A1104      60.253  -3.374  61.025  1.00 22.00           C  
ANISOU 2182  CB  LYS A1104     3671   1928   2759    162    797    128       C  
ATOM   2183  CG  LYS A1104      59.404  -2.161  61.370  1.00 27.95           C  
ANISOU 2183  CG  LYS A1104     4427   2670   3522    182    862    135       C  
ATOM   2184  CD  LYS A1104      60.129  -0.866  61.041  1.00 30.42           C  
ANISOU 2184  CD  LYS A1104     4738   2992   3828    193    818    134       C  
ATOM   2185  CE  LYS A1104      59.357  -0.043  60.022  1.00 37.37           C  
ANISOU 2185  CE  LYS A1104     5545   3882   4773    203    830    144       C  
ATOM   2186  NZ  LYS A1104      60.143   1.131  59.546  1.00 34.97           N  
ANISOU 2186  NZ  LYS A1104     5240   3583   4465    210    777    141       N  
ATOM   2187  N   TYR A1105      58.799  -4.905  58.679  1.00 26.22           N  
ANISOU 2187  N   TYR A1105     4042   2489   3431    142    785    139       N  
ATOM   2188  CA  TYR A1105      57.828  -4.902  57.586  1.00 21.98           C  
ANISOU 2188  CA  TYR A1105     3422   1963   2966    141    796    147       C  
ATOM   2189  C   TYR A1105      56.833  -6.050  57.734  1.00 20.45           C  
ANISOU 2189  C   TYR A1105     3222   1747   2801    131    835    150       C  
ATOM   2190  O   TYR A1105      55.627  -5.879  57.493  1.00 23.18           O  
ANISOU 2190  O   TYR A1105     3521   2085   3202    136    886    158       O  
ATOM   2191  CB  TYR A1105      58.543  -5.001  56.238  1.00 19.99           C  
ANISOU 2191  CB  TYR A1105     3118   1742   2738    133    716    145       C  
ATOM   2192  CG  TYR A1105      59.583  -3.933  55.972  1.00 16.84           C  
ANISOU 2192  CG  TYR A1105     2722   1361   2316    140    671    141       C  
ATOM   2193  CD1 TYR A1105      59.507  -2.684  56.577  1.00 19.50           C  
ANISOU 2193  CD1 TYR A1105     3086   1689   2635    156    703    143       C  
ATOM   2194  CD2 TYR A1105      60.640  -4.177  55.106  1.00 18.65           C  
ANISOU 2194  CD2 TYR A1105     2932   1612   2543    131    597    136       C  
ATOM   2195  CE1 TYR A1105      60.461  -1.712  56.326  1.00 19.16           C  
ANISOU 2195  CE1 TYR A1105     3051   1656   2574    161    658    138       C  
ATOM   2196  CE2 TYR A1105      61.593  -3.215  54.850  1.00 10.58           C  
ANISOU 2196  CE2 TYR A1105     1913    603   1506    135    558    132       C  
ATOM   2197  CZ  TYR A1105      61.501  -1.985  55.461  1.00 15.03           C  
ANISOU 2197  CZ  TYR A1105     2504   1155   2053    150    586    133       C  
ATOM   2198  OH  TYR A1105      62.455  -1.032  55.200  1.00 32.27           O  
ANISOU 2198  OH  TYR A1105     4694   3345   4223    153    543    128       O  
ATOM   2199  N   GLY A1106      57.323  -7.228  58.126  1.00 12.65           N  
ANISOU 2199  N   GLY A1106     2284    744   1779    114    809    145       N  
ATOM   2200  CA  GLY A1106      56.420  -8.341  58.375  1.00 25.87           C  
ANISOU 2200  CA  GLY A1106     3969   2385   3475    100    844    148       C  
ATOM   2201  C   GLY A1106      55.428  -8.042  59.482  1.00 38.46           C  
ANISOU 2201  C   GLY A1106     5595   3950   5066    108    939    149       C  
ATOM   2202  O   GLY A1106      54.251  -8.408  59.394  1.00 23.65           O  
ANISOU 2202  O   GLY A1106     3689   2054   3242    103    988    154       O  
ATOM   2203  N   GLN A 313      55.886  -7.360  60.534  1.00 13.89           N  
ANISOU 2203  N   GLN A 313     2548    833   1896    120    967    144       N  
ATOM   2204  CA  GLN A 313      54.982  -6.968  61.611  1.00 28.07           C  
ANISOU 2204  CA  GLN A 313     4382   2601   3684    131   1064    145       C  
ATOM   2205  C   GLN A 313      53.929  -5.983  61.117  1.00 32.69           C  
ANISOU 2205  C   GLN A 313     4889   3196   4337    149   1117    155       C  
ATOM   2206  O   GLN A 313      52.768  -6.044  61.537  1.00 41.02           O  
ANISOU 2206  O   GLN A 313     5934   4224   5427    153   1198    159       O  
ATOM   2207  CB  GLN A 313      55.777  -6.372  62.772  1.00 43.16           C  
ANISOU 2207  CB  GLN A 313     6383   4504   5512    141   1074    137       C  
ATOM   2208  CG  GLN A 313      54.930  -5.993  63.978  1.00 60.91           C  
ANISOU 2208  CG  GLN A 313     8686   6719   7739    152   1176    137       C  
ATOM   2209  CD  GLN A 313      54.214  -7.183  64.594  1.00 70.29           C  
ANISOU 2209  CD  GLN A 313     9915   7865   8927    132   1225    132       C  
ATOM   2210  OE1 GLN A 313      54.645  -8.329  64.452  1.00 77.20           O  
ANISOU 2210  OE1 GLN A 313    10815   8730   9790    107   1172    128       O  
ATOM   2211  NE2 GLN A 313      53.110  -6.915  65.282  1.00 72.65           N  
ANISOU 2211  NE2 GLN A 313    10226   8135   9243    141   1327    133       N  
ATOM   2212  N   SER A 314      54.318  -5.063  60.230  1.00 33.88           N  
ANISOU 2212  N   SER A 314     4986   3379   4508    160   1071    161       N  
ATOM   2213  CA  SER A 314      53.337  -4.151  59.641  1.00 24.62           C  
ANISOU 2213  CA  SER A 314     3740   2212   3402    175   1109    174       C  
ATOM   2214  C   SER A 314      52.264  -4.916  58.870  1.00 23.55           C  
ANISOU 2214  C   SER A 314     3529   2071   3347    165   1122    180       C  
ATOM   2215  O   SER A 314      51.063  -4.619  58.984  1.00 14.48           O  
ANISOU 2215  O   SER A 314     2342    906   2255    174   1193    190       O  
ATOM   2216  CB  SER A 314      54.038  -3.144  58.729  1.00 21.58           C  
ANISOU 2216  CB  SER A 314     3321   1858   3021    183   1043    177       C  
ATOM   2217  OG  SER A 314      54.974  -2.364  59.454  1.00 45.36           O  
ANISOU 2217  OG  SER A 314     6402   4868   5964    192   1030    171       O  
ATOM   2218  N   ILE A 315      52.681  -5.904  58.074  1.00 30.04           N  
ANISOU 2218  N   ILE A 315     4330   2904   4178    146   1053    175       N  
ATOM   2219  CA  ILE A 315      51.711  -6.699  57.320  1.00 22.90           C  
ANISOU 2219  CA  ILE A 315     3363   1989   3347    134   1054    180       C  
ATOM   2220  C   ILE A 315      50.794  -7.461  58.273  1.00 20.80           C  
ANISOU 2220  C   ILE A 315     3132   1679   3092    126   1129    179       C  
ATOM   2221  O   ILE A 315      49.579  -7.565  58.046  1.00 20.84           O  
ANISOU 2221  O   ILE A 315     3081   1666   3170    126   1176    186       O  
ATOM   2222  CB  ILE A 315      52.430  -7.646  56.342  1.00 23.98           C  
ANISOU 2222  CB  ILE A 315     3490   2141   3479    114    961    176       C  
ATOM   2223  CG1 ILE A 315      53.330  -6.853  55.393  1.00 31.37           C  
ANISOU 2223  CG1 ILE A 315     4394   3118   4406    122    893    176       C  
ATOM   2224  CG2 ILE A 315      51.420  -8.454  55.546  1.00 14.26           C  
ANISOU 2224  CG2 ILE A 315     2203    894   2320    100    955    183       C  
ATOM   2225  CD1 ILE A 315      54.023  -7.712  54.354  1.00 28.28           C  
ANISOU 2225  CD1 ILE A 315     3991   2742   4014    105    807    173       C  
ATOM   2226  N   SER A 316      51.356  -7.997  59.360  1.00 20.54           N  
ANISOU 2226  N   SER A 316     3193   1624   2988    116   1141    169       N  
ATOM   2227  CA  SER A 316      50.538  -8.713  60.337  1.00 27.87           C  
ANISOU 2227  CA  SER A 316     4170   2503   3918    102   1212    166       C  
ATOM   2228  C   SER A 316      49.539  -7.779  61.014  1.00 29.30           C  
ANISOU 2228  C   SER A 316     4335   2670   4129    126   1318    170       C  
ATOM   2229  O   SER A 316      48.413  -8.182  61.332  1.00 40.31           O  
ANISOU 2229  O   SER A 316     5716   4027   5572    118   1385    171       O  
ATOM   2230  CB  SER A 316      51.431  -9.389  61.377  1.00 38.15           C  
ANISOU 2230  CB  SER A 316     5584   3782   5128     86   1198    156       C  
ATOM   2231  OG  SER A 316      52.238 -10.389  60.778  1.00 58.60           O  
ANISOU 2231  OG  SER A 316     8190   6377   7700     61   1105    156       O  
ATOM   2232  N   ASN A 317      49.934  -6.525  61.245  1.00 32.72           N  
ANISOU 2232  N   ASN A 317     4771   3128   4532    152   1334    173       N  
ATOM   2233  CA  ASN A 317      49.009  -5.559  61.828  1.00 32.59           C  
ANISOU 2233  CA  ASN A 317     4742   3098   4544    175   1432    183       C  
ATOM   2234  C   ASN A 317      47.864  -5.258  60.871  1.00 32.40           C  
ANISOU 2234  C   ASN A 317     4605   3078   4628    182   1452    198       C  
ATOM   2235  O   ASN A 317      46.705  -5.129  61.292  1.00 26.30           O  
ANISOU 2235  O   ASN A 317     3807   2277   3909    189   1542    205       O  
ATOM   2236  CB  ASN A 317      49.750  -4.274  62.202  1.00 23.27           C  
ANISOU 2236  CB  ASN A 317     3601   1936   3305    196   1427    188       C  
ATOM   2237  CG  ASN A 317      50.746  -4.481  63.319  1.00 34.05           C  
ANISOU 2237  CG  ASN A 317     5082   3290   4566    192   1420    174       C  
ATOM   2238  OD1 ASN A 317      50.682  -5.470  64.043  1.00 41.44           O  
ANISOU 2238  OD1 ASN A 317     6077   4197   5472    176   1445    161       O  
ATOM   2239  ND2 ASN A 317      51.675  -3.542  63.467  1.00 43.54           N  
ANISOU 2239  ND2 ASN A 317     6321   4509   5712    205   1382    175       N  
ATOM   2240  N   GLU A 318      48.170  -5.141  59.576  1.00 33.02           N  
ANISOU 2240  N   GLU A 318     4615   3190   4740    178   1368    204       N  
ATOM   2241  CA  GLU A 318      47.100  -4.983  58.595  1.00 28.66           C  
ANISOU 2241  CA  GLU A 318     3958   2640   4291    181   1374    219       C  
ATOM   2242  C   GLU A 318      46.166  -6.187  58.604  1.00 31.31           C  
ANISOU 2242  C   GLU A 318     4271   2942   4685    163   1402    213       C  
ATOM   2243  O   GLU A 318      44.943  -6.037  58.491  1.00 30.78           O  
ANISOU 2243  O   GLU A 318     4138   2855   4703    169   1461    223       O  
ATOM   2244  CB  GLU A 318      47.678  -4.772  57.196  1.00 15.05           C  
ANISOU 2244  CB  GLU A 318     2181    955   2583    176   1272    222       C  
ATOM   2245  CG  GLU A 318      48.373  -3.438  56.998  1.00 21.41           C  
ANISOU 2245  CG  GLU A 318     2998   1783   3353    192   1241    229       C  
ATOM   2246  CD  GLU A 318      48.922  -3.280  55.596  1.00 22.86           C  
ANISOU 2246  CD  GLU A 318     3134   1998   3552    185   1144    228       C  
ATOM   2247  OE1 GLU A 318      49.858  -4.026  55.242  1.00 24.10           O  
ANISOU 2247  OE1 GLU A 318     3313   2174   3669    170   1078    215       O  
ATOM   2248  OE2 GLU A 318      48.409  -2.424  54.844  1.00 22.29           O  
ANISOU 2248  OE2 GLU A 318     3008   1930   3532    194   1133    242       O  
ATOM   2249  N   GLN A 319      46.725  -7.391  58.763  1.00 28.68           N  
ANISOU 2249  N   GLN A 319     3997   2594   4306    137   1357    199       N  
ATOM   2250  CA  GLN A 319      45.891  -8.590  58.825  1.00 16.78           C  
ANISOU 2250  CA  GLN A 319     2491   1041   2844    109   1371    197       C  
ATOM   2251  C   GLN A 319      44.967  -8.563  60.038  1.00 32.73           C  
ANISOU 2251  C   GLN A 319     4545   3014   4879    111   1485    192       C  
ATOM   2252  O   GLN A 319      43.778  -8.900  59.938  1.00 37.27           O  
ANISOU 2252  O   GLN A 319     5072   3552   5535    100   1527    197       O  
ATOM   2253  CB  GLN A 319      46.772  -9.838  58.864  1.00 39.09           C  
ANISOU 2253  CB  GLN A 319     5395   3852   5603     72   1296    189       C  
ATOM   2254  CG  GLN A 319      46.002 -11.135  59.051  1.00 53.53           C  
ANISOU 2254  CG  GLN A 319     7255   5624   7462     25   1301    193       C  
ATOM   2255  CD  GLN A 319      46.912 -12.322  59.305  1.00 71.02           C  
ANISOU 2255  CD  GLN A 319     9566   7819   9600    -17   1234    192       C  
ATOM   2256  OE1 GLN A 319      48.104 -12.159  59.560  1.00 79.10           O  
ANISOU 2256  OE1 GLN A 319    10639   8869  10547     -4   1199    184       O  
ATOM   2257  NE2 GLN A 319      46.352 -13.524  59.239  1.00 73.73           N  
ANISOU 2257  NE2 GLN A 319     9938   8113   9964    -74   1214    205       N  
ATOM   2258  N   LYS A 320      45.497  -8.160  61.195  1.00 27.19           N  
ANISOU 2258  N   LYS A 320     3927   2307   4098    123   1534    183       N  
ATOM   2259  CA  LYS A 320      44.675  -8.108  62.400  1.00 26.57           C  
ANISOU 2259  CA  LYS A 320     3891   2180   4023    125   1646    176       C  
ATOM   2260  C   LYS A 320      43.562  -7.078  62.263  1.00 26.84           C  
ANISOU 2260  C   LYS A 320     3835   2217   4144    159   1730    189       C  
ATOM   2261  O   LYS A 320      42.416  -7.336  62.654  1.00 26.42           O  
ANISOU 2261  O   LYS A 320     3763   2117   4157    154   1807    186       O  
ATOM   2262  CB  LYS A 320      45.530  -7.801  63.629  1.00 36.96           C  
ANISOU 2262  CB  LYS A 320     5321   3493   5229    134   1677    165       C  
ATOM   2263  CG  LYS A 320      44.712  -7.759  64.915  1.00 57.93           C  
ANISOU 2263  CG  LYS A 320     8034   6096   7881    136   1797    155       C  
ATOM   2264  CD  LYS A 320      45.498  -7.223  66.098  1.00 68.77           C  
ANISOU 2264  CD  LYS A 320     9516   7469   9146    151   1833    146       C  
ATOM   2265  CE  LYS A 320      44.586  -7.045  67.305  1.00 67.79           C  
ANISOU 2265  CE  LYS A 320     9441   7293   9025    155   1944    138       C  
ATOM   2266  NZ  LYS A 320      45.275  -6.395  68.454  1.00 64.04           N  
ANISOU 2266  NZ  LYS A 320     9065   6819   8448    166   1940    137       N  
ATOM   2267  N   ALA A 321      43.883  -5.897  61.727  1.00 31.31           N  
ANISOU 2267  N   ALA A 321     4352   2831   4713    186   1711    208       N  
ATOM   2268  CA  ALA A 321      42.851  -4.887  61.514  1.00 23.23           C  
ANISOU 2268  CA  ALA A 321     3254   1809   3765    202   1723    232       C  
ATOM   2269  C   ALA A 321      41.789  -5.385  60.541  1.00 27.96           C  
ANISOU 2269  C   ALA A 321     3746   2397   4482    194   1717    237       C  
ATOM   2270  O   ALA A 321      40.590  -5.143  60.738  1.00 31.19           O  
ANISOU 2270  O   ALA A 321     4110   2777   4963    198   1759    247       O  
ATOM   2271  CB  ALA A 321      43.480  -3.590  61.007  1.00 19.66           C  
ANISOU 2271  CB  ALA A 321     2788   1395   3285    219   1672    253       C  
ATOM   2272  N   CYS A 322      42.214  -6.088  59.486  1.00 24.06           N  
ANISOU 2272  N   CYS A 322     3213   1922   4008    182   1660    232       N  
ATOM   2273  CA  CYS A 322      41.269  -6.678  58.546  1.00 19.49           C  
ANISOU 2273  CA  CYS A 322     2544   1328   3535    169   1633    237       C  
ATOM   2274  C   CYS A 322      40.311  -7.628  59.253  1.00 26.45           C  
ANISOU 2274  C   CYS A 322     3452   2141   4459    147   1694    224       C  
ATOM   2275  O   CYS A 322      39.092  -7.563  59.054  1.00 25.99           O  
ANISOU 2275  O   CYS A 322     3317   2052   4505    151   1739    231       O  
ATOM   2276  CB  CYS A 322      42.033  -7.405  57.438  1.00 21.84           C  
ANISOU 2276  CB  CYS A 322     2838   1650   3811    146   1507    234       C  
ATOM   2277  SG  CYS A 322      41.024  -8.475  56.388  1.00 26.50           S  
ANISOU 2277  SG  CYS A 322     3357   2207   4503    114   1454    240       S  
ATOM   2278  N   LYS A 323      40.845  -8.511  60.098  1.00 37.79           N  
ANISOU 2278  N   LYS A 323     5001   3545   5813    113   1689    208       N  
ATOM   2279  CA  LYS A 323      39.990  -9.487  60.770  1.00 20.66           C  
ANISOU 2279  CA  LYS A 323     2878   1303   3670     61   1729    205       C  
ATOM   2280  C   LYS A 323      39.057  -8.823  61.782  1.00 25.48           C  
ANISOU 2280  C   LYS A 323     3486   1875   4322     86   1860    200       C  
ATOM   2281  O   LYS A 323      37.897  -9.228  61.922  1.00 28.14           O  
ANISOU 2281  O   LYS A 323     3798   2156   4737     46   1897    209       O  
ATOM   2282  CB  LYS A 323      40.845 -10.570  61.427  1.00 31.93           C  
ANISOU 2282  CB  LYS A 323     4434   2707   4990      4   1686    200       C  
ATOM   2283  CG  LYS A 323      41.595 -11.419  60.408  1.00 38.86           C  
ANISOU 2283  CG  LYS A 323     5317   3609   5840    -30   1560    209       C  
ATOM   2284  CD  LYS A 323      42.411 -12.527  61.052  1.00 46.07           C  
ANISOU 2284  CD  LYS A 323     6354   4497   6654    -88   1518    209       C  
ATOM   2285  CE  LYS A 323      43.023 -13.426  59.986  1.00 51.12           C  
ANISOU 2285  CE  LYS A 323     6994   5152   7278   -122   1397    222       C  
ATOM   2286  NZ  LYS A 323      43.831 -14.533  60.568  1.00 55.19           N  
ANISOU 2286  NZ  LYS A 323     7627   5642   7702   -178   1353    227       N  
ATOM   2287  N   VAL A 324      39.536  -7.797  62.488  1.00 35.06           N  
ANISOU 2287  N   VAL A 324     4726   3115   5479    140   1926    192       N  
ATOM   2288  CA  VAL A 324      38.682  -7.106  63.455  1.00 33.61           C  
ANISOU 2288  CA  VAL A 324     4550   2898   5321    162   2023    191       C  
ATOM   2289  C   VAL A 324      37.538  -6.390  62.743  1.00 35.53           C  
ANISOU 2289  C   VAL A 324     4673   3152   5676    179   2001    216       C  
ATOM   2290  O   VAL A 324      36.374  -6.457  63.168  1.00 40.77           O  
ANISOU 2290  O   VAL A 324     5316   3752   6423    176   2080    214       O  
ATOM   2291  CB  VAL A 324      39.514  -6.134  64.311  1.00 30.65           C  
ANISOU 2291  CB  VAL A 324     4252   2563   4830    182   2001    199       C  
ATOM   2292  CG1 VAL A 324      38.605  -5.296  65.198  1.00 22.16           C  
ANISOU 2292  CG1 VAL A 324     3182   1463   3775    198   2059    210       C  
ATOM   2293  CG2 VAL A 324      40.514  -6.904  65.158  1.00 31.21           C  
ANISOU 2293  CG2 VAL A 324     4452   2613   4794    163   2028    172       C  
ATOM   2294  N   LEU A 325      37.847  -5.689  61.649  1.00 36.58           N  
ANISOU 2294  N   LEU A 325     4733   3352   5816    192   1904    241       N  
ATOM   2295  CA  LEU A 325      36.787  -5.036  60.891  1.00 34.43           C  
ANISOU 2295  CA  LEU A 325     4353   3086   5642    202   1880    266       C  
ATOM   2296  C   LEU A 325      35.841  -6.053  60.266  1.00 36.84           C  
ANISOU 2296  C   LEU A 325     4587   3341   6071    186   1902    255       C  
ATOM   2297  O   LEU A 325      34.647  -5.774  60.116  1.00 45.83           O  
ANISOU 2297  O   LEU A 325     5655   4433   7325    196   1946    269       O  
ATOM   2298  CB  LEU A 325      37.387  -4.123  59.826  1.00 31.85           C  
ANISOU 2298  CB  LEU A 325     3982   2818   5301    210   1791    295       C  
ATOM   2299  CG  LEU A 325      38.157  -2.936  60.405  1.00 30.85           C  
ANISOU 2299  CG  LEU A 325     3927   2707   5089    227   1801    314       C  
ATOM   2300  CD1 LEU A 325      38.730  -2.089  59.298  1.00 29.61           C  
ANISOU 2300  CD1 LEU A 325     3735   2580   4937    236   1737    337       C  
ATOM   2301  CD2 LEU A 325      37.253  -2.102  61.300  1.00 21.15           C  
ANISOU 2301  CD2 LEU A 325     2717   1432   3889    242   1883    339       C  
ATOM   2302  N   GLY A 326      36.344  -7.240  59.920  1.00 21.66           N  
ANISOU 2302  N   GLY A 326     2681   1395   4153    164   1909    236       N  
ATOM   2303  CA  GLY A 326      35.456  -8.293  59.458  1.00 38.59           C  
ANISOU 2303  CA  GLY A 326     4803   3485   6375     93   1872    247       C  
ATOM   2304  C   GLY A 326      34.511  -8.765  60.545  1.00 44.57           C  
ANISOU 2304  C   GLY A 326     5610   4179   7146     11   1946    261       C  
ATOM   2305  O   GLY A 326      33.343  -9.054  60.279  1.00 51.04           O  
ANISOU 2305  O   GLY A 326     6358   4993   8041    -73   1950    295       O  
ATOM   2306  N   ILE A 327      35.004  -8.856  61.783  1.00 44.85           N  
ANISOU 2306  N   ILE A 327     5755   4195   7089      2   2005    246       N  
ATOM   2307  CA  ILE A 327      34.131  -9.173  62.912  1.00 43.80           C  
ANISOU 2307  CA  ILE A 327     5659   4032   6950    -94   2089    271       C  
ATOM   2308  C   ILE A 327      33.049  -8.110  63.063  1.00 48.38           C  
ANISOU 2308  C   ILE A 327     6149   4540   7695    -25   2270    275       C  
ATOM   2309  O   ILE A 327      31.874  -8.425  63.294  1.00 57.75           O  
ANISOU 2309  O   ILE A 327     7252   5753   8937   -140   2359    317       O  
ATOM   2310  CB  ILE A 327      34.953  -9.329  64.205  1.00 38.51           C  
ANISOU 2310  CB  ILE A 327     5131   3339   6163    -91   2135    248       C  
ATOM   2311  CG1 ILE A 327      35.790 -10.609  64.159  1.00 32.46           C  
ANISOU 2311  CG1 ILE A 327     4450   2582   5299   -175   2047    254       C  
ATOM   2312  CG2 ILE A 327      34.044  -9.321  65.428  1.00 32.75           C  
ANISOU 2312  CG2 ILE A 327     4421   2599   5423   -173   2245    276       C  
ATOM   2313  CD1 ILE A 327      36.577 -10.867  65.427  1.00 31.22           C  
ANISOU 2313  CD1 ILE A 327     4435   2403   5026   -185   2083    236       C  
ATOM   2314  N   VAL A 328      33.431  -6.837  62.942  1.00 45.05           N  
ANISOU 2314  N   VAL A 328     5715   4059   7344    156   2348    239       N  
ATOM   2315  CA  VAL A 328      32.454  -5.749  63.030  1.00 44.86           C  
ANISOU 2315  CA  VAL A 328     5633   3941   7469    204   2460    277       C  
ATOM   2316  C   VAL A 328      31.383  -5.906  61.953  1.00 40.44           C  
ANISOU 2316  C   VAL A 328     4917   3366   7084    166   2475    314       C  
ATOM   2317  O   VAL A 328      30.173  -5.848  62.229  1.00 32.62           O  
ANISOU 2317  O   VAL A 328     3789   2491   6113     73   2559    349       O  
ATOM   2318  CB  VAL A 328      33.160  -4.384  62.925  1.00 26.67           C  
ANISOU 2318  CB  VAL A 328     3347   1753   5032    267   2316    291       C  
ATOM   2319  CG1 VAL A 328      32.151  -3.278  62.657  1.00 28.07           C  
ANISOU 2319  CG1 VAL A 328     3478   1806   5379    253   2402    392       C  
ATOM   2320  CG2 VAL A 328      33.953  -4.095  64.192  1.00 40.37           C  
ANISOU 2320  CG2 VAL A 328     5198   3538   6603    271   2336    274       C  
ATOM   2321  N   PHE A 329      31.822  -6.097  60.705  1.00 42.03           N  
ANISOU 2321  N   PHE A 329     5067   3619   7286    197   2328    302       N  
ATOM   2322  CA  PHE A 329      30.899  -6.264  59.586  1.00 50.62           C  
ANISOU 2322  CA  PHE A 329     6007   4710   8518    153   2305    337       C  
ATOM   2323  C   PHE A 329      29.959  -7.438  59.827  1.00 50.33           C  
ANISOU 2323  C   PHE A 329     5879   4844   8402    -62   2304    364       C  
ATOM   2324  O   PHE A 329      28.743  -7.335  59.617  1.00 57.11           O  
ANISOU 2324  O   PHE A 329     6549   5832   9318   -125   2362    383       O  
ATOM   2325  CB  PHE A 329      31.681  -6.493  58.290  1.00 61.47           C  
ANISOU 2325  CB  PHE A 329     7356   6164   9835    190   2123    316       C  
ATOM   2326  CG  PHE A 329      32.643  -5.391  57.937  1.00 60.93           C  
ANISOU 2326  CG  PHE A 329     7313   6258   9580    223   1961    321       C  
ATOM   2327  CD1 PHE A 329      32.492  -4.112  58.447  1.00 57.04           C  
ANISOU 2327  CD1 PHE A 329     6818   5791   9064    224   2017    364       C  
ATOM   2328  CD2 PHE A 329      33.708  -5.646  57.087  1.00 51.94           C  
ANISOU 2328  CD2 PHE A 329     6192   5247   8297    195   1789    309       C  
ATOM   2329  CE1 PHE A 329      33.388  -3.110  58.115  1.00 50.97           C  
ANISOU 2329  CE1 PHE A 329     6104   5096   8168    209   1900    393       C  
ATOM   2330  CE2 PHE A 329      34.603  -4.650  56.751  1.00 44.94           C  
ANISOU 2330  CE2 PHE A 329     5334   4454   7286    193   1686    325       C  
ATOM   2331  CZ  PHE A 329      34.444  -3.381  57.266  1.00 44.58           C  
ANISOU 2331  CZ  PHE A 329     5312   4400   7226    203   1725    358       C  
ATOM   2332  N   PHE A 330      30.519  -8.572  60.254  1.00 39.48           N  
ANISOU 2332  N   PHE A 330     4617   3517   6866   -175   2221    360       N  
ATOM   2333  CA  PHE A 330      29.730  -9.778  60.469  1.00 43.76           C  
ANISOU 2333  CA  PHE A 330     5099   4202   7325   -388   2207    397       C  
ATOM   2334  C   PHE A 330      28.681  -9.557  61.548  1.00 47.45           C  
ANISOU 2334  C   PHE A 330     5462   4778   7789   -453   2384    408       C  
ATOM   2335  O   PHE A 330      27.520  -9.940  61.383  1.00 55.45           O  
ANISOU 2335  O   PHE A 330     6295   5962   8813   -572   2426    429       O  
ATOM   2336  CB  PHE A 330      30.651 -10.943  60.834  1.00 44.74           C  
ANISOU 2336  CB  PHE A 330     5392   4337   7270   -481   2068    405       C  
ATOM   2337  CG  PHE A 330      29.924 -12.218  61.165  1.00 51.08           C  
ANISOU 2337  CG  PHE A 330     6158   5266   7985   -700   2052    456       C  
ATOM   2338  CD1 PHE A 330      29.593 -13.114  60.162  1.00 51.45           C  
ANISOU 2338  CD1 PHE A 330     6150   5367   8031   -812   1947    485       C  
ATOM   2339  CD2 PHE A 330      29.584 -12.528  62.473  1.00 52.51           C  
ANISOU 2339  CD2 PHE A 330     6361   5499   8091   -791   2158    476       C  
ATOM   2340  CE1 PHE A 330      28.933 -14.293  60.454  1.00 46.70           C  
ANISOU 2340  CE1 PHE A 330     5513   4858   7371  -1009   1957    535       C  
ATOM   2341  CE2 PHE A 330      28.920 -13.704  62.770  1.00 53.32           C  
ANISOU 2341  CE2 PHE A 330     6422   5719   8118   -990   2150    532       C  
ATOM   2342  CZ  PHE A 330      28.596 -14.587  61.760  1.00 50.26           C  
ANISOU 2342  CZ  PHE A 330     5979   5368   7750  -1098   2060    560       C  
ATOM   2343  N   LEU A 331      29.077  -8.955  62.671  1.00 45.63           N  
ANISOU 2343  N   LEU A 331     5333   4482   7523   -376   2484    390       N  
ATOM   2344  CA  LEU A 331      28.121  -8.721  63.747  1.00 49.72           C  
ANISOU 2344  CA  LEU A 331     5750   5135   8005   -426   2648    393       C  
ATOM   2345  C   LEU A 331      26.982  -7.826  63.278  1.00 58.14           C  
ANISOU 2345  C   LEU A 331     6578   6340   9173   -354   2729    378       C  
ATOM   2346  O   LEU A 331      25.804  -8.143  63.486  1.00 69.81           O  
ANISOU 2346  O   LEU A 331     7865   8040  10621   -452   2799    380       O  
ATOM   2347  CB  LEU A 331      28.828  -8.111  64.958  1.00 45.19           C  
ANISOU 2347  CB  LEU A 331     5343   4451   7375   -334   2731    372       C  
ATOM   2348  CG  LEU A 331      29.685  -9.073  65.782  1.00 46.37           C  
ANISOU 2348  CG  LEU A 331     5686   4551   7383   -423   2671    379       C  
ATOM   2349  CD1 LEU A 331      30.236  -8.380  67.013  1.00 48.94           C  
ANISOU 2349  CD1 LEU A 331     6154   4785   7657   -332   2769    353       C  
ATOM   2350  CD2 LEU A 331      28.882 -10.301  66.176  1.00 36.55           C  
ANISOU 2350  CD2 LEU A 331     4366   3477   6045   -636   2678    424       C  
ATOM   2351  N   PHE A 332      27.314  -6.719  62.605  1.00 50.13           N  
ANISOU 2351  N   PHE A 332     5563   5215   8267   -178   2702    360       N  
ATOM   2352  CA  PHE A 332      26.274  -5.804  62.138  1.00 46.82           C  
ANISOU 2352  CA  PHE A 332     4916   4955   7917    -80   2739    335       C  
ATOM   2353  C   PHE A 332      25.317  -6.503  61.173  1.00 51.25           C  
ANISOU 2353  C   PHE A 332     5267   5689   8517   -189   2686    342       C  
ATOM   2354  O   PHE A 332      24.088  -6.447  61.340  1.00 53.77           O  
ANISOU 2354  O   PHE A 332     5361   6252   8816   -217   2755    319       O  
ATOM   2355  CB  PHE A 332      26.917  -4.581  61.482  1.00 42.36           C  
ANISOU 2355  CB  PHE A 332     4421   4235   7440    110   2672    328       C  
ATOM   2356  CG  PHE A 332      25.938  -3.663  60.809  1.00 40.37           C  
ANISOU 2356  CG  PHE A 332     3950   4156   7232    230   2648    291       C  
ATOM   2357  CD1 PHE A 332      25.184  -2.771  61.551  1.00 42.18           C  
ANISOU 2357  CD1 PHE A 332     4072   4556   7396    341   2727    237       C  
ATOM   2358  CD2 PHE A 332      25.781  -3.681  59.433  1.00 43.53           C  
ANISOU 2358  CD2 PHE A 332     4259   4556   7724    246   2532    300       C  
ATOM   2359  CE1 PHE A 332      24.287  -1.920  60.934  1.00 43.92           C  
ANISOU 2359  CE1 PHE A 332     4100   4951   7638    475   2682    186       C  
ATOM   2360  CE2 PHE A 332      24.883  -2.833  58.813  1.00 43.21           C  
ANISOU 2360  CE2 PHE A 332     4026   4686   7706    371   2489    255       C  
ATOM   2361  CZ  PHE A 332      24.136  -1.952  59.565  1.00 39.86           C  
ANISOU 2361  CZ  PHE A 332     3498   4437   7210    491   2560    195       C  
ATOM   2362  N   VAL A 333      25.868  -7.186  60.166  1.00 49.33           N  
ANISOU 2362  N   VAL A 333     5093   5330   8319   -251   2557    371       N  
ATOM   2363  CA  VAL A 333      25.034  -7.801  59.139  1.00 46.04           C  
ANISOU 2363  CA  VAL A 333     4493   5059   7942   -352   2488    381       C  
ATOM   2364  C   VAL A 333      24.196  -8.933  59.722  1.00 48.60           C  
ANISOU 2364  C   VAL A 333     4725   5579   8162   -564   2535    400       C  
ATOM   2365  O   VAL A 333      23.007  -9.062  59.411  1.00 42.14           O  
ANISOU 2365  O   VAL A 333     3671   4983   7358   -624   2561    392       O  
ATOM   2366  CB  VAL A 333      25.906  -8.287  57.968  1.00 42.86           C  
ANISOU 2366  CB  VAL A 333     4212   4484   7590   -364   2329    404       C  
ATOM   2367  CG1 VAL A 333      25.103  -9.199  57.054  1.00 42.17           C  
ANISOU 2367  CG1 VAL A 333     3974   4543   7505   -514   2251    420       C  
ATOM   2368  CG2 VAL A 333      26.458  -7.099  57.195  1.00 43.22           C  
ANISOU 2368  CG2 VAL A 333     4288   4375   7759   -162   2283    393       C  
ATOM   2369  N   VAL A 334      24.796  -9.777  60.565  1.00 45.78           N  
ANISOU 2369  N   VAL A 334     4549   5153   7691   -678   2537    428       N  
ATOM   2370  CA  VAL A 334      24.066 -10.897  61.145  1.00 43.88           C  
ANISOU 2370  CA  VAL A 334     4245   5085   7344   -889   2570    462       C  
ATOM   2371  C   VAL A 334      22.966 -10.403  62.071  1.00 49.28           C  
ANISOU 2371  C   VAL A 334     4741   5982   8000   -881   2738    441       C  
ATOM   2372  O   VAL A 334      21.891 -11.009  62.143  1.00 51.58           O  
ANISOU 2372  O   VAL A 334     4852   6491   8254  -1022   2777    461       O  
ATOM   2373  CB  VAL A 334      25.044 -11.847  61.863  1.00 40.46           C  
ANISOU 2373  CB  VAL A 334     4063   4525   6786   -987   2513    499       C  
ATOM   2374  CG1 VAL A 334      24.307 -12.778  62.811  1.00 54.12           C  
ANISOU 2374  CG1 VAL A 334     5740   6421   8403  -1176   2582    542       C  
ATOM   2375  CG2 VAL A 334      25.829 -12.649  60.842  1.00 38.53           C  
ANISOU 2375  CG2 VAL A 334     3947   4165   6529  -1032   2321    521       C  
ATOM   2376  N   MET A 335      23.192  -9.293  62.778  1.00 50.99           N  
ANISOU 2376  N   MET A 335     4992   6153   8227   -712   2836    400       N  
ATOM   2377  CA  MET A 335      22.149  -8.794  63.664  1.00 58.03           C  
ANISOU 2377  CA  MET A 335     5707   7266   9074   -684   2987    370       C  
ATOM   2378  C   MET A 335      21.021  -8.129  62.887  1.00 66.17           C  
ANISOU 2378  C   MET A 335     6453   8504  10183   -595   2994    328       C  
ATOM   2379  O   MET A 335      19.867  -8.163  63.330  1.00 78.53           O  
ANISOU 2379  O   MET A 335     7809  10326  11705   -638   3089    313       O  
ATOM   2380  CB  MET A 335      22.743  -7.836  64.694  1.00 52.11           C  
ANISOU 2380  CB  MET A 335     5097   6412   8290   -530   3077    337       C  
ATOM   2381  CG  MET A 335      23.547  -8.550  65.769  1.00 50.61           C  
ANISOU 2381  CG  MET A 335     5141   6097   7991   -636   3101    372       C  
ATOM   2382  SD  MET A 335      23.958  -7.512  67.181  1.00 62.65           S  
ANISOU 2382  SD  MET A 335     6793   7561   9449   -487   3232    333       S  
ATOM   2383  CE  MET A 335      24.607  -8.737  68.315  1.00 67.98           C  
ANISOU 2383  CE  MET A 335     7688   8156   9987   -671   3241    385       C  
ATOM   2384  N   TRP A 336      21.318  -7.523  61.736  1.00 59.29           N  
ANISOU 2384  N   TRP A 336     5568   7538   9423   -466   2890    308       N  
ATOM   2385  CA  TRP A 336      20.246  -6.930  60.942  1.00 55.61           C  
ANISOU 2385  CA  TRP A 336     4832   7275   9022   -374   2872    266       C  
ATOM   2386  C   TRP A 336      19.593  -7.902  59.965  1.00 54.32           C  
ANISOU 2386  C   TRP A 336     4519   7231   8890   -542   2791    296       C  
ATOM   2387  O   TRP A 336      18.555  -7.563  59.386  1.00 50.69           O  
ANISOU 2387  O   TRP A 336     3809   6980   8470   -494   2781    263       O  
ATOM   2388  CB  TRP A 336      20.755  -5.712  60.166  1.00 49.98           C  
ANISOU 2388  CB  TRP A 336     4160   6429   8402   -141   2789    229       C  
ATOM   2389  CG  TRP A 336      20.612  -4.429  60.917  1.00 50.51           C  
ANISOU 2389  CG  TRP A 336     4216   6543   8433     65   2864    170       C  
ATOM   2390  CD1 TRP A 336      21.611  -3.586  61.287  1.00 54.20           C  
ANISOU 2390  CD1 TRP A 336     4895   6806   8894    208   2853    160       C  
ATOM   2391  CD2 TRP A 336      19.394  -3.843  61.398  1.00 58.85           C  
ANISOU 2391  CD2 TRP A 336     5043   7876   9442    150   2951    109       C  
ATOM   2392  NE1 TRP A 336      21.099  -2.506  61.964  1.00 59.81           N  
ANISOU 2392  NE1 TRP A 336     5533   7644   9549    375   2918     95       N  
ATOM   2393  CE2 TRP A 336      19.738  -2.641  62.046  1.00 62.58           C  
ANISOU 2393  CE2 TRP A 336     5613   8290   9876    350   2982     60       C  
ATOM   2394  CE3 TRP A 336      18.047  -4.218  61.342  1.00 59.21           C  
ANISOU 2394  CE3 TRP A 336     4810   8219   9469     75   3001     92       C  
ATOM   2395  CZ2 TRP A 336      18.786  -1.811  62.635  1.00 65.77           C  
ANISOU 2395  CZ2 TRP A 336     5850   8918  10221    486   3060    -14       C  
ATOM   2396  CZ3 TRP A 336      17.104  -3.392  61.928  1.00 63.41           C  
ANISOU 2396  CZ3 TRP A 336     5166   8978   9949    212   3086     23       C  
ATOM   2397  CH2 TRP A 336      17.478  -2.204  62.566  1.00 66.64           C  
ANISOU 2397  CH2 TRP A 336     5683   9319  10319    420   3115    -32       C  
ATOM   2398  N   CYS A 337      20.154  -9.093  59.772  1.00 51.55           N  
ANISOU 2398  N   CYS A 337     4315   6763   8510   -730   2722    356       N  
ATOM   2399  CA  CYS A 337      19.604 -10.036  58.802  1.00 59.89           C  
ANISOU 2399  CA  CYS A 337     5255   7915   9584   -893   2627    387       C  
ATOM   2400  C   CYS A 337      18.222 -10.579  59.166  1.00 69.82           C  
ANISOU 2400  C   CYS A 337     6267   9478  10785  -1039   2705    400       C  
ATOM   2401  O   CYS A 337      17.376 -10.703  58.271  1.00 78.77           O  
ANISOU 2401  O   CYS A 337     7190  10771  11968  -1074   2651    393       O  
ATOM   2402  CB  CYS A 337      20.576 -11.203  58.594  1.00 65.54           C  
ANISOU 2402  CB  CYS A 337     6214   8437  10251  -1051   2521    446       C  
ATOM   2403  SG  CYS A 337      21.699 -10.992  57.192  1.00 71.80           S  
ANISOU 2403  SG  CYS A 337     7166   8971  11145   -946   2349    443       S  
ATOM   2404  N   PRO A 338      17.945 -10.942  60.429  1.00 69.00           N  
ANISOU 2404  N   PRO A 338     6175   9465  10577  -1131   2825    424       N  
ATOM   2405  CA  PRO A 338      16.583 -11.409  60.749  1.00 65.61           C  
ANISOU 2405  CA  PRO A 338     5491   9337  10101  -1261   2904    446       C  
ATOM   2406  C   PRO A 338      15.495 -10.415  60.383  1.00 63.74           C  
ANISOU 2406  C   PRO A 338     4958   9335   9924  -1106   2947    380       C  
ATOM   2407  O   PRO A 338      14.446 -10.818  59.862  1.00 67.87           O  
ANISOU 2407  O   PRO A 338     5247  10080  10463  -1200   2928    398       O  
ATOM   2408  CB  PRO A 338      16.649 -11.651  62.262  1.00 57.17           C  
ANISOU 2408  CB  PRO A 338     4514   8288   8919  -1322   3038    475       C  
ATOM   2409  CG  PRO A 338      18.061 -11.993  62.513  1.00 72.66           C  
ANISOU 2409  CG  PRO A 338     6804   9954  10851  -1337   2976    499       C  
ATOM   2410  CD  PRO A 338      18.849 -11.118  61.582  1.00 68.97           C  
ANISOU 2410  CD  PRO A 338     6419   9298  10489  -1148   2883    446       C  
ATOM   2411  N   PHE A 339      15.720  -9.122  60.630  1.00 61.57           N  
ANISOU 2411  N   PHE A 339     4692   9021   9680   -863   2992    307       N  
ATOM   2412  CA  PHE A 339      14.698  -8.127  60.320  1.00 65.94           C  
ANISOU 2412  CA  PHE A 339     4977   9804  10274   -687   3017    238       C  
ATOM   2413  C   PHE A 339      14.416  -8.070  58.826  1.00 64.59           C  
ANISOU 2413  C   PHE A 339     4678   9659  10203   -657   2873    225       C  
ATOM   2414  O   PHE A 339      13.255  -8.067  58.406  1.00 74.19           O  
ANISOU 2414  O   PHE A 339     5621  11135  11433   -667   2870    212       O  
ATOM   2415  CB  PHE A 339      15.108  -6.746  60.828  1.00 58.78           C  
ANISOU 2415  CB  PHE A 339     4145   8819   9370   -422   3066    166       C  
ATOM   2416  CG  PHE A 339      14.322  -5.628  60.204  1.00 60.01           C  
ANISOU 2416  CG  PHE A 339     4081   9144   9576   -201   3031     89       C  
ATOM   2417  CD1 PHE A 339      12.989  -5.441  60.527  1.00 63.15           C  
ANISOU 2417  CD1 PHE A 339     4195   9866   9933   -178   3115     58       C  
ATOM   2418  CD2 PHE A 339      14.908  -4.774  59.284  1.00 72.60           C  
ANISOU 2418  CD2 PHE A 339     5755  10578  11253    -12   2908     53       C  
ATOM   2419  CE1 PHE A 339      12.257  -4.420  59.951  1.00 64.38           C  
ANISOU 2419  CE1 PHE A 339     4153  10185  10125     37   3071    -16       C  
ATOM   2420  CE2 PHE A 339      14.180  -3.750  58.706  1.00 75.47           C  
ANISOU 2420  CE2 PHE A 339     5931  11096  11647    198   2859    -17       C  
ATOM   2421  CZ  PHE A 339      12.854  -3.573  59.041  1.00 62.47           C  
ANISOU 2421  CZ  PHE A 339     4005   9774   9956    226   2939    -57       C  
ATOM   2422  N   PHE A 340      15.466  -7.997  58.006  1.00 56.87           N  
ANISOU 2422  N   PHE A 340     3893   8418   9296   -611   2751    231       N  
ATOM   2423  CA  PHE A 340      15.263  -7.914  56.563  1.00 68.81           C  
ANISOU 2423  CA  PHE A 340     5303   9940  10903   -573   2609    219       C  
ATOM   2424  C   PHE A 340      14.637  -9.193  56.020  1.00 73.17           C  
ANISOU 2424  C   PHE A 340     5741  10618  11442   -826   2558    273       C  
ATOM   2425  O   PHE A 340      13.758  -9.138  55.149  1.00 81.19           O  
ANISOU 2425  O   PHE A 340     6530  11814  12503   -819   2495    255       O  
ATOM   2426  CB  PHE A 340      16.586  -7.611  55.862  1.00 63.46           C  
ANISOU 2426  CB  PHE A 340     4874   8943  10297   -478   2496    227       C  
ATOM   2427  CG  PHE A 340      17.008  -6.175  55.971  1.00 59.65           C  
ANISOU 2427  CG  PHE A 340     4452   8368   9845   -201   2498    173       C  
ATOM   2428  CD1 PHE A 340      17.698  -5.724  57.083  1.00 54.13           C  
ANISOU 2428  CD1 PHE A 340     3931   7542   9092   -128   2591    167       C  
ATOM   2429  CD2 PHE A 340      16.703  -5.271  54.967  1.00 59.13           C  
ANISOU 2429  CD2 PHE A 340     4274   8344   9847    -13   2398    129       C  
ATOM   2430  CE1 PHE A 340      18.084  -4.403  57.191  1.00 50.16           C  
ANISOU 2430  CE1 PHE A 340     3500   6956   8601    118   2580    120       C  
ATOM   2431  CE2 PHE A 340      17.085  -3.946  55.068  1.00 52.84           C  
ANISOU 2431  CE2 PHE A 340     3556   7465   9054    237   2381     82       C  
ATOM   2432  CZ  PHE A 340      17.777  -3.512  56.181  1.00 50.21           C  
ANISOU 2432  CZ  PHE A 340     3406   7007   8666    299   2471     78       C  
ATOM   2433  N   ILE A 341      15.075 -10.350  56.525  1.00 69.91           N  
ANISOU 2433  N   ILE A 341     5489  10115  10958  -1048   2574    342       N  
ATOM   2434  CA  ILE A 341      14.457 -11.621  56.146  1.00 70.17           C  
ANISOU 2434  CA  ILE A 341     5432  10272  10956  -1302   2526    405       C  
ATOM   2435  C   ILE A 341      12.958 -11.572  56.406  1.00 77.76           C  
ANISOU 2435  C   ILE A 341     6066  11581  11899  -1336   2608    406       C  
ATOM   2436  O   ILE A 341      12.141 -11.791  55.502  1.00 81.60           O  
ANISOU 2436  O   ILE A 341     6346  12231  12427  -1388   2535    411       O  
ATOM   2437  CB  ILE A 341      15.116 -12.792  56.896  1.00 63.45           C  
ANISOU 2437  CB  ILE A 341     4816   9287  10007  -1509   2540    485       C  
ATOM   2438  CG1 ILE A 341      16.525 -13.050  56.361  1.00 61.30           C  
ANISOU 2438  CG1 ILE A 341     4846   8696   9751  -1498   2420    494       C  
ATOM   2439  CG2 ILE A 341      14.263 -14.048  56.783  1.00 62.50           C  
ANISOU 2439  CG2 ILE A 341     4572   9338   9835  -1766   2516    569       C  
ATOM   2440  CD1 ILE A 341      17.282 -14.111  57.130  1.00 53.09           C  
ANISOU 2440  CD1 ILE A 341     4057   7512   8601  -1660   2414    565       C  
ATOM   2441  N   THR A 342      12.577 -11.271  57.652  1.00 76.13           N  
ANISOU 2441  N   THR A 342     5805  11493  11626  -1302   2761    406       N  
ATOM   2442  CA  THR A 342      11.165 -11.283  58.018  1.00 74.07           C  
ANISOU 2442  CA  THR A 342     5236  11564  11341  -1336   2852    427       C  
ATOM   2443  C   THR A 342      10.378 -10.210  57.275  1.00 67.93           C  
ANISOU 2443  C   THR A 342     4204  10971  10636  -1125   2820    348       C  
ATOM   2444  O   THR A 342       9.217 -10.433  56.921  1.00 70.00           O  
ANISOU 2444  O   THR A 342     4191  11490  10914  -1179   2817    383       O  
ATOM   2445  CB  THR A 342      11.017 -11.101  59.530  1.00 77.41           C  
ANISOU 2445  CB  THR A 342     5678  12057  11677  -1318   3026    440       C  
ATOM   2446  OG1 THR A 342      11.756 -12.126  60.206  1.00 75.21           O  
ANISOU 2446  OG1 THR A 342     5644  11605  11328  -1510   3042    518       O  
ATOM   2447  CG2 THR A 342       9.558 -11.193  59.947  1.00 83.21           C  
ANISOU 2447  CG2 THR A 342     6094  13128  12393  -1357   3130    489       C  
ATOM   2448  N   ASN A 343      11.000  -9.067  56.981  1.00 73.10           N  
ANISOU 2448  N   ASN A 343     4950  11486  11338   -879   2783    259       N  
ATOM   2449  CA  ASN A 343      10.290  -7.988  56.304  1.00 78.28           C  
ANISOU 2449  CA  ASN A 343     5387  12306  12052   -652   2738    183       C  
ATOM   2450  C   ASN A 343      10.008  -8.344  54.850  1.00 87.57           C  
ANISOU 2450  C   ASN A 343     6457  13510  13305   -707   2580    193       C  
ATOM   2451  O   ASN A 343       8.873  -8.207  54.377  1.00 99.80           O  
ANISOU 2451  O   ASN A 343     7724  15323  14872   -680   2559    189       O  
ATOM   2452  CB  ASN A 343      11.097  -6.692  56.400  1.00 70.58           C  
ANISOU 2452  CB  ASN A 343     4570  11147  11101   -375   2727    103       C  
ATOM   2453  CG  ASN A 343      10.228  -5.455  56.278  1.00 66.78           C  
ANISOU 2453  CG  ASN A 343     3868  10879  10625   -116   2734     22       C  
ATOM   2454  OD1 ASN A 343       9.082  -5.440  56.728  1.00 69.71           O  
ANISOU 2454  OD1 ASN A 343     3990  11545  10951   -121   2822     22       O  
ATOM   2455  ND2 ASN A 343      10.773  -4.408  55.669  1.00 65.16           N  
ANISOU 2455  ND2 ASN A 343     3760  10527  10470    118   2637    -38       N  
ATOM   2456  N   ILE A 344      11.030  -8.798  54.119  1.00 80.92           N  
ANISOU 2456  N   ILE A 344     5838  12399  12507   -779   2465    211       N  
ATOM   2457  CA  ILE A 344      10.813  -9.218  52.738  1.00 77.86           C  
ANISOU 2457  CA  ILE A 344     5373  12026  12185   -849   2312    220       C  
ATOM   2458  C   ILE A 344       9.852 -10.399  52.682  1.00 77.82           C  
ANISOU 2458  C   ILE A 344     5189  12238  12142  -1113   2319    295       C  
ATOM   2459  O   ILE A 344       9.020 -10.500  51.769  1.00 79.93           O  
ANISOU 2459  O   ILE A 344     5240  12681  12450  -1134   2234    298       O  
ATOM   2460  CB  ILE A 344      12.158  -9.539  52.058  1.00 69.08           C  
ANISOU 2460  CB  ILE A 344     4555  10573  11118   -880   2199    236       C  
ATOM   2461  CG1 ILE A 344      13.064  -8.307  52.077  1.00 63.79           C  
ANISOU 2461  CG1 ILE A 344     4047   9695  10495   -610   2187    186       C  
ATOM   2462  CG2 ILE A 344      11.939 -10.004  50.627  1.00 66.90           C  
ANISOU 2462  CG2 ILE A 344     4207  10309  10901   -957   2041    243       C  
ATOM   2463  CD1 ILE A 344      14.414  -8.536  51.441  1.00 55.08           C  
ANISOU 2463  CD1 ILE A 344     3227   8259   9441   -620   2082    216       C  
ATOM   2464  N   MET A 345       9.922 -11.294  53.673  1.00 76.18           N  
ANISOU 2464  N   MET A 345     5065  12024  11855  -1311   2414    372       N  
ATOM   2465  CA  MET A 345       9.001 -12.425  53.701  1.00 90.15           C  
ANISOU 2465  CA  MET A 345     6673  13984  13597  -1558   2420    480       C  
ATOM   2466  C   MET A 345       7.563 -11.963  53.911  1.00102.58           C  
ANISOU 2466  C   MET A 345     7927  15854  15194  -1469   2486    493       C  
ATOM   2467  O   MET A 345       6.650 -12.434  53.224  1.00111.06           O  
ANISOU 2467  O   MET A 345     8825  17053  16319  -1553   2412    552       O  
ATOM   2468  CB  MET A 345       9.424 -13.410  54.792  1.00 97.56           C  
ANISOU 2468  CB  MET A 345     7796  14820  14453  -1757   2504    574       C  
ATOM   2469  CG  MET A 345       8.496 -14.602  54.954  1.00111.43           C  
ANISOU 2469  CG  MET A 345     9443  16686  16209  -1981   2506    709       C  
ATOM   2470  SD  MET A 345       9.062 -15.745  56.230  1.00122.56           S  
ANISOU 2470  SD  MET A 345    11090  17942  17535  -2184   2591    826       S  
ATOM   2471  CE  MET A 345       9.004 -14.692  57.678  1.00129.69           C  
ANISOU 2471  CE  MET A 345    11949  18948  18381  -2008   2799    774       C  
ATOM   2472  N   ALA A 346       7.344 -11.027  54.838  1.00102.08           N  
ANISOU 2472  N   ALA A 346     7797  15886  15101  -1285   2618    447       N  
ATOM   2473  CA  ALA A 346       6.010 -10.490  55.069  1.00 99.42           C  
ANISOU 2473  CA  ALA A 346     7177  15808  14791  -1164   2683    465       C  
ATOM   2474  C   ALA A 346       5.510  -9.673  53.889  1.00 94.66           C  
ANISOU 2474  C   ALA A 346     6404  15304  14258   -977   2561    397       C  
ATOM   2475  O   ALA A 346       4.294  -9.543  53.716  1.00100.52           O  
ANISOU 2475  O   ALA A 346     6893  16241  15059   -927   2569    463       O  
ATOM   2476  CB  ALA A 346       6.001  -9.636  56.336  1.00101.75           C  
ANISOU 2476  CB  ALA A 346     7476  16163  15022   -996   2847    419       C  
ATOM   2477  N   VAL A 347       6.416  -9.118  53.083  1.00 90.77           N  
ANISOU 2477  N   VAL A 347     6045  14656  13787   -859   2452    295       N  
ATOM   2478  CA  VAL A 347       5.989  -8.446  51.859  1.00 92.06           C  
ANISOU 2478  CA  VAL A 347     6069  14892  14017   -695   2315    239       C  
ATOM   2479  C   VAL A 347       5.574  -9.470  50.810  1.00 93.09           C  
ANISOU 2479  C   VAL A 347     6125  15050  14193   -904   2186    310       C  
ATOM   2480  O   VAL A 347       4.617  -9.254  50.056  1.00 96.27           O  
ANISOU 2480  O   VAL A 347     6314  15615  14651   -839   2108    332       O  
ATOM   2481  CB  VAL A 347       7.102  -7.516  51.341  1.00 88.83           C  
ANISOU 2481  CB  VAL A 347     5833  14279  13639   -487   2240    137       C  
ATOM   2482  CG1 VAL A 347       6.741  -6.951  49.976  1.00 87.35           C  
ANISOU 2482  CG1 VAL A 347     5532  14139  13520   -338   2078     93       C  
ATOM   2483  CG2 VAL A 347       7.341  -6.381  52.326  1.00 91.60           C  
ANISOU 2483  CG2 VAL A 347     6236  14621  13948   -251   2354     72       C  
ATOM   2484  N   ILE A 348       6.272 -10.606  50.751  1.00 93.01           N  
ANISOU 2484  N   ILE A 348     6298  14876  14164  -1154   2157    358       N  
ATOM   2485  CA  ILE A 348       5.960 -11.616  49.742  1.00 95.52           C  
ANISOU 2485  CA  ILE A 348     6582  15196  14516  -1357   2025    420       C  
ATOM   2486  C   ILE A 348       4.652 -12.327  50.079  1.00103.43           C  
ANISOU 2486  C   ILE A 348     7365  16373  15562  -1492   2072    574       C  
ATOM   2487  O   ILE A 348       3.693 -12.296  49.299  1.00107.45           O  
ANISOU 2487  O   ILE A 348     7656  17002  16169  -1464   1995    631       O  
ATOM   2488  CB  ILE A 348       7.125 -12.607  49.579  1.00 87.46           C  
ANISOU 2488  CB  ILE A 348     5849  13922  13459  -1565   1973    436       C  
ATOM   2489  CG1 ILE A 348       8.314 -11.909  48.915  1.00 86.99           C  
ANISOU 2489  CG1 ILE A 348     5962  13655  13437  -1411   1899    340       C  
ATOM   2490  CG2 ILE A 348       6.693 -13.805  48.751  1.00 82.51           C  
ANISOU 2490  CG2 ILE A 348     5199  13305  12844  -1801   1852    517       C  
ATOM   2491  CD1 ILE A 348       9.573 -12.743  48.880  1.00 88.57           C  
ANISOU 2491  CD1 ILE A 348     6496  13548  13609  -1563   1858    366       C  
ATOM   2492  N   CYS A 349       4.591 -12.978  51.242  1.00138.03           N  
ANISOU 2492  N   CYS A 349    10685  21576  20185  -4311  -2411   -977       N  
ATOM   2493  CA  CYS A 349       3.376 -13.677  51.664  1.00144.23           C  
ANISOU 2493  CA  CYS A 349    10980  22417  21402  -4617  -2446  -1011       C  
ATOM   2494  C   CYS A 349       2.570 -12.743  52.559  1.00140.61           C  
ANISOU 2494  C   CYS A 349    10150  22064  21209  -4317  -2300   -780       C  
ATOM   2495  O   CYS A 349       2.928 -12.502  53.713  1.00143.71           O  
ANISOU 2495  O   CYS A 349    10552  22369  21683  -4159  -1884   -605       O  
ATOM   2496  CB  CYS A 349       3.697 -14.992  52.374  1.00153.89           C  
ANISOU 2496  CB  CYS A 349    12321  23335  22814  -4908  -2088  -1051       C  
ATOM   2497  SG  CYS A 349       4.990 -14.965  53.658  1.00155.83           S  
ANISOU 2497  SG  CYS A 349    12880  23369  22959  -4681  -1499   -846       S  
ATOM   2498  N   LYS A 350       1.490 -12.184  52.010  1.00138.56           N  
ANISOU 2498  N   LYS A 350     9584  21996  21068  -4223  -2642   -786       N  
ATOM   2499  CA  LYS A 350       0.596 -11.367  52.821  1.00136.19           C  
ANISOU 2499  CA  LYS A 350     8911  21773  21061  -3965  -2491   -597       C  
ATOM   2500  C   LYS A 350      -0.415 -12.218  53.578  1.00145.53           C  
ANISOU 2500  C   LYS A 350     9765  22777  22752  -4174  -2319   -606       C  
ATOM   2501  O   LYS A 350      -0.889 -11.809  54.644  1.00149.25           O  
ANISOU 2501  O   LYS A 350    10017  23212  23480  -4003  -1993   -465       O  
ATOM   2502  CB  LYS A 350      -0.126 -10.340  51.945  1.00128.18           C  
ANISOU 2502  CB  LYS A 350     7687  21053  19962  -3737  -2898   -582       C  
ATOM   2503  CG  LYS A 350       0.793  -9.516  51.056  1.00119.48           C  
ANISOU 2503  CG  LYS A 350     6902  20139  18357  -3535  -3100   -579       C  
ATOM   2504  CD  LYS A 350       1.856  -8.787  51.861  1.00113.99           C  
ANISOU 2504  CD  LYS A 350     6432  19406  17472  -3292  -2685   -412       C  
ATOM   2505  CE  LYS A 350       1.249  -7.804  52.851  1.00116.40           C  
ANISOU 2505  CE  LYS A 350     6469  19755  18003  -2990  -2407   -190       C  
ATOM   2506  NZ  LYS A 350       2.297  -7.133  53.672  1.00108.62           N  
ANISOU 2506  NZ  LYS A 350     5728  18712  16829  -2779  -2001    -53       N  
ATOM   2507  N   GLU A 351      -0.752 -13.397  53.051  1.00148.83           N  
ANISOU 2507  N   GLU A 351    10162  23074  23313  -4548  -2512   -785       N  
ATOM   2508  CA  GLU A 351      -1.692 -14.303  53.703  1.00154.92           C  
ANISOU 2508  CA  GLU A 351    10626  23651  24586  -4789  -2352   -778       C  
ATOM   2509  C   GLU A 351      -1.198 -15.736  53.817  1.00159.17           C  
ANISOU 2509  C   GLU A 351    11412  23918  25147  -5177  -2191   -843       C  
ATOM   2510  O   GLU A 351      -1.772 -16.499  54.603  1.00161.22           O  
ANISOU 2510  O   GLU A 351    11495  24007  25755  -5366  -1944   -712       O  
ATOM   2511  CB  GLU A 351      -3.041 -14.313  52.965  1.00159.23           C  
ANISOU 2511  CB  GLU A 351    10757  24334  25409  -4889  -2782   -898       C  
ATOM   2512  CG  GLU A 351      -3.820 -13.009  53.046  1.00155.69           C  
ANISOU 2512  CG  GLU A 351     9977  24159  25020  -4513  -2853   -842       C  
ATOM   2513  CD  GLU A 351      -3.339 -11.976  52.046  1.00149.56           C  
ANISOU 2513  CD  GLU A 351     9380  23657  23790  -4257  -3215   -826       C  
ATOM   2514  OE1 GLU A 351      -2.538 -12.336  51.158  1.00147.03           O  
ANISOU 2514  OE1 GLU A 351     9424  23334  23108  -4396  -3455   -938       O  
ATOM   2515  OE2 GLU A 351      -3.762 -10.805  52.147  1.00147.92           O  
ANISOU 2515  OE2 GLU A 351     8975  23667  23560  -3911  -3230   -702       O  
ATOM   2516  N   SER A 352      -0.167 -16.133  53.066  1.00159.86           N  
ANISOU 2516  N   SER A 352    11922  23973  24844  -5307  -2299  -1017       N  
ATOM   2517  CA  SER A 352       0.351 -17.492  53.178  1.00159.77           C  
ANISOU 2517  CA  SER A 352    12179  23684  24841  -5659  -2085  -1126       C  
ATOM   2518  C   SER A 352       0.980 -17.723  54.545  1.00161.73           C  
ANISOU 2518  C   SER A 352    12540  23755  25156  -5561  -1509   -913       C  
ATOM   2519  O   SER A 352       0.726 -18.746  55.193  1.00166.79           O  
ANISOU 2519  O   SER A 352    13155  24180  26038  -5791  -1224   -861       O  
ATOM   2520  CB  SER A 352       1.363 -17.764  52.064  1.00151.24           C  
ANISOU 2520  CB  SER A 352    11548  22595  23321  -5786  -2297  -1372       C  
ATOM   2521  OG  SER A 352       1.977 -19.030  52.229  1.00146.00           O  
ANISOU 2521  OG  SER A 352    11186  21629  22660  -6093  -2015  -1484       O  
ATOM   2522  N   CYS A 353       1.805 -16.785  54.998  1.00156.56           N  
ANISOU 2522  N   CYS A 353    12028  23201  24258  -5218  -1333   -781       N  
ATOM   2523  CA  CYS A 353       2.467 -16.898  56.287  1.00152.83           C  
ANISOU 2523  CA  CYS A 353    11683  22589  23795  -5081   -820   -582       C  
ATOM   2524  C   CYS A 353       1.668 -16.166  57.363  1.00141.44           C  
ANISOU 2524  C   CYS A 353     9909  21200  22632  -4826   -621   -331       C  
ATOM   2525  O   CYS A 353       0.960 -15.193  57.087  1.00130.20           O  
ANISOU 2525  O   CYS A 353     8226  19954  21290  -4636   -844   -328       O  
ATOM   2526  CB  CYS A 353       3.890 -16.337  56.201  1.00156.67           C  
ANISOU 2526  CB  CYS A 353    12537  23146  23845  -4876   -732   -580       C  
ATOM   2527  SG  CYS A 353       4.018 -14.697  55.430  1.00158.87           S  
ANISOU 2527  SG  CYS A 353    12791  23756  23816  -4539  -1090   -570       S  
ATOM   2528  N   ASN A 354       1.788 -16.651  58.598  1.00144.26           N  
ANISOU 2528  N   ASN A 354    10298  21408  23107  -4817   -179   -122       N  
ATOM   2529  CA  ASN A 354       1.057 -16.071  59.720  1.00149.60           C  
ANISOU 2529  CA  ASN A 354    10773  22153  23914  -4591     59    153       C  
ATOM   2530  C   ASN A 354       1.657 -14.722  60.100  1.00151.32           C  
ANISOU 2530  C   ASN A 354    11080  22407  24007  -4165    197     71       C  
ATOM   2531  O   ASN A 354       2.874 -14.603  60.273  1.00152.75           O  
ANISOU 2531  O   ASN A 354    11550  22590  23897  -4076    325    106       O  
ATOM   2532  CB  ASN A 354       1.083 -17.027  60.914  1.00148.92           C  
ANISOU 2532  CB  ASN A 354    10784  22087  23711  -4764    517    289       C  
ATOM   2533  CG  ASN A 354       0.250 -16.532  62.081  1.00149.15           C  
ANISOU 2533  CG  ASN A 354    10633  22355  23682  -4638    831    338       C  
ATOM   2534  OD1 ASN A 354      -0.577 -15.633  61.934  1.00151.73           O  
ANISOU 2534  OD1 ASN A 354    10715  22928  24010  -4519    706    234       O  
ATOM   2535  ND2 ASN A 354       0.464 -17.122  63.252  1.00147.32           N  
ANISOU 2535  ND2 ASN A 354    10511  21975  23488  -4638   1270    450       N  
ATOM   2536  N   GLU A 355       0.804 -13.703  60.242  1.00147.59           N  
ANISOU 2536  N   GLU A 355    10363  22125  23587  -3970    183    -48       N  
ATOM   2537  CA  GLU A 355       1.280 -12.337  60.425  1.00138.26           C  
ANISOU 2537  CA  GLU A 355     9246  21118  22170  -3640    200     43       C  
ATOM   2538  C   GLU A 355       1.288 -11.857  61.873  1.00129.59           C  
ANISOU 2538  C   GLU A 355     8217  20046  20976  -3441    658    135       C  
ATOM   2539  O   GLU A 355       1.906 -10.826  62.152  1.00125.34           O  
ANISOU 2539  O   GLU A 355     7835  19556  20235  -3166    720    251       O  
ATOM   2540  CB  GLU A 355       0.453 -11.362  59.577  1.00140.92           C  
ANISOU 2540  CB  GLU A 355     9312  21690  22539  -3517   -160     -1       C  
ATOM   2541  CG  GLU A 355       0.945 -11.242  58.145  1.00138.64           C  
ANISOU 2541  CG  GLU A 355     9152  21510  22016  -3566   -631    -51       C  
ATOM   2542  CD  GLU A 355       0.396 -10.022  57.435  1.00135.40           C  
ANISOU 2542  CD  GLU A 355     8564  21360  21523  -3335   -931    -32       C  
ATOM   2543  OE1 GLU A 355      -0.710  -9.569  57.796  1.00135.94           O  
ANISOU 2543  OE1 GLU A 355     8299  21516  21837  -3233   -879    -16       O  
ATOM   2544  OE2 GLU A 355       1.078  -9.509  56.523  1.00131.76           O  
ANISOU 2544  OE2 GLU A 355     8301  21038  20724  -3249  -1195    -41       O  
ATOM   2545  N   ASP A 356       0.641 -12.562  62.802  1.00129.03           N  
ANISOU 2545  N   ASP A 356     8077  20031  20916  -3597    954    142       N  
ATOM   2546  CA  ASP A 356       0.773 -12.190  64.209  1.00126.88           C  
ANISOU 2546  CA  ASP A 356     7914  19783  20514  -3423   1355    311       C  
ATOM   2547  C   ASP A 356       2.165 -12.535  64.725  1.00124.85           C  
ANISOU 2547  C   ASP A 356     8041  19352  20044  -3360   1562    373       C  
ATOM   2548  O   ASP A 356       2.873 -11.682  65.286  1.00123.88           O  
ANISOU 2548  O   ASP A 356     8100  19203  19766  -3098   1703    449       O  
ATOM   2549  CB  ASP A 356      -0.303 -12.887  65.044  1.00129.58           C  
ANISOU 2549  CB  ASP A 356     8045  20198  20993  -3599   1584    434       C  
ATOM   2550  CG  ASP A 356      -1.689 -12.323  64.798  1.00135.32           C  
ANISOU 2550  CG  ASP A 356     8378  21097  21942  -3580   1452    411       C  
ATOM   2551  OD1 ASP A 356      -1.799 -11.293  64.101  1.00136.35           O  
ANISOU 2551  OD1 ASP A 356     8400  21323  22083  -3397   1213    322       O  
ATOM   2552  OD2 ASP A 356      -2.669 -12.911  65.303  1.00140.52           O  
ANISOU 2552  OD2 ASP A 356     8831  21761  22798  -3728   1594    503       O  
ATOM   2553  N   VAL A 357       2.574 -13.792  64.535  1.00122.93           N  
ANISOU 2553  N   VAL A 357     7922  19016  19769  -3609   1578    373       N  
ATOM   2554  CA  VAL A 357       3.942 -14.186  64.842  1.00116.61           C  
ANISOU 2554  CA  VAL A 357     7463  18050  18794  -3546   1740    424       C  
ATOM   2555  C   VAL A 357       4.926 -13.377  64.010  1.00109.21           C  
ANISOU 2555  C   VAL A 357     6638  17028  17829  -3352   1495    435       C  
ATOM   2556  O   VAL A 357       6.025 -13.064  64.474  1.00101.78           O  
ANISOU 2556  O   VAL A 357     5966  16096  16608  -3175   1620    534       O  
ATOM   2557  CB  VAL A 357       4.121 -15.702  64.622  1.00118.63           C  
ANISOU 2557  CB  VAL A 357     7787  18244  19044  -3866   1745    556       C  
ATOM   2558  CG1 VAL A 357       5.515 -16.144  65.045  1.00112.39           C  
ANISOU 2558  CG1 VAL A 357     7326  17314  18064  -3775   1953    657       C  
ATOM   2559  CG2 VAL A 357       3.056 -16.477  65.383  1.00124.39           C  
ANISOU 2559  CG2 VAL A 357     8330  18916  20019  -4027   1979    667       C  
ATOM   2560  N   ILE A 358       4.545 -13.000  62.786  1.00113.37           N  
ANISOU 2560  N   ILE A 358     7016  17646  18413  -3406   1095    362       N  
ATOM   2561  CA  ILE A 358       5.430 -12.192  61.951  1.00 97.36           C  
ANISOU 2561  CA  ILE A 358     5179  15772  16040  -3275    830    349       C  
ATOM   2562  C   ILE A 358       5.617 -10.800  62.546  1.00104.91           C  
ANISOU 2562  C   ILE A 358     6193  16841  16825  -2948    942    432       C  
ATOM   2563  O   ILE A 358       6.724 -10.253  62.531  1.00102.95           O  
ANISOU 2563  O   ILE A 358     6206  16656  16257  -2801    955    456       O  
ATOM   2564  CB  ILE A 358       4.905 -12.133  60.504  1.00 99.45           C  
ANISOU 2564  CB  ILE A 358     5291  16154  16342  -3421    382    212       C  
ATOM   2565  CG1 ILE A 358       5.647 -13.151  59.635  1.00 99.23           C  
ANISOU 2565  CG1 ILE A 358     5468  16072  16164  -3688    229     85       C  
ATOM   2566  CG2 ILE A 358       5.039 -10.731  59.918  1.00 97.94           C  
ANISOU 2566  CG2 ILE A 358     5112  16177  15924  -3175    166    214       C  
ATOM   2567  CD1 ILE A 358       5.381 -12.997  58.162  1.00100.85           C  
ANISOU 2567  CD1 ILE A 358     5622  16415  16281  -3812   -228    -86       C  
ATOM   2568  N   GLY A 359       4.549 -10.204  63.078  1.00 97.04           N  
ANISOU 2568  N   GLY A 359     4965  15878  16030  -2845   1042    454       N  
ATOM   2569  CA  GLY A 359       4.691  -8.911  63.728  1.00 95.24           C  
ANISOU 2569  CA  GLY A 359     4815  15732  15640  -2558   1192    536       C  
ATOM   2570  C   GLY A 359       5.544  -8.985  64.979  1.00 94.80           C  
ANISOU 2570  C   GLY A 359     5029  15587  15403  -2456   1543    616       C  
ATOM   2571  O   GLY A 359       6.378  -8.105  65.232  1.00 91.43           O  
ANISOU 2571  O   GLY A 359     4817  15214  14708  -2263   1595    659       O  
ATOM   2572  N   ALA A 360       5.352 -10.039  65.779  1.00 95.50           N  
ANISOU 2572  N   ALA A 360     5113  15559  15612  -2591   1789    625       N  
ATOM   2573  CA  ALA A 360       6.213 -10.234  66.944  1.00 92.27           C  
ANISOU 2573  CA  ALA A 360     4970  15090  14997  -2495   2096    712       C  
ATOM   2574  C   ALA A 360       7.674 -10.390  66.529  1.00 96.18           C  
ANISOU 2574  C   ALA A 360     5739  15586  15220  -2462   1994    731       C  
ATOM   2575  O   ALA A 360       8.575  -9.794  67.140  1.00101.44           O  
ANISOU 2575  O   ALA A 360     6629  16299  15615  -2282   2103    779       O  
ATOM   2576  CB  ALA A 360       5.746 -11.450  67.744  1.00 94.59           C  
ANISOU 2576  CB  ALA A 360     5221  15312  15406  -2668   2360    732       C  
ATOM   2577  N   LEU A 361       7.923 -11.188  65.486  1.00 95.72           N  
ANISOU 2577  N   LEU A 361     5665  15503  15201  -2652   1780    673       N  
ATOM   2578  CA  LEU A 361       9.276 -11.361  64.970  1.00 95.39           C  
ANISOU 2578  CA  LEU A 361     5875  15505  14863  -2650   1678    651       C  
ATOM   2579  C   LEU A 361       9.858 -10.038  64.498  1.00 96.37           C  
ANISOU 2579  C   LEU A 361     6106  15778  14732  -2465   1511    604       C  
ATOM   2580  O   LEU A 361      11.036  -9.757  64.732  1.00107.72           O  
ANISOU 2580  O   LEU A 361     7778  17259  15890  -2352   1571    607       O  
ATOM   2581  CB  LEU A 361       9.283 -12.377  63.827  1.00 98.73           C  
ANISOU 2581  CB  LEU A 361     6261  15886  15365  -2922   1471    558       C  
ATOM   2582  CG  LEU A 361       9.002 -13.848  64.141  1.00102.54           C  
ANISOU 2582  CG  LEU A 361     6703  16196  16062  -3153   1656    592       C  
ATOM   2583  CD1 LEU A 361       9.127 -14.695  62.882  1.00103.23           C  
ANISOU 2583  CD1 LEU A 361     6811  16248  16164  -3443   1427    449       C  
ATOM   2584  CD2 LEU A 361       9.923 -14.362  65.232  1.00103.65           C  
ANISOU 2584  CD2 LEU A 361     7062  16278  16041  -3049   1992    722       C  
ATOM   2585  N   LEU A 362       9.055  -9.218  63.817  1.00 93.39           N  
ANISOU 2585  N   LEU A 362     5551  15483  14449  -2432   1311    559       N  
ATOM   2586  CA  LEU A 362       9.563  -7.946  63.317  1.00 83.39           C  
ANISOU 2586  CA  LEU A 362     4383  14353  12949  -2259   1187    520       C  
ATOM   2587  C   LEU A 362       9.928  -7.011  64.461  1.00102.86           C  
ANISOU 2587  C   LEU A 362     6981  16823  15276  -2039   1440    588       C  
ATOM   2588  O   LEU A 362      10.959  -6.336  64.404  1.00104.66           O  
ANISOU 2588  O   LEU A 362     7416  17113  15236  -1928   1446    551       O  
ATOM   2589  CB  LEU A 362       8.542  -7.292  62.385  1.00 85.28           C  
ANISOU 2589  CB  LEU A 362     4381  14698  13323  -2250    938    487       C  
ATOM   2590  CG  LEU A 362       8.598  -7.724  60.918  1.00 86.02           C  
ANISOU 2590  CG  LEU A 362     4437  14870  13376  -2419    591    372       C  
ATOM   2591  CD1 LEU A 362       7.576  -6.960  60.089  1.00 88.18           C  
ANISOU 2591  CD1 LEU A 362     4464  15290  13752  -2360    335    360       C  
ATOM   2592  CD2 LEU A 362       9.997  -7.525  60.357  1.00 83.10           C  
ANISOU 2592  CD2 LEU A 362     4347  14557  12672  -2390    542    295       C  
ATOM   2593  N   ASN A 363       9.108  -6.967  65.513  1.00 83.39           N  
ANISOU 2593  N   ASN A 363     4408  14292  12986  -1991   1662    667       N  
ATOM   2594  CA  ASN A 363       9.476  -6.203  66.705  1.00 94.16           C  
ANISOU 2594  CA  ASN A 363     5928  15656  14194  -1815   1919    719       C  
ATOM   2595  C   ASN A 363      10.818  -6.674  67.264  1.00 90.76           C  
ANISOU 2595  C   ASN A 363     5762  15216  13505  -1801   2018    723       C  
ATOM   2596  O   ASN A 363      11.765  -5.882  67.425  1.00104.56           O  
ANISOU 2596  O   ASN A 363     7703  17034  14992  -1684   2032    685       O  
ATOM   2597  CB  ASN A 363       8.379  -6.324  67.766  1.00103.74           C  
ANISOU 2597  CB  ASN A 363     6995  16795  15625  -1802   2167    788       C  
ATOM   2598  CG  ASN A 363       7.073  -5.695  67.333  1.00113.34           C  
ANISOU 2598  CG  ASN A 363     7937  18051  17076  -1780   2092    782       C  
ATOM   2599  OD1 ASN A 363       7.061  -4.709  66.602  1.00119.52           O  
ANISOU 2599  OD1 ASN A 363     8690  18929  17793  -1680   1938    763       O  
ATOM   2600  ND2 ASN A 363       5.962  -6.262  67.788  1.00115.81           N  
ANISOU 2600  ND2 ASN A 363     8041  18316  17646  -1870   2212    797       N  
ATOM   2601  N   VAL A 364      10.909  -7.974  67.567  1.00 81.28           N  
ANISOU 2601  N   VAL A 364     4564  13936  12382  -1923   2098    767       N  
ATOM   2602  CA  VAL A 364      12.119  -8.522  68.178  1.00 79.52           C  
ANISOU 2602  CA  VAL A 364     4564  13725  11926  -1890   2211    800       C  
ATOM   2603  C   VAL A 364      13.339  -8.246  67.305  1.00 77.16           C  
ANISOU 2603  C   VAL A 364     4421  13508  11389  -1877   2018    707       C  
ATOM   2604  O   VAL A 364      14.408  -7.873  67.803  1.00 82.07           O  
ANISOU 2604  O   VAL A 364     5227  14199  11757  -1767   2074    694       O  
ATOM   2605  CB  VAL A 364      11.942 -10.028  68.449  1.00 81.12           C  
ANISOU 2605  CB  VAL A 364     4724  13823  12273  -2033   2339    876       C  
ATOM   2606  CG1 VAL A 364      13.234 -10.631  68.973  1.00 92.81           C  
ANISOU 2606  CG1 VAL A 364     6421  15342  13502  -1977   2444    932       C  
ATOM   2607  CG2 VAL A 364      10.806 -10.257  69.433  1.00 83.57           C  
ANISOU 2607  CG2 VAL A 364     4904  14050  12799  -2039   2584    952       C  
ATOM   2608  N   PHE A 365      13.193  -8.397  65.990  1.00 77.19           N  
ANISOU 2608  N   PHE A 365     4347  13515  11466  -1994   1788    627       N  
ATOM   2609  CA  PHE A 365      14.335  -8.296  65.091  1.00 88.65           C  
ANISOU 2609  CA  PHE A 365     5949  15026  12709  -2005   1636    533       C  
ATOM   2610  C   PHE A 365      14.736  -6.848  64.847  1.00 87.14           C  
ANISOU 2610  C   PHE A 365     5838  14924  12347  -1858   1577    455       C  
ATOM   2611  O   PHE A 365      15.929  -6.562  64.689  1.00 86.05           O  
ANISOU 2611  O   PHE A 365     5873  14830  11994  -1805   1566    392       O  
ATOM   2612  CB  PHE A 365      14.018  -9.006  63.773  1.00 91.57           C  
ANISOU 2612  CB  PHE A 365     6224  15375  13194  -2203   1426    464       C  
ATOM   2613  CG  PHE A 365      13.766 -10.487  63.924  1.00 77.82           C  
ANISOU 2613  CG  PHE A 365     4432  13526  11611  -2388   1508    519       C  
ATOM   2614  CD1 PHE A 365      14.061 -11.143  65.110  1.00 78.03           C  
ANISOU 2614  CD1 PHE A 365     4527  13496  11626  -2339   1768    639       C  
ATOM   2615  CD2 PHE A 365      13.212 -11.217  62.885  1.00 79.47           C  
ANISOU 2615  CD2 PHE A 365     4570  13654  11973  -2598   1328    441       C  
ATOM   2616  CE1 PHE A 365      13.822 -12.496  65.253  1.00 79.76           C  
ANISOU 2616  CE1 PHE A 365     4708  13603  11994  -2507   1892    704       C  
ATOM   2617  CE2 PHE A 365      12.972 -12.573  63.023  1.00 81.25           C  
ANISOU 2617  CE2 PHE A 365     4800  13715  12356  -2772   1430    473       C  
ATOM   2618  CZ  PHE A 365      13.277 -13.212  64.208  1.00 81.35           C  
ANISOU 2618  CZ  PHE A 365     4860  13680  12370  -2725   1731    612       C  
ATOM   2619  N   VAL A 366      13.769  -5.925  64.817  1.00 82.13           N  
ANISOU 2619  N   VAL A 366     5074  14314  11819  -1791   1561    463       N  
ATOM   2620  CA  VAL A 366      14.099  -4.504  64.821  1.00 78.03           C  
ANISOU 2620  CA  VAL A 366     4640  13865  11144  -1642   1589    411       C  
ATOM   2621  C   VAL A 366      14.949  -4.171  66.036  1.00 72.26           C  
ANISOU 2621  C   VAL A 366     4092  13136  10226  -1544   1784    418       C  
ATOM   2622  O   VAL A 366      15.952  -3.451  65.936  1.00 70.69           O  
ANISOU 2622  O   VAL A 366     4052  12985   9823  -1483   1787    329       O  
ATOM   2623  CB  VAL A 366      12.814  -3.654  64.779  1.00 79.71           C  
ANISOU 2623  CB  VAL A 366     4664  14100  11523  -1569   1600    456       C  
ATOM   2624  CG1 VAL A 366      13.096  -2.235  65.246  1.00 75.92           C  
ANISOU 2624  CG1 VAL A 366     4294  13659  10892  -1407   1748    432       C  
ATOM   2625  CG2 VAL A 366      12.234  -3.630  63.380  1.00 84.57           C  
ANISOU 2625  CG2 VAL A 366     5113  14785  12234  -1629   1348    420       C  
ATOM   2626  N   TRP A 367      14.584  -4.711  67.201  1.00 73.31           N  
ANISOU 2626  N   TRP A 367     4204  13230  10423  -1539   1953    515       N  
ATOM   2627  CA  TRP A 367      15.363  -4.364  68.388  1.00 75.67           C  
ANISOU 2627  CA  TRP A 367     4666  13577  10511  -1448   2116    518       C  
ATOM   2628  C   TRP A 367      16.718  -5.069  68.418  1.00 73.83           C  
ANISOU 2628  C   TRP A 367     4572  13389  10089  -1470   2071    490       C  
ATOM   2629  O   TRP A 367      17.683  -4.517  68.958  1.00 73.87           O  
ANISOU 2629  O   TRP A 367     4714  13480   9874  -1402   2110    433       O  
ATOM   2630  CB  TRP A 367      14.542  -4.622  69.649  1.00 84.12           C  
ANISOU 2630  CB  TRP A 367     5676  14614  11673  -1415   2334    635       C  
ATOM   2631  CG  TRP A 367      13.536  -3.528  69.817  1.00 92.68           C  
ANISOU 2631  CG  TRP A 367     6674  15677  12864  -1344   2427    642       C  
ATOM   2632  CD1 TRP A 367      12.178  -3.634  69.758  1.00101.92           C  
ANISOU 2632  CD1 TRP A 367     7640  16774  14312  -1364   2477    712       C  
ATOM   2633  CD2 TRP A 367      13.823  -2.137  70.016  1.00 89.81           C  
ANISOU 2633  CD2 TRP A 367     6417  15364  12343  -1244   2493    571       C  
ATOM   2634  NE1 TRP A 367      11.600  -2.397  69.929  1.00103.06           N  
ANISOU 2634  NE1 TRP A 367     7755  16928  14475  -1261   2577    706       N  
ATOM   2635  CE2 TRP A 367      12.590  -1.462  70.089  1.00 95.24           C  
ANISOU 2635  CE2 TRP A 367     6965  16003  13216  -1188   2602    623       C  
ATOM   2636  CE3 TRP A 367      15.004  -1.401  70.154  1.00 82.66           C  
ANISOU 2636  CE3 TRP A 367     5702  14536  11168  -1205   2487    461       C  
ATOM   2637  CZ2 TRP A 367      12.504  -0.086  70.291  1.00 90.77           C  
ANISOU 2637  CZ2 TRP A 367     6468  15456  12565  -1084   2728    582       C  
ATOM   2638  CZ3 TRP A 367      14.917  -0.037  70.354  1.00 80.18           C  
ANISOU 2638  CZ3 TRP A 367     5457  14235  10775  -1126   2604    401       C  
ATOM   2639  CH2 TRP A 367      13.677   0.607  70.414  1.00 84.54           C  
ANISOU 2639  CH2 TRP A 367     5889  14727  11505  -1060   2734    469       C  
ATOM   2640  N   ILE A 368      16.830  -6.254  67.817  1.00 71.60           N  
ANISOU 2640  N   ILE A 368     4250  13062   9894  -1570   1992    524       N  
ATOM   2641  CA  ILE A 368      18.147  -6.878  67.659  1.00 72.65           C  
ANISOU 2641  CA  ILE A 368     4503  13237   9864  -1578   1953    504       C  
ATOM   2642  C   ILE A 368      19.038  -6.018  66.762  1.00 68.83           C  
ANISOU 2642  C   ILE A 368     4113  12789   9249  -1557   1824    361       C  
ATOM   2643  O   ILE A 368      20.217  -5.768  67.064  1.00 67.90           O  
ANISOU 2643  O   ILE A 368     4111  12743   8944  -1499   1835    311       O  
ATOM   2644  CB  ILE A 368      18.004  -8.308  67.107  1.00 71.29           C  
ANISOU 2644  CB  ILE A 368     4271  12989   9828  -1705   1931    572       C  
ATOM   2645  CG1 ILE A 368      17.215  -9.186  68.081  1.00 73.18           C  
ANISOU 2645  CG1 ILE A 368     4431  13176  10199  -1726   2113    718       C  
ATOM   2646  CG2 ILE A 368      19.371  -8.915  66.827  1.00 70.30           C  
ANISOU 2646  CG2 ILE A 368     4262  12903   9545  -1699   1911    565       C  
ATOM   2647  CD1 ILE A 368      16.927 -10.576  67.555  1.00 74.37           C  
ANISOU 2647  CD1 ILE A 368     4514  13225  10518  -1884   2130    780       C  
ATOM   2648  N   GLY A 369      18.488  -5.566  65.634  1.00 73.29           N  
ANISOU 2648  N   GLY A 369     4617  13317   9913  -1605   1702    295       N  
ATOM   2649  CA  GLY A 369      19.242  -4.690  64.752  1.00 67.32           C  
ANISOU 2649  CA  GLY A 369     3951  12588   9039  -1578   1622    165       C  
ATOM   2650  C   GLY A 369      19.654  -3.397  65.428  1.00 68.33           C  
ANISOU 2650  C   GLY A 369     4172  12763   9028  -1471   1717     96       C  
ATOM   2651  O   GLY A 369      20.729  -2.857  65.155  1.00 70.84           O  
ANISOU 2651  O   GLY A 369     4605  13102   9209  -1448   1712    -10       O  
ATOM   2652  N   TYR A 370      18.798  -2.871  66.307  1.00 67.66           N  
ANISOU 2652  N   TYR A 370     4035  12686   8987  -1419   1825    149       N  
ATOM   2653  CA  TYR A 370      19.177  -1.692  67.080  1.00 72.72           C  
ANISOU 2653  CA  TYR A 370     4774  13374   9482  -1343   1945     78       C  
ATOM   2654  C   TYR A 370      20.278  -2.017  68.085  1.00 67.26           C  
ANISOU 2654  C   TYR A 370     4179  12770   8607  -1335   1990     61       C  
ATOM   2655  O   TYR A 370      21.151  -1.181  68.347  1.00 66.79           O  
ANISOU 2655  O   TYR A 370     4219  12770   8389  -1318   2019    -58       O  
ATOM   2656  CB  TYR A 370      17.951  -1.107  67.781  1.00 75.36           C  
ANISOU 2656  CB  TYR A 370     5030  13693   9910  -1289   2080    149       C  
ATOM   2657  CG  TYR A 370      17.054  -0.293  66.872  1.00 79.75           C  
ANISOU 2657  CG  TYR A 370     5493  14215  10594  -1255   2057    141       C  
ATOM   2658  CD1 TYR A 370      17.562   0.338  65.744  1.00 82.31           C  
ANISOU 2658  CD1 TYR A 370     5867  14547  10858  -1248   1978     35       C  
ATOM   2659  CD2 TYR A 370      15.700  -0.154  67.143  1.00 79.36           C  
ANISOU 2659  CD2 TYR A 370     5290  14139  10726  -1217   2131    248       C  
ATOM   2660  CE1 TYR A 370      16.744   1.084  64.913  1.00 82.77           C  
ANISOU 2660  CE1 TYR A 370     5825  14617  11006  -1191   1965     44       C  
ATOM   2661  CE2 TYR A 370      14.877   0.591  66.323  1.00 78.35           C  
ANISOU 2661  CE2 TYR A 370     5043  14018  10709  -1162   2104    259       C  
ATOM   2662  CZ  TYR A 370      15.401   1.206  65.209  1.00 80.64           C  
ANISOU 2662  CZ  TYR A 370     5384  14346  10909  -1142   2016    162       C  
ATOM   2663  OH  TYR A 370      14.580   1.946  64.389  1.00 80.58           O  
ANISOU 2663  OH  TYR A 370     5242  14387  10988  -1059   1993    191       O  
ATOM   2664  N   LEU A 371      20.249  -3.223  68.663  1.00 70.61           N  
ANISOU 2664  N   LEU A 371     4561  13219   9050  -1349   2003    179       N  
ATOM   2665  CA  LEU A 371      21.319  -3.653  69.561  1.00 75.49           C  
ANISOU 2665  CA  LEU A 371     5238  13970   9477  -1321   2031    189       C  
ATOM   2666  C   LEU A 371      22.658  -3.717  68.837  1.00 76.93           C  
ANISOU 2666  C   LEU A 371     5479  14178   9573  -1338   1918     93       C  
ATOM   2667  O   LEU A 371      23.719  -3.527  69.455  1.00 81.48           O  
ANISOU 2667  O   LEU A 371     6094  14896   9971  -1312   1917     37       O  
ATOM   2668  CB  LEU A 371      20.975  -5.018  70.160  1.00 69.17           C  
ANISOU 2668  CB  LEU A 371     4375  13179   8726  -1317   2095    361       C  
ATOM   2669  CG  LEU A 371      21.996  -5.668  71.096  1.00 69.76           C  
ANISOU 2669  CG  LEU A 371     4481  13426   8596  -1259   2132    422       C  
ATOM   2670  CD1 LEU A 371      22.067  -4.922  72.419  1.00 70.76           C  
ANISOU 2670  CD1 LEU A 371     4644  13725   8518  -1199   2234    398       C  
ATOM   2671  CD2 LEU A 371      21.674  -7.140  71.314  1.00 70.79           C  
ANISOU 2671  CD2 LEU A 371     4563  13520   8815  -1255   2212    608       C  
ATOM   2672  N   SER A 372      22.624  -4.021  67.538  1.00 76.24           N  
ANISOU 2672  N   SER A 372     5383  13974   9609  -1386   1828     75       N  
ATOM   2673  CA  SER A 372      23.853  -4.018  66.746  1.00 65.08           C  
ANISOU 2673  CA  SER A 372     4032  12558   8137  -1397   1757    -15       C  
ATOM   2674  C   SER A 372      24.592  -2.689  66.873  1.00 72.94           C  
ANISOU 2674  C   SER A 372     5101  13598   9013  -1380   1776   -177       C  
ATOM   2675  O   SER A 372      25.829  -2.656  66.895  1.00 80.71           O  
ANISOU 2675  O   SER A 372     6117  14644   9907  -1376   1752   -246       O  
ATOM   2676  CB  SER A 372      23.540  -4.313  65.279  1.00 64.48           C  
ANISOU 2676  CB  SER A 372     3948  12361   8192  -1459   1683    -31       C  
ATOM   2677  OG  SER A 372      22.955  -3.187  64.647  1.00 64.16           O  
ANISOU 2677  OG  SER A 372     3916  12275   8187  -1459   1674   -123       O  
ATOM   2678  N   SER A 373      23.849  -1.581  66.951  1.00 64.74           N  
ANISOU 2678  N   SER A 373     4081  12527   7989  -1373   1835   -239       N  
ATOM   2679  CA  SER A 373      24.474  -0.264  67.057  1.00 69.48           C  
ANISOU 2679  CA  SER A 373     4763  13148   8489  -1376   1893   -404       C  
ATOM   2680  C   SER A 373      25.223  -0.088  68.374  1.00 75.64           C  
ANISOU 2680  C   SER A 373     5547  14103   9092  -1383   1926   -454       C  
ATOM   2681  O   SER A 373      26.237   0.618  68.418  1.00 81.59           O  
ANISOU 2681  O   SER A 373     6341  14907   9753  -1421   1931   -608       O  
ATOM   2682  CB  SER A 373      23.418   0.831  66.903  1.00 75.38           C  
ANISOU 2682  CB  SER A 373     5527  13823   9292  -1352   1990   -432       C  
ATOM   2683  OG  SER A 373      22.720   0.701  65.676  1.00 80.69           O  
ANISOU 2683  OG  SER A 373     6158  14398  10103  -1344   1940   -390       O  
ATOM   2684  N   ALA A 374      24.743  -0.711  69.451  1.00 66.44           N  
ANISOU 2684  N   ALA A 374     4326  13047   7871  -1355   1955   -336       N  
ATOM   2685  CA  ALA A 374      25.443  -0.673  70.730  1.00 70.40           C  
ANISOU 2685  CA  ALA A 374     4809  13780   8160  -1356   1975   -373       C  
ATOM   2686  C   ALA A 374      26.586  -1.673  70.816  1.00 74.75           C  
ANISOU 2686  C   ALA A 374     5295  14470   8638  -1337   1872   -324       C  
ATOM   2687  O   ALA A 374      27.486  -1.493  71.643  1.00 79.33           O  
ANISOU 2687  O   ALA A 374     5829  15286   9026  -1347   1848   -398       O  
ATOM   2688  CB  ALA A 374      24.466  -0.936  71.876  1.00 68.92           C  
ANISOU 2688  CB  ALA A 374     4597  13671   7917  -1313   2085   -249       C  
ATOM   2689  N   VAL A 375      26.554  -2.730  70.004  1.00 78.78           N  
ANISOU 2689  N   VAL A 375     5785  14860   9288  -1311   1820   -202       N  
ATOM   2690  CA  VAL A 375      27.568  -3.780  70.116  1.00 67.50           C  
ANISOU 2690  CA  VAL A 375     4292  13553   7802  -1265   1760   -115       C  
ATOM   2691  C   VAL A 375      28.968  -3.250  69.801  1.00 67.40           C  
ANISOU 2691  C   VAL A 375     4264  13615   7731  -1291   1688   -266       C  
ATOM   2692  O   VAL A 375      29.948  -3.637  70.449  1.00 79.57           O  
ANISOU 2692  O   VAL A 375     5709  15386   9139  -1249   1640   -244       O  
ATOM   2693  CB  VAL A 375      27.193  -4.973  69.217  1.00 68.88           C  
ANISOU 2693  CB  VAL A 375     4467  13554   8151  -1251   1757     33       C  
ATOM   2694  CG1 VAL A 375      28.391  -5.882  68.995  1.00 67.13           C  
ANISOU 2694  CG1 VAL A 375     4200  13404   7901  -1199   1721    103       C  
ATOM   2695  CG2 VAL A 375      26.047  -5.755  69.837  1.00 75.23           C  
ANISOU 2695  CG2 VAL A 375     5242  14345   8997  -1228   1841    203       C  
ATOM   2696  N   ASN A 376      29.083  -2.348  68.821  1.00 73.49           N  
ANISOU 2696  N   ASN A 376     5111  14210   8602  -1352   1692   -415       N  
ATOM   2697  CA  ASN A 376      30.385  -1.941  68.281  1.00 81.69           C  
ANISOU 2697  CA  ASN A 376     6139  15249   9649  -1383   1656   -547       C  
ATOM   2698  C   ASN A 376      31.423  -1.524  69.322  1.00 74.99           C  
ANISOU 2698  C   ASN A 376     5184  14681   8627  -1411   1611   -658       C  
ATOM   2699  O   ASN A 376      32.562  -2.018  69.248  1.00 69.59           O  
ANISOU 2699  O   ASN A 376     4402  14101   7939  -1382   1547   -641       O  
ATOM   2700  CB  ASN A 376      30.178  -0.820  67.252  1.00 87.27           C  
ANISOU 2700  CB  ASN A 376     6960  15737  10461  -1443   1718   -697       C  
ATOM   2701  CG  ASN A 376      30.240  -1.323  65.823  1.00 87.85           C  
ANISOU 2701  CG  ASN A 376     7087  15603  10688  -1424   1723   -648       C  
ATOM   2702  OD1 ASN A 376      30.904  -2.317  65.529  1.00 75.36           O  
ANISOU 2702  OD1 ASN A 376     5459  14033   9142  -1387   1690   -556       O  
ATOM   2703  ND2 ASN A 376      29.552  -0.631  64.923  1.00 96.01           N  
ANISOU 2703  ND2 ASN A 376     8214  16467  11799  -1444   1780   -706       N  
ATOM   2704  N   PRO A 377      31.137  -0.628  70.276  1.00 73.12           N  
ANISOU 2704  N   PRO A 377     4945  14595   8242  -1473   1644   -778       N  
ATOM   2705  CA  PRO A 377      32.195  -0.227  71.220  1.00 70.72           C  
ANISOU 2705  CA  PRO A 377     4511  14610   7752  -1532   1583   -919       C  
ATOM   2706  C   PRO A 377      32.719  -1.375  72.061  1.00 72.19           C  
ANISOU 2706  C   PRO A 377     4533  15105   7793  -1430   1487   -757       C  
ATOM   2707  O   PRO A 377      33.910  -1.394  72.399  1.00 73.73           O  
ANISOU 2707  O   PRO A 377     4569  15544   7900  -1442   1387   -827       O  
ATOM   2708  CB  PRO A 377      31.506   0.837  72.084  1.00 71.55           C  
ANISOU 2708  CB  PRO A 377     4671  14807   7709  -1619   1675  -1060       C  
ATOM   2709  CG  PRO A 377      30.391   1.335  71.238  1.00 69.82           C  
ANISOU 2709  CG  PRO A 377     4622  14243   7665  -1612   1789  -1041       C  
ATOM   2710  CD  PRO A 377      29.902   0.142  70.499  1.00 68.48           C  
ANISOU 2710  CD  PRO A 377     4462  13906   7650  -1502   1749   -813       C  
ATOM   2711  N   LEU A 378      31.862  -2.336  72.411  1.00 76.34           N  
ANISOU 2711  N   LEU A 378     5078  15632   8295  -1321   1524   -533       N  
ATOM   2712  CA  LEU A 378      32.337  -3.537  73.089  1.00 74.29           C  
ANISOU 2712  CA  LEU A 378     4680  15637   7910  -1186   1471   -332       C  
ATOM   2713  C   LEU A 378      33.368  -4.270  72.240  1.00 75.81           C  
ANISOU 2713  C   LEU A 378     4805  15756   8243  -1120   1405   -257       C  
ATOM   2714  O   LEU A 378      34.398  -4.726  72.752  1.00 79.10           O  
ANISOU 2714  O   LEU A 378     5046  16463   8543  -1037   1317   -201       O  
ATOM   2715  CB  LEU A 378      31.154  -4.449  73.414  1.00 73.25           C  
ANISOU 2715  CB  LEU A 378     4618  15427   7787  -1089   1576    -98       C  
ATOM   2716  CG  LEU A 378      31.460  -5.854  73.930  1.00 74.59           C  
ANISOU 2716  CG  LEU A 378     4691  15782   7867   -916   1586    167       C  
ATOM   2717  CD1 LEU A 378      32.078  -5.796  75.318  1.00 77.35           C  
ANISOU 2717  CD1 LEU A 378     4987  16499   7902   -822   1495    175       C  
ATOM   2718  CD2 LEU A 378      30.201  -6.707  73.932  1.00 74.11           C  
ANISOU 2718  CD2 LEU A 378     4736  15516   7906   -862   1731    374       C  
ATOM   2719  N   VAL A 379      33.112  -4.381  70.933  1.00 71.21           N  
ANISOU 2719  N   VAL A 379     4348  14806   7902  -1146   1455   -250       N  
ATOM   2720  CA  VAL A 379      34.059  -5.033  70.033  1.00 70.96           C  
ANISOU 2720  CA  VAL A 379     4277  14673   8012  -1089   1439   -184       C  
ATOM   2721  C   VAL A 379      35.366  -4.254  69.972  1.00 71.92           C  
ANISOU 2721  C   VAL A 379     4289  14909   8129  -1147   1363   -369       C  
ATOM   2722  O   VAL A 379      36.455  -4.841  69.950  1.00 73.13           O  
ANISOU 2722  O   VAL A 379     4300  15189   8299  -1061   1315   -293       O  
ATOM   2723  CB  VAL A 379      33.438  -5.203  68.636  1.00 72.49           C  
ANISOU 2723  CB  VAL A 379     4634  14482   8428  -1125   1521   -167       C  
ATOM   2724  CG1 VAL A 379      34.354  -6.032  67.746  1.00 68.82           C  
ANISOU 2724  CG1 VAL A 379     4137  13921   8091  -1055   1549    -72       C  
ATOM   2725  CG2 VAL A 379      32.066  -5.836  68.747  1.00 71.01           C  
ANISOU 2725  CG2 VAL A 379     4525  14194   8260  -1108   1583    -23       C  
ATOM   2726  N   TYR A 380      35.281  -2.920  69.930  1.00 71.64           N  
ANISOU 2726  N   TYR A 380     4311  14820   8088  -1293   1372   -610       N  
ATOM   2727  CA  TYR A 380      36.497  -2.111  69.974  1.00 72.97           C  
ANISOU 2727  CA  TYR A 380     4364  15104   8257  -1381   1317   -812       C  
ATOM   2728  C   TYR A 380      37.281  -2.385  71.250  1.00 94.44           C  
ANISOU 2728  C   TYR A 380     6843  18281  10760  -1343   1176   -800       C  
ATOM   2729  O   TYR A 380      38.516  -2.438  71.234  1.00 77.32           O  
ANISOU 2729  O   TYR A 380     4501  16252   8625  -1333   1092   -841       O  
ATOM   2730  CB  TYR A 380      36.162  -0.623  69.870  1.00 72.55           C  
ANISOU 2730  CB  TYR A 380     4422  14936   8208  -1551   1387  -1072       C  
ATOM   2731  CG  TYR A 380      35.486  -0.211  68.583  1.00 70.26           C  
ANISOU 2731  CG  TYR A 380     4347  14239   8111  -1571   1518  -1089       C  
ATOM   2732  CD1 TYR A 380      35.460  -1.055  67.480  1.00 68.88           C  
ANISOU 2732  CD1 TYR A 380     4236  13834   8102  -1478   1554   -933       C  
ATOM   2733  CD2 TYR A 380      34.878   1.031  68.470  1.00 69.76           C  
ANISOU 2733  CD2 TYR A 380     4415  14046   8046  -1677   1616  -1263       C  
ATOM   2734  CE1 TYR A 380      34.839  -0.676  66.306  1.00 67.14           C  
ANISOU 2734  CE1 TYR A 380     4190  13301   8018  -1495   1660   -957       C  
ATOM   2735  CE2 TYR A 380      34.257   1.419  67.301  1.00 77.98           C  
ANISOU 2735  CE2 TYR A 380     5632  14760   9238  -1669   1729  -1264       C  
ATOM   2736  CZ  TYR A 380      34.241   0.563  66.222  1.00 75.25           C  
ANISOU 2736  CZ  TYR A 380     5332  14227   9033  -1580   1739  -1115       C  
ATOM   2737  OH  TYR A 380      33.622   0.949  65.057  1.00 76.39           O  
ANISOU 2737  OH  TYR A 380     5632  14103   9290  -1574   1841  -1125       O  
ATOM   2738  N   THR A 381      36.575  -2.561  72.368  1.00 86.64           N  
ANISOU 2738  N   THR A 381     5827  17549   9542  -1311   1151   -738       N  
ATOM   2739  CA  THR A 381      37.247  -2.832  73.633  1.00 87.04           C  
ANISOU 2739  CA  THR A 381     5637  18100   9333  -1254   1009   -717       C  
ATOM   2740  C   THR A 381      37.920  -4.199  73.613  1.00 88.71           C  
ANISOU 2740  C   THR A 381     5708  18435   9564  -1033    948   -440       C  
ATOM   2741  O   THR A 381      39.021  -4.364  74.151  1.00 89.19           O  
ANISOU 2741  O   THR A 381     5531  18836   9521   -972    796   -439       O  
ATOM   2742  CB  THR A 381      36.248  -2.753  74.787  1.00 92.43           C  
ANISOU 2742  CB  THR A 381     6343  19022   9754  -1247   1047   -687       C  
ATOM   2743  OG1 THR A 381      35.457  -1.567  74.657  1.00 93.40           O  
ANISOU 2743  OG1 THR A 381     6640  18948   9902  -1425   1158   -903       O  
ATOM   2744  CG2 THR A 381      36.976  -2.722  76.123  1.00 96.34           C  
ANISOU 2744  CG2 THR A 381     6716  19953   9936  -1198    853   -728       C  
ATOM   2745  N   LEU A 382      37.271  -5.189  72.996  1.00 93.45           N  
ANISOU 2745  N   LEU A 382     6444  18766  10296   -910   1069   -202       N  
ATOM   2746  CA  LEU A 382      37.764  -6.562  73.064  1.00 79.78           C  
ANISOU 2746  CA  LEU A 382     4602  17147   8562   -681   1068     92       C  
ATOM   2747  C   LEU A 382      39.068  -6.733  72.291  1.00 80.36           C  
ANISOU 2747  C   LEU A 382     4562  17152   8820   -642   1024     86       C  
ATOM   2748  O   LEU A 382      40.050  -7.263  72.824  1.00 90.27           O  
ANISOU 2748  O   LEU A 382     5592  18721   9986   -488    918    206       O  
ATOM   2749  CB  LEU A 382      36.701  -7.528  72.538  1.00 77.93           C  
ANISOU 2749  CB  LEU A 382     4560  16607   8443   -601   1241    313       C  
ATOM   2750  CG  LEU A 382      35.414  -7.652  73.354  1.00 77.81           C  
ANISOU 2750  CG  LEU A 382     4700  16583   8281   -586   1304    391       C  
ATOM   2751  CD1 LEU A 382      34.414  -8.564  72.655  1.00 76.14           C  
ANISOU 2751  CD1 LEU A 382     4667  16016   8247   -554   1470    572       C  
ATOM   2752  CD2 LEU A 382      35.712  -8.151  74.758  1.00 85.93           C  
ANISOU 2752  CD2 LEU A 382     5680  17951   9017   -398   1217    543       C  
ATOM   2753  N   PHE A 383      39.103  -6.288  71.033  1.00 78.31           N  
ANISOU 2753  N   PHE A 383     4447  16494   8814   -762   1114    -39       N  
ATOM   2754  CA  PHE A 383      40.203  -6.611  70.131  1.00 82.41           C  
ANISOU 2754  CA  PHE A 383     4893  16875   9546   -705   1146     -1       C  
ATOM   2755  C   PHE A 383      41.132  -5.427  69.877  1.00 84.20           C  
ANISOU 2755  C   PHE A 383     5031  17094   9868   -866   1085   -275       C  
ATOM   2756  O   PHE A 383      41.849  -5.415  68.871  1.00 82.99           O  
ANISOU 2756  O   PHE A 383     4876  16709   9945   -870   1172   -294       O  
ATOM   2757  CB  PHE A 383      39.663  -7.143  68.802  1.00 82.40           C  
ANISOU 2757  CB  PHE A 383     5108  16441   9761   -696   1331     92       C  
ATOM   2758  CG  PHE A 383      38.773  -8.345  68.944  1.00 83.65           C  
ANISOU 2758  CG  PHE A 383     5358  16562   9865   -566   1422    351       C  
ATOM   2759  CD1 PHE A 383      39.311  -9.620  68.988  1.00 85.18           C  
ANISOU 2759  CD1 PHE A 383     5461  16834  10069   -352   1488    627       C  
ATOM   2760  CD2 PHE A 383      37.397  -8.200  69.022  1.00 83.19           C  
ANISOU 2760  CD2 PHE A 383     5474  16375   9761   -653   1465    329       C  
ATOM   2761  CE1 PHE A 383      38.495 -10.728  69.117  1.00 86.76           C  
ANISOU 2761  CE1 PHE A 383     5783  16951  10232   -240   1607    866       C  
ATOM   2762  CE2 PHE A 383      36.577  -9.304  69.150  1.00 84.87           C  
ANISOU 2762  CE2 PHE A 383     5763  16533   9951   -557   1568    559       C  
ATOM   2763  CZ  PHE A 383      37.127 -10.569  69.197  1.00 86.89           C  
ANISOU 2763  CZ  PHE A 383     5981  16817  10216   -356   1641    820       C  
ATOM   2764  N   ASN A 384      41.140  -4.436  70.763  1.00 87.12           N  
ANISOU 2764  N   ASN A 384     5326  17709  10068  -1004    965   -491       N  
ATOM   2765  CA  ASN A 384      42.004  -3.273  70.586  1.00 89.86           C  
ANISOU 2765  CA  ASN A 384     5588  18049  10507  -1183    928   -769       C  
ATOM   2766  C   ASN A 384      42.438  -2.791  71.959  1.00 96.71           C  
ANISOU 2766  C   ASN A 384     6238  19396  11113  -1249    727   -909       C  
ATOM   2767  O   ASN A 384      41.598  -2.382  72.767  1.00101.21           O  
ANISOU 2767  O   ASN A 384     6868  20130  11455  -1321    697   -991       O  
ATOM   2768  CB  ASN A 384      41.288  -2.161  69.815  1.00 79.38           C  
ANISOU 2768  CB  ASN A 384     4508  16360   9291  -1368   1075   -979       C  
ATOM   2769  CG  ASN A 384      42.234  -1.080  69.324  1.00 86.52           C  
ANISOU 2769  CG  ASN A 384     5356  17156  10360  -1531   1114  -1228       C  
ATOM   2770  OD1 ASN A 384      43.203  -0.730  69.997  1.00 91.63           O  
ANISOU 2770  OD1 ASN A 384     5772  18089  10955  -1599    986  -1355       O  
ATOM   2771  ND2 ASN A 384      41.959  -0.550  68.137  1.00 78.27           N  
ANISOU 2771  ND2 ASN A 384     4517  15707   9515  -1593   1297  -1296       N  
ATOM   2772  N   LYS A 385      43.747  -2.835  72.217  1.00 98.08           N  
ANISOU 2772  N   LYS A 385     6147  19802  11318  -1226    592   -940       N  
ATOM   2773  CA  LYS A 385      44.253  -2.441  73.527  1.00101.17           C  
ANISOU 2773  CA  LYS A 385     6306  20694  11441  -1285    360  -1079       C  
ATOM   2774  C   LYS A 385      44.185  -0.934  73.728  1.00105.60           C  
ANISOU 2774  C   LYS A 385     6916  21243  11965  -1590    368  -1464       C  
ATOM   2775  O   LYS A 385      43.976  -0.473  74.855  1.00111.27           O  
ANISOU 2775  O   LYS A 385     7561  22327  12390  -1686    232  -1615       O  
ATOM   2776  CB  LYS A 385      45.678  -2.957  73.723  1.00104.14           C  
ANISOU 2776  CB  LYS A 385     6373  21319  11876  -1160    198   -988       C  
ATOM   2777  CG  LYS A 385      45.756  -4.474  73.824  1.00103.20           C  
ANISOU 2777  CG  LYS A 385     6179  21316  11717   -828    180   -592       C  
ATOM   2778  CD  LYS A 385      47.167  -4.953  74.116  1.00105.31           C  
ANISOU 2778  CD  LYS A 385     6122  21866  12026   -679     10   -489       C  
ATOM   2779  CE  LYS A 385      47.193  -6.458  74.336  1.00104.07           C  
ANISOU 2779  CE  LYS A 385     5900  21854  11787   -317     11    -74       C  
ATOM   2780  NZ  LYS A 385      48.560  -6.955  74.652  1.00107.05           N  
ANISOU 2780  NZ  LYS A 385     5956  22519  12199   -135   -153     57       N  
ATOM   2781  N   THR A 386      44.367  -0.152  72.662  1.00103.30           N  
ANISOU 2781  N   THR A 386     6748  20548  11952  -1740    542  -1627       N  
ATOM   2782  CA  THR A 386      44.316   1.300  72.800  1.00101.80           C  
ANISOU 2782  CA  THR A 386     6620  20318  11743  -2025    597  -1990       C  
ATOM   2783  C   THR A 386      42.904   1.765  73.141  1.00101.15           C  
ANISOU 2783  C   THR A 386     6773  20185  11475  -2098    698  -2056       C  
ATOM   2784  O   THR A 386      42.710   2.568  74.062  1.00101.41           O  
ANISOU 2784  O   THR A 386     6771  20476  11284  -2276    645  -2295       O  
ATOM   2785  CB  THR A 386      44.810   1.969  71.516  1.00 97.76           C  
ANISOU 2785  CB  THR A 386     6199  19368  11577  -2130    798  -2106       C  
ATOM   2786  OG1 THR A 386      43.917   1.659  70.439  1.00 95.71           O  
ANISOU 2786  OG1 THR A 386     6218  18685  11464  -2025    998  -1939       O  
ATOM   2787  CG2 THR A 386      46.209   1.478  71.165  1.00 92.99           C  
ANISOU 2787  CG2 THR A 386     5338  18806  11187  -2051    728  -2021       C  
ATOM   2788  N   TYR A 387      41.904   1.261  72.410  1.00102.01           N  
ANISOU 2788  N   TYR A 387     7115  19965  11677  -1968    849  -1849       N  
ATOM   2789  CA  TYR A 387      40.514   1.570  72.737  1.00102.67           C  
ANISOU 2789  CA  TYR A 387     7404  19995  11610  -2001    947  -1860       C  
ATOM   2790  C   TYR A 387      40.159   1.101  74.142  1.00108.10           C  
ANISOU 2790  C   TYR A 387     7958  21154  11960  -1943    799  -1791       C  
ATOM   2791  O   TYR A 387      39.446   1.797  74.874  1.00111.74           O  
ANISOU 2791  O   TYR A 387     8477  21755  12223  -2069    844  -1945       O  
ATOM   2792  CB  TYR A 387      39.572   0.926  71.718  1.00 97.25           C  
ANISOU 2792  CB  TYR A 387     6954  18903  11092  -1850   1091  -1619       C  
ATOM   2793  CG  TYR A 387      39.246   1.772  70.507  1.00 92.70           C  
ANISOU 2793  CG  TYR A 387     6606  17873  10744  -1937   1285  -1732       C  
ATOM   2794  CD1 TYR A 387      38.573   2.980  70.639  1.00 88.35           C  
ANISOU 2794  CD1 TYR A 387     6201  17228  10139  -2092   1407  -1946       C  
ATOM   2795  CD2 TYR A 387      39.582   1.347  69.228  1.00 94.13           C  
ANISOU 2795  CD2 TYR A 387     6858  17730  11178  -1848   1367  -1614       C  
ATOM   2796  CE1 TYR A 387      38.261   3.751  69.533  1.00 76.00           C  
ANISOU 2796  CE1 TYR A 387     4844  15267   8765  -2138   1592  -2024       C  
ATOM   2797  CE2 TYR A 387      39.274   2.111  68.116  1.00 89.61           C  
ANISOU 2797  CE2 TYR A 387     6489  16778  10779  -1906   1546  -1703       C  
ATOM   2798  CZ  TYR A 387      38.614   3.311  68.275  1.00 80.17           C  
ANISOU 2798  CZ  TYR A 387     5434  15505   9524  -2041   1652  -1900       C  
ATOM   2799  OH  TYR A 387      38.306   4.072  67.171  1.00 73.16           O  
ANISOU 2799  OH  TYR A 387     4747  14257   8792  -2070   1838  -1969       O  
ATOM   2800  N   ARG A 388      40.649  -0.077  74.537  1.00107.18           N  
ANISOU 2800  N   ARG A 388     7661  21297  11765  -1739    644  -1548       N  
ATOM   2801  CA  ARG A 388      40.316  -0.608  75.855  1.00105.66           C  
ANISOU 2801  CA  ARG A 388     7338  21577  11233  -1639    512  -1441       C  
ATOM   2802  C   ARG A 388      40.923   0.242  76.965  1.00113.83           C  
ANISOU 2802  C   ARG A 388     8175  23070  12004  -1822    327  -1734       C  
ATOM   2803  O   ARG A 388      40.258   0.527  77.967  1.00117.64           O  
ANISOU 2803  O   ARG A 388     8829  23676  12191  -1836    301  -1784       O  
ATOM   2804  CB  ARG A 388      40.778  -2.060  75.974  1.00 97.13           C  
ANISOU 2804  CB  ARG A 388     6110  20663  10132  -1348    404  -1096       C  
ATOM   2805  CG  ARG A 388      40.467  -2.693  77.322  1.00 91.65           C  
ANISOU 2805  CG  ARG A 388     5425  20327   9072  -1165    268   -925       C  
ATOM   2806  CD  ARG A 388      40.591  -4.208  77.278  1.00 91.71           C  
ANISOU 2806  CD  ARG A 388     5407  20346   9094   -839    262   -525       C  
ATOM   2807  NE  ARG A 388      41.860  -4.647  76.704  1.00 94.46           N  
ANISOU 2807  NE  ARG A 388     5465  20796   9631   -761    176   -459       N  
ATOM   2808  CZ  ARG A 388      42.161  -5.916  76.446  1.00 96.14           C  
ANISOU 2808  CZ  ARG A 388     5633  20977   9919   -485    208   -123       C  
ATOM   2809  NH1 ARG A 388      41.284  -6.874  76.711  1.00 98.09           N  
ANISOU 2809  NH1 ARG A 388     6112  21088  10069   -279    324    163       N  
ATOM   2810  NH2 ARG A 388      43.339  -6.227  75.923  1.00 95.01           N  
ANISOU 2810  NH2 ARG A 388     5291  20846   9961   -412    149    -71       N  
ATOM   2811  N   SER A 389      42.181   0.659  76.802  1.00116.12           N  
ANISOU 2811  N   SER A 389     8307  23418  12395  -1925    199  -1910       N  
ATOM   2812  CA  SER A 389      42.799   1.548  77.780  1.00119.82           C  
ANISOU 2812  CA  SER A 389     8613  24277  12634  -2141     13  -2235       C  
ATOM   2813  C   SER A 389      42.077   2.888  77.836  1.00117.00           C  
ANISOU 2813  C   SER A 389     8434  23779  12242  -2440    196  -2569       C  
ATOM   2814  O   SER A 389      41.842   3.432  78.923  1.00123.74           O  
ANISOU 2814  O   SER A 389     9355  24885  12775  -2555    105  -2753       O  
ATOM   2815  CB  SER A 389      44.278   1.748  77.450  1.00124.39           C  
ANISOU 2815  CB  SER A 389     8999  24864  13402  -2201   -114  -2350       C  
ATOM   2816  OG  SER A 389      44.968   0.510  77.420  1.00126.44           O  
ANISOU 2816  OG  SER A 389     9081  25261  13700  -1913   -262  -2031       O  
ATOM   2817  N   ALA A 390      41.718   3.435  76.670  1.00107.81           N  
ANISOU 2817  N   ALA A 390     7487  22091  11385  -2517    465  -2620       N  
ATOM   2818  CA  ALA A 390      40.983   4.694  76.637  1.00103.18           C  
ANISOU 2818  CA  ALA A 390     7094  21324  10787  -2764    688  -2901       C  
ATOM   2819  C   ALA A 390      39.667   4.579  77.396  1.00107.36           C  
ANISOU 2819  C   ALA A 390     7849  21886  11055  -2680    762  -2792       C  
ATOM   2820  O   ALA A 390      39.327   5.449  78.204  1.00113.86           O  
ANISOU 2820  O   ALA A 390     8830  22779  11651  -2838    799  -3021       O  
ATOM   2821  CB  ALA A 390      40.738   5.121  75.190  1.00 92.61           C  
ANISOU 2821  CB  ALA A 390     5995  19386   9807  -2765    949  -2884       C  
ATOM   2822  N   PHE A 391      38.925   3.493  77.170  1.00102.02           N  
ANISOU 2822  N   PHE A 391     7268  21087  10408  -2410    794  -2429       N  
ATOM   2823  CA  PHE A 391      37.633   3.332  77.832  1.00 97.51           C  
ANISOU 2823  CA  PHE A 391     6972  20445   9633  -2295    892  -2284       C  
ATOM   2824  C   PHE A 391      37.802   3.101  79.330  1.00101.07           C  
ANISOU 2824  C   PHE A 391     7433  21298   9673  -2235    685  -2287       C  
ATOM   2825  O   PHE A 391      37.034   3.640  80.139  1.00101.71           O  
ANISOU 2825  O   PHE A 391     7748  21379   9519  -2282    776  -2373       O  
ATOM   2826  CB  PHE A 391      36.857   2.181  77.191  1.00 93.85           C  
ANISOU 2826  CB  PHE A 391     6579  19750   9331  -2046    978  -1910       C  
ATOM   2827  CG  PHE A 391      36.499   2.416  75.747  1.00 90.04           C  
ANISOU 2827  CG  PHE A 391     6147  18863   9202  -2090   1178  -1900       C  
ATOM   2828  CD1 PHE A 391      36.553   3.686  75.195  1.00 91.34           C  
ANISOU 2828  CD1 PHE A 391     6416  18792   9497  -2293   1319  -2175       C  
ATOM   2829  CD2 PHE A 391      36.113   1.360  74.940  1.00 82.31           C  
ANISOU 2829  CD2 PHE A 391     5238  17623   8413  -1890   1200  -1600       C  
ATOM   2830  CE1 PHE A 391      36.226   3.897  73.868  1.00 88.30           C  
ANISOU 2830  CE1 PHE A 391     6239  17904   9409  -2254   1449  -2120       C  
ATOM   2831  CE2 PHE A 391      35.784   1.563  73.613  1.00 78.18           C  
ANISOU 2831  CE2 PHE A 391     4914  16607   8183  -1882   1315  -1573       C  
ATOM   2832  CZ  PHE A 391      35.841   2.833  73.076  1.00 77.81           C  
ANISOU 2832  CZ  PHE A 391     4982  16335   8245  -2049   1432  -1822       C  
ATOM   2833  N   SER A 392      38.803   2.304  79.719  1.00104.26           N  
ANISOU 2833  N   SER A 392     7596  22046   9974  -2113    415  -2182       N  
ATOM   2834  CA  SER A 392      39.071   2.074  81.134  1.00109.35           C  
ANISOU 2834  CA  SER A 392     8242  23111  10193  -2033    184  -2183       C  
ATOM   2835  C   SER A 392      39.458   3.361  81.849  1.00121.94           C  
ANISOU 2835  C   SER A 392     9862  24897  11572  -2333    110  -2606       C  
ATOM   2836  O   SER A 392      39.161   3.523  83.038  1.00128.43           O  
ANISOU 2836  O   SER A 392    10858  25936  12004  -2318     33  -2663       O  
ATOM   2837  CB  SER A 392      40.168   1.022  81.298  1.00107.04           C  
ANISOU 2837  CB  SER A 392     7651  23161   9860  -1832    -97  -1988       C  
ATOM   2838  OG  SER A 392      39.761  -0.228  80.770  1.00 99.44           O  
ANISOU 2838  OG  SER A 392     6715  22014   9055  -1545     -4  -1589       O  
ATOM   2839  N   ARG A 393      40.133   4.280  81.154  1.00127.10           N  
ANISOU 2839  N   ARG A 393    10364  25465  12465  -2611    149  -2914       N  
ATOM   2840  CA  ARG A 393      40.460   5.558  81.776  1.00130.16           C  
ANISOU 2840  CA  ARG A 393    10798  25985  12673  -2936    123  -3347       C  
ATOM   2841  C   ARG A 393      39.290   6.534  81.725  1.00126.67           C  
ANISOU 2841  C   ARG A 393    10727  25175  12227  -3069    467  -3485       C  
ATOM   2842  O   ARG A 393      39.206   7.437  82.566  1.00131.40           O  
ANISOU 2842  O   ARG A 393    11492  25873  12559  -3270    483  -3777       O  
ATOM   2843  CB  ARG A 393      41.684   6.184  81.108  1.00131.83           C  
ANISOU 2843  CB  ARG A 393    10692  26245  13153  -3200     57  -3639       C  
ATOM   2844  CG  ARG A 393      42.984   5.445  81.372  1.00133.34           C  
ANISOU 2844  CG  ARG A 393    10474  26880  13309  -3116   -313  -3578       C  
ATOM   2845  CD  ARG A 393      44.165   6.136  80.705  1.00131.90           C  
ANISOU 2845  CD  ARG A 393    10021  26659  13434  -3374   -324  -3862       C  
ATOM   2846  NE  ARG A 393      44.121   6.047  79.248  1.00123.11           N  
ANISOU 2846  NE  ARG A 393     8980  25019  12777  -3297    -43  -3710       N  
ATOM   2847  CZ  ARG A 393      43.683   7.020  78.454  1.00117.97           C  
ANISOU 2847  CZ  ARG A 393     8527  23944  12353  -3491    281  -3899       C  
ATOM   2848  NH1 ARG A 393      43.255   8.162  78.974  1.00121.27           N  
ANISOU 2848  NH1 ARG A 393     9063  24401  12614  -3796    400  -4255       N  
ATOM   2849  NH2 ARG A 393      43.678   6.853  77.139  1.00111.89           N  
ANISOU 2849  NH2 ARG A 393     7860  22701  11952  -3374    491  -3730       N  
ATOM   2850  N   TYR A 394      38.383   6.370  80.759  1.00118.46           N  
ANISOU 2850  N   TYR A 394     9821  23717  11472  -2956    743  -3279       N  
ATOM   2851  CA  TYR A 394      37.238   7.269  80.650  1.00112.31           C  
ANISOU 2851  CA  TYR A 394     9369  22589  10717  -3043   1079  -3370       C  
ATOM   2852  C   TYR A 394      36.163   6.946  81.680  1.00109.97           C  
ANISOU 2852  C   TYR A 394     9344  22333  10107  -2871   1134  -3195       C  
ATOM   2853  O   TYR A 394      35.502   7.858  82.189  1.00106.02           O  
ANISOU 2853  O   TYR A 394     9112  21715   9456  -2991   1336  -3369       O  
ATOM   2854  CB  TYR A 394      36.648   7.221  79.239  1.00106.81           C  
ANISOU 2854  CB  TYR A 394     8701  21459  10423  -2972   1327  -3211       C  
ATOM   2855  CG  TYR A 394      37.568   7.750  78.164  1.00104.30           C  
ANISOU 2855  CG  TYR A 394     8195  21015  10421  -3152   1369  -3407       C  
ATOM   2856  CD1 TYR A 394      38.647   8.565  78.484  1.00105.84           C  
ANISOU 2856  CD1 TYR A 394     8249  21401  10565  -3432   1279  -3774       C  
ATOM   2857  CD2 TYR A 394      37.359   7.435  76.828  1.00 99.75           C  
ANISOU 2857  CD2 TYR A 394     7589  20121  10190  -3049   1508  -3231       C  
ATOM   2858  CE1 TYR A 394      39.492   9.049  77.503  1.00103.56           C  
ANISOU 2858  CE1 TYR A 394     7785  20974  10590  -3600   1356  -3950       C  
ATOM   2859  CE2 TYR A 394      38.199   7.914  75.840  1.00 97.63           C  
ANISOU 2859  CE2 TYR A 394     7177  19713  10203  -3196   1580  -3397       C  
ATOM   2860  CZ  TYR A 394      39.263   8.721  76.183  1.00101.01           C  
ANISOU 2860  CZ  TYR A 394     7458  20319  10603  -3469   1519  -3751       C  
ATOM   2861  OH  TYR A 394      40.102   9.203  75.205  1.00 92.35           O  
ANISOU 2861  OH  TYR A 394     6363  18929   9796  -3548   1586  -3869       O  
ATOM   2862  N   ILE A 395      35.954   5.662  81.984  1.00112.23           N  
ANISOU 2862  N   ILE A 395     9584  22755  10304  -2585    995  -2843       N  
ATOM   2863  CA  ILE A 395      34.939   5.310  82.975  1.00115.30           C  
ANISOU 2863  CA  ILE A 395    10236  23165  10408  -2410   1079  -2661       C  
ATOM   2864  C   ILE A 395      35.287   5.923  84.327  1.00127.28           C  
ANISOU 2864  C   ILE A 395    11889  24996  11475  -2535    956  -2920       C  
ATOM   2865  O   ILE A 395      34.401   6.325  85.091  1.00132.69           O  
ANISOU 2865  O   ILE A 395    12882  25602  11934  -2523   1141  -2939       O  
ATOM   2866  CB  ILE A 395      34.768   3.781  83.070  1.00108.49           C  
ANISOU 2866  CB  ILE A 395     9296  22392   9534  -2084    965  -2242       C  
ATOM   2867  CG1 ILE A 395      36.075   3.101  83.486  1.00105.29           C  
ANISOU 2867  CG1 ILE A 395     8632  22411   8960  -2010    603  -2220       C  
ATOM   2868  CG2 ILE A 395      34.261   3.219  81.753  1.00102.54           C  
ANISOU 2868  CG2 ILE A 395     8467  21289   9205  -1984   1116  -2008       C  
ATOM   2869  CD1 ILE A 395      35.926   1.627  83.797  1.00 99.96           C  
ANISOU 2869  CD1 ILE A 395     7933  21846   8200  -1667    517  -1809       C  
ATOM   2870  N   GLN A 396      36.577   5.999  84.643  1.00130.27           N  
ANISOU 2870  N   GLN A 396    12040  25740  11716  -2657    642  -3124       N  
ATOM   2871  CA  GLN A 396      37.056   6.598  85.880  1.00134.16           C  
ANISOU 2871  CA  GLN A 396    12632  26575  11769  -2811    466  -3415       C  
ATOM   2872  C   GLN A 396      37.330   8.092  85.750  1.00135.05           C  
ANISOU 2872  C   GLN A 396    12814  26574  11926  -3203    595  -3884       C  
ATOM   2873  O   GLN A 396      37.769   8.712  86.725  1.00144.47           O  
ANISOU 2873  O   GLN A 396    14098  28033  12762  -3391    455  -4190       O  
ATOM   2874  CB  GLN A 396      38.322   5.873  86.344  1.00138.52           C  
ANISOU 2874  CB  GLN A 396    12873  27625  12135  -2733     26  -3392       C  
ATOM   2875  CG  GLN A 396      38.089   4.397  86.599  1.00138.82           C  
ANISOU 2875  CG  GLN A 396    12880  27783  12081  -2328    -79  -2926       C  
ATOM   2876  CD  GLN A 396      39.327   3.683  87.083  1.00141.98           C  
ANISOU 2876  CD  GLN A 396    12976  28686  12283  -2209   -503  -2872       C  
ATOM   2877  OE1 GLN A 396      40.417   4.256  87.127  1.00145.72           O  
ANISOU 2877  OE1 GLN A 396    13199  29430  12737  -2442   -745  -3184       O  
ATOM   2878  NE2 GLN A 396      39.172   2.411  87.427  1.00139.94           N  
ANISOU 2878  NE2 GLN A 396    12723  28552  11896  -1837   -583  -2467       N  
ATOM   2879  N   CYS A 397      37.081   8.677  84.574  1.00127.29           N  
ANISOU 2879  N   CYS A 397    11808  25198  11358  -3328    866  -3950       N  
ATOM   2880  CA  CYS A 397      37.300  10.102  84.315  1.00109.41           C  
ANISOU 2880  CA  CYS A 397     9628  22755   9189  -3686   1061  -4373       C  
ATOM   2881  C   CYS A 397      38.754  10.495  84.594  1.00123.49           C  
ANISOU 2881  C   CYS A 397    11135  24896  10889  -3966    755  -4734       C  
ATOM   2882  O   CYS A 397      39.054  11.303  85.475  1.00126.68           O  
ANISOU 2882  O   CYS A 397    11666  25475  10992  -4216    698  -5089       O  
ATOM   2883  CB  CYS A 397      36.326  10.962  85.128  1.00110.75           C  
ANISOU 2883  CB  CYS A 397    10228  22765   9085  -3764   1338  -4516       C  
ATOM   2884  SG  CYS A 397      34.583  10.696  84.732  1.00106.48           S  
ANISOU 2884  SG  CYS A 397     9972  21776   8708  -3475   1743  -4128       S  
ATOM   2885  N   GLN A 398      39.660   9.902  83.817  1.00122.45           N  
ANISOU 2885  N   GLN A 398    10616  24870  11040  -3926    562  -4642       N  
ATOM   2886  CA  GLN A 398      41.101  10.135  83.942  1.00133.41           C  
ANISOU 2886  CA  GLN A 398    11649  26608  12432  -4164    259  -4937       C  
ATOM   2887  C   GLN A 398      41.661  10.459  82.559  1.00130.18           C  
ANISOU 2887  C   GLN A 398    11001  25926  12535  -4301    417  -5013       C  
ATOM   2888  O   GLN A 398      42.069   9.561  81.817  1.00129.47           O  
ANISOU 2888  O   GLN A 398    10642  25851  12699  -4105    316  -4744       O  
ATOM   2889  CB  GLN A 398      41.786   8.926  84.567  1.00142.52           C  
ANISOU 2889  CB  GLN A 398    12530  28252  13367  -3922   -180  -4705       C  
ATOM   2890  CG  GLN A 398      41.275   8.595  85.959  1.00150.25           C  
ANISOU 2890  CG  GLN A 398    13771  29507  13809  -3766   -330  -4622       C  
ATOM   2891  CD  GLN A 398      41.686   7.213  86.422  1.00153.58           C  
ANISOU 2891  CD  GLN A 398    13988  30319  14047  -3412   -678  -4263       C  
ATOM   2892  OE1 GLN A 398      42.063   6.362  85.616  1.00151.77           O  
ANISOU 2892  OE1 GLN A 398    13481  30064  14121  -3222   -733  -3990       O  
ATOM   2893  NE2 GLN A 398      41.609   6.980  87.726  1.00158.23           N  
ANISOU 2893  NE2 GLN A 398    14740  31259  14122  -3306   -894  -4254       N  
ATOM   2894  N   TYR A 399      41.676  11.743  82.217  1.00130.40           N  
ANISOU 2894  N   TYR A 399    11155  25685  12706  -4629    695  -5377       N  
ATOM   2895  CA  TYR A 399      42.060  12.185  80.882  1.00117.80           C  
ANISOU 2895  CA  TYR A 399     9420  23753  11588  -4753    933  -5453       C  
ATOM   2896  C   TYR A 399      43.496  12.700  80.858  1.00117.64           C  
ANISOU 2896  C   TYR A 399     9038  23965  11694  -5090    763  -5829       C  
ATOM   2897  O   TYR A 399      44.299  12.293  80.018  1.00115.65           O  
ANISOU 2897  O   TYR A 399     8565  23609  11768  -4973    727  -5683       O  
ATOM   2898  CB  TYR A 399      41.100  13.269  80.393  1.00110.42           C  
ANISOU 2898  CB  TYR A 399     8870  22313  10773  -4862   1413  -5574       C  
ATOM   2899  CG  TYR A 399      39.662  12.995  80.766  1.00108.01           C  
ANISOU 2899  CG  TYR A 399     8929  21845  10267  -4601   1568  -5296       C  
ATOM   2900  CD1 TYR A 399      38.877  12.138  80.005  1.00103.61           C  
ANISOU 2900  CD1 TYR A 399     8402  21071   9895  -4266   1654  -4869       C  
ATOM   2901  CD2 TYR A 399      39.093  13.581  81.889  1.00112.39           C  
ANISOU 2901  CD2 TYR A 399     9794  22461  10449  -4696   1635  -5465       C  
ATOM   2902  CE1 TYR A 399      37.565  11.880  80.349  1.00101.74           C  
ANISOU 2902  CE1 TYR A 399     8456  20692   9507  -4042   1798  -4619       C  
ATOM   2903  CE2 TYR A 399      37.782  13.329  82.241  1.00108.49           C  
ANISOU 2903  CE2 TYR A 399     9614  21811   9797  -4451   1803  -5201       C  
ATOM   2904  CZ  TYR A 399      37.023  12.478  81.468  1.00104.17           C  
ANISOU 2904  CZ  TYR A 399     9051  21059   9468  -4128   1882  -4778       C  
ATOM   2905  OH  TYR A 399      35.716  12.226  81.816  1.00103.69           O  
ANISOU 2905  OH  TYR A 399     9266  20847   9285  -3901   2054  -4520       O  
TER    2906      TYR A 399                                                      
ATOM   2907  N   GLN B  72       4.189 -15.931  30.154  1.00111.37           N  
ANISOU 2907  N   GLN B  72     9431  16822  16062  -5895   1330   -224       N  
ATOM   2908  CA  GLN B  72       5.160 -16.916  30.619  1.00116.06           C  
ANISOU 2908  CA  GLN B  72    10538  16907  16652  -6101   1373   -279       C  
ATOM   2909  C   GLN B  72       6.182 -17.224  29.527  1.00119.11           C  
ANISOU 2909  C   GLN B  72    11176  17274  16806  -6110    960   -737       C  
ATOM   2910  O   GLN B  72       7.351 -17.490  29.809  1.00121.74           O  
ANISOU 2910  O   GLN B  72    11996  17332  16927  -6073   1012   -794       O  
ATOM   2911  CB  GLN B  72       4.441 -18.195  31.062  1.00123.22           C  
ANISOU 2911  CB  GLN B  72    11362  17363  18093  -6535   1425   -172       C  
ATOM   2912  CG  GLN B  72       5.353 -19.372  31.363  1.00123.25           C  
ANISOU 2912  CG  GLN B  72    11878  16772  18178  -6766   1409   -250       C  
ATOM   2913  CD  GLN B  72       6.325 -19.092  32.493  1.00118.02           C  
ANISOU 2913  CD  GLN B  72    11710  15955  17179  -6536   1793     48       C  
ATOM   2914  OE1 GLN B  72       6.003 -19.283  33.665  1.00119.93           O  
ANISOU 2914  OE1 GLN B  72    12009  16019  17539  -6548   2180    470       O  
ATOM   2915  NE2 GLN B  72       7.524 -18.640  32.145  1.00112.41           N  
ANISOU 2915  NE2 GLN B  72    11346  15333  16033  -6309   1680   -164       N  
ATOM   2916  N   GLU B  73       5.726 -17.164  28.275  1.00118.54           N  
ANISOU 2916  N   GLU B  73    10767  17520  16754  -6121    545  -1060       N  
ATOM   2917  CA  GLU B  73       6.618 -17.373  27.138  1.00111.30           C  
ANISOU 2917  CA  GLU B  73    10054  16668  15566  -6042    130  -1515       C  
ATOM   2918  C   GLU B  73       7.659 -16.261  27.026  1.00102.34           C  
ANISOU 2918  C   GLU B  73     9157  15812  13918  -5558    208  -1457       C  
ATOM   2919  O   GLU B  73       8.814 -16.516  26.667  1.00 88.69           O  
ANISOU 2919  O   GLU B  73     7886  13874  11936  -5346     53  -1660       O  
ATOM   2920  CB  GLU B  73       5.800 -17.476  25.848  1.00107.63           C  
ANISOU 2920  CB  GLU B  73     9167  16548  15181  -6074   -325  -1834       C  
ATOM   2921  CG  GLU B  73       4.848 -18.673  25.787  1.00112.22           C  
ANISOU 2921  CG  GLU B  73     9551  16783  16305  -6511   -492  -1957       C  
ATOM   2922  CD  GLU B  73       3.493 -18.384  26.414  1.00117.31           C  
ANISOU 2922  CD  GLU B  73     9704  17557  17312  -6637   -247  -1582       C  
ATOM   2923  OE1 GLU B  73       3.317 -17.283  26.976  1.00113.94           O  
ANISOU 2923  OE1 GLU B  73     9146  17439  16705  -6358     81  -1229       O  
ATOM   2924  OE2 GLU B  73       2.601 -19.257  26.342  1.00119.42           O  
ANISOU 2924  OE2 GLU B  73     9714  17598  18063  -6996   -383  -1645       O  
ATOM   2925  N   LYS B  74       7.258 -15.022  27.325  1.00 99.73           N  
ANISOU 2925  N   LYS B  74     8550  15888  13454  -5290    454  -1157       N  
ATOM   2926  CA  LYS B  74       8.125 -13.850  27.189  1.00100.45           C  
ANISOU 2926  CA  LYS B  74     8843  16196  13127  -4755    537  -1060       C  
ATOM   2927  C   LYS B  74       9.359 -13.901  28.089  1.00108.00           C  
ANISOU 2927  C   LYS B  74    10403  16730  13904  -4575    775   -946       C  
ATOM   2928  O   LYS B  74      10.387 -13.288  27.763  1.00109.99           O  
ANISOU 2928  O   LYS B  74    10921  17040  13831  -4190    727   -996       O  
ATOM   2929  CB  LYS B  74       7.322 -12.585  27.490  1.00 96.34           C  
ANISOU 2929  CB  LYS B  74     7894  16104  12605  -4552    807   -745       C  
ATOM   2930  CG  LYS B  74       6.308 -12.207  26.428  1.00102.53           C  
ANISOU 2930  CG  LYS B  74     8141  17371  13443  -4487    532   -816       C  
ATOM   2931  CD  LYS B  74       5.433 -11.055  26.896  1.00105.68           C  
ANISOU 2931  CD  LYS B  74     8256  17979  13918  -4184    830   -451       C  
ATOM   2932  CE  LYS B  74       4.742 -11.376  28.215  1.00108.90           C  
ANISOU 2932  CE  LYS B  74     8678  18053  14644  -4371   1197   -194       C  
ATOM   2933  NZ  LYS B  74       3.946 -10.217  28.706  1.00109.35           N  
ANISOU 2933  NZ  LYS B  74     8508  18269  14770  -4028   1497    115       N  
ATOM   2934  N   ASN B  75       9.263 -14.575  29.238  1.00111.47           N  
ANISOU 2934  N   ASN B  75    11033  16776  14545  -4831   1044   -764       N  
ATOM   2935  CA  ASN B  75      10.321 -14.509  30.247  1.00108.84           C  
ANISOU 2935  CA  ASN B  75    11216  16125  14012  -4630   1298   -601       C  
ATOM   2936  C   ASN B  75      11.675 -14.985  29.718  1.00111.52           C  
ANISOU 2936  C   ASN B  75    12028  16209  14134  -4453   1037   -859       C  
ATOM   2937  O   ASN B  75      12.715 -14.453  30.113  1.00105.63           O  
ANISOU 2937  O   ASN B  75    11613  15410  13112  -4125   1145   -792       O  
ATOM   2938  CB  ASN B  75       9.908 -15.311  31.483  1.00106.39           C  
ANISOU 2938  CB  ASN B  75    11012  15464  13949  -4948   1606   -342       C  
ATOM   2939  CG  ASN B  75       8.861 -14.595  32.319  1.00104.24           C  
ANISOU 2939  CG  ASN B  75    10373  15459  13774  -4981   1995    -11       C  
ATOM   2940  OD1 ASN B  75       8.729 -13.370  32.262  1.00101.33           O  
ANISOU 2940  OD1 ASN B  75     9815  15456  13229  -4667   2100     54       O  
ATOM   2941  ND2 ASN B  75       8.110 -15.359  33.103  1.00107.31           N  
ANISOU 2941  ND2 ASN B  75    10693  15613  14466  -5270   2204    217       N  
ATOM   2942  N   TRP B  76      11.698 -16.000  28.851  1.00121.19           N  
ANISOU 2942  N   TRP B  76    13285  17268  15492  -4665    695  -1174       N  
ATOM   2943  CA  TRP B  76      12.979 -16.455  28.308  1.00122.83           C  
ANISOU 2943  CA  TRP B  76    13928  17253  15489  -4461    463  -1433       C  
ATOM   2944  C   TRP B  76      13.607 -15.408  27.388  1.00118.55           C  
ANISOU 2944  C   TRP B  76    13339  17122  14582  -4030    316  -1547       C  
ATOM   2945  O   TRP B  76      14.836 -15.221  27.391  1.00128.48           O  
ANISOU 2945  O   TRP B  76    14953  18273  15588  -3723    315  -1577       O  
ATOM   2946  CB  TRP B  76      12.800 -17.799  27.611  1.00131.37           C  
ANISOU 2946  CB  TRP B  76    15056  18039  16819  -4785    148  -1782       C  
ATOM   2947  CG  TRP B  76      12.672 -18.896  28.620  1.00136.46           C  
ANISOU 2947  CG  TRP B  76    15928  18120  17801  -5120    337  -1622       C  
ATOM   2948  CD1 TRP B  76      11.518 -19.436  29.112  1.00140.92           C  
ANISOU 2948  CD1 TRP B  76    16213  18543  18785  -5566    473  -1475       C  
ATOM   2949  CD2 TRP B  76      13.744 -19.549  29.310  1.00136.75           C  
ANISOU 2949  CD2 TRP B  76    16501  17672  17788  -5013    445  -1532       C  
ATOM   2950  NE1 TRP B  76      11.808 -20.402  30.047  1.00143.19           N  
ANISOU 2950  NE1 TRP B  76    16851  18264  19291  -5745    673  -1281       N  
ATOM   2951  CE2 TRP B  76      13.168 -20.489  30.186  1.00141.18           C  
ANISOU 2951  CE2 TRP B  76    17104  17798  18741  -5397    649  -1312       C  
ATOM   2952  CE3 TRP B  76      15.136 -19.439  29.262  1.00133.49           C  
ANISOU 2952  CE3 TRP B  76    16511  17160  17049  -4622    392  -1598       C  
ATOM   2953  CZ2 TRP B  76      13.936 -21.316  31.007  1.00142.76           C  
ANISOU 2953  CZ2 TRP B  76    17777  17472  18992  -5373    796  -1136       C  
ATOM   2954  CZ3 TRP B  76      15.897 -20.263  30.078  1.00133.95           C  
ANISOU 2954  CZ3 TRP B  76    17017  16716  17162  -4604    515  -1455       C  
ATOM   2955  CH2 TRP B  76      15.295 -21.186  30.939  1.00138.90           C  
ANISOU 2955  CH2 TRP B  76    17698  16921  18159  -4964    714  -1216       C  
ATOM   2956  N   SER B  77      12.789 -14.738  26.571  1.00104.76           N  
ANISOU 2956  N   SER B  77    11137  15853  12813  -3995    193  -1591       N  
ATOM   2957  CA  SER B  77      13.302 -13.622  25.784  1.00 89.81           C  
ANISOU 2957  CA  SER B  77     9169  14364  10593  -3564    126  -1592       C  
ATOM   2958  C   SER B  77      13.876 -12.555  26.706  1.00 80.32           C  
ANISOU 2958  C   SER B  77     8111  13138   9268  -3280    480  -1282       C  
ATOM   2959  O   SER B  77      14.943 -11.985  26.436  1.00 78.36           O  
ANISOU 2959  O   SER B  77     8072  12924   8776  -2939    479  -1290       O  
ATOM   2960  CB  SER B  77      12.191 -13.038  24.907  1.00 72.37           C  
ANISOU 2960  CB  SER B  77     6411  12688   8399  -3562    -22  -1604       C  
ATOM   2961  OG  SER B  77      11.751 -13.974  23.938  1.00 81.57           O  
ANISOU 2961  OG  SER B  77     7437  13931   9625  -3795   -411  -1966       O  
ATOM   2962  N   ALA B  78      13.181 -12.290  27.814  1.00 77.21           N  
ANISOU 2962  N   ALA B  78     7599  12685   9053  -3424    792  -1021       N  
ATOM   2963  CA  ALA B  78      13.684 -11.341  28.802  1.00 76.58           C  
ANISOU 2963  CA  ALA B  78     7674  12561   8862  -3180   1125   -785       C  
ATOM   2964  C   ALA B  78      15.013 -11.811  29.387  1.00 76.92           C  
ANISOU 2964  C   ALA B  78     8241  12228   8759  -3085   1145   -835       C  
ATOM   2965  O   ALA B  78      15.892 -10.995  29.685  1.00 75.19           O  
ANISOU 2965  O   ALA B  78     8191  12018   8362  -2788   1262   -778       O  
ATOM   2966  CB  ALA B  78      12.648 -11.134  29.906  1.00 80.32           C  
ANISOU 2966  CB  ALA B  78     7942  13048   9529  -3360   1458   -531       C  
ATOM   2967  N   LEU B  79      15.168 -13.124  29.570  1.00 81.92           N  
ANISOU 2967  N   LEU B  79     9117  12515   9493  -3335   1034   -937       N  
ATOM   2968  CA  LEU B  79      16.412 -13.674  30.103  1.00 83.01           C  
ANISOU 2968  CA  LEU B  79     9739  12299   9501  -3227   1033   -966       C  
ATOM   2969  C   LEU B  79      17.576 -13.413  29.158  1.00 76.69           C  
ANISOU 2969  C   LEU B  79     9091  11573   8474  -2912    813  -1171       C  
ATOM   2970  O   LEU B  79      18.657 -12.982  29.582  1.00 72.19           O  
ANISOU 2970  O   LEU B  79     8767  10935   7729  -2655    892  -1125       O  
ATOM   2971  CB  LEU B  79      16.264 -15.176  30.349  1.00 88.98           C  
ANISOU 2971  CB  LEU B  79    10699  12644  10467  -3549    953  -1021       C  
ATOM   2972  CG  LEU B  79      17.366 -15.782  31.223  1.00 89.73           C  
ANISOU 2972  CG  LEU B  79    11277  12356  10459  -3446   1029   -940       C  
ATOM   2973  CD1 LEU B  79      17.390 -15.139  32.612  1.00 88.22           C  
ANISOU 2973  CD1 LEU B  79    11162  12209  10149  -3351   1372   -630       C  
ATOM   2974  CD2 LEU B  79      17.235 -17.293  31.322  1.00 93.34           C  
ANISOU 2974  CD2 LEU B  79    11937  12356  11171  -3741    944   -986       C  
ATOM   2975  N   LEU B  80      17.387 -13.716  27.873  1.00 74.63           N  
ANISOU 2975  N   LEU B  80     8681  11467   8208  -2929    530  -1409       N  
ATOM   2976  CA  LEU B  80      18.451 -13.449  26.909  1.00 71.43           C  
ANISOU 2976  CA  LEU B  80     8392  11187   7559  -2605    350  -1580       C  
ATOM   2977  C   LEU B  80      18.763 -11.957  26.840  1.00 69.18           C  
ANISOU 2977  C   LEU B  80     7947  11212   7127  -2286    512  -1402       C  
ATOM   2978  O   LEU B  80      19.933 -11.556  26.728  1.00 67.11           O  
ANISOU 2978  O   LEU B  80     7869  10928   6701  -2006    525  -1409       O  
ATOM   2979  CB  LEU B  80      18.067 -13.992  25.533  1.00 73.75           C  
ANISOU 2979  CB  LEU B  80     8528  11670   7825  -2663     25  -1877       C  
ATOM   2980  CG  LEU B  80      17.997 -15.518  25.430  1.00 78.04           C  
ANISOU 2980  CG  LEU B  80     9282  11835   8535  -2946   -174  -2145       C  
ATOM   2981  CD1 LEU B  80      17.716 -15.964  24.002  1.00 81.56           C  
ANISOU 2981  CD1 LEU B  80     9579  12512   8897  -2958   -526  -2518       C  
ATOM   2982  CD2 LEU B  80      19.274 -16.156  25.955  1.00 76.90           C  
ANISOU 2982  CD2 LEU B  80     9612  11271   8336  -2814   -137  -2169       C  
ATOM   2983  N   THR B  81      17.727 -11.119  26.932  1.00 71.23           N  
ANISOU 2983  N   THR B  81     7847  11737   7480  -2326    651  -1231       N  
ATOM   2984  CA  THR B  81      17.933  -9.676  26.996  1.00 71.89           C  
ANISOU 2984  CA  THR B  81     7779  12036   7499  -2038    851  -1040       C  
ATOM   2985  C   THR B  81      18.800  -9.286  28.191  1.00 68.89           C  
ANISOU 2985  C   THR B  81     7679  11399   7096  -1939   1079   -941       C  
ATOM   2986  O   THR B  81      19.722  -8.472  28.065  1.00 71.96           O  
ANISOU 2986  O   THR B  81     8129  11818   7394  -1669   1137   -913       O  
ATOM   2987  CB  THR B  81      16.581  -8.966  27.063  1.00 77.03           C  
ANISOU 2987  CB  THR B  81     8010  12958   8300  -2110    989   -866       C  
ATOM   2988  OG1 THR B  81      16.005  -8.890  25.752  1.00 75.88           O  
ANISOU 2988  OG1 THR B  81     7548  13180   8102  -2056    762   -931       O  
ATOM   2989  CG2 THR B  81      16.750  -7.577  27.640  1.00 79.41           C  
ANISOU 2989  CG2 THR B  81     8237  13313   8623  -1869   1289   -656       C  
ATOM   2990  N   ALA B  82      18.508  -9.854  29.364  1.00 66.65           N  
ANISOU 2990  N   ALA B  82     7551  10879   6895  -2155   1212   -883       N  
ATOM   2991  CA  ALA B  82      19.288  -9.544  30.558  1.00 48.59           C  
ANISOU 2991  CA  ALA B  82     5530   8399   4532  -2055   1401   -812       C  
ATOM   2992  C   ALA B  82      20.734  -9.992  30.402  1.00 49.48           C  
ANISOU 2992  C   ALA B  82     5974   8328   4498  -1898   1240   -944       C  
ATOM   2993  O   ALA B  82      21.659  -9.320  30.879  1.00 54.50           O  
ANISOU 2993  O   ALA B  82     6730   8931   5047  -1698   1324   -934       O  
ATOM   2994  CB  ALA B  82      18.652 -10.195  31.786  1.00 50.58           C  
ANISOU 2994  CB  ALA B  82     5890   8479   4851  -2300   1571   -692       C  
ATOM   2995  N   VAL B  83      20.945 -11.140  29.757  1.00 48.10           N  
ANISOU 2995  N   VAL B  83     5937   8025   4313  -1987   1007  -1089       N  
ATOM   2996  CA  VAL B  83      22.303 -11.597  29.472  1.00 59.81           C  
ANISOU 2996  CA  VAL B  83     7703   9357   5664  -1802    852  -1221       C  
ATOM   2997  C   VAL B  83      23.045 -10.550  28.651  1.00 57.60           C  
ANISOU 2997  C   VAL B  83     7287   9312   5287  -1503    834  -1246       C  
ATOM   2998  O   VAL B  83      24.189 -10.182  28.959  1.00 58.96           O  
ANISOU 2998  O   VAL B  83     7600   9420   5383  -1306    866  -1246       O  
ATOM   2999  CB  VAL B  83      22.273 -12.958  28.753  1.00 49.16           C  
ANISOU 2999  CB  VAL B  83     6491   7839   4348  -1930    611  -1412       C  
ATOM   3000  CG1 VAL B  83      23.644 -13.293  28.182  1.00 48.08           C  
ANISOU 3000  CG1 VAL B  83     6580   7625   4065  -1671    454  -1568       C  
ATOM   3001  CG2 VAL B  83      21.801 -14.049  29.699  1.00 51.57           C  
ANISOU 3001  CG2 VAL B  83     6990   7809   4796  -2209    662  -1343       C  
ATOM   3002  N   VAL B  84      22.400 -10.057  27.590  1.00 54.16           N  
ANISOU 3002  N   VAL B  84     6554   9165   4861  -1463    785  -1248       N  
ATOM   3003  CA  VAL B  84      23.032  -9.041  26.748  1.00 52.90           C  
ANISOU 3003  CA  VAL B  84     6242   9237   4621  -1169    805  -1204       C  
ATOM   3004  C   VAL B  84      23.318  -7.777  27.556  1.00 48.48           C  
ANISOU 3004  C   VAL B  84     5612   8659   4151  -1058   1057  -1042       C  
ATOM   3005  O   VAL B  84      24.369  -7.142  27.395  1.00 42.74           O  
ANISOU 3005  O   VAL B  84     4908   7929   3403   -843   1101  -1023       O  
ATOM   3006  CB  VAL B  84      22.158  -8.744  25.515  1.00 46.92           C  
ANISOU 3006  CB  VAL B  84     5163   8834   3829  -1130    714  -1188       C  
ATOM   3007  CG1 VAL B  84      22.844  -7.736  24.612  1.00 44.39           C  
ANISOU 3007  CG1 VAL B  84     4699   8753   3414   -800    763  -1080       C  
ATOM   3008  CG2 VAL B  84      21.871 -10.023  24.748  1.00 47.86           C  
ANISOU 3008  CG2 VAL B  84     5357   8967   3862  -1261    434  -1429       C  
ATOM   3009  N   ILE B  85      22.391  -7.401  28.442  1.00 49.68           N  
ANISOU 3009  N   ILE B  85     5667   8789   4421  -1206   1233   -940       N  
ATOM   3010  CA  ILE B  85      22.567  -6.202  29.263  1.00 48.14           C  
ANISOU 3010  CA  ILE B  85     5413   8558   4320  -1106   1476   -844       C  
ATOM   3011  C   ILE B  85      23.814  -6.329  30.129  1.00 54.36           C  
ANISOU 3011  C   ILE B  85     6492   9126   5038  -1047   1473   -938       C  
ATOM   3012  O   ILE B  85      24.667  -5.429  30.172  1.00 56.69           O  
ANISOU 3012  O   ILE B  85     6755   9400   5385   -875   1544   -946       O  
ATOM   3013  CB  ILE B  85      21.319  -5.962  30.134  1.00 42.58           C  
ANISOU 3013  CB  ILE B  85     4586   7875   3719  -1269   1672   -750       C  
ATOM   3014  CG1 ILE B  85      20.118  -5.547  29.285  1.00 58.01           C  
ANISOU 3014  CG1 ILE B  85     6170  10095   5776  -1275   1695   -631       C  
ATOM   3015  CG2 ILE B  85      21.605  -4.916  31.202  1.00 41.87           C  
ANISOU 3015  CG2 ILE B  85     4525   7693   3690  -1174   1911   -734       C  
ATOM   3016  CD1 ILE B  85      18.834  -5.421  30.078  1.00 45.87           C  
ANISOU 3016  CD1 ILE B  85     4470   8604   4354  -1438   1889   -530       C  
ATOM   3017  N   ILE B  86      23.922  -7.449  30.847  1.00 55.40           N  
ANISOU 3017  N   ILE B  86     6891   9087   5071  -1190   1390   -999       N  
ATOM   3018  CA  ILE B  86      25.045  -7.655  31.755  1.00 53.69           C  
ANISOU 3018  CA  ILE B  86     6945   8703   4753  -1120   1364  -1070       C  
ATOM   3019  C   ILE B  86      26.355  -7.689  30.982  1.00 55.20           C  
ANISOU 3019  C   ILE B  86     7184   8886   4904   -922   1208  -1157       C  
ATOM   3020  O   ILE B  86      27.360  -7.104  31.409  1.00 53.36           O  
ANISOU 3020  O   ILE B  86     6984   8617   4673   -789   1230  -1205       O  
ATOM   3021  CB  ILE B  86      24.836  -8.939  32.580  1.00 58.72           C  
ANISOU 3021  CB  ILE B  86     7856   9164   5292  -1287   1313  -1053       C  
ATOM   3022  CG1 ILE B  86      23.575  -8.817  33.438  1.00 59.49           C  
ANISOU 3022  CG1 ILE B  86     7878   9295   5429  -1471   1522   -931       C  
ATOM   3023  CG2 ILE B  86      26.049  -9.220  33.453  1.00 58.55           C  
ANISOU 3023  CG2 ILE B  86     8107   9013   5125  -1167   1250  -1104       C  
ATOM   3024  CD1 ILE B  86      23.222 -10.082  34.188  1.00 61.06           C  
ANISOU 3024  CD1 ILE B  86     8310   9318   5571  -1655   1520   -843       C  
ATOM   3025  N   LEU B  87      26.369  -8.369  29.831  1.00 59.05           N  
ANISOU 3025  N   LEU B  87     7658   9423   5354   -896   1050  -1197       N  
ATOM   3026  CA  LEU B  87      27.586  -8.423  29.027  1.00 54.03           C  
ANISOU 3026  CA  LEU B  87     7050   8816   4660   -679    933  -1268       C  
ATOM   3027  C   LEU B  87      28.009  -7.029  28.579  1.00 56.07           C  
ANISOU 3027  C   LEU B  87     7054   9224   5027   -507   1068  -1185       C  
ATOM   3028  O   LEU B  87      29.187  -6.663  28.681  1.00 65.52           O  
ANISOU 3028  O   LEU B  87     8265  10380   6249   -361   1070  -1212       O  
ATOM   3029  CB  LEU B  87      27.384  -9.342  27.822  1.00 47.95           C  
ANISOU 3029  CB  LEU B  87     6301   8116   3803   -665    756  -1356       C  
ATOM   3030  CG  LEU B  87      27.315 -10.837  28.138  1.00 44.82           C  
ANISOU 3030  CG  LEU B  87     6194   7480   3357   -801    604  -1472       C  
ATOM   3031  CD1 LEU B  87      27.103 -11.649  26.870  1.00 44.09           C  
ANISOU 3031  CD1 LEU B  87     6103   7455   3195   -784    420  -1633       C  
ATOM   3032  CD2 LEU B  87      28.574 -11.286  28.866  1.00 40.52           C  
ANISOU 3032  CD2 LEU B  87     5906   6734   2755   -675    558  -1503       C  
ATOM   3033  N   THR B  88      27.055  -6.233  28.085  1.00 50.65           N  
ANISOU 3033  N   THR B  88     6111   8701   4432   -521   1189  -1065       N  
ATOM   3034  CA  THR B  88      27.361  -4.866  27.672  1.00 46.91           C  
ANISOU 3034  CA  THR B  88     5390   8320   4115   -356   1356   -936       C  
ATOM   3035  C   THR B  88      27.992  -4.079  28.813  1.00 47.79           C  
ANISOU 3035  C   THR B  88     5534   8247   4375   -363   1485   -981       C  
ATOM   3036  O   THR B  88      29.084  -3.507  28.665  1.00 50.56           O  
ANISOU 3036  O   THR B  88     5826   8555   4829   -233   1515   -985       O  
ATOM   3037  CB  THR B  88      26.088  -4.169  27.187  1.00 43.09           C  
ANISOU 3037  CB  THR B  88     4638   8014   3721   -368   1480   -775       C  
ATOM   3038  OG1 THR B  88      25.638  -4.775  25.969  1.00 49.68           O  
ANISOU 3038  OG1 THR B  88     5395   9084   4396   -323   1328   -755       O  
ATOM   3039  CG2 THR B  88      26.342  -2.688  26.950  1.00 37.88           C  
ANISOU 3039  CG2 THR B  88     3771   7292   3330   -193   1658   -586       C  
ATOM   3040  N   ILE B  89      27.314  -4.046  29.964  1.00 49.33           N  
ANISOU 3040  N   ILE B  89     5812   8349   4582   -516   1562  -1030       N  
ATOM   3041  CA  ILE B  89      27.789  -3.234  31.082  1.00 36.67           C  
ANISOU 3041  CA  ILE B  89     4238   6597   3097   -514   1668  -1119       C  
ATOM   3042  C   ILE B  89      29.181  -3.681  31.514  1.00 55.58           C  
ANISOU 3042  C   ILE B  89     6810   8913   5396   -464   1518  -1268       C  
ATOM   3043  O   ILE B  89      30.095  -2.860  31.665  1.00 57.07           O  
ANISOU 3043  O   ILE B  89     6902   9040   5743   -385   1555  -1337       O  
ATOM   3044  CB  ILE B  89      26.788  -3.287  32.251  1.00 37.53           C  
ANISOU 3044  CB  ILE B  89     4439   6648   3171   -650   1754  -1137       C  
ATOM   3045  CG1 ILE B  89      25.426  -2.749  31.807  1.00 38.62           C  
ANISOU 3045  CG1 ILE B  89     4355   6860   3457   -663   1890   -969       C  
ATOM   3046  CG2 ILE B  89      27.314  -2.493  33.436  1.00 38.06           C  
ANISOU 3046  CG2 ILE B  89     4562   6590   3307   -623   1825  -1284       C  
ATOM   3047  CD1 ILE B  89      24.371  -2.787  32.890  1.00 39.45           C  
ANISOU 3047  CD1 ILE B  89     4510   6936   3542   -773   2004   -959       C  
ATOM   3048  N   ALA B  90      29.370  -4.992  31.694  1.00 45.25           N  
ANISOU 3048  N   ALA B  90     5745   7584   3866   -503   1338  -1310       N  
ATOM   3049  CA  ALA B  90      30.641  -5.495  32.206  1.00 42.53           C  
ANISOU 3049  CA  ALA B  90     5571   7168   3420   -426   1180  -1424       C  
ATOM   3050  C   ALA B  90      31.781  -5.224  31.231  1.00 46.21           C  
ANISOU 3050  C   ALA B  90     5891   7676   3990   -255   1124  -1420       C  
ATOM   3051  O   ALA B  90      32.849  -4.737  31.627  1.00 36.14           O  
ANISOU 3051  O   ALA B  90     4558   6369   2804   -185   1095  -1509       O  
ATOM   3052  CB  ALA B  90      30.530  -6.990  32.504  1.00 40.24           C  
ANISOU 3052  CB  ALA B  90     5570   6811   2907   -477   1026  -1421       C  
ATOM   3053  N   GLY B  91      31.580  -5.541  29.948  1.00 45.98           N  
ANISOU 3053  N   GLY B  91     5784   7744   3942   -182   1108  -1324       N  
ATOM   3054  CA  GLY B  91      32.637  -5.325  28.975  1.00 44.41           C  
ANISOU 3054  CA  GLY B  91     5443   7625   3804      7   1092  -1287       C  
ATOM   3055  C   GLY B  91      33.021  -3.865  28.836  1.00 57.27           C  
ANISOU 3055  C   GLY B  91     6784   9256   5717     55   1277  -1209       C  
ATOM   3056  O   GLY B  91      34.209  -3.527  28.767  1.00 71.21           O  
ANISOU 3056  O   GLY B  91     8444  11005   7609    152   1271  -1231       O  
ATOM   3057  N   ASN B  92      32.028  -2.971  28.794  1.00 53.29           N  
ANISOU 3057  N   ASN B  92     6132   8756   5358    -14   1454  -1109       N  
ATOM   3058  CA  ASN B  92      32.371  -1.565  28.623  1.00 46.19           C  
ANISOU 3058  CA  ASN B  92     4963   7795   4792     36   1656  -1016       C  
ATOM   3059  C   ASN B  92      32.977  -0.972  29.891  1.00 39.18           C  
ANISOU 3059  C   ASN B  92     4091   6717   4079    -61   1660  -1223       C  
ATOM   3060  O   ASN B  92      33.815  -0.067  29.805  1.00 37.86           O  
ANISOU 3060  O   ASN B  92     3722   6455   4210    -27   1751  -1223       O  
ATOM   3061  CB  ASN B  92      31.146  -0.781  28.162  1.00 53.01           C  
ANISOU 3061  CB  ASN B  92     5659   8706   5777     36   1851   -828       C  
ATOM   3062  CG  ASN B  92      30.786  -1.081  26.719  1.00 60.73           C  
ANISOU 3062  CG  ASN B  92     6571   9855   6647    182   1809   -589       C  
ATOM   3063  OD1 ASN B  92      31.448  -0.614  25.791  1.00 55.77           O  
ANISOU 3063  OD1 ASN B  92     5802   9249   6138    337   1872   -412       O  
ATOM   3064  ND2 ASN B  92      29.744  -1.879  26.522  1.00 73.89           N  
ANISOU 3064  ND2 ASN B  92     8337  11652   8087    121   1699   -601       N  
ATOM   3065  N   ILE B  93      32.615  -1.492  31.069  1.00 39.78           N  
ANISOU 3065  N   ILE B  93     4396   6749   3970   -180   1558  -1405       N  
ATOM   3066  CA  ILE B  93      33.303  -1.073  32.287  1.00 47.79           C  
ANISOU 3066  CA  ILE B  93     5449   7653   5057   -242   1505  -1647       C  
ATOM   3067  C   ILE B  93      34.754  -1.538  32.259  1.00 48.13           C  
ANISOU 3067  C   ILE B  93     5492   7726   5071   -160   1313  -1730       C  
ATOM   3068  O   ILE B  93      35.663  -0.814  32.688  1.00 47.13           O  
ANISOU 3068  O   ILE B  93     5217   7525   5166   -176   1295  -1881       O  
ATOM   3069  CB  ILE B  93      32.560  -1.596  33.530  1.00 56.00           C  
ANISOU 3069  CB  ILE B  93     6745   8703   5829   -346   1453  -1780       C  
ATOM   3070  CG1 ILE B  93      31.266  -0.812  33.748  1.00 67.36           C  
ANISOU 3070  CG1 ILE B  93     8112  10102   7381   -417   1685  -1742       C  
ATOM   3071  CG2 ILE B  93      33.444  -1.516  34.767  1.00 51.88           C  
ANISOU 3071  CG2 ILE B  93     6316   8160   5235   -363   1311  -2047       C  
ATOM   3072  CD1 ILE B  93      30.482  -1.257  34.963  1.00 73.55           C  
ANISOU 3072  CD1 ILE B  93     9121  10925   7902   -506   1690  -1843       C  
ATOM   3073  N   LEU B  94      34.996  -2.745  31.740  1.00 52.04           N  
ANISOU 3073  N   LEU B  94     6133   8321   5318    -70   1167  -1650       N  
ATOM   3074  CA  LEU B  94      36.367  -3.215  31.571  1.00 55.22           C  
ANISOU 3074  CA  LEU B  94     6507   8769   5703     54   1007  -1696       C  
ATOM   3075  C   LEU B  94      37.155  -2.298  30.643  1.00 51.80           C  
ANISOU 3075  C   LEU B  94     5737   8342   5601    133   1142  -1592       C  
ATOM   3076  O   LEU B  94      38.314  -1.968  30.921  1.00 53.46           O  
ANISOU 3076  O   LEU B  94     5790   8537   5985    156   1076  -1692       O  
ATOM   3077  CB  LEU B  94      36.370  -4.645  31.031  1.00 37.26           C  
ANISOU 3077  CB  LEU B  94     4452   6568   3139    164    868  -1623       C  
ATOM   3078  CG  LEU B  94      36.087  -5.773  32.023  1.00 41.46           C  
ANISOU 3078  CG  LEU B  94     5318   7056   3378    122    700  -1704       C  
ATOM   3079  CD1 LEU B  94      36.271  -7.122  31.348  1.00 37.50           C  
ANISOU 3079  CD1 LEU B  94     5003   6558   2688    249    577  -1647       C  
ATOM   3080  CD2 LEU B  94      36.983  -5.654  33.244  1.00 44.29           C  
ANISOU 3080  CD2 LEU B  94     5706   7418   3703    136    558  -1866       C  
ATOM   3081  N   VAL B  95      36.542  -1.881  29.533  1.00 46.74           N  
ANISOU 3081  N   VAL B  95     4963   7743   5054    181   1333  -1370       N  
ATOM   3082  CA  VAL B  95      37.223  -0.981  28.601  1.00 43.73           C  
ANISOU 3082  CA  VAL B  95     4258   7372   4987    273   1514  -1193       C  
ATOM   3083  C   VAL B  95      37.521   0.361  29.265  1.00 46.56           C  
ANISOU 3083  C   VAL B  95     4396   7522   5773    139   1639  -1286       C  
ATOM   3084  O   VAL B  95      38.607   0.935  29.086  1.00 46.07           O  
ANISOU 3084  O   VAL B  95     4080   7406   6019    153   1688  -1273       O  
ATOM   3085  CB  VAL B  95      36.386  -0.805  27.320  1.00 39.80           C  
ANISOU 3085  CB  VAL B  95     3677   7001   4444    381   1692   -907       C  
ATOM   3086  CG1 VAL B  95      37.005   0.251  26.416  1.00 40.32           C  
ANISOU 3086  CG1 VAL B  95     3401   7069   4851    486   1935   -654       C  
ATOM   3087  CG2 VAL B  95      36.259  -2.130  26.588  1.00 38.02           C  
ANISOU 3087  CG2 VAL B  95     3645   6980   3819    516   1543   -885       C  
ATOM   3088  N   ILE B  96      36.558   0.889  30.025  1.00 51.20           N  
ANISOU 3088  N   ILE B  96     5062   7980   6413      3   1704  -1392       N  
ATOM   3089  CA  ILE B  96      36.769   2.146  30.743  1.00 50.00           C  
ANISOU 3089  CA  ILE B  96     4737   7593   6668   -127   1814  -1556       C  
ATOM   3090  C   ILE B  96      37.951   2.023  31.695  1.00 50.32           C  
ANISOU 3090  C   ILE B  96     4765   7610   6744   -199   1590  -1869       C  
ATOM   3091  O   ILE B  96      38.831   2.893  31.735  1.00 53.60           O  
ANISOU 3091  O   ILE B  96     4908   7883   7575   -263   1641  -1949       O  
ATOM   3092  CB  ILE B  96      35.488   2.563  31.487  1.00 46.83           C  
ANISOU 3092  CB  ILE B  96     4469   7091   6235   -224   1909  -1660       C  
ATOM   3093  CG1 ILE B  96      34.396   2.962  30.494  1.00 41.57           C  
ANISOU 3093  CG1 ILE B  96     3710   6440   5643   -143   2150  -1331       C  
ATOM   3094  CG2 ILE B  96      35.776   3.704  32.452  1.00 44.47           C  
ANISOU 3094  CG2 ILE B  96     4057   6543   6298   -356   1968  -1952       C  
ATOM   3095  CD1 ILE B  96      33.008   2.979  31.092  1.00 41.11           C  
ANISOU 3095  CD1 ILE B  96     3804   6378   5440   -200   2216  -1383       C  
ATOM   3096  N   MET B  97      37.984   0.944  32.483  1.00 50.45           N  
ANISOU 3096  N   MET B  97     5059   7769   6343   -190   1336  -2040       N  
ATOM   3097  CA  MET B  97      39.087   0.751  33.420  1.00 56.59           C  
ANISOU 3097  CA  MET B  97     5825   8588   7087   -220   1086  -2324       C  
ATOM   3098  C   MET B  97      40.416   0.611  32.690  1.00 60.54           C  
ANISOU 3098  C   MET B  97     6076   9159   7766   -123   1030  -2226       C  
ATOM   3099  O   MET B  97      41.438   1.136  33.143  1.00 57.33           O  
ANISOU 3099  O   MET B  97     5442   8715   7627   -191    932  -2424       O  
ATOM   3100  CB  MET B  97      38.840  -0.475  34.300  1.00 55.66           C  
ANISOU 3100  CB  MET B  97     6065   8629   6456   -176    849  -2429       C  
ATOM   3101  CG  MET B  97      37.764  -0.295  35.351  1.00 57.65           C  
ANISOU 3101  CG  MET B  97     6535   8849   6522   -278    884  -2585       C  
ATOM   3102  SD  MET B  97      37.594  -1.771  36.371  1.00 59.49           S  
ANISOU 3102  SD  MET B  97     7168   9268   6166   -207    638  -2626       S  
ATOM   3103  CE  MET B  97      39.259  -1.924  37.016  1.00 47.82           C  
ANISOU 3103  CE  MET B  97     5577   7921   4671   -129    322  -2855       C  
ATOM   3104  N   ALA B  98      40.422  -0.098  31.560  1.00 64.96           N  
ANISOU 3104  N   ALA B  98     6660   9838   8183     40   1089  -1941       N  
ATOM   3105  CA  ALA B  98      41.662  -0.287  30.817  1.00 64.90           C  
ANISOU 3105  CA  ALA B  98     6415   9932   8311    172   1071  -1827       C  
ATOM   3106  C   ALA B  98      42.199   1.037  30.292  1.00 60.99           C  
ANISOU 3106  C   ALA B  98     5507   9295   8372     94   1306  -1726       C  
ATOM   3107  O   ALA B  98      43.400   1.312  30.394  1.00 67.63           O  
ANISOU 3107  O   ALA B  98     6068  10142   9486     75   1244  -1803       O  
ATOM   3108  CB  ALA B  98      41.445  -1.272  29.670  1.00 68.09           C  
ANISOU 3108  CB  ALA B  98     6950  10501   8420    384   1115  -1572       C  
ATOM   3109  N   VAL B  99      41.327   1.879  29.736  1.00 54.61           N  
ANISOU 3109  N   VAL B  99     4633   8347   7769     50   1583  -1533       N  
ATOM   3110  CA  VAL B  99      41.813   3.148  29.200  1.00 54.95           C  
ANISOU 3110  CA  VAL B  99     4286   8205   8387    -15   1847  -1377       C  
ATOM   3111  C   VAL B  99      42.193   4.111  30.321  1.00 51.52           C  
ANISOU 3111  C   VAL B  99     3701   7509   8367   -258   1786  -1729       C  
ATOM   3112  O   VAL B  99      43.158   4.874  30.189  1.00 54.43           O  
ANISOU 3112  O   VAL B  99     3709   7739   9233   -351   1868  -1734       O  
ATOM   3113  CB  VAL B  99      40.769   3.763  28.249  1.00 56.17           C  
ANISOU 3113  CB  VAL B  99     4412   8291   8637     52   2169  -1023       C  
ATOM   3114  CG1 VAL B  99      41.230   5.128  27.755  1.00 58.79           C  
ANISOU 3114  CG1 VAL B  99     4381   8370   9588    -11   2454   -804       C  
ATOM   3115  CG2 VAL B  99      40.522   2.831  27.073  1.00 53.36           C  
ANISOU 3115  CG2 VAL B  99     4168   8242   7866    299   2199   -720       C  
ATOM   3116  N   SER B 100      41.471   4.087  31.445  1.00 52.71           N  
ANISOU 3116  N   SER B 100     4107   7596   8324   -367   1643  -2047       N  
ATOM   3117  CA  SER B 100      41.752   5.031  32.521  1.00 59.12           C  
ANISOU 3117  CA  SER B 100     4798   8174   9489   -583   1578  -2444       C  
ATOM   3118  C   SER B 100      42.971   4.635  33.346  1.00 64.97           C  
ANISOU 3118  C   SER B 100     5452   9059  10176   -638   1236  -2782       C  
ATOM   3119  O   SER B 100      43.650   5.509  33.898  1.00 66.12           O  
ANISOU 3119  O   SER B 100     5336   9028  10759   -821   1183  -3079       O  
ATOM   3120  CB  SER B 100      40.531   5.166  33.431  1.00 52.96           C  
ANISOU 3120  CB  SER B 100     4321   7321   8478   -642   1570  -2668       C  
ATOM   3121  OG  SER B 100      39.385   5.547  32.692  1.00 51.54           O  
ANISOU 3121  OG  SER B 100     4187   7033   8362   -579   1873  -2354       O  
ATOM   3122  N   LEU B 101      43.265   3.339  33.444  1.00 65.32           N  
ANISOU 3122  N   LEU B 101     5694   9411   9714   -478    994  -2752       N  
ATOM   3123  CA  LEU B 101      44.321   2.834  34.314  1.00 67.33           C  
ANISOU 3123  CA  LEU B 101     5902   9857   9825   -478    636  -3050       C  
ATOM   3124  C   LEU B 101      45.595   2.462  33.569  1.00 72.54           C  
ANISOU 3124  C   LEU B 101     6257  10662  10641   -366    593  -2870       C  
ATOM   3125  O   LEU B 101      46.693   2.733  34.065  1.00 87.94           O  
ANISOU 3125  O   LEU B 101     7917  12661  12835   -450    398  -3109       O  
ATOM   3126  CB  LEU B 101      43.819   1.619  35.099  1.00 64.36           C  
ANISOU 3126  CB  LEU B 101     5961   9712   8781   -350    390  -3136       C  
ATOM   3127  CG  LEU B 101      42.661   1.874  36.067  1.00 63.64           C  
ANISOU 3127  CG  LEU B 101     6167   9549   8464   -445    400  -3351       C  
ATOM   3128  CD1 LEU B 101      42.125   0.562  36.618  1.00 64.56           C  
ANISOU 3128  CD1 LEU B 101     6702   9886   7941   -301    230  -3299       C  
ATOM   3129  CD2 LEU B 101      43.101   2.795  37.195  1.00 63.37           C  
ANISOU 3129  CD2 LEU B 101     5984   9449   8644   -620    247  -3828       C  
ATOM   3130  N   GLU B 102      45.486   1.847  32.394  1.00 97.09           N  
ANISOU 3130  N   GLU B 102     6434  14606  15848    528   2129   2994       N  
ATOM   3131  CA  GLU B 102      46.672   1.396  31.680  1.00 95.86           C  
ANISOU 3131  CA  GLU B 102     6120  14486  15815    586   2150   3084       C  
ATOM   3132  C   GLU B 102      47.362   2.594  31.046  1.00 95.24           C  
ANISOU 3132  C   GLU B 102     5883  14362  15940    516   2205   3100       C  
ATOM   3133  O   GLU B 102      46.750   3.353  30.288  1.00 92.22           O  
ANISOU 3133  O   GLU B 102     5552  13913  15576    487   2317   3100       O  
ATOM   3134  CB  GLU B 102      46.312   0.354  30.624  1.00 96.48           C  
ANISOU 3134  CB  GLU B 102     6245  14586  15825    692   2285   3170       C  
ATOM   3135  CG  GLU B 102      45.661  -0.887  31.207  1.00 96.29           C  
ANISOU 3135  CG  GLU B 102     6379  14601  15607    761   2248   3154       C  
ATOM   3136  CD  GLU B 102      46.538  -1.576  32.236  1.00 97.17           C  
ANISOU 3136  CD  GLU B 102     6454  14758  15707    789   2087   3150       C  
ATOM   3137  OE1 GLU B 102      47.774  -1.592  32.057  1.00 87.68           O  
ANISOU 3137  OE1 GLU B 102     5081  13579  14654    806   2048   3199       O  
ATOM   3138  OE2 GLU B 102      45.990  -2.099  33.230  1.00 96.09           O  
ANISOU 3138  OE2 GLU B 102     6458  14637  15414    794   2000   3100       O  
ATOM   3139  N   LYS B 103      48.645   2.755  31.363  1.00 99.62           N  
ANISOU 3139  N   LYS B 103     6277  14945  16628    489   2113   3100       N  
ATOM   3140  CA  LYS B 103      49.422   3.889  30.890  1.00103.48           C  
ANISOU 3140  CA  LYS B 103     6621  15387  17308    409   2151   3094       C  
ATOM   3141  C   LYS B 103      49.885   3.736  29.446  1.00101.39           C  
ANISOU 3141  C   LYS B 103     6419  15058  17048    451   2249   3118       C  
ATOM   3142  O   LYS B 103      50.233   4.738  28.812  1.00100.80           O  
ANISOU 3142  O   LYS B 103     6319  14908  17070    385   2306   3097       O  
ATOM   3143  CB  LYS B 103      50.615   4.067  31.829  1.00111.70           C  
ANISOU 3143  CB  LYS B 103     7510  16482  18451    354   1993   3050       C  
ATOM   3144  CG  LYS B 103      50.163   4.160  33.285  1.00117.28           C  
ANISOU 3144  CG  LYS B 103     8324  17209  19027    292   1837   2946       C  
ATOM   3145  CD  LYS B 103      51.296   4.361  34.272  1.00118.98           C  
ANISOU 3145  CD  LYS B 103     8405  17489  19312    223   1661   2891       C  
ATOM   3146  CE  LYS B 103      50.744   4.387  35.694  1.00115.64           C  
ANISOU 3146  CE  LYS B 103     8114  17094  18729    157   1515   2789       C  
ATOM   3147  NZ  LYS B 103      51.798   4.568  36.728  1.00115.61           N  
ANISOU 3147  NZ  LYS B 103     7987  17172  18767     80   1329   2732       N  
ATOM   3148  N   LYS B 104      49.898   2.513  28.915  1.00105.04           N  
ANISOU 3148  N   LYS B 104     6956  15545  17407    552   2277   3162       N  
ATOM   3149  CA  LYS B 104      50.200   2.278  27.508  1.00 89.56           C  
ANISOU 3149  CA  LYS B 104     5071  13528  15429    583   2381   3183       C  
ATOM   3150  C   LYS B 104      49.021   2.574  26.585  1.00102.86           C  
ANISOU 3150  C   LYS B 104     6938  15152  16993    580   2497   3184       C  
ATOM   3151  O   LYS B 104      49.195   2.559  25.362  1.00 88.06           O  
ANISOU 3151  O   LYS B 104     5126  13232  15101    587   2585   3201       O  
ATOM   3152  CB  LYS B 104      50.675   0.833  27.311  1.00 89.56           C  
ANISOU 3152  CB  LYS B 104     5078  13574  15376    684   2374   3223       C  
ATOM   3153  CG  LYS B 104      51.472   0.606  26.031  1.00 89.98           C  
ANISOU 3153  CG  LYS B 104     5138  13581  15471    699   2458   3234       C  
ATOM   3154  CD  LYS B 104      51.928  -0.836  25.892  1.00 90.09           C  
ANISOU 3154  CD  LYS B 104     5155  13629  15446    797   2462   3269       C  
ATOM   3155  CE  LYS B 104      52.768  -1.025  24.638  1.00 90.66           C  
ANISOU 3155  CE  LYS B 104     5221  13653  15572    799   2552   3271       C  
ATOM   3156  NZ  LYS B 104      53.219  -2.433  24.471  1.00 90.87           N  
ANISOU 3156  NZ  LYS B 104     5251  13700  15576    893   2571   3302       N  
ATOM   3157  N   LEU B 105      47.838   2.856  27.134  1.00 94.87           N  
ANISOU 3157  N   LEU B 105     6005  14142  15899    566   2497   3166       N  
ATOM   3158  CA  LEU B 105      46.629   3.014  26.330  1.00 97.20           C  
ANISOU 3158  CA  LEU B 105     6471  14395  16066    576   2592   3170       C  
ATOM   3159  C   LEU B 105      46.017   4.405  26.437  1.00 98.76           C  
ANISOU 3159  C   LEU B 105     6674  14527  16324    502   2617   3148       C  
ATOM   3160  O   LEU B 105      44.807   4.535  26.639  1.00103.37           O  
ANISOU 3160  O   LEU B 105     7358  15105  16813    506   2642   3135       O  
ATOM   3161  CB  LEU B 105      45.576   1.984  26.742  1.00 84.73           C  
ANISOU 3161  CB  LEU B 105     5009  12872  14315    638   2592   3167       C  
ATOM   3162  CG  LEU B 105      45.820   0.505  26.459  1.00 84.80           C  
ANISOU 3162  CG  LEU B 105     5064  12928  14226    721   2605   3191       C  
ATOM   3163  CD1 LEU B 105      44.695  -0.320  27.059  1.00 83.25           C  
ANISOU 3163  CD1 LEU B 105     4978  12783  13871    766   2608   3179       C  
ATOM   3164  CD2 LEU B 105      45.910   0.278  24.964  1.00 86.06           C  
ANISOU 3164  CD2 LEU B 105     5313  13050  14335    734   2701   3209       C  
ATOM   3165  N   GLN B 106      46.833   5.450  26.325  1.00 96.91           N  
ANISOU 3165  N   GLN B 106     6331  14238  16251    433   2618   3141       N  
ATOM   3166  CA  GLN B 106      46.365   6.814  26.543  1.00 97.26           C  
ANISOU 3166  CA  GLN B 106     6363  14209  16383    358   2647   3119       C  
ATOM   3167  C   GLN B 106      46.708   7.704  25.351  1.00 99.06           C  
ANISOU 3167  C   GLN B 106     6603  14351  16686    327   2735   3154       C  
ATOM   3168  O   GLN B 106      47.241   8.806  25.496  1.00102.70           O  
ANISOU 3168  O   GLN B 106     6970  14749  17303    250   2747   3136       O  
ATOM   3169  CB  GLN B 106      46.915   7.372  27.852  1.00 98.36           C  
ANISOU 3169  CB  GLN B 106     6346  14362  16662    280   2562   3065       C  
ATOM   3170  CG  GLN B 106      46.392   6.621  29.067  1.00 96.22           C  
ANISOU 3170  CG  GLN B 106     6072  14178  16310    302   2482   3040       C  
ATOM   3171  CD  GLN B 106      46.522   7.404  30.356  1.00 97.15           C  
ANISOU 3171  CD  GLN B 106     6063  14301  16549    202   2416   2981       C  
ATOM   3172  OE1 GLN B 106      47.411   8.240  30.504  1.00 96.04           O  
ANISOU 3172  OE1 GLN B 106     5794  14129  16568    119   2396   2952       O  
ATOM   3173  NE2 GLN B 106      45.620   7.144  31.297  1.00 88.43           N  
ANISOU 3173  NE2 GLN B 106     5080  13210  15308    196   2353   2912       N  
ATOM   3174  N   ASN B 107      46.403   7.224  24.146  1.00 93.25           N  
ANISOU 3174  N   ASN B 107     5980  13613  15837    382   2802   3205       N  
ATOM   3175  CA  ASN B 107      46.465   8.035  22.943  1.00 89.91           C  
ANISOU 3175  CA  ASN B 107     5593  13115  15452    360   2893   3256       C  
ATOM   3176  C   ASN B 107      45.050   8.486  22.579  1.00 86.87           C  
ANISOU 3176  C   ASN B 107     5336  12697  14975    380   2946   3288       C  
ATOM   3177  O   ASN B 107      44.094   8.262  23.326  1.00 93.59           O  
ANISOU 3177  O   ASN B 107     6235  13574  15750    399   2914   3257       O  
ATOM   3178  CB  ASN B 107      47.143   7.266  21.804  1.00 93.44           C  
ANISOU 3178  CB  ASN B 107     6066  13589  15847    395   2934   3292       C  
ATOM   3179  CG  ASN B 107      46.563   5.876  21.601  1.00 99.04           C  
ANISOU 3179  CG  ASN B 107     6883  14374  16371    470   2927   3294       C  
ATOM   3180  OD1 ASN B 107      45.402   5.616  21.919  1.00102.07           O  
ANISOU 3180  OD1 ASN B 107     7362  14783  16637    500   2918   3286       O  
ATOM   3181  ND2 ASN B 107      47.372   4.975  21.056  1.00100.43           N  
ANISOU 3181  ND2 ASN B 107     7046  14584  16529    497   2939   3299       N  
ATOM   3182  N   ALA B 108      44.905   9.130  21.418  1.00 87.13           N  
ANISOU 3182  N   ALA B 108     5417  12674  15014    375   3028   3355       N  
ATOM   3183  CA  ALA B 108      43.604   9.674  21.037  1.00 86.54           C  
ANISOU 3183  CA  ALA B 108     5443  12566  14872    397   3075   3400       C  
ATOM   3184  C   ALA B 108      42.588   8.567  20.782  1.00 87.98           C  
ANISOU 3184  C   ALA B 108     5750  12832  14844    465   3063   3400       C  
ATOM   3185  O   ALA B 108      41.440   8.652  21.240  1.00 85.82           O  
ANISOU 3185  O   ALA B 108     5537  12565  14506    485   3054   3384       O  
ATOM   3186  CB  ALA B 108      43.748  10.565  19.805  1.00 87.31           C  
ANISOU 3186  CB  ALA B 108     5554  12593  15024    383   3163   3490       C  
ATOM   3187  N   THR B 109      42.993   7.520  20.058  1.00 87.25           N  
ANISOU 3187  N   THR B 109     5698  12803  14649    495   3071   3409       N  
ATOM   3188  CA  THR B 109      42.061   6.451  19.714  1.00 83.57           C  
ANISOU 3188  CA  THR B 109     5354  12415  13983    548   3073   3402       C  
ATOM   3189  C   THR B 109      41.515   5.771  20.962  1.00 82.75           C  
ANISOU 3189  C   THR B 109     5264  12358  13818    570   3009   3329       C  
ATOM   3190  O   THR B 109      40.329   5.436  21.022  1.00 81.79           O  
ANISOU 3190  O   THR B 109     5239  12272  13564    600   3012   3314       O  
ATOM   3191  CB  THR B 109      42.740   5.428  18.800  1.00 83.55           C  
ANISOU 3191  CB  THR B 109     5378  12462  13904    564   3101   3411       C  
ATOM   3192  OG1 THR B 109      43.145   6.069  17.584  1.00 90.06           O  
ANISOU 3192  OG1 THR B 109     6199  13249  14771    538   3170   3481       O  
ATOM   3193  CG2 THR B 109      41.786   4.288  18.467  1.00 82.35           C  
ANISOU 3193  CG2 THR B 109     5353  12389  13547    607   3110   3389       C  
ATOM   3194  N   ASN B 110      42.355   5.583  21.981  1.00 83.21           N  
ANISOU 3194  N   ASN B 110     5222  12420  13972    554   2951   3284       N  
ATOM   3195  CA  ASN B 110      41.892   4.915  23.193  1.00 87.93           C  
ANISOU 3195  CA  ASN B 110     5827  13069  14513    574   2892   3225       C  
ATOM   3196  C   ASN B 110      40.954   5.804  24.005  1.00 87.11           C  
ANISOU 3196  C   ASN B 110     5725  12929  14445    547   2883   3197       C  
ATOM   3197  O   ASN B 110      39.988   5.310  24.597  1.00 88.70           O  
ANISOU 3197  O   ASN B 110     5994  13171  14538    571   2869   3158       O  
ATOM   3198  CB  ASN B 110      43.088   4.475  24.032  1.00 91.80           C  
ANISOU 3198  CB  ASN B 110     6194  13585  15099    566   2825   3200       C  
ATOM   3199  CG  ASN B 110      43.636   3.130  23.599  1.00 95.17           C  
ANISOU 3199  CG  ASN B 110     6647  14070  15444    618   2828   3209       C  
ATOM   3200  OD1 ASN B 110      42.886   2.171  23.412  1.00 92.74           O  
ANISOU 3200  OD1 ASN B 110     6451  13808  14977    664   2850   3199       O  
ATOM   3201  ND2 ASN B 110      44.950   3.055  23.424  1.00101.38           N  
ANISOU 3201  ND2 ASN B 110     7328  14849  16343    609   2814   3222       N  
ATOM   3202  N   TYR B 111      41.210   7.115  24.041  1.00 84.83           N  
ANISOU 3202  N   TYR B 111     5363  12557  14312    495   2900   3213       N  
ATOM   3203  CA  TYR B 111      40.259   8.027  24.673  1.00 94.98           C  
ANISOU 3203  CA  TYR B 111     6656  13789  15642    469   2913   3188       C  
ATOM   3204  C   TYR B 111      38.910   7.986  23.964  1.00 96.36           C  
ANISOU 3204  C   TYR B 111     6960  13971  15681    516   2961   3218       C  
ATOM   3205  O   TYR B 111      37.853   7.939  24.611  1.00101.16           O  
ANISOU 3205  O   TYR B 111     7615  14590  16230    526   2957   3174       O  
ATOM   3206  CB  TYR B 111      40.806   9.455  24.672  1.00105.10           C  
ANISOU 3206  CB  TYR B 111     7843  14965  17124    403   2944   3206       C  
ATOM   3207  CG  TYR B 111      42.099   9.657  25.433  1.00113.67           C  
ANISOU 3207  CG  TYR B 111     8786  16046  18359    340   2893   3164       C  
ATOM   3208  CD1 TYR B 111      42.397   8.899  26.559  1.00117.18           C  
ANISOU 3208  CD1 TYR B 111     9173  16565  18785    332   2812   3104       C  
ATOM   3209  CD2 TYR B 111      43.015  10.620  25.030  1.00117.96           C  
ANISOU 3209  CD2 TYR B 111     9242  16511  19064    284   2928   3187       C  
ATOM   3210  CE1 TYR B 111      43.578   9.092  27.256  1.00119.01           C  
ANISOU 3210  CE1 TYR B 111     9258  16806  19154    272   2753   3070       C  
ATOM   3211  CE2 TYR B 111      44.195  10.819  25.718  1.00119.08           C  
ANISOU 3211  CE2 TYR B 111     9244  16657  19344    219   2878   3140       C  
ATOM   3212  CZ  TYR B 111      44.473  10.054  26.829  1.00117.63           C  
ANISOU 3212  CZ  TYR B 111     8998  16558  19138    213   2785   3082       C  
ATOM   3213  OH  TYR B 111      45.649  10.256  27.513  1.00115.51           O  
ANISOU 3213  OH  TYR B 111     8575  16307  19007    145   2724   3040       O  
ATOM   3214  N   PHE B 112      38.931   8.011  22.630  1.00 86.90           N  
ANISOU 3214  N   PHE B 112     5813  12771  14434    541   3008   3293       N  
ATOM   3215  CA  PHE B 112      37.689   7.927  21.869  1.00 81.68           C  
ANISOU 3215  CA  PHE B 112     5262  12135  13638    585   3045   3329       C  
ATOM   3216  C   PHE B 112      36.974   6.607  22.119  1.00 80.45           C  
ANISOU 3216  C   PHE B 112     5198  12077  13291    623   3019   3270       C  
ATOM   3217  O   PHE B 112      35.745   6.571  22.230  1.00 79.79           O  
ANISOU 3217  O   PHE B 112     5185  12015  13116    646   3028   3250       O  
ATOM   3218  CB  PHE B 112      37.975   8.114  20.383  1.00 84.87           C  
ANISOU 3218  CB  PHE B 112     5691  12535  14019    596   3096   3424       C  
ATOM   3219  CG  PHE B 112      38.022   9.548  19.954  1.00 91.74           C  
ANISOU 3219  CG  PHE B 112     6514  13306  15038    576   3146   3505       C  
ATOM   3220  CD1 PHE B 112      36.878  10.188  19.509  1.00 95.83           C  
ANISOU 3220  CD1 PHE B 112     7079  13802  15530    607   3182   3566       C  
ATOM   3221  CD2 PHE B 112      39.208  10.259  19.999  1.00 92.52           C  
ANISOU 3221  CD2 PHE B 112     6514  13329  15308    527   3161   3521       C  
ATOM   3222  CE1 PHE B 112      36.920  11.508  19.115  1.00 97.25           C  
ANISOU 3222  CE1 PHE B 112     7213  13880  15857    596   3237   3654       C  
ATOM   3223  CE2 PHE B 112      39.255  11.577  19.607  1.00 94.45           C  
ANISOU 3223  CE2 PHE B 112     6718  13471  15695    506   3220   3596       C  
ATOM   3224  CZ  PHE B 112      38.110  12.201  19.164  1.00 96.30           C  
ANISOU 3224  CZ  PHE B 112     7004  13678  15907    544   3261   3668       C  
ATOM   3225  N   LEU B 113      37.726   5.507  22.196  1.00 83.33           N  
ANISOU 3225  N   LEU B 113     5562  12499  13600    632   2993   3242       N  
ATOM   3226  CA  LEU B 113      37.113   4.211  22.462  1.00 83.10           C  
ANISOU 3226  CA  LEU B 113     5621  12555  13399    666   2980   3186       C  
ATOM   3227  C   LEU B 113      36.539   4.144  23.870  1.00 80.77           C  
ANISOU 3227  C   LEU B 113     5316  12267  13105    661   2945   3114       C  
ATOM   3228  O   LEU B 113      35.537   3.464  24.093  1.00 77.86           O  
ANISOU 3228  O   LEU B 113     5038  11951  12594    684   2952   3067       O  
ATOM   3229  CB  LEU B 113      38.122   3.085  22.240  1.00 79.16           C  
ANISOU 3229  CB  LEU B 113     5114  12100  12864    681   2972   3181       C  
ATOM   3230  CG  LEU B 113      38.561   2.863  20.789  1.00 79.39           C  
ANISOU 3230  CG  LEU B 113     5175  12137  12852    684   3021   3234       C  
ATOM   3231  CD1 LEU B 113      39.439   1.625  20.670  1.00 79.38           C  
ANISOU 3231  CD1 LEU B 113     5172  12175  12813    703   3022   3214       C  
ATOM   3232  CD2 LEU B 113      37.366   2.780  19.852  1.00 78.75           C  
ANISOU 3232  CD2 LEU B 113     5207  12095  12621    697   3063   3249       C  
ATOM   3233  N   MET B 114      37.153   4.837  24.831  1.00 80.64           N  
ANISOU 3233  N   MET B 114     5191  12204  13247    622   2910   3099       N  
ATOM   3234  CA  MET B 114      36.586   4.872  26.176  1.00 81.26           C  
ANISOU 3234  CA  MET B 114     5253  12289  13332    604   2884   3031       C  
ATOM   3235  C   MET B 114      35.301   5.692  26.207  1.00 83.35           C  
ANISOU 3235  C   MET B 114     5567  12511  13592    597   2923   3013       C  
ATOM   3236  O   MET B 114      34.348   5.339  26.911  1.00 86.75           O  
ANISOU 3236  O   MET B 114     6051  12972  13939    602   2926   2950       O  
ATOM   3237  CB  MET B 114      37.605   5.434  27.166  1.00 83.29           C  
ANISOU 3237  CB  MET B 114     5369  12514  13765    550   2836   3016       C  
ATOM   3238  CG  MET B 114      37.144   5.391  28.614  1.00 82.05           C  
ANISOU 3238  CG  MET B 114     5182  12378  13616    518   2806   2946       C  
ATOM   3239  SD  MET B 114      38.266   6.257  29.729  1.00 82.68           S  
ANISOU 3239  SD  MET B 114     5080  12422  13915    430   2749   2925       S  
ATOM   3240  CE  MET B 114      38.220   7.909  29.036  1.00 91.31           C  
ANISOU 3240  CE  MET B 114     6145  13380  15169    383   2812   2946       C  
ATOM   3241  N   SER B 115      35.253   6.786  25.444  1.00 84.93           N  
ANISOU 3241  N   SER B 115     5747  12636  13885    588   2959   3071       N  
ATOM   3242  CA  SER B 115      33.996   7.518  25.299  1.00 79.47           C  
ANISOU 3242  CA  SER B 115     5103  11904  13188    599   3000   3072       C  
ATOM   3243  C   SER B 115      32.932   6.648  24.634  1.00 92.78           C  
ANISOU 3243  C   SER B 115     6909  13673  14670    651   3014   3068       C  
ATOM   3244  O   SER B 115      31.760   6.657  25.035  1.00 77.94           O  
ANISOU 3244  O   SER B 115     5078  11804  12730    662   3028   3017       O  
ATOM   3245  CB  SER B 115      34.230   8.800  24.501  1.00 80.45           C  
ANISOU 3245  CB  SER B 115     5180  11934  13453    590   3041   3159       C  
ATOM   3246  OG  SER B 115      33.019   9.506  24.299  1.00 80.44           O  
ANISOU 3246  OG  SER B 115     5215  11893  13456    613   3083   3178       O  
ATOM   3247  N   LEU B 116      33.333   5.886  23.614  1.00 86.14           N  
ANISOU 3247  N   LEU B 116     6113  12891  13726    676   3015   3111       N  
ATOM   3248  CA  LEU B 116      32.452   4.902  22.992  1.00 80.33           C  
ANISOU 3248  CA  LEU B 116     5489  12244  12789    710   3028   3091       C  
ATOM   3249  C   LEU B 116      31.940   3.892  24.011  1.00 82.62           C  
ANISOU 3249  C   LEU B 116     5832  12591  12969    713   3012   2989       C  
ATOM   3250  O   LEU B 116      30.763   3.512  23.990  1.00 80.85           O  
ANISOU 3250  O   LEU B 116     5688  12414  12618    728   3028   2941       O  
ATOM   3251  CB  LEU B 116      33.205   4.188  21.871  1.00 77.23           C  
ANISOU 3251  CB  LEU B 116     5123  11897  12325    720   3037   3139       C  
ATOM   3252  CG  LEU B 116      32.429   3.193  21.015  1.00 76.46           C  
ANISOU 3252  CG  LEU B 116     5135  11891  12026    741   3059   3121       C  
ATOM   3253  CD1 LEU B 116      31.419   3.933  20.183  1.00 76.87           C  
ANISOU 3253  CD1 LEU B 116     5209  11950  12049    755   3082   3177       C  
ATOM   3254  CD2 LEU B 116      33.374   2.398  20.130  1.00 79.68           C  
ANISOU 3254  CD2 LEU B 116     5558  12332  12386    738   3074   3146       C  
ATOM   3255  N   ALA B 117      32.824   3.427  24.894  1.00 87.01           N  
ANISOU 3255  N   ALA B 117     6340  13150  13571    699   2981   2959       N  
ATOM   3256  CA  ALA B 117      32.438   2.450  25.903  1.00 85.30           C  
ANISOU 3256  CA  ALA B 117     6167  12987  13254    703   2972   2878       C  
ATOM   3257  C   ALA B 117      31.468   3.057  26.904  1.00 85.21           C  
ANISOU 3257  C   ALA B 117     6152  12949  13273    681   2981   2815       C  
ATOM   3258  O   ALA B 117      30.554   2.377  27.377  1.00 83.23           O  
ANISOU 3258  O   ALA B 117     5980  12748  12895    688   2999   2744       O  
ATOM   3259  CB  ALA B 117      33.677   1.909  26.614  1.00 86.21           C  
ANISOU 3259  CB  ALA B 117     6210  13115  13431    699   2933   2885       C  
ATOM   3260  N   ILE B 118      31.649   4.336  27.235  1.00 86.44           N  
ANISOU 3260  N   ILE B 118     6219  13022  13602    648   2979   2835       N  
ATOM   3261  CA  ILE B 118      30.700   5.000  28.122  1.00 86.66           C  
ANISOU 3261  CA  ILE B 118     6240  13008  13677    621   3002   2770       C  
ATOM   3262  C   ILE B 118      29.344   5.125  27.440  1.00 76.08           C  
ANISOU 3262  C   ILE B 118     4985  11680  12241    654   3041   2760       C  
ATOM   3263  O   ILE B 118      28.297   4.941  28.071  1.00 82.80           O  
ANISOU 3263  O   ILE B 118     5885  12548  13027    650   3065   2679       O  
ATOM   3264  CB  ILE B 118      31.243   6.374  28.557  1.00 77.69           C  
ANISOU 3264  CB  ILE B 118     4989  11766  12764    572   3003   2790       C  
ATOM   3265  CG1 ILE B 118      32.509   6.208  29.399  1.00 78.27           C  
ANISOU 3265  CG1 ILE B 118     4964  11847  12928    528   2955   2784       C  
ATOM   3266  CG2 ILE B 118      30.185   7.151  29.329  1.00 77.84           C  
ANISOU 3266  CG2 ILE B 118     5005  11723  12846    543   3046   2721       C  
ATOM   3267  CD1 ILE B 118      33.113   7.518  29.855  1.00 79.46           C  
ANISOU 3267  CD1 ILE B 118     4996  11896  13300    461   2958   2787       C  
ATOM   3268  N   ALA B 119      29.341   5.398  26.133  1.00 76.22           N  
ANISOU 3268  N   ALA B 119     5018  11697  12244    685   3048   2843       N  
ATOM   3269  CA  ALA B 119      28.085   5.443  25.389  1.00 75.86           C  
ANISOU 3269  CA  ALA B 119     5039  11684  12099    719   3074   2847       C  
ATOM   3270  C   ALA B 119      27.391   4.085  25.397  1.00 79.92           C  
ANISOU 3270  C   ALA B 119     5661  12305  12402    731   3076   2768       C  
ATOM   3271  O   ALA B 119      26.180   3.991  25.634  1.00 80.94           O  
ANISOU 3271  O   ALA B 119     5838  12460  12455    737   3098   2702       O  
ATOM   3272  CB  ALA B 119      28.339   5.914  23.957  1.00 76.34           C  
ANISOU 3272  CB  ALA B 119     5088  11740  12176    746   3080   2967       C  
ATOM   3273  N   ASP B 120      28.150   3.015  25.145  1.00 76.46           N  
ANISOU 3273  N   ASP B 120     5258  11922  11872    733   3061   2769       N  
ATOM   3274  CA  ASP B 120      27.572   1.673  25.135  1.00 73.53           C  
ANISOU 3274  CA  ASP B 120     4993  11639  11305    739   3075   2691       C  
ATOM   3275  C   ASP B 120      27.073   1.266  26.517  1.00 73.13           C  
ANISOU 3275  C   ASP B 120     4969  11596  11221    721   3087   2589       C  
ATOM   3276  O   ASP B 120      26.022   0.625  26.642  1.00 72.49           O  
ANISOU 3276  O   ASP B 120     4975  11568  11000    720   3114   2505       O  
ATOM   3277  CB  ASP B 120      28.600   0.663  24.626  1.00 87.42           C  
ANISOU 3277  CB  ASP B 120     6777  13437  13004    746   3067   2719       C  
ATOM   3278  CG  ASP B 120      28.776   0.715  23.123  1.00 92.80           C  
ANISOU 3278  CG  ASP B 120     7471  14140  13648    756   3075   2792       C  
ATOM   3279  OD1 ASP B 120      27.791   1.015  22.419  1.00 96.66           O  
ANISOU 3279  OD1 ASP B 120     7993  14660  14075    762   3089   2798       O  
ATOM   3280  OD2 ASP B 120      29.902   0.454  22.648  1.00 95.96           O  
ANISOU 3280  OD2 ASP B 120     7844  14531  14085    757   3069   2844       O  
ATOM   3281  N   MET B 121      27.809   1.636  27.568  1.00 73.58           N  
ANISOU 3281  N   MET B 121     4949  11605  11404    700   3069   2591       N  
ATOM   3282  CA  MET B 121      27.382   1.327  28.927  1.00 77.33           C  
ANISOU 3282  CA  MET B 121     5439  12089  11853    675   3087   2503       C  
ATOM   3283  C   MET B 121      26.109   2.080  29.289  1.00 73.87           C  
ANISOU 3283  C   MET B 121     5013  11618  11437    659   3123   2438       C  
ATOM   3284  O   MET B 121      25.204   1.514  29.912  1.00 72.84           O  
ANISOU 3284  O   MET B 121     4955  11525  11196    647   3160   2342       O  
ATOM   3285  CB  MET B 121      28.504   1.657  29.911  1.00 85.22           C  
ANISOU 3285  CB  MET B 121     6331  13053  12994    647   3056   2531       C  
ATOM   3286  CG  MET B 121      28.156   1.411  31.369  1.00 89.14           C  
ANISOU 3286  CG  MET B 121     6905  13529  13437    599   3025   2410       C  
ATOM   3287  SD  MET B 121      29.439   2.019  32.479  1.00 90.11           S  
ANISOU 3287  SD  MET B 121     6995  13561  13682    532   2899   2376       S  
ATOM   3288  CE  MET B 121      29.360   3.778  32.156  1.00 90.36           C  
ANISOU 3288  CE  MET B 121     6908  13490  13936    501   2928   2411       C  
ATOM   3289  N   LEU B 122      26.020   3.355  28.906  1.00 74.01           N  
ANISOU 3289  N   LEU B 122     4959  11560  11600    659   3122   2487       N  
ATOM   3290  CA  LEU B 122      24.796   4.110  29.146  1.00 75.79           C  
ANISOU 3290  CA  LEU B 122     5187  11745  11865    653   3162   2433       C  
ATOM   3291  C   LEU B 122      23.628   3.530  28.358  1.00 75.48           C  
ANISOU 3291  C   LEU B 122     5239  11782  11658    685   3178   2400       C  
ATOM   3292  O   LEU B 122      22.489   3.529  28.838  1.00 73.27           O  
ANISOU 3292  O   LEU B 122     4994  11509  11334    677   3215   2308       O  
ATOM   3293  CB  LEU B 122      25.013   5.583  28.801  1.00 77.91           C  
ANISOU 3293  CB  LEU B 122     5359  11908  12334    656   3163   2510       C  
ATOM   3294  CG  LEU B 122      25.970   6.340  29.724  1.00 79.01           C  
ANISOU 3294  CG  LEU B 122     5401  11958  12662    604   3160   2514       C  
ATOM   3295  CD1 LEU B 122      26.124   7.784  29.273  1.00 80.16           C  
ANISOU 3295  CD1 LEU B 122     5464  11988  13003    605   3176   2587       C  
ATOM   3296  CD2 LEU B 122      25.495   6.267  31.167  1.00 75.88           C  
ANISOU 3296  CD2 LEU B 122     5042  11529  12259    544   3171   2374       C  
ATOM   3297  N   LEU B 123      23.888   3.032  27.147  1.00 81.00           N  
ANISOU 3297  N   LEU B 123     5971  12540  12264    715   3153   2466       N  
ATOM   3298  CA  LEU B 123      22.833   2.377  26.378  1.00 72.70           C  
ANISOU 3298  CA  LEU B 123     5002  11575  11044    731   3166   2427       C  
ATOM   3299  C   LEU B 123      22.348   1.115  27.079  1.00 71.87           C  
ANISOU 3299  C   LEU B 123     4997  11535  10776    707   3192   2300       C  
ATOM   3300  O   LEU B 123      21.140   0.880  27.200  1.00 82.92           O  
ANISOU 3300  O   LEU B 123     6448  12973  12083    699   3222   2210       O  
ATOM   3301  CB  LEU B 123      23.328   2.055  24.968  1.00 77.67           C  
ANISOU 3301  CB  LEU B 123     5646  12256  11611    753   3143   2519       C  
ATOM   3302  CG  LEU B 123      22.269   1.506  24.009  1.00 72.36           C  
ANISOU 3302  CG  LEU B 123     5039  11679  10777    761   3153   2492       C  
ATOM   3303  CD1 LEU B 123      21.267   2.588  23.638  1.00 72.95           C  
ANISOU 3303  CD1 LEU B 123     5057  11741  10920    789   3157   2534       C  
ATOM   3304  CD2 LEU B 123      22.915   0.918  22.763  1.00 72.34           C  
ANISOU 3304  CD2 LEU B 123     5063  11731  10691    764   3141   2560       C  
ATOM   3305  N   GLY B 124      23.280   0.289  27.549  1.00 71.62           N  
ANISOU 3305  N   GLY B 124     4990  11514  10707    695   3186   2295       N  
ATOM   3306  CA  GLY B 124      22.926  -0.941  28.234  1.00 70.95           C  
ANISOU 3306  CA  GLY B 124     5006  11482  10469    676   3220   2190       C  
ATOM   3307  C   GLY B 124      22.413  -0.770  29.648  1.00 74.96           C  
ANISOU 3307  C   GLY B 124     5517  11964  11001    646   3258   2102       C  
ATOM   3308  O   GLY B 124      21.890  -1.728  30.225  1.00 78.67           O  
ANISOU 3308  O   GLY B 124     6083  12477  11330    627   3300   2006       O  
ATOM   3309  N   PHE B 125      22.555   0.425  30.215  1.00 72.85           N  
ANISOU 3309  N   PHE B 125     5152  11619  10908    635   3253   2128       N  
ATOM   3310  CA  PHE B 125      22.124   0.707  31.576  1.00 75.60           C  
ANISOU 3310  CA  PHE B 125     5493  11932  11301    594   3299   2043       C  
ATOM   3311  C   PHE B 125      20.855   1.541  31.666  1.00 75.71           C  
ANISOU 3311  C   PHE B 125     5497  11905  11366    584   3339   1973       C  
ATOM   3312  O   PHE B 125      20.111   1.402  32.638  1.00 76.28           O  
ANISOU 3312  O   PHE B 125     5666  11940  11377    535   3351   1827       O  
ATOM   3313  CB  PHE B 125      23.249   1.424  32.337  1.00 81.42           C  
ANISOU 3313  CB  PHE B 125     6204  12558  12173    552   3208   2050       C  
ATOM   3314  CG  PHE B 125      22.917   1.744  33.765  1.00 89.70           C  
ANISOU 3314  CG  PHE B 125     7355  13510  13217    471   3166   1892       C  
ATOM   3315  CD1 PHE B 125      22.869   0.744  34.722  1.00 93.64           C  
ANISOU 3315  CD1 PHE B 125     8002  14024  13553    430   3136   1782       C  
ATOM   3316  CD2 PHE B 125      22.669   3.050  34.153  1.00 94.67           C  
ANISOU 3316  CD2 PHE B 125     7935  14030  14005    433   3164   1855       C  
ATOM   3317  CE1 PHE B 125      22.567   1.041  36.038  1.00 98.29           C  
ANISOU 3317  CE1 PHE B 125     8692  14530  14125    344   3100   1635       C  
ATOM   3318  CE2 PHE B 125      22.367   3.354  35.466  1.00 99.28           C  
ANISOU 3318  CE2 PHE B 125     8614  14525  14581    346   3136   1700       C  
ATOM   3319  CZ  PHE B 125      22.317   2.348  36.410  1.00101.11           C  
ANISOU 3319  CZ  PHE B 125     8997  14783  14638    298   3101   1589       C  
ATOM   3320  N   LEU B 126      20.585   2.399  30.680  1.00 78.01           N  
ANISOU 3320  N   LEU B 126     5733  12167  11739    618   3314   2039       N  
ATOM   3321  CA  LEU B 126      19.408   3.255  30.698  1.00 78.85           C  
ANISOU 3321  CA  LEU B 126     5812  12231  11916    623   3350   1991       C  
ATOM   3322  C   LEU B 126      18.346   2.874  29.677  1.00 82.15           C  
ANISOU 3322  C   LEU B 126     6279  12732  12203    657   3344   1974       C  
ATOM   3323  O   LEU B 126      17.176   3.210  29.881  1.00 82.31           O  
ANISOU 3323  O   LEU B 126     6297  12746  12232    656   3383   1898       O  
ATOM   3324  CB  LEU B 126      19.811   4.718  30.458  1.00 77.69           C  
ANISOU 3324  CB  LEU B 126     5548  11974  11995    640   3337   2089       C  
ATOM   3325  CG  LEU B 126      20.807   5.346  31.434  1.00 74.29           C  
ANISOU 3325  CG  LEU B 126     5047  11447  11734    593   3345   2099       C  
ATOM   3326  CD1 LEU B 126      21.125   6.774  31.023  1.00 75.31           C  
ANISOU 3326  CD1 LEU B 126     5072  11462  12079    609   3341   2191       C  
ATOM   3327  CD2 LEU B 126      20.260   5.306  32.850  1.00 74.34           C  
ANISOU 3327  CD2 LEU B 126     5168  11376  11700    513   3338   1905       C  
ATOM   3328  N   VAL B 127      18.715   2.196  28.594  1.00 86.23           N  
ANISOU 3328  N   VAL B 127     6832  13327  12606    680   3303   2038       N  
ATOM   3329  CA  VAL B 127      17.809   1.916  27.486  1.00 84.23           C  
ANISOU 3329  CA  VAL B 127     6606  13158  12240    703   3293   2039       C  
ATOM   3330  C   VAL B 127      17.448   0.436  27.417  1.00 74.65           C  
ANISOU 3330  C   VAL B 127     5513  12042  10808    672   3309   1934       C  
ATOM   3331  O   VAL B 127      16.270   0.077  27.374  1.00 70.76           O  
ANISOU 3331  O   VAL B 127     5064  11605  10217    656   3337   1833       O  
ATOM   3332  CB  VAL B 127      18.408   2.402  26.147  1.00 72.29           C  
ANISOU 3332  CB  VAL B 127     5038  11655  10774    746   3245   2197       C  
ATOM   3333  CG1 VAL B 127      17.542   1.949  24.982  1.00 72.17           C  
ANISOU 3333  CG1 VAL B 127     5055  11749  10619    760   3236   2200       C  
ATOM   3334  CG2 VAL B 127      18.558   3.916  26.151  1.00 73.27           C  
ANISOU 3334  CG2 VAL B 127     5050  11675  11114    778   3241   2297       C  
ATOM   3335  N   MET B 128      18.454  -0.437  27.399  1.00 70.56           N  
ANISOU 3335  N   MET B 128     5047  11540  10221    660   3297   1953       N  
ATOM   3336  CA  MET B 128      18.189  -1.867  27.269  1.00 73.38           C  
ANISOU 3336  CA  MET B 128     5525  11974  10382    629   3322   1859       C  
ATOM   3337  C   MET B 128      17.335  -2.439  28.399  1.00 72.15           C  
ANISOU 3337  C   MET B 128     5449  11825  10140    588   3381   1704       C  
ATOM   3338  O   MET B 128      16.446  -3.256  28.102  1.00 73.03           O  
ANISOU 3338  O   MET B 128     5645  12001  10103    558   3410   1599       O  
ATOM   3339  CB  MET B 128      19.516  -2.626  27.141  1.00 69.63           C  
ANISOU 3339  CB  MET B 128     5080  11495   9879    633   3305   1918       C  
ATOM   3340  CG  MET B 128      20.288  -2.293  25.873  1.00 69.96           C  
ANISOU 3340  CG  MET B 128     5067  11544   9971    662   3260   2050       C  
ATOM   3341  SD  MET B 128      21.855  -3.172  25.746  1.00 69.84           S  
ANISOU 3341  SD  MET B 128     5075  11518   9943    668   3248   2111       S  
ATOM   3342  CE  MET B 128      21.307  -4.855  25.992  1.00 75.35           C  
ANISOU 3342  CE  MET B 128     5926  12273  10431    631   3304   1969       C  
ATOM   3343  N   PRO B 129      17.536  -2.090  29.677  1.00 69.60           N  
ANISOU 3343  N   PRO B 129     5109  11442   9895    575   3409   1675       N  
ATOM   3344  CA  PRO B 129      16.598  -2.580  30.702  1.00 73.16           C  
ANISOU 3344  CA  PRO B 129     5642  11901  10254    531   3479   1522       C  
ATOM   3345  C   PRO B 129      15.178  -2.076  30.507  1.00 80.21           C  
ANISOU 3345  C   PRO B 129     6515  12810  11149    522   3502   1437       C  
ATOM   3346  O   PRO B 129      14.224  -2.802  30.813  1.00 79.99           O  
ANISOU 3346  O   PRO B 129     6578  12824  10990    481   3553   1296       O  
ATOM   3347  CB  PRO B 129      17.210  -2.070  32.015  1.00 69.98           C  
ANISOU 3347  CB  PRO B 129     5200  11425   9966    518   3504   1536       C  
ATOM   3348  CG  PRO B 129      18.113  -0.956  31.615  1.00 72.34           C  
ANISOU 3348  CG  PRO B 129     5367  11665  10454    553   3445   1678       C  
ATOM   3349  CD  PRO B 129      18.661  -1.358  30.286  1.00 73.53           C  
ANISOU 3349  CD  PRO B 129     5521  11864  10554    589   3387   1770       C  
ATOM   3350  N   VAL B 130      15.005  -0.852  30.005  1.00 88.62           N  
ANISOU 3350  N   VAL B 130     7464  13841  12366    560   3469   1518       N  
ATOM   3351  CA  VAL B 130      13.661  -0.364  29.710  1.00 70.43           C  
ANISOU 3351  CA  VAL B 130     5124  11560  10075    566   3487   1456       C  
ATOM   3352  C   VAL B 130      13.047  -1.153  28.560  1.00 70.11           C  
ANISOU 3352  C   VAL B 130     5131  11630   9879    563   3467   1432       C  
ATOM   3353  O   VAL B 130      11.845  -1.441  28.557  1.00 70.08           O  
ANISOU 3353  O   VAL B 130     5153  11676   9797    537   3501   1313       O  
ATOM   3354  CB  VAL B 130      13.695   1.146  29.413  1.00 71.32           C  
ANISOU 3354  CB  VAL B 130     5099  11600  10398    619   3459   1570       C  
ATOM   3355  CG1 VAL B 130      12.292   1.669  29.151  1.00 71.80           C  
ANISOU 3355  CG1 VAL B 130     5110  11684  10485    637   3479   1515       C  
ATOM   3356  CG2 VAL B 130      14.332   1.894  30.571  1.00 71.70           C  
ANISOU 3356  CG2 VAL B 130     5104  11529  10609    604   3489   1577       C  
ATOM   3357  N   SER B 131      13.862  -1.536  27.574  1.00 76.52           N  
ANISOU 3357  N   SER B 131     5952  12478  10646    580   3419   1535       N  
ATOM   3358  CA  SER B 131      13.364  -2.395  26.504  1.00 76.20           C  
ANISOU 3358  CA  SER B 131     5965  12535  10450    561   3411   1502       C  
ATOM   3359  C   SER B 131      12.980  -3.771  27.039  1.00 80.63           C  
ANISOU 3359  C   SER B 131     6668  13127  10841    492   3468   1336       C  
ATOM   3360  O   SER B 131      12.014  -4.382  26.566  1.00 68.95           O  
ANISOU 3360  O   SER B 131     5236  11715   9247    454   3490   1236       O  
ATOM   3361  CB  SER B 131      14.409  -2.514  25.396  1.00 69.74           C  
ANISOU 3361  CB  SER B 131     5133  11738   9628    586   3361   1641       C  
ATOM   3362  OG  SER B 131      13.894  -3.229  24.286  1.00 69.66           O  
ANISOU 3362  OG  SER B 131     5164  11822   9481    561   3359   1614       O  
ATOM   3363  N   MET B 132      13.726  -4.273  28.026  1.00 68.61           N  
ANISOU 3363  N   MET B 132     5213  11552   9304    475   3494   1309       N  
ATOM   3364  CA  MET B 132      13.354  -5.530  28.669  1.00 68.06           C  
ANISOU 3364  CA  MET B 132     5285  11496   9078    413   3558   1157       C  
ATOM   3365  C   MET B 132      12.024  -5.398  29.401  1.00 82.28           C  
ANISOU 3365  C   MET B 132     7107  13302  10854    373   3615   1004       C  
ATOM   3366  O   MET B 132      11.176  -6.295  29.336  1.00 79.90           O  
ANISOU 3366  O   MET B 132     6902  13038  10419    314   3662    863       O  
ATOM   3367  CB  MET B 132      14.455  -5.966  29.635  1.00 67.85           C  
ANISOU 3367  CB  MET B 132     5312  11416   9052    417   3575   1187       C  
ATOM   3368  CG  MET B 132      14.204  -7.300  30.315  1.00 81.72           C  
ANISOU 3368  CG  MET B 132     7226  13178  10644    361   3645   1052       C  
ATOM   3369  SD  MET B 132      15.605  -7.825  31.321  1.00 95.19           S  
ANISOU 3369  SD  MET B 132     8980  14837  12352    385   3659   1130       S  
ATOM   3370  CE  MET B 132      15.454  -6.710  32.713  1.00103.78           C  
ANISOU 3370  CE  MET B 132    10000  15873  13558    388   3685   1127       C  
ATOM   3371  N   LEU B 133      11.836  -4.290  30.119  1.00 78.02           N  
ANISOU 3371  N   LEU B 133     6480  12713  10452    397   3621   1022       N  
ATOM   3372  CA  LEU B 133      10.549  -4.026  30.755  1.00 77.29           C  
ANISOU 3372  CA  LEU B 133     6387  12621  10358    364   3679    880       C  
ATOM   3373  C   LEU B 133       9.428  -3.974  29.724  1.00 79.72           C  
ANISOU 3373  C   LEU B 133     6653  13003  10635    362   3664    840       C  
ATOM   3374  O   LEU B 133       8.316  -4.454  29.976  1.00 82.36           O  
ANISOU 3374  O   LEU B 133     7041  13367  10885    308   3720    681       O  
ATOM   3375  CB  LEU B 133      10.612  -2.719  31.543  1.00 69.39           C  
ANISOU 3375  CB  LEU B 133     5282  11539   9544    395   3689    923       C  
ATOM   3376  CG  LEU B 133       9.331  -2.316  32.274  1.00 69.76           C  
ANISOU 3376  CG  LEU B 133     5315  11569   9619    363   3758    776       C  
ATOM   3377  CD1 LEU B 133       9.062  -3.267  33.427  1.00 71.75           C  
ANISOU 3377  CD1 LEU B 133     5715  11814   9733    287   3845    615       C  
ATOM   3378  CD2 LEU B 133       9.410  -0.878  32.761  1.00 70.53           C  
ANISOU 3378  CD2 LEU B 133     5290  11567   9940    401   3764    838       C  
ATOM   3379  N   THR B 134       9.706  -3.391  28.556  1.00 78.59           N  
ANISOU 3379  N   THR B 134     6411  12891  10559    419   3594    985       N  
ATOM   3380  CA  THR B 134       8.706  -3.322  27.494  1.00 77.65           C  
ANISOU 3380  CA  THR B 134     6240  12856  10407    426   3576    976       C  
ATOM   3381  C   THR B 134       8.336  -4.714  26.995  1.00 84.64           C  
ANISOU 3381  C   THR B 134     7248  13802  11108    355   3606    864       C  
ATOM   3382  O   THR B 134       7.151  -5.048  26.876  1.00 86.33           O  
ANISOU 3382  O   THR B 134     7480  14060  11263    314   3645    740       O  
ATOM   3383  CB  THR B 134       9.226  -2.458  26.344  1.00 70.32           C  
ANISOU 3383  CB  THR B 134     5194  11950   9572    501   3498   1175       C  
ATOM   3384  OG1 THR B 134       9.297  -1.092  26.769  1.00 70.97           O  
ANISOU 3384  OG1 THR B 134     5160  11960   9847    562   3484   1262       O  
ATOM   3385  CG2 THR B 134       8.310  -2.561  25.135  1.00 70.76           C  
ANISOU 3385  CG2 THR B 134     5207  12116   9564    506   3477   1185       C  
ATOM   3386  N   ILE B 135       9.339  -5.547  26.701  1.00 87.50           N  
ANISOU 3386  N   ILE B 135     7698  14157  11391    338   3595    903       N  
ATOM   3387  CA  ILE B 135       9.045  -6.898  26.233  1.00 87.78           C  
ANISOU 3387  CA  ILE B 135     7860  14225  11268    266   3636    794       C  
ATOM   3388  C   ILE B 135       8.411  -7.743  27.333  1.00 86.94           C  
ANISOU 3388  C   ILE B 135     7883  14072  11077    191   3725    602       C  
ATOM   3389  O   ILE B 135       7.780  -8.764  27.036  1.00 89.34           O  
ANISOU 3389  O   ILE B 135     8293  14380  11273    124   3781    482       O  
ATOM   3390  CB  ILE B 135      10.299  -7.600  25.672  1.00 88.06           C  
ANISOU 3390  CB  ILE B 135     7955  14252  11253    267   3613    877       C  
ATOM   3391  CG1 ILE B 135      11.227  -8.057  26.801  1.00 81.91           C  
ANISOU 3391  CG1 ILE B 135     7258  13398  10467    262   3639    864       C  
ATOM   3392  CG2 ILE B 135      11.026  -6.700  24.681  1.00 91.13           C  
ANISOU 3392  CG2 ILE B 135     8220  14671  11734    339   3534   1071       C  
ATOM   3393  CD1 ILE B 135      12.490  -8.732  26.316  1.00 72.61           C  
ANISOU 3393  CD1 ILE B 135     6125  12206   9256    272   3620    948       C  
ATOM   3394  N   LEU B 136       8.561  -7.347  28.600  1.00 82.78           N  
ANISOU 3394  N   LEU B 136     7360  13491  10601    198   3750    572       N  
ATOM   3395  CA  LEU B 136       7.870  -8.045  29.679  1.00 79.76           C  
ANISOU 3395  CA  LEU B 136     7101  13067  10135    125   3842    389       C  
ATOM   3396  C   LEU B 136       6.403  -7.644  29.779  1.00 83.00           C  
ANISOU 3396  C   LEU B 136     7469  13490  10578    100   3886    270       C  
ATOM   3397  O   LEU B 136       5.571  -8.457  30.196  1.00 89.34           O  
ANISOU 3397  O   LEU B 136     8395  14245  11305     31   3979    114       O  
ATOM   3398  CB  LEU B 136       8.576  -7.793  31.012  1.00 75.51           C  
ANISOU 3398  CB  LEU B 136     6587  12478   9626    137   3859    403       C  
ATOM   3399  CG  LEU B 136       9.742  -8.732  31.326  1.00 70.02           C  
ANISOU 3399  CG  LEU B 136     6004  11754   8847    132   3863    447       C  
ATOM   3400  CD1 LEU B 136      10.257  -8.498  32.737  1.00 67.14           C  
ANISOU 3400  CD1 LEU B 136     5668  11343   8501    141   3896    455       C  
ATOM   3401  CD2 LEU B 136       9.319 -10.180  31.141  1.00 69.88           C  
ANISOU 3401  CD2 LEU B 136     6152  11729   8672     52   3927    310       C  
ATOM   3402  N   TYR B 137       6.066  -6.406  29.408  1.00 76.21           N  
ANISOU 3402  N   TYR B 137     6441  12669   9846    163   3833    353       N  
ATOM   3403  CA  TYR B 137       4.691  -5.921  29.445  1.00 71.22           C  
ANISOU 3403  CA  TYR B 137     5738  12056   9265    155   3870    257       C  
ATOM   3404  C   TYR B 137       3.953  -6.136  28.130  1.00 73.27           C  
ANISOU 3404  C   TYR B 137     5956  12389   9495    161   3847    279       C  
ATOM   3405  O   TYR B 137       3.005  -5.398  27.829  1.00 73.52           O  
ANISOU 3405  O   TYR B 137     5864  12467   9605    194   3837    279       O  
ATOM   3406  CB  TYR B 137       4.660  -4.442  29.835  1.00 69.88           C  
ANISOU 3406  CB  TYR B 137     5407  11880   9263    225   3834    334       C  
ATOM   3407  CG  TYR B 137       4.572  -4.194  31.324  1.00 70.69           C  
ANISOU 3407  CG  TYR B 137     5545  11919   9395    193   3900    226       C  
ATOM   3408  CD1 TYR B 137       5.696  -4.276  32.135  1.00 73.27           C  
ANISOU 3408  CD1 TYR B 137     5934  12189   9715    194   3902    278       C  
ATOM   3409  CD2 TYR B 137       3.358  -3.874  31.919  1.00 76.08           C  
ANISOU 3409  CD2 TYR B 137     6193  12605  10109    162   3964     76       C  
ATOM   3410  CE1 TYR B 137       5.611  -4.048  33.498  1.00 77.38           C  
ANISOU 3410  CE1 TYR B 137     6491  12659  10249    164   3967    191       C  
ATOM   3411  CE2 TYR B 137       3.265  -3.645  33.278  1.00 79.98           C  
ANISOU 3411  CE2 TYR B 137     6716  13080  10592    132   4014    -19       C  
ATOM   3412  CZ  TYR B 137       4.393  -3.733  34.063  1.00 79.38           C  
ANISOU 3412  CZ  TYR B 137     6716  12939  10507    135   4019     48       C  
ATOM   3413  OH  TYR B 137       4.301  -3.504  35.417  1.00 79.10           O  
ANISOU 3413  OH  TYR B 137     6741  12833  10482    121   4081     -8       O  
ATOM   3414  N   GLY B 138       4.357  -7.128  27.340  1.00 77.16           N  
ANISOU 3414  N   GLY B 138     6543  12899   9877    132   3841    301       N  
ATOM   3415  CA  GLY B 138       3.716  -7.367  26.058  1.00 82.76           C  
ANISOU 3415  CA  GLY B 138     7213  13691  10542    133   3819    331       C  
ATOM   3416  C   GLY B 138       3.858  -6.230  25.074  1.00 85.25           C  
ANISOU 3416  C   GLY B 138     7345  14109  10939    218   3718    507       C  
ATOM   3417  O   GLY B 138       2.932  -5.970  24.298  1.00 89.89           O  
ANISOU 3417  O   GLY B 138     7841  14786  11528    236   3700    523       O  
ATOM   3418  N   TYR B 139       4.994  -5.530  25.099  1.00 85.75           N  
ANISOU 3418  N   TYR B 139     7351  14152  11076    278   3656    653       N  
ATOM   3419  CA  TYR B 139       5.277  -4.393  24.225  1.00 70.99           C  
ANISOU 3419  CA  TYR B 139     5325  12343   9306    369   3570    849       C  
ATOM   3420  C   TYR B 139       4.308  -3.236  24.448  1.00 71.90           C  
ANISOU 3420  C   TYR B 139     5292  12474   9551    426   3562    862       C  
ATOM   3421  O   TYR B 139       4.166  -2.364  23.585  1.00 73.48           O  
ANISOU 3421  O   TYR B 139     5358  12739   9822    502   3501   1015       O  
ATOM   3422  CB  TYR B 139       5.286  -4.814  22.750  1.00 71.29           C  
ANISOU 3422  CB  TYR B 139     5352  12489   9247    366   3531    932       C  
ATOM   3423  CG  TYR B 139       6.235  -5.956  22.464  1.00 70.52           C  
ANISOU 3423  CG  TYR B 139     5395  12364   9035    309   3547    914       C  
ATOM   3424  CD1 TYR B 139       7.609  -5.754  22.440  1.00 70.20           C  
ANISOU 3424  CD1 TYR B 139     5360  12275   9036    343   3509   1037       C  
ATOM   3425  CD2 TYR B 139       5.757  -7.239  22.231  1.00 71.83           C  
ANISOU 3425  CD2 TYR B 139     5687  12540   9067    223   3608    775       C  
ATOM   3426  CE1 TYR B 139       8.480  -6.797  22.185  1.00 71.45           C  
ANISOU 3426  CE1 TYR B 139     5637  12407   9104    296   3527   1018       C  
ATOM   3427  CE2 TYR B 139       6.620  -8.288  21.975  1.00 72.33           C  
ANISOU 3427  CE2 TYR B 139     5878  12562   9043    174   3633    756       C  
ATOM   3428  CZ  TYR B 139       7.980  -8.061  21.954  1.00 73.35           C  
ANISOU 3428  CZ  TYR B 139     6000  12655   9213    211   3590    875       C  
ATOM   3429  OH  TYR B 139       8.843  -9.103  21.699  1.00 74.22           O  
ANISOU 3429  OH  TYR B 139     6228  12726   9248    165   3618    853       O  
ATOM   3430  N   ARG B 140       3.641  -3.217  25.599  1.00 71.80           N  
ANISOU 3430  N   ARG B 140     5304  12402   9576    393   3629    707       N  
ATOM   3431  CA  ARG B 140       2.793  -2.107  26.013  1.00 72.68           C  
ANISOU 3431  CA  ARG B 140     5279  12502   9833    445   3635    699       C  
ATOM   3432  C   ARG B 140       3.584  -1.207  26.952  1.00 74.20           C  
ANISOU 3432  C   ARG B 140     5442  12582  10169    486   3634    758       C  
ATOM   3433  O   ARG B 140       4.203  -1.693  27.905  1.00 78.29           O  
ANISOU 3433  O   ARG B 140     6072  13028  10648    435   3675    681       O  
ATOM   3434  CB  ARG B 140       1.531  -2.614  26.713  1.00 79.35           C  
ANISOU 3434  CB  ARG B 140     6167  13342  10641    376   3724    480       C  
ATOM   3435  CG  ARG B 140       0.723  -1.525  27.403  1.00 79.63           C  
ANISOU 3435  CG  ARG B 140     6075  13345  10837    418   3749    436       C  
ATOM   3436  CD  ARG B 140      -0.238  -0.841  26.448  1.00 80.63           C  
ANISOU 3436  CD  ARG B 140     6035  13568  11034    490   3704    517       C  
ATOM   3437  NE  ARG B 140      -1.353  -1.712  26.088  1.00 74.95           N  
ANISOU 3437  NE  ARG B 140     5347  12923  10210    431   3747    387       N  
ATOM   3438  CZ  ARG B 140      -2.389  -1.331  25.347  1.00 78.85           C  
ANISOU 3438  CZ  ARG B 140     5702  13520  10739    478   3720    421       C  
ATOM   3439  NH1 ARG B 140      -2.455  -0.091  24.884  1.00 77.18           N  
ANISOU 3439  NH1 ARG B 140     5314  13345  10666    589   3651    584       N  
ATOM   3440  NH2 ARG B 140      -3.359  -2.191  25.070  1.00 82.69           N  
ANISOU 3440  NH2 ARG B 140     6228  14063  11128    421   3764    309       N  
ATOM   3441  N   TRP B 141       3.570   0.088  26.681  1.00 73.91           N  
ANISOU 3441  N   TRP B 141     5259  12523  10302    578   3591    902       N  
ATOM   3442  CA  TRP B 141       4.333   1.024  27.492  1.00 80.74           C  
ANISOU 3442  CA  TRP B 141     6091  13257  11330    617   3596    971       C  
ATOM   3443  C   TRP B 141       3.689   1.179  28.864  1.00 86.77           C  
ANISOU 3443  C   TRP B 141     6873  13946  12149    575   3681    795       C  
ATOM   3444  O   TRP B 141       2.586   1.735  28.956  1.00 83.75           O  
ANISOU 3444  O   TRP B 141     6398  13574  11850    599   3707    737       O  
ATOM   3445  CB  TRP B 141       4.433   2.378  26.793  1.00 82.45           C  
ANISOU 3445  CB  TRP B 141     6155  13446  11728    725   3541   1173       C  
ATOM   3446  CG  TRP B 141       5.342   3.341  27.490  1.00 80.54           C  
ANISOU 3446  CG  TRP B 141     5886  13049  11668    758   3548   1258       C  
ATOM   3447  CD1 TRP B 141       4.983   4.491  28.129  1.00 77.85           C  
ANISOU 3447  CD1 TRP B 141     5456  12591  11533    800   3584   1262       C  
ATOM   3448  CD2 TRP B 141       6.765   3.237  27.620  1.00 81.52           C  
ANISOU 3448  CD2 TRP B 141     6069  13109  11794    747   3525   1346       C  
ATOM   3449  NE1 TRP B 141       6.095   5.111  28.650  1.00 76.75           N  
ANISOU 3449  NE1 TRP B 141     5322  12314  11525    807   3589   1342       N  
ATOM   3450  CE2 TRP B 141       7.201   4.361  28.350  1.00 80.28           C  
ANISOU 3450  CE2 TRP B 141     5854  12800  11850    776   3549   1396       C  
ATOM   3451  CE3 TRP B 141       7.712   2.303  27.190  1.00 78.71           C  
ANISOU 3451  CE3 TRP B 141     5808  12806  11294    713   3491   1382       C  
ATOM   3452  CZ2 TRP B 141       8.543   4.575  28.659  1.00 79.86           C  
ANISOU 3452  CZ2 TRP B 141     5826  12655  11861    769   3536   1481       C  
ATOM   3453  CZ3 TRP B 141       9.042   2.517  27.497  1.00 73.20           C  
ANISOU 3453  CZ3 TRP B 141     5132  12020  10662    715   3475   1471       C  
ATOM   3454  CH2 TRP B 141       9.446   3.644  28.224  1.00 74.45           C  
ANISOU 3454  CH2 TRP B 141     5224  12038  11027    741   3496   1520       C  
ATOM   3455  N   PRO B 142       4.321   0.710  29.943  1.00 93.11           N  
ANISOU 3455  N   PRO B 142     7789  14679  12908    513   3730    709       N  
ATOM   3456  CA  PRO B 142       3.715   0.820  31.273  1.00 95.32           C  
ANISOU 3456  CA  PRO B 142     8101  14894  13223    464   3820    539       C  
ATOM   3457  C   PRO B 142       4.054   2.106  32.009  1.00 95.46           C  
ANISOU 3457  C   PRO B 142     8041  14760  13468    506   3844    601       C  
ATOM   3458  O   PRO B 142       3.422   2.397  33.034  1.00 99.23           O  
ANISOU 3458  O   PRO B 142     8528  15165  14009    471   3925    466       O  
ATOM   3459  CB  PRO B 142       4.296  -0.399  32.007  1.00 95.52           C  
ANISOU 3459  CB  PRO B 142     8300  14921  13071    376   3862    436       C  
ATOM   3460  CG  PRO B 142       5.587  -0.743  31.261  1.00 95.72           C  
ANISOU 3460  CG  PRO B 142     8356  14958  13054    403   3788    598       C  
ATOM   3461  CD  PRO B 142       5.657   0.096  30.007  1.00 95.21           C  
ANISOU 3461  CD  PRO B 142     8156  14921  13097    491   3706    776       C  
ATOM   3462  N   LEU B 143       5.023   2.866  31.519  1.00 90.50           N  
ANISOU 3462  N   LEU B 143     7347  14070  12968    570   3785    790       N  
ATOM   3463  CA  LEU B 143       5.548   4.048  32.188  1.00 85.88           C  
ANISOU 3463  CA  LEU B 143     6702  13318  12610    594   3812    851       C  
ATOM   3464  C   LEU B 143       4.806   5.293  31.718  1.00 88.53           C  
ANISOU 3464  C   LEU B 143     6889  13604  13143    677   3803    923       C  
ATOM   3465  O   LEU B 143       3.949   5.220  30.832  1.00 91.59           O  
ANISOU 3465  O   LEU B 143     7213  14103  13483    722   3767    945       O  
ATOM   3466  CB  LEU B 143       7.049   4.146  31.912  1.00 85.02           C  
ANISOU 3466  CB  LEU B 143     6605  13170  12529    611   3756   1012       C  
ATOM   3467  CG  LEU B 143       7.871   2.987  32.482  1.00 87.49           C  
ANISOU 3467  CG  LEU B 143     7056  13513  12674    539   3769    954       C  
ATOM   3468  CD1 LEU B 143       9.300   3.010  31.954  1.00 84.27           C  
ANISOU 3468  CD1 LEU B 143     6640  13096  12282    567   3697   1125       C  
ATOM   3469  CD2 LEU B 143       7.850   3.016  34.002  1.00 93.83           C  
ANISOU 3469  CD2 LEU B 143     7923  14204  13523    464   3870    809       C  
ATOM   3470  N   PRO B 144       5.078   6.458  32.318  1.00 90.68           N  
ANISOU 3470  N   PRO B 144     7102  13703  13648    695   3844    956       N  
ATOM   3471  CA  PRO B 144       4.437   7.693  31.849  1.00 93.51           C  
ANISOU 3471  CA  PRO B 144     7321  13994  14214    785   3839   1043       C  
ATOM   3472  C   PRO B 144       4.694   7.968  30.372  1.00 90.49           C  
ANISOU 3472  C   PRO B 144     6856  13699  13825    880   3740   1261       C  
ATOM   3473  O   PRO B 144       5.613   7.426  29.754  1.00 77.77           O  
ANISOU 3473  O   PRO B 144     5292  12160  12095    875   3676   1361       O  
ATOM   3474  CB  PRO B 144       5.068   8.773  32.732  1.00 93.46           C  
ANISOU 3474  CB  PRO B 144     7294  13769  14447    768   3901   1051       C  
ATOM   3475  CG  PRO B 144       5.366   8.068  34.002  1.00 78.02           C  
ANISOU 3475  CG  PRO B 144     5465  11772  12408    650   3974    872       C  
ATOM   3476  CD  PRO B 144       5.719   6.648  33.634  1.00 76.68           C  
ANISOU 3476  CD  PRO B 144     5395  11778  11962    618   3921    866       C  
ATOM   3477  N   SER B 145       3.850   8.839  29.808  1.00 88.83           N  
ANISOU 3477  N   SER B 145     6524  13477  13752    967   3732   1335       N  
ATOM   3478  CA  SER B 145       3.847   9.055  28.363  1.00 96.94           C  
ANISOU 3478  CA  SER B 145     7470  14607  14755   1058   3644   1536       C  
ATOM   3479  C   SER B 145       5.068   9.843  27.897  1.00111.98           C  
ANISOU 3479  C   SER B 145     9349  16414  16785   1104   3609   1742       C  
ATOM   3480  O   SER B 145       5.663   9.516  26.863  1.00117.98           O  
ANISOU 3480  O   SER B 145    10116  17274  17436   1128   3536   1886       O  
ATOM   3481  CB  SER B 145       2.558   9.767  27.950  1.00 94.48           C  
ANISOU 3481  CB  SER B 145     7028  14312  14560   1143   3650   1562       C  
ATOM   3482  OG  SER B 145       1.431   8.929  28.144  1.00 91.75           O  
ANISOU 3482  OG  SER B 145     6696  14093  14071   1100   3670   1383       O  
ATOM   3483  N   LYS B 146       5.449  10.890  28.633  1.00118.15           N  
ANISOU 3483  N   LYS B 146    10100  16996  17798   1110   3666   1754       N  
ATOM   3484  CA  LYS B 146       6.596  11.703  28.234  1.00121.57           C  
ANISOU 3484  CA  LYS B 146    10503  17322  18366   1147   3644   1939       C  
ATOM   3485  C   LYS B 146       7.894  10.904  28.296  1.00118.20           C  
ANISOU 3485  C   LYS B 146    10176  16938  17798   1076   3608   1947       C  
ATOM   3486  O   LYS B 146       8.808  11.112  27.478  1.00119.98           O  
ANISOU 3486  O   LYS B 146    10387  17173  18027   1109   3555   2119       O  
ATOM   3487  CB  LYS B 146       6.683  12.943  29.126  1.00124.95           C  
ANISOU 3487  CB  LYS B 146    10885  17515  19076   1148   3731   1914       C  
ATOM   3488  CG  LYS B 146       5.397  13.766  29.203  1.00127.27           C  
ANISOU 3488  CG  LYS B 146    11082  17737  19536   1217   3782   1890       C  
ATOM   3489  CD  LYS B 146       5.007  14.366  27.855  1.00128.72           C  
ANISOU 3489  CD  LYS B 146    11157  17980  19771   1346   3723   2113       C  
ATOM   3490  CE  LYS B 146       3.818  15.306  27.992  1.00130.99           C  
ANISOU 3490  CE  LYS B 146    11338  18169  20262   1425   3778   2105       C  
ATOM   3491  NZ  LYS B 146       3.498  15.975  26.700  1.00133.67           N  
ANISOU 3491  NZ  LYS B 146    11564  18554  20669   1558   3723   2348       N  
ATOM   3492  N   LEU B 147       7.990   9.987  29.260  1.00110.88           N  
ANISOU 3492  N   LEU B 147     9348  16035  16747    981   3639   1765       N  
ATOM   3493  CA  LEU B 147       9.180   9.160  29.388  1.00101.13           C  
ANISOU 3493  CA  LEU B 147     8204  14842  15379    919   3607   1768       C  
ATOM   3494  C   LEU B 147       9.399   8.290  28.161  1.00 95.05           C  
ANISOU 3494  C   LEU B 147     7465  14246  14403    942   3524   1863       C  
ATOM   3495  O   LEU B 147      10.525   7.852  27.928  1.00 96.42           O  
ANISOU 3495  O   LEU B 147     7688  14440  14507    918   3485   1927       O  
ATOM   3496  CB  LEU B 147       9.094   8.300  30.648  1.00 96.13           C  
ANISOU 3496  CB  LEU B 147     7672  14208  14645    820   3665   1561       C  
ATOM   3497  CG  LEU B 147       9.059   9.092  31.958  1.00 94.54           C  
ANISOU 3497  CG  LEU B 147     7457  13823  14640    770   3760   1451       C  
ATOM   3498  CD1 LEU B 147       9.243   8.171  33.152  1.00 97.31           C  
ANISOU 3498  CD1 LEU B 147     7921  14179  14873    664   3815   1275       C  
ATOM   3499  CD2 LEU B 147      10.108  10.196  31.956  1.00 90.92           C  
ANISOU 3499  CD2 LEU B 147     6935  13215  14395    785   3758   1580       C  
ATOM   3500  N   CYS B 148       8.357   8.044  27.365  1.00 88.74           N  
ANISOU 3500  N   CYS B 148     6632  13570  13513    984   3499   1872       N  
ATOM   3501  CA  CYS B 148       8.544   7.339  26.100  1.00 87.27           C  
ANISOU 3501  CA  CYS B 148     6466  13542  13152   1002   3428   1971       C  
ATOM   3502  C   CYS B 148       9.431   8.143  25.159  1.00 96.11           C  
ANISOU 3502  C   CYS B 148     7525  14621  14373   1065   3383   2199       C  
ATOM   3503  O   CYS B 148      10.394   7.616  24.583  1.00101.43           O  
ANISOU 3503  O   CYS B 148     8249  15346  14944   1046   3341   2274       O  
ATOM   3504  CB  CYS B 148       7.190   7.054  25.454  1.00 85.37           C  
ANISOU 3504  CB  CYS B 148     6181  13437  12817   1031   3416   1938       C  
ATOM   3505  SG  CYS B 148       7.294   6.531  23.732  1.00 86.28           S  
ANISOU 3505  SG  CYS B 148     6285  13736  12761   1064   3336   2097       S  
ATOM   3506  N   ALA B 149       9.110   9.426  24.980  1.00100.29           N  
ANISOU 3506  N   ALA B 149     7945  15051  15108   1142   3398   2313       N  
ATOM   3507  CA  ALA B 149       9.958  10.289  24.168  1.00 94.32           C  
ANISOU 3507  CA  ALA B 149     7133  14236  14470   1200   3371   2532       C  
ATOM   3508  C   ALA B 149      11.350  10.405  24.772  1.00 81.62           C  
ANISOU 3508  C   ALA B 149     5573  12508  12933   1147   3384   2532       C  
ATOM   3509  O   ALA B 149      12.349  10.390  24.045  1.00 79.68           O  
ANISOU 3509  O   ALA B 149     5335  12279  12661   1153   3346   2665       O  
ATOM   3510  CB  ALA B 149       9.317  11.669  24.017  1.00 97.85           C  
ANISOU 3510  CB  ALA B 149     7459  14572  15147   1291   3401   2642       C  
ATOM   3511  N   VAL B 150      11.437  10.499  26.103  1.00 79.47           N  
ANISOU 3511  N   VAL B 150     5327  12121  12745   1089   3439   2382       N  
ATOM   3512  CA  VAL B 150      12.748  10.584  26.749  1.00 79.09           C  
ANISOU 3512  CA  VAL B 150     5314  11972  12765   1032   3449   2374       C  
ATOM   3513  C   VAL B 150      13.580   9.333  26.463  1.00 84.21           C  
ANISOU 3513  C   VAL B 150     6053  12743  13200    983   3396   2361       C  
ATOM   3514  O   VAL B 150      14.784   9.413  26.186  1.00 77.77           O  
ANISOU 3514  O   VAL B 150     5240  11898  12410    973   3370   2455       O  
ATOM   3515  CB  VAL B 150      12.580  10.821  28.262  1.00 79.08           C  
ANISOU 3515  CB  VAL B 150     5327  11846  12875    968   3524   2203       C  
ATOM   3516  CG1 VAL B 150      13.920  10.711  28.974  1.00 78.65           C  
ANISOU 3516  CG1 VAL B 150     5307  11721  12857    895   3528   2181       C  
ATOM   3517  CG2 VAL B 150      11.947  12.180  28.518  1.00 80.50           C  
ANISOU 3517  CG2 VAL B 150     5415  11868  13303   1013   3587   2225       C  
ATOM   3518  N   TRP B 151      12.947   8.160  26.513  1.00 85.17           N  
ANISOU 3518  N   TRP B 151     6248  12998  13114    952   3387   2241       N  
ATOM   3519  CA  TRP B 151      13.658   6.899  26.331  1.00 75.78           C  
ANISOU 3519  CA  TRP B 151     5154  11911  11728    904   3352   2209       C  
ATOM   3520  C   TRP B 151      14.094   6.707  24.883  1.00 79.28           C  
ANISOU 3520  C   TRP B 151     5591  12447  12087    942   3294   2363       C  
ATOM   3521  O   TRP B 151      15.218   6.258  24.620  1.00 82.62           O  
ANISOU 3521  O   TRP B 151     6053  12880  12460    919   3267   2412       O  
ATOM   3522  CB  TRP B 151      12.766   5.750  26.802  1.00 74.93           C  
ANISOU 3522  CB  TRP B 151     5130  11903  11436    857   3374   2030       C  
ATOM   3523  CG  TRP B 151      13.229   4.382  26.429  1.00 73.89           C  
ANISOU 3523  CG  TRP B 151     5101  11884  11090    816   3346   1995       C  
ATOM   3524  CD1 TRP B 151      14.333   3.732  26.893  1.00 75.93           C  
ANISOU 3524  CD1 TRP B 151     5425  12123  11300    774   3341   1977       C  
ATOM   3525  CD2 TRP B 151      12.572   3.474  25.538  1.00 73.52           C  
ANISOU 3525  CD2 TRP B 151     5100  11981  10854    811   3327   1966       C  
ATOM   3526  NE1 TRP B 151      14.416   2.480  26.332  1.00 73.24           N  
ANISOU 3526  NE1 TRP B 151     5174  11895  10760    748   3323   1942       N  
ATOM   3527  CE2 TRP B 151      13.345   2.298  25.497  1.00 72.61           C  
ANISOU 3527  CE2 TRP B 151     5086  11912  10589    763   3317   1928       C  
ATOM   3528  CE3 TRP B 151      11.411   3.545  24.765  1.00 73.99           C  
ANISOU 3528  CE3 TRP B 151     5117  12133  10862    840   3319   1970       C  
ATOM   3529  CZ2 TRP B 151      12.993   1.202  24.714  1.00 74.11           C  
ANISOU 3529  CZ2 TRP B 151     5347  12225  10587    736   3308   1883       C  
ATOM   3530  CZ3 TRP B 151      11.063   2.457  23.987  1.00 73.51           C  
ANISOU 3530  CZ3 TRP B 151     5120  12209  10602    809   3304   1927       C  
ATOM   3531  CH2 TRP B 151      11.851   1.301  23.967  1.00 72.58           C  
ANISOU 3531  CH2 TRP B 151     5113  12120  10343    754   3302   1878       C  
ATOM   3532  N   ILE B 152      13.222   7.046  23.929  1.00 77.57           N  
ANISOU 3532  N   ILE B 152     5318  12300  11855    999   3279   2444       N  
ATOM   3533  CA  ILE B 152      13.625   6.999  22.525  1.00 83.72           C  
ANISOU 3533  CA  ILE B 152     6079  13164  12566   1033   3234   2608       C  
ATOM   3534  C   ILE B 152      14.762   7.983  22.274  1.00 93.70           C  
ANISOU 3534  C   ILE B 152     7291  14312  14001   1062   3229   2769       C  
ATOM   3535  O   ILE B 152      15.693   7.703  21.505  1.00 99.65           O  
ANISOU 3535  O   ILE B 152     8065  15101  14696   1054   3202   2864       O  
ATOM   3536  CB  ILE B 152      12.417   7.268  21.608  1.00 82.18           C  
ANISOU 3536  CB  ILE B 152     5817  13073  12334   1092   3220   2677       C  
ATOM   3537  CG1 ILE B 152      11.354   6.184  21.800  1.00 82.07           C  
ANISOU 3537  CG1 ILE B 152     5860  13184  12138   1049   3226   2503       C  
ATOM   3538  CG2 ILE B 152      12.850   7.327  20.150  1.00 78.20           C  
ANISOU 3538  CG2 ILE B 152     5287  12659  11767   1126   3181   2865       C  
ATOM   3539  CD1 ILE B 152      10.186   6.293  20.843  1.00 83.33           C  
ANISOU 3539  CD1 ILE B 152     5949  13476  12236   1098   3206   2564       C  
ATOM   3540  N   TYR B 153      14.712   9.143  22.937  1.00 93.79           N  
ANISOU 3540  N   TYR B 153     7232  14173  14230   1088   3266   2791       N  
ATOM   3541  CA  TYR B 153      15.787  10.121  22.821  1.00 87.99           C  
ANISOU 3541  CA  TYR B 153     6448  13308  13677   1104   3275   2925       C  
ATOM   3542  C   TYR B 153      17.107   9.544  23.312  1.00 87.73           C  
ANISOU 3542  C   TYR B 153     6474  13248  13612   1035   3262   2873       C  
ATOM   3543  O   TYR B 153      18.139   9.695  22.654  1.00 90.60           O  
ANISOU 3543  O   TYR B 153     6828  13599  13996   1037   3243   2991       O  
ATOM   3544  CB  TYR B 153      15.424  11.384  23.604  1.00 85.41           C  
ANISOU 3544  CB  TYR B 153     6046  12812  13593   1129   3331   2920       C  
ATOM   3545  CG  TYR B 153      16.594  12.302  23.879  1.00 83.71           C  
ANISOU 3545  CG  TYR B 153     5793  12437  13576   1114   3357   2995       C  
ATOM   3546  CD1 TYR B 153      17.166  13.054  22.863  1.00 89.88           C  
ANISOU 3546  CD1 TYR B 153     6522  13183  14445   1162   3354   3193       C  
ATOM   3547  CD2 TYR B 153      17.124  12.419  25.158  1.00 80.46           C  
ANISOU 3547  CD2 TYR B 153     5394  11913  13263   1045   3391   2868       C  
ATOM   3548  CE1 TYR B 153      18.232  13.898  23.111  1.00 91.65           C  
ANISOU 3548  CE1 TYR B 153     6709  13258  14854   1140   3385   3253       C  
ATOM   3549  CE2 TYR B 153      18.191  13.259  25.415  1.00 81.12           C  
ANISOU 3549  CE2 TYR B 153     5436  11856  13531   1020   3417   2926       C  
ATOM   3550  CZ  TYR B 153      18.741  13.995  24.388  1.00 88.86           C  
ANISOU 3550  CZ  TYR B 153     6367  12798  14599   1067   3415   3113       C  
ATOM   3551  OH  TYR B 153      19.804  14.832  24.639  1.00 92.13           O  
ANISOU 3551  OH  TYR B 153     6737  13069  15198   1034   3449   3162       O  
ATOM   3552  N   LEU B 154      17.094   8.876  24.469  1.00 86.65           N  
ANISOU 3552  N   LEU B 154     6393  13103  13426    975   3276   2702       N  
ATOM   3553  CA  LEU B 154      18.329   8.292  24.990  1.00 76.71           C  
ANISOU 3553  CA  LEU B 154     5180  11827  12139    917   3262   2660       C  
ATOM   3554  C   LEU B 154      18.857   7.193  24.074  1.00 79.40           C  
ANISOU 3554  C   LEU B 154     5586  12295  12289    909   3218   2696       C  
ATOM   3555  O   LEU B 154      20.070   7.098  23.839  1.00 79.85           O  
ANISOU 3555  O   LEU B 154     5642  12331  12366    893   3198   2760       O  
ATOM   3556  CB  LEU B 154      18.111   7.745  26.401  1.00 76.04           C  
ANISOU 3556  CB  LEU B 154     5143  11724  12026    857   3291   2481       C  
ATOM   3557  CG  LEU B 154      17.933   8.758  27.530  1.00 76.74           C  
ANISOU 3557  CG  LEU B 154     5174  11665  12318    836   3347   2422       C  
ATOM   3558  CD1 LEU B 154      17.742   8.041  28.856  1.00 79.56           C  
ANISOU 3558  CD1 LEU B 154     5590  12029  12612    769   3380   2249       C  
ATOM   3559  CD2 LEU B 154      19.132   9.691  27.592  1.00 77.50           C  
ANISOU 3559  CD2 LEU B 154     5203  11640  12605    824   3348   2518       C  
ATOM   3560  N   ASP B 155      17.962   6.354  23.548  1.00 75.49           N  
ANISOU 3560  N   ASP B 155     5143  11929  11612    915   3208   2648       N  
ATOM   3561  CA  ASP B 155      18.379   5.291  22.636  1.00 79.05           C  
ANISOU 3561  CA  ASP B 155     5658  12494  11882    900   3179   2669       C  
ATOM   3562  C   ASP B 155      19.071   5.870  21.406  1.00 88.80           C  
ANISOU 3562  C   ASP B 155     6844  13730  13167    935   3159   2851       C  
ATOM   3563  O   ASP B 155      20.209   5.497  21.073  1.00 95.70           O  
ANISOU 3563  O   ASP B 155     7740  14602  14021    913   3145   2893       O  
ATOM   3564  CB  ASP B 155      17.164   4.451  22.235  1.00 74.48           C  
ANISOU 3564  CB  ASP B 155     5132  12048  11120    894   3181   2584       C  
ATOM   3565  CG  ASP B 155      17.542   3.192  21.476  1.00 82.41           C  
ANISOU 3565  CG  ASP B 155     6219  13160  11931    860   3166   2563       C  
ATOM   3566  OD1 ASP B 155      18.751   2.916  21.328  1.00 85.45           O  
ANISOU 3566  OD1 ASP B 155     6624  13516  12325    845   3155   2608       O  
ATOM   3567  OD2 ASP B 155      16.623   2.473  21.030  1.00 85.33           O  
ANISOU 3567  OD2 ASP B 155     6633  13641  12149    845   3170   2495       O  
ATOM   3568  N   VAL B 156      18.385   6.784  20.711  1.00 86.49           N  
ANISOU 3568  N   VAL B 156     6480  13441  12942    990   3162   2965       N  
ATOM   3569  CA  VAL B 156      18.953   7.392  19.512  1.00 87.34           C  
ANISOU 3569  CA  VAL B 156     6538  13553  13095   1025   3153   3153       C  
ATOM   3570  C   VAL B 156      20.236   8.139  19.849  1.00 87.73           C  
ANISOU 3570  C   VAL B 156     6549  13462  13321   1016   3164   3220       C  
ATOM   3571  O   VAL B 156      21.211   8.093  19.092  1.00 86.65           O  
ANISOU 3571  O   VAL B 156     6412  13332  13177   1009   3156   3315       O  
ATOM   3572  CB  VAL B 156      17.917   8.313  18.840  1.00 78.60           C  
ANISOU 3572  CB  VAL B 156     5351  12469  12046   1096   3159   3276       C  
ATOM   3573  CG1 VAL B 156      18.541   9.056  17.667  1.00 79.67           C  
ANISOU 3573  CG1 VAL B 156     5429  12596  12244   1135   3160   3489       C  
ATOM   3574  CG2 VAL B 156      16.715   7.505  18.380  1.00 78.29           C  
ANISOU 3574  CG2 VAL B 156     5340  12591  11817   1098   3143   3213       C  
ATOM   3575  N   LEU B 157      20.269   8.811  21.003  1.00 88.94           N  
ANISOU 3575  N   LEU B 157     6669  13487  13638   1009   3187   3160       N  
ATOM   3576  CA  LEU B 157      21.453   9.557  21.410  1.00 89.16           C  
ANISOU 3576  CA  LEU B 157     6652  13380  13845    989   3201   3206       C  
ATOM   3577  C   LEU B 157      22.661   8.645  21.537  1.00 89.97           C  
ANISOU 3577  C   LEU B 157     6803  13511  13869    936   3176   3160       C  
ATOM   3578  O   LEU B 157      23.717   8.914  20.958  1.00 95.40           O  
ANISOU 3578  O   LEU B 157     7466  14169  14614    931   3173   3258       O  
ATOM   3579  CB  LEU B 157      21.188  10.277  22.733  1.00 87.46           C  
ANISOU 3579  CB  LEU B 157     6398  13035  13798    972   3236   3116       C  
ATOM   3580  CG  LEU B 157      22.432  10.795  23.458  1.00 79.15           C  
ANISOU 3580  CG  LEU B 157     5308  11857  12909    924   3248   3107       C  
ATOM   3581  CD1 LEU B 157      23.073  11.930  22.678  1.00 85.03           C  
ANISOU 3581  CD1 LEU B 157     5982  12509  13816    951   3272   3274       C  
ATOM   3582  CD2 LEU B 157      22.095  11.231  24.876  1.00 79.27           C  
ANISOU 3582  CD2 LEU B 157     5300  11769  13048    887   3285   2979       C  
ATOM   3583  N   PHE B 158      22.525   7.559  22.298  1.00 85.05           N  
ANISOU 3583  N   PHE B 158     6247  12945  13122    899   3162   3013       N  
ATOM   3584  CA  PHE B 158      23.674   6.695  22.539  1.00 79.00           C  
ANISOU 3584  CA  PHE B 158     5519  12198  12301    857   3141   2972       C  
ATOM   3585  C   PHE B 158      24.117   5.986  21.263  1.00 78.30           C  
ANISOU 3585  C   PHE B 158     5470  12203  12079    863   3126   3041       C  
ATOM   3586  O   PHE B 158      25.320   5.889  20.990  1.00 81.52           O  
ANISOU 3586  O   PHE B 158     5863  12586  12525    847   3118   3090       O  
ATOM   3587  CB  PHE B 158      23.345   5.703  23.652  1.00 75.20           C  
ANISOU 3587  CB  PHE B 158     5101  11754  11719    823   3141   2812       C  
ATOM   3588  CG  PHE B 158      23.097   6.361  24.981  1.00 76.05           C  
ANISOU 3588  CG  PHE B 158     5167  11767  11963    802   3164   2737       C  
ATOM   3589  CD1 PHE B 158      23.717   7.561  25.294  1.00 77.98           C  
ANISOU 3589  CD1 PHE B 158     5323  11887  12418    794   3176   2797       C  
ATOM   3590  CD2 PHE B 158      22.229   5.802  25.902  1.00 80.87           C  
ANISOU 3590  CD2 PHE B 158     5827  12407  12492    782   3183   2601       C  
ATOM   3591  CE1 PHE B 158      23.490   8.180  26.507  1.00 81.12           C  
ANISOU 3591  CE1 PHE B 158     5682  12194  12948    762   3207   2718       C  
ATOM   3592  CE2 PHE B 158      21.997   6.418  27.119  1.00 83.08           C  
ANISOU 3592  CE2 PHE B 158     6069  12599  12899    753   3216   2526       C  
ATOM   3593  CZ  PHE B 158      22.627   7.610  27.420  1.00 83.10           C  
ANISOU 3593  CZ  PHE B 158     5981  12477  13115    741   3227   2583       C  
ATOM   3594  N   SER B 159      23.168   5.525  20.442  1.00 75.77           N  
ANISOU 3594  N   SER B 159     5192  11989  11610    882   3126   3046       N  
ATOM   3595  CA  SER B 159      23.566   4.834  19.215  1.00 75.70           C  
ANISOU 3595  CA  SER B 159     5221  12070  11470    875   3120   3101       C  
ATOM   3596  C   SER B 159      24.217   5.791  18.215  1.00 80.88           C  
ANISOU 3596  C   SER B 159     5810  12688  12231    899   3127   3273       C  
ATOM   3597  O   SER B 159      25.227   5.448  17.578  1.00 84.98           O  
ANISOU 3597  O   SER B 159     6341  13219  12730    879   3129   3318       O  
ATOM   3598  CB  SER B 159      22.357   4.134  18.600  1.00 83.07           C  
ANISOU 3598  CB  SER B 159     6209  13135  12220    878   3120   3057       C  
ATOM   3599  OG  SER B 159      21.842   3.145  19.474  1.00 83.54           O  
ANISOU 3599  OG  SER B 159     6341  13227  12174    848   3124   2892       O  
ATOM   3600  N   THR B 160      23.654   6.994  18.064  1.00 79.25           N  
ANISOU 3600  N   THR B 160     5535  12432  12146    941   3139   3372       N  
ATOM   3601  CA  THR B 160      24.237   7.994  17.179  1.00 78.79           C  
ANISOU 3601  CA  THR B 160     5411  12323  12202    966   3158   3547       C  
ATOM   3602  C   THR B 160      25.612   8.423  17.671  1.00 83.78           C  
ANISOU 3602  C   THR B 160     6008  12833  12991    937   3166   3556       C  
ATOM   3603  O   THR B 160      26.538   8.607  16.871  1.00 86.04           O  
ANISOU 3603  O   THR B 160     6276  13108  13307    928   3179   3653       O  
ATOM   3604  CB  THR B 160      23.296   9.197  17.080  1.00 95.66           C  
ANISOU 3604  CB  THR B 160     7477  14414  14454   1025   3176   3648       C  
ATOM   3605  OG1 THR B 160      22.002   8.757  16.651  1.00 97.67           O  
ANISOU 3605  OG1 THR B 160     7753  14796  14561   1053   3163   3633       O  
ATOM   3606  CG2 THR B 160      23.823  10.221  16.097  1.00 93.11           C  
ANISOU 3606  CG2 THR B 160     7090  14043  14245   1056   3205   3846       C  
ATOM   3607  N   ALA B 161      25.767   8.582  18.989  1.00 83.17           N  
ANISOU 3607  N   ALA B 161     5916  12669  13015    915   3162   3452       N  
ATOM   3608  CA  ALA B 161      27.074   8.891  19.552  1.00 81.13           C  
ANISOU 3608  CA  ALA B 161     5617  12312  12898    877   3164   3444       C  
ATOM   3609  C   ALA B 161      28.073   7.787  19.248  1.00 78.44           C  
ANISOU 3609  C   ALA B 161     5319  12036  12450    845   3144   3409       C  
ATOM   3610  O   ALA B 161      29.235   8.063  18.943  1.00 78.99           O  
ANISOU 3610  O   ALA B 161     5348  12056  12607    825   3151   3467       O  
ATOM   3611  CB  ALA B 161      26.960   9.113  21.060  1.00 78.79           C  
ANISOU 3611  CB  ALA B 161     5298  11937  12702    851   3161   3325       C  
ATOM   3612  N   LYS B 162      27.630   6.530  19.301  1.00 77.43           N  
ANISOU 3612  N   LYS B 162     5271  12012  12138    838   3125   3314       N  
ATOM   3613  CA  LYS B 162      28.523   5.420  18.986  1.00 76.96           C  
ANISOU 3613  CA  LYS B 162     5254  12007  11980    813   3116   3280       C  
ATOM   3614  C   LYS B 162      29.006   5.491  17.540  1.00 83.36           C  
ANISOU 3614  C   LYS B 162     6062  12853  12757    815   3137   3393       C  
ATOM   3615  O   LYS B 162      30.217   5.436  17.265  1.00 88.70           O  
ANISOU 3615  O   LYS B 162     6712  13496  13493    794   3144   3425       O  
ATOM   3616  CB  LYS B 162      27.808   4.095  19.255  1.00 78.68           C  
ANISOU 3616  CB  LYS B 162     5564  12322  12009    806   3108   3158       C  
ATOM   3617  CG  LYS B 162      28.441   2.890  18.582  1.00 88.50           C  
ANISOU 3617  CG  LYS B 162     6867  13635  13125    786   3115   3134       C  
ATOM   3618  CD  LYS B 162      28.058   1.604  19.292  1.00 95.88           C  
ANISOU 3618  CD  LYS B 162     7883  14622  13926    773   3113   2998       C  
ATOM   3619  CE  LYS B 162      29.099   0.518  19.074  1.00104.68           C  
ANISOU 3619  CE  LYS B 162     9030  15754  14991    756   3123   2971       C  
ATOM   3620  NZ  LYS B 162      28.732  -0.746  19.772  1.00110.40           N  
ANISOU 3620  NZ  LYS B 162     9836  16521  15592    747   3132   2850       N  
ATOM   3621  N   ILE B 163      28.069   5.617  16.598  1.00 80.57           N  
ANISOU 3621  N   ILE B 163     5731  12574  12310    838   3149   3455       N  
ATOM   3622  CA  ILE B 163      28.462   5.588  15.190  1.00 78.33           C  
ANISOU 3622  CA  ILE B 163     5450  12343  11970    833   3173   3560       C  
ATOM   3623  C   ILE B 163      29.298   6.815  14.833  1.00 79.49           C  
ANISOU 3623  C   ILE B 163     5516  12391  12298    839   3197   3696       C  
ATOM   3624  O   ILE B 163      30.255   6.723  14.052  1.00 82.32           O  
ANISOU 3624  O   ILE B 163     5867  12750  12663    816   3221   3750       O  
ATOM   3625  CB  ILE B 163      27.229   5.443  14.279  1.00 78.42           C  
ANISOU 3625  CB  ILE B 163     5492  12473  11833    853   3176   3602       C  
ATOM   3626  CG1 ILE B 163      27.667   5.199  12.832  1.00 79.00           C  
ANISOU 3626  CG1 ILE B 163     5578  12622  11818    833   3203   3691       C  
ATOM   3627  CG2 ILE B 163      26.335   6.663  14.376  1.00 89.78           C  
ANISOU 3627  CG2 ILE B 163     6868  13874  13371    904   3177   3698       C  
ATOM   3628  CD1 ILE B 163      26.536   4.814  11.905  1.00 79.09           C  
ANISOU 3628  CD1 ILE B 163     5622  12777  11653    838   3203   3714       C  
ATOM   3629  N   TRP B 164      28.989   7.974  15.423  1.00 80.05           N  
ANISOU 3629  N   TRP B 164     5524  12365  12525    866   3201   3743       N  
ATOM   3630  CA  TRP B 164      29.778   9.160  15.113  1.00 81.23           C  
ANISOU 3630  CA  TRP B 164     5599  12408  12858    867   3235   3866       C  
ATOM   3631  C   TRP B 164      31.123   9.159  15.826  1.00 92.94           C  
ANISOU 3631  C   TRP B 164     7047  13801  14465    822   3232   3805       C  
ATOM   3632  O   TRP B 164      32.077   9.757  15.322  1.00 96.82           O  
ANISOU 3632  O   TRP B 164     7491  14231  15064    805   3264   3888       O  
ATOM   3633  CB  TRP B 164      28.986  10.423  15.450  1.00 93.69           C  
ANISOU 3633  CB  TRP B 164     7121  13900  14576    909   3254   3940       C  
ATOM   3634  CG  TRP B 164      27.975  10.769  14.398  1.00 95.56           C  
ANISOU 3634  CG  TRP B 164     7355  14212  14740    962   3269   4073       C  
ATOM   3635  CD1 TRP B 164      26.654  10.441  14.394  1.00 98.14           C  
ANISOU 3635  CD1 TRP B 164     7708  14631  14950    997   3247   4048       C  
ATOM   3636  CD2 TRP B 164      28.207  11.510  13.193  1.00 95.68           C  
ANISOU 3636  CD2 TRP B 164     7332  14225  14796    984   3311   4260       C  
ATOM   3637  NE1 TRP B 164      26.045  10.929  13.263  1.00 99.85           N  
ANISOU 3637  NE1 TRP B 164     7897  14912  15130   1043   3266   4212       N  
ATOM   3638  CE2 TRP B 164      26.978  11.591  12.509  1.00 96.73           C  
ANISOU 3638  CE2 TRP B 164     7464  14460  14828   1038   3306   4350       C  
ATOM   3639  CE3 TRP B 164      29.335  12.113  12.628  1.00 93.78           C  
ANISOU 3639  CE3 TRP B 164     7055  13910  14667    962   3355   4361       C  
ATOM   3640  CZ2 TRP B 164      26.844  12.250  11.289  1.00 93.00           C  
ANISOU 3640  CZ2 TRP B 164     6954  14024  14360   1074   3341   4551       C  
ATOM   3641  CZ3 TRP B 164      29.200  12.767  11.417  1.00 92.70           C  
ANISOU 3641  CZ3 TRP B 164     6890  13799  14534    994   3397   4552       C  
ATOM   3642  CH2 TRP B 164      27.964  12.830  10.760  1.00 92.06           C  
ANISOU 3642  CH2 TRP B 164     6805  13825  14347   1052   3389   4652       C  
ATOM   3643  N   HIS B 165      31.239   8.466  16.961  1.00 84.63           N  
ANISOU 3643  N   HIS B 165     6013  12749  13394    802   3195   3664       N  
ATOM   3644  CA  HIS B 165      32.553   8.224  17.543  1.00 80.42           C  
ANISOU 3644  CA  HIS B 165     5442  12166  12947    761   3183   3608       C  
ATOM   3645  C   HIS B 165      33.410   7.393  16.602  1.00 80.39           C  
ANISOU 3645  C   HIS B 165     5466  12224  12854    744   3194   3625       C  
ATOM   3646  O   HIS B 165      34.583   7.709  16.370  1.00 83.84           O  
ANISOU 3646  O   HIS B 165     5849  12607  13399    717   3212   3662       O  
ATOM   3647  CB  HIS B 165      32.413   7.529  18.898  1.00 79.53           C  
ANISOU 3647  CB  HIS B 165     5345  12064  12809    750   3141   3469       C  
ATOM   3648  CG  HIS B 165      32.327   8.474  20.055  1.00 81.48           C  
ANISOU 3648  CG  HIS B 165     5527  12211  13222    735   3136   3437       C  
ATOM   3649  ND1 HIS B 165      31.182   9.179  20.358  1.00 83.33           N  
ANISOU 3649  ND1 HIS B 165     5761  12411  13489    758   3151   3441       N  
ATOM   3650  CD2 HIS B 165      33.246   8.831  20.982  1.00 82.29           C  
ANISOU 3650  CD2 HIS B 165     5555  12240  13472    695   3122   3394       C  
ATOM   3651  CE1 HIS B 165      31.400   9.929  21.423  1.00 83.93           C  
ANISOU 3651  CE1 HIS B 165     5773  12389  13727    729   3154   3397       C  
ATOM   3652  NE2 HIS B 165      32.644   9.738  21.821  1.00 82.37           N  
ANISOU 3652  NE2 HIS B 165     5528  12171  13598    686   3134   3367       N  
ATOM   3653  N   LEU B 166      32.837   6.322  16.047  1.00 79.65           N  
ANISOU 3653  N   LEU B 166     5454  12241  12567    753   3191   3590       N  
ATOM   3654  CA  LEU B 166      33.578   5.512  15.081  1.00 79.70           C  
ANISOU 3654  CA  LEU B 166     5491  12304  12486    731   3214   3598       C  
ATOM   3655  C   LEU B 166      34.004   6.346  13.874  1.00 83.64           C  
ANISOU 3655  C   LEU B 166     5955  12783  13043    724   3261   3734       C  
ATOM   3656  O   LEU B 166      35.155   6.270  13.414  1.00 97.43           O  
ANISOU 3656  O   LEU B 166     7673  14504  14843    695   3288   3754       O  
ATOM   3657  CB  LEU B 166      32.730   4.319  14.639  1.00 78.83           C  
ANISOU 3657  CB  LEU B 166     5478  12314  12161    734   3214   3533       C  
ATOM   3658  CG  LEU B 166      32.350   3.285  15.700  1.00 77.73           C  
ANISOU 3658  CG  LEU B 166     5391  12203  11941    737   3182   3396       C  
ATOM   3659  CD1 LEU B 166      31.628   2.109  15.060  1.00 77.07           C  
ANISOU 3659  CD1 LEU B 166     5403  12231  11649    727   3198   3333       C  
ATOM   3660  CD2 LEU B 166      33.574   2.816  16.469  1.00 77.68           C  
ANISOU 3660  CD2 LEU B 166     5348  12146  12021    724   3169   3342       C  
ATOM   3661  N   CYS B 167      33.077   7.153  13.349  1.00 81.29           N  
ANISOU 3661  N   CYS B 167     5653  12496  12737    753   3275   3834       N  
ATOM   3662  CA  CYS B 167      33.382   7.998  12.197  1.00 84.62           C  
ANISOU 3662  CA  CYS B 167     6040  12901  13209    752   3325   3984       C  
ATOM   3663  C   CYS B 167      34.490   8.996  12.511  1.00 84.69           C  
ANISOU 3663  C   CYS B 167     5967  12776  13435    733   3350   4031       C  
ATOM   3664  O   CYS B 167      35.406   9.196  11.700  1.00 84.92           O  
ANISOU 3664  O   CYS B 167     5973  12787  13505    704   3395   4094       O  
ATOM   3665  CB  CYS B 167      32.117   8.726  11.744  1.00 88.89           C  
ANISOU 3665  CB  CYS B 167     6578  13475  13720    800   3330   4095       C  
ATOM   3666  SG  CYS B 167      32.345   9.802  10.319  1.00 93.79           S  
ANISOU 3666  SG  CYS B 167     7156  14085  14396    810   3395   4309       S  
ATOM   3667  N   ALA B 168      34.422   9.636  13.681  1.00 83.39           N  
ANISOU 3667  N   ALA B 168     5755  12516  13411    740   3328   3991       N  
ATOM   3668  CA  ALA B 168      35.447  10.597  14.066  1.00 84.33           C  
ANISOU 3668  CA  ALA B 168     5792  12507  13742    710   3354   4018       C  
ATOM   3669  C   ALA B 168      36.797   9.920  14.248  1.00 90.37           C  
ANISOU 3669  C   ALA B 168     6535  13269  14532    664   3345   3937       C  
ATOM   3670  O   ALA B 168      37.832  10.494  13.902  1.00 91.10           O  
ANISOU 3670  O   ALA B 168     6570  13294  14749    630   3384   3984       O  
ATOM   3671  CB  ALA B 168      35.033  11.323  15.345  1.00 84.31           C  
ANISOU 3671  CB  ALA B 168     5746  12412  13874    717   3333   3969       C  
ATOM   3672  N   ILE B 169      36.807   8.699  14.788  1.00 90.34           N  
ANISOU 3672  N   ILE B 169     6572  13337  14417    662   3298   3820       N  
ATOM   3673  CA  ILE B 169      38.058   7.957  14.929  1.00 89.36           C  
ANISOU 3673  CA  ILE B 169     6421  13219  14314    630   3289   3752       C  
ATOM   3674  C   ILE B 169      38.691   7.720  13.565  1.00 87.80           C  
ANISOU 3674  C   ILE B 169     6239  13054  14067    610   3345   3815       C  
ATOM   3675  O   ILE B 169      39.887   7.973  13.359  1.00 84.58           O  
ANISOU 3675  O   ILE B 169     5769  12595  13773    575   3373   3827       O  
ATOM   3676  CB  ILE B 169      37.814   6.633  15.673  1.00 81.97           C  
ANISOU 3676  CB  ILE B 169     5535  12356  13255    643   3239   3633       C  
ATOM   3677  CG1 ILE B 169      37.454   6.906  17.130  1.00 81.60           C  
ANISOU 3677  CG1 ILE B 169     5456  12268  13281    649   3187   3565       C  
ATOM   3678  CG2 ILE B 169      39.037   5.734  15.582  1.00 88.04           C  
ANISOU 3678  CG2 ILE B 169     6282  13142  14028    623   3240   3584       C  
ATOM   3679  CD1 ILE B 169      37.005   5.683  17.877  1.00 80.47           C  
ANISOU 3679  CD1 ILE B 169     5369  12196  13008    668   3145   3462       C  
ATOM   3680  N   SER B 170      37.898   7.219  12.614  1.00 86.79           N  
ANISOU 3680  N   SER B 170     6190  13017  13768    626   3365   3848       N  
ATOM   3681  CA  SER B 170      38.421   6.967  11.273  1.00 85.86           C  
ANISOU 3681  CA  SER B 170     6093  12942  13590    598   3424   3902       C  
ATOM   3682  C   SER B 170      38.966   8.250  10.648  1.00 89.49           C  
ANISOU 3682  C   SER B 170     6489  13321  14191    580   3480   4027       C  
ATOM   3683  O   SER B 170      40.101   8.284  10.142  1.00 94.85           O  
ANISOU 3683  O   SER B 170     7132  13969  14937    539   3525   4036       O  
ATOM   3684  CB  SER B 170      37.332   6.353  10.393  1.00 83.56           C  
ANISOU 3684  CB  SER B 170     5890  12768  13091    611   3433   3921       C  
ATOM   3685  OG  SER B 170      37.883   5.806   9.207  1.00 84.02           O  
ANISOU 3685  OG  SER B 170     5975  12881  13066    572   3489   3933       O  
ATOM   3686  N   LEU B 171      38.164   9.318  10.677  1.00 86.73           N  
ANISOU 3686  N   LEU B 171     6127  12932  13896    610   3484   4124       N  
ATOM   3687  CA  LEU B 171      38.567  10.580  10.063  1.00 91.23           C  
ANISOU 3687  CA  LEU B 171     6643  13418  14603    599   3548   4258       C  
ATOM   3688  C   LEU B 171      39.827  11.134  10.716  1.00 91.64           C  
ANISOU 3688  C   LEU B 171     6611  13352  14858    557   3561   4217       C  
ATOM   3689  O   LEU B 171      40.729  11.631  10.028  1.00 91.03           O  
ANISOU 3689  O   LEU B 171     6496  13226  14866    519   3625   4276       O  
ATOM   3690  CB  LEU B 171      37.417  11.583  10.162  1.00 97.34           C  
ANISOU 3690  CB  LEU B 171     7411  14158  15414    649   3549   4364       C  
ATOM   3691  CG  LEU B 171      37.594  12.988   9.593  1.00101.65           C  
ANISOU 3691  CG  LEU B 171     7906  14606  16111    653   3621   4524       C  
ATOM   3692  CD1 LEU B 171      37.757  12.943   8.083  1.00103.47           C  
ANISOU 3692  CD1 LEU B 171     8164  14906  16244    640   3680   4643       C  
ATOM   3693  CD2 LEU B 171      36.403  13.848   9.983  1.00102.70           C  
ANISOU 3693  CD2 LEU B 171     8027  14697  16299    713   3614   4603       C  
ATOM   3694  N   ASP B 172      39.908  11.049  12.046  1.00 95.18           N  
ANISOU 3694  N   ASP B 172     7024  13758  15382    558   3503   4112       N  
ATOM   3695  CA  ASP B 172      41.065  11.563  12.764  1.00 98.87           C  
ANISOU 3695  CA  ASP B 172     7400  14127  16041    512   3507   4062       C  
ATOM   3696  C   ASP B 172      42.318  10.776  12.421  1.00 92.83           C  
ANISOU 3696  C   ASP B 172     6611  13393  15267    472   3517   4003       C  
ATOM   3697  O   ASP B 172      43.387  11.363  12.241  1.00 89.26           O  
ANISOU 3697  O   ASP B 172     6087  12870  14957    426   3561   4018       O  
ATOM   3698  CB  ASP B 172      40.805  11.532  14.269  1.00105.25           C  
ANISOU 3698  CB  ASP B 172     8177  14906  16908    517   3436   3957       C  
ATOM   3699  CG  ASP B 172      41.854  12.292  15.056  1.00112.71           C  
ANISOU 3699  CG  ASP B 172     9015  15748  18063    463   3440   3914       C  
ATOM   3700  OD1 ASP B 172      41.945  13.526  14.888  1.00116.21           O  
ANISOU 3700  OD1 ASP B 172     9415  16087  18651    442   3497   3986       O  
ATOM   3701  OD2 ASP B 172      42.585  11.656  15.844  1.00113.88           O  
ANISOU 3701  OD2 ASP B 172     9117  15919  18235    440   3387   3809       O  
ATOM   3702  N   ARG B 173      42.213   9.447  12.322  1.00 93.70           N  
ANISOU 3702  N   ARG B 173     6778  13604  15220    488   3485   3933       N  
ATOM   3703  CA  ARG B 173      43.388   8.658  11.964  1.00 96.76           C  
ANISOU 3703  CA  ARG B 173     7141  14016  15608    456   3504   3879       C  
ATOM   3704  C   ARG B 173      43.865   8.981  10.553  1.00100.66           C  
ANISOU 3704  C   ARG B 173     7643  14508  16096    422   3593   3964       C  
ATOM   3705  O   ARG B 173      45.076   9.070  10.302  1.00 99.69           O  
ANISOU 3705  O   ARG B 173     7457  14346  16076    378   3633   3948       O  
ATOM   3706  CB  ARG B 173      43.089   7.166  12.098  1.00 94.46           C  
ANISOU 3706  CB  ARG B 173     6916  13823  15151    482   3466   3791       C  
ATOM   3707  CG  ARG B 173      42.875   6.705  13.525  1.00 91.37           C  
ANISOU 3707  CG  ARG B 173     6507  13435  14774    509   3383   3700       C  
ATOM   3708  CD  ARG B 173      42.661   5.206  13.582  1.00 91.13           C  
ANISOU 3708  CD  ARG B 173     6545  13493  14588    534   3362   3622       C  
ATOM   3709  NE  ARG B 173      43.791   4.476  13.015  1.00 93.97           N  
ANISOU 3709  NE  ARG B 173     6879  13865  14961    512   3401   3593       N  
ATOM   3710  CZ  ARG B 173      44.865   4.109  13.706  1.00 97.36           C  
ANISOU 3710  CZ  ARG B 173     7222  14269  15499    510   3374   3539       C  
ATOM   3711  NH1 ARG B 173      45.847   3.448  13.108  1.00 98.83           N  
ANISOU 3711  NH1 ARG B 173     7384  14466  15700    493   3419   3517       N  
ATOM   3712  NH2 ARG B 173      44.960   4.405  14.995  1.00 98.28           N  
ANISOU 3712  NH2 ARG B 173     7272  14356  15714    521   3302   3506       N  
ATOM   3713  N   TYR B 174      42.930   9.174   9.618  1.00102.89           N  
ANISOU 3713  N   TYR B 174     7998  14836  16258    440   3627   4058       N  
ATOM   3714  CA  TYR B 174      43.330   9.532   8.258  1.00106.85           C  
ANISOU 3714  CA  TYR B 174     8510  15343  16747    404   3715   4150       C  
ATOM   3715  C   TYR B 174      44.041  10.882   8.235  1.00111.25           C  
ANISOU 3715  C   TYR B 174     8987  15778  17504    373   3768   4225       C  
ATOM   3716  O   TYR B 174      45.153  11.008   7.698  1.00112.94           O  
ANISOU 3716  O   TYR B 174     9159  15959  17795    320   3829   4224       O  
ATOM   3717  CB  TYR B 174      42.111   9.546   7.336  1.00105.39           C  
ANISOU 3717  CB  TYR B 174     8408  15241  16395    432   3732   4248       C  
ATOM   3718  CG  TYR B 174      42.424   9.872   5.892  1.00105.09           C  
ANISOU 3718  CG  TYR B 174     8386  15225  16318    392   3821   4352       C  
ATOM   3719  CD1 TYR B 174      43.039   8.937   5.068  1.00104.97           C  
ANISOU 3719  CD1 TYR B 174     8402  15277  16203    344   3865   4294       C  
ATOM   3720  CD2 TYR B 174      42.094  11.106   5.347  1.00105.90           C  
ANISOU 3720  CD2 TYR B 174     8473  15279  16484    402   3869   4509       C  
ATOM   3721  CE1 TYR B 174      43.322   9.225   3.747  1.00108.32           C  
ANISOU 3721  CE1 TYR B 174     8845  15728  16585    298   3952   4382       C  
ATOM   3722  CE2 TYR B 174      42.373  11.403   4.024  1.00109.82           C  
ANISOU 3722  CE2 TYR B 174     8987  15802  16937    363   3953   4612       C  
ATOM   3723  CZ  TYR B 174      42.987  10.458   3.230  1.00113.10           C  
ANISOU 3723  CZ  TYR B 174     9437  16292  17245    307   3993   4543       C  
ATOM   3724  OH  TYR B 174      43.269  10.746   1.914  1.00120.25           O  
ANISOU 3724  OH  TYR B 174    10363  17227  18100    258   4082   4638       O  
ATOM   3725  N   VAL B 175      43.407  11.907   8.814  1.00110.46           N  
ANISOU 3725  N   VAL B 175     8865  15606  17498    401   3752   4286       N  
ATOM   3726  CA  VAL B 175      44.018  13.234   8.875  1.00106.15           C  
ANISOU 3726  CA  VAL B 175     8245  14930  17155    368   3810   4351       C  
ATOM   3727  C   VAL B 175      45.368  13.175   9.581  1.00102.31           C  
ANISOU 3727  C   VAL B 175     7669  14386  16819    314   3802   4238       C  
ATOM   3728  O   VAL B 175      46.310  13.889   9.213  1.00 94.30           O  
ANISOU 3728  O   VAL B 175     6597  13294  15940    261   3872   4266       O  
ATOM   3729  CB  VAL B 175      43.059  14.228   9.560  1.00101.28           C  
ANISOU 3729  CB  VAL B 175     7620  14240  16622    409   3793   4410       C  
ATOM   3730  CG1 VAL B 175      43.731  15.578   9.761  1.00101.10           C  
ANISOU 3730  CG1 VAL B 175     7519  14067  16827    368   3859   4456       C  
ATOM   3731  CG2 VAL B 175      41.787  14.382   8.741  1.00 99.57           C  
ANISOU 3731  CG2 VAL B 175     7475  14084  16273    467   3808   4544       C  
ATOM   3732  N   ALA B 176      45.489  12.316  10.595  1.00102.44           N  
ANISOU 3732  N   ALA B 176     7668  14444  16812    325   3717   4110       N  
ATOM   3733  CA  ALA B 176      46.746  12.183  11.321  1.00106.34           C  
ANISOU 3733  CA  ALA B 176     8062  14900  17441    280   3695   4006       C  
ATOM   3734  C   ALA B 176      47.849  11.645  10.423  1.00113.38           C  
ANISOU 3734  C   ALA B 176     8936  15821  18324    240   3752   3989       C  
ATOM   3735  O   ALA B 176      48.930  12.237  10.329  1.00121.16           O  
ANISOU 3735  O   ALA B 176     9837  16738  19460    183   3800   3981       O  
ATOM   3736  CB  ALA B 176      46.553  11.277  12.539  1.00103.67           C  
ANISOU 3736  CB  ALA B 176     7714  14617  17059    310   3591   3891       C  
ATOM   3737  N   ILE B 177      47.604  10.511   9.761  1.00110.40           N  
ANISOU 3737  N   ILE B 177     8633  15543  17773    262   3753   3975       N  
ATOM   3738  CA  ILE B 177      48.667   9.953   8.933  1.00109.20           C  
ANISOU 3738  CA  ILE B 177     8461  15413  17617    220   3814   3946       C  
ATOM   3739  C   ILE B 177      48.962  10.817   7.713  1.00111.44           C  
ANISOU 3739  C   ILE B 177     8752  15654  17935    172   3923   4048       C  
ATOM   3740  O   ILE B 177      50.054  10.712   7.145  1.00107.08           O  
ANISOU 3740  O   ILE B 177     8155  15089  17442    120   3988   4022       O  
ATOM   3741  CB  ILE B 177      48.353   8.513   8.479  1.00107.70           C  
ANISOU 3741  CB  ILE B 177     8351  15332  17238    245   3804   3896       C  
ATOM   3742  CG1 ILE B 177      47.343   8.513   7.329  1.00110.17           C  
ANISOU 3742  CG1 ILE B 177     8775  15706  17381    252   3852   3986       C  
ATOM   3743  CG2 ILE B 177      47.860   7.674   9.651  1.00103.99           C  
ANISOU 3743  CG2 ILE B 177     7892  14903  16715    299   3703   3813       C  
ATOM   3744  CD1 ILE B 177      47.200   7.170   6.650  1.00112.28           C  
ANISOU 3744  CD1 ILE B 177     9117  16074  17470    251   3870   3929       C  
ATOM   3745  N   GLN B 178      48.031  11.677   7.285  1.00119.40           N  
ANISOU 3745  N   GLN B 178     9812  16640  18913    190   3951   4169       N  
ATOM   3746  CA  GLN B 178      48.381  12.596   6.204  1.00124.01           C  
ANISOU 3746  CA  GLN B 178    10395  17172  19549    145   4059   4278       C  
ATOM   3747  C   GLN B 178      49.159  13.812   6.702  1.00126.65           C  
ANISOU 3747  C   GLN B 178    10635  17374  20114    102   4095   4287       C  
ATOM   3748  O   GLN B 178      50.237  14.124   6.183  1.00125.63           O  
ANISOU 3748  O   GLN B 178    10456  17199  20080     38   4173   4281       O  
ATOM   3749  CB  GLN B 178      47.120  13.039   5.462  1.00120.19           C  
ANISOU 3749  CB  GLN B 178     9998  16721  18947    185   4081   4422       C  
ATOM   3750  CG  GLN B 178      46.381  11.910   4.758  1.00111.94           C  
ANISOU 3750  CG  GLN B 178     9049  15817  17668    208   4062   4416       C  
ATOM   3751  CD  GLN B 178      47.223  11.237   3.691  1.00104.59           C  
ANISOU 3751  CD  GLN B 178     8135  14938  16668    145   4137   4381       C  
ATOM   3752  OE1 GLN B 178      47.185  10.016   3.533  1.00 94.69           O  
ANISOU 3752  OE1 GLN B 178     6922  13775  15280    144   4116   4291       O  
ATOM   3753  NE2 GLN B 178      47.985  12.031   2.949  1.00 97.02           N  
ANISOU 3753  NE2 GLN B 178     7144  13915  15802     88   4233   4449       N  
ATOM   3754  N   ASN B 179      48.632  14.503   7.709  1.00128.83           N  
ANISOU 3754  N   ASN B 179    10882  17584  20482    130   4045   4293       N  
ATOM   3755  CA  ASN B 179      49.237  15.743   8.195  1.00132.32           C  
ANISOU 3755  CA  ASN B 179    11240  17893  21144     83   4088   4300       C  
ATOM   3756  C   ASN B 179      50.419  15.434   9.110  1.00132.68           C  
ANISOU 3756  C   ASN B 179    11176  17923  21312     35   4044   4151       C  
ATOM   3757  O   ASN B 179      50.275  14.646  10.049  1.00131.90           O  
ANISOU 3757  O   ASN B 179    11060  17882  21172     66   3943   4054       O  
ATOM   3758  CB  ASN B 179      48.192  16.583   8.932  1.00132.33           C  
ANISOU 3758  CB  ASN B 179    11252  17827  21200    126   4059   4353       C  
ATOM   3759  CG  ASN B 179      48.681  17.985   9.260  1.00132.26           C  
ANISOU 3759  CG  ASN B 179    11171  17665  21416     73   4129   4378       C  
ATOM   3760  OD1 ASN B 179      49.740  18.413   8.808  1.00133.55           O  
ANISOU 3760  OD1 ASN B 179    11285  17772  21685      5   4207   4374       O  
ATOM   3761  ND2 ASN B 179      47.894  18.712  10.045  1.00131.43           N  
ANISOU 3761  ND2 ASN B 179    11062  17487  21387    100   4109   4398       N  
ATOM   3762  N   PRO B 180      51.599  16.033   8.877  1.00132.13           N  
ANISOU 3762  N   PRO B 180    11027  17782  21396    -41   4117   4130       N  
ATOM   3763  CA  PRO B 180      52.702  15.891   9.837  1.00130.68           C  
ANISOU 3763  CA  PRO B 180    10719  17584  21349    -89   4069   3993       C  
ATOM   3764  C   PRO B 180      52.382  16.496  11.203  1.00130.49           C  
ANISOU 3764  C   PRO B 180    10638  17504  21437    -90   4000   3941       C  
ATOM   3765  O   PRO B 180      51.446  17.289  11.310  1.00129.27           O  
ANISOU 3765  O   PRO B 180    10533  17286  21297    -68   4020   4018       O  
ATOM   3766  CB  PRO B 180      53.856  16.649   9.166  1.00131.23           C  
ANISOU 3766  CB  PRO B 180    10725  17575  21561   -174   4182   4002       C  
ATOM   3767  CG  PRO B 180      53.206  17.525   8.139  1.00131.18           C  
ANISOU 3767  CG  PRO B 180    10808  17506  21530   -171   4287   4156       C  
ATOM   3768  CD  PRO B 180      52.023  16.747   7.662  1.00131.81           C  
ANISOU 3768  CD  PRO B 180    11004  17684  21393    -88   4247   4227       C  
ATOM   3769  N   SER B 188      47.572  15.447  21.689  1.00105.67           N  
ANISOU 3769  N   SER B 188     7353  14524  18271      3   3266   3357       N  
ATOM   3770  CA  SER B 188      47.360  16.079  22.987  1.00108.40           C  
ANISOU 3770  CA  SER B 188     7633  14830  18726    -63   3236   3270       C  
ATOM   3771  C   SER B 188      46.059  15.613  23.635  1.00110.66           C  
ANISOU 3771  C   SER B 188     8002  15156  18889     -9   3191   3254       C  
ATOM   3772  O   SER B 188      45.025  15.460  22.969  1.00111.10           O  
ANISOU 3772  O   SER B 188     8177  15209  18828     68   3227   3330       O  
ATOM   3773  CB  SER B 188      47.369  17.604  22.868  1.00108.72           C  
ANISOU 3773  CB  SER B 188     7645  14716  18946   -136   3342   3285       C  
ATOM   3774  OG  SER B 188      47.072  18.209  24.117  1.00108.94           O  
ANISOU 3774  OG  SER B 188     7619  14698  19076   -208   3325   3191       O  
ATOM   3775  N   ARG B 189      46.135  15.391  24.950  1.00112.07           N  
ANISOU 3775  N   ARG B 189     8108  15379  19095    -55   3110   3154       N  
ATOM   3776  CA  ARG B 189      44.962  14.988  25.718  1.00117.19           C  
ANISOU 3776  CA  ARG B 189     8822  16063  19641    -19   3071   3122       C  
ATOM   3777  C   ARG B 189      43.841  16.007  25.583  1.00129.48           C  
ANISOU 3777  C   ARG B 189    10451  17502  21245    -17   3162   3152       C  
ATOM   3778  O   ARG B 189      42.670  15.638  25.428  1.00136.23           O  
ANISOU 3778  O   ARG B 189    11412  18378  21972     57   3168   3184       O  
ATOM   3779  CB  ARG B 189      45.359  14.824  27.183  1.00113.55           C  
ANISOU 3779  CB  ARG B 189     8249  15654  19241    -96   2982   3010       C  
ATOM   3780  CG  ARG B 189      44.221  14.549  28.132  1.00111.66           C  
ANISOU 3780  CG  ARG B 189     8061  15440  18925    -85   2952   2961       C  
ATOM   3781  CD  ARG B 189      44.719  14.608  29.568  1.00115.87           C  
ANISOU 3781  CD  ARG B 189     8464  16013  19547   -188   2874   2854       C  
ATOM   3782  NE  ARG B 189      43.649  14.394  30.536  1.00122.58           N  
ANISOU 3782  NE  ARG B 189     9379  16878  20316   -193   2846   2790       N  
ATOM   3783  CZ  ARG B 189      43.348  13.221  31.079  1.00128.81           C  
ANISOU 3783  CZ  ARG B 189    10247  17777  20919   -141   2738   2757       C  
ATOM   3784  NH1 ARG B 189      42.354  13.131  31.954  1.00128.68           N  
ANISOU 3784  NH1 ARG B 189    10360  17747  20786   -157   2697   2661       N  
ATOM   3785  NH2 ARG B 189      44.037  12.136  30.751  1.00133.22           N  
ANISOU 3785  NH2 ARG B 189    10755  18451  21413    -75   2682   2818       N  
ATOM   3786  N   THR B 190      44.178  17.295  25.652  1.00131.19           N  
ANISOU 3786  N   THR B 190    10605  17589  21650    -99   3238   3139       N  
ATOM   3787  CA  THR B 190      43.158  18.326  25.519  1.00129.45           C  
ANISOU 3787  CA  THR B 190    10446  17240  21500    -93   3336   3174       C  
ATOM   3788  C   THR B 190      42.555  18.310  24.118  1.00125.11           C  
ANISOU 3788  C   THR B 190    10003  16673  20858     11   3396   3319       C  
ATOM   3789  O   THR B 190      41.348  18.535  23.954  1.00126.11           O  
ANISOU 3789  O   THR B 190    10211  16764  20941     71   3433   3366       O  
ATOM   3790  CB  THR B 190      43.752  19.691  25.859  1.00131.87           C  
ANISOU 3790  CB  THR B 190    10664  17401  22039   -208   3417   3128       C  
ATOM   3791  OG1 THR B 190      44.281  19.653  27.189  1.00133.00           O  
ANISOU 3791  OG1 THR B 190    10701  17578  22255   -316   3352   2986       O  
ATOM   3792  CG2 THR B 190      42.686  20.772  25.795  1.00131.49           C  
ANISOU 3792  CG2 THR B 190    10674  17202  22083   -198   3527   3163       C  
ATOM   3793  N   LYS B 191      43.372  18.019  23.098  1.00118.85           N  
ANISOU 3793  N   LYS B 191     9208  15916  20035     31   3404   3389       N  
ATOM   3794  CA  LYS B 191      42.839  17.904  21.743  1.00110.54           C  
ANISOU 3794  CA  LYS B 191     8253  14869  18877    120   3454   3527       C  
ATOM   3795  C   LYS B 191      41.810  16.788  21.673  1.00107.19           C  
ANISOU 3795  C   LYS B 191     7927  14562  18237    210   3391   3537       C  
ATOM   3796  O   LYS B 191      40.711  16.964  21.130  1.00109.42           O  
ANISOU 3796  O   LYS B 191     8292  14830  18453    277   3428   3618       O  
ATOM   3797  CB  LYS B 191      43.951  17.594  20.737  1.00106.93           C  
ANISOU 3797  CB  LYS B 191     7775  14447  18407    114   3468   3579       C  
ATOM   3798  CG  LYS B 191      45.033  18.616  20.490  1.00105.46           C  
ANISOU 3798  CG  LYS B 191     7502  14154  18413     31   3544   3585       C  
ATOM   3799  CD  LYS B 191      45.968  18.006  19.445  1.00102.52           C  
ANISOU 3799  CD  LYS B 191     7127  13846  17978     42   3549   3633       C  
ATOM   3800  CE  LYS B 191      47.181  18.854  19.144  1.00107.84           C  
ANISOU 3800  CE  LYS B 191     7712  14434  18830    -44   3621   3628       C  
ATOM   3801  NZ  LYS B 191      48.025  18.190  18.107  1.00112.48           N  
ANISOU 3801  NZ  LYS B 191     8303  15088  19347    -30   3631   3669       N  
ATOM   3802  N   ALA B 192      42.159  15.627  22.228  1.00 99.77           N  
ANISOU 3802  N   ALA B 192     6976  13741  17191    212   3298   3457       N  
ATOM   3803  CA  ALA B 192      41.235  14.501  22.219  1.00 90.76           C  
ANISOU 3803  CA  ALA B 192     5931  12710  15844    289   3244   3452       C  
ATOM   3804  C   ALA B 192      39.954  14.838  22.969  1.00 89.71           C  
ANISOU 3804  C   ALA B 192     5838  12545  15704    304   3249   3418       C  
ATOM   3805  O   ALA B 192      38.856  14.481  22.525  1.00 87.21           O  
ANISOU 3805  O   ALA B 192     5616  12269  15252    375   3255   3462       O  
ATOM   3806  CB  ALA B 192      41.908  13.268  22.814  1.00 87.99           C  
ANISOU 3806  CB  ALA B 192     5549  12473  15409    285   3153   3372       C  
ATOM   3807  N   PHE B 193      40.071  15.532  24.103  1.00 91.83           N  
ANISOU 3807  N   PHE B 193     6031  12741  16119    231   3250   3333       N  
ATOM   3808  CA  PHE B 193      38.879  15.905  24.861  1.00 94.83           C  
ANISOU 3808  CA  PHE B 193     6443  13077  16511    236   3267   3287       C  
ATOM   3809  C   PHE B 193      37.976  16.837  24.061  1.00 99.57           C  
ANISOU 3809  C   PHE B 193     7096  13578  17158    285   3358   3390       C  
ATOM   3810  O   PHE B 193      36.751  16.663  24.046  1.00 98.89           O  
ANISOU 3810  O   PHE B 193     7082  13512  16981    346   3363   3403       O  
ATOM   3811  CB  PHE B 193      39.278  16.558  26.186  1.00100.79           C  
ANISOU 3811  CB  PHE B 193     7099  13763  17432    129   3265   3171       C  
ATOM   3812  CG  PHE B 193      39.737  15.579  27.231  1.00107.36           C  
ANISOU 3812  CG  PHE B 193     7884  14710  18198     92   3165   3070       C  
ATOM   3813  CD1 PHE B 193      39.559  14.219  27.047  1.00109.66           C  
ANISOU 3813  CD1 PHE B 193     8238  15138  18290    165   3095   3082       C  
ATOM   3814  CD2 PHE B 193      40.345  16.017  28.397  1.00110.64           C  
ANISOU 3814  CD2 PHE B 193     8190  15095  18752    -20   3144   2966       C  
ATOM   3815  CE1 PHE B 193      39.978  13.312  28.005  1.00109.50           C  
ANISOU 3815  CE1 PHE B 193     8172  15219  18215    141   3007   3008       C  
ATOM   3816  CE2 PHE B 193      40.765  15.115  29.357  1.00110.41           C  
ANISOU 3816  CE2 PHE B 193     8106  15181  18664    -51   3045   2892       C  
ATOM   3817  CZ  PHE B 193      40.582  13.761  29.160  1.00109.57           C  
ANISOU 3817  CZ  PHE B 193     8062  15206  18362     37   2977   2920       C  
ATOM   3818  N   LEU B 194      38.561  17.830  23.384  1.00104.33           N  
ANISOU 3818  N   LEU B 194     7659  14075  17906    261   3433   3468       N  
ATOM   3819  CA  LEU B 194      37.753  18.749  22.586  1.00104.44           C  
ANISOU 3819  CA  LEU B 194     7713  13990  17979    315   3524   3590       C  
ATOM   3820  C   LEU B 194      37.054  18.023  21.444  1.00 96.46           C  
ANISOU 3820  C   LEU B 194     6793  13084  16772    418   3505   3702       C  
ATOM   3821  O   LEU B 194      35.870  18.265  21.172  1.00 97.36           O  
ANISOU 3821  O   LEU B 194     6957  13184  16851    485   3532   3763       O  
ATOM   3822  CB  LEU B 194      38.626  19.881  22.043  1.00106.59           C  
ANISOU 3822  CB  LEU B 194     7927  14132  18441    267   3613   3659       C  
ATOM   3823  CG  LEU B 194      39.257  20.829  23.066  1.00104.18           C  
ANISOU 3823  CG  LEU B 194     7530  13699  18355    153   3656   3553       C  
ATOM   3824  CD1 LEU B 194      40.193  21.824  22.388  1.00105.69           C  
ANISOU 3824  CD1 LEU B 194     7671  13772  18713    105   3749   3624       C  
ATOM   3825  CD2 LEU B 194      38.183  21.556  23.859  1.00 98.99           C  
ANISOU 3825  CD2 LEU B 194     6881  12934  17795    149   3709   3507       C  
ATOM   3826  N   LYS B 195      37.766  17.115  20.773  1.00 89.24           N  
ANISOU 3826  N   LYS B 195     5897  12278  15732    427   3461   3723       N  
ATOM   3827  CA  LYS B 195      37.156  16.354  19.686  1.00 88.42           C  
ANISOU 3827  CA  LYS B 195     5879  12283  15432    507   3446   3813       C  
ATOM   3828  C   LYS B 195      36.016  15.470  20.193  1.00 92.05           C  
ANISOU 3828  C   LYS B 195     6407  12840  15726    554   3385   3746       C  
ATOM   3829  O   LYS B 195      34.946  15.395  19.570  1.00 93.03           O  
ANISOU 3829  O   LYS B 195     6592  13005  15750    621   3397   3819       O  
ATOM   3830  CB  LYS B 195      38.232  15.522  18.989  1.00 92.02           C  
ANISOU 3830  CB  LYS B 195     6337  12825  15802    492   3419   3822       C  
ATOM   3831  CG  LYS B 195      39.383  16.346  18.436  1.00 89.92           C  
ANISOU 3831  CG  LYS B 195     6005  12469  15693    441   3484   3882       C  
ATOM   3832  CD  LYS B 195      40.597  15.478  18.125  1.00 89.52           C  
ANISOU 3832  CD  LYS B 195     5933  12495  15587    410   3450   3842       C  
ATOM   3833  CE  LYS B 195      41.842  16.331  17.911  1.00 91.10           C  
ANISOU 3833  CE  LYS B 195     6046  12598  15970    340   3509   3860       C  
ATOM   3834  NZ  LYS B 195      43.086  15.509  17.880  1.00 90.99           N  
ANISOU 3834  NZ  LYS B 195     5986  12652  15933    303   3469   3794       N  
ATOM   3835  N   ILE B 196      36.224  14.800  21.331  1.00 91.14           N  
ANISOU 3835  N   ILE B 196     6277  12769  15582    517   3322   3609       N  
ATOM   3836  CA  ILE B 196      35.183  13.949  21.904  1.00 87.95           C  
ANISOU 3836  CA  ILE B 196     5938  12453  15026    553   3274   3534       C  
ATOM   3837  C   ILE B 196      33.957  14.774  22.272  1.00 85.30           C  
ANISOU 3837  C   ILE B 196     5612  12041  14758    577   3316   3538       C  
ATOM   3838  O   ILE B 196      32.814  14.349  22.053  1.00 84.54           O  
ANISOU 3838  O   ILE B 196     5584  12009  14530    636   3306   3547       O  
ATOM   3839  CB  ILE B 196      35.731  13.175  23.118  1.00 88.39           C  
ANISOU 3839  CB  ILE B 196     5963  12558  15062    504   3207   3399       C  
ATOM   3840  CG1 ILE B 196      36.804  12.174  22.681  1.00 87.28           C  
ANISOU 3840  CG1 ILE B 196     5820  12507  14835    501   3163   3401       C  
ATOM   3841  CG2 ILE B 196      34.610  12.457  23.855  1.00 83.42           C  
ANISOU 3841  CG2 ILE B 196     5397  11998  14302    531   3174   3316       C  
ATOM   3842  CD1 ILE B 196      37.511  11.492  23.839  1.00 84.04           C  
ANISOU 3842  CD1 ILE B 196     5356  12142  14433    458   3096   3294       C  
ATOM   3843  N   ILE B 197      34.170  15.952  22.863  1.00 89.47           N  
ANISOU 3843  N   ILE B 197     6070  12428  15498    528   3369   3523       N  
ATOM   3844  CA  ILE B 197      33.042  16.805  23.226  1.00 91.91           C  
ANISOU 3844  CA  ILE B 197     6381  12643  15898    551   3424   3525       C  
ATOM   3845  C   ILE B 197      32.303  17.270  21.977  1.00 92.45           C  
ANISOU 3845  C   ILE B 197     6483  12698  15947    637   3472   3686       C  
ATOM   3846  O   ILE B 197      31.070  17.376  21.973  1.00 89.60           O  
ANISOU 3846  O   ILE B 197     6154  12342  15549    695   3485   3702       O  
ATOM   3847  CB  ILE B 197      33.514  17.989  24.092  1.00 92.94           C  
ANISOU 3847  CB  ILE B 197     6428  12611  16274    470   3486   3468       C  
ATOM   3848  CG1 ILE B 197      34.068  17.483  25.427  1.00 97.88           C  
ANISOU 3848  CG1 ILE B 197     7014  13272  16905    382   3430   3306       C  
ATOM   3849  CG2 ILE B 197      32.375  18.966  24.345  1.00 88.80           C  
ANISOU 3849  CG2 ILE B 197     5905  11964  15871    498   3564   3482       C  
ATOM   3850  CD1 ILE B 197      34.733  18.558  26.270  1.00102.50           C  
ANISOU 3850  CD1 ILE B 197     7508  13715  17722    275   3484   3233       C  
ATOM   3851  N   ALA B 198      33.039  17.545  20.896  1.00 93.75           N  
ANISOU 3851  N   ALA B 198     6634  12851  16134    645   3500   3810       N  
ATOM   3852  CA  ALA B 198      32.379  17.909  19.645  1.00 93.03           C  
ANISOU 3852  CA  ALA B 198     6570  12770  16008    726   3541   3981       C  
ATOM   3853  C   ALA B 198      31.500  16.771  19.139  1.00 93.54           C  
ANISOU 3853  C   ALA B 198     6711  13003  15826    787   3479   3987       C  
ATOM   3854  O   ALA B 198      30.377  17.001  18.670  1.00 94.55           O  
ANISOU 3854  O   ALA B 198     6859  13152  15915    858   3495   4071       O  
ATOM   3855  CB  ALA B 198      33.419  18.297  18.594  1.00 89.29           C  
ANISOU 3855  CB  ALA B 198     6072  12267  15589    711   3584   4105       C  
ATOM   3856  N   VAL B 199      31.982  15.530  19.261  1.00 92.53           N  
ANISOU 3856  N   VAL B 199     6624  12997  15536    760   3409   3896       N  
ATOM   3857  CA  VAL B 199      31.190  14.387  18.809  1.00 90.56           C  
ANISOU 3857  CA  VAL B 199     6452  12904  15051    805   3359   3882       C  
ATOM   3858  C   VAL B 199      29.944  14.215  19.676  1.00 90.08           C  
ANISOU 3858  C   VAL B 199     6417  12860  14949    829   3339   3789       C  
ATOM   3859  O   VAL B 199      28.843  13.960  19.166  1.00 83.80           O  
ANISOU 3859  O   VAL B 199     5661  12143  14035    886   3333   3830       O  
ATOM   3860  CB  VAL B 199      32.051  13.109  18.796  1.00 87.81           C  
ANISOU 3860  CB  VAL B 199     6140  12661  14562    768   3304   3801       C  
ATOM   3861  CG1 VAL B 199      31.215  11.903  18.389  1.00 90.55           C  
ANISOU 3861  CG1 VAL B 199     6574  13160  14673    804   3264   3769       C  
ATOM   3862  CG2 VAL B 199      33.239  13.275  17.862  1.00 84.60           C  
ANISOU 3862  CG2 VAL B 199     5707  12239  14197    745   3332   3890       C  
ATOM   3863  N   TRP B 200      30.096  14.353  20.997  1.00 87.59           N  
ANISOU 3863  N   TRP B 200     6074  12477  14730    781   3333   3659       N  
ATOM   3864  CA  TRP B 200      28.946  14.244  21.895  1.00 88.83           C  
ANISOU 3864  CA  TRP B 200     6253  12637  14862    794   3327   3559       C  
ATOM   3865  C   TRP B 200      27.912  15.326  21.608  1.00 88.78           C  
ANISOU 3865  C   TRP B 200     6220  12547  14967    851   3386   3647       C  
ATOM   3866  O   TRP B 200      26.701  15.066  21.636  1.00 83.90           O  
ANISOU 3866  O   TRP B 200     5635  11984  14259    898   3378   3626       O  
ATOM   3867  CB  TRP B 200      29.401  14.325  23.353  1.00 92.66           C  
ANISOU 3867  CB  TRP B 200     6701  13055  15450    720   3321   3413       C  
ATOM   3868  CG  TRP B 200      29.744  13.003  23.978  1.00 93.26           C  
ANISOU 3868  CG  TRP B 200     6817  13245  15372    687   3254   3297       C  
ATOM   3869  CD1 TRP B 200      30.992  12.543  24.285  1.00 95.59           C  
ANISOU 3869  CD1 TRP B 200     7084  13562  15676    636   3218   3261       C  
ATOM   3870  CD2 TRP B 200      28.827  11.980  24.390  1.00 90.68           C  
ANISOU 3870  CD2 TRP B 200     6563  13023  14869    707   3223   3205       C  
ATOM   3871  NE1 TRP B 200      30.909  11.295  24.855  1.00 94.81           N  
ANISOU 3871  NE1 TRP B 200     7033  13571  15420    630   3166   3166       N  
ATOM   3872  CE2 TRP B 200      29.592  10.927  24.931  1.00 91.33           C  
ANISOU 3872  CE2 TRP B 200     6660  13180  14861    670   3172   3127       C  
ATOM   3873  CE3 TRP B 200      27.435  11.851  24.350  1.00 89.02           C  
ANISOU 3873  CE3 TRP B 200     6401  12850  14572    752   3235   3182       C  
ATOM   3874  CZ2 TRP B 200      29.012   9.761  25.427  1.00 88.49           C  
ANISOU 3874  CZ2 TRP B 200     6371  12923  14329    676   3143   3032       C  
ATOM   3875  CZ3 TRP B 200      26.861  10.691  24.844  1.00 87.37           C  
ANISOU 3875  CZ3 TRP B 200     6261  12747  14187    751   3204   3073       C  
ATOM   3876  CH2 TRP B 200      27.649   9.662  25.375  1.00 87.27           C  
ANISOU 3876  CH2 TRP B 200     6271  12800  14088    712   3162   3001       C  
ATOM   3877  N   THR B 201      28.371  16.550  21.334  1.00 94.04           N  
ANISOU 3877  N   THR B 201     6823  13073  15835    848   3451   3748       N  
ATOM   3878  CA  THR B 201      27.453  17.635  21.006  1.00 95.69           C  
ANISOU 3878  CA  THR B 201     6999  13187  16174    912   3518   3855       C  
ATOM   3879  C   THR B 201      26.729  17.366  19.693  1.00 93.74           C  
ANISOU 3879  C   THR B 201     6779  13055  15784    999   3503   4006       C  
ATOM   3880  O   THR B 201      25.528  17.635  19.577  1.00 91.12           O  
ANISOU 3880  O   THR B 201     6441  12730  15450   1066   3517   4047       O  
ATOM   3881  CB  THR B 201      28.211  18.961  20.941  1.00 97.88           C  
ANISOU 3881  CB  THR B 201     7206  13283  16701    887   3602   3938       C  
ATOM   3882  OG1 THR B 201      28.831  19.217  22.207  1.00 88.81           O  
ANISOU 3882  OG1 THR B 201     6025  12037  15683    794   3616   3784       O  
ATOM   3883  CG2 THR B 201      27.264  20.104  20.610  1.00105.11           C  
ANISOU 3883  CG2 THR B 201     8083  14083  17769    963   3682   4062       C  
ATOM   3884  N   ILE B 202      27.443  16.841  18.693  1.00 94.06           N  
ANISOU 3884  N   ILE B 202     6843  13189  15707    995   3477   4089       N  
ATOM   3885  CA  ILE B 202      26.791  16.468  17.440  1.00 90.62           C  
ANISOU 3885  CA  ILE B 202     6433  12886  15111   1062   3460   4221       C  
ATOM   3886  C   ILE B 202      25.705  15.431  17.694  1.00 90.62           C  
ANISOU 3886  C   ILE B 202     6489  13029  14913   1083   3400   4115       C  
ATOM   3887  O   ILE B 202      24.600  15.518  17.144  1.00 85.68           O  
ANISOU 3887  O   ILE B 202     5857  12470  14225   1150   3399   4195       O  
ATOM   3888  CB  ILE B 202      27.831  15.962  16.423  1.00 86.58           C  
ANISOU 3888  CB  ILE B 202     5945  12453  14500   1035   3447   4294       C  
ATOM   3889  CG1 ILE B 202      28.716  17.113  15.940  1.00 98.35           C  
ANISOU 3889  CG1 ILE B 202     7375  13807  16185   1027   3521   4433       C  
ATOM   3890  CG2 ILE B 202      27.148  15.281  15.246  1.00 86.34           C  
ANISOU 3890  CG2 ILE B 202     5953  12595  14258   1082   3419   4387       C  
ATOM   3891  CD1 ILE B 202      29.819  16.680  14.997  1.00 99.82           C  
ANISOU 3891  CD1 ILE B 202     7579  14054  16293    991   3520   4491       C  
ATOM   3892  N   SER B 203      25.996  14.443  18.543  1.00 95.69           N  
ANISOU 3892  N   SER B 203     7181  13721  15457   1025   3352   3937       N  
ATOM   3893  CA  SER B 203      25.015  13.399  18.824  1.00 97.77           C  
ANISOU 3893  CA  SER B 203     7505  14114  15530   1035   3305   3823       C  
ATOM   3894  C   SER B 203      23.782  13.971  19.518  1.00 94.90           C  
ANISOU 3894  C   SER B 203     7115  13694  15249   1073   3328   3780       C  
ATOM   3895  O   SER B 203      22.640  13.658  19.149  1.00 90.38           O  
ANISOU 3895  O   SER B 203     6558  13220  14563   1120   3312   3791       O  
ATOM   3896  CB  SER B 203      25.656  12.307  19.678  1.00103.88           C  
ANISOU 3896  CB  SER B 203     8332  14930  16210    967   3264   3653       C  
ATOM   3897  OG  SER B 203      26.956  12.004  19.204  1.00106.24           O  
ANISOU 3897  OG  SER B 203     8632  15237  16496    931   3254   3690       O  
ATOM   3898  N   VAL B 204      23.995  14.823  20.525  1.00 95.41           N  
ANISOU 3898  N   VAL B 204     7133  13600  15517   1047   3370   3725       N  
ATOM   3899  CA  VAL B 204      22.873  15.442  21.228  1.00 93.97           C  
ANISOU 3899  CA  VAL B 204     6922  13342  15441   1078   3406   3675       C  
ATOM   3900  C   VAL B 204      22.043  16.287  20.270  1.00 94.95           C  
ANISOU 3900  C   VAL B 204     6996  13450  15632   1172   3441   3854       C  
ATOM   3901  O   VAL B 204      20.806  16.272  20.316  1.00 97.49           O  
ANISOU 3901  O   VAL B 204     7310  13813  15919   1224   3439   3838       O  
ATOM   3902  CB  VAL B 204      23.378  16.269  22.425  1.00 92.14           C  
ANISOU 3902  CB  VAL B 204     6647  12930  15431   1020   3459   3585       C  
ATOM   3903  CG1 VAL B 204      22.244  17.086  23.027  1.00 85.42           C  
ANISOU 3903  CG1 VAL B 204     5758  11972  14724   1056   3518   3550       C  
ATOM   3904  CG2 VAL B 204      23.993  15.359  23.477  1.00 93.91           C  
ANISOU 3904  CG2 VAL B 204     6912  13194  15573    934   3419   3407       C  
ATOM   3905  N   GLY B 205      22.707  17.031  19.382  1.00 91.76           N  
ANISOU 3905  N   GLY B 205     6550  12988  15326   1196   3474   4032       N  
ATOM   3906  CA  GLY B 205      21.979  17.851  18.426  1.00 89.65           C  
ANISOU 3906  CA  GLY B 205     6226  12709  15127   1291   3510   4231       C  
ATOM   3907  C   GLY B 205      21.162  17.025  17.452  1.00 92.78           C  
ANISOU 3907  C   GLY B 205     6648  13314  15291   1342   3451   4296       C  
ATOM   3908  O   GLY B 205      20.039  17.395  17.100  1.00 88.10           O  
ANISOU 3908  O   GLY B 205     6010  12751  14711   1422   3459   4382       O  
ATOM   3909  N   ILE B 206      21.714  15.897  16.999  1.00 93.85           N  
ANISOU 3909  N   ILE B 206     6848  13594  15215   1294   3396   4254       N  
ATOM   3910  CA  ILE B 206      20.955  15.022  16.112  1.00 94.82           C  
ANISOU 3910  CA  ILE B 206     7000  13921  15106   1323   3345   4289       C  
ATOM   3911  C   ILE B 206      19.758  14.429  16.845  1.00 98.99           C  
ANISOU 3911  C   ILE B 206     7552  14517  15544   1329   3315   4129       C  
ATOM   3912  O   ILE B 206      18.690  14.234  16.250  1.00102.77           O  
ANISOU 3912  O   ILE B 206     8012  15120  15916   1381   3293   4182       O  
ATOM   3913  CB  ILE B 206      21.863  13.924  15.528  1.00 89.72           C  
ANISOU 3913  CB  ILE B 206     6425  13395  14269   1260   3307   4257       C  
ATOM   3914  CG1 ILE B 206      22.984  14.542  14.695  1.00 87.99           C  
ANISOU 3914  CG1 ILE B 206     6177  13118  14139   1256   3344   4422       C  
ATOM   3915  CG2 ILE B 206      21.062  12.975  14.662  1.00 86.31           C  
ANISOU 3915  CG2 ILE B 206     6027  13173  13595   1275   3263   4269       C  
ATOM   3916  CD1 ILE B 206      23.971  13.530  14.156  1.00 85.08           C  
ANISOU 3916  CD1 ILE B 206     5873  12844  13611   1191   3317   4382       C  
ATOM   3917  N   SER B 207      19.901  14.144  18.138  1.00 97.79           N  
ANISOU 3917  N   SER B 207     7436  14290  15430   1273   3316   3934       N  
ATOM   3918  CA  SER B 207      18.815  13.550  18.907  1.00 98.93           C  
ANISOU 3918  CA  SER B 207     7610  14491  15490   1268   3298   3768       C  
ATOM   3919  C   SER B 207      17.857  14.586  19.486  1.00 99.86           C  
ANISOU 3919  C   SER B 207     7657  14489  15795   1323   3344   3771       C  
ATOM   3920  O   SER B 207      16.798  14.207  19.999  1.00 94.24           O  
ANISOU 3920  O   SER B 207     6956  13828  15024   1330   3336   3650       O  
ATOM   3921  CB  SER B 207      19.383  12.686  20.034  1.00 98.40           C  
ANISOU 3921  CB  SER B 207     7615  14411  15362   1180   3282   3561       C  
ATOM   3922  OG  SER B 207      20.311  11.752  19.516  1.00 98.49           O  
ANISOU 3922  OG  SER B 207     7685  14514  15221   1136   3245   3560       O  
ATOM   3923  N   MET B 208      18.204  15.871  19.414  1.00107.82           N  
ANISOU 3923  N   MET B 208     8596  15336  17037   1360   3401   3901       N  
ATOM   3924  CA  MET B 208      17.351  16.913  19.978  1.00111.19           C  
ANISOU 3924  CA  MET B 208     8954  15623  17670   1413   3459   3904       C  
ATOM   3925  C   MET B 208      15.935  16.980  19.397  1.00109.30           C  
ANISOU 3925  C   MET B 208     8667  15482  17380   1505   3444   3977       C  
ATOM   3926  O   MET B 208      15.028  17.386  20.145  1.00110.58           O  
ANISOU 3926  O   MET B 208     8797  15566  17654   1530   3478   3889       O  
ATOM   3927  CB  MET B 208      18.048  18.274  19.822  1.00118.63           C  
ANISOU 3927  CB  MET B 208     9831  16370  18872   1438   3533   4054       C  
ATOM   3928  CG  MET B 208      17.411  19.396  20.620  1.00124.89           C  
ANISOU 3928  CG  MET B 208    10563  16969  19920   1473   3614   4025       C  
ATOM   3929  SD  MET B 208      17.659  19.198  22.395  1.00128.90           S  
ANISOU 3929  SD  MET B 208    11116  17362  20500   1359   3645   3739       S  
ATOM   3930  CE  MET B 208      19.423  19.472  22.526  1.00132.30           C  
ANISOU 3930  CE  MET B 208    11556  17694  21018   1271   3665   3758       C  
ATOM   3931  N   PRO B 209      15.676  16.668  18.118  1.00103.30           N  
ANISOU 3931  N   PRO B 209     7891  14886  16473   1555   3400   4135       N  
ATOM   3932  CA  PRO B 209      14.285  16.704  17.632  1.00101.37           C  
ANISOU 3932  CA  PRO B 209     7587  14752  16178   1639   3380   4195       C  
ATOM   3933  C   PRO B 209      13.314  15.829  18.415  1.00 98.57           C  
ANISOU 3933  C   PRO B 209     7272  14483  15698   1605   3352   3968       C  
ATOM   3934  O   PRO B 209      12.105  16.092  18.376  1.00 98.45           O  
ANISOU 3934  O   PRO B 209     7194  14501  15713   1671   3352   3978       O  
ATOM   3935  CB  PRO B 209      14.415  16.227  16.182  1.00 99.54           C  
ANISOU 3935  CB  PRO B 209     7350  14715  15755   1662   3329   4368       C  
ATOM   3936  CG  PRO B 209      15.755  16.691  15.773  1.00 96.17           C  
ANISOU 3936  CG  PRO B 209     6933  14195  15411   1640   3360   4494       C  
ATOM   3937  CD  PRO B 209      16.625  16.569  16.991  1.00 99.06           C  
ANISOU 3937  CD  PRO B 209     7362  14415  15859   1551   3384   4303       C  
ATOM   3938  N   ILE B 210      13.791  14.803  19.110  1.00 97.19           N  
ANISOU 3938  N   ILE B 210     7194  14346  15387   1506   3331   3770       N  
ATOM   3939  CA  ILE B 210      12.909  13.863  19.801  1.00 95.18           C  
ANISOU 3939  CA  ILE B 210     6987  14184  14993   1465   3311   3557       C  
ATOM   3940  C   ILE B 210      12.257  14.485  21.036  1.00 95.88           C  
ANISOU 3940  C   ILE B 210     7046  14119  15265   1469   3369   3423       C  
ATOM   3941  O   ILE B 210      11.033  14.357  21.191  1.00 95.17           O  
ANISOU 3941  O   ILE B 210     6926  14088  15147   1501   3368   3352       O  
ATOM   3942  CB  ILE B 210      13.658  12.568  20.163  1.00 92.12           C  
ANISOU 3942  CB  ILE B 210     6714  13875  14411   1362   3280   3401       C  
ATOM   3943  CG1 ILE B 210      14.166  11.874  18.899  1.00 94.02           C  
ANISOU 3943  CG1 ILE B 210     6987  14275  14463   1355   3231   3514       C  
ATOM   3944  CG2 ILE B 210      12.757  11.630  20.959  1.00 90.48           C  
ANISOU 3944  CG2 ILE B 210     6560  13746  14074   1317   3276   3179       C  
ATOM   3945  CD1 ILE B 210      15.127  10.742  19.175  1.00 95.47           C  
ANISOU 3945  CD1 ILE B 210     7277  14500  14498   1264   3210   3392       C  
ATOM   3946  N   PRO B 211      12.988  15.150  21.943  1.00 95.82           N  
ANISOU 3946  N   PRO B 211     7043  13918  15446   1433   3424   3375       N  
ATOM   3947  CA  PRO B 211      12.292  15.784  23.079  1.00 98.42           C  
ANISOU 3947  CA  PRO B 211     7341  14098  15956   1433   3491   3246       C  
ATOM   3948  C   PRO B 211      11.318  16.885  22.689  1.00104.90           C  
ANISOU 3948  C   PRO B 211     8055  14844  16958   1543   3528   3372       C  
ATOM   3949  O   PRO B 211      10.235  16.970  23.276  1.00110.13           O  
ANISOU 3949  O   PRO B 211     8690  15485  17667   1560   3557   3256       O  
ATOM   3950  CB  PRO B 211      13.445  16.331  23.933  1.00 96.00           C  
ANISOU 3950  CB  PRO B 211     7053  13608  15816   1365   3543   3201       C  
ATOM   3951  CG  PRO B 211      14.605  15.488  23.589  1.00 94.03           C  
ANISOU 3951  CG  PRO B 211     6871  13454  15401   1305   3487   3216       C  
ATOM   3952  CD  PRO B 211      14.450  15.166  22.136  1.00 94.59           C  
ANISOU 3952  CD  PRO B 211     6930  13686  15326   1368   3428   3389       C  
ATOM   3953  N   VAL B 212      11.664  17.738  21.725  1.00104.65           N  
ANISOU 3953  N   VAL B 212     7959  14768  17037   1620   3534   3609       N  
ATOM   3954  CA  VAL B 212      10.785  18.853  21.373  1.00106.84           C  
ANISOU 3954  CA  VAL B 212     8128  14955  17510   1735   3577   3749       C  
ATOM   3955  C   VAL B 212       9.475  18.340  20.781  1.00109.02           C  
ANISOU 3955  C   VAL B 212     8362  15423  17639   1800   3519   3764       C  
ATOM   3956  O   VAL B 212       8.393  18.518  21.360  1.00106.87           O  
ANISOU 3956  O   VAL B 212     8050  15116  17439   1828   3546   3656       O  
ATOM   3957  CB  VAL B 212      11.498  19.819  20.411  1.00106.27           C  
ANISOU 3957  CB  VAL B 212     8001  14803  17575   1803   3600   4019       C  
ATOM   3958  CG1 VAL B 212      10.544  20.910  19.948  1.00111.24           C  
ANISOU 3958  CG1 VAL B 212     8515  15354  18396   1936   3640   4191       C  
ATOM   3959  CG2 VAL B 212      12.724  20.422  21.080  1.00101.91           C  
ANISOU 3959  CG2 VAL B 212     7478  14045  17197   1733   3669   3985       C  
ATOM   3960  N   PHE B 213       9.562  17.650  19.642  1.00111.84           N  
ANISOU 3960  N   PHE B 213     8726  15990  17778   1814   3442   3883       N  
ATOM   3961  CA  PHE B 213       8.367  17.204  18.938  1.00111.70           C  
ANISOU 3961  CA  PHE B 213     8653  16172  17617   1873   3385   3921       C  
ATOM   3962  C   PHE B 213       7.725  15.989  19.588  1.00107.41           C  
ANISOU 3962  C   PHE B 213     8176  15757  16878   1793   3357   3662       C  
ATOM   3963  O   PHE B 213       6.528  15.756  19.389  1.00106.67           O  
ANISOU 3963  O   PHE B 213     8026  15782  16721   1834   3332   3630       O  
ATOM   3964  CB  PHE B 213       8.702  16.891  17.477  1.00114.05           C  
ANISOU 3964  CB  PHE B 213     8933  16655  17745   1904   3323   4137       C  
ATOM   3965  CG  PHE B 213       9.040  18.105  16.655  1.00115.52           C  
ANISOU 3965  CG  PHE B 213     9033  16748  18112   2004   3351   4427       C  
ATOM   3966  CD1 PHE B 213       8.102  18.658  15.799  1.00114.41           C  
ANISOU 3966  CD1 PHE B 213     8775  16688  18010   2125   3331   4626       C  
ATOM   3967  CD2 PHE B 213      10.292  18.694  16.738  1.00116.30           C  
ANISOU 3967  CD2 PHE B 213     9162  16681  18344   1979   3401   4504       C  
ATOM   3968  CE1 PHE B 213       8.403  19.773  15.040  1.00115.54           C  
ANISOU 3968  CE1 PHE B 213     8837  16742  18320   2222   3365   4908       C  
ATOM   3969  CE2 PHE B 213      10.600  19.812  15.981  1.00117.40           C  
ANISOU 3969  CE2 PHE B 213     9224  16728  18655   2068   3441   4772       C  
ATOM   3970  CZ  PHE B 213       9.653  20.352  15.131  1.00117.26           C  
ANISOU 3970  CZ  PHE B 213     9094  16786  18674   2193   3425   4980       C  
ATOM   3971  N   GLY B 214       8.490  15.209  20.352  1.00104.27           N  
ANISOU 3971  N   GLY B 214     7891  15341  16385   1680   3362   3482       N  
ATOM   3972  CA  GLY B 214       7.907  14.065  21.029  1.00 97.83           C  
ANISOU 3972  CA  GLY B 214     7144  14631  15394   1602   3350   3239       C  
ATOM   3973  C   GLY B 214       7.064  14.479  22.219  1.00 91.68           C  
ANISOU 3973  C   GLY B 214     6341  13724  14769   1600   3414   3068       C  
ATOM   3974  O   GLY B 214       6.000  13.907  22.467  1.00 91.89           O  
ANISOU 3974  O   GLY B 214     6362  13852  14701   1589   3408   2927       O  
ATOM   3975  N   LEU B 215       7.533  15.471  22.980  1.00 87.17           N  
ANISOU 3975  N   LEU B 215     5755  12925  14439   1603   3483   3067       N  
ATOM   3976  CA  LEU B 215       6.757  15.966  24.109  1.00 91.28           C  
ANISOU 3976  CA  LEU B 215     6250  13304  15128   1598   3559   2907       C  
ATOM   3977  C   LEU B 215       5.629  16.895  23.673  1.00105.86           C  
ANISOU 3977  C   LEU B 215     7971  15114  17138   1719   3576   3018       C  
ATOM   3978  O   LEU B 215       4.571  16.909  24.314  1.00115.50           O  
ANISOU 3978  O   LEU B 215     9162  16315  18409   1723   3613   2870       O  
ATOM   3979  CB  LEU B 215       7.666  16.674  25.113  1.00 87.71           C  
ANISOU 3979  CB  LEU B 215     5830  12620  14877   1542   3637   2851       C  
ATOM   3980  CG  LEU B 215       8.768  15.805  25.728  1.00 86.03           C  
ANISOU 3980  CG  LEU B 215     5730  12431  14526   1421   3624   2729       C  
ATOM   3981  CD1 LEU B 215       9.552  16.572  26.786  1.00 86.32           C  
ANISOU 3981  CD1 LEU B 215     5780  12242  14775   1361   3707   2661       C  
ATOM   3982  CD2 LEU B 215       8.209  14.508  26.284  1.00 93.80           C  
ANISOU 3982  CD2 LEU B 215     6792  13560  15286   1347   3606   2517       C  
ATOM   3983  N   GLN B 216       5.821  17.678  22.605  1.00108.65           N  
ANISOU 3983  N   GLN B 216     8245  15455  17581   1820   3555   3279       N  
ATOM   3984  CA  GLN B 216       4.715  18.501  22.119  1.00111.55           C  
ANISOU 3984  CA  GLN B 216     8486  15806  18093   1947   3563   3404       C  
ATOM   3985  C   GLN B 216       3.579  17.646  21.566  1.00110.94           C  
ANISOU 3985  C   GLN B 216     8369  15975  17808   1970   3490   3365       C  
ATOM   3986  O   GLN B 216       2.402  17.990  21.732  1.00110.81           O  
ANISOU 3986  O   GLN B 216     8267  15951  17886   2033   3506   3326       O  
ATOM   3987  CB  GLN B 216       5.201  19.494  21.063  1.00115.36           C  
ANISOU 3987  CB  GLN B 216     8896  16230  18708   2051   3559   3711       C  
ATOM   3988  CG  GLN B 216       5.881  20.726  21.640  1.00119.48           C  
ANISOU 3988  CG  GLN B 216     9408  16461  19528   2062   3661   3759       C  
ATOM   3989  CD  GLN B 216       5.880  21.895  20.673  1.00125.44           C  
ANISOU 3989  CD  GLN B 216    10061  17133  20469   2196   3680   4060       C  
ATOM   3990  OE1 GLN B 216       5.064  21.951  19.752  1.00126.24           O  
ANISOU 3990  OE1 GLN B 216    10075  17372  20519   2299   3625   4218       O  
ATOM   3991  NE2 GLN B 216       6.792  22.837  20.880  1.00129.85           N  
ANISOU 3991  NE2 GLN B 216    10626  17468  21243   2194   3762   4144       N  
ATOM   3992  N   ASP B 217       3.903  16.533  20.911  1.00111.71           N  
ANISOU 3992  N   ASP B 217     8526  16289  17629   1916   3414   3367       N  
ATOM   3993  CA  ASP B 217       2.913  15.709  20.225  1.00113.99           C  
ANISOU 3993  CA  ASP B 217     8775  16828  17709   1930   3344   3349       C  
ATOM   3994  C   ASP B 217       3.064  14.266  20.682  1.00116.21           C  
ANISOU 3994  C   ASP B 217     9178  17238  17737   1797   3327   3115       C  
ATOM   3995  O   ASP B 217       4.117  13.655  20.474  1.00116.89           O  
ANISOU 3995  O   ASP B 217     9362  17364  17687   1728   3305   3125       O  
ATOM   3996  CB  ASP B 217       3.072  15.812  18.705  1.00111.36           C  
ANISOU 3996  CB  ASP B 217     8378  16654  17281   2005   3273   3625       C  
ATOM   3997  CG  ASP B 217       1.964  15.101  17.949  1.00110.60           C  
ANISOU 3997  CG  ASP B 217     8216  16819  16989   2026   3204   3622       C  
ATOM   3998  OD1 ASP B 217       0.989  14.654  18.590  1.00110.13           O  
ANISOU 3998  OD1 ASP B 217     8146  16800  16900   1996   3215   3415       O  
ATOM   3999  OD2 ASP B 217       2.067  14.987  16.709  1.00111.64           O  
ANISOU 3999  OD2 ASP B 217     8303  17119  16995   2066   3142   3826       O  
ATOM   4000  N   ASP B 218       2.007  13.720  21.289  1.00115.90           N  
ANISOU 4000  N   ASP B 218     9134  17261  17641   1763   3343   2905       N  
ATOM   4001  CA  ASP B 218       2.041  12.344  21.774  1.00111.24           C  
ANISOU 4001  CA  ASP B 218     8662  16784  16820   1638   3340   2675       C  
ATOM   4002  C   ASP B 218       2.067  11.324  20.643  1.00102.64           C  
ANISOU 4002  C   ASP B 218     7597  15940  15463   1610   3265   2733       C  
ATOM   4003  O   ASP B 218       2.479  10.181  20.868  1.00100.00           O  
ANISOU 4003  O   ASP B 218     7383  15678  14934   1504   3263   2589       O  
ATOM   4004  CB  ASP B 218       0.834  12.072  22.675  1.00119.12           C  
ANISOU 4004  CB  ASP B 218     9641  17784  17834   1608   3387   2440       C  
ATOM   4005  CG  ASP B 218       0.813  12.952  23.909  1.00124.99           C  
ANISOU 4005  CG  ASP B 218    10379  18285  18825   1611   3476   2344       C  
ATOM   4006  OD1 ASP B 218       1.884  13.463  24.298  1.00126.58           O  
ANISOU 4006  OD1 ASP B 218    10632  18324  19141   1595   3506   2398       O  
ATOM   4007  OD2 ASP B 218      -0.278  13.130  24.492  1.00127.81           O  
ANISOU 4007  OD2 ASP B 218    10680  18615  19265   1623   3521   2208       O  
ATOM   4008  N   SER B 219       1.641  11.706  19.438  1.00100.29           N  
ANISOU 4008  N   SER B 219     7189  15767  15151   1702   3209   2943       N  
ATOM   4009  CA  SER B 219       1.507  10.741  18.352  1.00 93.70           C  
ANISOU 4009  CA  SER B 219     6365  15180  14057   1669   3145   2987       C  
ATOM   4010  C   SER B 219       2.843  10.420  17.697  1.00 97.91           C  
ANISOU 4010  C   SER B 219     6986  15737  14480   1631   3119   3111       C  
ATOM   4011  O   SER B 219       3.002   9.337  17.123  1.00 98.84           O  
ANISOU 4011  O   SER B 219     7171  16021  14362   1558   3088   3067       O  
ATOM   4012  CB  SER B 219       0.531  11.268  17.299  1.00 91.42           C  
ANISOU 4012  CB  SER B 219     5915  15037  13783   1779   3092   3174       C  
ATOM   4013  OG  SER B 219       1.084  12.370  16.601  1.00 91.02           O  
ANISOU 4013  OG  SER B 219     5793  14916  13876   1883   3076   3459       O  
ATOM   4014  N   LYS B 220       3.806  11.339  17.769  1.00100.91           N  
ANISOU 4014  N   LYS B 220     7365  15945  15033   1674   3138   3258       N  
ATOM   4015  CA  LYS B 220       5.089  11.152  17.103  1.00100.47           C  
ANISOU 4015  CA  LYS B 220     7376  15901  14896   1645   3118   3390       C  
ATOM   4016  C   LYS B 220       5.988  10.143  17.809  1.00 97.71           C  
ANISOU 4016  C   LYS B 220     7183  15513  14430   1522   3137   3197       C  
ATOM   4017  O   LYS B 220       6.998   9.734  17.228  1.00 96.03           O  
ANISOU 4017  O   LYS B 220     7035  15338  14113   1483   3117   3271       O  
ATOM   4018  CB  LYS B 220       5.795  12.503  16.982  1.00101.75           C  
ANISOU 4018  CB  LYS B 220     7480  15882  15297   1728   3142   3603       C  
ATOM   4019  CG  LYS B 220       4.994  13.511  16.171  1.00105.40           C  
ANISOU 4019  CG  LYS B 220     7789  16382  15877   1861   3123   3832       C  
ATOM   4020  CD  LYS B 220       5.735  14.818  15.954  1.00108.76           C  
ANISOU 4020  CD  LYS B 220     8164  16624  16535   1941   3157   4059       C  
ATOM   4021  CE  LYS B 220       4.871  15.788  15.159  1.00111.75           C  
ANISOU 4021  CE  LYS B 220     8388  17040  17032   2082   3140   4295       C  
ATOM   4022  NZ  LYS B 220       5.569  17.063  14.844  1.00112.03           N  
ANISOU 4022  NZ  LYS B 220     8375  16897  17294   2164   3183   4537       N  
ATOM   4023  N   VAL B 221       5.654   9.738  19.034  1.00 96.36           N  
ANISOU 4023  N   VAL B 221     7071  15267  14275   1462   3178   2960       N  
ATOM   4024  CA  VAL B 221       6.434   8.755  19.775  1.00 91.63           C  
ANISOU 4024  CA  VAL B 221     6615  14635  13564   1351   3197   2781       C  
ATOM   4025  C   VAL B 221       5.625   7.527  20.164  1.00 92.57           C  
ANISOU 4025  C   VAL B 221     6802  14874  13498   1271   3207   2551       C  
ATOM   4026  O   VAL B 221       6.175   6.614  20.787  1.00 87.68           O  
ANISOU 4026  O   VAL B 221     6306  14235  12774   1180   3227   2399       O  
ATOM   4027  CB  VAL B 221       7.083   9.380  21.028  1.00 89.26           C  
ANISOU 4027  CB  VAL B 221     6345  14112  13458   1336   3250   2712       C  
ATOM   4028  CG1 VAL B 221       8.119  10.418  20.626  1.00 89.90           C  
ANISOU 4028  CG1 VAL B 221     6386  14070  13703   1390   3247   2923       C  
ATOM   4029  CG2 VAL B 221       6.020   9.994  21.926  1.00 88.70           C  
ANISOU 4029  CG2 VAL B 221     6209  13950  13542   1366   3299   2603       C  
ATOM   4030  N   PHE B 222       4.340   7.471  19.821  1.00100.18           N  
ANISOU 4030  N   PHE B 222     7686  15958  14420   1300   3197   2522       N  
ATOM   4031  CA  PHE B 222       3.486   6.343  20.168  1.00 97.96           C  
ANISOU 4031  CA  PHE B 222     7462  15787  13973   1220   3215   2298       C  
ATOM   4032  C   PHE B 222       2.863   5.725  18.924  1.00 81.62           C  
ANISOU 4032  C   PHE B 222     5355  13942  11717   1217   3168   2353       C  
ATOM   4033  O   PHE B 222       2.508   6.432  17.976  1.00 83.05           O  
ANISOU 4033  O   PHE B 222     5411  14204  11940   1306   3124   2550       O  
ATOM   4034  CB  PHE B 222       2.380   6.766  21.138  1.00 81.64           C  
ANISOU 4034  CB  PHE B 222     5333  13651  12035   1237   3264   2153       C  
ATOM   4035  CG  PHE B 222       2.837   6.889  22.563  1.00 80.81           C  
ANISOU 4035  CG  PHE B 222     5305  13361  12037   1189   3329   2006       C  
ATOM   4036  CD1 PHE B 222       3.021   5.759  23.342  1.00 79.35           C  
ANISOU 4036  CD1 PHE B 222     5258  13183  11710   1078   3367   1797       C  
ATOM   4037  CD2 PHE B 222       3.077   8.131  23.125  1.00 81.59           C  
ANISOU 4037  CD2 PHE B 222     5340  13279  12381   1253   3357   2081       C  
ATOM   4038  CE1 PHE B 222       3.440   5.866  24.654  1.00 78.71           C  
ANISOU 4038  CE1 PHE B 222     5243  12950  11715   1032   3427   1675       C  
ATOM   4039  CE2 PHE B 222       3.496   8.245  24.437  1.00 80.93           C  
ANISOU 4039  CE2 PHE B 222     5325  13036  12390   1199   3421   1945       C  
ATOM   4040  CZ  PHE B 222       3.677   7.110  25.202  1.00 79.51           C  
ANISOU 4040  CZ  PHE B 222     5274  12882  12052   1090   3453   1746       C  
ATOM   4041  N   LYS B 223       2.737   4.395  18.936  1.00 80.53           N  
ANISOU 4041  N   LYS B 223     5327  13900  11372   1113   3181   2182       N  
ATOM   4042  CA  LYS B 223       2.173   3.631  17.818  1.00 86.06           C  
ANISOU 4042  CA  LYS B 223     6012  14813  11873   1083   3147   2198       C  
ATOM   4043  C   LYS B 223       1.271   2.548  18.409  1.00 91.36           C  
ANISOU 4043  C   LYS B 223     6754  15533  12424    987   3195   1933       C  
ATOM   4044  O   LYS B 223       1.726   1.435  18.690  1.00 90.02           O  
ANISOU 4044  O   LYS B 223     6735  15348  12121    886   3228   1789       O  
ATOM   4045  CB  LYS B 223       3.260   3.031  16.936  1.00 80.32           C  
ANISOU 4045  CB  LYS B 223     5370  14145  11003   1041   3120   2292       C  
ATOM   4046  CG  LYS B 223       2.723   2.362  15.679  1.00 83.72           C  
ANISOU 4046  CG  LYS B 223     5774  14800  11234   1012   3086   2332       C  
ATOM   4047  CD  LYS B 223       3.839   1.860  14.777  1.00 85.97           C  
ANISOU 4047  CD  LYS B 223     6138  15132  11395    972   3067   2431       C  
ATOM   4048  CE  LYS B 223       3.277   1.285  13.485  1.00 86.87           C  
ANISOU 4048  CE  LYS B 223     6214  15479  11312    941   3035   2480       C  
ATOM   4049  NZ  LYS B 223       4.349   0.818  12.562  1.00 86.00           N  
ANISOU 4049  NZ  LYS B 223     6178  15413  11086    897   3024   2571       N  
ATOM   4050  N   GLU B 224      -0.006   2.889  18.596  1.00 92.26           N  
ANISOU 4050  N   GLU B 224     6758  15698  12598   1021   3203   1874       N  
ATOM   4051  CA  GLU B 224      -1.008   1.970  19.141  1.00 91.59           C  
ANISOU 4051  CA  GLU B 224     6722  15656  12420    934   3256   1625       C  
ATOM   4052  C   GLU B 224      -0.588   1.418  20.505  1.00 89.06           C  
ANISOU 4052  C   GLU B 224     6553  15170  12114    849   3334   1416       C  
ATOM   4053  O   GLU B 224      -0.544   0.206  20.724  1.00 78.18           O  
ANISOU 4053  O   GLU B 224     5317  13803  10585    742   3377   1252       O  
ATOM   4054  CB  GLU B 224      -1.314   0.839  18.155  1.00 98.06           C  
ANISOU 4054  CB  GLU B 224     7588  16660  13008    859   3239   1590       C  
ATOM   4055  CG  GLU B 224      -1.848   1.321  16.815  1.00107.88           C  
ANISOU 4055  CG  GLU B 224     8674  18106  14211    934   3162   1789       C  
ATOM   4056  CD  GLU B 224      -2.402   0.195  15.967  1.00118.93           C  
ANISOU 4056  CD  GLU B 224    10106  19699  15382    848   3155   1715       C  
ATOM   4057  OE1 GLU B 224      -2.479  -0.946  16.467  1.00122.77           O  
ANISOU 4057  OE1 GLU B 224    10741  20142  15764    734   3219   1499       O  
ATOM   4058  OE2 GLU B 224      -2.761   0.452  14.799  1.00124.95           O  
ANISOU 4058  OE2 GLU B 224    10748  20657  16070    894   3090   1879       O  
ATOM   4059  N   GLY B 225      -0.274   2.327  21.427  1.00 89.43           N  
ANISOU 4059  N   GLY B 225     6572  15059  12349    898   3355   1428       N  
ATOM   4060  CA  GLY B 225       0.097   1.980  22.780  1.00 90.45           C  
ANISOU 4060  CA  GLY B 225     6822  15042  12505    827   3427   1250       C  
ATOM   4061  C   GLY B 225       1.560   1.637  22.975  1.00 91.10           C  
ANISOU 4061  C   GLY B 225     7030  15039  12543    793   3420   1297       C  
ATOM   4062  O   GLY B 225       2.083   1.822  24.076  1.00 88.96           O  
ANISOU 4062  O   GLY B 225     6816  14632  12353    773   3461   1230       O  
ATOM   4063  N   SER B 226       2.232   1.144  21.938  1.00 90.66           N  
ANISOU 4063  N   SER B 226     7015  15067  12365    784   3372   1410       N  
ATOM   4064  CA  SER B 226       3.644   0.813  22.046  1.00 84.96           C  
ANISOU 4064  CA  SER B 226     6401  14269  11610    757   3363   1461       C  
ATOM   4065  C   SER B 226       4.494   2.057  21.821  1.00 90.41           C  
ANISOU 4065  C   SER B 226     7004  14878  12469    851   3319   1678       C  
ATOM   4066  O   SER B 226       4.156   2.921  21.006  1.00 94.12           O  
ANISOU 4066  O   SER B 226     7346  15401  13016    935   3276   1843       O  
ATOM   4067  CB  SER B 226       4.018  -0.272  21.037  1.00 75.39           C  
ANISOU 4067  CB  SER B 226     5275  13166  10204    701   3342   1476       C  
ATOM   4068  OG  SER B 226       3.632   0.097  19.724  1.00 79.82           O  
ANISOU 4068  OG  SER B 226     5727  13867  10733    754   3286   1632       O  
ATOM   4069  N   CYS B 227       5.603   2.144  22.553  1.00 88.74           N  
ANISOU 4069  N   CYS B 227     6861  14536  12320    836   3332   1682       N  
ATOM   4070  CA  CYS B 227       6.496   3.300  22.486  1.00 93.26           C  
ANISOU 4070  CA  CYS B 227     7365  15002  13068    911   3305   1867       C  
ATOM   4071  C   CYS B 227       7.488   3.083  21.349  1.00 97.05           C  
ANISOU 4071  C   CYS B 227     7865  15538  13472    920   3254   2029       C  
ATOM   4072  O   CYS B 227       8.564   2.510  21.532  1.00 95.46           O  
ANISOU 4072  O   CYS B 227     7758  15294  13218    875   3255   2015       O  
ATOM   4073  CB  CYS B 227       7.200   3.511  23.819  1.00 92.01           C  
ANISOU 4073  CB  CYS B 227     7260  14684  13016    883   3346   1791       C  
ATOM   4074  SG  CYS B 227       8.414   4.842  23.805  1.00 92.08           S  
ANISOU 4074  SG  CYS B 227     7199  14542  13246    953   3323   1997       S  
ATOM   4075  N   LEU B 228       7.123   3.557  20.160  1.00 97.29           N  
ANISOU 4075  N   LEU B 228     7800  15669  13498    980   3212   2189       N  
ATOM   4076  CA  LEU B 228       7.953   3.440  18.971  1.00 87.34           C  
ANISOU 4076  CA  LEU B 228     6545  14477  12163    990   3170   2353       C  
ATOM   4077  C   LEU B 228       8.009   4.780  18.254  1.00 94.68           C  
ANISOU 4077  C   LEU B 228     7341  15391  13243   1094   3138   2592       C  
ATOM   4078  O   LEU B 228       7.074   5.582  18.331  1.00 79.66           O  
ANISOU 4078  O   LEU B 228     5331  13488  11449   1160   3138   2631       O  
ATOM   4079  CB  LEU B 228       7.417   2.369  18.010  1.00 77.13           C  
ANISOU 4079  CB  LEU B 228     5289  13367  10649    937   3157   2306       C  
ATOM   4080  CG  LEU B 228       7.278   0.942  18.540  1.00 75.87           C  
ANISOU 4080  CG  LEU B 228     5271  13228  10330    830   3197   2075       C  
ATOM   4081  CD1 LEU B 228       6.723   0.028  17.458  1.00 76.07           C  
ANISOU 4081  CD1 LEU B 228     5318  13425  10159    780   3188   2047       C  
ATOM   4082  CD2 LEU B 228       8.613   0.427  19.048  1.00 79.68           C  
ANISOU 4082  CD2 LEU B 228     5869  13600  10806    785   3213   2041       C  
ATOM   4083  N   LEU B 229       9.111   5.016  17.546  1.00104.48           N  
ANISOU 4083  N   LEU B 229     8588  16616  14494   1108   3116   2753       N  
ATOM   4084  CA  LEU B 229       9.233   6.210  16.712  1.00106.43           C  
ANISOU 4084  CA  LEU B 229     8718  16858  14864   1202   3092   3000       C  
ATOM   4085  C   LEU B 229       8.311   6.049  15.510  1.00113.37           C  
ANISOU 4085  C   LEU B 229     9523  17941  15609   1229   3057   3093       C  
ATOM   4086  O   LEU B 229       8.667   5.415  14.514  1.00115.91           O  
ANISOU 4086  O   LEU B 229     9880  18392  15769   1192   3037   3148       O  
ATOM   4087  CB  LEU B 229      10.679   6.415  16.276  1.00101.84           C  
ANISOU 4087  CB  LEU B 229     8170  16208  14317   1197   3086   3133       C  
ATOM   4088  CG  LEU B 229      10.961   7.686  15.471  1.00 98.72           C  
ANISOU 4088  CG  LEU B 229     7666  15781  14064   1288   3075   3395       C  
ATOM   4089  CD1 LEU B 229      10.678   8.927  16.305  1.00 96.45           C  
ANISOU 4089  CD1 LEU B 229     7299  15321  14026   1358   3103   3429       C  
ATOM   4090  CD2 LEU B 229      12.391   7.698  14.952  1.00 97.81           C  
ANISOU 4090  CD2 LEU B 229     7593  15619  13950   1264   3076   3504       C  
ATOM   4091  N   ALA B 230       7.114   6.628  15.602  1.00113.62           N  
ANISOU 4091  N   ALA B 230     9448  18009  15713   1293   3053   3108       N  
ATOM   4092  CA  ALA B 230       6.071   6.414  14.609  1.00106.52           C  
ANISOU 4092  CA  ALA B 230     8467  17323  14682   1316   3017   3170       C  
ATOM   4093  C   ALA B 230       6.034   7.482  13.524  1.00109.04           C  
ANISOU 4093  C   ALA B 230     8652  17703  15076   1422   2982   3464       C  
ATOM   4094  O   ALA B 230       5.360   7.281  12.508  1.00114.87           O  
ANISOU 4094  O   ALA B 230     9319  18647  15679   1438   2944   3555       O  
ATOM   4095  CB  ALA B 230       4.702   6.340  15.294  1.00102.28           C  
ANISOU 4095  CB  ALA B 230     7880  16812  14168   1323   3030   3011       C  
ATOM   4096  N   ASP B 231       6.728   8.603  13.706  1.00104.83           N  
ANISOU 4096  N   ASP B 231     8081  16999  14752   1491   2998   3616       N  
ATOM   4097  CA  ASP B 231       6.711   9.658  12.702  1.00107.76           C  
ANISOU 4097  CA  ASP B 231     8328  17409  15208   1596   2975   3909       C  
ATOM   4098  C   ASP B 231       7.549   9.233  11.500  1.00114.40           C  
ANISOU 4098  C   ASP B 231     9204  18380  15885   1559   2954   4049       C  
ATOM   4099  O   ASP B 231       8.720   8.869  11.644  1.00116.99           O  
ANISOU 4099  O   ASP B 231     9638  18620  16193   1494   2975   4004       O  
ATOM   4100  CB  ASP B 231       7.233  10.968  13.288  1.00105.54           C  
ANISOU 4100  CB  ASP B 231     8005  16883  15211   1672   3014   4018       C  
ATOM   4101  CG  ASP B 231       6.745  12.181  12.519  1.00110.44           C  
ANISOU 4101  CG  ASP B 231     8473  17520  15968   1804   3001   4295       C  
ATOM   4102  OD1 ASP B 231       5.591  12.598  12.752  1.00112.70           O  
ANISOU 4102  OD1 ASP B 231     8663  17820  16336   1873   2994   4286       O  
ATOM   4103  OD2 ASP B 231       7.496  12.703  11.670  1.00112.20           O  
ANISOU 4103  OD2 ASP B 231     8671  17743  16218   1839   3002   4523       O  
ATOM   4104  N   ASP B 232       6.944   9.277  10.310  1.00118.26           N  
ANISOU 4104  N   ASP B 232     9597  19084  16253   1598   2913   4218       N  
ATOM   4105  CA  ASP B 232       7.604   8.748   9.118  1.00119.51           C  
ANISOU 4105  CA  ASP B 232     9788  19397  16221   1547   2896   4328       C  
ATOM   4106  C   ASP B 232       8.830   9.567   8.725  1.00109.95           C  
ANISOU 4106  C   ASP B 232     8578  18061  15136   1583   2921   4535       C  
ATOM   4107  O   ASP B 232       9.866   8.997   8.362  1.00104.60           O  
ANISOU 4107  O   ASP B 232     7996  17384  14362   1506   2934   4514       O  
ATOM   4108  CB  ASP B 232       6.612   8.687   7.957  1.00132.65           C  
ANISOU 4108  CB  ASP B 232    11335  21338  17729   1582   2846   4473       C  
ATOM   4109  CG  ASP B 232       5.466   7.730   8.221  1.00141.77           C  
ANISOU 4109  CG  ASP B 232    12496  22640  18730   1526   2825   4254       C  
ATOM   4110  OD1 ASP B 232       5.636   6.814   9.053  1.00143.17           O  
ANISOU 4110  OD1 ASP B 232    12803  22738  18857   1431   2854   3988       O  
ATOM   4111  OD2 ASP B 232       4.397   7.891   7.594  1.00147.07           O  
ANISOU 4111  OD2 ASP B 232    13039  23509  19331   1575   2781   4351       O  
ATOM   4112  N   ASN B 233       8.733  10.898   8.772  1.00109.52           N  
ANISOU 4112  N   ASN B 233     8417  17891  15305   1697   2933   4734       N  
ATOM   4113  CA  ASN B 233       9.877  11.734   8.414  1.00106.63           C  
ANISOU 4113  CA  ASN B 233     8048  17391  15075   1730   2968   4933       C  
ATOM   4114  C   ASN B 233      11.052  11.505   9.356  1.00 99.79           C  
ANISOU 4114  C   ASN B 233     7310  16311  14296   1655   3009   4763       C  
ATOM   4115  O   ASN B 233      12.208  11.427   8.916  1.00 96.42           O  
ANISOU 4115  O   ASN B 233     6939  15849  13849   1612   3028   4826       O  
ATOM   4116  CB  ASN B 233       9.476  13.209   8.414  1.00109.88           C  
ANISOU 4116  CB  ASN B 233     8325  17690  15734   1867   2985   5159       C  
ATOM   4117  CG  ASN B 233       8.480  13.543   7.323  1.00113.92           C  
ANISOU 4117  CG  ASN B 233     8693  18423  16167   1955   2940   5387       C  
ATOM   4118  OD1 ASN B 233       8.507  12.957   6.241  1.00115.58           O  
ANISOU 4118  OD1 ASN B 233     8897  18865  16154   1916   2907   5475       O  
ATOM   4119  ND2 ASN B 233       7.597  14.495   7.600  1.00115.78           N  
ANISOU 4119  ND2 ASN B 233     8810  18591  16589   2073   2940   5486       N  
ATOM   4120  N   PHE B 234      10.774  11.403  10.659  1.00 97.27           N  
ANISOU 4120  N   PHE B 234     7032  15851  14075   1638   3023   4549       N  
ATOM   4121  CA  PHE B 234      11.834  11.193  11.639  1.00 96.99           C  
ANISOU 4121  CA  PHE B 234     7106  15627  14121   1569   3057   4390       C  
ATOM   4122  C   PHE B 234      12.613   9.915  11.364  1.00 98.14           C  
ANISOU 4122  C   PHE B 234     7372  15859  14056   1458   3045   4263       C  
ATOM   4123  O   PHE B 234      13.843   9.909  11.451  1.00 98.14           O  
ANISOU 4123  O   PHE B 234     7434  15753  14102   1417   3067   4267       O  
ATOM   4124  CB  PHE B 234      11.249  11.170  13.050  1.00 98.71           C  
ANISOU 4124  CB  PHE B 234     7343  15721  14439   1561   3072   4173       C  
ATOM   4125  CG  PHE B 234      11.034  12.534  13.640  1.00102.44           C  
ANISOU 4125  CG  PHE B 234     7730  16002  15190   1648   3109   4260       C  
ATOM   4126  CD1 PHE B 234       9.976  13.324  13.227  1.00106.37           C  
ANISOU 4126  CD1 PHE B 234     8102  16540  15773   1754   3102   4408       C  
ATOM   4127  CD2 PHE B 234      11.888  13.024  14.613  1.00101.71           C  
ANISOU 4127  CD2 PHE B 234     7679  15686  15280   1624   3154   4193       C  
ATOM   4128  CE1 PHE B 234       9.774  14.579  13.769  1.00108.24           C  
ANISOU 4128  CE1 PHE B 234     8264  16581  16282   1836   3146   4484       C  
ATOM   4129  CE2 PHE B 234      11.691  14.278  15.159  1.00103.14           C  
ANISOU 4129  CE2 PHE B 234     7785  15678  15725   1696   3200   4260       C  
ATOM   4130  CZ  PHE B 234      10.633  15.057  14.736  1.00106.69           C  
ANISOU 4130  CZ  PHE B 234     8117  16152  16267   1803   3200   4404       C  
ATOM   4131  N   VAL B 235      11.921   8.828  11.013  1.00 99.12           N  
ANISOU 4131  N   VAL B 235     7531  16174  13957   1407   3016   4149       N  
ATOM   4132  CA  VAL B 235      12.601   7.550  10.803  1.00 95.77           C  
ANISOU 4132  CA  VAL B 235     7230  15815  13343   1299   3015   4008       C  
ATOM   4133  C   VAL B 235      13.636   7.666   9.689  1.00104.78           C  
ANISOU 4133  C   VAL B 235     8376  16993  14442   1286   3021   4180       C  
ATOM   4134  O   VAL B 235      14.803   7.296   9.860  1.00110.19           O  
ANISOU 4134  O   VAL B 235     9147  17585  15136   1228   3041   4120       O  
ATOM   4135  CB  VAL B 235      11.577   6.441  10.505  1.00 85.00           C  
ANISOU 4135  CB  VAL B 235     5892  14649  11755   1246   2992   3869       C  
ATOM   4136  CG1 VAL B 235      12.266   5.224   9.900  1.00 82.82           C  
ANISOU 4136  CG1 VAL B 235     5727  14460  11282   1143   2998   3780       C  
ATOM   4137  CG2 VAL B 235      10.827   6.059  11.770  1.00 84.36           C  
ANISOU 4137  CG2 VAL B 235     5846  14503  11703   1227   3001   3641       C  
ATOM   4138  N   LEU B 236      13.232   8.211   8.540  1.00104.85           N  
ANISOU 4138  N   LEU B 236     8288  17139  14410   1341   3005   4403       N  
ATOM   4139  CA  LEU B 236      14.135   8.267   7.394  1.00101.65           C  
ANISOU 4139  CA  LEU B 236     7887  16793  13941   1320   3016   4566       C  
ATOM   4140  C   LEU B 236      15.236   9.303   7.595  1.00 94.77           C  
ANISOU 4140  C   LEU B 236     6999  15718  13289   1359   3053   4699       C  
ATOM   4141  O   LEU B 236      16.409   9.040   7.287  1.00 88.96           O  
ANISOU 4141  O   LEU B 236     6329  14934  12537   1302   3077   4698       O  
ATOM   4142  CB  LEU B 236      13.339   8.549   6.121  1.00105.93           C  
ANISOU 4142  CB  LEU B 236     8324  17560  14365   1365   2987   4776       C  
ATOM   4143  CG  LEU B 236      12.211   7.545   5.868  1.00103.75           C  
ANISOU 4143  CG  LEU B 236     8053  17501  13867   1319   2950   4643       C  
ATOM   4144  CD1 LEU B 236      11.368   7.952   4.669  1.00101.93           C  
ANISOU 4144  CD1 LEU B 236     7692  17507  13532   1374   2914   4871       C  
ATOM   4145  CD2 LEU B 236      12.770   6.138   5.691  1.00102.85           C  
ANISOU 4145  CD2 LEU B 236     8078  17437  13562   1188   2962   4435       C  
ATOM   4146  N   ILE B 237      14.884  10.490   8.098  1.00 96.99           N  
ANISOU 4146  N   ILE B 237     7193  15873  13786   1453   3066   4810       N  
ATOM   4147  CA  ILE B 237      15.905  11.510   8.323  1.00 99.20           C  
ANISOU 4147  CA  ILE B 237     7456  15948  14288   1484   3111   4927       C  
ATOM   4148  C   ILE B 237      16.901  11.050   9.381  1.00102.67           C  
ANISOU 4148  C   ILE B 237     7999  16221  14789   1408   3129   4716       C  
ATOM   4149  O   ILE B 237      18.093  11.366   9.297  1.00 99.83           O  
ANISOU 4149  O   ILE B 237     7663  15748  14521   1384   3161   4767       O  
ATOM   4150  CB  ILE B 237      15.249  12.856   8.689  1.00 99.41           C  
ANISOU 4150  CB  ILE B 237     7369  15858  14545   1598   3131   5073       C  
ATOM   4151  CG1 ILE B 237      14.404  13.361   7.518  1.00101.78           C  
ANISOU 4151  CG1 ILE B 237     7552  16331  14790   1683   3113   5328       C  
ATOM   4152  CG2 ILE B 237      16.301  13.894   9.049  1.00 90.30           C  
ANISOU 4152  CG2 ILE B 237     6206  14469  13637   1618   3189   5163       C  
ATOM   4153  CD1 ILE B 237      13.698  14.672   7.788  1.00106.23           C  
ANISOU 4153  CD1 ILE B 237     7995  16782  15586   1807   3135   5489       C  
ATOM   4154  N   GLY B 238      16.448  10.272  10.367  1.00113.43           N  
ANISOU 4154  N   GLY B 238     9423  17577  16098   1367   3109   4479       N  
ATOM   4155  CA  GLY B 238      17.368   9.737  11.354  1.00112.76           C  
ANISOU 4155  CA  GLY B 238     9432  17362  16048   1296   3121   4288       C  
ATOM   4156  C   GLY B 238      18.222   8.619  10.796  1.00111.81           C  
ANISOU 4156  C   GLY B 238     9404  17324  15756   1211   3116   4216       C  
ATOM   4157  O   GLY B 238      19.392   8.484  11.156  1.00120.39           O  
ANISOU 4157  O   GLY B 238    10539  18300  16904   1167   3134   4164       O  
ATOM   4158  N   SER B 239      17.655   7.802   9.907  1.00104.51           N  
ANISOU 4158  N   SER B 239     8499  16593  14617   1183   3096   4208       N  
ATOM   4159  CA  SER B 239      18.469   6.807   9.223  1.00100.16           C  
ANISOU 4159  CA  SER B 239     8031  16114  13912   1101   3103   4153       C  
ATOM   4160  C   SER B 239      19.584   7.475   8.429  1.00107.19           C  
ANISOU 4160  C   SER B 239     8892  16952  14882   1108   3132   4333       C  
ATOM   4161  O   SER B 239      20.721   6.991   8.412  1.00114.54           O  
ANISOU 4161  O   SER B 239     9887  17824  15809   1049   3152   4268       O  
ATOM   4162  CB  SER B 239      17.593   5.945   8.313  1.00 95.13           C  
ANISOU 4162  CB  SER B 239     7408  15696  13040   1067   3084   4126       C  
ATOM   4163  OG  SER B 239      16.667   5.184   9.069  1.00 92.35           O  
ANISOU 4163  OG  SER B 239     7097  15384  12608   1044   3067   3931       O  
ATOM   4164  N   PHE B 240      19.290   8.612   7.797  1.00105.57           N  
ANISOU 4164  N   PHE B 240     8588  16760  14765   1182   3139   4563       N  
ATOM   4165  CA  PHE B 240      20.320   9.281   7.004  1.00101.97           C  
ANISOU 4165  CA  PHE B 240     8105  16254  14385   1186   3175   4742       C  
ATOM   4166  C   PHE B 240      21.345  10.000   7.878  1.00106.22           C  
ANISOU 4166  C   PHE B 240     8640  16562  15155   1193   3207   4731       C  
ATOM   4167  O   PHE B 240      22.552   9.767   7.747  1.00113.56           O  
ANISOU 4167  O   PHE B 240     9615  17428  16104   1138   3232   4700       O  
ATOM   4168  CB  PHE B 240      19.681  10.259   6.018  1.00 95.28           C  
ANISOU 4168  CB  PHE B 240     7150  15497  13556   1265   3179   5010       C  
ATOM   4169  CG  PHE B 240      19.529   9.701   4.632  1.00 99.94           C  
ANISOU 4169  CG  PHE B 240     7744  16305  13925   1227   3170   5095       C  
ATOM   4170  CD1 PHE B 240      20.596   9.707   3.747  1.00102.03           C  
ANISOU 4170  CD1 PHE B 240     8034  16570  14162   1179   3207   5180       C  
ATOM   4171  CD2 PHE B 240      18.324   9.160   4.216  1.00104.85           C  
ANISOU 4171  CD2 PHE B 240     8343  17132  14365   1230   3128   5079       C  
ATOM   4172  CE1 PHE B 240      20.463   9.190   2.474  1.00104.97           C  
ANISOU 4172  CE1 PHE B 240     8415  17143  14328   1132   3204   5246       C  
ATOM   4173  CE2 PHE B 240      18.185   8.641   2.943  1.00107.65           C  
ANISOU 4173  CE2 PHE B 240     8699  17695  14509   1183   3120   5149       C  
ATOM   4174  CZ  PHE B 240      19.256   8.657   2.071  1.00107.48           C  
ANISOU 4174  CZ  PHE B 240     8708  17670  14459   1133   3159   5231       C  
ATOM   4175  N   VAL B 241      20.889  10.880   8.772  1.00100.13           N  
ANISOU 4175  N   VAL B 241     7815  15666  14566   1256   3210   4748       N  
ATOM   4176  CA  VAL B 241      21.812  11.721   9.530  1.00 96.47           C  
ANISOU 4176  CA  VAL B 241     7334  14985  14334   1261   3247   4756       C  
ATOM   4177  C   VAL B 241      22.527  10.911  10.606  1.00 95.68           C  
ANISOU 4177  C   VAL B 241     7315  14807  14232   1188   3234   4522       C  
ATOM   4178  O   VAL B 241      23.716  11.127  10.878  1.00100.36           O  
ANISOU 4178  O   VAL B 241     7917  15279  14936   1153   3259   4508       O  
ATOM   4179  CB  VAL B 241      21.061  12.926  10.125  1.00 92.46           C  
ANISOU 4179  CB  VAL B 241     6741  14362  14027   1346   3265   4842       C  
ATOM   4180  CG1 VAL B 241      21.972  13.742  11.033  1.00 89.23           C  
ANISOU 4180  CG1 VAL B 241     6320  13725  13860   1335   3307   4814       C  
ATOM   4181  CG2 VAL B 241      20.500  13.798   9.010  1.00 93.90           C  
ANISOU 4181  CG2 VAL B 241     6832  14613  14233   1427   3284   5110       C  
ATOM   4182  N   SER B 242      21.828   9.962  11.228  1.00 90.44           N  
ANISOU 4182  N   SER B 242     6705  14215  13444   1165   3197   4341       N  
ATOM   4183  CA  SER B 242      22.377   9.211  12.346  1.00 86.24           C  
ANISOU 4183  CA  SER B 242     6242  13612  12913   1107   3186   4131       C  
ATOM   4184  C   SER B 242      23.033   7.905  11.930  1.00 85.68           C  
ANISOU 4184  C   SER B 242     6257  13632  12667   1035   3177   4029       C  
ATOM   4185  O   SER B 242      23.842   7.370  12.694  1.00 86.43           O  
ANISOU 4185  O   SER B 242     6398  13655  12787    991   3175   3900       O  
ATOM   4186  CB  SER B 242      21.273   8.892  13.363  1.00 85.69           C  
ANISOU 4186  CB  SER B 242     6188  13554  12816   1117   3162   3982       C  
ATOM   4187  OG  SER B 242      20.563  10.056  13.743  1.00 86.01           O  
ANISOU 4187  OG  SER B 242     6147  13511  13020   1185   3176   4063       O  
ATOM   4188  N   PHE B 243      22.698   7.366  10.758  1.00 87.54           N  
ANISOU 4188  N   PHE B 243     6511  14022  12729   1022   3175   4081       N  
ATOM   4189  CA  PHE B 243      23.285   6.105  10.320  1.00 91.12           C  
ANISOU 4189  CA  PHE B 243     7049  14551  13022    949   3179   3973       C  
ATOM   4190  C   PHE B 243      24.006   6.207   8.985  1.00106.07           C  
ANISOU 4190  C   PHE B 243     8932  16498  14872    927   3208   4107       C  
ATOM   4191  O   PHE B 243      25.162   5.783   8.884  1.00115.02           O  
ANISOU 4191  O   PHE B 243    10102  17581  16019    879   3231   4062       O  
ATOM   4192  CB  PHE B 243      22.205   5.013  10.256  1.00 85.80           C  
ANISOU 4192  CB  PHE B 243     6432  14020  12146    922   3159   3841       C  
ATOM   4193  CG  PHE B 243      22.752   3.631  10.046  1.00 79.29           C  
ANISOU 4193  CG  PHE B 243     5705  13244  11178    844   3173   3694       C  
ATOM   4194  CD1 PHE B 243      23.526   3.024  11.021  1.00 78.26           C  
ANISOU 4194  CD1 PHE B 243     5628  13013  11095    814   3177   3555       C  
ATOM   4195  CD2 PHE B 243      22.488   2.937   8.877  1.00 87.24           C  
ANISOU 4195  CD2 PHE B 243     6745  14397  12005    799   3186   3698       C  
ATOM   4196  CE1 PHE B 243      24.032   1.751  10.831  1.00 84.45           C  
ANISOU 4196  CE1 PHE B 243     6496  13830  11760    749   3198   3428       C  
ATOM   4197  CE2 PHE B 243      22.989   1.664   8.682  1.00 86.54           C  
ANISOU 4197  CE2 PHE B 243     6747  14335  11799    723   3211   3554       C  
ATOM   4198  CZ  PHE B 243      23.762   1.070   9.660  1.00 85.37           C  
ANISOU 4198  CZ  PHE B 243     6651  14076  11710    702   3219   3423       C  
ATOM   4199  N   PHE B 244      23.371   6.772   7.954  1.00116.02           N  
ANISOU 4199  N   PHE B 244     9349  21668  13065   1639   1617   5988       N  
ATOM   4200  CA  PHE B 244      23.918   6.660   6.602  1.00115.52           C  
ANISOU 4200  CA  PHE B 244     9266  21721  12905   1645   1533   6050       C  
ATOM   4201  C   PHE B 244      25.119   7.574   6.378  1.00110.93           C  
ANISOU 4201  C   PHE B 244     8766  21052  12329   1663   1617   6001       C  
ATOM   4202  O   PHE B 244      26.130   7.143   5.812  1.00110.58           O  
ANISOU 4202  O   PHE B 244     8764  21065  12186   1616   1552   5937       O  
ATOM   4203  CB  PHE B 244      22.834   6.941   5.559  1.00118.04           C  
ANISOU 4203  CB  PHE B 244     9462  22160  13227   1723   1495   6251       C  
ATOM   4204  CG  PHE B 244      21.866   5.806   5.367  1.00119.03           C  
ANISOU 4204  CG  PHE B 244     9499  22421  13307   1681   1378   6278       C  
ATOM   4205  CD1 PHE B 244      22.321   4.558   4.964  1.00120.67           C  
ANISOU 4205  CD1 PHE B 244     9704  22743  13404   1586   1257   6186       C  
ATOM   4206  CD2 PHE B 244      20.507   5.988   5.561  1.00118.62           C  
ANISOU 4206  CD2 PHE B 244     9359  22372  13339   1729   1399   6386       C  
ATOM   4207  CE1 PHE B 244      21.441   3.508   4.777  1.00121.34           C  
ANISOU 4207  CE1 PHE B 244     9701  22930  13472   1536   1166   6186       C  
ATOM   4208  CE2 PHE B 244      19.620   4.942   5.377  1.00120.04           C  
ANISOU 4208  CE2 PHE B 244     9455  22664  13492   1681   1300   6392       C  
ATOM   4209  CZ  PHE B 244      20.088   3.699   4.983  1.00121.49           C  
ANISOU 4209  CZ  PHE B 244     9636  22949  13575   1581   1187   6286       C  
ATOM   4210  N   ILE B 245      25.024   8.843   6.785  1.00105.44           N  
ANISOU 4210  N   ILE B 245     8090  20210  11761   1727   1771   6026       N  
ATOM   4211  CA  ILE B 245      26.138   9.771   6.572  1.00101.76           C  
ANISOU 4211  CA  ILE B 245     7697  19640  11329   1741   1874   5976       C  
ATOM   4212  C   ILE B 245      27.407   9.313   7.287  1.00100.13           C  
ANISOU 4212  C   ILE B 245     7600  19384  11060   1642   1872   5755       C  
ATOM   4213  O   ILE B 245      28.461   9.230   6.636  1.00103.49           O  
ANISOU 4213  O   ILE B 245     8073  19834  11415   1615   1839   5713       O  
ATOM   4214  CB  ILE B 245      25.719  11.202   6.950  1.00 99.42           C  
ANISOU 4214  CB  ILE B 245     7386  19176  11215   1821   2062   6032       C  
ATOM   4215  CG1 ILE B 245      24.610  11.697   6.019  1.00 96.86           C  
ANISOU 4215  CG1 ILE B 245     6944  18912  10945   1933   2057   6287       C  
ATOM   4216  CG2 ILE B 245      26.918  12.141   6.907  1.00 99.87           C  
ANISOU 4216  CG2 ILE B 245     7519  19095  11331   1818   2193   5946       C  
ATOM   4217  CD1 ILE B 245      24.107  13.086   6.350  1.00 95.30           C  
ANISOU 4217  CD1 ILE B 245     6715  18538  10957   2020   2249   6364       C  
ATOM   4218  N   PRO B 246      27.387   9.005   8.594  1.00 96.86           N  
ANISOU 4218  N   PRO B 246     7225  18915  10662   1589   1904   5614       N  
ATOM   4219  CA  PRO B 246      28.618   8.499   9.221  1.00 96.92           C  
ANISOU 4219  CA  PRO B 246     7324  18909  10592   1500   1887   5424       C  
ATOM   4220  C   PRO B 246      29.074   7.172   8.647  1.00 99.66           C  
ANISOU 4220  C   PRO B 246     7673  19386  10806   1441   1718   5414       C  
ATOM   4221  O   PRO B 246      30.281   6.922   8.589  1.00101.23           O  
ANISOU 4221  O   PRO B 246     7940  19582  10942   1387   1698   5301       O  
ATOM   4222  CB  PRO B 246      28.235   8.379  10.703  1.00 89.82           C  
ANISOU 4222  CB  PRO B 246     6436  17968   9723   1471   1945   5319       C  
ATOM   4223  CG  PRO B 246      26.761   8.241  10.701  1.00 88.64           C  
ANISOU 4223  CG  PRO B 246     6199  17850   9628   1521   1926   5459       C  
ATOM   4224  CD  PRO B 246      26.286   9.096   9.571  1.00 91.62           C  
ANISOU 4224  CD  PRO B 246     6520  18212  10078   1606   1960   5624       C  
ATOM   4225  N   LEU B 247      28.146   6.323   8.199  1.00 97.02           N  
ANISOU 4225  N   LEU B 247     7259  19164  10438   1447   1607   5523       N  
ATOM   4226  CA  LEU B 247      28.522   5.061   7.567  1.00 95.96           C  
ANISOU 4226  CA  LEU B 247     7110  19153  10199   1384   1461   5506       C  
ATOM   4227  C   LEU B 247      29.338   5.300   6.300  1.00103.90           C  
ANISOU 4227  C   LEU B 247     8124  20213  11139   1389   1430   5526       C  
ATOM   4228  O   LEU B 247      30.415   4.714   6.114  1.00115.73           O  
ANISOU 4228  O   LEU B 247     9672  21732  12566   1324   1379   5421       O  
ATOM   4229  CB  LEU B 247      27.262   4.251   7.255  1.00 88.98           C  
ANISOU 4229  CB  LEU B 247     6121  18377   9312   1388   1372   5615       C  
ATOM   4230  CG  LEU B 247      27.294   3.105   6.245  1.00 92.78           C  
ANISOU 4230  CG  LEU B 247     6541  19008   9703   1334   1236   5629       C  
ATOM   4231  CD1 LEU B 247      28.207   1.985   6.713  1.00 90.98           C  
ANISOU 4231  CD1 LEU B 247     6364  18769   9437   1240   1182   5492       C  
ATOM   4232  CD2 LEU B 247      25.882   2.589   5.999  1.00 97.53           C  
ANISOU 4232  CD2 LEU B 247     7030  19698  10329   1345   1182   5732       C  
ATOM   4233  N   THR B 248      28.836   6.165   5.415  1.00 96.57           N  
ANISOU 4233  N   THR B 248     7143  19312  10235   1470   1463   5670       N  
ATOM   4234  CA  THR B 248      29.550   6.451   4.175  1.00 89.54           C  
ANISOU 4234  CA  THR B 248     6254  18491   9278   1486   1440   5712       C  
ATOM   4235  C   THR B 248      30.886   7.128   4.446  1.00 89.43           C  
ANISOU 4235  C   THR B 248     6351  18338   9290   1466   1537   5591       C  
ATOM   4236  O   THR B 248      31.899   6.792   3.815  1.00 89.24           O  
ANISOU 4236  O   THR B 248     6363  18359   9184   1422   1491   5526       O  
ATOM   4237  CB  THR B 248      28.688   7.319   3.257  1.00 93.60           C  
ANISOU 4237  CB  THR B 248     6678  19066   9818   1594   1469   5922       C  
ATOM   4238  OG1 THR B 248      28.371   8.551   3.917  1.00 99.09           O  
ANISOU 4238  OG1 THR B 248     7397  19589  10664   1664   1625   5965       O  
ATOM   4239  CG2 THR B 248      27.400   6.593   2.890  1.00 93.78           C  
ANISOU 4239  CG2 THR B 248     6581  19256   9797   1604   1363   6033       C  
ATOM   4240  N   ILE B 249      30.911   8.091   5.374  1.00 92.45           N  
ANISOU 4240  N   ILE B 249     6782  18556   9790   1493   1681   5547       N  
ATOM   4241  CA  ILE B 249      32.175   8.745   5.707  1.00 91.79           C  
ANISOU 4241  CA  ILE B 249     6795  18342   9739   1463   1787   5410       C  
ATOM   4242  C   ILE B 249      33.174   7.731   6.253  1.00 89.40           C  
ANISOU 4242  C   ILE B 249     6558  18065   9347   1361   1711   5229       C  
ATOM   4243  O   ILE B 249      34.363   7.764   5.909  1.00 85.15           O  
ANISOU 4243  O   ILE B 249     6079  17506   8769   1322   1717   5140       O  
ATOM   4244  CB  ILE B 249      31.948   9.910   6.689  1.00 88.23           C  
ANISOU 4244  CB  ILE B 249     6364  17723   9436   1497   1966   5368       C  
ATOM   4245  CG1 ILE B 249      31.012  10.951   6.073  1.00 88.97           C  
ANISOU 4245  CG1 ILE B 249     6385  17775   9643   1606   2053   5566       C  
ATOM   4246  CG2 ILE B 249      33.271  10.568   7.040  1.00 88.92           C  
ANISOU 4246  CG2 ILE B 249     6537  17688   9561   1454   2083   5204       C  
ATOM   4247  CD1 ILE B 249      30.660  12.086   7.011  1.00 89.88           C  
ANISOU 4247  CD1 ILE B 249     6500  17719   9931   1638   2242   5525       C  
ATOM   4248  N   MET B 250      32.709   6.810   7.102  1.00 94.95           N  
ANISOU 4248  N   MET B 250     7244  18811  10022   1321   1642   5186       N  
ATOM   4249  CA  MET B 250      33.583   5.778   7.648  1.00103.53           C  
ANISOU 4249  CA  MET B 250     8376  19928  11033   1235   1569   5047       C  
ATOM   4250  C   MET B 250      34.171   4.917   6.542  1.00110.60           C  
ANISOU 4250  C   MET B 250     9260  20925  11837   1194   1451   5052       C  
ATOM   4251  O   MET B 250      35.376   4.646   6.527  1.00117.63           O  
ANISOU 4251  O   MET B 250    10209  21802  12685   1139   1439   4937       O  
ATOM   4252  CB  MET B 250      32.811   4.907   8.640  1.00102.31           C  
ANISOU 4252  CB  MET B 250     8187  19809  10876   1214   1518   5046       C  
ATOM   4253  CG  MET B 250      33.173   5.129  10.092  1.00101.60           C  
ANISOU 4253  CG  MET B 250     8148  19655  10802   1190   1597   4920       C  
ATOM   4254  SD  MET B 250      32.012   4.310  11.201  1.00102.78           S  
ANISOU 4254  SD  MET B 250     8244  19847  10962   1190   1561   4966       S  
ATOM   4255  CE  MET B 250      31.794   2.740  10.364  1.00100.19           C  
ANISOU 4255  CE  MET B 250     7858  19625  10585   1151   1396   5048       C  
ATOM   4256  N   VAL B 251      33.328   4.465   5.611  1.00106.18           N  
ANISOU 4256  N   VAL B 251     8615  20482  11245   1216   1366   5178       N  
ATOM   4257  CA  VAL B 251      33.811   3.612   4.526  1.00100.02           C  
ANISOU 4257  CA  VAL B 251     7806  19825  10372   1168   1259   5168       C  
ATOM   4258  C   VAL B 251      34.867   4.344   3.702  1.00 95.60           C  
ANISOU 4258  C   VAL B 251     7300  19242   9783   1177   1305   5142       C  
ATOM   4259  O   VAL B 251      35.969   3.824   3.457  1.00 86.48           O  
ANISOU 4259  O   VAL B 251     6188  18098   8574   1112   1270   5032       O  
ATOM   4260  CB  VAL B 251      32.636   3.143   3.648  1.00 97.92           C  
ANISOU 4260  CB  VAL B 251     7423  19715  10069   1190   1174   5300       C  
ATOM   4261  CG1 VAL B 251      33.149   2.421   2.414  1.00 92.23           C  
ANISOU 4261  CG1 VAL B 251     6660  19143   9240   1139   1081   5276       C  
ATOM   4262  CG2 VAL B 251      31.707   2.242   4.446  1.00101.16           C  
ANISOU 4262  CG2 VAL B 251     7783  20136  10516   1163   1129   5307       C  
ATOM   4263  N   ILE B 252      34.543   5.566   3.266  1.00 98.84           N  
ANISOU 4263  N   ILE B 252     7704  19610  10239   1261   1393   5250       N  
ATOM   4264  CA  ILE B 252      35.470   6.339   2.441  1.00 95.22           C  
ANISOU 4264  CA  ILE B 252     7292  19118   9770   1280   1454   5252       C  
ATOM   4265  C   ILE B 252      36.796   6.535   3.166  1.00 92.53           C  
ANISOU 4265  C   ILE B 252     7061  18639   9459   1221   1526   5074       C  
ATOM   4266  O   ILE B 252      37.874   6.273   2.613  1.00 89.18           O  
ANISOU 4266  O   ILE B 252     6678  18232   8976   1173   1503   4994       O  
ATOM   4267  CB  ILE B 252      34.842   7.691   2.053  1.00 92.30           C  
ANISOU 4267  CB  ILE B 252     6893  18692   9484   1389   1565   5416       C  
ATOM   4268  CG1 ILE B 252      33.572   7.481   1.227  1.00 94.12           C  
ANISOU 4268  CG1 ILE B 252     7000  19096   9666   1453   1481   5606       C  
ATOM   4269  CG2 ILE B 252      35.845   8.550   1.297  1.00 86.38           C  
ANISOU 4269  CG2 ILE B 252     6197  17879   8747   1412   1652   5425       C  
ATOM   4270  CD1 ILE B 252      32.797   8.757   0.970  1.00 98.59           C  
ANISOU 4270  CD1 ILE B 252     7519  19607  10332   1573   1589   5796       C  
ATOM   4271  N   THR B 253      36.733   6.989   4.420  1.00 83.55           N  
ANISOU 4271  N   THR B 253     5962  17377   8407   1221   1617   5001       N  
ATOM   4272  CA  THR B 253      37.949   7.300   5.161  1.00 82.95           C  
ANISOU 4272  CA  THR B 253     5971  17190   8356   1169   1698   4828       C  
ATOM   4273  C   THR B 253      38.776   6.050   5.430  1.00 96.16           C  
ANISOU 4273  C   THR B 253     7668  18928   9939   1080   1588   4702       C  
ATOM   4274  O   THR B 253      40.007   6.084   5.327  1.00 99.73           O  
ANISOU 4274  O   THR B 253     8177  19344  10370   1034   1610   4588       O  
ATOM   4275  CB  THR B 253      37.588   7.999   6.470  1.00 83.28           C  
ANISOU 4275  CB  THR B 253     6026  17126   8492   1183   1814   4768       C  
ATOM   4276  OG1 THR B 253      36.844   9.191   6.186  1.00 84.50           O  
ANISOU 4276  OG1 THR B 253     6149  17201   8756   1266   1934   4888       O  
ATOM   4277  CG2 THR B 253      38.833   8.369   7.226  1.00 82.89           C  
ANISOU 4277  CG2 THR B 253     6045  16991   8459   1126   1903   4577       C  
ATOM   4278  N   TYR B 254      38.122   4.930   5.745  1.00 89.83           N  
ANISOU 4278  N   TYR B 254     6817  18218   9096   1058   1476   4728       N  
ATOM   4279  CA  TYR B 254      38.848   3.697   6.027  1.00 85.40           C  
ANISOU 4279  CA  TYR B 254     6264  17708   8474    980   1382   4631       C  
ATOM   4280  C   TYR B 254      39.591   3.204   4.792  1.00 90.34           C  
ANISOU 4280  C   TYR B 254     6888  18402   9036    941   1318   4615       C  
ATOM   4281  O   TYR B 254      40.765   2.813   4.871  1.00 88.64           O  
ANISOU 4281  O   TYR B 254     6716  18169   8793    883   1307   4498       O  
ATOM   4282  CB  TYR B 254      37.881   2.633   6.549  1.00 80.46           C  
ANISOU 4282  CB  TYR B 254     5574  17152   7846    970   1296   4688       C  
ATOM   4283  CG  TYR B 254      38.542   1.328   6.925  1.00 79.73           C  
ANISOU 4283  CG  TYR B 254     5477  17098   7719    898   1214   4613       C  
ATOM   4284  CD1 TYR B 254      39.124   1.163   8.175  1.00 79.37           C  
ANISOU 4284  CD1 TYR B 254     5469  17012   7676    876   1239   4528       C  
ATOM   4285  CD2 TYR B 254      38.575   0.257   6.041  1.00 82.33           C  
ANISOU 4285  CD2 TYR B 254     5753  17513   8017    852   1120   4629       C  
ATOM   4286  CE1 TYR B 254      39.729  -0.024   8.531  1.00 78.88           C  
ANISOU 4286  CE1 TYR B 254     5393  16984   7594    822   1171   4487       C  
ATOM   4287  CE2 TYR B 254      39.178  -0.938   6.389  1.00 83.98           C  
ANISOU 4287  CE2 TYR B 254     5949  17736   8223    788   1062   4569       C  
ATOM   4288  CZ  TYR B 254      39.753  -1.072   7.636  1.00 80.73           C  
ANISOU 4288  CZ  TYR B 254     5577  17273   7823    779   1088   4512       C  
ATOM   4289  OH  TYR B 254      40.355  -2.257   7.992  1.00 78.39           O  
ANISOU 4289  OH  TYR B 254     5259  16991   7535    726   1036   4479       O  
ATOM   4290  N   PHE B 255      38.920   3.200   3.636  1.00 97.37           N  
ANISOU 4290  N   PHE B 255     7717  19385   9893    972   1275   4729       N  
ATOM   4291  CA  PHE B 255      39.591   2.710   2.434  1.00100.21           C  
ANISOU 4291  CA  PHE B 255     8064  19837  10174    930   1215   4703       C  
ATOM   4292  C   PHE B 255      40.704   3.656   1.989  1.00 92.36           C  
ANISOU 4292  C   PHE B 255     7148  18761   9182    939   1304   4652       C  
ATOM   4293  O   PHE B 255      41.780   3.206   1.566  1.00 83.54           O  
ANISOU 4293  O   PHE B 255     6062  17660   8020    878   1281   4553       O  
ATOM   4294  CB  PHE B 255      38.578   2.483   1.313  1.00105.96           C  
ANISOU 4294  CB  PHE B 255     8692  20727  10843    960   1146   4832       C  
ATOM   4295  CG  PHE B 255      37.794   1.207   1.460  1.00110.44           C  
ANISOU 4295  CG  PHE B 255     9170  21397  11395    915   1046   4838       C  
ATOM   4296  CD1 PHE B 255      38.351  -0.007   1.090  1.00112.85           C  
ANISOU 4296  CD1 PHE B 255     9444  21777  11658    825    971   4740       C  
ATOM   4297  CD2 PHE B 255      36.506   1.219   1.968  1.00111.07           C  
ANISOU 4297  CD2 PHE B 255     9194  21486  11520    958   1038   4936       C  
ATOM   4298  CE1 PHE B 255      37.638  -1.185   1.224  1.00113.34           C  
ANISOU 4298  CE1 PHE B 255     9419  21908  11737    777    898   4736       C  
ATOM   4299  CE2 PHE B 255      35.787   0.045   2.104  1.00112.33           C  
ANISOU 4299  CE2 PHE B 255     9272  21723  11685    911    959   4937       C  
ATOM   4300  CZ  PHE B 255      36.354  -1.158   1.731  1.00112.91           C  
ANISOU 4300  CZ  PHE B 255     9314  21857  11731    820    892   4835       C  
ATOM   4301  N   LEU B 256      40.487   4.970   2.105  1.00 91.89           N  
ANISOU 4301  N   LEU B 256     7120  18603   9191   1010   1420   4716       N  
ATOM   4302  CA  LEU B 256      41.566   5.901   1.793  1.00 93.27           C  
ANISOU 4302  CA  LEU B 256     7369  18674   9397   1013   1528   4663       C  
ATOM   4303  C   LEU B 256      42.745   5.720   2.745  1.00 89.01           C  
ANISOU 4303  C   LEU B 256     6899  18041   8879    943   1563   4477       C  
ATOM   4304  O   LEU B 256      43.906   5.829   2.333  1.00 90.08           O  
ANISOU 4304  O   LEU B 256     7084  18143   8999    904   1594   4389       O  
ATOM   4305  CB  LEU B 256      41.050   7.338   1.827  1.00 82.69           C  
ANISOU 4305  CB  LEU B 256     6034  17226   8159   1102   1667   4770       C  
ATOM   4306  CG  LEU B 256      40.055   7.687   0.716  1.00 86.36           C  
ANISOU 4306  CG  LEU B 256     6424  17791   8600   1187   1645   4978       C  
ATOM   4307  CD1 LEU B 256      39.692   9.162   0.758  1.00 85.09           C  
ANISOU 4307  CD1 LEU B 256     6267  17495   8569   1278   1805   5092       C  
ATOM   4308  CD2 LEU B 256      40.606   7.301  -0.651  1.00 86.35           C  
ANISOU 4308  CD2 LEU B 256     6408  17918   8483   1170   1577   5003       C  
ATOM   4309  N   THR B 257      42.469   5.399   4.012  1.00 86.83           N  
ANISOU 4309  N   THR B 257     6621  17740   8630    926   1555   4419       N  
ATOM   4310  CA  THR B 257      43.546   5.194   4.975  1.00 86.66           C  
ANISOU 4310  CA  THR B 257     6649  17668   8612    865   1578   4253       C  
ATOM   4311  C   THR B 257      44.347   3.936   4.660  1.00 92.01           C  
ANISOU 4311  C   THR B 257     7321  18424   9217    794   1466   4184       C  
ATOM   4312  O   THR B 257      45.582   3.948   4.732  1.00 99.39           O  
ANISOU 4312  O   THR B 257     8299  19322  10144    748   1494   4063       O  
ATOM   4313  CB  THR B 257      42.975   5.121   6.393  1.00 83.37           C  
ANISOU 4313  CB  THR B 257     6216  17239   8220    872   1590   4225       C  
ATOM   4314  OG1 THR B 257      42.427   6.394   6.754  1.00 83.43           O  
ANISOU 4314  OG1 THR B 257     6230  17156   8314    927   1723   4251       O  
ATOM   4315  CG2 THR B 257      44.060   4.748   7.392  1.00 80.58           C  
ANISOU 4315  CG2 THR B 257     5893  16884   7842    813   1590   4067       C  
ATOM   4316  N   ILE B 258      43.668   2.839   4.313  1.00 90.07           N  
ANISOU 4316  N   ILE B 258     7012  18283   8928    782   1349   4254       N  
ATOM   4317  CA  ILE B 258      44.403   1.619   3.985  1.00 88.09           C  
ANISOU 4317  CA  ILE B 258     6743  18098   8632    710   1260   4187       C  
ATOM   4318  C   ILE B 258      45.236   1.823   2.721  1.00 87.93           C  
ANISOU 4318  C   ILE B 258     6745  18094   8571    687   1273   4152       C  
ATOM   4319  O   ILE B 258      46.376   1.340   2.626  1.00 85.66           O  
ANISOU 4319  O   ILE B 258     6480  17799   8268    627   1261   4043       O  
ATOM   4320  CB  ILE B 258      43.454   0.407   3.878  1.00 86.44           C  
ANISOU 4320  CB  ILE B 258     6445  17988   8408    694   1154   4260       C  
ATOM   4321  CG1 ILE B 258      44.253  -0.895   3.822  1.00 90.64           C  
ANISOU 4321  CG1 ILE B 258     6950  18557   8931    616   1085   4179       C  
ATOM   4322  CG2 ILE B 258      42.551   0.493   2.666  1.00 83.03           C  
ANISOU 4322  CG2 ILE B 258     5955  17654   7939    721   1120   4365       C  
ATOM   4323  CD1 ILE B 258      43.387  -2.134   3.722  1.00 93.32           C  
ANISOU 4323  CD1 ILE B 258     7195  18974   9290    588   1002   4235       C  
ATOM   4324  N   LYS B 259      44.708   2.575   1.749  1.00 93.09           N  
ANISOU 4324  N   LYS B 259     7391  18773   9207    738   1304   4250       N  
ATOM   4325  CA  LYS B 259      45.492   2.848   0.547  1.00 97.80           C  
ANISOU 4325  CA  LYS B 259     8011  19394   9757    723   1326   4230       C  
ATOM   4326  C   LYS B 259      46.703   3.723   0.863  1.00 94.00           C  
ANISOU 4326  C   LYS B 259     7617  18772   9326    714   1441   4129       C  
ATOM   4327  O   LYS B 259      47.799   3.498   0.331  1.00 94.88           O  
ANISOU 4327  O   LYS B 259     7758  18884   9409    663   1445   4039       O  
ATOM   4328  CB  LYS B 259      44.608   3.495  -0.518  1.00106.90           C  
ANISOU 4328  CB  LYS B 259     9123  20622  10872    794   1335   4385       C  
ATOM   4329  CG  LYS B 259      43.625   2.524  -1.151  1.00111.82           C  
ANISOU 4329  CG  LYS B 259     9641  21430  11416    784   1215   4455       C  
ATOM   4330  CD  LYS B 259      44.323   1.250  -1.610  1.00110.19           C  
ANISOU 4330  CD  LYS B 259     9401  21319  11146    687   1135   4335       C  
ATOM   4331  CE  LYS B 259      43.321   0.208  -2.085  1.00106.59           C  
ANISOU 4331  CE  LYS B 259     8824  21042  10633    660   1029   4375       C  
ATOM   4332  NZ  LYS B 259      43.989  -0.957  -2.727  1.00103.72           N  
ANISOU 4332  NZ  LYS B 259     8411  20779  10217    562    971   4249       N  
ATOM   4333  N   SER B 260      46.529   4.719   1.738  1.00 92.48           N  
ANISOU 4333  N   SER B 260     7459  18463   9215    757   1543   4132       N  
ATOM   4334  CA  SER B 260      47.649   5.574   2.117  1.00 91.24           C  
ANISOU 4334  CA  SER B 260     7369  18178   9120    739   1667   4017       C  
ATOM   4335  C   SER B 260      48.717   4.783   2.862  1.00 78.17           C  
ANISOU 4335  C   SER B 260     5728  16527   7447    662   1625   3855       C  
ATOM   4336  O   SER B 260      49.917   5.027   2.688  1.00 78.02           O  
ANISOU 4336  O   SER B 260     5749  16455   7440    623   1682   3746       O  
ATOM   4337  CB  SER B 260      47.154   6.743   2.967  1.00 79.67           C  
ANISOU 4337  CB  SER B 260     5914  16601   7754    791   1793   4034       C  
ATOM   4338  OG  SER B 260      46.138   7.468   2.298  1.00 80.63           O  
ANISOU 4338  OG  SER B 260     6011  16716   7908    871   1835   4204       O  
ATOM   4339  N   LEU B 261      48.301   3.833   3.702  1.00 77.67           N  
ANISOU 4339  N   LEU B 261     5626  16527   7359    644   1531   3848       N  
ATOM   4340  CA  LEU B 261      49.273   3.007   4.413  1.00 78.81           C  
ANISOU 4340  CA  LEU B 261     5769  16692   7484    582   1485   3724       C  
ATOM   4341  C   LEU B 261      50.030   2.093   3.455  1.00 80.61           C  
ANISOU 4341  C   LEU B 261     5984  16973   7670    526   1416   3687       C  
ATOM   4342  O   LEU B 261      51.239   1.875   3.620  1.00 79.33           O  
ANISOU 4342  O   LEU B 261     5841  16791   7511    477   1428   3569       O  
ATOM   4343  CB  LEU B 261      48.576   2.191   5.501  1.00 77.58           C  
ANISOU 4343  CB  LEU B 261     5565  16593   7318    587   1407   3759       C  
ATOM   4344  CG  LEU B 261      48.045   3.000   6.685  1.00 79.18           C  
ANISOU 4344  CG  LEU B 261     5776  16758   7552    628   1479   3753       C  
ATOM   4345  CD1 LEU B 261      47.488   2.081   7.762  1.00 82.18           C  
ANISOU 4345  CD1 LEU B 261     6108  17209   7906    630   1400   3789       C  
ATOM   4346  CD2 LEU B 261      49.135   3.898   7.250  1.00 81.25           C  
ANISOU 4346  CD2 LEU B 261     6078  16957   7838    607   1589   3603       C  
ATOM   4347  N   GLN B 262      49.342   1.551   2.445  1.00 85.30           N  
ANISOU 4347  N   GLN B 262     6538  17648   8225    529   1348   3778       N  
ATOM   4348  CA  GLN B 262      50.050   0.789   1.418  1.00 86.27           C  
ANISOU 4348  CA  GLN B 262     6642  17831   8306    471   1302   3726       C  
ATOM   4349  C   GLN B 262      51.073   1.659   0.694  1.00 85.57           C  
ANISOU 4349  C   GLN B 262     6618  17681   8215    463   1393   3663       C  
ATOM   4350  O   GLN B 262      52.201   1.219   0.432  1.00 83.28           O  
ANISOU 4350  O   GLN B 262     6337  17387   7920    404   1392   3554       O  
ATOM   4351  CB  GLN B 262      49.065   0.178   0.421  1.00 89.00           C  
ANISOU 4351  CB  GLN B 262     6917  18301   8597    473   1225   3819       C  
ATOM   4352  CG  GLN B 262      48.345  -1.058   0.935  1.00 94.37           C  
ANISOU 4352  CG  GLN B 262     7516  19045   9295    449   1131   3846       C  
ATOM   4353  CD  GLN B 262      47.356  -1.616  -0.071  1.00102.37           C  
ANISOU 4353  CD  GLN B 262     8443  20195  10257    442   1065   3916       C  
ATOM   4354  OE1 GLN B 262      47.225  -1.101  -1.182  1.00101.24           O  
ANISOU 4354  OE1 GLN B 262     8298  20126  10044    460   1079   3951       O  
ATOM   4355  NE2 GLN B 262      46.659  -2.680   0.311  1.00109.55           N  
ANISOU 4355  NE2 GLN B 262     9272  21149  11204    417    997   3938       N  
ATOM   4356  N   LYS B 263      50.693   2.895   0.354  1.00 86.13           N  
ANISOU 4356  N   LYS B 263     6726  17696   8302    525   1482   3739       N  
ATOM   4357  CA  LYS B 263      51.639   3.817  -0.273  1.00 81.33           C  
ANISOU 4357  CA  LYS B 263     6178  17008   7716    524   1593   3695       C  
ATOM   4358  C   LYS B 263      52.850   4.074   0.621  1.00 80.18           C  
ANISOU 4358  C   LYS B 263     6073  16760   7634    481   1663   3539       C  
ATOM   4359  O   LYS B 263      53.994   4.083   0.145  1.00 79.49           O  
ANISOU 4359  O   LYS B 263     6011  16644   7547    436   1702   3444       O  
ATOM   4360  CB  LYS B 263      50.937   5.131  -0.616  1.00 82.11           C  
ANISOU 4360  CB  LYS B 263     6298  17045   7856    607   1694   3825       C  
ATOM   4361  CG  LYS B 263      51.875   6.249  -1.038  1.00 83.15           C  
ANISOU 4361  CG  LYS B 263     6488  17056   8050    614   1843   3791       C  
ATOM   4362  CD  LYS B 263      52.415   6.023  -2.441  1.00 87.33           C  
ANISOU 4362  CD  LYS B 263     7025  17655   8502    595   1828   3811       C  
ATOM   4363  CE  LYS B 263      53.137   7.257  -2.959  1.00 91.50           C  
ANISOU 4363  CE  LYS B 263     7605  18056   9103    620   1992   3826       C  
ATOM   4364  NZ  LYS B 263      53.810   6.999  -4.262  1.00 93.19           N  
ANISOU 4364  NZ  LYS B 263     7832  18343   9234    595   1982   3828       N  
ATOM   4365  N   GLU B 264      52.616   4.288   1.920  1.00 80.11           N  
ANISOU 4365  N   GLU B 264     6058  16710   7670    494   1682   3505       N  
ATOM   4366  CA  GLU B 264      53.717   4.504   2.856  1.00 76.95           C  
ANISOU 4366  CA  GLU B 264     5674  16252   7312    454   1740   3347       C  
ATOM   4367  C   GLU B 264      54.665   3.312   2.874  1.00 76.27           C  
ANISOU 4367  C   GLU B 264     5564  16229   7185    387   1649   3253       C  
ATOM   4368  O   GLU B 264      55.892   3.474   2.808  1.00 76.18           O  
ANISOU 4368  O   GLU B 264     5570  16177   7197    343   1701   3130       O  
ATOM   4369  CB  GLU B 264      53.177   4.761   4.265  1.00 85.70           C  
ANISOU 4369  CB  GLU B 264     6762  17356   8445    477   1754   3328       C  
ATOM   4370  CG  GLU B 264      52.674   6.169   4.519  1.00 94.67           C  
ANISOU 4370  CG  GLU B 264     7917  18392   9660    527   1896   3349       C  
ATOM   4371  CD  GLU B 264      52.507   6.459   6.000  1.00108.55           C  
ANISOU 4371  CD  GLU B 264     9650  20156  11438    528   1932   3264       C  
ATOM   4372  OE1 GLU B 264      53.374   6.029   6.790  1.00113.95           O  
ANISOU 4372  OE1 GLU B 264    10316  20889  12091    482   1903   3132       O  
ATOM   4373  OE2 GLU B 264      51.507   7.107   6.375  1.00115.70           O  
ANISOU 4373  OE2 GLU B 264    10546  21030  12386    576   1988   3329       O  
ATOM   4374  N   ALA B 265      54.108   2.102   2.979  1.00 75.88           N  
ANISOU 4374  N   ALA B 265     5464  16275   7093    377   1522   3311       N  
ATOM   4375  CA  ALA B 265      54.944   0.907   3.033  1.00 75.39           C  
ANISOU 4375  CA  ALA B 265     5362  16264   7019    317   1444   3238       C  
ATOM   4376  C   ALA B 265      55.742   0.732   1.747  1.00 80.81           C  
ANISOU 4376  C   ALA B 265     6061  16949   7692    272   1459   3186       C  
ATOM   4377  O   ALA B 265      56.924   0.368   1.785  1.00 83.67           O  
ANISOU 4377  O   ALA B 265     6417  17299   8074    221   1465   3072       O  
ATOM   4378  CB  ALA B 265      54.081  -0.324   3.305  1.00 75.21           C  
ANISOU 4378  CB  ALA B 265     5271  16324   6980    317   1328   3325       C  
ATOM   4379  N   ALA B1001      55.117   0.999   0.597  1.00 75.84           N  
ANISOU 4379  N   ALA B1001     5444  16346   7025    292   1466   3269       N  
ATOM   4380  CA  ALA B1001      55.823   0.879  -0.674  1.00 76.06           C  
ANISOU 4380  CA  ALA B1001     5483  16396   7021    251   1485   3223       C  
ATOM   4381  C   ALA B1001      56.980   1.868  -0.760  1.00 76.20           C  
ANISOU 4381  C   ALA B1001     5565  16307   7081    242   1607   3131       C  
ATOM   4382  O   ALA B1001      58.091   1.510  -1.175  1.00 80.59           O  
ANISOU 4382  O   ALA B1001     6122  16857   7643    185   1620   3023       O  
ATOM   4383  CB  ALA B1001      54.849   1.083  -1.834  1.00 76.75           C  
ANISOU 4383  CB  ALA B1001     5561  16564   7037    286   1470   3345       C  
ATOM   4384  N   ASP B1002      56.737   3.125  -0.374  1.00 76.59           N  
ANISOU 4384  N   ASP B1002     5660  16264   7177    294   1709   3167       N  
ATOM   4385  CA  ASP B1002      57.798   4.127  -0.434  1.00 76.90           C  
ANISOU 4385  CA  ASP B1002     5748  16188   7283    282   1847   3075       C  
ATOM   4386  C   ASP B1002      58.946   3.776   0.507  1.00 77.50           C  
ANISOU 4386  C   ASP B1002     5804  16242   7400    226   1847   2908       C  
ATOM   4387  O   ASP B1002      60.124   3.921   0.148  1.00 83.01           O  
ANISOU 4387  O   ASP B1002     6517  16895   8129    182   1908   2798       O  
ATOM   4388  CB  ASP B1002      57.234   5.508  -0.103  1.00 77.59           C  
ANISOU 4388  CB  ASP B1002     5865  16174   7442    346   1971   3140       C  
ATOM   4389  CG  ASP B1002      56.227   5.989  -1.130  1.00 80.34           C  
ANISOU 4389  CG  ASP B1002     6226  16541   7760    411   1987   3320       C  
ATOM   4390  OD1 ASP B1002      55.915   5.220  -2.064  1.00 83.70           O  
ANISOU 4390  OD1 ASP B1002     6631  17082   8089    404   1890   3384       O  
ATOM   4391  OD2 ASP B1002      55.751   7.137  -1.007  1.00 79.11           O  
ANISOU 4391  OD2 ASP B1002     6086  16292   7678    469   2100   3395       O  
ATOM   4392  N   LEU B1003      58.623   3.299   1.713  1.00 75.97           N  
ANISOU 4392  N   LEU B1003     5571  16093   7202    231   1777   2892       N  
ATOM   4393  CA  LEU B1003      59.671   2.907   2.649  1.00 76.96           C  
ANISOU 4393  CA  LEU B1003     5661  16232   7347    187   1761   2751       C  
ATOM   4394  C   LEU B1003      60.485   1.736   2.112  1.00 83.63           C  
ANISOU 4394  C   LEU B1003     6472  17128   8176    130   1683   2700       C  
ATOM   4395  O   LEU B1003      61.718   1.717   2.232  1.00 85.44           O  
ANISOU 4395  O   LEU B1003     6689  17334   8440     86   1717   2569       O  
ATOM   4396  CB  LEU B1003      59.065   2.553   4.006  1.00 77.33           C  
ANISOU 4396  CB  LEU B1003     5665  16345   7373    212   1692   2774       C  
ATOM   4397  CG  LEU B1003      60.086   2.066   5.036  1.00 77.60           C  
ANISOU 4397  CG  LEU B1003     5646  16433   7405    178   1658   2652       C  
ATOM   4398  CD1 LEU B1003      61.129   3.143   5.315  1.00 79.72           C  
ANISOU 4398  CD1 LEU B1003     5925  16637   7725    154   1784   2489       C  
ATOM   4399  CD2 LEU B1003      59.403   1.617   6.314  1.00 75.40           C  
ANISOU 4399  CD2 LEU B1003     5320  16246   7083    211   1581   2706       C  
ATOM   4400  N   GLU B1004      59.811   0.740   1.528  1.00 75.03           N  
ANISOU 4400  N   GLU B1004     5354  16110   7045    127   1585   2791       N  
ATOM   4401  CA  GLU B1004      60.522  -0.400   0.962  1.00 74.80           C  
ANISOU 4401  CA  GLU B1004     5277  16123   7021     67   1526   2733       C  
ATOM   4402  C   GLU B1004      61.438   0.032  -0.176  1.00 85.01           C  
ANISOU 4402  C   GLU B1004     6610  17371   8319     29   1608   2653       C  
ATOM   4403  O   GLU B1004      62.567  -0.462  -0.298  1.00 87.29           O  
ANISOU 4403  O   GLU B1004     6871  17652   8644    -25   1610   2538       O  
ATOM   4404  CB  GLU B1004      59.521  -1.449   0.480  1.00 74.77           C  
ANISOU 4404  CB  GLU B1004     5222  16202   6986     65   1427   2832       C  
ATOM   4405  CG  GLU B1004      60.155  -2.684  -0.132  1.00 78.16           C  
ANISOU 4405  CG  GLU B1004     5583  16670   7444     -3   1377   2761       C  
ATOM   4406  CD  GLU B1004      60.825  -3.563   0.905  1.00 82.47           C  
ANISOU 4406  CD  GLU B1004     6060  17209   8065    -22   1326   2715       C  
ATOM   4407  OE1 GLU B1004      60.468  -3.458   2.098  1.00 86.92           O  
ANISOU 4407  OE1 GLU B1004     6617  17778   8630     21   1301   2771       O  
ATOM   4408  OE2 GLU B1004      61.711  -4.358   0.529  1.00 84.80           O  
ANISOU 4408  OE2 GLU B1004     6303  17499   8418    -78   1314   2627       O  
ATOM   4409  N   ASP B1005      60.975   0.966  -1.012  1.00 80.19           N  
ANISOU 4409  N   ASP B1005     6061  16731   7677     62   1680   2720       N  
ATOM   4410  CA  ASP B1005      61.823   1.475  -2.086  1.00 80.42           C  
ANISOU 4410  CA  ASP B1005     6132  16716   7708     34   1773   2663       C  
ATOM   4411  C   ASP B1005      63.055   2.180  -1.531  1.00 75.96           C  
ANISOU 4411  C   ASP B1005     5588  16046   7227     12   1876   2529       C  
ATOM   4412  O   ASP B1005      64.172   1.981  -2.029  1.00 83.95           O  
ANISOU 4412  O   ASP B1005     6596  17036   8263    -41   1912   2421       O  
ATOM   4413  CB  ASP B1005      61.028   2.418  -2.989  1.00 86.85           C  
ANISOU 4413  CB  ASP B1005     6999  17520   8478     90   1836   2793       C  
ATOM   4414  CG  ASP B1005      60.281   1.684  -4.084  1.00 96.87           C  
ANISOU 4414  CG  ASP B1005     8238  18925   9644     86   1752   2875       C  
ATOM   4415  OD1 ASP B1005      60.678   0.548  -4.416  1.00100.92           O  
ANISOU 4415  OD1 ASP B1005     8696  19515  10132     23   1682   2794       O  
ATOM   4416  OD2 ASP B1005      59.302   2.246  -4.618  1.00101.67           O  
ANISOU 4416  OD2 ASP B1005     8863  19569  10199    145   1761   3014       O  
ATOM   4417  N   ASN B1006      62.873   3.014  -0.503  1.00 76.04           N  
ANISOU 4417  N   ASN B1006     5609  15996   7285     47   1930   2522       N  
ATOM   4418  CA  ASN B1006      64.018   3.702   0.090  1.00 76.21           C  
ANISOU 4418  CA  ASN B1006     5630  15936   7391     20   2033   2372       C  
ATOM   4419  C   ASN B1006      65.016   2.715   0.689  1.00 85.07           C  
ANISOU 4419  C   ASN B1006     6686  17114   8522    -33   1954   2245       C  
ATOM   4420  O   ASN B1006      66.233   2.884   0.542  1.00 91.01           O  
ANISOU 4420  O   ASN B1006     7429  17821   9331    -79   2018   2111       O  
ATOM   4421  CB  ASN B1006      63.541   4.701   1.144  1.00 76.54           C  
ANISOU 4421  CB  ASN B1006     5675  15930   7479     61   2103   2369       C  
ATOM   4422  CG  ASN B1006      62.784   5.869   0.538  1.00 77.26           C  
ANISOU 4422  CG  ASN B1006     5820  15930   7605    114   2221   2481       C  
ATOM   4423  OD1 ASN B1006      63.080   6.305  -0.574  1.00 81.76           O  
ANISOU 4423  OD1 ASN B1006     6431  16441   8194    113   2303   2517       O  
ATOM   4424  ND2 ASN B1006      61.803   6.384   1.270  1.00 77.47           N  
ANISOU 4424  ND2 ASN B1006     5843  15948   7644    164   2234   2545       N  
ATOM   4425  N   TRP B1007      64.520   1.672   1.361  1.00 75.28           N  
ANISOU 4425  N   TRP B1007     5391  15970   7240    -26   1820   2293       N  
ATOM   4426  CA  TRP B1007      65.415   0.668   1.935  1.00 74.99           C  
ANISOU 4426  CA  TRP B1007     5279  15991   7225    -65   1743   2205       C  
ATOM   4427  C   TRP B1007      66.185  -0.084   0.855  1.00 82.14           C  
ANISOU 4427  C   TRP B1007     6167  16889   8152   -121   1732   2152       C  
ATOM   4428  O   TRP B1007      67.397  -0.316   0.990  1.00 94.84           O  
ANISOU 4428  O   TRP B1007     7735  18484   9815   -164   1747   2025       O  
ATOM   4429  CB  TRP B1007      64.621  -0.301   2.812  1.00 74.72           C  
ANISOU 4429  CB  TRP B1007     5186  16050   7154    -36   1615   2303       C  
ATOM   4430  CG  TRP B1007      65.419  -1.481   3.285  1.00 86.42           C  
ANISOU 4430  CG  TRP B1007     6578  17588   8672    -66   1530   2258       C  
ATOM   4431  CD1 TRP B1007      66.234  -1.541   4.378  1.00 84.34           C  
ANISOU 4431  CD1 TRP B1007     6253  17370   8421    -65   1512   2179       C  
ATOM   4432  CD2 TRP B1007      65.432  -2.792   2.705  1.00 84.50           C  
ANISOU 4432  CD2 TRP B1007     6277  17364   8463    -96   1453   2296       C  
ATOM   4433  NE1 TRP B1007      66.777  -2.798   4.496  1.00 85.72           N  
ANISOU 4433  NE1 TRP B1007     6342  17583   8643    -85   1428   2186       N  
ATOM   4434  CE2 TRP B1007      66.297  -3.586   3.483  1.00 86.77           C  
ANISOU 4434  CE2 TRP B1007     6475  17687   8805   -107   1398   2251       C  
ATOM   4435  CE3 TRP B1007      64.804  -3.367   1.596  1.00 82.46           C  
ANISOU 4435  CE3 TRP B1007     6024  17104   8202   -116   1431   2353       C  
ATOM   4436  CZ2 TRP B1007      66.551  -4.924   3.187  1.00 88.46           C  
ANISOU 4436  CZ2 TRP B1007     6608  17902   9101   -135   1330   2269       C  
ATOM   4437  CZ3 TRP B1007      65.057  -4.695   1.303  1.00 83.64           C  
ANISOU 4437  CZ3 TRP B1007     6088  17269   8423   -155   1366   2344       C  
ATOM   4438  CH2 TRP B1007      65.922  -5.459   2.096  1.00 87.52           C  
ANISOU 4438  CH2 TRP B1007     6494  17762   8997   -163   1321   2306       C  
ATOM   4439  N   GLU B1008      65.502  -0.477  -0.222  1.00 79.35           N  
ANISOU 4439  N   GLU B1008     5836  16558   7757   -124   1707   2237       N  
ATOM   4440  CA  GLU B1008      66.187  -1.164  -1.311  1.00 74.99           C  
ANISOU 4440  CA  GLU B1008     5261  16013   7217   -184   1708   2170       C  
ATOM   4441  C   GLU B1008      67.242  -0.269  -1.946  1.00 75.34           C  
ANISOU 4441  C   GLU B1008     5358  15977   7292   -211   1835   2066       C  
ATOM   4442  O   GLU B1008      68.340  -0.732  -2.278  1.00 75.38           O  
ANISOU 4442  O   GLU B1008     5327  15966   7347   -267   1850   1947       O  
ATOM   4443  CB  GLU B1008      65.174  -1.634  -2.354  1.00 81.77           C  
ANISOU 4443  CB  GLU B1008     6123  16941   8004   -183   1664   2267       C  
ATOM   4444  CG  GLU B1008      64.233  -2.714  -1.848  1.00 84.40           C  
ANISOU 4444  CG  GLU B1008     6384  17347   8337   -172   1544   2349       C  
ATOM   4445  CD  GLU B1008      63.114  -3.022  -2.821  1.00 95.28           C  
ANISOU 4445  CD  GLU B1008     7755  18808   9639   -168   1507   2437       C  
ATOM   4446  OE1 GLU B1008      63.118  -2.455  -3.934  1.00 99.98           O  
ANISOU 4446  OE1 GLU B1008     8399  19423  10165   -173   1566   2437       O  
ATOM   4447  OE2 GLU B1008      62.229  -3.831  -2.472  1.00 99.52           O  
ANISOU 4447  OE2 GLU B1008     8230  19399  10185   -159   1421   2507       O  
ATOM   4448  N   THR B1009      66.934   1.021  -2.107  1.00 75.72           N  
ANISOU 4448  N   THR B1009     5482  15959   7328   -172   1938   2111       N  
ATOM   4449  CA  THR B1009      67.908   1.957  -2.659  1.00 79.03           C  
ANISOU 4449  CA  THR B1009     5946  16280   7800   -194   2081   2026       C  
ATOM   4450  C   THR B1009      69.132   2.069  -1.757  1.00 81.61           C  
ANISOU 4450  C   THR B1009     6227  16561   8221   -229   2114   1861       C  
ATOM   4451  O   THR B1009      70.277   2.041  -2.231  1.00 76.32           O  
ANISOU 4451  O   THR B1009     5547  15848   7605   -279   2174   1742       O  
ATOM   4452  CB  THR B1009      67.255   3.328  -2.854  1.00 76.80           C  
ANISOU 4452  CB  THR B1009     5738  15921   7523   -136   2196   2124       C  
ATOM   4453  OG1 THR B1009      66.195   3.222  -3.813  1.00 77.07           O  
ANISOU 4453  OG1 THR B1009     5806  16017   7462   -100   2160   2280       O  
ATOM   4454  CG2 THR B1009      68.270   4.350  -3.336  1.00 77.49           C  
ANISOU 4454  CG2 THR B1009     5861  15885   7695   -156   2365   2043       C  
ATOM   4455  N   LEU B1010      68.905   2.189  -0.445  1.00 80.89           N  
ANISOU 4455  N   LEU B1010     6099  16493   8143   -202   2074   1847       N  
ATOM   4456  CA  LEU B1010      70.017   2.302   0.493  1.00 78.19           C  
ANISOU 4456  CA  LEU B1010     5695  16144   7870   -231   2093   1686       C  
ATOM   4457  C   LEU B1010      70.910   1.069   0.445  1.00 75.75           C  
ANISOU 4457  C   LEU B1010     5310  15890   7583   -279   2003   1611       C  
ATOM   4458  O   LEU B1010      72.141   1.186   0.409  1.00 76.00           O  
ANISOU 4458  O   LEU B1010     5308  15883   7686   -323   2056   1464       O  
ATOM   4459  CB  LEU B1010      69.489   2.528   1.910  1.00 76.05           C  
ANISOU 4459  CB  LEU B1010     5387  15932   7576   -192   2047   1694       C  
ATOM   4460  CG  LEU B1010      68.914   3.913   2.208  1.00 76.57           C  
ANISOU 4460  CG  LEU B1010     5500  15925   7667   -156   2168   1704       C  
ATOM   4461  CD1 LEU B1010      68.043   3.881   3.455  1.00 76.53           C  
ANISOU 4461  CD1 LEU B1010     5463  16007   7607   -112   2096   1751       C  
ATOM   4462  CD2 LEU B1010      70.034   4.927   2.367  1.00 83.23           C  
ANISOU 4462  CD2 LEU B1010     6326  16680   8618   -193   2316   1522       C  
ATOM   4463  N   ASN B1011      70.309  -0.124   0.424  1.00 75.34           N  
ANISOU 4463  N   ASN B1011     5221  15917   7489   -271   1875   1707       N  
ATOM   4464  CA  ASN B1011      71.110  -1.347   0.392  1.00 75.22           C  
ANISOU 4464  CA  ASN B1011     5118  15936   7526   -313   1798   1645       C  
ATOM   4465  C   ASN B1011      71.875  -1.477  -0.924  1.00 80.50           C  
ANISOU 4465  C   ASN B1011     5805  16549   8234   -372   1867   1561       C  
ATOM   4466  O   ASN B1011      73.068  -1.825  -0.930  1.00 75.54           O  
ANISOU 4466  O   ASN B1011     5119  15897   7686   -416   1878   1433       O  
ATOM   4467  CB  ASN B1011      70.210  -2.563   0.614  1.00 78.70           C  
ANISOU 4467  CB  ASN B1011     5506  16451   7945   -293   1668   1772       C  
ATOM   4468  CG  ASN B1011      70.250  -3.067   2.045  1.00 87.00           C  
ANISOU 4468  CG  ASN B1011     6474  17572   9009   -258   1576   1803       C  
ATOM   4469  OD1 ASN B1011      70.621  -2.336   2.963  1.00 86.66           O  
ANISOU 4469  OD1 ASN B1011     6425  17552   8949   -238   1602   1745       O  
ATOM   4470  ND2 ASN B1011      69.856  -4.321   2.241  1.00 93.32           N  
ANISOU 4470  ND2 ASN B1011     7203  18413   9844   -250   1474   1893       N  
ATOM   4471  N   ASP B1012      71.202  -1.202  -2.046  1.00 79.87           N  
ANISOU 4471  N   ASP B1012     5799  16457   8090   -371   1911   1633       N  
ATOM   4472  CA  ASP B1012      71.854  -1.252  -3.350  1.00 80.58           C  
ANISOU 4472  CA  ASP B1012     5912  16515   8190   -424   1984   1561       C  
ATOM   4473  C   ASP B1012      73.074  -0.341  -3.388  1.00 82.86           C  
ANISOU 4473  C   ASP B1012     6224  16709   8552   -449   2111   1430       C  
ATOM   4474  O   ASP B1012      74.151  -0.743  -3.842  1.00 87.12           O  
ANISOU 4474  O   ASP B1012     6725  17221   9156   -506   2140   1306       O  
ATOM   4475  CB  ASP B1012      70.860  -0.866  -4.446  1.00 86.34           C  
ANISOU 4475  CB  ASP B1012     6719  17273   8812   -403   2017   1678       C  
ATOM   4476  CG  ASP B1012      69.830  -1.947  -4.705  1.00 94.38           C  
ANISOU 4476  CG  ASP B1012     7692  18397   9769   -402   1899   1763       C  
ATOM   4477  OD1 ASP B1012      69.971  -3.050  -4.139  1.00 98.64           O  
ANISOU 4477  OD1 ASP B1012     8140  18966  10373   -423   1806   1729       O  
ATOM   4478  OD2 ASP B1012      68.878  -1.690  -5.473  1.00 99.02           O  
ANISOU 4478  OD2 ASP B1012     8326  19040  10256   -377   1902   1867       O  
ATOM   4479  N   ASN B1013      72.930   0.892  -2.897  1.00 83.86           N  
ANISOU 4479  N   ASN B1013     6402  16774   8688   -412   2197   1446       N  
ATOM   4480  CA  ASN B1013      74.047   1.824  -2.987  1.00 76.92           C  
ANISOU 4480  CA  ASN B1013     5536  15791   7900   -440   2338   1316       C  
ATOM   4481  C   ASN B1013      75.126   1.530  -1.952  1.00 76.86           C  
ANISOU 4481  C   ASN B1013     5432  15792   7979   -470   2303   1157       C  
ATOM   4482  O   ASN B1013      76.301   1.817  -2.199  1.00 81.98           O  
ANISOU 4482  O   ASN B1013     6060  16373   8716   -515   2389   1014       O  
ATOM   4483  CB  ASN B1013      73.551   3.263  -2.860  1.00 77.40           C  
ANISOU 4483  CB  ASN B1013     5666  15768   7975   -395   2464   1373       C  
ATOM   4484  CG  ASN B1013      72.720   3.697  -4.052  1.00 90.20           C  
ANISOU 4484  CG  ASN B1013     7377  17370   9526   -363   2524   1529       C  
ATOM   4485  OD1 ASN B1013      73.254   4.004  -5.119  1.00 93.85           O  
ANISOU 4485  OD1 ASN B1013     7878  17780  10001   -386   2627   1517       O  
ATOM   4486  ND2 ASN B1013      71.406   3.717  -3.879  1.00 87.41           N  
ANISOU 4486  ND2 ASN B1013     7051  17069   9091   -306   2459   1682       N  
ATOM   4487  N   LEU B1014      74.768   0.939  -0.810  1.00 76.49           N  
ANISOU 4487  N   LEU B1014     5320  15836   7908   -442   2175   1183       N  
ATOM   4488  CA  LEU B1014      75.798   0.460   0.105  1.00 76.73           C  
ANISOU 4488  CA  LEU B1014     5242  15908   8004   -464   2116   1052       C  
ATOM   4489  C   LEU B1014      76.667  -0.593  -0.565  1.00 79.50           C  
ANISOU 4489  C   LEU B1014     5537  16252   8417   -516   2080    987       C  
ATOM   4490  O   LEU B1014      77.900  -0.579  -0.435  1.00 76.89           O  
ANISOU 4490  O   LEU B1014     5147  15891   8177   -554   2112    835       O  
ATOM   4491  CB  LEU B1014      75.153  -0.108   1.368  1.00 76.36           C  
ANISOU 4491  CB  LEU B1014     5132  15980   7900   -416   1978   1132       C  
ATOM   4492  CG  LEU B1014      74.760   0.919   2.426  1.00 76.67           C  
ANISOU 4492  CG  LEU B1014     5179  16048   7903   -378   2012   1114       C  
ATOM   4493  CD1 LEU B1014      74.050   0.245   3.584  1.00 76.51           C  
ANISOU 4493  CD1 LEU B1014     5101  16164   7807   -328   1872   1216       C  
ATOM   4494  CD2 LEU B1014      75.995   1.662   2.910  1.00 90.75           C  
ANISOU 4494  CD2 LEU B1014     6908  17806   9766   -413   2093    907       C  
ATOM   4495  N   LYS B1015      76.038  -1.510  -1.300  1.00 79.16           N  
ANISOU 4495  N   LYS B1015     5504  16236   8338   -520   2019   1086       N  
ATOM   4496  CA  LYS B1015      76.816  -2.526  -2.000  1.00 84.79           C  
ANISOU 4496  CA  LYS B1015     6156  16934   9126   -575   1998   1009       C  
ATOM   4497  C   LYS B1015      77.620  -1.919  -3.148  1.00 87.82           C  
ANISOU 4497  C   LYS B1015     6595  17231   9540   -628   2139    900       C  
ATOM   4498  O   LYS B1015      78.757  -2.337  -3.401  1.00 98.21           O  
ANISOU 4498  O   LYS B1015     7851  18510  10955   -679   2159    766       O  
ATOM   4499  CB  LYS B1015      75.900  -3.651  -2.470  1.00 91.61           C  
ANISOU 4499  CB  LYS B1015     6999  17851   9958   -575   1906   1118       C  
ATOM   4500  CG  LYS B1015      75.998  -4.908  -1.637  1.00 93.45           C  
ANISOU 4500  CG  LYS B1015     7109  18124  10275   -563   1777   1145       C  
ATOM   4501  CD  LYS B1015      76.685  -4.675  -0.288  1.00 94.31           C  
ANISOU 4501  CD  LYS B1015     7154  18258  10423   -530   1739   1107       C  
ATOM   4502  CE  LYS B1015      76.569  -5.854   0.643  1.00 95.82           C  
ANISOU 4502  CE  LYS B1015     7229  18502  10675   -494   1605   1194       C  
ATOM   4503  NZ  LYS B1015      77.346  -5.651   1.883  1.00 93.70           N  
ANISOU 4503  NZ  LYS B1015     6887  18289  10426   -461   1564   1151       N  
ATOM   4504  N   VAL B1016      77.052  -0.924  -3.843  1.00 84.34           N  
ANISOU 4504  N   VAL B1016     6266  16755   9024   -613   2240    965       N  
ATOM   4505  CA  VAL B1016      77.799  -0.194  -4.870  1.00 77.47           C  
ANISOU 4505  CA  VAL B1016     5454  15798   8183   -651   2392    886       C  
ATOM   4506  C   VAL B1016      79.061   0.421  -4.277  1.00 77.80           C  
ANISOU 4506  C   VAL B1016     5454  15759   8349   -676   2470    725       C  
ATOM   4507  O   VAL B1016      80.144   0.353  -4.873  1.00 78.20           O  
ANISOU 4507  O   VAL B1016     5484  15749   8478   -730   2543    598       O  
ATOM   4508  CB  VAL B1016      76.904   0.873  -5.527  1.00 77.79           C  
ANISOU 4508  CB  VAL B1016     5611  15811   8133   -609   2489   1021       C  
ATOM   4509  CG1 VAL B1016      77.735   1.826  -6.376  1.00 78.57           C  
ANISOU 4509  CG1 VAL B1016     5766  15801   8287   -635   2667    958       C  
ATOM   4510  CG2 VAL B1016      75.832   0.206  -6.379  1.00 77.70           C  
ANISOU 4510  CG2 VAL B1016     5631  15897   7995   -597   2417   1150       C  
ATOM   4511  N   ILE B1017      78.935   1.045  -3.105  1.00 80.27           N  
ANISOU 4511  N   ILE B1017     5744  16074   8679   -640   2460    714       N  
ATOM   4512  CA  ILE B1017      80.091   1.637  -2.438  1.00 88.66           C  
ANISOU 4512  CA  ILE B1017     6748  17083   9858   -666   2525    538       C  
ATOM   4513  C   ILE B1017      81.101   0.560  -2.063  1.00 95.44           C  
ANISOU 4513  C   ILE B1017     7489  17986  10788   -702   2425    421       C  
ATOM   4514  O   ILE B1017      82.314   0.742  -2.231  1.00 91.90           O  
ANISOU 4514  O   ILE B1017     6999  17471  10449   -749   2495    261       O  
ATOM   4515  CB  ILE B1017      79.640   2.442  -1.204  1.00 85.32           C  
ANISOU 4515  CB  ILE B1017     6310  16687   9422   -623   2521    537       C  
ATOM   4516  CG1 ILE B1017      78.848   3.679  -1.627  1.00 82.03           C  
ANISOU 4516  CG1 ILE B1017     5997  16183   8989   -592   2660    629       C  
ATOM   4517  CG2 ILE B1017      80.834   2.843  -0.352  1.00 78.96           C  
ANISOU 4517  CG2 ILE B1017     5408  15868   8723   -654   2551    329       C  
ATOM   4518  CD1 ILE B1017      78.104   4.336  -0.488  1.00 78.75           C  
ANISOU 4518  CD1 ILE B1017     5570  15804   8548   -545   2647    653       C  
ATOM   4519  N   GLU B1018      80.620  -0.577  -1.547  1.00102.43           N  
ANISOU 4519  N   GLU B1018     8313  18975  11632   -676   2264    505       N  
ATOM   4520  CA  GLU B1018      81.529  -1.642  -1.124  1.00107.74           C  
ANISOU 4520  CA  GLU B1018     8860  19684  12394   -697   2166    423       C  
ATOM   4521  C   GLU B1018      82.406  -2.136  -2.269  1.00102.76           C  
ANISOU 4521  C   GLU B1018     8219  18972  11853   -762   2227    325       C  
ATOM   4522  O   GLU B1018      83.573  -2.485  -2.051  1.00101.78           O  
ANISOU 4522  O   GLU B1018     8002  18823  11845   -793   2216    190       O  
ATOM   4523  CB  GLU B1018      80.739  -2.807  -0.526  1.00118.90           C  
ANISOU 4523  CB  GLU B1018    10213  21197  13767   -653   2004    568       C  
ATOM   4524  CG  GLU B1018      81.601  -3.990  -0.102  1.00124.13           C  
ANISOU 4524  CG  GLU B1018    10737  21883  14545   -661   1903    521       C  
ATOM   4525  CD  GLU B1018      80.812  -5.055   0.633  1.00125.41           C  
ANISOU 4525  CD  GLU B1018    10833  22129  14689   -605   1755    686       C  
ATOM   4526  OE1 GLU B1018      79.725  -4.731   1.154  1.00126.52           O  
ANISOU 4526  OE1 GLU B1018    11022  22334  14713   -556   1721    811       O  
ATOM   4527  OE2 GLU B1018      81.278  -6.213   0.692  1.00125.36           O  
ANISOU 4527  OE2 GLU B1018    10722  22111  14799   -609   1681    694       O  
ATOM   4528  N   LYS B1019      81.874  -2.165  -3.491  1.00 99.21           N  
ANISOU 4528  N   LYS B1019     7856  18491  11347   -783   2289    385       N  
ATOM   4529  CA  LYS B1019      82.602  -2.651  -4.656  1.00 94.28           C  
ANISOU 4529  CA  LYS B1019     7227  17810  10786   -849   2352    289       C  
ATOM   4530  C   LYS B1019      82.983  -1.522  -5.608  1.00 98.05           C  
ANISOU 4530  C   LYS B1019     7806  18199  11250   -877   2529    237       C  
ATOM   4531  O   LYS B1019      83.177  -1.759  -6.804  1.00104.07           O  
ANISOU 4531  O   LYS B1019     8603  18939  11998   -921   2597    209       O  
ATOM   4532  CB  LYS B1019      81.781  -3.716  -5.383  1.00 87.48           C  
ANISOU 4532  CB  LYS B1019     6364  17005   9870   -859   2283    377       C  
ATOM   4533  CG  LYS B1019      81.524  -4.958  -4.541  1.00 85.56           C  
ANISOU 4533  CG  LYS B1019     6004  16815   9689   -835   2126    428       C  
ATOM   4534  CD  LYS B1019      80.777  -6.029  -5.317  1.00 91.45           C  
ANISOU 4534  CD  LYS B1019     6741  17583  10422   -856   2071    479       C  
ATOM   4535  CE  LYS B1019      80.581  -7.274  -4.465  1.00 97.38           C  
ANISOU 4535  CE  LYS B1019     7378  18339  11282   -828   1928    537       C  
ATOM   4536  NZ  LYS B1019      79.869  -8.356  -5.196  1.00101.22           N  
ANISOU 4536  NZ  LYS B1019     7837  18829  11794   -857   1885    562       N  
ATOM   4537  N   ALA B1020      83.089  -0.299  -5.097  1.00 95.92           N  
ANISOU 4537  N   ALA B1020     7576  17879  10991   -853   2614    222       N  
ATOM   4538  CA  ALA B1020      83.368   0.868  -5.917  1.00 91.64           C  
ANISOU 4538  CA  ALA B1020     7125  17232  10462   -868   2798    204       C  
ATOM   4539  C   ALA B1020      84.842   0.914  -6.310  1.00 92.13           C  
ANISOU 4539  C   ALA B1020     7143  17198  10664   -933   2893     17       C  
ATOM   4540  O   ALA B1020      85.695   0.245  -5.719  1.00 90.62           O  
ANISOU 4540  O   ALA B1020     6844  17015  10571   -959   2815   -112       O  
ATOM   4541  CB  ALA B1020      82.979   2.149  -5.180  1.00 86.87           C  
ANISOU 4541  CB  ALA B1020     6558  16584   9864   -824   2870    239       C  
ATOM   4542  N   ASP B1021      85.134   1.717  -7.332  1.00 94.49           N  
ANISOU 4542  N   ASP B1021     7523  17404  10976   -953   3065     16       N  
ATOM   4543  CA  ASP B1021      86.481   1.845  -7.874  1.00 96.19           C  
ANISOU 4543  CA  ASP B1021     7713  17514  11321  -1014   3179   -148       C  
ATOM   4544  C   ASP B1021      87.105   3.203  -7.591  1.00 96.83           C  
ANISOU 4544  C   ASP B1021     7805  17459  11526  -1015   3343   -224       C  
ATOM   4545  O   ASP B1021      88.244   3.273  -7.117  1.00 99.25           O  
ANISOU 4545  O   ASP B1021     8032  17698  11981  -1054   3364   -406       O  
ATOM   4546  CB  ASP B1021      86.455   1.589  -9.389  1.00 99.10           C  
ANISOU 4546  CB  ASP B1021     8153  17886  11616  -1043   3260   -100       C  
ATOM   4547  CG  ASP B1021      87.790   1.119  -9.928  1.00103.93           C  
ANISOU 4547  CG  ASP B1021     8712  18429  12348  -1114   3314   -281       C  
ATOM   4548  OD1 ASP B1021      88.692   0.823  -9.117  1.00106.24           O  
ANISOU 4548  OD1 ASP B1021     8904  18680  12782  -1139   3262   -434       O  
ATOM   4549  OD2 ASP B1021      87.936   1.042 -11.166  1.00106.89           O  
ANISOU 4549  OD2 ASP B1021     9141  18800  12671  -1143   3405   -269       O  
ATOM   4550  N   ASN B1022      86.393   4.291  -7.870  1.00 95.97           N  
ANISOU 4550  N   ASN B1022     7785  17301  11379   -974   3466    -90       N  
ATOM   4551  CA  ASN B1022      86.894   5.640  -7.660  1.00 98.68           C  
ANISOU 4551  CA  ASN B1022     8132  17495  11869   -974   3651   -152       C  
ATOM   4552  C   ASN B1022      85.960   6.404  -6.730  1.00106.14           C  
ANISOU 4552  C   ASN B1022     9083  18449  12797   -918   3644    -74       C  
ATOM   4553  O   ASN B1022      84.893   5.922  -6.344  1.00111.35           O  
ANISOU 4553  O   ASN B1022     9759  19230  13318   -874   3501     48       O  
ATOM   4554  CB  ASN B1022      87.049   6.390  -8.990  1.00 96.78           C  
ANISOU 4554  CB  ASN B1022     7979  17145  11647   -975   3862    -60       C  
ATOM   4555  CG  ASN B1022      85.801   6.325  -9.843  1.00 96.17           C  
ANISOU 4555  CG  ASN B1022     8004  17155  11381   -923   3851    182       C  
ATOM   4556  OD1 ASN B1022      85.134   5.293  -9.911  1.00 94.45           O  
ANISOU 4556  OD1 ASN B1022     7792  17083  11011   -915   3678    241       O  
ATOM   4557  ND2 ASN B1022      85.479   7.430 -10.505  1.00 98.97           N  
ANISOU 4557  ND2 ASN B1022     8431  17417  11754   -885   4038    325       N  
ATOM   4558  N   ALA B1023      86.382   7.619  -6.368  1.00104.87           N  
ANISOU 4558  N   ALA B1023     8901  18150  12796   -921   3809   -156       N  
ATOM   4559  CA  ALA B1023      85.613   8.423  -5.424  1.00 99.22           C  
ANISOU 4559  CA  ALA B1023     8172  17427  12098   -877   3825   -125       C  
ATOM   4560  C   ALA B1023      84.346   8.988  -6.056  1.00101.91           C  
ANISOU 4560  C   ALA B1023     8617  17755  12351   -813   3905    128       C  
ATOM   4561  O   ALA B1023      83.380   9.281  -5.343  1.00110.17           O  
ANISOU 4561  O   ALA B1023     9666  18843  13348   -766   3857    202       O  
ATOM   4562  CB  ALA B1023      86.477   9.551  -4.865  1.00 94.63           C  
ANISOU 4562  CB  ALA B1023     7522  16692  11741   -907   3989   -314       C  
ATOM   4563  N   ALA B1024      84.338   9.169  -7.380  1.00 98.29           N  
ANISOU 4563  N   ALA B1024     8239  17240  11866   -806   4027    262       N  
ATOM   4564  CA  ALA B1024      83.183   9.761  -8.051  1.00 91.87           C  
ANISOU 4564  CA  ALA B1024     7521  16414  10971   -739   4105    512       C  
ATOM   4565  C   ALA B1024      81.938   8.896  -7.883  1.00 96.64           C  
ANISOU 4565  C   ALA B1024     8167  17194  11360   -694   3887    654       C  
ATOM   4566  O   ALA B1024      80.871   9.386  -7.493  1.00101.20           O  
ANISOU 4566  O   ALA B1024     8771  17778  11901   -635   3880    784       O  
ATOM   4567  CB  ALA B1024      83.494   9.981  -9.532  1.00 86.48           C  
ANISOU 4567  CB  ALA B1024     6911  15675  10272   -743   4253    622       C  
ATOM   4568  N   GLN B1025      82.051   7.600  -8.185  1.00 98.51           N  
ANISOU 4568  N   GLN B1025     8399  17564  11466   -722   3717    629       N  
ATOM   4569  CA  GLN B1025      80.892   6.726  -8.042  1.00 99.17           C  
ANISOU 4569  CA  GLN B1025     8507  17807  11367   -684   3519    756       C  
ATOM   4570  C   GLN B1025      80.541   6.503  -6.577  1.00 90.98           C  
ANISOU 4570  C   GLN B1025     7402  16825  10341   -670   3385    692       C  
ATOM   4571  O   GLN B1025      79.371   6.268  -6.253  1.00 89.23           O  
ANISOU 4571  O   GLN B1025     7205  16690  10006   -619   3274    827       O  
ATOM   4572  CB  GLN B1025      81.137   5.396  -8.755  1.00103.57           C  
ANISOU 4572  CB  GLN B1025     9056  18482  11816   -726   3394    726       C  
ATOM   4573  CG  GLN B1025      82.309   4.593  -8.228  1.00105.68           C  
ANISOU 4573  CG  GLN B1025     9225  18753  12177   -793   3324    508       C  
ATOM   4574  CD  GLN B1025      82.369   3.205  -8.832  1.00105.75           C  
ANISOU 4574  CD  GLN B1025     9210  18877  12094   -830   3196    485       C  
ATOM   4575  OE1 GLN B1025      83.447   2.657  -9.053  1.00105.74           O  
ANISOU 4575  OE1 GLN B1025     9153  18851  12173   -891   3204    330       O  
ATOM   4576  NE2 GLN B1025      81.204   2.628  -9.103  1.00105.40           N  
ANISOU 4576  NE2 GLN B1025     9198  18953  11897   -797   3083    629       N  
ATOM   4577  N   VAL B1026      81.530   6.577  -5.683  1.00 88.25           N  
ANISOU 4577  N   VAL B1026     6966  16441  10125   -712   3391    487       N  
ATOM   4578  CA  VAL B1026      81.239   6.587  -4.251  1.00 81.36           C  
ANISOU 4578  CA  VAL B1026     6024  15628   9262   -693   3289    421       C  
ATOM   4579  C   VAL B1026      80.320   7.754  -3.913  1.00 95.34           C  
ANISOU 4579  C   VAL B1026     7834  17333  11056   -639   3394    521       C  
ATOM   4580  O   VAL B1026      79.309   7.594  -3.218  1.00 95.75           O  
ANISOU 4580  O   VAL B1026     7890  17473  11018   -594   3285    608       O  
ATOM   4581  CB  VAL B1026      82.543   6.643  -3.435  1.00 81.71           C  
ANISOU 4581  CB  VAL B1026     5958  15643   9444   -748   3298    170       C  
ATOM   4582  CG1 VAL B1026      82.243   6.962  -1.978  1.00 81.71           C  
ANISOU 4582  CG1 VAL B1026     5888  15706   9452   -726   3232     93       C  
ATOM   4583  CG2 VAL B1026      83.296   5.331  -3.546  1.00 86.07           C  
ANISOU 4583  CG2 VAL B1026     6454  16280   9971   -789   3158     89       C  
ATOM   4584  N   LYS B1027      80.662   8.949  -4.405  1.00 90.36           N  
ANISOU 4584  N   LYS B1027     7227  16539  10565   -643   3619    512       N  
ATOM   4585  CA  LYS B1027      79.827  10.123  -4.169  1.00 89.94           C  
ANISOU 4585  CA  LYS B1027     7200  16397  10576   -592   3751    609       C  
ATOM   4586  C   LYS B1027      78.445   9.954  -4.786  1.00 92.55           C  
ANISOU 4586  C   LYS B1027     7628  16789  10749   -523   3689    874       C  
ATOM   4587  O   LYS B1027      77.443  10.380  -4.204  1.00 95.75           O  
ANISOU 4587  O   LYS B1027     8041  17204  11136   -473   3676    961       O  
ATOM   4588  CB  LYS B1027      80.506  11.375  -4.726  1.00 88.69           C  
ANISOU 4588  CB  LYS B1027     7037  16036  10624   -610   4025    570       C  
ATOM   4589  CG  LYS B1027      79.669  12.637  -4.587  1.00 86.06           C  
ANISOU 4589  CG  LYS B1027     6720  15584  10396   -557   4195    679       C  
ATOM   4590  CD  LYS B1027      80.374  13.851  -5.161  1.00 87.70           C  
ANISOU 4590  CD  LYS B1027     6909  15575  10839   -576   4487    648       C  
ATOM   4591  CE  LYS B1027      79.521  15.101  -5.002  1.00 88.83           C  
ANISOU 4591  CE  LYS B1027     7052  15588  11113   -528   4666    754       C  
ATOM   4592  NZ  LYS B1027      80.211  16.317  -5.513  1.00 90.65           N  
ANISOU 4592  NZ  LYS B1027     7245  15594  11602   -556   4967    711       N  
ATOM   4593  N   ASP B1028      78.371   9.334  -5.964  1.00 92.47           N  
ANISOU 4593  N   ASP B1028     7684  16827  10622   -521   3649    994       N  
ATOM   4594  CA  ASP B1028      77.078   9.138  -6.619  1.00 94.60           C  
ANISOU 4594  CA  ASP B1028     8037  17175  10731   -457   3577   1234       C  
ATOM   4595  C   ASP B1028      76.181   8.210  -5.803  1.00 87.84           C  
ANISOU 4595  C   ASP B1028     7162  16473   9741   -435   3352   1266       C  
ATOM   4596  O   ASP B1028      74.997   8.502  -5.569  1.00 90.02           O  
ANISOU 4596  O   ASP B1028     7469  16773   9960   -373   3319   1413       O  
ATOM   4597  CB  ASP B1028      77.289   8.586  -8.030  1.00104.04           C  
ANISOU 4597  CB  ASP B1028     9289  18423  11818   -471   3571   1313       C  
ATOM   4598  CG  ASP B1028      75.993   8.443  -8.801  1.00109.98           C  
ANISOU 4598  CG  ASP B1028    10115  19273  12399   -405   3501   1549       C  
ATOM   4599  OD1 ASP B1028      75.239   9.434  -8.889  1.00112.51           O  
ANISOU 4599  OD1 ASP B1028    10473  19524  12750   -341   3599   1704       O  
ATOM   4600  OD2 ASP B1028      75.730   7.339  -9.323  1.00111.48           O  
ANISOU 4600  OD2 ASP B1028    10312  19613  12433   -419   3350   1573       O  
ATOM   4601  N   ALA B1029      76.733   7.076  -5.365  1.00 82.98           N  
ANISOU 4601  N   ALA B1029     6487  15957   9086   -482   3201   1136       N  
ATOM   4602  CA  ALA B1029      75.971   6.143  -4.545  1.00 79.81           C  
ANISOU 4602  CA  ALA B1029     6053  15694   8577   -462   2999   1168       C  
ATOM   4603  C   ALA B1029      75.575   6.775  -3.217  1.00 82.86           C  
ANISOU 4603  C   ALA B1029     6399  16066   9016   -433   3002   1130       C  
ATOM   4604  O   ALA B1029      74.459   6.562  -2.729  1.00 79.35           O  
ANISOU 4604  O   ALA B1029     5967  15698   8483   -385   2900   1245       O  
ATOM   4605  CB  ALA B1029      76.776   4.865  -4.317  1.00 79.16           C  
ANISOU 4605  CB  ALA B1029     5897  15700   8479   -517   2863   1037       C  
ATOM   4606  N   LEU B1030      76.473   7.564  -2.620  1.00 81.59           N  
ANISOU 4606  N   LEU B1030     6184  15815   9002   -464   3123    958       N  
ATOM   4607  CA  LEU B1030      76.136   8.254  -1.380  1.00 82.67           C  
ANISOU 4607  CA  LEU B1030     6271  15945   9192   -444   3146    890       C  
ATOM   4608  C   LEU B1030      75.058   9.307  -1.598  1.00 81.57           C  
ANISOU 4608  C   LEU B1030     6194  15717   9083   -385   3269   1045       C  
ATOM   4609  O   LEU B1030      74.245   9.547  -0.703  1.00 83.16           O  
ANISOU 4609  O   LEU B1030     6377  15960   9262   -349   3229   1068       O  
ATOM   4610  CB  LEU B1030      77.386   8.888  -0.771  1.00 81.50           C  
ANISOU 4610  CB  LEU B1030     6036  15723   9205   -499   3258    642       C  
ATOM   4611  CG  LEU B1030      78.278   7.953   0.047  1.00 89.47           C  
ANISOU 4611  CG  LEU B1030     6949  16858  10187   -542   3105    468       C  
ATOM   4612  CD1 LEU B1030      79.562   8.652   0.457  1.00 92.12           C  
ANISOU 4612  CD1 LEU B1030     7200  17112  10689   -599   3226    216       C  
ATOM   4613  CD2 LEU B1030      77.528   7.451   1.271  1.00 80.56           C  
ANISOU 4613  CD2 LEU B1030     5777  15890   8942   -506   2937    491       C  
ATOM   4614  N   THR B1031      75.025   9.933  -2.775  1.00 81.99           N  
ANISOU 4614  N   THR B1031     6314  15655   9185   -370   3417   1160       N  
ATOM   4615  CA  THR B1031      73.971  10.895  -3.078  1.00 82.70           C  
ANISOU 4615  CA  THR B1031     6457  15659   9305   -305   3530   1338       C  
ATOM   4616  C   THR B1031      72.619  10.201  -3.181  1.00 84.18           C  
ANISOU 4616  C   THR B1031     6696  15977   9310   -246   3355   1536       C  
ATOM   4617  O   THR B1031      71.615  10.682  -2.637  1.00 82.03           O  
ANISOU 4617  O   THR B1031     6427  15697   9042   -195   3361   1620       O  
ATOM   4618  CB  THR B1031      74.296  11.639  -4.373  1.00 83.81           C  
ANISOU 4618  CB  THR B1031     6652  15664   9526   -297   3719   1437       C  
ATOM   4619  OG1 THR B1031      75.613  12.197  -4.287  1.00 88.58           O  
ANISOU 4619  OG1 THR B1031     7200  16145  10313   -359   3883   1242       O  
ATOM   4620  CG2 THR B1031      73.294  12.757  -4.614  1.00 84.83           C  
ANISOU 4620  CG2 THR B1031     6819  15689   9725   -226   3857   1621       C  
ATOM   4621  N   LYS B1032      72.572   9.072  -3.892  1.00 81.14           N  
ANISOU 4621  N   LYS B1032     6345  15710   8777   -255   3208   1602       N  
ATOM   4622  CA  LYS B1032      71.328   8.305  -3.953  1.00 80.42           C  
ANISOU 4622  CA  LYS B1032     6282  15751   8522   -209   3035   1763       C  
ATOM   4623  C   LYS B1032      70.903   7.829  -2.564  1.00 87.22           C  
ANISOU 4623  C   LYS B1032     7087  16698   9354   -204   2901   1701       C  
ATOM   4624  O   LYS B1032      69.712   7.867  -2.223  1.00 88.00           O  
ANISOU 4624  O   LYS B1032     7202  16841   9392   -149   2839   1828       O  
ATOM   4625  CB  LYS B1032      71.474   7.127  -4.917  1.00 79.93           C  
ANISOU 4625  CB  LYS B1032     6239  15802   8329   -236   2913   1797       C  
ATOM   4626  CG  LYS B1032      71.757   7.546  -6.354  1.00 85.01           C  
ANISOU 4626  CG  LYS B1032     6941  16399   8961   -233   3030   1879       C  
ATOM   4627  CD  LYS B1032      71.862   6.345  -7.281  1.00 90.76           C  
ANISOU 4627  CD  LYS B1032     7673  17263   9550   -267   2910   1886       C  
ATOM   4628  CE  LYS B1032      72.065   6.783  -8.724  1.00 94.89           C  
ANISOU 4628  CE  LYS B1032     8252  17770  10032   -259   3022   1976       C  
ATOM   4629  NZ  LYS B1032      72.018   5.634  -9.672  1.00 97.57           N  
ANISOU 4629  NZ  LYS B1032     8585  18270  10218   -293   2906   1975       N  
ATOM   4630  N   MET B1033      71.863   7.385  -1.747  1.00 92.95           N  
ANISOU 4630  N   MET B1033     7741  17457  10117   -257   2855   1511       N  
ATOM   4631  CA  MET B1033      71.553   6.987  -0.377  1.00 78.77           C  
ANISOU 4631  CA  MET B1033     5883  15760   8287   -249   2736   1452       C  
ATOM   4632  C   MET B1033      71.002   8.152   0.433  1.00 79.44           C  
ANISOU 4632  C   MET B1033     5957  15779   8447   -215   2845   1437       C  
ATOM   4633  O   MET B1033      70.068   7.980   1.223  1.00 79.13           O  
ANISOU 4633  O   MET B1033     5907  15819   8341   -177   2756   1499       O  
ATOM   4634  CB  MET B1033      72.794   6.414   0.306  1.00 78.60           C  
ANISOU 4634  CB  MET B1033     5774  15791   8297   -307   2680   1252       C  
ATOM   4635  CG  MET B1033      72.965   4.921   0.138  1.00 86.69           C  
ANISOU 4635  CG  MET B1033     6772  16935   9231   -326   2504   1278       C  
ATOM   4636  SD  MET B1033      74.469   4.324   0.926  1.00 91.61           S  
ANISOU 4636  SD  MET B1033     7279  17615   9912   -384   2448   1059       S  
ATOM   4637  CE  MET B1033      74.181   4.851   2.615  1.00 78.17           C  
ANISOU 4637  CE  MET B1033     5508  15994   8198   -356   2421    980       C  
ATOM   4638  N   ARG B1034      71.592   9.339   0.278  1.00 80.45           N  
ANISOU 4638  N   ARG B1034     6078  15761   8731   -232   3048   1345       N  
ATOM   4639  CA  ARG B1034      71.109  10.505   1.007  1.00 81.31           C  
ANISOU 4639  CA  ARG B1034     6159  15789   8947   -208   3181   1309       C  
ATOM   4640  C   ARG B1034      69.691  10.853   0.587  1.00 81.40           C  
ANISOU 4640  C   ARG B1034     6238  15772   8919   -134   3193   1541       C  
ATOM   4641  O   ARG B1034      68.860  11.210   1.427  1.00 81.56           O  
ANISOU 4641  O   ARG B1034     6236  15812   8942   -101   3190   1556       O  
ATOM   4642  CB  ARG B1034      72.039  11.697   0.787  1.00 88.52           C  
ANISOU 4642  CB  ARG B1034     7039  16527  10068   -244   3421   1169       C  
ATOM   4643  CG  ARG B1034      71.694  12.893   1.659  1.00 83.67           C  
ANISOU 4643  CG  ARG B1034     6365  15825   9601   -234   3577   1074       C  
ATOM   4644  CD  ARG B1034      72.475  14.133   1.264  1.00 85.13           C  
ANISOU 4644  CD  ARG B1034     6513  15803  10029   -264   3846    968       C  
ATOM   4645  NE  ARG B1034      72.338  15.192   2.260  1.00 86.32           N  
ANISOU 4645  NE  ARG B1034     6572  15878  10346   -273   3997    807       N  
ATOM   4646  CZ  ARG B1034      71.359  16.091   2.268  1.00 95.71           C  
ANISOU 4646  CZ  ARG B1034     7767  16961  11636   -225   4132    916       C  
ATOM   4647  NH1 ARG B1034      70.422  16.063   1.330  1.00 91.61           N  
ANISOU 4647  NH1 ARG B1034     7345  16407  11054   -157   4118   1201       N  
ATOM   4648  NH2 ARG B1034      71.315  17.018   3.216  1.00 94.51           N  
ANISOU 4648  NH2 ARG B1034     7516  16743  11652   -243   4278    733       N  
ATOM   4649  N   ALA B1035      69.398  10.761  -0.711  1.00 81.42           N  
ANISOU 4649  N   ALA B1035     6317  15741   8880   -106   3206   1721       N  
ATOM   4650  CA  ALA B1035      68.035  10.994  -1.178  1.00 81.58           C  
ANISOU 4650  CA  ALA B1035     6392  15760   8842    -30   3191   1954       C  
ATOM   4651  C   ALA B1035      67.067   9.997  -0.549  1.00 84.43           C  
ANISOU 4651  C   ALA B1035     6749  16282   9048     -4   2978   2022       C  
ATOM   4652  O   ALA B1035      65.996  10.376  -0.056  1.00 80.68           O  
ANISOU 4652  O   ALA B1035     6273  15808   8573     47   2977   2111       O  
ATOM   4653  CB  ALA B1035      67.980  10.914  -2.704  1.00 81.89           C  
ANISOU 4653  CB  ALA B1035     6503  15784   8828     -8   3212   2122       C  
ATOM   4654  N   ALA B1036      67.437   8.713  -0.551  1.00 82.03           N  
ANISOU 4654  N   ALA B1036     6434  16107   8628    -41   2807   1980       N  
ATOM   4655  CA  ALA B1036      66.578   7.687   0.034  1.00 81.40           C  
ANISOU 4655  CA  ALA B1036     6338  16171   8419    -20   2614   2048       C  
ATOM   4656  C   ALA B1036      66.331   7.947   1.517  1.00 81.30           C  
ANISOU 4656  C   ALA B1036     6270  16190   8431    -13   2603   1957       C  
ATOM   4657  O   ALA B1036      65.193   7.865   1.993  1.00 82.02           O  
ANISOU 4657  O   ALA B1036     6364  16332   8469     34   2538   2063       O  
ATOM   4658  CB  ALA B1036      67.195   6.304  -0.176  1.00 82.12           C  
ANISOU 4658  CB  ALA B1036     6405  16373   8426    -67   2464   1998       C  
ATOM   4659  N   ALA B1037      67.393   8.255   2.266  1.00 78.96           N  
ANISOU 4659  N   ALA B1037     5914  15876   8210    -61   2664   1752       N  
ATOM   4660  CA  ALA B1037      67.256   8.477   3.703  1.00 79.19           C  
ANISOU 4660  CA  ALA B1037     5876  15970   8241    -60   2649   1638       C  
ATOM   4661  C   ALA B1037      66.463   9.745   4.000  1.00 80.09           C  
ANISOU 4661  C   ALA B1037     5995  15982   8451    -22   2800   1660       C  
ATOM   4662  O   ALA B1037      65.677   9.782   4.954  1.00 80.14           O  
ANISOU 4662  O   ALA B1037     5975  16060   8416      5   2756   1668       O  
ATOM   4663  CB  ALA B1037      68.636   8.544   4.356  1.00 79.55           C  
ANISOU 4663  CB  ALA B1037     5843  16039   8342   -122   2679   1396       C  
ATOM   4664  N   LEU B1038      66.663  10.794   3.200  1.00 80.93           N  
ANISOU 4664  N   LEU B1038     6130  15920   8698    -20   2991   1675       N  
ATOM   4665  CA  LEU B1038      65.920  12.036   3.374  1.00 95.24           C  
ANISOU 4665  CA  LEU B1038     7937  17611  10639     19   3160   1711       C  
ATOM   4666  C   LEU B1038      64.437  11.843   3.096  1.00 99.23           C  
ANISOU 4666  C   LEU B1038     8495  18148  11059     93   3080   1950       C  
ATOM   4667  O   LEU B1038      63.591  12.441   3.773  1.00105.90           O  
ANISOU 4667  O   LEU B1038     9315  18971  11950    127   3135   1965       O  
ATOM   4668  CB  LEU B1038      66.500  13.118   2.464  1.00 83.08           C  
ANISOU 4668  CB  LEU B1038     6409  15875   9281     11   3386   1706       C  
ATOM   4669  CG  LEU B1038      65.981  14.543   2.654  1.00 84.52           C  
ANISOU 4669  CG  LEU B1038     6560  15893   9661     41   3611   1710       C  
ATOM   4670  CD1 LEU B1038      66.412  15.098   4.002  1.00 85.25           C  
ANISOU 4670  CD1 LEU B1038     6545  15986   9860     -8   3699   1437       C  
ATOM   4671  CD2 LEU B1038      66.461  15.438   1.521  1.00 86.89           C  
ANISOU 4671  CD2 LEU B1038     6883  16002  10127     46   3816   1776       C  
ATOM   4672  N   ASP B1039      64.100  11.020   2.099  1.00 96.52           N  
ANISOU 4672  N   ASP B1039     8216  17861  10597    117   2955   2126       N  
ATOM   4673  CA  ASP B1039      62.695  10.809   1.767  1.00 99.23           C  
ANISOU 4673  CA  ASP B1039     8598  18247  10859    187   2872   2347       C  
ATOM   4674  C   ASP B1039      61.935  10.193   2.936  1.00 99.76           C  
ANISOU 4674  C   ASP B1039     8630  18440  10835    199   2734   2336       C  
ATOM   4675  O   ASP B1039      60.780  10.555   3.193  1.00100.54           O  
ANISOU 4675  O   ASP B1039     8731  18530  10940    254   2743   2448       O  
ATOM   4676  CB  ASP B1039      62.581   9.928   0.523  1.00106.56           C  
ANISOU 4676  CB  ASP B1039     9578  19245  11665    197   2752   2494       C  
ATOM   4677  CG  ASP B1039      61.233  10.052  -0.157  1.00116.60           C  
ANISOU 4677  CG  ASP B1039    10883  20534  12886    275   2719   2728       C  
ATOM   4678  OD1 ASP B1039      60.469  10.973   0.200  1.00121.75           O  
ANISOU 4678  OD1 ASP B1039    11525  21109  13625    325   2818   2794       O  
ATOM   4679  OD2 ASP B1039      60.941   9.232  -1.052  1.00120.42           O  
ANISOU 4679  OD2 ASP B1039    11390  21116  13248    283   2597   2839       O  
ATOM   4680  N   ALA B1040      62.563   9.258   3.656  1.00 97.53           N  
ANISOU 4680  N   ALA B1040     8311  18277  10471    153   2608   2212       N  
ATOM   4681  CA  ALA B1040      61.869   8.585   4.750  1.00 91.53           C  
ANISOU 4681  CA  ALA B1040     7516  17649   9614    168   2472   2223       C  
ATOM   4682  C   ALA B1040      61.689   9.503   5.954  1.00 94.62           C  
ANISOU 4682  C   ALA B1040     7855  18023  10074    171   2578   2097       C  
ATOM   4683  O   ALA B1040      60.744   9.325   6.731  1.00 98.20           O  
ANISOU 4683  O   ALA B1040     8291  18552  10469    203   2515   2150       O  
ATOM   4684  CB  ALA B1040      62.624   7.319   5.157  1.00 82.81           C  
ANISOU 4684  CB  ALA B1040     6374  16680   8410    126   2315   2149       C  
ATOM   4685  N   GLY B1041      62.573  10.482   6.123  1.00 93.31           N  
ANISOU 4685  N   GLY B1041     7655  17760  10038    133   2746   1919       N  
ATOM   4686  CA  GLY B1041      62.503  11.394   7.251  1.00 95.30           C  
ANISOU 4686  CA  GLY B1041     7838  17998  10371    122   2866   1755       C  
ATOM   4687  C   GLY B1041      61.351  12.376   7.180  1.00 98.60           C  
ANISOU 4687  C   GLY B1041     8268  18302  10894    175   2997   1858       C  
ATOM   4688  O   GLY B1041      60.559  12.486   8.117  1.00101.72           O  
ANISOU 4688  O   GLY B1041     8629  18762  11259    195   2981   1843       O  
ATOM   4689  N   GLY B1045      66.852   9.317   9.428  1.00106.50           N  
ANISOU 4689  N   GLY B1045     9023  19869  11571    -71   2574   1108       N  
ATOM   4690  CA  GLY B1045      66.086  10.548   9.473  1.00111.80           C  
ANISOU 4690  CA  GLY B1045     9707  20410  12363    -53   2747   1096       C  
ATOM   4691  C   GLY B1045      66.942  11.780   9.698  1.00117.17           C  
ANISOU 4691  C   GLY B1045    10319  20981  13218   -105   2950    839       C  
ATOM   4692  O   GLY B1045      66.986  12.678   8.856  1.00116.50           O  
ANISOU 4692  O   GLY B1045    10265  20692  13309   -107   3132    856       O  
ATOM   4693  N   ASP B1066      67.620  11.827  10.836  1.00123.37           N  
ANISOU 4693  N   ASP B1066    11004  21911  13961   -146   2923    604       N  
ATOM   4694  CA  ASP B1066      68.451  12.982  11.164  1.00122.18           C  
ANISOU 4694  CA  ASP B1066    10769  21669  13986   -204   3111    321       C  
ATOM   4695  C   ASP B1066      69.865  12.592  11.564  1.00111.80           C  
ANISOU 4695  C   ASP B1066     9375  20473  12631   -263   3037    106       C  
ATOM   4696  O   ASP B1066      70.816  13.267  11.162  1.00107.18           O  
ANISOU 4696  O   ASP B1066     8758  19749  12217   -313   3179    -61       O  
ATOM   4697  CB  ASP B1066      67.796  13.797  12.289  1.00129.55           C  
ANISOU 4697  CB  ASP B1066    11631  22646  14945   -204   3196    177       C  
ATOM   4698  CG  ASP B1066      67.646  15.263  11.934  1.00132.17           C  
ANISOU 4698  CG  ASP B1066    11943  22724  15553   -217   3475     84       C  
ATOM   4699  OD1 ASP B1066      68.545  15.808  11.259  1.00133.13           O  
ANISOU 4699  OD1 ASP B1066    12051  22680  15853   -254   3615     -9       O  
ATOM   4700  OD2 ASP B1066      66.625  15.867  12.326  1.00131.71           O  
ANISOU 4700  OD2 ASP B1066    11873  22624  15546   -187   3564    112       O  
ATOM   4701  N   ILE B1067      70.033  11.525  12.347  1.00106.25           N  
ANISOU 4701  N   ILE B1067     8632  20023  11715   -255   2825    114       N  
ATOM   4702  CA  ILE B1067      71.387  11.058  12.618  1.00 99.42           C  
ANISOU 4702  CA  ILE B1067     7688  19276  10809   -303   2742    -56       C  
ATOM   4703  C   ILE B1067      71.920  10.325  11.397  1.00 92.05           C  
ANISOU 4703  C   ILE B1067     6827  18244   9905   -303   2696     93       C  
ATOM   4704  O   ILE B1067      73.121  10.387  11.090  1.00 91.91           O  
ANISOU 4704  O   ILE B1067     6769  18183   9970   -353   2730    -58       O  
ATOM   4705  CB  ILE B1067      71.408  10.163  13.870  1.00 97.85           C  
ANISOU 4705  CB  ILE B1067     7407  19395  10376   -285   2538    -75       C  
ATOM   4706  CG1 ILE B1067      70.923  10.932  15.104  1.00 94.08           C  
ANISOU 4706  CG1 ILE B1067     6853  19038   9856   -292   2589   -250       C  
ATOM   4707  CG2 ILE B1067      72.802   9.599  14.113  1.00101.39           C  
ANISOU 4707  CG2 ILE B1067     7766  19979  10778   -323   2441   -221       C  
ATOM   4708  CD1 ILE B1067      69.443  10.767  15.402  1.00 89.89           C  
ANISOU 4708  CD1 ILE B1067     6379  18545   9231   -229   2553    -44       C  
ATOM   4709  N   LEU B1068      71.025   9.665  10.660  1.00 89.25           N  
ANISOU 4709  N   LEU B1068     6575  17846   9492   -251   2627    375       N  
ATOM   4710  CA  LEU B1068      71.430   8.903   9.488  1.00 84.91           C  
ANISOU 4710  CA  LEU B1068     6090  17218   8954   -252   2576    515       C  
ATOM   4711  C   LEU B1068      71.950   9.832   8.403  1.00 83.47           C  
ANISOU 4711  C   LEU B1068     5950  16797   8968   -286   2775    456       C  
ATOM   4712  O   LEU B1068      72.990   9.568   7.791  1.00 85.65           O  
ANISOU 4712  O   LEU B1068     6220  17026   9297   -325   2782    394       O  
ATOM   4713  CB  LEU B1068      70.259   8.065   8.978  1.00 83.52           C  
ANISOU 4713  CB  LEU B1068     6004  17053   8676   -192   2463    807       C  
ATOM   4714  CG  LEU B1068      70.559   7.256   7.722  1.00 80.08           C  
ANISOU 4714  CG  LEU B1068     5634  16544   8247   -197   2412    945       C  
ATOM   4715  CD1 LEU B1068      71.699   6.311   8.011  1.00 79.94           C  
ANISOU 4715  CD1 LEU B1068     5539  16649   8185   -229   2292    855       C  
ATOM   4716  CD2 LEU B1068      69.329   6.489   7.277  1.00 81.09           C  
ANISOU 4716  CD2 LEU B1068     5836  16691   8283   -143   2305   1205       C  
ATOM   4717  N   VAL B1069      71.221  10.921   8.144  1.00 83.24           N  
ANISOU 4717  N   VAL B1069     5959  16612   9057   -268   2946    488       N  
ATOM   4718  CA  VAL B1069      71.659  11.907   7.162  1.00 83.85           C  
ANISOU 4718  CA  VAL B1069     6064  16456   9338   -291   3162    454       C  
ATOM   4719  C   VAL B1069      72.969  12.550   7.591  1.00 98.65           C  
ANISOU 4719  C   VAL B1069     7838  18293  11351   -361   3272    151       C  
ATOM   4720  O   VAL B1069      73.812  12.870   6.749  1.00101.32           O  
ANISOU 4720  O   VAL B1069     8186  18485  11825   -395   3388    105       O  
ATOM   4721  CB  VAL B1069      70.555  12.960   6.940  1.00 84.47           C  
ANISOU 4721  CB  VAL B1069     6181  16385   9530   -248   3330    560       C  
ATOM   4722  CG1 VAL B1069      70.993  13.986   5.905  1.00 85.31           C  
ANISOU 4722  CG1 VAL B1069     6307  16247   9860   -262   3570    558       C  
ATOM   4723  CG2 VAL B1069      69.263  12.284   6.514  1.00 86.67           C  
ANISOU 4723  CG2 VAL B1069     6555  16711   9666   -179   3203    852       C  
ATOM   4724  N   GLY B1070      73.174  12.738   8.897  1.00 91.38           N  
ANISOU 4724  N   GLY B1070     6816  17511  10394   -386   3234    -64       N  
ATOM   4725  CA  GLY B1070      74.451  13.262   9.360  1.00 91.71           C  
ANISOU 4725  CA  GLY B1070     6752  17542  10551   -456   3309   -373       C  
ATOM   4726  C   GLY B1070      75.608  12.327   9.064  1.00 93.20           C  
ANISOU 4726  C   GLY B1070     6923  17812  10677   -489   3180   -414       C  
ATOM   4727  O   GLY B1070      76.671  12.759   8.603  1.00 97.19           O  
ANISOU 4727  O   GLY B1070     7401  18189  11340   -540   3291   -565       O  
ATOM   4728  N   GLN B1071      75.418  11.029   9.315  1.00 85.41           N  
ANISOU 4728  N   GLN B1071     5947  17028   9478   -457   2952   -276       N  
ATOM   4729  CA  GLN B1071      76.472  10.069   8.997  1.00 84.84           C  
ANISOU 4729  CA  GLN B1071     5851  17024   9362   -482   2833   -293       C  
ATOM   4730  C   GLN B1071      76.697   9.972   7.488  1.00 93.10           C  
ANISOU 4730  C   GLN B1071     6993  17871  10508   -488   2916   -157       C  
ATOM   4731  O   GLN B1071      77.840   9.834   7.029  1.00 91.84           O  
ANISOU 4731  O   GLN B1071     6807  17659  10431   -534   2940   -267       O  
ATOM   4732  CB  GLN B1071      76.132   8.705   9.596  1.00 84.00           C  
ANISOU 4732  CB  GLN B1071     5722  17160   9032   -438   2590   -149       C  
ATOM   4733  CG  GLN B1071      75.914   8.733  11.103  1.00 86.88           C  
ANISOU 4733  CG  GLN B1071     5986  17758   9265   -426   2499   -262       C  
ATOM   4734  CD  GLN B1071      75.660   7.357  11.685  1.00 84.29           C  
ANISOU 4734  CD  GLN B1071     5626  17669   8732   -376   2272    -94       C  
ATOM   4735  OE1 GLN B1071      75.952   6.340  11.056  1.00 83.32           O  
ANISOU 4735  OE1 GLN B1071     5526  17540   8591   -364   2177     49       O  
ATOM   4736  NE2 GLN B1071      75.110   7.319  12.893  1.00 84.98           N  
ANISOU 4736  NE2 GLN B1071     5651  17964   8673   -345   2193   -109       N  
ATOM   4737  N   ILE B1072      75.619  10.047   6.702  1.00 83.33           N  
ANISOU 4737  N   ILE B1072     5867  16534   9261   -441   2959     80       N  
ATOM   4738  CA  ILE B1072      75.757  10.049   5.247  1.00 82.83           C  
ANISOU 4738  CA  ILE B1072     5895  16302   9274   -444   3047    214       C  
ATOM   4739  C   ILE B1072      76.517  11.285   4.787  1.00 84.03           C  
ANISOU 4739  C   ILE B1072     6028  16247   9652   -487   3289     61       C  
ATOM   4740  O   ILE B1072      77.315  11.226   3.847  1.00 86.19           O  
ANISOU 4740  O   ILE B1072     6326  16417  10004   -518   3356     54       O  
ATOM   4741  CB  ILE B1072      74.376   9.953   4.567  1.00 82.09           C  
ANISOU 4741  CB  ILE B1072     5914  16167   9112   -379   3038    495       C  
ATOM   4742  CG1 ILE B1072      73.688   8.632   4.908  1.00 87.64           C  
ANISOU 4742  CG1 ILE B1072     6630  17053   9614   -341   2804    649       C  
ATOM   4743  CG2 ILE B1072      74.507  10.096   3.057  1.00 81.92           C  
ANISOU 4743  CG2 ILE B1072     5981  15989   9157   -379   3143    626       C  
ATOM   4744  CD1 ILE B1072      72.331   8.466   4.262  1.00 80.28           C  
ANISOU 4744  CD1 ILE B1072     5799  16093   8611   -281   2776    909       C  
ATOM   4745  N   ASP B1073      76.302  12.418   5.457  1.00 88.04           N  
ANISOU 4745  N   ASP B1073     6484  16687  10281   -493   3433    -73       N  
ATOM   4746  CA  ASP B1073      77.024  13.635   5.104  1.00 93.30           C  
ANISOU 4746  CA  ASP B1073     7113  17138  11198   -534   3681   -228       C  
ATOM   4747  C   ASP B1073      78.498  13.524   5.467  1.00 90.55           C  
ANISOU 4747  C   ASP B1073     6673  16816  10915   -606   3661   -501       C  
ATOM   4748  O   ASP B1073      79.362  14.033   4.745  1.00 87.86           O  
ANISOU 4748  O   ASP B1073     6329  16302  10751   -643   3815   -574       O  
ATOM   4749  CB  ASP B1073      76.388  14.836   5.802  1.00103.68           C  
ANISOU 4749  CB  ASP B1073     8379  18370  12646   -523   3841   -317       C  
ATOM   4750  CG  ASP B1073      75.199  15.383   5.044  1.00108.13           C  
ANISOU 4750  CG  ASP B1073     9027  18796  13263   -459   3971    -56       C  
ATOM   4751  OD1 ASP B1073      75.141  15.187   3.813  1.00108.28           O  
ANISOU 4751  OD1 ASP B1073     9135  18727  13281   -437   4007    150       O  
ATOM   4752  OD2 ASP B1073      74.325  16.009   5.679  1.00110.01           O  
ANISOU 4752  OD2 ASP B1073     9238  19021  13540   -431   4035    -59       O  
ATOM   4753  N   ASP B1074      78.803  12.852   6.579  1.00 91.33           N  
ANISOU 4753  N   ASP B1074     6692  17138  10870   -622   3470   -642       N  
ATOM   4754  CA  ASP B1074      80.198  12.584   6.920  1.00 92.98           C  
ANISOU 4754  CA  ASP B1074     6809  17406  11113   -683   3414   -881       C  
ATOM   4755  C   ASP B1074      80.867  11.733   5.845  1.00 87.07           C  
ANISOU 4755  C   ASP B1074     6112  16619  10350   -694   3363   -773       C  
ATOM   4756  O   ASP B1074      81.971  12.048   5.376  1.00 87.25           O  
ANISOU 4756  O   ASP B1074     6109  16517  10527   -745   3463   -915       O  
ATOM   4757  CB  ASP B1074      80.282  11.893   8.281  1.00101.93           C  
ANISOU 4757  CB  ASP B1074     7844  18827  12058   -682   3198   -996       C  
ATOM   4758  CG  ASP B1074      79.795  12.772   9.413  1.00112.01           C  
ANISOU 4758  CG  ASP B1074     9053  20161  13347   -686   3252  -1162       C  
ATOM   4759  OD1 ASP B1074      80.007  14.001   9.350  1.00116.46           O  
ANISOU 4759  OD1 ASP B1074     9592  20532  14127   -722   3461  -1326       O  
ATOM   4760  OD2 ASP B1074      79.202  12.232  10.370  1.00115.59           O  
ANISOU 4760  OD2 ASP B1074     9470  20848  13600   -652   3092  -1126       O  
ATOM   4761  N   ALA B1075      80.210  10.638   5.451  1.00 85.18           N  
ANISOU 4761  N   ALA B1075     5944  16484   9935   -647   3208   -529       N  
ATOM   4762  CA  ALA B1075      80.742   9.794   4.384  1.00 84.28           C  
ANISOU 4762  CA  ALA B1075     5882  16335   9807   -658   3163   -425       C  
ATOM   4763  C   ALA B1075      80.890  10.570   3.079  1.00 93.52           C  
ANISOU 4763  C   ALA B1075     7132  17265  11135   -671   3381   -361       C  
ATOM   4764  O   ALA B1075      81.863  10.380   2.340  1.00 96.92           O  
ANISOU 4764  O   ALA B1075     7564  17616  11644   -712   3426   -416       O  
ATOM   4765  CB  ALA B1075      79.844   8.574   4.184  1.00 82.87           C  
ANISOU 4765  CB  ALA B1075     5764  16290   9431   -605   2976   -175       C  
ATOM   4766  N   LEU B1076      79.943  11.464   2.787  1.00 92.02           N  
ANISOU 4766  N   LEU B1076     7004  16961  11001   -634   3526   -238       N  
ATOM   4767  CA  LEU B1076      79.985  12.220   1.540  1.00 92.64           C  
ANISOU 4767  CA  LEU B1076     7153  16826  11220   -631   3742   -132       C  
ATOM   4768  C   LEU B1076      81.117  13.239   1.547  1.00 95.39           C  
ANISOU 4768  C   LEU B1076     7430  17000  11815   -687   3946   -359       C  
ATOM   4769  O   LEU B1076      81.757  13.470   0.516  1.00 94.55           O  
ANISOU 4769  O   LEU B1076     7357  16750  11817   -707   4080   -328       O  
ATOM   4770  CB  LEU B1076      78.637  12.905   1.311  1.00 92.60           C  
ANISOU 4770  CB  LEU B1076     7215  16753  11216   -567   3840     75       C  
ATOM   4771  CG  LEU B1076      78.261  13.323  -0.110  1.00 91.93           C  
ANISOU 4771  CG  LEU B1076     7230  16520  11179   -534   3992    305       C  
ATOM   4772  CD1 LEU B1076      78.684  12.262  -1.108  1.00 91.14           C  
ANISOU 4772  CD1 LEU B1076     7196  16482  10953   -546   3880    400       C  
ATOM   4773  CD2 LEU B1076      76.762  13.563  -0.195  1.00 91.39           C  
ANISOU 4773  CD2 LEU B1076     7230  16462  11032   -459   3984    539       C  
ATOM   4774  N   LYS B1077      81.394  13.844   2.703  1.00 98.40           N  
ANISOU 4774  N   LYS B1077     7711  17393  12285   -714   3969   -595       N  
ATOM   4775  CA  LYS B1077      82.545  14.733   2.819  1.00 99.10           C  
ANISOU 4775  CA  LYS B1077     7721  17321  12609   -773   4131   -845       C  
ATOM   4776  C   LYS B1077      83.847  13.961   2.645  1.00 96.43           C  
ANISOU 4776  C   LYS B1077     7349  17032  12256   -828   4028   -983       C  
ATOM   4777  O   LYS B1077      84.753  14.402   1.922  1.00 93.79           O  
ANISOU 4777  O   LYS B1077     7018  16524  12095   -863   4174  -1047       O  
ATOM   4778  CB  LYS B1077      82.516  15.453   4.168  1.00100.82           C  
ANISOU 4778  CB  LYS B1077     7836  17574  12896   -794   4143  -1089       C  
ATOM   4779  CG  LYS B1077      83.669  16.420   4.383  1.00104.09           C  
ANISOU 4779  CG  LYS B1077     8167  17822  13561   -858   4295  -1375       C  
ATOM   4780  CD  LYS B1077      83.551  17.118   5.729  1.00108.53           C  
ANISOU 4780  CD  LYS B1077     8626  18438  14172   -884   4296  -1631       C  
ATOM   4781  CE  LYS B1077      84.689  18.101   5.946  1.00111.53           C  
ANISOU 4781  CE  LYS B1077     8923  18646  14808   -956   4439  -1936       C  
ATOM   4782  NZ  LYS B1077      84.570  18.807   7.252  1.00113.58           N  
ANISOU 4782  NZ  LYS B1077     9077  18967  15111   -990   4441  -2213       N  
ATOM   4783  N   LEU B1078      83.964  12.809   3.315  1.00 93.66           N  
ANISOU 4783  N   LEU B1078     6959  16917  11709   -831   3780  -1022       N  
ATOM   4784  CA  LEU B1078      85.138  11.960   3.128  1.00 88.67           C  
ANISOU 4784  CA  LEU B1078     6287  16342  11061   -875   3672  -1126       C  
ATOM   4785  C   LEU B1078      85.329  11.590   1.661  1.00 87.21           C  
ANISOU 4785  C   LEU B1078     6200  16040  10896   -874   3741   -949       C  
ATOM   4786  O   LEU B1078      86.460  11.561   1.163  1.00 95.59           O  
ANISOU 4786  O   LEU B1078     7239  17007  12071   -922   3797  -1064       O  
ATOM   4787  CB  LEU B1078      85.025  10.705   3.991  1.00 88.21           C  
ANISOU 4787  CB  LEU B1078     6174  16560  10783   -857   3399  -1118       C  
ATOM   4788  CG  LEU B1078      85.277  10.910   5.486  1.00 87.97           C  
ANISOU 4788  CG  LEU B1078     6014  16693  10716   -872   3306  -1348       C  
ATOM   4789  CD1 LEU B1078      84.964   9.643   6.266  1.00 87.11           C  
ANISOU 4789  CD1 LEU B1078     5859  16867  10372   -832   3046  -1261       C  
ATOM   4790  CD2 LEU B1078      86.711  11.356   5.732  1.00 89.32           C  
ANISOU 4790  CD2 LEU B1078     6085  16801  11051   -942   3363  -1646       C  
ATOM   4791  N   ALA B1079      84.233  11.302   0.954  1.00 86.26           N  
ANISOU 4791  N   ALA B1079     6186  15933  10657   -820   3733   -676       N  
ATOM   4792  CA  ALA B1079      84.328  10.981  -0.468  1.00 85.81           C  
ANISOU 4792  CA  ALA B1079     6222  15791  10593   -818   3798   -507       C  
ATOM   4793  C   ALA B1079      84.759  12.194  -1.284  1.00 87.11           C  
ANISOU 4793  C   ALA B1079     6411  15714  10972   -832   4075   -515       C  
ATOM   4794  O   ALA B1079      85.571  12.069  -2.209  1.00 87.72           O  
ANISOU 4794  O   ALA B1079     6513  15703  11114   -863   4151   -520       O  
ATOM   4795  CB  ALA B1079      82.991  10.441  -0.975  1.00 84.73           C  
ANISOU 4795  CB  ALA B1079     6186  15740  10267   -755   3713   -222       C  
ATOM   4796  N   ASN B1080      84.220  13.374  -0.964  1.00 89.33           N  
ANISOU 4796  N   ASN B1080     6682  15883  11377   -807   4237   -507       N  
ATOM   4797  CA  ASN B1080      84.582  14.582  -1.697  1.00 94.04           C  
ANISOU 4797  CA  ASN B1080     7288  16239  12203   -807   4516   -486       C  
ATOM   4798  C   ASN B1080      86.055  14.924  -1.524  1.00 98.01           C  
ANISOU 4798  C   ASN B1080     7715  16629  12894   -876   4579   -752       C  
ATOM   4799  O   ASN B1080      86.687  15.435  -2.455  1.00 91.50           O  
ANISOU 4799  O   ASN B1080     6917  15637  12212   -886   4753   -715       O  
ATOM   4800  CB  ASN B1080      83.712  15.756  -1.246  1.00 94.92           C  
ANISOU 4800  CB  ASN B1080     7380  16252  12433   -763   4669   -437       C  
ATOM   4801  CG  ASN B1080      82.343  15.747  -1.893  1.00 95.07           C  
ANISOU 4801  CG  ASN B1080     7491  16296  12335   -690   4700   -121       C  
ATOM   4802  OD1 ASN B1080      82.206  15.443  -3.078  1.00 89.70           O  
ANISOU 4802  OD1 ASN B1080     6898  15600  11582   -671   4735     81       O  
ATOM   4803  ND2 ASN B1080      81.319  16.083  -1.117  1.00 95.05           N  
ANISOU 4803  ND2 ASN B1080     7473  16337  12307   -652   4679    -90       N  
ATOM   4804  N   GLU B1081      86.620  14.654  -0.345  1.00 93.24           N  
ANISOU 4804  N   GLU B1081     7017  16125  12285   -921   4436  -1016       N  
ATOM   4805  CA  GLU B1081      88.050  14.873  -0.158  1.00 93.90           C  
ANISOU 4805  CA  GLU B1081     7026  16120  12530   -990   4466  -1283       C  
ATOM   4806  C   GLU B1081      88.904  13.862  -0.913  1.00 95.28           C  
ANISOU 4806  C   GLU B1081     7225  16334  12644  -1021   4382  -1272       C  
ATOM   4807  O   GLU B1081      90.115  14.075  -1.039  1.00100.02           O  
ANISOU 4807  O   GLU B1081     7781  16829  13396  -1075   4437  -1456       O  
ATOM   4808  CB  GLU B1081      88.404  14.836   1.330  1.00 92.15           C  
ANISOU 4808  CB  GLU B1081     6685  16032  12297  -1028   4325  -1569       C  
ATOM   4809  CG  GLU B1081      87.738  15.924   2.154  1.00 93.29           C  
ANISOU 4809  CG  GLU B1081     6789  16125  12532  -1014   4421  -1648       C  
ATOM   4810  CD  GLU B1081      87.922  15.719   3.643  1.00 93.67           C  
ANISOU 4810  CD  GLU B1081     6721  16373  12498  -1045   4250  -1908       C  
ATOM   4811  OE1 GLU B1081      88.941  15.116   4.038  1.00 94.42           O  
ANISOU 4811  OE1 GLU B1081     6741  16577  12558  -1093   4117  -2095       O  
ATOM   4812  OE2 GLU B1081      87.050  16.164   4.419  1.00 94.16           O  
ANISOU 4812  OE2 GLU B1081     6760  16493  12523  -1021   4250  -1921       O  
ATOM   4813  N   GLY B1082      88.312  12.780  -1.416  1.00 93.69           N  
ANISOU 4813  N   GLY B1082     7089  16275  12234   -990   4249  -1072       N  
ATOM   4814  CA  GLY B1082      89.035  11.766  -2.155  1.00 88.69           C  
ANISOU 4814  CA  GLY B1082     6475  15682  11541  -1019   4168  -1060       C  
ATOM   4815  C   GLY B1082      89.409  10.532  -1.363  1.00100.22           C  
ANISOU 4815  C   GLY B1082     7858  17348  12872  -1039   3912  -1175       C  
ATOM   4816  O   GLY B1082      89.949   9.585  -1.948  1.00 98.16           O  
ANISOU 4816  O   GLY B1082     7604  17125  12565  -1059   3834  -1158       O  
ATOM   4817  N   LYS B1083      89.139  10.510  -0.060  1.00 98.95           N  
ANISOU 4817  N   LYS B1083     7616  17326  12655  -1029   3785  -1283       N  
ATOM   4818  CA  LYS B1083      89.497   9.385   0.803  1.00108.98           C  
ANISOU 4818  CA  LYS B1083     8793  18811  13803  -1034   3544  -1372       C  
ATOM   4819  C   LYS B1083      88.448   8.291   0.633  1.00109.71           C  
ANISOU 4819  C   LYS B1083     8942  19063  13681   -981   3384  -1128       C  
ATOM   4820  O   LYS B1083      87.344   8.381   1.174  1.00119.29           O  
ANISOU 4820  O   LYS B1083    10177  20371  14777   -933   3329  -1016       O  
ATOM   4821  CB  LYS B1083      89.608   9.845   2.251  1.00109.58           C  
ANISOU 4821  CB  LYS B1083     8756  18995  13886  -1041   3479  -1574       C  
ATOM   4822  CG  LYS B1083      90.471  11.089   2.427  1.00112.92           C  
ANISOU 4822  CG  LYS B1083     9128  19241  14535  -1094   3654  -1820       C  
ATOM   4823  CD  LYS B1083      90.446  11.597   3.859  1.00114.44           C  
ANISOU 4823  CD  LYS B1083     9208  19558  14714  -1104   3592  -2032       C  
ATOM   4824  CE  LYS B1083      91.336  12.819   4.026  1.00116.97           C  
ANISOU 4824  CE  LYS B1083     9472  19696  15276  -1165   3763  -2300       C  
ATOM   4825  NZ  LYS B1083      91.203  13.425   5.381  1.00117.21           N  
ANISOU 4825  NZ  LYS B1083     9396  19845  15292  -1180   3722  -2521       N  
ATOM   4826  N   VAL B1084      88.794   7.247  -0.122  1.00116.14           N  
ANISOU 4826  N   VAL B1084     9559  16964  17604    649   4836    699       N  
ATOM   4827  CA  VAL B1084      87.814   6.229  -0.497  1.00 90.34           C  
ANISOU 4827  CA  VAL B1084     6514  13715  14095    735   4772    895       C  
ATOM   4828  C   VAL B1084      87.668   5.170   0.593  1.00106.14           C  
ANISOU 4828  C   VAL B1084     8376  16048  15905    724   4594    889       C  
ATOM   4829  O   VAL B1084      86.550   4.774   0.944  1.00109.78           O  
ANISOU 4829  O   VAL B1084     8911  16628  16171    741   4504    925       O  
ATOM   4830  CB  VAL B1084      88.197   5.603  -1.851  1.00 89.71           C  
ANISOU 4830  CB  VAL B1084     6682  13375  14028    831   4874   1124       C  
ATOM   4831  CG1 VAL B1084      87.194   4.532  -2.246  1.00 87.77           C  
ANISOU 4831  CG1 VAL B1084     6658  13161  13528    908   4811   1306       C  
ATOM   4832  CG2 VAL B1084      88.287   6.680  -2.926  1.00 90.38           C  
ANISOU 4832  CG2 VAL B1084     6907  13139  14296    857   5054   1147       C  
ATOM   4833  N   LYS B1085      88.790   4.682   1.129  1.00 90.97           N  
ANISOU 4833  N   LYS B1085     6255  14274  14037    703   4545    858       N  
ATOM   4834  CA  LYS B1085      88.746   3.627   2.141  1.00103.93           C  
ANISOU 4834  CA  LYS B1085     7767  16213  15511    714   4386    888       C  
ATOM   4835  C   LYS B1085      87.986   4.084   3.383  1.00107.13           C  
ANISOU 4835  C   LYS B1085     7984  16896  15824    639   4269    692       C  
ATOM   4836  O   LYS B1085      87.150   3.349   3.934  1.00114.55           O  
ANISOU 4836  O   LYS B1085     8974  17981  16568    675   4153    771       O  
ATOM   4837  CB  LYS B1085      90.172   3.206   2.505  1.00 92.44           C  
ANISOU 4837  CB  LYS B1085     6098  14870  14156    708   4366    878       C  
ATOM   4838  CG  LYS B1085      91.003   2.702   1.328  1.00 92.35           C  
ANISOU 4838  CG  LYS B1085     6259  14582  14246    780   4484   1069       C  
ATOM   4839  CD  LYS B1085      92.441   2.417   1.748  1.00 99.73           C  
ANISOU 4839  CD  LYS B1085     6954  15643  15297    768   4467   1039       C  
ATOM   4840  CE  LYS B1085      93.277   1.905   0.582  1.00 98.26           C  
ANISOU 4840  CE  LYS B1085     6943  15170  15222    840   4592   1230       C  
ATOM   4841  NZ  LYS B1085      94.683   1.611   0.982  1.00 98.69           N  
ANISOU 4841  NZ  LYS B1085     6760  15347  15391    835   4576   1212       N  
ATOM   4842  N   GLU B1086      88.276   5.302   3.843  1.00112.16           N  
ANISOU 4842  N   GLU B1086     8406  17608  16601    535   4302    438       N  
ATOM   4843  CA  GLU B1086      87.602   5.840   5.018  1.00116.14           C  
ANISOU 4843  CA  GLU B1086     8712  18377  17040    447   4209    213       C  
ATOM   4844  C   GLU B1086      86.110   6.003   4.757  1.00111.66           C  
ANISOU 4844  C   GLU B1086     8372  17703  16350    477   4213    276       C  
ATOM   4845  O   GLU B1086      85.279   5.725   5.634  1.00111.06           O  
ANISOU 4845  O   GLU B1086     8254  17801  16142    462   4102    231       O  
ATOM   4846  CB  GLU B1086      88.245   7.176   5.394  1.00123.33           C  
ANISOU 4846  CB  GLU B1086     9367  19392  18100    349   4257    -14       C  
ATOM   4847  CG  GLU B1086      89.747   7.075   5.647  1.00129.16           C  
ANISOU 4847  CG  GLU B1086     9863  20270  18944    325   4246    -59       C  
ATOM   4848  CD  GLU B1086      90.390   8.412   5.969  1.00134.98           C  
ANISOU 4848  CD  GLU B1086    10414  20971  19902    249   4314   -191       C  
ATOM   4849  OE1 GLU B1086      91.352   8.790   5.266  1.00137.61           O  
ANISOU 4849  OE1 GLU B1086    10774  21061  20452    228   4436   -220       O  
ATOM   4850  OE2 GLU B1086      89.930   9.092   6.909  1.00137.11           O  
ANISOU 4850  OE2 GLU B1086    10551  21341  20202    187   4266   -310       O  
ATOM   4851  N   ALA B1087      85.752   6.425   3.542  1.00108.32           N  
ANISOU 4851  N   ALA B1087     8208  16963  15985    531   4344    400       N  
ATOM   4852  CA  ALA B1087      84.346   6.536   3.171  1.00104.48           C  
ANISOU 4852  CA  ALA B1087     7947  16376  15376    573   4351    482       C  
ATOM   4853  C   ALA B1087      83.658   5.177   3.189  1.00 98.32           C  
ANISOU 4853  C   ALA B1087     7328  15674  14355    653   4239    681       C  
ATOM   4854  O   ALA B1087      82.495   5.069   3.589  1.00103.47           O  
ANISOU 4854  O   ALA B1087     8043  16420  14850    658   4162    685       O  
ATOM   4855  CB  ALA B1087      84.216   7.188   1.795  1.00 88.44           C  
ANISOU 4855  CB  ALA B1087     6155  13983  13464    630   4519    594       C  
ATOM   4856  N   GLN B1088      84.355   4.127   2.748  1.00 86.65           N  
ANISOU 4856  N   GLN B1088     5925  14150  12847    718   4233    857       N  
ATOM   4857  CA  GLN B1088      83.764   2.790   2.766  1.00 85.22           C  
ANISOU 4857  CA  GLN B1088     5897  14038  12444    794   4137   1055       C  
ATOM   4858  C   GLN B1088      83.535   2.298   4.196  1.00 96.52           C  
ANISOU 4858  C   GLN B1088     7147  15786  13740    775   3965   1002       C  
ATOM   4859  O   GLN B1088      82.502   1.675   4.493  1.00111.09           O  
ANISOU 4859  O   GLN B1088     9105  17723  15383    812   3870   1091       O  
ATOM   4860  CB  GLN B1088      84.649   1.828   1.974  1.00 85.20           C  
ANISOU 4860  CB  GLN B1088     6003  13898  12471    863   4193   1242       C  
ATOM   4861  CG  GLN B1088      84.660   2.137   0.478  1.00 84.72           C  
ANISOU 4861  CG  GLN B1088     6175  13525  12488    902   4348   1334       C  
ATOM   4862  CD  GLN B1088      85.735   1.386  -0.284  1.00 91.03           C  
ANISOU 4862  CD  GLN B1088     7046  14175  13367    952   4424   1476       C  
ATOM   4863  OE1 GLN B1088      86.850   1.204   0.205  1.00 91.83           O  
ANISOU 4863  OE1 GLN B1088     6963  14355  13575    937   4407   1448       O  
ATOM   4864  NE2 GLN B1088      85.406   0.956  -1.497  1.00 84.18           N  
ANISOU 4864  NE2 GLN B1088     6436  13104  12443   1012   4509   1623       N  
ATOM   4865  N   ALA B1089      84.483   2.565   5.097  1.00 92.71           N  
ANISOU 4865  N   ALA B1089     6383  15483  13359    720   3917    861       N  
ATOM   4866  CA  ALA B1089      84.257   2.226   6.504  1.00 97.04           C  
ANISOU 4866  CA  ALA B1089     6754  16353  13765    708   3738    811       C  
ATOM   4867  C   ALA B1089      83.052   2.986   7.060  1.00 97.43           C  
ANISOU 4867  C   ALA B1089     6802  16480  13739    651   3687    666       C  
ATOM   4868  O   ALA B1089      82.211   2.419   7.786  1.00100.51           O  
ANISOU 4868  O   ALA B1089     7229  17057  13905    682   3540    729       O  
ATOM   4869  CB  ALA B1089      85.511   2.523   7.326  1.00 90.17           C  
ANISOU 4869  CB  ALA B1089     5569  15665  13025    653   3697    664       C  
ATOM   4870  N   ALA B1090      82.952   4.275   6.722  1.00 95.00           N  
ANISOU 4870  N   ALA B1090     6453  16022  13620    569   3818    473       N  
ATOM   4871  CA  ALA B1090      81.780   5.056   7.098  1.00 93.63           C  
ANISOU 4871  CA  ALA B1090     6300  15869  13407    521   3806    348       C  
ATOM   4872  C   ALA B1090      80.505   4.425   6.553  1.00 87.30           C  
ANISOU 4872  C   ALA B1090     5784  15001  12386    604   3770    542       C  
ATOM   4873  O   ALA B1090      79.466   4.435   7.219  1.00 89.16           O  
ANISOU 4873  O   ALA B1090     6040  15373  12465    596   3663    513       O  
ATOM   4874  CB  ALA B1090      81.925   6.494   6.604  1.00 88.21           C  
ANISOU 4874  CB  ALA B1090     5549  14985  12980    435   3996    139       C  
ATOM   4875  N   ALA B1091      80.563   3.888   5.333  1.00 84.06           N  
ANISOU 4875  N   ALA B1091     5597  14380  11963    680   3856    734       N  
ATOM   4876  CA  ALA B1091      79.397   3.234   4.745  1.00 82.22           C  
ANISOU 4876  CA  ALA B1091     5628  14079  11531    752   3831    908       C  
ATOM   4877  C   ALA B1091      79.001   1.983   5.522  1.00100.97           C  
ANISOU 4877  C   ALA B1091     8019  16667  13678    795   3665   1024       C  
ATOM   4878  O   ALA B1091      77.814   1.664   5.632  1.00104.30           O  
ANISOU 4878  O   ALA B1091     8569  17139  13921    817   3597   1075       O  
ATOM   4879  CB  ALA B1091      79.671   2.890   3.282  1.00 81.60           C  
ANISOU 4879  CB  ALA B1091     5769  13741  11493    817   3958   1074       C  
ATOM   4880  N   GLU B1092      79.979   1.248   6.053  1.00 94.61           N  
ANISOU 4880  N   GLU B1092     7084  15987  12875    815   3605   1078       N  
ATOM   4881  CA  GLU B1092      79.648   0.093   6.895  1.00101.95           C  
ANISOU 4881  CA  GLU B1092     8010  17131  13594    867   3455   1200       C  
ATOM   4882  C   GLU B1092      78.901   0.535   8.157  1.00100.78           C  
ANISOU 4882  C   GLU B1092     7734  17241  13318    821   3306   1062       C  
ATOM   4883  O   GLU B1092      77.868  -0.052   8.548  1.00105.95           O  
ANISOU 4883  O   GLU B1092     8489  17996  13773    853   3212   1136       O  
ATOM   4884  CB  GLU B1092      80.923  -0.671   7.255  1.00115.53           C  
ANISOU 4884  CB  GLU B1092     9592  18947  15356    910   3429   1293       C  
ATOM   4885  CG  GLU B1092      80.691  -1.956   8.033  1.00123.98           C  
ANISOU 4885  CG  GLU B1092    10667  20211  16229    989   3307   1466       C  
ATOM   4886  CD  GLU B1092      80.028  -3.034   7.195  1.00127.59           C  
ANISOU 4886  CD  GLU B1092    11390  20482  16605   1055   3375   1660       C  
ATOM   4887  OE1 GLU B1092      80.141  -2.976   5.952  1.00128.01           O  
ANISOU 4887  OE1 GLU B1092    11604  20271  16761   1052   3513   1691       O  
ATOM   4888  OE2 GLU B1092      79.396  -3.939   7.779  1.00128.49           O  
ANISOU 4888  OE2 GLU B1092    11548  20716  16554   1106   3295   1774       O  
ATOM   4889  N   GLN B1093      79.411   1.586   8.805  1.00 95.35           N  
ANISOU 4889  N   GLN B1093     6821  16658  12749    737   3290    845       N  
ATOM   4890  CA  GLN B1093      78.702   2.131   9.962  1.00 91.55           C  
ANISOU 4890  CA  GLN B1093     6223  16409  12153    677   3157    681       C  
ATOM   4891  C   GLN B1093      77.293   2.572   9.564  1.00 84.54           C  
ANISOU 4891  C   GLN B1093     5517  15399  11204    665   3191    659       C  
ATOM   4892  O   GLN B1093      76.317   2.360  10.307  1.00 85.49           O  
ANISOU 4892  O   GLN B1093     5664  15688  11130    666   3064    651       O  
ATOM   4893  CB  GLN B1093      79.487   3.306  10.549  1.00 97.35           C  
ANISOU 4893  CB  GLN B1093     6699  17222  13067    569   3172    418       C  
ATOM   4894  CG  GLN B1093      80.924   2.984  10.961  1.00100.39           C  
ANISOU 4894  CG  GLN B1093     6875  17749  13518    572   3133    415       C  
ATOM   4895  CD  GLN B1093      81.020   1.933  12.052  1.00101.16           C  
ANISOU 4895  CD  GLN B1093     6890  18188  13359    637   2932    531       C  
ATOM   4896  OE1 GLN B1093      80.130   1.807  12.893  1.00104.27           O  
ANISOU 4896  OE1 GLN B1093     7290  18786  13541    636   2797    507       O  
ATOM   4897  NE2 GLN B1093      82.112   1.175  12.045  1.00 98.74           N  
ANISOU 4897  NE2 GLN B1093     6500  17945  13071    703   2922    667       N  
ATOM   4898  N   LEU B1094      77.180   3.187   8.384  1.00 84.90           N  
ANISOU 4898  N   LEU B1094     5689  15160  11410    662   3364    660       N  
ATOM   4899  CA  LEU B1094      75.885   3.573   7.839  1.00 87.73           C  
ANISOU 4899  CA  LEU B1094     6232  15392  11710    671   3409    674       C  
ATOM   4900  C   LEU B1094      74.976   2.367   7.669  1.00 93.33           C  
ANISOU 4900  C   LEU B1094     7142  16141  12179    746   3323    867       C  
ATOM   4901  O   LEU B1094      73.762   2.469   7.854  1.00 96.10           O  
ANISOU 4901  O   LEU B1094     7582  16535  12397    744   3268    854       O  
ATOM   4902  CB  LEU B1094      76.082   4.269   6.494  1.00 80.70           C  
ANISOU 4902  CB  LEU B1094     5452  14201  11010    682   3611    692       C  
ATOM   4903  CG  LEU B1094      76.353   5.767   6.530  1.00 82.00           C  
ANISOU 4903  CG  LEU B1094     5472  14264  11422    602   3743    480       C  
ATOM   4904  CD1 LEU B1094      76.588   6.301   5.128  1.00 81.95           C  
ANISOU 4904  CD1 LEU B1094     5603  13967  11567    638   3933    548       C  
ATOM   4905  CD2 LEU B1094      75.178   6.451   7.176  1.00 81.81           C  
ANISOU 4905  CD2 LEU B1094     5431  14316  11336    562   3700    363       C  
ATOM   4906  N   LYS B1095      75.546   1.221   7.296  1.00 93.81           N  
ANISOU 4906  N   LYS B1095     7272  16172  12198    809   3325   1040       N  
ATOM   4907  CA  LYS B1095      74.757   0.000   7.154  1.00 89.87           C  
ANISOU 4907  CA  LYS B1095     6949  15692  11504    870   3269   1208       C  
ATOM   4908  C   LYS B1095      74.080  -0.352   8.468  1.00 84.62           C  
ANISOU 4908  C   LYS B1095     6206  15291  10656    866   3101   1183       C  
ATOM   4909  O   LYS B1095      72.873  -0.636   8.513  1.00 76.80           O  
ANISOU 4909  O   LYS B1095     5342  14322   9516    876   3053   1212       O  
ATOM   4910  CB  LYS B1095      75.644  -1.154   6.686  1.00 91.55           C  
ANISOU 4910  CB  LYS B1095     7213  15829  11744    931   3318   1379       C  
ATOM   4911  CG  LYS B1095      74.875  -2.385   6.233  1.00 92.60           C  
ANISOU 4911  CG  LYS B1095     7551  15899  11735    982   3324   1536       C  
ATOM   4912  CD  LYS B1095      75.816  -3.475   5.744  1.00 92.45           C  
ANISOU 4912  CD  LYS B1095     7574  15773  11778   1034   3402   1690       C  
ATOM   4913  CE  LYS B1095      76.804  -2.940   4.720  1.00 93.76           C  
ANISOU 4913  CE  LYS B1095     7753  15741  12129   1025   3535   1674       C  
ATOM   4914  NZ  LYS B1095      77.842  -3.950   4.374  1.00 95.95           N  
ANISOU 4914  NZ  LYS B1095     8045  15930  12484   1074   3605   1815       N  
ATOM   4915  N   THR B1096      74.858  -0.349   9.552  1.00 80.62           N  
ANISOU 4915  N   THR B1096     5484  15000  10147    853   3007   1128       N  
ATOM   4916  CA  THR B1096      74.265  -0.650  10.859  1.00 79.81           C  
ANISOU 4916  CA  THR B1096     5297  15178   9851    855   2842   1105       C  
ATOM   4917  C   THR B1096      73.154   0.346  11.208  1.00 81.60           C  
ANISOU 4917  C   THR B1096     5530  15446  10030    785   2799    931       C  
ATOM   4918  O   THR B1096      72.028  -0.046  11.578  1.00 86.48           O  
ANISOU 4918  O   THR B1096     6241  16141  10475    802   2721    969       O  
ATOM   4919  CB  THR B1096      75.344  -0.650  11.943  1.00 89.29           C  
ANISOU 4919  CB  THR B1096     6245  16635  11046    849   2744   1054       C  
ATOM   4920  OG1 THR B1096      76.295  -1.689  11.679  1.00107.24           O  
ANISOU 4920  OG1 THR B1096     8517  18880  13351    932   2781   1249       O  
ATOM   4921  CG2 THR B1096      74.722  -0.874  13.316  1.00 82.06           C  
ANISOU 4921  CG2 THR B1096     5237  16034   9907    854   2570   1024       C  
ATOM   4922  N   THR B1097      73.451   1.645  11.077  1.00 83.35           N  
ANISOU 4922  N   THR B1097     5653  15597  10421    707   2866    737       N  
ATOM   4923  CA  THR B1097      72.457   2.666  11.416  1.00 86.94           C  
ANISOU 4923  CA  THR B1097     6101  16068  10864    639   2850    565       C  
ATOM   4924  C   THR B1097      71.192   2.519  10.570  1.00 84.97           C  
ANISOU 4924  C   THR B1097     6089  15653  10544    679   2901    667       C  
ATOM   4925  O   THR B1097      70.068   2.692  11.070  1.00 77.23           O  
ANISOU 4925  O   THR B1097     5148  14760   9437    661   2826    615       O  
ATOM   4926  CB  THR B1097      73.061   4.061  11.247  1.00 90.03           C  
ANISOU 4926  CB  THR B1097     6356  16346  11505    554   2968    357       C  
ATOM   4927  OG1 THR B1097      74.171   4.211  12.141  1.00 96.75           O  
ANISOU 4927  OG1 THR B1097     6969  17390  12402    502   2900    229       O  
ATOM   4928  CG2 THR B1097      72.031   5.138  11.556  1.00 86.61           C  
ANISOU 4928  CG2 THR B1097     5921  15896  11092    489   2983    186       C  
ATOM   4929  N   ILE B1098      71.359   2.174   9.290  1.00 84.21           N  
ANISOU 4929  N   ILE B1098     6150  15330  10515    731   3024    807       N  
ATOM   4930  CA  ILE B1098      70.234   2.060   8.372  1.00 83.57           C  
ANISOU 4930  CA  ILE B1098     6288  15105  10362    767   3074    896       C  
ATOM   4931  C   ILE B1098      69.354   0.885   8.756  1.00 77.80           C  
ANISOU 4931  C   ILE B1098     5662  14493   9406    803   2958   1005       C  
ATOM   4932  O   ILE B1098      68.123   0.992   8.752  1.00 73.80           O  
ANISOU 4932  O   ILE B1098     5251  14000   8787    800   2921    991       O  
ATOM   4933  CB  ILE B1098      70.738   1.932   6.921  1.00 75.30           C  
ANISOU 4933  CB  ILE B1098     5373  13815   9423    811   3226   1010       C  
ATOM   4934  CG1 ILE B1098      71.135   3.295   6.359  1.00 76.06           C  
ANISOU 4934  CG1 ILE B1098     5415  13747   9736    784   3370    909       C  
ATOM   4935  CG2 ILE B1098      69.686   1.280   6.034  1.00 74.00           C  
ANISOU 4935  CG2 ILE B1098     5437  13567   9113    858   3238   1133       C  
ATOM   4936  CD1 ILE B1098      72.033   3.212   5.146  1.00 76.26           C  
ANISOU 4936  CD1 ILE B1098     5518  13564   9894    823   3513   1005       C  
ATOM   4937  N   ASN B1099      69.963  -0.261   9.071  1.00 78.37           N  
ANISOU 4937  N   ASN B1099     5714  14639   9422    842   2915   1120       N  
ATOM   4938  CA  ASN B1099      69.169  -1.396   9.530  1.00 83.30           C  
ANISOU 4938  CA  ASN B1099     6422  15365   9863    878   2829   1223       C  
ATOM   4939  C   ASN B1099      68.306  -1.002  10.722  1.00 79.58           C  
ANISOU 4939  C   ASN B1099     5869  15104   9263    845   2696   1117       C  
ATOM   4940  O   ASN B1099      67.091  -1.259  10.742  1.00 73.65           O  
ANISOU 4940  O   ASN B1099     5232  14362   8388    847   2657   1131       O  
ATOM   4941  CB  ASN B1099      70.078  -2.573   9.889  1.00 89.22           C  
ANISOU 4941  CB  ASN B1099     7120  16175  10603    933   2818   1366       C  
ATOM   4942  CG  ASN B1099      70.587  -3.310   8.668  1.00 90.07           C  
ANISOU 4942  CG  ASN B1099     7365  16058  10800    970   2954   1494       C  
ATOM   4943  OD1 ASN B1099      70.017  -3.203   7.582  1.00 94.56           O  
ANISOU 4943  OD1 ASN B1099     8097  16454  11379    958   3036   1493       O  
ATOM   4944  ND2 ASN B1099      71.663  -4.068   8.840  1.00 88.47           N  
ANISOU 4944  ND2 ASN B1099     7092  15867  10654   1016   2978   1605       N  
ATOM   4945  N   ALA B1100      68.913  -0.329  11.707  1.00 83.41           N  
ANISOU 4945  N   ALA B1100     6151  15762   9777    805   2626    989       N  
ATOM   4946  CA  ALA B1100      68.152   0.054  12.898  1.00 86.50           C  
ANISOU 4946  CA  ALA B1100     6457  16372  10038    766   2497    870       C  
ATOM   4947  C   ALA B1100      66.968   0.958  12.547  1.00 87.73           C  
ANISOU 4947  C   ALA B1100     6705  16428  10202    721   2526    762       C  
ATOM   4948  O   ALA B1100      65.812   0.669  12.905  1.00 85.53           O  
ANISOU 4948  O   ALA B1100     6506  16215   9776    728   2457    777       O  
ATOM   4949  CB  ALA B1100      69.072   0.740  13.909  1.00 88.36           C  
ANISOU 4949  CB  ALA B1100     6451  16809  10314    713   2430    711       C  
ATOM   4950  N   TYR B1101      67.236   2.049  11.822  1.00 90.17           N  
ANISOU 4950  N   TYR B1101     7003  16565  10691    684   2643    666       N  
ATOM   4951  CA  TYR B1101      66.182   3.027  11.554  1.00 93.19           C  
ANISOU 4951  CA  TYR B1101     7446  16858  11103    653   2686    571       C  
ATOM   4952  C   TYR B1101      65.089   2.451  10.656  1.00 87.04           C  
ANISOU 4952  C   TYR B1101     6885  15966  10219    708   2708    713       C  
ATOM   4953  O   TYR B1101      63.894   2.724  10.862  1.00 83.98           O  
ANISOU 4953  O   TYR B1101     6555  15612   9742    699   2666    675       O  
ATOM   4954  CB  TYR B1101      66.788   4.285  10.932  1.00107.29           C  
ANISOU 4954  CB  TYR B1101     9167  18465  13134    618   2840    465       C  
ATOM   4955  CG  TYR B1101      65.772   5.278  10.410  1.00115.55           C  
ANISOU 4955  CG  TYR B1101    10291  19369  14243    614   2932    420       C  
ATOM   4956  CD1 TYR B1101      64.809   5.826  11.248  1.00120.59           C  
ANISOU 4956  CD1 TYR B1101    10887  20110  14820    569   2867    295       C  
ATOM   4957  CD2 TYR B1101      65.786   5.678   9.080  1.00114.71           C  
ANISOU 4957  CD2 TYR B1101    10296  19031  14257    664   3089    513       C  
ATOM   4958  CE1 TYR B1101      63.881   6.736  10.772  1.00119.26           C  
ANISOU 4958  CE1 TYR B1101    10783  19809  14723    578   2964    272       C  
ATOM   4959  CE2 TYR B1101      64.865   6.588   8.596  1.00113.21           C  
ANISOU 4959  CE2 TYR B1101    10170  18724  14123    682   3180    501       C  
ATOM   4960  CZ  TYR B1101      63.915   7.113   9.446  1.00113.92           C  
ANISOU 4960  CZ  TYR B1101    10211  18909  14164    640   3121    385       C  
ATOM   4961  OH  TYR B1101      62.996   8.019   8.968  1.00110.09           O  
ANISOU 4961  OH  TYR B1101     9782  18302  13746    668   3223    390       O  
ATOM   4962  N   ILE B1102      65.475   1.650   9.659  1.00 91.64           N  
ANISOU 4962  N   ILE B1102     7588  16422  10811    761   2774    864       N  
ATOM   4963  CA  ILE B1102      64.496   1.045   8.764  1.00 80.94           C  
ANISOU 4963  CA  ILE B1102     6429  14976   9349    800   2795    973       C  
ATOM   4964  C   ILE B1102      63.578   0.105   9.528  1.00 73.60           C  
ANISOU 4964  C   ILE B1102     5541  14192   8232    802   2674   1005       C  
ATOM   4965  O   ILE B1102      62.356   0.121   9.330  1.00 70.19           O  
ANISOU 4965  O   ILE B1102     5209  13760   7702    802   2648   1001       O  
ATOM   4966  CB  ILE B1102      65.202   0.323   7.601  1.00 71.34           C  
ANISOU 4966  CB  ILE B1102     5319  13606   8183    841   2896   1101       C  
ATOM   4967  CG1 ILE B1102      65.760   1.339   6.602  1.00 71.77           C  
ANISOU 4967  CG1 ILE B1102     5378  13488   8404    851   3033   1086       C  
ATOM   4968  CG2 ILE B1102      64.245  -0.635   6.914  1.00 70.43           C  
ANISOU 4968  CG2 ILE B1102     5382  13452   7926    864   2893   1189       C  
ATOM   4969  CD1 ILE B1102      64.725   2.308   6.071  1.00 71.53           C  
ANISOU 4969  CD1 ILE B1102     5414  13398   8366    861   3075   1054       C  
ATOM   4970  N   GLN B1103      64.139  -0.736  10.406  1.00 86.06           N  
ANISOU 4970  N   GLN B1103     7040  15899   9762    812   2605   1049       N  
ATOM   4971  CA  GLN B1103      63.267  -1.622  11.170  1.00 95.48           C  
ANISOU 4971  CA  GLN B1103     8268  17219  10792    824   2510   1092       C  
ATOM   4972  C   GLN B1103      62.313  -0.830  12.054  1.00 92.03           C  
ANISOU 4972  C   GLN B1103     7773  16918  10276    784   2416    964       C  
ATOM   4973  O   GLN B1103      61.130  -1.179  12.166  1.00 85.62           O  
ANISOU 4973  O   GLN B1103     7052  16131   9350    784   2372    976       O  
ATOM   4974  CB  GLN B1103      64.074  -2.607  12.013  1.00105.20           C  
ANISOU 4974  CB  GLN B1103     9407  18574  11989    862   2466   1188       C  
ATOM   4975  CG  GLN B1103      63.172  -3.604  12.738  1.00111.83           C  
ANISOU 4975  CG  GLN B1103    10294  19517  12680    889   2399   1261       C  
ATOM   4976  CD  GLN B1103      63.888  -4.866  13.173  1.00117.10           C  
ANISOU 4976  CD  GLN B1103    10927  20230  13337    956   2413   1424       C  
ATOM   4977  OE1 GLN B1103      65.115  -4.907  13.244  1.00121.56           O  
ANISOU 4977  OE1 GLN B1103    11391  20819  13978    984   2434   1470       O  
ATOM   4978  NE2 GLN B1103      63.117  -5.909  13.465  1.00116.12           N  
ANISOU 4978  NE2 GLN B1103    10880  20109  13131    987   2415   1516       N  
ATOM   4979  N   LYS B1104      62.796   0.251  12.676  1.00 95.24           N  
ANISOU 4979  N   LYS B1104     8027  17406  10754    741   2393    825       N  
ATOM   4980  CA  LYS B1104      61.907   1.035  13.533  1.00 96.79           C  
ANISOU 4980  CA  LYS B1104     8165  17722  10888    693   2318    683       C  
ATOM   4981  C   LYS B1104      60.736   1.620  12.743  1.00 96.81           C  
ANISOU 4981  C   LYS B1104     8296  17586  10901    689   2371    665       C  
ATOM   4982  O   LYS B1104      59.568   1.491  13.145  1.00 96.66           O  
ANISOU 4982  O   LYS B1104     8329  17635  10763    684   2304    651       O  
ATOM   4983  CB  LYS B1104      62.695   2.147  14.229  1.00 97.91           C  
ANISOU 4983  CB  LYS B1104     8115  17949  11137    630   2314    503       C  
ATOM   4984  CG  LYS B1104      61.892   2.916  15.268  1.00 97.19           C  
ANISOU 4984  CG  LYS B1104     7943  18001  10984    569   2239    332       C  
ATOM   4985  CD  LYS B1104      62.599   4.199  15.678  1.00 97.20           C  
ANISOU 4985  CD  LYS B1104     7771  18018  11145    486   2283    114       C  
ATOM   4986  CE  LYS B1104      63.997   3.918  16.200  1.00 95.64           C  
ANISOU 4986  CE  LYS B1104     7414  17962  10964    474   2241     88       C  
ATOM   4987  NZ  LYS B1104      64.711   5.174  16.558  1.00 94.97           N  
ANISOU 4987  NZ  LYS B1104     7150  17881  11053    376   2295   -155       N  
ATOM   4988  N   TYR B1105      61.024   2.238  11.593  1.00 94.93           N  
ANISOU 4988  N   TYR B1105     8109  17159  10801    701   2495    680       N  
ATOM   4989  CA  TYR B1105      59.946   2.857  10.820  1.00 93.57           C  
ANISOU 4989  CA  TYR B1105     8043  16878  10633    716   2549    684       C  
ATOM   4990  C   TYR B1105      58.992   1.812  10.243  1.00 85.28           C  
ANISOU 4990  C   TYR B1105     7156  15819   9427    752   2513    801       C  
ATOM   4991  O   TYR B1105      57.767   2.016  10.233  1.00 87.79           O  
ANISOU 4991  O   TYR B1105     7534  16162   9662    753   2479    784       O  
ATOM   4992  CB  TYR B1105      60.523   3.739   9.714  1.00104.05           C  
ANISOU 4992  CB  TYR B1105     9381  18014  12139    738   2702    699       C  
ATOM   4993  CG  TYR B1105      59.543   4.774   9.204  1.00116.01           C  
ANISOU 4993  CG  TYR B1105    10940  19441  13696    758   2773    682       C  
ATOM   4994  CD1 TYR B1105      59.236   5.900   9.958  1.00122.00           C  
ANISOU 4994  CD1 TYR B1105    11587  20218  14551    714   2794    539       C  
ATOM   4995  CD2 TYR B1105      58.923   4.625   7.971  1.00121.12           C  
ANISOU 4995  CD2 TYR B1105    11734  19998  14288    823   2824    807       C  
ATOM   4996  CE1 TYR B1105      58.339   6.848   9.496  1.00126.45           C  
ANISOU 4996  CE1 TYR B1105    12185  20687  15173    746   2879    545       C  
ATOM   4997  CE2 TYR B1105      58.027   5.567   7.501  1.00125.93           C  
ANISOU 4997  CE2 TYR B1105    12374  20546  14928    861   2888    820       C  
ATOM   4998  CZ  TYR B1105      57.738   6.676   8.267  1.00129.14           C  
ANISOU 4998  CZ  TYR B1105    12670  20949  15449    828   2922    700       C  
ATOM   4999  OH  TYR B1105      56.846   7.614   7.800  1.00133.05           O  
ANISOU 4999  OH  TYR B1105    13191  21368  15993    878   3006    733       O  
ATOM   5000  N   GLY B1106      59.530   0.694   9.747  1.00 80.24           N  
ANISOU 5000  N   GLY B1106     6586  15140   8760    778   2531    909       N  
ATOM   5001  CA  GLY B1106      58.672  -0.367   9.246  1.00 78.30           C  
ANISOU 5001  CA  GLY B1106     6480  14882   8387    792   2513    985       C  
ATOM   5002  C   GLY B1106      57.761  -0.935  10.316  1.00 77.39           C  
ANISOU 5002  C   GLY B1106     6355  14907   8143    773   2403    961       C  
ATOM   5003  O   GLY B1106      56.591  -1.232  10.055  1.00 75.16           O  
ANISOU 5003  O   GLY B1106     6163  14630   7764    768   2378    961       O  
ATOM   5004  N   GLN B 313      58.279  -1.088  11.538  1.00 80.38           N  
ANISOU 5004  N   GLN B 313     6616  15413   8512    764   2337    938       N  
ATOM   5005  CA  GLN B 313      57.439  -1.554  12.634  1.00 81.87           C  
ANISOU 5005  CA  GLN B 313     6786  15747   8576    755   2237    922       C  
ATOM   5006  C   GLN B 313      56.344  -0.546  12.952  1.00 74.71           C  
ANISOU 5006  C   GLN B 313     5867  14888   7631    723   2189    811       C  
ATOM   5007  O   GLN B 313      55.211  -0.930  13.266  1.00 67.77           O  
ANISOU 5007  O   GLN B 313     5043  14059   6647    717   2136    808       O  
ATOM   5008  CB  GLN B 313      58.290  -1.835  13.872  1.00 90.23           C  
ANISOU 5008  CB  GLN B 313     7704  16966   9614    764   2174    930       C  
ATOM   5009  CG  GLN B 313      57.503  -2.397  15.049  1.00 93.53           C  
ANISOU 5009  CG  GLN B 313     8097  17546   9892    770   2079    939       C  
ATOM   5010  CD  GLN B 313      56.845  -3.731  14.736  1.00 94.61           C  
ANISOU 5010  CD  GLN B 313     8362  17608   9978    799   2113   1057       C  
ATOM   5011  OE1 GLN B 313      57.290  -4.468  13.855  1.00 98.78           O  
ANISOU 5011  OE1 GLN B 313     8968  17994  10570    818   2204   1145       O  
ATOM   5012  NE2 GLN B 313      55.777  -4.045  15.459  1.00 91.80           N  
ANISOU 5012  NE2 GLN B 313     8024  17338   9519    795   2053   1047       N  
ATOM   5013  N   SER B 314      56.660   0.750  12.880  1.00 80.22           N  
ANISOU 5013  N   SER B 314     6490  15558   8433    703   2224    715       N  
ATOM   5014  CA  SER B 314      55.625   1.763  13.091  1.00 74.78           C  
ANISOU 5014  CA  SER B 314     5792  14882   7740    679   2210    617       C  
ATOM   5015  C   SER B 314      54.508   1.632  12.058  1.00 67.80           C  
ANISOU 5015  C   SER B 314     5048  13909   6804    707   2238    681       C  
ATOM   5016  O   SER B 314      53.314   1.668  12.399  1.00 67.46           O  
ANISOU 5016  O   SER B 314     5034  13924   6672    698   2181    652       O  
ATOM   5017  CB  SER B 314      56.241   3.161  13.042  1.00 86.87           C  
ANISOU 5017  CB  SER B 314     7218  16350   9440    654   2290    510       C  
ATOM   5018  OG  SER B 314      57.216   3.326  14.057  1.00 95.75           O  
ANISOU 5018  OG  SER B 314     8191  17589  10601    612   2252    413       O  
ATOM   5019  N   ILE B 315      54.879   1.463  10.786  1.00 76.05           N  
ANISOU 5019  N   ILE B 315     6174  14828   7893    742   2322    766       N  
ATOM   5020  CA  ILE B 315      53.868   1.325   9.737  1.00 73.82           C  
ANISOU 5020  CA  ILE B 315     6012  14498   7539    770   2341    820       C  
ATOM   5021  C   ILE B 315      53.043   0.058   9.943  1.00 70.20           C  
ANISOU 5021  C   ILE B 315     5627  14108   6939    752   2269    841       C  
ATOM   5022  O   ILE B 315      51.816   0.060   9.765  1.00 72.02           O  
ANISOU 5022  O   ILE B 315     5907  14378   7081    750   2232    826       O  
ATOM   5023  CB  ILE B 315      54.524   1.353   8.344  1.00 71.20           C  
ANISOU 5023  CB  ILE B 315     5745  14041   7267    811   2446    901       C  
ATOM   5024  CG1 ILE B 315      55.308   2.652   8.145  1.00 73.58           C  
ANISOU 5024  CG1 ILE B 315     5969  14252   7737    832   2542    884       C  
ATOM   5025  CG2 ILE B 315      53.471   1.196   7.253  1.00 67.20           C  
ANISOU 5025  CG2 ILE B 315     5345  13533   6655    841   2454    949       C  
ATOM   5026  CD1 ILE B 315      55.923   2.788   6.771  1.00 74.57           C  
ANISOU 5026  CD1 ILE B 315     6158  14251   7924    884   2655    975       C  
ATOM   5027  N   SER B 316      53.696  -1.041  10.327  1.00 66.65           N  
ANISOU 5027  N   SER B 316     5177  13667   6478    741   2261    879       N  
ATOM   5028  CA  SER B 316      52.970  -2.288  10.557  1.00 66.35           C  
ANISOU 5028  CA  SER B 316     5202  13663   6344    723   2228    900       C  
ATOM   5029  C   SER B 316      52.011  -2.169  11.736  1.00 67.98           C  
ANISOU 5029  C   SER B 316     5365  13990   6474    704   2134    844       C  
ATOM   5030  O   SER B 316      50.912  -2.737  11.708  1.00 65.93           O  
ANISOU 5030  O   SER B 316     5164  13751   6135    686   2109    833       O  
ATOM   5031  CB  SER B 316      53.955  -3.434  10.781  1.00 73.54           C  
ANISOU 5031  CB  SER B 316     6110  14540   7293    730   2269    973       C  
ATOM   5032  OG  SER B 316      53.273  -4.658  10.988  1.00 73.76           O  
ANISOU 5032  OG  SER B 316     6196  14568   7262    714   2275    996       O  
ATOM   5033  N   ASN B 317      52.401  -1.431  12.777  1.00 68.71           N  
ANISOU 5033  N   ASN B 317     5347  14168   6591    700   2086    795       N  
ATOM   5034  CA  ASN B 317      51.505  -1.226  13.911  1.00 66.54           C  
ANISOU 5034  CA  ASN B 317     5028  14016   6240    680   2000    732       C  
ATOM   5035  C   ASN B 317      50.297  -0.388  13.514  1.00 75.49           C  
ANISOU 5035  C   ASN B 317     6196  15135   7352    671   1991    674       C  
ATOM   5036  O   ASN B 317      49.169  -0.668  13.946  1.00 65.96           O  
ANISOU 5036  O   ASN B 317     5013  13986   6061    657   1937    651       O  
ATOM   5037  CB  ASN B 317      52.255  -0.567  15.066  1.00 67.93           C  
ANISOU 5037  CB  ASN B 317     5064  14307   6439    669   1956    665       C  
ATOM   5038  CG  ASN B 317      53.321  -1.467  15.655  1.00 72.47           C  
ANISOU 5038  CG  ASN B 317     5585  14950   7003    692   1945    740       C  
ATOM   5039  OD1 ASN B 317      53.309  -2.682  15.447  1.00 74.32           O  
ANISOU 5039  OD1 ASN B 317     5886  15142   7208    719   1971    848       O  
ATOM   5040  ND2 ASN B 317      54.253  -0.876  16.392  1.00 75.87           N  
ANISOU 5040  ND2 ASN B 317     5880  15485   7461    682   1917    680       N  
ATOM   5041  N   GLU B 318      50.513   0.649  12.699  1.00 70.88           N  
ANISOU 5041  N   GLU B 318     5608  14472   6852    687   2052    661       N  
ATOM   5042  CA  GLU B 318      49.377   1.420  12.203  1.00 74.08           C  
ANISOU 5042  CA  GLU B 318     6043  14863   7242    701   2060    642       C  
ATOM   5043  C   GLU B 318      48.449   0.548  11.363  1.00 69.74           C  
ANISOU 5043  C   GLU B 318     5598  14313   6588    709   2045    692       C  
ATOM   5044  O   GLU B 318      47.221   0.661  11.459  1.00 68.51           O  
ANISOU 5044  O   GLU B 318     5458  14212   6361    704   2001    666       O  
ATOM   5045  CB  GLU B 318      49.861   2.629  11.403  1.00 84.33           C  
ANISOU 5045  CB  GLU B 318     7316  16061   8665    737   2158    653       C  
ATOM   5046  CG  GLU B 318      50.555   3.695  12.243  1.00 91.53           C  
ANISOU 5046  CG  GLU B 318     8105  16964   9708    712   2192    558       C  
ATOM   5047  CD  GLU B 318      49.678   4.245  13.358  1.00 94.65           C  
ANISOU 5047  CD  GLU B 318     8438  17445  10080    676   2139    453       C  
ATOM   5048  OE1 GLU B 318      48.437   4.241  13.210  1.00 95.25           O  
ANISOU 5048  OE1 GLU B 318     8565  17546  10080    692   2109    472       O  
ATOM   5049  OE2 GLU B 318      50.234   4.684  14.386  1.00 96.70           O  
ANISOU 5049  OE2 GLU B 318     8589  17758  10393    628   2128    341       O  
ATOM   5050  N   GLN B 319      49.020  -0.354  10.559  1.00 65.78           N  
ANISOU 5050  N   GLN B 319     5160  13755   6079    712   2087    749       N  
ATOM   5051  CA  GLN B 319      48.203  -1.269   9.765  1.00 65.64           C  
ANISOU 5051  CA  GLN B 319     5228  13744   5968    698   2086    761       C  
ATOM   5052  C   GLN B 319      47.390  -2.206  10.655  1.00 67.93           C  
ANISOU 5052  C   GLN B 319     5525  14094   6190    655   2030    723       C  
ATOM   5053  O   GLN B 319      46.210  -2.468  10.386  1.00 78.08           O  
ANISOU 5053  O   GLN B 319     6842  15427   7398    636   2002    688       O  
ATOM   5054  CB  GLN B 319      49.098  -2.065   8.814  1.00 75.00           C  
ANISOU 5054  CB  GLN B 319     6471  14845   7179    698   2164    808       C  
ATOM   5055  CG  GLN B 319      48.387  -3.143   8.016  1.00 79.31           C  
ANISOU 5055  CG  GLN B 319     7093  15398   7642    662   2185    785       C  
ATOM   5056  CD  GLN B 319      49.355  -4.016   7.240  1.00 79.43           C  
ANISOU 5056  CD  GLN B 319     7161  15318   7702    650   2280    815       C  
ATOM   5057  OE1 GLN B 319      50.566  -3.958   7.450  1.00 66.19           O  
ANISOU 5057  OE1 GLN B 319     5462  13571   6118    671   2321    867       O  
ATOM   5058  NE2 GLN B 319      48.823  -4.832   6.337  1.00 72.46           N  
ANISOU 5058  NE2 GLN B 319     6337  14439   6754    609   2323    770       N  
ATOM   5059  N   LYS B 320      48.008  -2.721  11.720  1.00 67.44           N  
ANISOU 5059  N   LYS B 320     5425  14042   6158    645   2017    736       N  
ATOM   5060  CA  LYS B 320      47.305  -3.618  12.634  1.00 69.38           C  
ANISOU 5060  CA  LYS B 320     5673  14337   6351    619   1983    723       C  
ATOM   5061  C   LYS B 320      46.155  -2.903  13.336  1.00 67.93           C  
ANISOU 5061  C   LYS B 320     5455  14245   6111    611   1904    660       C  
ATOM   5062  O   LYS B 320      45.047  -3.450  13.454  1.00 67.22           O  
ANISOU 5062  O   LYS B 320     5395  14182   5963    584   1885    632       O  
ATOM   5063  CB  LYS B 320      48.291  -4.186  13.656  1.00 65.67           C  
ANISOU 5063  CB  LYS B 320     5152  13883   5915    636   1987    779       C  
ATOM   5064  CG  LYS B 320      47.687  -5.146  14.667  1.00 70.80           C  
ANISOU 5064  CG  LYS B 320     5798  14580   6521    630   1973    800       C  
ATOM   5065  CD  LYS B 320      48.690  -5.459  15.769  1.00 80.16           C  
ANISOU 5065  CD  LYS B 320     6906  15832   7719    671   1961    874       C  
ATOM   5066  CE  LYS B 320      48.065  -6.278  16.887  1.00 87.64           C  
ANISOU 5066  CE  LYS B 320     7839  16846   8615    685   1948    915       C  
ATOM   5067  NZ  LYS B 320      49.011  -6.466  18.024  1.00 92.41           N  
ANISOU 5067  NZ  LYS B 320     8345  17567   9198    742   1920   1000       N  
ATOM   5068  N   ALA B 321      46.401  -1.680  13.815  1.00 70.06           N  
ANISOU 5068  N   ALA B 321     5654  14556   6410    626   1872    628       N  
ATOM   5069  CA  ALA B 321      45.332  -0.907  14.439  1.00 71.73           C  
ANISOU 5069  CA  ALA B 321     5830  14839   6584    617   1816    562       C  
ATOM   5070  C   ALA B 321      44.215  -0.616  13.445  1.00 73.91           C  
ANISOU 5070  C   ALA B 321     6154  15104   6825    624   1821    556       C  
ATOM   5071  O   ALA B 321      43.027  -0.670  13.796  1.00 79.69           O  
ANISOU 5071  O   ALA B 321     6888  15894   7497    609   1776    520       O  
ATOM   5072  CB  ALA B 321      45.890   0.392  15.019  1.00 65.60           C  
ANISOU 5072  CB  ALA B 321     4963  14085   5877    622   1816    507       C  
ATOM   5073  N   CYS B 322      44.580  -0.304  12.198  1.00 71.84           N  
ANISOU 5073  N   CYS B 322     5922  14783   6589    654   1874    598       N  
ATOM   5074  CA  CYS B 322      43.586  -0.099  11.151  1.00 70.94           C  
ANISOU 5074  CA  CYS B 322     5841  14697   6414    675   1875    610       C  
ATOM   5075  C   CYS B 322      42.714  -1.335  10.976  1.00 73.82           C  
ANISOU 5075  C   CYS B 322     6254  15107   6689    628   1848    577       C  
ATOM   5076  O   CYS B 322      41.488  -1.233  10.876  1.00 80.42           O  
ANISOU 5076  O   CYS B 322     7081  16019   7455    622   1807    545       O  
ATOM   5077  CB  CYS B 322      44.282   0.265   9.839  1.00 75.60           C  
ANISOU 5077  CB  CYS B 322     6457  15232   7034    722   1943    675       C  
ATOM   5078  SG  CYS B 322      43.214   0.229   8.382  1.00 79.05           S  
ANISOU 5078  SG  CYS B 322     6929  15754   7354    754   1939    703       S  
ATOM   5079  N   LYS B 323      43.334  -2.517  10.937  1.00 65.28           N  
ANISOU 5079  N   LYS B 323     5212  13971   5618    592   1886    581       N  
ATOM   5080  CA  LYS B 323      42.565  -3.741  10.722  1.00 65.44           C  
ANISOU 5080  CA  LYS B 323     5272  14006   5586    536   1900    533       C  
ATOM   5081  C   LYS B 323      41.642  -4.038  11.901  1.00 65.29           C  
ANISOU 5081  C   LYS B 323     5228  14032   5545    508   1853    493       C  
ATOM   5082  O   LYS B 323      40.498  -4.472  11.709  1.00 65.50           O  
ANISOU 5082  O   LYS B 323     5261  14110   5515    469   1841    433       O  
ATOM   5083  CB  LYS B 323      43.511  -4.916  10.474  1.00 77.18           C  
ANISOU 5083  CB  LYS B 323     6804  15395   7126    508   1988    554       C  
ATOM   5084  CG  LYS B 323      44.320  -4.800   9.192  1.00 83.30           C  
ANISOU 5084  CG  LYS B 323     7613  16125   7914    525   2046    580       C  
ATOM   5085  CD  LYS B 323      45.223  -6.006   8.987  1.00 94.00           C  
ANISOU 5085  CD  LYS B 323     9011  17371   9336    494   2151    597       C  
ATOM   5086  CE  LYS B 323      45.929  -5.938   7.642  1.00 92.88           C  
ANISOU 5086  CE  LYS B 323     8907  17189   9196    504   2214    609       C  
ATOM   5087  NZ  LYS B 323      46.824  -7.107   7.417  1.00 88.98           N  
ANISOU 5087  NZ  LYS B 323     8453  16573   8782    471   2336    622       N  
ATOM   5088  N   VAL B 324      42.109  -3.791  13.127  1.00 69.69           N  
ANISOU 5088  N   VAL B 324     5750  14589   6140    525   1827    519       N  
ATOM   5089  CA  VAL B 324      41.267  -4.043  14.297  1.00 65.01           C  
ANISOU 5089  CA  VAL B 324     5133  14048   5520    507   1786    490       C  
ATOM   5090  C   VAL B 324      40.072  -3.091  14.314  1.00 66.31           C  
ANISOU 5090  C   VAL B 324     5268  14291   5635    511   1722    439       C  
ATOM   5091  O   VAL B 324      38.924  -3.501  14.550  1.00 68.85           O  
ANISOU 5091  O   VAL B 324     5592  14654   5915    480   1704    394       O  
ATOM   5092  CB  VAL B 324      42.095  -3.936  15.589  1.00 65.03           C  
ANISOU 5092  CB  VAL B 324     5089  14071   5550    532   1766    529       C  
ATOM   5093  CG1 VAL B 324      41.193  -4.044  16.810  1.00 65.10           C  
ANISOU 5093  CG1 VAL B 324     5068  14153   5514    522   1720    501       C  
ATOM   5094  CG2 VAL B 324      43.169  -5.012  15.619  1.00 65.29           C  
ANISOU 5094  CG2 VAL B 324     5142  14037   5630    541   1837    603       C  
ATOM   5095  N   LEU B 325      40.321  -1.803  14.062  1.00 64.91           N  
ANISOU 5095  N   LEU B 325     5058  14128   5479    551   1705    448       N  
ATOM   5096  CA  LEU B 325      39.219  -0.848  14.017  1.00 65.02           C  
ANISOU 5096  CA  LEU B 325     5038  14203   5465    569   1668    420       C  
ATOM   5097  C   LEU B 325      38.278  -1.134  12.853  1.00 71.91           C  
ANISOU 5097  C   LEU B 325     5931  15125   6267    567   1665    415       C  
ATOM   5098  O   LEU B 325      37.074  -0.867  12.951  1.00 80.71           O  
ANISOU 5098  O   LEU B 325     7018  16314   7334    566   1626    385       O  
ATOM   5099  CB  LEU B 325      39.765   0.576  13.946  1.00 65.20           C  
ANISOU 5099  CB  LEU B 325     5015  14200   5557    618   1692    441       C  
ATOM   5100  CG  LEU B 325      40.538   0.985  15.203  1.00 65.18           C  
ANISOU 5100  CG  LEU B 325     4963  14190   5614    604   1688    404       C  
ATOM   5101  CD1 LEU B 325      41.065   2.401  15.089  1.00 74.31           C  
ANISOU 5101  CD1 LEU B 325     6064  15300   6871    636   1743    395       C  
ATOM   5102  CD2 LEU B 325      39.671   0.829  16.444  1.00 65.14           C  
ANISOU 5102  CD2 LEU B 325     4932  14255   5563    572   1634    344       C  
ATOM   5103  N   GLY B 326      38.797  -1.684  11.755  1.00 65.51           N  
ANISOU 5103  N   GLY B 326     5160  14291   5442    563   1704    435       N  
ATOM   5104  CA  GLY B 326      37.928  -2.111  10.673  1.00 66.05           C  
ANISOU 5104  CA  GLY B 326     5233  14441   5420    546   1697    402       C  
ATOM   5105  C   GLY B 326      37.036  -3.269  11.075  1.00 74.80           C  
ANISOU 5105  C   GLY B 326     6349  15578   6495    467   1693    315       C  
ATOM   5106  O   GLY B 326      35.869  -3.328  10.682  1.00 76.26           O  
ANISOU 5106  O   GLY B 326     6501  15871   6603    448   1659    261       O  
ATOM   5107  N   ILE B 327      37.574  -4.207  11.858  1.00 65.87           N  
ANISOU 5107  N   ILE B 327     5251  14353   5425    425   1738    306       N  
ATOM   5108  CA  ILE B 327      36.741  -5.278  12.402  1.00 66.09           C  
ANISOU 5108  CA  ILE B 327     5283  14378   5451    358   1764    237       C  
ATOM   5109  C   ILE B 327      35.627  -4.693  13.261  1.00 65.94           C  
ANISOU 5109  C   ILE B 327     5220  14434   5402    367   1693    216       C  
ATOM   5110  O   ILE B 327      34.466  -5.119  13.182  1.00 66.35           O  
ANISOU 5110  O   ILE B 327     5250  14546   5413    321   1687    141       O  
ATOM   5111  CB  ILE B 327      37.599  -6.279  13.199  1.00 65.99           C  
ANISOU 5111  CB  ILE B 327     5306  14245   5523    343   1843    275       C  
ATOM   5112  CG1 ILE B 327      38.496  -7.088  12.263  1.00 74.69           C  
ANISOU 5112  CG1 ILE B 327     6451  15262   6664    318   1941    278       C  
ATOM   5113  CG2 ILE B 327      36.716  -7.207  14.022  1.00 66.29           C  
ANISOU 5113  CG2 ILE B 327     5341  14267   5580    295   1885    231       C  
ATOM   5114  CD1 ILE B 327      39.323  -8.139  12.974  1.00 71.14           C  
ANISOU 5114  CD1 ILE B 327     6029  14688   6311    315   2044    336       C  
ATOM   5115  N   VAL B 328      35.966  -3.707  14.096  1.00 65.49           N  
ANISOU 5115  N   VAL B 328     5140  14373   5369    420   1648    267       N  
ATOM   5116  CA  VAL B 328      34.958  -3.058  14.938  1.00 65.41           C  
ANISOU 5116  CA  VAL B 328     5088  14426   5339    429   1592    243       C  
ATOM   5117  C   VAL B 328      33.864  -2.424  14.079  1.00 65.81           C  
ANISOU 5117  C   VAL B 328     5099  14579   5327    445   1554    219       C  
ATOM   5118  O   VAL B 328      32.663  -2.623  14.318  1.00 66.06           O  
ANISOU 5118  O   VAL B 328     5102  14677   5320    416   1529    166       O  
ATOM   5119  CB  VAL B 328      35.618  -2.021  15.864  1.00 65.10           C  
ANISOU 5119  CB  VAL B 328     5021  14371   5342    473   1568    277       C  
ATOM   5120  CG1 VAL B 328      34.567  -1.103  16.470  1.00 65.17           C  
ANISOU 5120  CG1 VAL B 328     4983  14442   5337    486   1526    245       C  
ATOM   5121  CG2 VAL B 328      36.411  -2.718  16.957  1.00 64.97           C  
ANISOU 5121  CG2 VAL B 328     5017  14314   5354    461   1586    297       C  
ATOM   5122  N   PHE B 329      34.269  -1.628  13.083  1.00 66.01           N  
ANISOU 5122  N   PHE B 329     5114  14628   5340    500   1553    271       N  
ATOM   5123  CA  PHE B 329      33.307  -0.972  12.199  1.00 68.08           C  
ANISOU 5123  CA  PHE B 329     5325  15012   5530    541   1521    283       C  
ATOM   5124  C   PHE B 329      32.415  -1.994  11.505  1.00 67.92           C  
ANISOU 5124  C   PHE B 329     5290  15095   5420    478   1508    200       C  
ATOM   5125  O   PHE B 329      31.191  -1.818  11.421  1.00 71.59           O  
ANISOU 5125  O   PHE B 329     5696  15681   5822    477   1465    167       O  
ATOM   5126  CB  PHE B 329      34.034  -0.116  11.158  1.00 73.44           C  
ANISOU 5126  CB  PHE B 329     5999  15692   6211    622   1546    375       C  
ATOM   5127  CG  PHE B 329      34.907   0.962  11.743  1.00 78.75           C  
ANISOU 5127  CG  PHE B 329     6671  16259   6992    676   1583    437       C  
ATOM   5128  CD1 PHE B 329      34.703   1.429  13.032  1.00 91.90           C  
ANISOU 5128  CD1 PHE B 329     8314  17884   8719    664   1576    405       C  
ATOM   5129  CD2 PHE B 329      35.930   1.516  10.991  1.00 73.99           C  
ANISOU 5129  CD2 PHE B 329     6080  15601   6432    733   1635    514       C  
ATOM   5130  CE1 PHE B 329      35.511   2.421  13.560  1.00 87.25           C  
ANISOU 5130  CE1 PHE B 329     7707  17209   8235    695   1622    427       C  
ATOM   5131  CE2 PHE B 329      36.738   2.508  11.514  1.00 75.52           C  
ANISOU 5131  CE2 PHE B 329     6258  15692   6744    769   1688    548       C  
ATOM   5132  CZ  PHE B 329      36.527   2.961  12.799  1.00 80.62           C  
ANISOU 5132  CZ  PHE B 329     6873  16306   7453    745   1683    493       C  
ATOM   5133  N   PHE B 330      33.021  -3.063  10.980  1.00 67.40           N  
ANISOU 5133  N   PHE B 330     5269  14986   5353    419   1555    155       N  
ATOM   5134  CA  PHE B 330      32.263  -4.087  10.271  1.00 68.24           C  
ANISOU 5134  CA  PHE B 330     5353  15186   5388    338   1567     41       C  
ATOM   5135  C   PHE B 330      31.234  -4.733  11.183  1.00 79.32           C  
ANISOU 5135  C   PHE B 330     6738  16590   6811    269   1571    -46       C  
ATOM   5136  O   PHE B 330      30.073  -4.903  10.799  1.00 81.03           O  
ANISOU 5136  O   PHE B 330     6889  16947   6952    232   1540   -130       O  
ATOM   5137  CB  PHE B 330      33.213  -5.142   9.702  1.00 68.41           C  
ANISOU 5137  CB  PHE B 330     5433  15118   5441    279   1652      0       C  
ATOM   5138  CG  PHE B 330      32.514  -6.326   9.087  1.00 72.83           C  
ANISOU 5138  CG  PHE B 330     5969  15746   5957    170   1700   -153       C  
ATOM   5139  CD1 PHE B 330      32.133  -6.315   7.755  1.00 78.14           C  
ANISOU 5139  CD1 PHE B 330     6587  16594   6507    154   1674   -219       C  
ATOM   5140  CD2 PHE B 330      32.255  -7.461   9.842  1.00 69.51           C  
ANISOU 5140  CD2 PHE B 330     5571  15219   5621     83   1785   -235       C  
ATOM   5141  CE1 PHE B 330      31.495  -7.406   7.193  1.00 76.61           C  
ANISOU 5141  CE1 PHE B 330     6356  16478   6273     35   1725   -396       C  
ATOM   5142  CE2 PHE B 330      31.617  -8.553   9.287  1.00 70.68           C  
ANISOU 5142  CE2 PHE B 330     5689  15411   5754    -30   1859   -398       C  
ATOM   5143  CZ  PHE B 330      31.237  -8.527   7.960  1.00 74.33           C  
ANISOU 5143  CZ  PHE B 330     6092  16059   6093    -64   1825   -495       C  
ATOM   5144  N   LEU B 331      31.645  -5.116  12.393  1.00 82.13           N  
ANISOU 5144  N   LEU B 331     7141  16803   7262    255   1611    -24       N  
ATOM   5145  CA  LEU B 331      30.709  -5.749  13.314  1.00 67.68           C  
ANISOU 5145  CA  LEU B 331     5297  14959   5460    199   1632    -89       C  
ATOM   5146  C   LEU B 331      29.557  -4.813  13.653  1.00 67.72           C  
ANISOU 5146  C   LEU B 331     5238  15079   5414    235   1547    -89       C  
ATOM   5147  O   LEU B 331      28.388  -5.216  13.620  1.00 68.34           O  
ANISOU 5147  O   LEU B 331     5268  15240   5458    182   1543   -178       O  
ATOM   5148  CB  LEU B 331      31.441  -6.212  14.573  1.00 67.09           C  
ANISOU 5148  CB  LEU B 331     5276  14734   5481    206   1688    -31       C  
ATOM   5149  CG  LEU B 331      32.276  -7.470  14.324  1.00 67.44           C  
ANISOU 5149  CG  LEU B 331     5372  14657   5594    160   1809    -40       C  
ATOM   5150  CD1 LEU B 331      32.902  -7.983  15.604  1.00 67.10           C  
ANISOU 5150  CD1 LEU B 331     5365  14495   5636    184   1870     42       C  
ATOM   5151  CD2 LEU B 331      31.425  -8.552  13.672  1.00 68.42           C  
ANISOU 5151  CD2 LEU B 331     5476  14799   5720     60   1891   -177       C  
ATOM   5152  N   PHE B 332      29.865  -3.548  13.957  1.00 67.21           N  
ANISOU 5152  N   PHE B 332     5165  15018   5353    321   1494      4       N  
ATOM   5153  CA  PHE B 332      28.810  -2.595  14.296  1.00 69.10           C  
ANISOU 5153  CA  PHE B 332     5344  15348   5564    362   1437     15       C  
ATOM   5154  C   PHE B 332      27.813  -2.441  13.153  1.00 68.33           C  
ANISOU 5154  C   PHE B 332     5170  15429   5365    368   1396    -17       C  
ATOM   5155  O   PHE B 332      26.594  -2.559  13.351  1.00 68.82           O  
ANISOU 5155  O   PHE B 332     5173  15584   5391    341   1371    -77       O  
ATOM   5156  CB  PHE B 332      29.427  -1.242  14.653  1.00 75.63           C  
ANISOU 5156  CB  PHE B 332     6170  16131   6435    450   1424    111       C  
ATOM   5157  CG  PHE B 332      28.420  -0.134  14.800  1.00 80.77           C  
ANISOU 5157  CG  PHE B 332     6754  16861   7074    507   1393    139       C  
ATOM   5158  CD1 PHE B 332      27.668  -0.009  15.955  1.00 79.78           C  
ANISOU 5158  CD1 PHE B 332     6614  16721   6977    487   1386    101       C  
ATOM   5159  CD2 PHE B 332      28.229   0.786  13.780  1.00 83.45           C  
ANISOU 5159  CD2 PHE B 332     7042  17288   7375    590   1385    217       C  
ATOM   5160  CE1 PHE B 332      26.745   1.010  16.090  1.00 67.53           C  
ANISOU 5160  CE1 PHE B 332     5001  15228   5430    540   1374    129       C  
ATOM   5161  CE2 PHE B 332      27.306   1.805  13.910  1.00 79.71           C  
ANISOU 5161  CE2 PHE B 332     6503  16877   6908    656   1379    264       C  
ATOM   5162  CZ  PHE B 332      26.563   1.917  15.068  1.00 71.20           C  
ANISOU 5162  CZ  PHE B 332     5413  15770   5870    626   1375    214       C  
ATOM   5163  N   VAL B 333      28.316  -2.189  11.942  1.00 75.83           N  
ANISOU 5163  N   VAL B 333     6109  16446   6258    408   1389     24       N  
ATOM   5164  CA  VAL B 333      27.425  -1.930  10.816  1.00 78.55           C  
ANISOU 5164  CA  VAL B 333     6361  17007   6478    435   1340     14       C  
ATOM   5165  C   VAL B 333      26.630  -3.180  10.459  1.00 81.87           C  
ANISOU 5165  C   VAL B 333     6742  17529   6836    317   1343   -149       C  
ATOM   5166  O   VAL B 333      25.423  -3.108  10.208  1.00 88.29           O  
ANISOU 5166  O   VAL B 333     7459  18521   7566    308   1295   -202       O  
ATOM   5167  CB  VAL B 333      28.225  -1.397   9.614  1.00 75.94           C  
ANISOU 5167  CB  VAL B 333     6028  16730   6094    514   1340    108       C  
ATOM   5168  CG1 VAL B 333      27.372  -1.418   8.353  1.00 71.97           C  
ANISOU 5168  CG1 VAL B 333     5421  16493   5431    532   1288     83       C  
ATOM   5169  CG2 VAL B 333      28.720   0.013   9.897  1.00 77.87           C  
ANISOU 5169  CG2 VAL B 333     6283  16896   6410    638   1355    265       C  
ATOM   5170  N   VAL B 334      27.284  -4.343  10.437  1.00 75.59           N  
ANISOU 5170  N   VAL B 334     6011  16621   6090    223   1414   -237       N  
ATOM   5171  CA  VAL B 334      26.600  -5.577  10.064  1.00 75.97           C  
ANISOU 5171  CA  VAL B 334     6019  16739   6108     95   1455   -415       C  
ATOM   5172  C   VAL B 334      25.538  -5.943  11.094  1.00 79.92           C  
ANISOU 5172  C   VAL B 334     6493  17214   6658     40   1468   -487       C  
ATOM   5173  O   VAL B 334      24.477  -6.470  10.744  1.00 85.81           O  
ANISOU 5173  O   VAL B 334     7155  18101   7349    -39   1464   -627       O  
ATOM   5174  CB  VAL B 334      27.629  -6.706   9.869  1.00 76.46           C  
ANISOU 5174  CB  VAL B 334     6163  16644   6246     16   1565   -476       C  
ATOM   5175  CG1 VAL B 334      26.955  -8.072   9.892  1.00 72.59           C  
ANISOU 5175  CG1 VAL B 334     5646  16140   5793   -128   1660   -667       C  
ATOM   5176  CG2 VAL B 334      28.375  -6.506   8.562  1.00 77.73           C  
ANISOU 5176  CG2 VAL B 334     6321  16889   6324     45   1552   -455       C  
ATOM   5177  N   MET B 335      25.793  -5.670  12.376  1.00 78.73           N  
ANISOU 5177  N   MET B 335     6407  16899   6610     78   1485   -401       N  
ATOM   5178  CA  MET B 335      24.801  -6.010  13.388  1.00 81.78           C  
ANISOU 5178  CA  MET B 335     6773  17256   7045     34   1506   -457       C  
ATOM   5179  C   MET B 335      23.637  -5.027  13.423  1.00 84.95           C  
ANISOU 5179  C   MET B 335     7083  17822   7372     88   1413   -437       C  
ATOM   5180  O   MET B 335      22.509  -5.431  13.727  1.00 81.32           O  
ANISOU 5180  O   MET B 335     6566  17422   6910     29   1420   -532       O  
ATOM   5181  CB  MET B 335      25.463  -6.110  14.762  1.00 78.77           C  
ANISOU 5181  CB  MET B 335     6481  16670   6779     59   1557   -374       C  
ATOM   5182  CG  MET B 335      26.300  -7.368  14.918  1.00 74.26           C  
ANISOU 5182  CG  MET B 335     5981  15937   6299     -1   1681   -399       C  
ATOM   5183  SD  MET B 335      26.806  -7.713  16.611  1.00 69.55           S  
ANISOU 5183  SD  MET B 335     5458  15155   5815     31   1751   -302       S  
ATOM   5184  CE  MET B 335      27.471  -9.365  16.417  1.00 72.45           C  
ANISOU 5184  CE  MET B 335     5875  15361   6291    -42   1933   -340       C  
ATOM   5185  N   TRP B 336      23.868  -3.748  13.122  1.00 84.02           N  
ANISOU 5185  N   TRP B 336     6947  17770   7208    202   1343   -310       N  
ATOM   5186  CA  TRP B 336      22.754  -2.805  13.108  1.00 80.02           C  
ANISOU 5186  CA  TRP B 336     6347  17415   6642    266   1276   -271       C  
ATOM   5187  C   TRP B 336      22.048  -2.703  11.760  1.00 82.89           C  
ANISOU 5187  C   TRP B 336     6591  18045   6858    280   1216   -304       C  
ATOM   5188  O   TRP B 336      20.983  -2.082  11.688  1.00 82.48           O  
ANISOU 5188  O   TRP B 336     6442  18151   6745    330   1165   -277       O  
ATOM   5189  CB  TRP B 336      23.217  -1.411  13.544  1.00 75.33           C  
ANISOU 5189  CB  TRP B 336     5777  16749   6095    390   1262   -112       C  
ATOM   5190  CG  TRP B 336      23.103  -1.178  15.024  1.00 77.93           C  
ANISOU 5190  CG  TRP B 336     6153  16930   6528    385   1289   -104       C  
ATOM   5191  CD1 TRP B 336      24.116  -0.882  15.886  1.00 83.72           C  
ANISOU 5191  CD1 TRP B 336     6967  17495   7349    403   1322    -54       C  
ATOM   5192  CD2 TRP B 336      21.906  -1.229  15.816  1.00 77.77           C  
ANISOU 5192  CD2 TRP B 336     6091  16936   6521    357   1284   -156       C  
ATOM   5193  NE1 TRP B 336      23.628  -0.738  17.162  1.00 85.02           N  
ANISOU 5193  NE1 TRP B 336     7140  17594   7570    390   1335    -74       N  
ATOM   5194  CE2 TRP B 336      22.274  -0.947  17.146  1.00 81.31           C  
ANISOU 5194  CE2 TRP B 336     6603  17228   7063    363   1317   -131       C  
ATOM   5195  CE3 TRP B 336      20.561  -1.483  15.528  1.00 74.23           C  
ANISOU 5195  CE3 TRP B 336     5550  16643   6012    325   1256   -227       C  
ATOM   5196  CZ2 TRP B 336      21.347  -0.912  18.187  1.00 78.92           C  
ANISOU 5196  CZ2 TRP B 336     6284  16907   6795    343   1327   -167       C  
ATOM   5197  CZ3 TRP B 336      19.643  -1.450  16.563  1.00 71.14           C  
ANISOU 5197  CZ3 TRP B 336     5144  16218   5669    305   1269   -261       C  
ATOM   5198  CH2 TRP B 336      20.040  -1.168  17.876  1.00 69.79           C  
ANISOU 5198  CH2 TRP B 336     5047  15877   5593    315   1307   -227       C  
ATOM   5199  N   CYS B 337      22.600  -3.289  10.698  1.00 82.35           N  
ANISOU 5199  N   CYS B 337     6519  18047   6722    240   1222   -359       N  
ATOM   5200  CA  CYS B 337      21.984  -3.191   9.379  1.00 88.27           C  
ANISOU 5200  CA  CYS B 337     7142  19094   7304    256   1157   -395       C  
ATOM   5201  C   CYS B 337      20.647  -3.923   9.272  1.00 85.64           C  
ANISOU 5201  C   CYS B 337     6692  18944   6901    150   1136   -576       C  
ATOM   5202  O   CYS B 337      19.729  -3.393   8.635  1.00 88.53           O  
ANISOU 5202  O   CYS B 337     6921  19585   7130    206   1056   -557       O  
ATOM   5203  CB  CYS B 337      22.948  -3.704   8.304  1.00100.24           C  
ANISOU 5203  CB  CYS B 337     8683  20637   8765    226   1178   -432       C  
ATOM   5204  SG  CYS B 337      23.938  -2.409   7.516  1.00109.36           S  
ANISOU 5204  SG  CYS B 337     9858  21819   9874    404   1150   -198       S  
ATOM   5205  N   PRO B 338      20.486  -5.135   9.829  1.00 76.11           N  
ANISOU 5205  N   PRO B 338     5524  17608   5786      1   1215   -749       N  
ATOM   5206  CA  PRO B 338      19.158  -5.772   9.763  1.00 80.65           C  
ANISOU 5206  CA  PRO B 338     5979  18350   6313   -105   1208   -934       C  
ATOM   5207  C   PRO B 338      18.051  -4.913  10.343  1.00 84.55           C  
ANISOU 5207  C   PRO B 338     6399  18939   6786    -27   1143   -855       C  
ATOM   5208  O   PRO B 338      16.951  -4.865   9.776  1.00 88.33           O  
ANISOU 5208  O   PRO B 338     6727  19693   7139    -43   1078   -936       O  
ATOM   5209  CB  PRO B 338      19.355  -7.067  10.560  1.00 77.05           C  
ANISOU 5209  CB  PRO B 338     5613  17641   6023   -246   1344  -1075       C  
ATOM   5210  CG  PRO B 338      20.781  -7.389  10.377  1.00 76.21           C  
ANISOU 5210  CG  PRO B 338     5627  17352   5979   -243   1409  -1022       C  
ATOM   5211  CD  PRO B 338      21.487  -6.063  10.385  1.00 75.09           C  
ANISOU 5211  CD  PRO B 338     5531  17199   5803    -78   1328   -792       C  
ATOM   5212  N   PHE B 339      18.313  -4.220  11.455  1.00 82.13           N  
ANISOU 5212  N   PHE B 339     6187  18423   6595     56   1160   -705       N  
ATOM   5213  CA  PHE B 339      17.279  -3.389  12.061  1.00 80.31           C  
ANISOU 5213  CA  PHE B 339     5894  18255   6364    128   1118   -632       C  
ATOM   5214  C   PHE B 339      16.855  -2.267  11.125  1.00 79.35           C  
ANISOU 5214  C   PHE B 339     5654  18399   6097    266   1026   -500       C  
ATOM   5215  O   PHE B 339      15.659  -2.046  10.914  1.00 86.18           O  
ANISOU 5215  O   PHE B 339     6387  19482   6875    281    975   -525       O  
ATOM   5216  CB  PHE B 339      17.759  -2.806  13.389  1.00 79.91           C  
ANISOU 5216  CB  PHE B 339     5965  17936   6461    188   1161   -507       C  
ATOM   5217  CG  PHE B 339      16.932  -1.640  13.856  1.00 78.94           C  
ANISOU 5217  CG  PHE B 339     5785  17865   6341    293   1126   -393       C  
ATOM   5218  CD1 PHE B 339      15.644  -1.833  14.324  1.00 78.59           C  
ANISOU 5218  CD1 PHE B 339     5666  17894   6301    250   1121   -472       C  
ATOM   5219  CD2 PHE B 339      17.434  -0.349  13.804  1.00 78.63           C  
ANISOU 5219  CD2 PHE B 339     5765  17792   6318    434   1116   -209       C  
ATOM   5220  CE1 PHE B 339      14.876  -0.764  14.744  1.00 77.24           C  
ANISOU 5220  CE1 PHE B 339     5443  17760   6145    349   1101   -364       C  
ATOM   5221  CE2 PHE B 339      16.671   0.724  14.223  1.00 78.15           C  
ANISOU 5221  CE2 PHE B 339     5651  17756   6285    531   1112   -104       C  
ATOM   5222  CZ  PHE B 339      15.390   0.516  14.693  1.00 75.06           C  
ANISOU 5222  CZ  PHE B 339     5189  17439   5892    490   1101   -178       C  
ATOM   5223  N   PHE B 340      17.821  -1.534  10.564  1.00 78.47           N  
ANISOU 5223  N   PHE B 340     5583  18273   5960    376   1015   -344       N  
ATOM   5224  CA  PHE B 340      17.473  -0.432   9.672  1.00 83.71           C  
ANISOU 5224  CA  PHE B 340     6135  19174   6497    533    953   -178       C  
ATOM   5225  C   PHE B 340      16.807  -0.936   8.399  1.00 93.75           C  
ANISOU 5225  C   PHE B 340     7247  20813   7561    499    877   -284       C  
ATOM   5226  O   PHE B 340      15.836  -0.335   7.922  1.00101.18           O  
ANISOU 5226  O   PHE B 340     8043  22027   8375    591    814   -210       O  
ATOM   5227  CB  PHE B 340      18.715   0.393   9.335  1.00 83.74           C  
ANISOU 5227  CB  PHE B 340     6221  19058   6539    655    982      7       C  
ATOM   5228  CG  PHE B 340      19.129   1.336  10.426  1.00 82.93           C  
ANISOU 5228  CG  PHE B 340     6215  18685   6608    731   1046    141       C  
ATOM   5229  CD1 PHE B 340      19.921   0.902  11.474  1.00 80.17           C  
ANISOU 5229  CD1 PHE B 340     6003  18052   6404    646   1102     75       C  
ATOM   5230  CD2 PHE B 340      18.725   2.661  10.400  1.00 81.71           C  
ANISOU 5230  CD2 PHE B 340     6005  18570   6473    889   1060    332       C  
ATOM   5231  CE1 PHE B 340      20.302   1.771  12.478  1.00 74.76           C  
ANISOU 5231  CE1 PHE B 340     5388  17153   5862    703   1157    168       C  
ATOM   5232  CE2 PHE B 340      19.102   3.535  11.401  1.00 75.71           C  
ANISOU 5232  CE2 PHE B 340     5323  17556   5886    941   1137    422       C  
ATOM   5233  CZ  PHE B 340      19.892   3.090  12.441  1.00 74.03           C  
ANISOU 5233  CZ  PHE B 340     5239  17089   5800    841   1179    326       C  
ATOM   5234  N   ILE B 341      17.308  -2.043   7.842  1.00 93.70           N  
ANISOU 5234  N   ILE B 341     7257  20827   7516    365    889   -462       N  
ATOM   5235  CA  ILE B 341      16.683  -2.650   6.668  1.00 93.33           C  
ANISOU 5235  CA  ILE B 341     7047  21142   7272    297    824   -620       C  
ATOM   5236  C   ILE B 341      15.214  -2.939   6.943  1.00 92.29           C  
ANISOU 5236  C   ILE B 341     6781  21196   7088    227    787   -757       C  
ATOM   5237  O   ILE B 341      14.323  -2.458   6.235  1.00 94.32           O  
ANISOU 5237  O   ILE B 341     6865  21809   7164    305    697   -717       O  
ATOM   5238  CB  ILE B 341      17.435  -3.927   6.252  1.00 90.73           C  
ANISOU 5238  CB  ILE B 341     6775  20734   6964    127    881   -833       C  
ATOM   5239  CG1 ILE B 341      18.794  -3.578   5.642  1.00 82.12           C  
ANISOU 5239  CG1 ILE B 341     5777  19554   5870    211    897   -694       C  
ATOM   5240  CG2 ILE B 341      16.603  -4.743   5.273  1.00 90.90           C  
ANISOU 5240  CG2 ILE B 341     6617  21110   6811      1    833  -1078       C  
ATOM   5241  CD1 ILE B 341      19.646  -4.787   5.319  1.00 81.99           C  
ANISOU 5241  CD1 ILE B 341     5841  19409   5904     55    975   -881       C  
ATOM   5242  N   THR B 342      14.941  -3.721   7.992  1.00 89.12           N  
ANISOU 5242  N   THR B 342     6455  20562   6847     90    861   -908       N  
ATOM   5243  CA  THR B 342      13.568  -4.118   8.284  1.00 90.27           C  
ANISOU 5243  CA  THR B 342     6480  20854   6966      3    844  -1065       C  
ATOM   5244  C   THR B 342      12.702  -2.933   8.701  1.00 89.71           C  
ANISOU 5244  C   THR B 342     6345  20870   6871    159    790   -872       C  
ATOM   5245  O   THR B 342      11.507  -2.912   8.396  1.00 92.50           O  
ANISOU 5245  O   THR B 342     6536  21505   7103    150    729   -942       O  
ATOM   5246  CB  THR B 342      13.558  -5.203   9.361  1.00 91.24           C  
ANISOU 5246  CB  THR B 342     6710  20665   7292   -162    963  -1239       C  
ATOM   5247  OG1 THR B 342      14.349  -6.308   8.913  1.00 96.52           O  
ANISOU 5247  OG1 THR B 342     7433  21246   7995   -299   1038  -1408       O  
ATOM   5248  CG2 THR B 342      12.142  -5.692   9.627  1.00 88.28           C  
ANISOU 5248  CG2 THR B 342     6209  20427   6908   -265    962  -1422       C  
ATOM   5249  N   ASN B 343      13.277  -1.929   9.365  1.00 86.32           N  
ANISOU 5249  N   ASN B 343     6032  20210   6554    300    817   -635       N  
ATOM   5250  CA  ASN B 343      12.487  -0.785   9.806  1.00 90.57           C  
ANISOU 5250  CA  ASN B 343     6519  20788   7104    445    796   -452       C  
ATOM   5251  C   ASN B 343      12.067   0.075   8.620  1.00105.10           C  
ANISOU 5251  C   ASN B 343     8201  22995   8739    606    711   -291       C  
ATOM   5252  O   ASN B 343      10.885   0.412   8.467  1.00115.49           O  
ANISOU 5252  O   ASN B 343     9374  24551   9958    657    662   -266       O  
ATOM   5253  CB  ASN B 343      13.288   0.035  10.819  1.00 86.76           C  
ANISOU 5253  CB  ASN B 343     6200  19953   6813    534    869   -273       C  
ATOM   5254  CG  ASN B 343      12.404   0.838  11.750  1.00 88.76           C  
ANISOU 5254  CG  ASN B 343     6435  20129   7160    606    892   -177       C  
ATOM   5255  OD1 ASN B 343      11.313   0.403  12.119  1.00 87.48           O  
ANISOU 5255  OD1 ASN B 343     6201  20045   6994    532    880   -297       O  
ATOM   5256  ND2 ASN B 343      12.874   2.016  12.142  1.00 92.18           N  
ANISOU 5256  ND2 ASN B 343     6933  20396   7695    745    938     30       N  
ATOM   5257  N   ILE B 344      13.025   0.435   7.760  1.00104.44           N  
ANISOU 5257  N   ILE B 344     8136  22964   8582    697    698   -167       N  
ATOM   5258  CA  ILE B 344      12.685   1.177   6.553  1.00106.15           C  
ANISOU 5258  CA  ILE B 344     8195  23552   8585    862    624      2       C  
ATOM   5259  C   ILE B 344      11.753   0.355   5.673  1.00113.83           C  
ANISOU 5259  C   ILE B 344     8973  24953   9324    763    527   -208       C  
ATOM   5260  O   ILE B 344      10.863   0.907   5.017  1.00114.73           O  
ANISOU 5260  O   ILE B 344     8914  25430   9248    883    455   -100       O  
ATOM   5261  CB  ILE B 344      13.964   1.600   5.804  1.00100.94           C  
ANISOU 5261  CB  ILE B 344     7600  22847   7905    966    643    159       C  
ATOM   5262  CG1 ILE B 344      14.838   2.474   6.706  1.00 95.90           C  
ANISOU 5262  CG1 ILE B 344     7139  21795   7502   1056    747    346       C  
ATOM   5263  CG2 ILE B 344      13.618   2.355   4.530  1.00102.51           C  
ANISOU 5263  CG2 ILE B 344     7628  23447   7874   1156    574    360       C  
ATOM   5264  CD1 ILE B 344      16.127   2.928   6.059  1.00 93.67           C  
ANISOU 5264  CD1 ILE B 344     6932  21427   7231   1154    785    498       C  
ATOM   5265  N   MET B 345      11.920  -0.971   5.660  1.00120.77           N  
ANISOU 5265  N   MET B 345     9872  25800  10217    540    536   -513       N  
ATOM   5266  CA  MET B 345      11.032  -1.835   4.887  1.00127.70           C  
ANISOU 5266  CA  MET B 345    10558  27067  10894    408    462   -771       C  
ATOM   5267  C   MET B 345       9.607  -1.803   5.426  1.00126.50           C  
ANISOU 5267  C   MET B 345    10302  27036  10726    382    440   -838       C  
ATOM   5268  O   MET B 345       8.646  -1.730   4.652  1.00131.91           O  
ANISOU 5268  O   MET B 345    10784  28159  11176    409    348   -882       O  
ATOM   5269  CB  MET B 345      11.579  -3.262   4.896  1.00132.79           C  
ANISOU 5269  CB  MET B 345    11270  27560  11622    164    523  -1088       C  
ATOM   5270  CG  MET B 345      10.702  -4.288   4.210  1.00138.78           C  
ANISOU 5270  CG  MET B 345    11841  28665  12223    -21    479  -1420       C  
ATOM   5271  SD  MET B 345      11.454  -5.926   4.259  1.00140.24           S  
ANISOU 5271  SD  MET B 345    12131  28592  12564   -300    604  -1772       S  
ATOM   5272  CE  MET B 345      10.004  -6.972   4.154  1.00142.79           C  
ANISOU 5272  CE  MET B 345    12259  29175  12819   -525    603  -2163       C  
ATOM   5273  N   ALA B 346       9.450  -1.860   6.750  1.00121.39           N  
ANISOU 5273  N   ALA B 346     9787  26020  10318    332    523   -848       N  
ATOM   5274  CA  ALA B 346       8.122  -1.780   7.345  1.00120.68           C  
ANISOU 5274  CA  ALA B 346     9610  25998  10244    315    515   -896       C  
ATOM   5275  C   ALA B 346       7.510  -0.404   7.138  1.00125.45           C  
ANISOU 5275  C   ALA B 346    10125  26792  10749    552    465   -593       C  
ATOM   5276  O   ALA B 346       6.282  -0.267   7.145  1.00131.38           O  
ANISOU 5276  O   ALA B 346    10740  27764  11415    568    426   -618       O  
ATOM   5277  CB  ALA B 346       8.188  -2.116   8.835  1.00114.47           C  
ANISOU 5277  CB  ALA B 346     8990  24760   9742    223    624   -951       C  
ATOM   5278  N   VAL B 347       8.345   0.620   6.967  1.00121.18           N  
ANISOU 5278  N   VAL B 347     9660  26146  10236    740    483   -303       N  
ATOM   5279  CA  VAL B 347       7.829   1.936   6.602  1.00117.25           C  
ANISOU 5279  CA  VAL B 347     9069  25834   9648    982    460      9       C  
ATOM   5280  C   VAL B 347       7.411   1.972   5.131  1.00120.90           C  
ANISOU 5280  C   VAL B 347     9325  26840   9772   1063    351     39       C  
ATOM   5281  O   VAL B 347       6.429   2.636   4.776  1.00122.81           O  
ANISOU 5281  O   VAL B 347     9423  27371   9867   1204    314    195       O  
ATOM   5282  CB  VAL B 347       8.864   3.028   6.924  1.00109.05           C  
ANISOU 5282  CB  VAL B 347     8178  24474   8781   1151    545    300       C  
ATOM   5283  CG1 VAL B 347       8.410   4.380   6.390  1.00 99.97           C  
ANISOU 5283  CG1 VAL B 347     6925  23509   7550   1413    549    642       C  
ATOM   5284  CG2 VAL B 347       9.096   3.108   8.423  1.00110.12           C  
ANISOU 5284  CG2 VAL B 347     8487  24137   9215   1082    646    269       C  
ATOM   5285  N   ILE B 348       8.121   1.250   4.261  1.00122.02           N  
ANISOU 5285  N   ILE B 348     9442  27140   9779    975    303   -109       N  
ATOM   5286  CA  ILE B 348       7.836   1.305   2.828  1.00120.88           C  
ANISOU 5286  CA  ILE B 348     9095  27540   9293   1058    195    -78       C  
ATOM   5287  C   ILE B 348       6.506   0.627   2.523  1.00124.97           C  
ANISOU 5287  C   ILE B 348     9424  28463   9597    935    120   -331       C  
ATOM   5288  O   ILE B 348       5.566   1.260   2.028  1.00123.93           O  
ANISOU 5288  O   ILE B 348     9141  28702   9244   1084     73   -177       O  
ATOM   5289  CB  ILE B 348       8.984   0.665   2.026  1.00113.89           C  
ANISOU 5289  CB  ILE B 348     8229  26692   8352    977    171   -198       C  
ATOM   5290  CG1 ILE B 348      10.243   1.533   2.090  1.00105.29           C  
ANISOU 5290  CG1 ILE B 348     7300  25286   7418   1146    244    101       C  
ATOM   5291  CG2 ILE B 348       8.569   0.438   0.579  1.00116.96           C  
ANISOU 5291  CG2 ILE B 348     8371  27694   8374   1003     42   -266       C  
ATOM   5292  CD1 ILE B 348      11.471   0.867   1.505  1.00 99.86           C  
ANISOU 5292  CD1 ILE B 348     6675  24524   6743   1050    250    -22       C  
ATOM   5293  N   CYS B 349       6.408  -0.669   2.805  1.00160.00           N  
ANISOU 5293  N   CYS B 349    13849  29095  17850    400  -5249    181       N  
ATOM   5294  CA  CYS B 349       5.171  -1.421   2.608  1.00170.76           C  
ANISOU 5294  CA  CYS B 349    14936  30331  19616    293  -5784     49       C  
ATOM   5295  C   CYS B 349       4.455  -1.513   3.951  1.00169.35           C  
ANISOU 5295  C   CYS B 349    14174  29932  20240    166  -5453    -52       C  
ATOM   5296  O   CYS B 349       4.856  -2.275   4.833  1.00177.55           O  
ANISOU 5296  O   CYS B 349    15186  30982  21291     43  -5040   -274       O  
ATOM   5297  CB  CYS B 349       5.448  -2.793   1.996  1.00180.12           C  
ANISOU 5297  CB  CYS B 349    16578  31541  20319    206  -6013   -194       C  
ATOM   5298  SG  CYS B 349       6.825  -3.741   2.699  1.00178.40           S  
ANISOU 5298  SG  CYS B 349    16641  31538  19605    114  -5392   -452       S  
ATOM   5299  N   LYS B 350       3.399  -0.713   4.114  1.00163.60           N  
ANISOU 5299  N   LYS B 350    13003  28968  20189    201  -5612    119       N  
ATOM   5300  CA  LYS B 350       2.591  -0.804   5.323  1.00153.43           C  
ANISOU 5300  CA  LYS B 350    11189  27395  19711     90  -5300     36       C  
ATOM   5301  C   LYS B 350       1.565  -1.925   5.230  1.00160.41           C  
ANISOU 5301  C   LYS B 350    11906  28028  21014    -52  -5677   -154       C  
ATOM   5302  O   LYS B 350       1.163  -2.480   6.258  1.00159.34           O  
ANISOU 5302  O   LYS B 350    11480  27695  21366   -181  -5343   -312       O  
ATOM   5303  CB  LYS B 350       1.884   0.527   5.595  1.00143.30           C  
ANISOU 5303  CB  LYS B 350     9494  25918  19037    192  -5252    299       C  
ATOM   5304  CG  LYS B 350       2.793   1.748   5.592  1.00135.21           C  
ANISOU 5304  CG  LYS B 350     8622  25103  17649    346  -4945    532       C  
ATOM   5305  CD  LYS B 350       3.923   1.617   6.597  1.00131.51           C  
ANISOU 5305  CD  LYS B 350     8295  24779  16894    304  -4260    420       C  
ATOM   5306  CE  LYS B 350       3.411   1.487   8.025  1.00128.59           C  
ANISOU 5306  CE  LYS B 350     7562  24104  17192    191  -3764    302       C  
ATOM   5307  NZ  LYS B 350       4.529   1.306   8.996  1.00120.87           N  
ANISOU 5307  NZ  LYS B 350     6788  23222  15913    141  -3147    181       N  
ATOM   5308  N   GLU B 351       1.136  -2.269   4.016  1.00166.62           N  
ANISOU 5308  N   GLU B 351    12903  28787  21620    -31  -6368   -131       N  
ATOM   5309  CA  GLU B 351       0.174  -3.344   3.804  1.00171.20           C  
ANISOU 5309  CA  GLU B 351    13357  29108  22583   -165  -6808   -287       C  
ATOM   5310  C   GLU B 351       0.583  -4.342   2.732  1.00177.22           C  
ANISOU 5310  C   GLU B 351    14697  29985  22653   -194  -7257   -419       C  
ATOM   5311  O   GLU B 351       0.000  -5.431   2.683  1.00180.50           O  
ANISOU 5311  O   GLU B 351    15081  30212  23290   -332  -7524   -581       O  
ATOM   5312  CB  GLU B 351      -1.204  -2.770   3.442  1.00173.02           C  
ANISOU 5312  CB  GLU B 351    13149  29002  23588   -129  -7332   -111       C  
ATOM   5313  CG  GLU B 351      -1.873  -2.001   4.570  1.00168.58           C  
ANISOU 5313  CG  GLU B 351    11964  28206  23885   -123  -6891    -25       C  
ATOM   5314  CD  GLU B 351      -3.268  -1.529   4.210  1.00172.10           C  
ANISOU 5314  CD  GLU B 351    11951  28348  25090    -21  -7368    -32       C  
ATOM   5315  OE1 GLU B 351      -3.705  -1.775   3.067  1.00175.76           O  
ANISOU 5315  OE1 GLU B 351    12582  29046  25153     51  -7932    -95       O  
ATOM   5316  OE2 GLU B 351      -3.929  -0.912   5.073  1.00171.77           O  
ANISOU 5316  OE2 GLU B 351    11399  28345  25519     20  -6883    -50       O  
ATOM   5317  N   SER B 352       1.549  -4.012   1.870  1.00178.50           N  
ANISOU 5317  N   SER B 352    15404  30416  22001    -69  -7331   -338       N  
ATOM   5318  CA  SER B 352       1.985  -4.954   0.844  1.00178.72           C  
ANISOU 5318  CA  SER B 352    16057  30508  21342    -86  -7696   -461       C  
ATOM   5319  C   SER B 352       2.687  -6.159   1.462  1.00172.70           C  
ANISOU 5319  C   SER B 352    15472  29843  20302   -217  -7267   -748       C  
ATOM   5320  O   SER B 352       2.400  -7.307   1.104  1.00172.14           O  
ANISOU 5320  O   SER B 352    15608  29636  20163   -326  -7569   -918       O  
ATOM   5321  CB  SER B 352       2.899  -4.250  -0.159  1.00178.81           C  
ANISOU 5321  CB  SER B 352    16628  30750  20562     91  -7772   -289       C  
ATOM   5322  OG  SER B 352       3.441  -5.168  -1.093  1.00180.14           O  
ANISOU 5322  OG  SER B 352    17468  30952  20025     81  -8007   -412       O  
ATOM   5323  N   CYS B 353       3.610  -5.918   2.389  1.00167.43           N  
ANISOU 5323  N   CYS B 353    14742  29389  19483   -212  -6579   -796       N  
ATOM   5324  CA  CYS B 353       4.361  -6.986   3.033  1.00165.40           C  
ANISOU 5324  CA  CYS B 353    14660  29220  18965   -330  -6145  -1061       C  
ATOM   5325  C   CYS B 353       3.712  -7.390   4.352  1.00151.57           C  
ANISOU 5325  C   CYS B 353    12383  27272  17935   -480  -5822  -1204       C  
ATOM   5326  O   CYS B 353       3.016  -6.600   4.996  1.00140.74           O  
ANISOU 5326  O   CYS B 353    10516  25757  17202   -467  -5702  -1077       O  
ATOM   5327  CB  CYS B 353       5.809  -6.562   3.282  1.00173.01           C  
ANISOU 5327  CB  CYS B 353    15901  30493  19342   -248  -5602  -1034       C  
ATOM   5328  SG  CYS B 353       5.991  -4.960   4.096  1.00176.26           S  
ANISOU 5328  SG  CYS B 353    15890  31003  20078   -140  -5176   -784       S  
ATOM   5329  N   ASN B 354       3.947  -8.640   4.746  1.00152.27           N  
ANISOU 5329  N   ASN B 354    12617  27322  17917   -618  -5657  -1465       N  
ATOM   5330  CA  ASN B 354       3.375  -9.170   5.978  1.00155.32           C  
ANISOU 5330  CA  ASN B 354    12593  27497  18925   -766  -5331  -1617       C  
ATOM   5331  C   ASN B 354       4.055  -8.540   7.189  1.00157.31           C  
ANISOU 5331  C   ASN B 354    12682  27839  19248   -758  -4634  -1614       C  
ATOM   5332  O   ASN B 354       5.286  -8.508   7.276  1.00159.52           O  
ANISOU 5332  O   ASN B 354    13292  28363  18955   -724  -4311  -1659       O  
ATOM   5333  CB  ASN B 354       3.527 -10.691   6.012  1.00151.98           C  
ANISOU 5333  CB  ASN B 354    12433  27013  18298   -905  -5349  -1886       C  
ATOM   5334  CG  ASN B 354       2.871 -11.320   7.226  1.00147.07           C  
ANISOU 5334  CG  ASN B 354    11428  26145  18308  -1058  -5041  -2037       C  
ATOM   5335  OD1 ASN B 354       2.061 -10.691   7.905  1.00147.94           O  
ANISOU 5335  OD1 ASN B 354    11054  26063  19094  -1066  -4910  -1929       O  
ATOM   5336  ND2 ASN B 354       3.223 -12.570   7.507  1.00142.34           N  
ANISOU 5336  ND2 ASN B 354    11065  25524  17494  -1174  -4896  -2277       N  
ATOM   5337  N   GLU B 355       3.249  -8.040   8.129  1.00154.61           N  
ANISOU 5337  N   GLU B 355    11851  27260  19634   -789  -4399  -1550       N  
ATOM   5338  CA  GLU B 355       3.756  -7.263   9.252  1.00142.83           C  
ANISOU 5338  CA  GLU B 355    10223  25775  18271   -766  -3774  -1500       C  
ATOM   5339  C   GLU B 355       3.887  -8.050  10.553  1.00139.36           C  
ANISOU 5339  C   GLU B 355     9752  25166  18031   -913  -3254  -1728       C  
ATOM   5340  O   GLU B 355       4.534  -7.561  11.483  1.00132.64           O  
ANISOU 5340  O   GLU B 355     8934  24315  17148   -906  -2728  -1721       O  
ATOM   5341  CB  GLU B 355       2.866  -6.035   9.490  1.00136.30           C  
ANISOU 5341  CB  GLU B 355     8949  24750  18088   -680  -3769  -1248       C  
ATOM   5342  CG  GLU B 355       3.219  -4.847   8.609  1.00131.18           C  
ANISOU 5342  CG  GLU B 355     8392  24318  17134   -502  -4001   -986       C  
ATOM   5343  CD  GLU B 355       2.601  -3.552   9.096  1.00129.70           C  
ANISOU 5343  CD  GLU B 355     7805  23940  17537   -413  -3823   -745       C  
ATOM   5344  OE1 GLU B 355       1.533  -3.607   9.742  1.00130.67           O  
ANISOU 5344  OE1 GLU B 355     7525  23720  18405   -477  -3740   -749       O  
ATOM   5345  OE2 GLU B 355       3.185  -2.479   8.836  1.00128.74           O  
ANISOU 5345  OE2 GLU B 355     7778  23992  17147   -274  -3747   -540       O  
ATOM   5346  N   ASP B 356       3.310  -9.250  10.647  1.00144.61           N  
ANISOU 5346  N   ASP B 356    10390  25666  18890  -1045  -3393  -1920       N  
ATOM   5347  CA  ASP B 356       3.513 -10.074  11.839  1.00146.03           C  
ANISOU 5347  CA  ASP B 356    10613  25693  19178  -1181  -2908  -2143       C  
ATOM   5348  C   ASP B 356       4.938 -10.619  11.886  1.00144.81           C  
ANISOU 5348  C   ASP B 356    10936  25799  18288  -1206  -2684  -2314       C  
ATOM   5349  O   ASP B 356       5.661 -10.447  12.883  1.00146.51           O  
ANISOU 5349  O   ASP B 356    11253  25994  18420  -1234  -2172  -2374       O  
ATOM   5350  CB  ASP B 356       2.490 -11.214  11.850  1.00148.54           C  
ANISOU 5350  CB  ASP B 356    10769  25766  19902  -1307  -3145  -2276       C  
ATOM   5351  CG  ASP B 356       2.348 -11.871  13.210  1.00144.27           C  
ANISOU 5351  CG  ASP B 356    10167  24975  19674  -1435  -2624  -2449       C  
ATOM   5352  OD1 ASP B 356       3.322 -11.868  13.991  1.00138.12           O  
ANISOU 5352  OD1 ASP B 356     9646  24264  18571  -1454  -2154  -2557       O  
ATOM   5353  OD2 ASP B 356       1.253 -12.400  13.497  1.00145.99           O  
ANISOU 5353  OD2 ASP B 356    10093  24908  20467  -1518  -2694  -2464       O  
ATOM   5354  N   VAL B 357       5.358 -11.279  10.804  1.00138.90           N  
ANISOU 5354  N   VAL B 357    10508  25257  17012  -1194  -3067  -2381       N  
ATOM   5355  CA  VAL B 357       6.746 -11.702  10.682  1.00123.68           C  
ANISOU 5355  CA  VAL B 357     9032  23574  14389  -1194  -2874  -2500       C  
ATOM   5356  C   VAL B 357       7.670 -10.496  10.738  1.00118.41           C  
ANISOU 5356  C   VAL B 357     8423  23115  13454  -1075  -2631  -2322       C  
ATOM   5357  O   VAL B 357       8.789 -10.589  11.249  1.00111.30           O  
ANISOU 5357  O   VAL B 357     7748  22320  12220  -1098  -2262  -2401       O  
ATOM   5358  CB  VAL B 357       6.942 -12.515   9.386  1.00116.04           C  
ANISOU 5358  CB  VAL B 357     8429  22731  12929  -1173  -3329  -2555       C  
ATOM   5359  CG1 VAL B 357       8.360 -13.062   9.305  1.00107.29           C  
ANISOU 5359  CG1 VAL B 357     7786  21811  11168  -1175  -3071  -2678       C  
ATOM   5360  CG2 VAL B 357       5.922 -13.642   9.310  1.00113.29           C  
ANISOU 5360  CG2 VAL B 357     7989  22140  12914  -1287  -3616  -2696       C  
ATOM   5361  N   ILE B 358       7.212  -9.342  10.245  1.00122.10           N  
ANISOU 5361  N   ILE B 358     8677  23622  14095   -948  -2837  -2067       N  
ATOM   5362  CA  ILE B 358       8.028  -8.132  10.302  1.00117.87           C  
ANISOU 5362  CA  ILE B 358     8171  23266  13348   -825  -2608  -1866       C  
ATOM   5363  C   ILE B 358       8.229  -7.681  11.745  1.00118.16           C  
ANISOU 5363  C   ILE B 358     8052  23116  13727   -873  -2037  -1877       C  
ATOM   5364  O   ILE B 358       9.322  -7.247  12.124  1.00120.40           O  
ANISOU 5364  O   ILE B 358     8514  23510  13724   -841  -1710  -1836       O  
ATOM   5365  CB  ILE B 358       7.402  -7.023   9.433  1.00116.46           C  
ANISOU 5365  CB  ILE B 358     7810  23137  13304   -673  -2979  -1582       C  
ATOM   5366  CG1 ILE B 358       8.022  -7.036   8.035  1.00120.59           C  
ANISOU 5366  CG1 ILE B 358     8721  23940  13159   -563  -3356  -1502       C  
ATOM   5367  CG2 ILE B 358       7.566  -5.653  10.080  1.00109.02           C  
ANISOU 5367  CG2 ILE B 358     6655  22159  12611   -578  -2632  -1359       C  
ATOM   5368  CD1 ILE B 358       7.566  -5.896   7.157  1.00125.34           C  
ANISOU 5368  CD1 ILE B 358     9233  24590  13803   -401  -3709  -1209       C  
ATOM   5369  N   GLY B 359       7.188  -7.777  12.575  1.00118.19           N  
ANISOU 5369  N   GLY B 359     7760  22788  14359   -948  -1901  -1919       N  
ATOM   5370  CA  GLY B 359       7.349  -7.438  13.980  1.00101.38           C  
ANISOU 5370  CA  GLY B 359     5592  20403  12524   -995  -1342  -1940       C  
ATOM   5371  C   GLY B 359       8.292  -8.386  14.696  1.00 97.55           C  
ANISOU 5371  C   GLY B 359     5439  19911  11715  -1117  -1031  -2187       C  
ATOM   5372  O   GLY B 359       9.122  -7.959  15.510  1.00105.11           O  
ANISOU 5372  O   GLY B 359     6570  20799  12568  -1116   -634  -2170       O  
ATOM   5373  N   ALA B 360       8.183  -9.684  14.401  1.00 98.00           N  
ANISOU 5373  N   ALA B 360     5611  20006  11617  -1222  -1226  -2413       N  
ATOM   5374  CA  ALA B 360       9.136 -10.638  14.969  1.00 94.48           C  
ANISOU 5374  CA  ALA B 360     5501  19572  10826  -1333   -974  -2649       C  
ATOM   5375  C   ALA B 360      10.566 -10.313  14.536  1.00103.28           C  
ANISOU 5375  C   ALA B 360     6897  20983  11360  -1268   -923  -2595       C  
ATOM   5376  O   ALA B 360      11.501 -10.337  15.355  1.00102.18           O  
ANISOU 5376  O   ALA B 360     6964  20779  11082  -1315   -566  -2662       O  
ATOM   5377  CB  ALA B 360       8.758 -12.063  14.562  1.00 95.73           C  
ANISOU 5377  CB  ALA B 360     5748  19729  10897  -1435  -1230  -2873       C  
ATOM   5378  N   LEU B 361      10.748 -10.001  13.249  1.00 99.18           N  
ANISOU 5378  N   LEU B 361     6413  20760  10512  -1156  -1285  -2461       N  
ATOM   5379  CA  LEU B 361      12.059  -9.618  12.737  1.00 95.55           C  
ANISOU 5379  CA  LEU B 361     6241  20533   9529  -1065  -1223  -2361       C  
ATOM   5380  C   LEU B 361      12.585  -8.380  13.445  1.00 98.02           C  
ANISOU 5380  C   LEU B 361     6543  20713   9985   -983   -858  -2150       C  
ATOM   5381  O   LEU B 361      13.775  -8.301  13.765  1.00101.51           O  
ANISOU 5381  O   LEU B 361     7252  21149  10168   -976   -592  -2142       O  
ATOM   5382  CB  LEU B 361      11.987  -9.369  11.230  1.00 95.79           C  
ANISOU 5382  CB  LEU B 361     6385  20789   9223   -928  -1652  -2204       C  
ATOM   5383  CG  LEU B 361      11.738 -10.548  10.287  1.00 98.06           C  
ANISOU 5383  CG  LEU B 361     6859  21184   9215   -972  -2036  -2373       C  
ATOM   5384  CD1 LEU B 361      11.774 -10.084   8.838  1.00101.36           C  
ANISOU 5384  CD1 LEU B 361     7462  21793   9257   -815  -2425  -2180       C  
ATOM   5385  CD2 LEU B 361      12.745 -11.660  10.522  1.00 95.26           C  
ANISOU 5385  CD2 LEU B 361     6860  20826   8509  -1061  -1806  -2592       C  
ATOM   5386  N   LEU B 362      11.719  -7.392  13.678  1.00 92.01           N  
ANISOU 5386  N   LEU B 362     5475  19830   9656   -917   -856  -1969       N  
ATOM   5387  CA  LEU B 362      12.158  -6.168  14.338  1.00 90.26           C  
ANISOU 5387  CA  LEU B 362     5250  19469   9577   -834   -526  -1760       C  
ATOM   5388  C   LEU B 362      12.583  -6.442  15.773  1.00106.22           C  
ANISOU 5388  C   LEU B 362     7366  21242  11750   -958    -92  -1915       C  
ATOM   5389  O   LEU B 362      13.581  -5.884  16.243  1.00106.76           O  
ANISOU 5389  O   LEU B 362     7644  21235  11685   -922    169  -1823       O  
ATOM   5390  CB  LEU B 362      11.056  -5.112  14.288  1.00 92.94           C  
ANISOU 5390  CB  LEU B 362     5229  19713  10371   -741   -617  -1546       C  
ATOM   5391  CG  LEU B 362      11.042  -4.272  13.009  1.00 95.54           C  
ANISOU 5391  CG  LEU B 362     5559  20243  10499   -566   -949  -1282       C  
ATOM   5392  CD1 LEU B 362       9.959  -3.204  13.065  1.00105.41           C  
ANISOU 5392  CD1 LEU B 362     6434  21368  12249   -480  -1023  -1070       C  
ATOM   5393  CD2 LEU B 362      12.408  -3.645  12.772  1.00 93.36           C  
ANISOU 5393  CD2 LEU B 362     5609  20066   9798   -462   -771  -1124       C  
ATOM   5394  N   ASN B 363      11.855  -7.313  16.477  1.00103.10           N  
ANISOU 5394  N   ASN B 363     6924  20619  11631  -1092    -20  -2132       N  
ATOM   5395  CA  ASN B 363      12.289  -7.739  17.806  1.00 83.89           C  
ANISOU 5395  CA  ASN B 363     4750  17854   9270  -1206    357  -2288       C  
ATOM   5396  C   ASN B 363      13.708  -8.299  17.753  1.00102.35           C  
ANISOU 5396  C   ASN B 363     7420  20338  11131  -1252    416  -2399       C  
ATOM   5397  O   ASN B 363      14.630  -7.811  18.433  1.00103.74           O  
ANISOU 5397  O   ASN B 363     7839  20338  11238  -1238    664  -2329       O  
ATOM   5398  CB  ASN B 363      11.333  -8.804  18.352  1.00 84.74           C  
ANISOU 5398  CB  ASN B 363     4791  17741   9665  -1339    375  -2518       C  
ATOM   5399  CG  ASN B 363       9.927  -8.285  18.563  1.00 87.67           C  
ANISOU 5399  CG  ASN B 363     4818  17888  10604  -1303    380  -2405       C  
ATOM   5400  OD1 ASN B 363       9.725  -7.118  18.882  1.00 88.06           O  
ANISOU 5400  OD1 ASN B 363     4768  17791  10898  -1206    539  -2188       O  
ATOM   5401  ND2 ASN B 363       8.943  -9.158  18.383  1.00 89.91           N  
ANISOU 5401  ND2 ASN B 363     4913  18122  11127  -1378    207  -2541       N  
ATOM   5402  N   VAL B 364      13.890  -9.327  16.917  1.00 91.78           N  
ANISOU 5402  N   VAL B 364     6105  19291   9478  -1304    165  -2564       N  
ATOM   5403  CA  VAL B 364      15.178 -10.014  16.833  1.00 84.51           C  
ANISOU 5403  CA  VAL B 364     5470  18502   8138  -1359    225  -2693       C  
ATOM   5404  C   VAL B 364      16.291  -9.040  16.462  1.00 81.94           C  
ANISOU 5404  C   VAL B 364     5316  18236   7583  -1217    307  -2442       C  
ATOM   5405  O   VAL B 364      17.386  -9.073  17.040  1.00 76.63           O  
ANISOU 5405  O   VAL B 364     4873  17446   6797  -1252    528  -2464       O  
ATOM   5406  CB  VAL B 364      15.089 -11.182  15.833  1.00 86.08           C  
ANISOU 5406  CB  VAL B 364     5733  18948   8027  -1399    -89  -2865       C  
ATOM   5407  CG1 VAL B 364      16.449 -11.832  15.648  1.00 90.68           C  
ANISOU 5407  CG1 VAL B 364     6657  19614   8183  -1425     -9  -2959       C  
ATOM   5408  CG2 VAL B 364      14.061 -12.202  16.302  1.00 81.47           C  
ANISOU 5408  CG2 VAL B 364     5076  18181   7700  -1527   -134  -3094       C  
ATOM   5409  N   PHE B 365      16.025  -8.138  15.517  1.00 80.51           N  
ANISOU 5409  N   PHE B 365     5023  18210   7359  -1058    126  -2192       N  
ATOM   5410  CA  PHE B 365      17.084  -7.289  14.984  1.00 93.64           C  
ANISOU 5410  CA  PHE B 365     6852  19953   8772   -915    188  -1951       C  
ATOM   5411  C   PHE B 365      17.427  -6.148  15.934  1.00 91.19           C  
ANISOU 5411  C   PHE B 365     6520  19407   8722   -876    472  -1774       C  
ATOM   5412  O   PHE B 365      18.597  -5.760  16.039  1.00100.33           O  
ANISOU 5412  O   PHE B 365     7869  20516   9735   -831    631  -1665       O  
ATOM   5413  CB  PHE B 365      16.678  -6.753  13.609  1.00 88.62           C  
ANISOU 5413  CB  PHE B 365     6152  19556   7966   -757   -115  -1749       C  
ATOM   5414  CG  PHE B 365      16.474  -7.827  12.571  1.00 90.23           C  
ANISOU 5414  CG  PHE B 365     6465  19976   7841   -779   -422  -1902       C  
ATOM   5415  CD1 PHE B 365      16.870  -9.134  12.813  1.00 87.85           C  
ANISOU 5415  CD1 PHE B 365     6325  19683   7371   -918   -382  -2182       C  
ATOM   5416  CD2 PHE B 365      15.882  -7.532  11.358  1.00 88.76           C  
ANISOU 5416  CD2 PHE B 365     6248  19968   7509   -663   -769  -1767       C  
ATOM   5417  CE1 PHE B 365      16.678 -10.123  11.866  1.00 86.80           C  
ANISOU 5417  CE1 PHE B 365     6318  19735   6926   -938   -667  -2324       C  
ATOM   5418  CE2 PHE B 365      15.691  -8.517  10.405  1.00 90.86           C  
ANISOU 5418  CE2 PHE B 365     6667  20403   7451   -683  -1076  -1908       C  
ATOM   5419  CZ  PHE B 365      16.088  -9.814  10.660  1.00 89.33           C  
ANISOU 5419  CZ  PHE B 365     6632  20220   7088   -819  -1018  -2188       C  
ATOM   5420  N   VAL B 366      16.431  -5.606  16.642  1.00 80.97           N  
ANISOU 5420  N   VAL B 366     4997  17937   7829   -891    546  -1741       N  
ATOM   5421  CA  VAL B 366      16.720  -4.666  17.719  1.00 77.04           C  
ANISOU 5421  CA  VAL B 366     4590  17102   7578   -871    826  -1609       C  
ATOM   5422  C   VAL B 366      17.645  -5.309  18.740  1.00 74.28           C  
ANISOU 5422  C   VAL B 366     4614  16435   7173   -992   1012  -1773       C  
ATOM   5423  O   VAL B 366      18.623  -4.695  19.193  1.00 80.04           O  
ANISOU 5423  O   VAL B 366     5566  16959   7887   -955   1141  -1641       O  
ATOM   5424  CB  VAL B 366      15.411  -4.174  18.368  1.00 79.55           C  
ANISOU 5424  CB  VAL B 366     4711  17162   8352   -872    893  -1572       C  
ATOM   5425  CG1 VAL B 366      15.683  -3.583  19.744  1.00 76.38           C  
ANISOU 5425  CG1 VAL B 366     4543  16290   8186   -896   1202  -1525       C  
ATOM   5426  CG2 VAL B 366      14.730  -3.148  17.480  1.00 82.80           C  
ANISOU 5426  CG2 VAL B 366     4796  17791   8872   -719    718  -1322       C  
ATOM   5427  N   TRP B 367      17.384  -6.572  19.092  1.00 73.40           N  
ANISOU 5427  N   TRP B 367     4578  16272   7040  -1139    992  -2058       N  
ATOM   5428  CA  TRP B 367      18.228  -7.172  20.122  1.00 79.26           C  
ANISOU 5428  CA  TRP B 367     5677  16681   7755  -1256   1134  -2207       C  
ATOM   5429  C   TRP B 367      19.616  -7.537  19.596  1.00 79.10           C  
ANISOU 5429  C   TRP B 367     5857  16789   7410  -1247   1073  -2202       C  
ATOM   5430  O   TRP B 367      20.593  -7.479  20.352  1.00 82.15           O  
ANISOU 5430  O   TRP B 367     6515  16865   7831  -1285   1166  -2187       O  
ATOM   5431  CB  TRP B 367      17.520  -8.369  20.750  1.00 88.76           C  
ANISOU 5431  CB  TRP B 367     6918  17748   9059  -1413   1153  -2501       C  
ATOM   5432  CG  TRP B 367      16.432  -7.898  21.663  1.00 99.14           C  
ANISOU 5432  CG  TRP B 367     8145  18752  10770  -1423   1323  -2477       C  
ATOM   5433  CD1 TRP B 367      15.091  -8.112  21.527  1.00108.33           C  
ANISOU 5433  CD1 TRP B 367     9026  19952  12183  -1436   1290  -2534       C  
ATOM   5434  CD2 TRP B 367      16.590  -7.058  22.813  1.00 97.63           C  
ANISOU 5434  CD2 TRP B 367     8137  18158  10799  -1409   1566  -2365       C  
ATOM   5435  NE1 TRP B 367      14.408  -7.488  22.545  1.00111.40           N  
ANISOU 5435  NE1 TRP B 367     9413  19969  12944  -1429   1534  -2464       N  
ATOM   5436  CE2 TRP B 367      15.306  -6.833  23.346  1.00105.40           C  
ANISOU 5436  CE2 TRP B 367     8952  18951  12146  -1413   1711  -2367       C  
ATOM   5437  CE3 TRP B 367      17.695  -6.490  23.456  1.00 90.24           C  
ANISOU 5437  CE3 TRP B 367     7489  16992   9805  -1397   1672  -2265       C  
ATOM   5438  CZ2 TRP B 367      15.098  -6.064  24.489  1.00103.61           C  
ANISOU 5438  CZ2 TRP B 367     8861  18328  12178  -1399   1992  -2277       C  
ATOM   5439  CZ3 TRP B 367      17.486  -5.728  24.588  1.00 88.98           C  
ANISOU 5439  CZ3 TRP B 367     7460  16457   9891  -1392   1914  -2186       C  
ATOM   5440  CH2 TRP B 367      16.197  -5.517  25.089  1.00 95.69           C  
ANISOU 5440  CH2 TRP B 367     8164  17137  11057  -1390   2086  -2195       C  
ATOM   5441  N   ILE B 368      19.743  -7.867  18.309  1.00 80.35           N  
ANISOU 5441  N   ILE B 368     5875  17383   7272  -1191    921  -2199       N  
ATOM   5442  CA  ILE B 368      21.074  -8.062  17.725  1.00 80.07           C  
ANISOU 5442  CA  ILE B 368     6030  17431   6961  -1149    908  -2140       C  
ATOM   5443  C   ILE B 368      21.866  -6.754  17.746  1.00 69.32           C  
ANISOU 5443  C   ILE B 368     4729  15927   5680  -1015   1006  -1830       C  
ATOM   5444  O   ILE B 368      23.056  -6.717  18.111  1.00 67.54           O  
ANISOU 5444  O   ILE B 368     4733  15445   5482  -1023   1070  -1772       O  
ATOM   5445  CB  ILE B 368      20.958  -8.628  16.298  1.00 78.76           C  
ANISOU 5445  CB  ILE B 368     5727  17781   6417  -1097    771  -2192       C  
ATOM   5446  CG1 ILE B 368      20.263  -9.991  16.313  1.00 72.40           C  
ANISOU 5446  CG1 ILE B 368     4905  17055   5548  -1239    638  -2507       C  
ATOM   5447  CG2 ILE B 368      22.332  -8.737  15.651  1.00 75.16           C  
ANISOU 5447  CG2 ILE B 368     5523  17307   5726  -1024    786  -2083       C  
ATOM   5448  CD1 ILE B 368      20.900 -10.997  17.245  1.00 69.78           C  
ANISOU 5448  CD1 ILE B 368     4835  16385   5294  -1397    693  -2715       C  
ATOM   5449  N   GLY B 369      21.221  -5.661  17.328  1.00 71.06           N  
ANISOU 5449  N   GLY B 369     4716  16311   5972   -889   1002  -1619       N  
ATOM   5450  CA  GLY B 369      21.884  -4.370  17.360  1.00 72.60           C  
ANISOU 5450  CA  GLY B 369     4952  16372   6259   -761   1094  -1320       C  
ATOM   5451  C   GLY B 369      22.317  -3.979  18.759  1.00 79.05           C  
ANISOU 5451  C   GLY B 369     5973  16695   7366   -827   1233  -1307       C  
ATOM   5452  O   GLY B 369      23.368  -3.362  18.946  1.00 84.08           O  
ANISOU 5452  O   GLY B 369     6744  17154   8050   -776   1305  -1139       O  
ATOM   5453  N   TYR B 370      21.510  -4.331  19.762  1.00 80.01           N  
ANISOU 5453  N   TYR B 370     6117  16593   7688   -941   1285  -1482       N  
ATOM   5454  CA  TYR B 370      21.929  -4.104  21.142  1.00 72.87           C  
ANISOU 5454  CA  TYR B 370     5445  15245   6999  -1020   1432  -1507       C  
ATOM   5455  C   TYR B 370      23.095  -5.006  21.531  1.00 63.74           C  
ANISOU 5455  C   TYR B 370     4549  13925   5745  -1129   1415  -1655       C  
ATOM   5456  O   TYR B 370      23.962  -4.593  22.309  1.00 62.24           O  
ANISOU 5456  O   TYR B 370     4532  13453   5663  -1153   1499  -1588       O  
ATOM   5457  CB  TYR B 370      20.748  -4.306  22.090  1.00 66.02           C  
ANISOU 5457  CB  TYR B 370     4558  14173   6352  -1108   1533  -1659       C  
ATOM   5458  CG  TYR B 370      19.797  -3.132  22.122  1.00 67.66           C  
ANISOU 5458  CG  TYR B 370     4554  14369   6786  -1001   1616  -1466       C  
ATOM   5459  CD1 TYR B 370      20.239  -1.851  21.826  1.00 67.94           C  
ANISOU 5459  CD1 TYR B 370     4533  14426   6853   -862   1637  -1179       C  
ATOM   5460  CD2 TYR B 370      18.457  -3.305  22.442  1.00 84.82           C  
ANISOU 5460  CD2 TYR B 370     6568  16488   9172  -1035   1677  -1563       C  
ATOM   5461  CE1 TYR B 370      19.377  -0.772  21.852  1.00 86.35           C  
ANISOU 5461  CE1 TYR B 370     6669  16736   9402   -761   1706   -998       C  
ATOM   5462  CE2 TYR B 370      17.585  -2.232  22.471  1.00 88.60           C  
ANISOU 5462  CE2 TYR B 370     6833  16926   9904   -933   1759  -1377       C  
ATOM   5463  CZ  TYR B 370      18.051  -0.968  22.174  1.00 87.96           C  
ANISOU 5463  CZ  TYR B 370     6713  16879   9830   -797   1767  -1098       C  
ATOM   5464  OH  TYR B 370      17.191   0.106  22.200  1.00 86.42           O  
ANISOU 5464  OH  TYR B 370     6306  16637   9894   -693   1843   -910       O  
ATOM   5465  N   LEU B 371      23.130  -6.235  21.007  1.00 63.82           N  
ANISOU 5465  N   LEU B 371     4573  14112   5565  -1201   1301  -1856       N  
ATOM   5466  CA  LEU B 371      24.241  -7.145  21.281  1.00 62.09           C  
ANISOU 5466  CA  LEU B 371     4575  13740   5278  -1299   1268  -1987       C  
ATOM   5467  C   LEU B 371      25.572  -6.596  20.774  1.00 63.38           C  
ANISOU 5467  C   LEU B 371     4778  13901   5402  -1201   1283  -1771       C  
ATOM   5468  O   LEU B 371      26.626  -6.889  21.353  1.00 60.25           O  
ANISOU 5468  O   LEU B 371     4550  13265   5076  -1272   1310  -1808       O  
ATOM   5469  CB  LEU B 371      23.949  -8.508  20.650  1.00 62.59           C  
ANISOU 5469  CB  LEU B 371     4611  14024   5148  -1376   1136  -2217       C  
ATOM   5470  CG  LEU B 371      24.989  -9.622  20.769  1.00 61.11           C  
ANISOU 5470  CG  LEU B 371     4610  13700   4910  -1478   1076  -2359       C  
ATOM   5471  CD1 LEU B 371      25.073 -10.129  22.197  1.00 59.16           C  
ANISOU 5471  CD1 LEU B 371     4563  13069   4847  -1641   1121  -2536       C  
ATOM   5472  CD2 LEU B 371      24.658 -10.757  19.811  1.00 62.21           C  
ANISOU 5472  CD2 LEU B 371     4665  14123   4850  -1507    941  -2512       C  
ATOM   5473  N   SER B 372      25.547  -5.823  19.686  1.00 63.50           N  
ANISOU 5473  N   SER B 372     4629  14184   5314  -1041   1274  -1547       N  
ATOM   5474  CA  SER B 372      26.786  -5.214  19.182  1.00 63.53           C  
ANISOU 5474  CA  SER B 372     4662  14163   5315   -933   1328  -1313       C  
ATOM   5475  C   SER B 372      27.525  -4.410  20.262  1.00 80.63           C  
ANISOU 5475  C   SER B 372     6917  15978   7739   -955   1429  -1193       C  
ATOM   5476  O   SER B 372      28.774  -4.392  20.315  1.00 79.90           O  
ANISOU 5476  O   SER B 372     6896  15746   7718   -955   1472  -1112       O  
ATOM   5477  CB  SER B 372      26.472  -4.322  17.981  1.00 65.76           C  
ANISOU 5477  CB  SER B 372     4762  14763   5462   -752   1325  -1071       C  
ATOM   5478  OG  SER B 372      25.854  -3.115  18.394  1.00 66.07           O  
ANISOU 5478  OG  SER B 372     4688  14742   5673   -688   1370   -903       O  
ATOM   5479  N   SER B 373      26.763  -3.733  21.132  1.00 61.71           N  
ANISOU 5479  N   SER B 373     4507  13440   5501   -978   1480  -1177       N  
ATOM   5480  CA  SER B 373      27.363  -2.904  22.174  1.00 63.88           C  
ANISOU 5480  CA  SER B 373     4867  13411   5992  -1005   1578  -1066       C  
ATOM   5481  C   SER B 373      28.176  -3.741  23.150  1.00 58.75           C  
ANISOU 5481  C   SER B 373     4422  12506   5394  -1181   1587  -1270       C  
ATOM   5482  O   SER B 373      29.178  -3.264  23.693  1.00 64.32           O  
ANISOU 5482  O   SER B 373     5174  13026   6238  -1216   1637  -1168       O  
ATOM   5483  CB  SER B 373      26.273  -2.128  22.916  1.00 60.84           C  
ANISOU 5483  CB  SER B 373     4454  12921   5741  -1002   1659  -1038       C  
ATOM   5484  OG  SER B 373      25.502  -1.344  22.021  1.00 62.64           O  
ANISOU 5484  OG  SER B 373     4467  13390   5944   -846   1639   -851       O  
ATOM   5485  N   ALA B 374      27.758  -4.983  23.391  1.00 58.19           N  
ANISOU 5485  N   ALA B 374     4458  12426   5226  -1306   1532  -1557       N  
ATOM   5486  CA  ALA B 374      28.570  -5.907  24.167  1.00 60.51           C  
ANISOU 5486  CA  ALA B 374     4947  12506   5539  -1475   1517  -1766       C  
ATOM   5487  C   ALA B 374      29.659  -6.542  23.318  1.00 69.48           C  
ANISOU 5487  C   ALA B 374     6045  13751   6604  -1448   1453  -1744       C  
ATOM   5488  O   ALA B 374      30.662  -7.016  23.864  1.00 68.08           O  
ANISOU 5488  O   ALA B 374     5971  13395   6501  -1565   1457  -1835       O  
ATOM   5489  CB  ALA B 374      27.695  -6.999  24.782  1.00 58.64           C  
ANISOU 5489  CB  ALA B 374     4850  12184   5246  -1616   1484  -2072       C  
ATOM   5490  N   VAL B 375      29.464  -6.579  21.999  1.00 72.85           N  
ANISOU 5490  N   VAL B 375     6332  14462   6884  -1308   1412  -1636       N  
ATOM   5491  CA  VAL B 375      30.444  -7.202  21.113  1.00 72.87           C  
ANISOU 5491  CA  VAL B 375     6325  14557   6806  -1269   1397  -1611       C  
ATOM   5492  C   VAL B 375      31.764  -6.444  21.159  1.00 73.50           C  
ANISOU 5492  C   VAL B 375     6356  14493   7076  -1215   1497  -1381       C  
ATOM   5493  O   VAL B 375      32.843  -7.049  21.135  1.00 74.37           O  
ANISOU 5493  O   VAL B 375     6498  14504   7257  -1266   1522  -1419       O  
ATOM   5494  CB  VAL B 375      29.888  -7.286  19.679  1.00 74.80           C  
ANISOU 5494  CB  VAL B 375     6457  15143   6819  -1131   1360  -1538       C  
ATOM   5495  CG1 VAL B 375      31.007  -7.533  18.677  1.00 62.67           C  
ANISOU 5495  CG1 VAL B 375     4920  13671   5221  -1041   1423  -1419       C  
ATOM   5496  CG2 VAL B 375      28.844  -8.383  19.587  1.00 84.08           C  
ANISOU 5496  CG2 VAL B 375     7652  16459   7838  -1224   1239  -1802       C  
ATOM   5497  N   ASN B 376      31.698  -5.113  21.223  1.00 74.58           N  
ANISOU 5497  N   ASN B 376     6392  14610   7334  -1114   1558  -1130       N  
ATOM   5498  CA  ASN B 376      32.918  -4.302  21.110  1.00 72.72           C  
ANISOU 5498  CA  ASN B 376     6059  14255   7317  -1045   1645   -863       C  
ATOM   5499  C   ASN B 376      34.062  -4.724  22.044  1.00 66.15           C  
ANISOU 5499  C   ASN B 376     5276  13131   6725  -1208   1637   -946       C  
ATOM   5500  O   ASN B 376      35.193  -4.916  21.554  1.00 59.84           O  
ANISOU 5500  O   ASN B 376     4405  12271   6060  -1172   1686   -838       O  
ATOM   5501  CB  ASN B 376      32.571  -2.821  21.328  1.00 74.56           C  
ANISOU 5501  CB  ASN B 376     6194  14461   7675   -948   1682   -609       C  
ATOM   5502  CG  ASN B 376      32.531  -2.030  20.036  1.00 77.90           C  
ANISOU 5502  CG  ASN B 376     6491  15087   8019   -732   1734   -335       C  
ATOM   5503  OD1 ASN B 376      31.534  -2.040  19.315  1.00 87.44           O  
ANISOU 5503  OD1 ASN B 376     7678  16541   9005   -653   1698   -359       O  
ATOM   5504  ND2 ASN B 376      33.617  -1.327  19.744  1.00 70.88           N  
ANISOU 5504  ND2 ASN B 376     5507  14094   7328   -644   1820    -70       N  
ATOM   5505  N   PRO B 377      33.863  -4.881  23.361  1.00 65.55           N  
ANISOU 5505  N   PRO B 377     5424  12714   6767  -1361   1514  -1109       N  
ATOM   5506  CA  PRO B 377      35.003  -5.236  24.229  1.00 58.36           C  
ANISOU 5506  CA  PRO B 377     4684  11348   6143  -1488   1382  -1151       C  
ATOM   5507  C   PRO B 377      35.621  -6.590  23.922  1.00 55.47           C  
ANISOU 5507  C   PRO B 377     4318  11035   5723  -1576   1380  -1353       C  
ATOM   5508  O   PRO B 377      36.832  -6.761  24.108  1.00 55.50           O  
ANISOU 5508  O   PRO B 377     4330  10745   6014  -1615   1312  -1284       O  
ATOM   5509  CB  PRO B 377      34.393  -5.204  25.637  1.00 60.72           C  
ANISOU 5509  CB  PRO B 377     5288  11313   6471  -1630   1265  -1321       C  
ATOM   5510  CG  PRO B 377      33.202  -4.325  25.512  1.00 65.52           C  
ANISOU 5510  CG  PRO B 377     5827  12122   6945  -1529   1365  -1232       C  
ATOM   5511  CD  PRO B 377      32.651  -4.620  24.158  1.00 68.67           C  
ANISOU 5511  CD  PRO B 377     5949  13062   7081  -1416   1494  -1228       C  
ATOM   5512  N   LEU B 378      34.825  -7.571  23.490  1.00 55.33           N  
ANISOU 5512  N   LEU B 378     4289  11358   5376  -1614   1440  -1601       N  
ATOM   5513  CA  LEU B 378      35.397  -8.839  23.050  1.00 55.29           C  
ANISOU 5513  CA  LEU B 378     4272  11445   5291  -1678   1461  -1779       C  
ATOM   5514  C   LEU B 378      36.371  -8.624  21.899  1.00 69.08           C  
ANISOU 5514  C   LEU B 378     5812  13316   7121  -1529   1604  -1540       C  
ATOM   5515  O   LEU B 378      37.444  -9.241  21.854  1.00 76.63           O  
ANISOU 5515  O   LEU B 378     6760  14093   8264  -1573   1611  -1557       O  
ATOM   5516  CB  LEU B 378      34.288  -9.806  22.639  1.00 55.37           C  
ANISOU 5516  CB  LEU B 378     4365  11717   4958  -1689   1425  -2018       C  
ATOM   5517  CG  LEU B 378      34.749 -11.090  21.946  1.00 56.51           C  
ANISOU 5517  CG  LEU B 378     4547  11927   4998  -1700   1398  -2151       C  
ATOM   5518  CD1 LEU B 378      35.508 -11.983  22.914  1.00 55.43           C  
ANISOU 5518  CD1 LEU B 378     4505  11561   4996  -1913   1367  -2392       C  
ATOM   5519  CD2 LEU B 378      33.568 -11.828  21.335  1.00 55.88           C  
ANISOU 5519  CD2 LEU B 378     4520  12047   4666  -1672   1284  -2280       C  
ATOM   5520  N   VAL B 379      36.010  -7.748  20.959  1.00 70.26           N  
ANISOU 5520  N   VAL B 379     5868  13659   7171  -1326   1683  -1291       N  
ATOM   5521  CA  VAL B 379      36.899  -7.440  19.844  1.00 70.44           C  
ANISOU 5521  CA  VAL B 379     5768  13719   7275  -1156   1835  -1032       C  
ATOM   5522  C   VAL B 379      38.184  -6.809  20.356  1.00 68.39           C  
ANISOU 5522  C   VAL B 379     5349  13164   7470  -1189   1884   -829       C  
ATOM   5523  O   VAL B 379      39.278  -7.108  19.862  1.00 61.15           O  
ANISOU 5523  O   VAL B 379     4338  12145   6754  -1149   2005   -728       O  
ATOM   5524  CB  VAL B 379      36.188  -6.527  18.829  1.00 72.79           C  
ANISOU 5524  CB  VAL B 379     6030  14246   7379   -951   1889   -813       C  
ATOM   5525  CG1 VAL B 379      37.049  -6.343  17.588  1.00 73.78           C  
ANISOU 5525  CG1 VAL B 379     6090  14411   7533   -779   2085   -580       C  
ATOM   5526  CG2 VAL B 379      34.829  -7.094  18.473  1.00 74.28           C  
ANISOU 5526  CG2 VAL B 379     6334  14684   7206   -955   1769  -1014       C  
ATOM   5527  N   TYR B 380      38.075  -5.916  21.345  1.00 68.06           N  
ANISOU 5527  N   TYR B 380     5374  12828   7657  -1230   1726   -735       N  
ATOM   5528  CA  TYR B 380      39.292  -5.371  21.947  1.00 69.86           C  
ANISOU 5528  CA  TYR B 380     5579  12575   8388  -1252   1628   -535       C  
ATOM   5529  C   TYR B 380      40.146  -6.470  22.572  1.00 71.99           C  
ANISOU 5529  C   TYR B 380     5946  12523   8885  -1418   1499   -727       C  
ATOM   5530  O   TYR B 380      41.378  -6.444  22.473  1.00 66.20           O  
ANISOU 5530  O   TYR B 380     5091  11507   8555  -1404   1508   -566       O  
ATOM   5531  CB  TYR B 380      38.952  -4.320  23.002  1.00 66.21           C  
ANISOU 5531  CB  TYR B 380     5247  11822   8089  -1286   1443   -441       C  
ATOM   5532  CG  TYR B 380      38.222  -3.109  22.481  1.00 68.16           C  
ANISOU 5532  CG  TYR B 380     5383  12319   8195  -1122   1551   -217       C  
ATOM   5533  CD1 TYR B 380      38.150  -2.841  21.121  1.00 66.22           C  
ANISOU 5533  CD1 TYR B 380     4926  12466   7771   -943   1781    -49       C  
ATOM   5534  CD2 TYR B 380      37.607  -2.227  23.356  1.00 73.25           C  
ANISOU 5534  CD2 TYR B 380     6165  12784   8882  -1143   1427   -172       C  
ATOM   5535  CE1 TYR B 380      37.478  -1.733  20.649  1.00 68.28           C  
ANISOU 5535  CE1 TYR B 380     5095  12942   7906   -795   1856    155       C  
ATOM   5536  CE2 TYR B 380      36.936  -1.118  22.896  1.00 75.85           C  
ANISOU 5536  CE2 TYR B 380     6383  13331   9105   -993   1521     33       C  
ATOM   5537  CZ  TYR B 380      36.874  -0.875  21.543  1.00 74.35           C  
ANISOU 5537  CZ  TYR B 380     5962  13538   8748   -822   1722    196       C  
ATOM   5538  OH  TYR B 380      36.201   0.231  21.090  1.00 78.22           O  
ANISOU 5538  OH  TYR B 380     6351  14233   9137   -676   1794    401       O  
ATOM   5539  N   THR B 381      39.505  -7.443  23.221  1.00 80.99           N  
ANISOU 5539  N   THR B 381     7295  13683   9797  -1577   1380  -1065       N  
ATOM   5540  CA  THR B 381      40.244  -8.500  23.909  1.00 80.28           C  
ANISOU 5540  CA  THR B 381     7330  13268   9904  -1748   1224  -1267       C  
ATOM   5541  C   THR B 381      40.970  -9.421  22.934  1.00 77.74           C  
ANISOU 5541  C   THR B 381     6838  13111   9590  -1708   1408  -1294       C  
ATOM   5542  O   THR B 381      42.100  -9.845  23.200  1.00 80.56           O  
ANISOU 5542  O   THR B 381     7159  13121  10331  -1774   1334  -1272       O  
ATOM   5543  CB  THR B 381      39.296  -9.316  24.789  1.00 84.74           C  
ANISOU 5543  CB  THR B 381     8176  13838  10185  -1918   1086  -1624       C  
ATOM   5544  OG1 THR B 381      38.474  -8.433  25.559  1.00 88.85           O  
ANISOU 5544  OG1 THR B 381     8860  14250  10647  -1928    996  -1592       O  
ATOM   5545  CG2 THR B 381      40.083 -10.218  25.729  1.00 82.24           C  
ANISOU 5545  CG2 THR B 381     8048  13086  10112  -2107    864  -1810       C  
ATOM   5546  N   LEU B 382      40.339  -9.745  21.804  1.00 74.21           N  
ANISOU 5546  N   LEU B 382     6299  13162   8734  -1599   1641  -1340       N  
ATOM   5547  CA  LEU B 382      40.896 -10.766  20.919  1.00 70.65           C  
ANISOU 5547  CA  LEU B 382     5765  12872   8209  -1572   1828  -1417       C  
ATOM   5548  C   LEU B 382      42.188 -10.301  20.253  1.00 71.05           C  
ANISOU 5548  C   LEU B 382     5596  12742   8657  -1441   2018  -1102       C  
ATOM   5549  O   LEU B 382      43.197 -11.016  20.274  1.00 75.14           O  
ANISOU 5549  O   LEU B 382     6057  13021   9470  -1494   2050  -1131       O  
ATOM   5550  CB  LEU B 382      39.864 -11.169  19.864  1.00 66.10           C  
ANISOU 5550  CB  LEU B 382     5261  12765   7091  -1459   1952  -1512       C  
ATOM   5551  CG  LEU B 382      38.620 -11.895  20.376  1.00 64.04           C  
ANISOU 5551  CG  LEU B 382     5212  12642   6480  -1578   1762  -1833       C  
ATOM   5552  CD1 LEU B 382      37.640 -12.143  19.241  1.00 68.33           C  
ANISOU 5552  CD1 LEU B 382     5861  13476   6624  -1429   1755  -1831       C  
ATOM   5553  CD2 LEU B 382      39.003 -13.202  21.054  1.00 56.93           C  
ANISOU 5553  CD2 LEU B 382     4401  11602   5629  -1781   1678  -2144       C  
ATOM   5554  N   PHE B 383      42.180  -9.109  19.657  1.00 58.04           N  
ANISOU 5554  N   PHE B 383     6338  11569   4145    709  -1146  -1110       N  
ATOM   5555  CA  PHE B 383      43.258  -8.673  18.775  1.00 65.89           C  
ANISOU 5555  CA  PHE B 383     7157  12910   4969   1077   -866  -1006       C  
ATOM   5556  C   PHE B 383      44.156  -7.606  19.398  1.00 68.15           C  
ANISOU 5556  C   PHE B 383     6963  13379   5552   1009   -587   -767       C  
ATOM   5557  O   PHE B 383      44.804  -6.850  18.667  1.00 75.06           O  
ANISOU 5557  O   PHE B 383     7573  14563   6382   1197   -320   -579       O  
ATOM   5558  CB  PHE B 383      42.676  -8.167  17.454  1.00 70.38           C  
ANISOU 5558  CB  PHE B 383     7762  13667   5311   1157   -814   -929       C  
ATOM   5559  CG  PHE B 383      41.808  -9.172  16.749  1.00 71.90           C  
ANISOU 5559  CG  PHE B 383     8448  13662   5210   1226  -1139  -1151       C  
ATOM   5560  CD1 PHE B 383      42.363 -10.110  15.894  1.00 74.37           C  
ANISOU 5560  CD1 PHE B 383     9129  13907   5221   1650  -1163  -1300       C  
ATOM   5561  CD2 PHE B 383      40.436  -9.176  16.940  1.00 69.16           C  
ANISOU 5561  CD2 PHE B 383     8203  13021   5054    834  -1378  -1149       C  
ATOM   5562  CE1 PHE B 383      41.565 -11.036  15.247  1.00 75.55           C  
ANISOU 5562  CE1 PHE B 383     9764  13688   5254   1646  -1456  -1454       C  
ATOM   5563  CE2 PHE B 383      39.635 -10.098  16.296  1.00 71.40           C  
ANISOU 5563  CE2 PHE B 383     8935  12967   5227    832  -1675  -1288       C  
ATOM   5564  CZ  PHE B 383      40.200 -11.029  15.448  1.00 74.15           C  
ANISOU 5564  CZ  PHE B 383     9671  13236   5268   1219  -1729  -1446       C  
ATOM   5565  N   ASN B 384      44.215  -7.525  20.725  1.00 62.16           N  
ANISOU 5565  N   ASN B 384     6100  12421   5095    751   -654   -760       N  
ATOM   5566  CA  ASN B 384      45.021  -6.501  21.385  1.00 58.62           C  
ANISOU 5566  CA  ASN B 384     5238  12092   4945    651   -461   -539       C  
ATOM   5567  C   ASN B 384      45.606  -7.080  22.663  1.00 60.76           C  
ANISOU 5567  C   ASN B 384     5559  12135   5392    613   -587   -641       C  
ATOM   5568  O   ASN B 384      44.861  -7.498  23.554  1.00 61.16           O  
ANISOU 5568  O   ASN B 384     5827  11880   5532    377   -784   -761       O  
ATOM   5569  CB  ASN B 384      44.185  -5.252  21.685  1.00 52.31           C  
ANISOU 5569  CB  ASN B 384     4229  11279   4368    276   -405   -345       C  
ATOM   5570  CG  ASN B 384      45.034  -4.049  22.054  1.00 47.34           C  
ANISOU 5570  CG  ASN B 384     3181  10804   4001    202   -207    -88       C  
ATOM   5571  OD1 ASN B 384      46.065  -4.176  22.714  1.00 50.27           O  
ANISOU 5571  OD1 ASN B 384     3427  11153   4520    278   -207    -70       O  
ATOM   5572  ND2 ASN B 384      44.605  -2.869  21.620  1.00 46.56           N  
ANISOU 5572  ND2 ASN B 384     2866  10853   3971     47    -61    122       N  
ATOM   5573  N   LYS B 385      46.940  -7.103  22.746  1.00 62.28           N  
ANISOU 5573  N   LYS B 385     5542  12479   5642    855   -469   -572       N  
ATOM   5574  CA  LYS B 385      47.610  -7.708  23.894  1.00 63.05           C  
ANISOU 5574  CA  LYS B 385     5692  12374   5888    865   -603   -672       C  
ATOM   5575  C   LYS B 385      47.457  -6.859  25.150  1.00 54.14           C  
ANISOU 5575  C   LYS B 385     4408  11060   5104    497   -667   -556       C  
ATOM   5576  O   LYS B 385      47.317  -7.398  26.255  1.00 60.09           O  
ANISOU 5576  O   LYS B 385     5370  11516   5947    380   -853   -692       O  
ATOM   5577  CB  LYS B 385      49.092  -7.916  23.576  1.00 74.48           C  
ANISOU 5577  CB  LYS B 385     6916  14056   7326   1237   -457   -589       C  
ATOM   5578  CG  LYS B 385      49.367  -8.942  22.488  1.00 82.96           C  
ANISOU 5578  CG  LYS B 385     8235  15267   8020   1682   -399   -730       C  
ATOM   5579  CD  LYS B 385      50.862  -9.139  22.281  1.00 87.50           C  
ANISOU 5579  CD  LYS B 385     8558  16074   8615   2074   -222   -606       C  
ATOM   5580  CE  LYS B 385      51.528  -7.864  21.785  1.00 87.11           C  
ANISOU 5580  CE  LYS B 385     7976  16358   8765   2082     63   -243       C  
ATOM   5581  NZ  LYS B 385      52.982  -8.056  21.526  1.00 89.49           N  
ANISOU 5581  NZ  LYS B 385     7980  16907   9118   2478    261    -67       N  
ATOM   5582  N   THR B 386      47.474  -5.533  25.004  1.00 51.31           N  
ANISOU 5582  N   THR B 386     3719  10855   4922    327   -519   -304       N  
ATOM   5583  CA  THR B 386      47.378  -4.656  26.168  1.00 55.40           C  
ANISOU 5583  CA  THR B 386     4130  11182   5739      9   -589   -185       C  
ATOM   5584  C   THR B 386      45.994  -4.722  26.802  1.00 57.87           C  
ANISOU 5584  C   THR B 386     4742  11203   6043   -267   -709   -282       C  
ATOM   5585  O   THR B 386      45.867  -4.849  28.027  1.00 68.79           O  
ANISOU 5585  O   THR B 386     6286  12291   7561   -416   -851   -339       O  
ATOM   5586  CB  THR B 386      47.720  -3.220  25.771  1.00 55.60           C  
ANISOU 5586  CB  THR B 386     3847  11337   5941    -94   -393    113       C  
ATOM   5587  OG1 THR B 386      46.743  -2.739  24.841  1.00 70.38           O  
ANISOU 5587  OG1 THR B 386     5769  13307   7665   -157   -262    170       O  
ATOM   5588  CG2 THR B 386      49.099  -3.158  25.129  1.00 48.83           C  
ANISOU 5588  CG2 THR B 386     2729  10699   5126    176   -246    256       C  
ATOM   5589  N   TYR B 387      44.943  -4.624  25.983  1.00 49.70           N  
ANISOU 5589  N   TYR B 387     3783  10245   4857   -327   -650   -279       N  
ATOM   5590  CA  TYR B 387      43.585  -4.760  26.500  1.00 40.79           C  
ANISOU 5590  CA  TYR B 387     2902   8859   3739   -572   -752   -334       C  
ATOM   5591  C   TYR B 387      43.383  -6.122  27.150  1.00 40.83           C  
ANISOU 5591  C   TYR B 387     3256   8583   3674   -526   -953   -574       C  
ATOM   5592  O   TYR B 387      42.724  -6.234  28.190  1.00 46.70           O  
ANISOU 5592  O   TYR B 387     4178   9035   4532   -719  -1042   -591       O  
ATOM   5593  CB  TYR B 387      42.569  -4.552  25.377  1.00 48.40           C  
ANISOU 5593  CB  TYR B 387     3867   9971   4552   -612   -689   -290       C  
ATOM   5594  CG  TYR B 387      42.170  -3.110  25.154  1.00 51.66           C  
ANISOU 5594  CG  TYR B 387     4065  10474   5088   -782   -505    -38       C  
ATOM   5595  CD1 TYR B 387      41.523  -2.383  26.145  1.00 51.24           C  
ANISOU 5595  CD1 TYR B 387     4152  10076   5239   -997   -459     82       C  
ATOM   5596  CD2 TYR B 387      42.431  -2.479  23.944  1.00 54.76           C  
ANISOU 5596  CD2 TYR B 387     4268  11159   5378   -660   -335     84       C  
ATOM   5597  CE1 TYR B 387      41.156  -1.065  25.941  1.00 54.06           C  
ANISOU 5597  CE1 TYR B 387     4511  10350   5679  -1068   -293    290       C  
ATOM   5598  CE2 TYR B 387      42.067  -1.164  23.730  1.00 56.05           C  
ANISOU 5598  CE2 TYR B 387     4454  11200   5642   -766   -168    299       C  
ATOM   5599  CZ  TYR B 387      41.430  -0.461  24.731  1.00 56.87           C  
ANISOU 5599  CZ  TYR B 387     4736  10935   5936   -959   -170    387       C  
ATOM   5600  OH  TYR B 387      41.066   0.849  24.518  1.00 59.76           O  
ANISOU 5600  OH  TYR B 387     5166  11162   6378  -1005    -68    560       O  
ATOM   5601  N   ARG B 388      43.953  -7.169  26.550  1.00 42.84           N  
ANISOU 5601  N   ARG B 388     3633   8914   3731   -251  -1015   -748       N  
ATOM   5602  CA  ARG B 388      43.794  -8.515  27.089  1.00 43.24           C  
ANISOU 5602  CA  ARG B 388     4038   8693   3697   -192  -1218   -982       C  
ATOM   5603  C   ARG B 388      44.492  -8.660  28.435  1.00 49.44           C  
ANISOU 5603  C   ARG B 388     4861   9268   4656   -212  -1290  -1016       C  
ATOM   5604  O   ARG B 388      43.940  -9.263  29.362  1.00 48.68           O  
ANISOU 5604  O   ARG B 388     5033   8857   4605   -333  -1427  -1115       O  
ATOM   5605  CB  ARG B 388      44.324  -9.537  26.085  1.00 45.88           C  
ANISOU 5605  CB  ARG B 388     4522   9161   3751    150  -1262  -1155       C  
ATOM   5606  CG  ARG B 388      44.219 -10.983  26.526  1.00 53.57           C  
ANISOU 5606  CG  ARG B 388     5892   9855   4608    239  -1487  -1408       C  
ATOM   5607  CD  ARG B 388      44.405 -11.903  25.332  1.00 59.90           C  
ANISOU 5607  CD  ARG B 388     6915  10767   5078    558  -1546  -1571       C  
ATOM   5608  NE  ARG B 388      45.597 -11.554  24.565  1.00 69.69           N  
ANISOU 5608  NE  ARG B 388     7918  12349   6213    892  -1338  -1490       N  
ATOM   5609  CZ  ARG B 388      45.927 -12.108  23.403  1.00 81.16           C  
ANISOU 5609  CZ  ARG B 388     9521  13967   7350   1244  -1306  -1577       C  
ATOM   5610  NH1 ARG B 388      47.031 -11.727  22.774  1.00 84.58           N  
ANISOU 5610  NH1 ARG B 388     9699  14721   7717   1561  -1067  -1451       N  
ATOM   5611  NH2 ARG B 388      45.151 -13.040  22.867  1.00 87.18           N  
ANISOU 5611  NH2 ARG B 388    10700  14561   7863   1289  -1519  -1773       N  
ATOM   5612  N   SER B 389      45.704  -8.112  28.566  1.00 49.04           N  
ANISOU 5612  N   SER B 389     4543   9377   4715    -94  -1209   -917       N  
ATOM   5613  CA  SER B 389      46.389  -8.141  29.855  1.00 50.61           C  
ANISOU 5613  CA  SER B 389     4771   9364   5094   -127  -1316   -933       C  
ATOM   5614  C   SER B 389      45.618  -7.349  30.903  1.00 55.93           C  
ANISOU 5614  C   SER B 389     5514   9791   5947   -435  -1339   -826       C  
ATOM   5615  O   SER B 389      45.466  -7.797  32.050  1.00 73.30           O  
ANISOU 5615  O   SER B 389     7974  11675   8201   -497  -1471   -916       O  
ATOM   5616  CB  SER B 389      47.808  -7.591  29.707  1.00 44.25           C  
ANISOU 5616  CB  SER B 389     3608   8790   4415     29  -1246   -797       C  
ATOM   5617  OG  SER B 389      48.543  -8.327  28.746  1.00 54.69           O  
ANISOU 5617  OG  SER B 389     4871  10350   5558    367  -1181   -867       O  
ATOM   5618  N   ALA B 390      45.116  -6.170  30.524  1.00 49.70           N  
ANISOU 5618  N   ALA B 390     4520   9133   5231   -605  -1199   -625       N  
ATOM   5619  CA  ALA B 390      44.330  -5.361  31.450  1.00 47.22           C  
ANISOU 5619  CA  ALA B 390     4296   8591   5055   -860  -1191   -504       C  
ATOM   5620  C   ALA B 390      43.107  -6.124  31.939  1.00 46.53           C  
ANISOU 5620  C   ALA B 390     4545   8232   4902   -960  -1247   -601       C  
ATOM   5621  O   ALA B 390      42.812  -6.142  33.138  1.00 49.50           O  
ANISOU 5621  O   ALA B 390     5145   8302   5360  -1051  -1305   -599       O  
ATOM   5622  CB  ALA B 390      43.917  -4.049  30.780  1.00 36.90           C  
ANISOU 5622  CB  ALA B 390     2726   7494   3801   -996  -1018   -278       C  
ATOM   5623  N   PHE B 391      42.392  -6.780  31.023  1.00 42.73           N  
ANISOU 5623  N   PHE B 391     4115   7843   4277   -937  -1243   -674       N  
ATOM   5624  CA  PHE B 391      41.189  -7.505  31.416  1.00 36.63           C  
ANISOU 5624  CA  PHE B 391     3616   6815   3488  -1060  -1312   -725       C  
ATOM   5625  C   PHE B 391      41.529  -8.727  32.261  1.00 42.10           C  
ANISOU 5625  C   PHE B 391     4612   7235   4150   -962  -1477   -923       C  
ATOM   5626  O   PHE B 391      40.826  -9.030  33.231  1.00 43.72           O  
ANISOU 5626  O   PHE B 391     5045   7139   4426  -1077  -1510   -906       O  
ATOM   5627  CB  PHE B 391      40.386  -7.909  30.179  1.00 37.42           C  
ANISOU 5627  CB  PHE B 391     3699   7063   3457  -1073  -1329   -750       C  
ATOM   5628  CG  PHE B 391      39.862  -6.744  29.383  1.00 48.98           C  
ANISOU 5628  CG  PHE B 391     4898   8766   4946  -1183  -1172   -547       C  
ATOM   5629  CD1 PHE B 391      39.828  -5.468  29.925  1.00 50.31           C  
ANISOU 5629  CD1 PHE B 391     4907   8945   5264  -1309  -1022   -343       C  
ATOM   5630  CD2 PHE B 391      39.395  -6.928  28.093  1.00 45.81           C  
ANISOU 5630  CD2 PHE B 391     4444   8559   4402  -1149  -1192   -565       C  
ATOM   5631  CE1 PHE B 391      39.349  -4.399  29.189  1.00 52.19           C  
ANISOU 5631  CE1 PHE B 391     4956   9338   5535  -1370   -847   -150       C  
ATOM   5632  CE2 PHE B 391      38.910  -5.863  27.354  1.00 47.58           C  
ANISOU 5632  CE2 PHE B 391     4454   8970   4654  -1226  -1035   -374       C  
ATOM   5633  CZ  PHE B 391      38.887  -4.598  27.904  1.00 47.86           C  
ANISOU 5633  CZ  PHE B 391     4344   8982   4858  -1332   -846   -163       C  
ATOM   5634  N   SER B 392      42.602  -9.443  31.910  1.00 50.79           N  
ANISOU 5634  N   SER B 392     5722   8436   5140   -728  -1566  -1095       N  
ATOM   5635  CA  SER B 392      43.014 -10.598  32.701  1.00 57.18           C  
ANISOU 5635  CA  SER B 392     6822   8993   5910   -611  -1726  -1289       C  
ATOM   5636  C   SER B 392      43.393 -10.199  34.119  1.00 68.68           C  
ANISOU 5636  C   SER B 392     8364  10212   7518   -664  -1749  -1241       C  
ATOM   5637  O   SER B 392      43.172 -10.971  35.060  1.00 83.75           O  
ANISOU 5637  O   SER B 392    10579  11813   9428   -667  -1850  -1338       O  
ATOM   5638  CB  SER B 392      44.184 -11.310  32.023  1.00 70.94           C  
ANISOU 5638  CB  SER B 392     8530  10921   7504   -312  -1788  -1452       C  
ATOM   5639  OG  SER B 392      43.807 -11.815  30.754  1.00 90.68           O  
ANISOU 5639  OG  SER B 392    11058  13585   9811   -221  -1796  -1525       O  
ATOM   5640  N   ARG B 393      43.960  -9.005  34.296  1.00 64.74           N  
ANISOU 5640  N   ARG B 393     7626   9831   7141   -704  -1672  -1087       N  
ATOM   5641  CA  ARG B 393      44.283  -8.551  35.644  1.00 56.60           C  
ANISOU 5641  CA  ARG B 393     6728   8539   6237   -756  -1734  -1039       C  
ATOM   5642  C   ARG B 393      43.081  -7.945  36.362  1.00 52.62           C  
ANISOU 5642  C   ARG B 393     6391   7810   5794   -957  -1637   -888       C  
ATOM   5643  O   ARG B 393      43.041  -7.951  37.598  1.00 52.86           O  
ANISOU 5643  O   ARG B 393     6694   7528   5864   -967  -1694   -887       O  
ATOM   5644  CB  ARG B 393      45.445  -7.559  35.594  1.00 55.96           C  
ANISOU 5644  CB  ARG B 393     6350   8632   6279   -721  -1747   -930       C  
ATOM   5645  CG  ARG B 393      46.775  -8.219  35.261  1.00 60.81           C  
ANISOU 5645  CG  ARG B 393     6828   9401   6875   -486  -1851  -1049       C  
ATOM   5646  CD  ARG B 393      47.921  -7.224  35.185  1.00 65.71           C  
ANISOU 5646  CD  ARG B 393     7094  10200   7673   -473  -1871   -889       C  
ATOM   5647  NE  ARG B 393      47.826  -6.376  34.000  1.00 66.08           N  
ANISOU 5647  NE  ARG B 393     6784  10590   7733   -518  -1682   -718       N  
ATOM   5648  CZ  ARG B 393      47.332  -5.143  33.992  1.00 61.14           C  
ANISOU 5648  CZ  ARG B 393     6043   9984   7205   -723  -1591   -526       C  
ATOM   5649  NH1 ARG B 393      47.291  -4.458  32.859  1.00 50.29           N  
ANISOU 5649  NH1 ARG B 393     4349   8930   5827   -739  -1416   -378       N  
ATOM   5650  NH2 ARG B 393      46.879  -4.595  35.112  1.00 63.58           N  
ANISOU 5650  NH2 ARG B 393     6584   9982   7593   -887  -1668   -477       N  
ATOM   5651  N   TYR B 394      42.100  -7.420  35.624  1.00 51.66           N  
ANISOU 5651  N   TYR B 394     6124   7834   5670  -1093  -1484   -748       N  
ATOM   5652  CA  TYR B 394      40.930  -6.835  36.274  1.00 52.66           C  
ANISOU 5652  CA  TYR B 394     6384   7764   5858  -1254  -1359   -570       C  
ATOM   5653  C   TYR B 394      39.936  -7.899  36.727  1.00 51.26           C  
ANISOU 5653  C   TYR B 394     6485   7335   5658  -1290  -1372   -612       C  
ATOM   5654  O   TYR B 394      39.347  -7.779  37.808  1.00 38.92           O  
ANISOU 5654  O   TYR B 394     5162   5485   4142  -1332  -1307   -511       O  
ATOM   5655  CB  TYR B 394      40.240  -5.847  35.331  1.00 49.98           C  
ANISOU 5655  CB  TYR B 394     5767   7679   5545  -1382  -1191   -379       C  
ATOM   5656  CG  TYR B 394      41.075  -4.641  34.966  1.00 48.36           C  
ANISOU 5656  CG  TYR B 394     5292   7693   5392  -1381  -1150   -280       C  
ATOM   5657  CD1 TYR B 394      42.174  -4.270  35.731  1.00 51.34           C  
ANISOU 5657  CD1 TYR B 394     5708   7964   5836  -1319  -1263   -303       C  
ATOM   5658  CD2 TYR B 394      40.767  -3.877  33.847  1.00 41.51           C  
ANISOU 5658  CD2 TYR B 394     4128   7124   4518  -1448  -1018   -149       C  
ATOM   5659  CE1 TYR B 394      42.941  -3.170  35.393  1.00 52.31           C  
ANISOU 5659  CE1 TYR B 394     5562   8268   6044  -1344  -1251   -182       C  
ATOM   5660  CE2 TYR B 394      41.526  -2.778  33.503  1.00 47.91           C  
ANISOU 5660  CE2 TYR B 394     4684   8127   5394  -1456   -975    -35       C  
ATOM   5661  CZ  TYR B 394      42.612  -2.428  34.278  1.00 53.75           C  
ANISOU 5661  CZ  TYR B 394     5447   8751   6225  -1414  -1095    -44       C  
ATOM   5662  OH  TYR B 394      43.370  -1.333  33.937  1.00 58.16           O  
ANISOU 5662  OH  TYR B 394     5757   9451   6891  -1426  -1060     98       O  
ATOM   5663  N   ILE B 395      39.733  -8.942  35.916  1.00 57.29           N  
ANISOU 5663  N   ILE B 395     7238   8184   6346  -1264  -1458   -746       N  
ATOM   5664  CA  ILE B 395      38.780  -9.994  36.269  1.00 51.45           C  
ANISOU 5664  CA  ILE B 395     6739   7196   5615  -1327  -1503   -768       C  
ATOM   5665  C   ILE B 395      39.227 -10.732  37.525  1.00 53.08           C  
ANISOU 5665  C   ILE B 395     7281   7076   5810  -1222  -1595   -886       C  
ATOM   5666  O   ILE B 395      38.403 -11.112  38.367  1.00 64.96           O  
ANISOU 5666  O   ILE B 395     9015   8295   7373  -1286  -1546   -797       O  
ATOM   5667  CB  ILE B 395      38.579 -10.955  35.082  1.00 53.12           C  
ANISOU 5667  CB  ILE B 395     6908   7545   5732  -1315  -1638   -907       C  
ATOM   5668  CG1 ILE B 395      38.007 -10.202  33.879  1.00 56.07           C  
ANISOU 5668  CG1 ILE B 395     6987   8212   6107  -1419  -1552   -773       C  
ATOM   5669  CG2 ILE B 395      37.658 -12.104  35.468  1.00 55.30           C  
ANISOU 5669  CG2 ILE B 395     7436   7530   6046  -1402  -1735   -924       C  
ATOM   5670  CD1 ILE B 395      36.738  -9.434  34.183  1.00 56.41           C  
ANISOU 5670  CD1 ILE B 395     6948   8185   6300  -1624  -1386   -492       C  
ATOM   5671  N   GLN B 396      40.532 -10.930  37.685  1.00 42.26           N  
ANISOU 5671  N   GLN B 396     5938   5744   4376  -1050  -1721  -1065       N  
ATOM   5672  CA  GLN B 396      41.065 -11.596  38.866  1.00 47.07           C  
ANISOU 5672  CA  GLN B 396     6868   6052   4965   -930  -1833  -1189       C  
ATOM   5673  C   GLN B 396      41.326 -10.638  40.020  1.00 41.81           C  
ANISOU 5673  C   GLN B 396     6320   5207   4360   -925  -1783  -1073       C  
ATOM   5674  O   GLN B 396      41.814 -11.076  41.068  1.00 42.92           O  
ANISOU 5674  O   GLN B 396     6740   5086   4481   -807  -1874  -1161       O  
ATOM   5675  CB  GLN B 396      42.357 -12.343  38.522  1.00 56.20           C  
ANISOU 5675  CB  GLN B 396     7968   7333   6051   -716  -1944  -1397       C  
ATOM   5676  CG  GLN B 396      42.187 -13.472  37.519  1.00 63.54           C  
ANISOU 5676  CG  GLN B 396     8881   8373   6888   -663  -1965  -1511       C  
ATOM   5677  CD  GLN B 396      43.492 -14.186  37.230  1.00 72.73           C  
ANISOU 5677  CD  GLN B 396    10032   9629   7973   -437  -2026  -1652       C  
ATOM   5678  OE1 GLN B 396      44.558 -13.750  37.664  1.00 78.50           O  
ANISOU 5678  OE1 GLN B 396    10690  10394   8741   -328  -2073  -1664       O  
ATOM   5679  NE2 GLN B 396      43.413 -15.293  36.500  1.00 74.50           N  
ANISOU 5679  NE2 GLN B 396    10338   9871   8096   -358  -2053  -1750       N  
ATOM   5680  N   CYS B 397      41.013  -9.353  39.852  1.00 40.31           N  
ANISOU 5680  N   CYS B 397     5944   5138   4235  -1031  -1642   -875       N  
ATOM   5681  CA  CYS B 397      41.209  -8.338  40.884  1.00 39.45           C  
ANISOU 5681  CA  CYS B 397     5985   4841   4163  -1024  -1613   -755       C  
ATOM   5682  C   CYS B 397      42.669  -8.298  41.341  1.00 41.09           C  
ANISOU 5682  C   CYS B 397     6230   5010   4373   -891  -1838   -900       C  
ATOM   5683  O   CYS B 397      43.002  -8.553  42.501  1.00 58.64           O  
ANISOU 5683  O   CYS B 397     8793   6920   6567   -794  -1953   -963       O  
ATOM   5684  CB  CYS B 397      40.256  -8.563  42.062  1.00 42.25           C  
ANISOU 5684  CB  CYS B 397     6731   4821   4500  -1018  -1502   -649       C  
ATOM   5685  SG  CYS B 397      38.513  -8.424  41.612  1.00 61.53           S  
ANISOU 5685  SG  CYS B 397     9067   7307   7004  -1185  -1225   -392       S  
ATOM   5686  N   GLN B 398      43.541  -7.974  40.388  1.00 35.23           N  
ANISOU 5686  N   GLN B 398     5120   4594   3673   -880  -1901   -933       N  
ATOM   5687  CA  GLN B 398      44.979  -7.840  40.610  1.00 40.31           C  
ANISOU 5687  CA  GLN B 398     5671   5271   4373   -772  -2111  -1017       C  
ATOM   5688  C   GLN B 398      45.357  -6.494  40.001  1.00 49.66           C  
ANISOU 5688  C   GLN B 398     6497   6702   5671   -874  -2067   -842       C  
ATOM   5689  O   GLN B 398      45.731  -6.413  38.828  1.00 64.84           O  
ANISOU 5689  O   GLN B 398     8042   8979   7616   -864  -2008   -825       O  
ATOM   5690  CB  GLN B 398      45.754  -8.999  39.987  1.00 43.96           C  
ANISOU 5690  CB  GLN B 398     6018   5901   4785   -612  -2214  -1213       C  
ATOM   5691  CG  GLN B 398      45.369 -10.366  40.538  1.00 49.90           C  
ANISOU 5691  CG  GLN B 398     7094   6416   5451   -512  -2166  -1336       C  
ATOM   5692  CD  GLN B 398      45.879 -11.509  39.680  1.00 53.31           C  
ANISOU 5692  CD  GLN B 398     7423   7030   5801   -368  -2191  -1487       C  
ATOM   5693  OE1 GLN B 398      46.225 -11.319  38.515  1.00 55.80           O  
ANISOU 5693  OE1 GLN B 398     7442   7673   6086   -335  -2208  -1509       O  
ATOM   5694  NE2 GLN B 398      45.927 -12.706  40.255  1.00 53.25           N  
ANISOU 5694  NE2 GLN B 398     7671   6808   5755   -256  -2185  -1579       N  
ATOM   5695  N   TYR B 399      45.260  -5.436  40.806  1.00 42.43           N  
ANISOU 5695  N   TYR B 399     5728   5581   4811   -955  -2095   -706       N  
ATOM   5696  CA  TYR B 399      45.430  -4.070  40.332  1.00 43.25           C  
ANISOU 5696  CA  TYR B 399     5553   5859   5021  -1080  -2049   -515       C  
ATOM   5697  C   TYR B 399      46.814  -3.512  40.639  1.00 59.74           C  
ANISOU 5697  C   TYR B 399     7504   7932   7264  -1066  -2310   -492       C  
ATOM   5698  O   TYR B 399      46.985  -2.290  40.698  1.00 66.09           O  
ANISOU 5698  O   TYR B 399     8216   8725   8170  -1183  -2349   -324       O  
ATOM   5699  CB  TYR B 399      44.347  -3.169  40.927  1.00 40.13           C  
ANISOU 5699  CB  TYR B 399     5416   5247   4584  -1180  -1908   -350       C  
ATOM   5700  CG  TYR B 399      42.975  -3.808  40.965  1.00 43.88           C  
ANISOU 5700  CG  TYR B 399     6083   5643   4945  -1183  -1684   -342       C  
ATOM   5701  CD1 TYR B 399      42.163  -3.817  39.839  1.00 48.04           C  
ANISOU 5701  CD1 TYR B 399     6333   6457   5463  -1270  -1476   -267       C  
ATOM   5702  CD2 TYR B 399      42.490  -4.394  42.128  1.00 41.05           C  
ANISOU 5702  CD2 TYR B 399     6179   4915   4502  -1098  -1690   -387       C  
ATOM   5703  CE1 TYR B 399      40.910  -4.397  39.868  1.00 46.31           C  
ANISOU 5703  CE1 TYR B 399     6252   6157   5188  -1298  -1308   -227       C  
ATOM   5704  CE2 TYR B 399      41.235  -4.975  42.166  1.00 33.27           C  
ANISOU 5704  CE2 TYR B 399     5325   3857   3459  -1114  -1480   -332       C  
ATOM   5705  CZ  TYR B 399      40.450  -4.973  41.033  1.00 41.14           C  
ANISOU 5705  CZ  TYR B 399     6007   5141   4482  -1227  -1304   -246       C  
ATOM   5706  OH  TYR B 399      39.202  -5.551  41.066  1.00 47.52           O  
ANISOU 5706  OH  TYR B 399     6911   5867   5276  -1267  -1131   -161       O  
ATOM   5707  N   LYS B 400      47.800  -4.380  40.836  1.00 56.31           N  
ANISOU 5707  N   LYS B 400     7049   7487   6861   -930  -2505   -642       N  
ATOM   5708  CA  LYS B 400      49.184  -3.967  40.990  1.00 51.67           C  
ANISOU 5708  CA  LYS B 400     6237   6934   6460   -899  -2706   -589       C  
ATOM   5709  C   LYS B 400      50.070  -4.874  40.148  1.00 54.01           C  
ANISOU 5709  C   LYS B 400     6186   7541   6793   -754  -2744   -679       C  
ATOM   5710  O   LYS B 400      49.700  -6.001  39.810  1.00 63.10           O  
ANISOU 5710  O   LYS B 400     7428   8757   7789   -632  -2657   -845       O  
ATOM   5711  CB  LYS B 400      49.627  -3.988  42.462  1.00 52.48           C  
ANISOU 5711  CB  LYS B 400     6747   6610   6582   -827  -2889   -632       C  
ATOM   5712  CG  LYS B 400      49.222  -5.234  43.235  1.00 41.00           C  
ANISOU 5712  CG  LYS B 400     5705   4907   4966   -673  -2865   -815       C  
ATOM   5713  CD  LYS B 400      49.603  -5.106  44.703  1.00 42.05           C  
ANISOU 5713  CD  LYS B 400     6247   4613   5117   -588  -3026   -812       C  
ATOM   5714  CE  LYS B 400      49.093  -6.282  45.520  1.00 53.03           C  
ANISOU 5714  CE  LYS B 400     8042   5753   6354   -426  -2945   -938       C  
ATOM   5715  NZ  LYS B 400      49.430  -6.144  46.965  1.00 42.82           N  
ANISOU 5715  NZ  LYS B 400     7153   4056   5061   -310  -3095   -904       N  
ATOM   5716  N   GLU B 401      51.244  -4.359  39.799  1.00 49.16           N  
ANISOU 5716  N   GLU B 401     5180   7116   6382   -748  -2832   -547       N  
ATOM   5717  CA  GLU B 401      52.169  -5.087  38.940  1.00 67.62           C  
ANISOU 5717  CA  GLU B 401     7131   9783   8780   -575  -2854   -578       C  
ATOM   5718  C   GLU B 401      53.604  -4.951  39.438  1.00 72.75           C  
ANISOU 5718  C   GLU B 401     7609  10389   9644   -518  -3047   -485       C  
ATOM   5719  O   GLU B 401      54.270  -5.948  39.718  1.00 74.37           O  
ANISOU 5719  O   GLU B 401     7859  10557   9840   -333  -3176   -609       O  
ATOM   5720  CB  GLU B 401      52.051  -4.590  37.495  1.00 82.39           C  
ANISOU 5720  CB  GLU B 401     8556  12085  10665   -596  -2580   -421       C  
ATOM   5721  CG  GLU B 401      53.181  -5.033  36.579  1.00 94.55           C  
ANISOU 5721  CG  GLU B 401     9649  13988  12289   -386  -2525   -360       C  
ATOM   5722  CD  GLU B 401      54.278  -3.992  36.464  1.00102.61           C  
ANISOU 5722  CD  GLU B 401    10246  15102  13638   -453  -2600   -100       C  
ATOM   5723  OE1 GLU B 401      53.980  -2.792  36.641  1.00103.20           O  
ANISOU 5723  OE1 GLU B 401    10371  15041  13800   -643  -2534     10       O  
ATOM   5724  OE2 GLU B 401      55.439  -4.373  36.205  1.00107.68           O  
ANISOU 5724  OE2 GLU B 401    10583  15899  14432   -274  -2648    -34       O  
TER    5725      GLU B 401                                                      
HETATM 5726  C01 8NU A3001      10.875   1.419  64.653  1.00 57.80           C  
HETATM 5727  C02 8NU A3001      10.080   0.261  63.799  1.00 60.76           C  
HETATM 5728  C03 8NU A3001      10.374   0.003  62.501  1.00 61.26           C  
HETATM 5729  C04 8NU A3001      11.470   0.727  61.658  1.00 59.44           C  
HETATM 5730  C05 8NU A3001      12.830   0.068  61.846  1.00 57.82           C  
HETATM 5731  C07 8NU A3001      15.146   0.265  61.467  1.00 56.90           C  
HETATM 5732  C08 8NU A3001      16.322   0.413  60.488  1.00 55.16           C  
HETATM 5733  C09 8NU A3001      16.083  -0.311  59.137  1.00 51.65           C  
HETATM 5734  C10 8NU A3001      14.715   0.102  58.567  1.00 54.43           C  
HETATM 5735  C11 8NU A3001      13.560   0.020  59.563  1.00 56.18           C  
HETATM 5736  C12 8NU A3001      17.141  -0.071  58.039  1.00 48.66           C  
HETATM 5737  C15 8NU A3001      19.100  -0.151  56.794  1.00 45.58           C  
HETATM 5738  C16 8NU A3001      18.510  -0.680  57.963  1.00 45.79           C  
HETATM 5739  C17 8NU A3001      19.285  -1.590  58.742  1.00 47.44           C  
HETATM 5740  C18 8NU A3001      20.583  -1.964  58.373  1.00 48.81           C  
HETATM 5741  C19 8NU A3001      21.161  -1.415  57.177  1.00 48.18           C  
HETATM 5742  C21 8NU A3001      20.431  -0.505  56.377  1.00 49.24           C  
HETATM 5743  C22 8NU A3001       9.625  -1.097  61.699  1.00 64.77           C  
HETATM 5744  C25 8NU A3001       7.681  -3.012  61.764  1.00 72.65           C  
HETATM 5745  C26 8NU A3001       7.073  -4.050  62.731  1.00 71.55           C  
HETATM 5746  C27 8NU A3001       6.258  -3.328  63.779  1.00 70.07           C  
HETATM 5747  C28 8NU A3001       7.148  -2.341  64.561  1.00 68.67           C  
HETATM 5748  C29 8NU A3001       8.346  -1.460  63.819  1.00 67.34           C  
HETATM 5749  F20 8NU A3001      22.384  -1.780  56.847  1.00 47.25           F  
HETATM 5750  N06 8NU A3001      13.833   0.656  60.893  1.00 57.73           N  
HETATM 5751  N13 8NU A3001      17.018   0.735  56.974  1.00 47.73           N  
HETATM 5752  N24 8NU A3001       8.535  -1.862  62.455  1.00 68.25           N  
HETATM 5753  N30 8NU A3001       9.017  -0.518  64.459  1.00 65.25           N  
HETATM 5754  O14 8NU A3001      18.146   0.709  56.222  1.00 44.53           O  
HETATM 5755  O23 8NU A3001       9.841  -1.383  60.528  1.00 63.17           O  
HETATM 5756  C1  CLR A3002      22.552  15.650  56.415  1.00 63.04           C  
HETATM 5757  C2  CLR A3002      21.096  15.936  56.070  1.00 65.26           C  
HETATM 5758  C3  CLR A3002      20.187  15.037  56.892  1.00 69.59           C  
HETATM 5759  C4  CLR A3002      20.327  15.446  58.350  1.00 67.72           C  
HETATM 5760  C5  CLR A3002      21.774  15.315  58.765  1.00 63.09           C  
HETATM 5761  C6  CLR A3002      22.039  14.705  59.932  1.00 58.17           C  
HETATM 5762  C7  CLR A3002      23.427  14.495  60.493  1.00 57.42           C  
HETATM 5763  C8  CLR A3002      24.496  15.227  59.697  1.00 58.99           C  
HETATM 5764  C9  CLR A3002      24.192  15.205  58.207  1.00 59.57           C  
HETATM 5765  C10 CLR A3002      22.867  15.886  57.890  1.00 63.75           C  
HETATM 5766  C11 CLR A3002      25.342  15.801  57.389  1.00 60.30           C  
HETATM 5767  C12 CLR A3002      26.676  15.104  57.668  1.00 62.35           C  
HETATM 5768  C13 CLR A3002      26.986  15.169  59.156  1.00 64.80           C  
HETATM 5769  C14 CLR A3002      25.832  14.535  59.908  1.00 62.85           C  
HETATM 5770  C15 CLR A3002      26.321  14.414  61.341  1.00 66.46           C  
HETATM 5771  C16 CLR A3002      27.816  14.160  61.165  1.00 68.43           C  
HETATM 5772  C17 CLR A3002      28.144  14.327  59.682  1.00 63.43           C  
HETATM 5773  C18 CLR A3002      27.176  16.617  59.596  1.00 69.19           C  
HETATM 5774  C19 CLR A3002      22.967  17.381  58.170  1.00 67.22           C  
HETATM 5775  C20 CLR A3002      29.569  14.861  59.547  1.00 55.43           C  
HETATM 5776  C21 CLR A3002      30.093  14.857  58.115  1.00 53.19           C  
HETATM 5777  C22 CLR A3002      30.468  14.008  60.438  1.00 50.54           C  
HETATM 5778  C23 CLR A3002      31.933  14.423  60.405  1.00 49.56           C  
HETATM 5779  C24 CLR A3002      32.781  13.348  61.074  1.00 50.21           C  
HETATM 5780  C25 CLR A3002      34.255  13.734  61.096  1.00 54.42           C  
HETATM 5781  C26 CLR A3002      34.556  14.684  62.250  1.00 61.70           C  
HETATM 5782  C27 CLR A3002      35.138  12.494  61.154  1.00 48.31           C  
HETATM 5783  O1  CLR A3002      18.828  15.200  56.471  1.00 73.73           O  
HETATM 5784 ZN    ZN A3003      50.570  -3.050  53.682  1.00 13.10          ZN  
HETATM 5785  OH3 1PE A3004       1.786  -7.169  59.685  1.00 74.51           O  
HETATM 5786  C13 1PE A3004       0.189  -5.435  60.236  1.00 76.12           C  
HETATM 5787  C23 1PE A3004       1.521  -5.769  59.561  1.00 75.87           C  
HETATM 5788  OH4 1PE A3004      -0.075  -4.034  60.107  1.00 75.83           O  
HETATM 5789  C14 1PE A3004       0.628  -3.478  62.358  1.00 70.08           C  
HETATM 5790  C24 1PE A3004       0.868  -3.263  60.861  1.00 72.96           C  
HETATM 5791  OH5 1PE A3004       1.563  -2.706  63.122  1.00 70.02           O  
HETATM 5792  C15 1PE A3004       1.801  -4.542  64.681  1.00 77.48           C  
HETATM 5793  C25 1PE A3004       2.524  -3.554  63.761  1.00 72.97           C  
HETATM 5794  OH6 1PE A3004       2.752  -5.391  65.328  1.00 80.67           O  
HETATM 5795  C16 1PE A3004       1.433  -7.343  64.799  1.00 81.05           C  
HETATM 5796  C26 1PE A3004       2.070  -6.505  65.911  1.00 83.09           C  
HETATM 5797  OH7 1PE A3004       0.746  -8.462  65.364  1.00 78.23           O  
HETATM 5798  OH2 1PE A3005      49.948 -15.517  53.671  1.00 54.16           O  
HETATM 5799  C12 1PE A3005      51.347 -15.335  53.894  1.00 56.13           C  
HETATM 5800  C22 1PE A3005      52.137 -15.994  52.762  1.00 55.77           C  
HETATM 5801  OH3 1PE A3005      53.538 -15.808  52.983  1.00 50.50           O  
HETATM 5802  C13 1PE A3005      55.427 -16.171  54.431  1.00 41.69           C  
HETATM 5803  C23 1PE A3005      53.939 -16.432  54.205  1.00 46.06           C  
HETATM 5804  OH4 1PE A3005      55.665 -14.763  54.520  1.00 40.83           O  
HETATM 5805  C14 1PE A3005      55.563 -12.780  55.904  1.00 40.77           C  
HETATM 5806  C24 1PE A3005      55.286 -14.284  55.815  1.00 40.99           C  
HETATM 5807  OH5 1PE A3005      55.205 -12.277  57.198  1.00 36.64           O  
HETATM 5808  C15 1PE A3005      52.760 -12.223  57.196  1.00 35.37           C  
HETATM 5809  C25 1PE A3005      54.060 -11.412  57.156  1.00 34.55           C  
HETATM 5810  OH6 1PE A3005      51.641 -11.331  57.161  1.00 40.36           O  
HETATM 5811  C16 1PE A3005      49.976 -12.889  56.282  1.00 42.50           C  
HETATM 5812  C26 1PE A3005      50.438 -12.043  57.471  1.00 48.81           C  
HETATM 5813  OH7 1PE A3005      49.713 -12.043  55.159  1.00 24.02           O  
HETATM 5814  OH2 1PE A3006      61.293 -23.270  56.961  1.00 84.84           O  
HETATM 5815  C12 1PE A3006      62.080 -23.612  55.815  1.00 81.75           C  
HETATM 5816  C22 1PE A3006      61.432 -23.054  54.544  1.00 79.15           C  
HETATM 5817  OH3 1PE A3006      61.335 -21.631  54.636  1.00 74.28           O  
HETATM 5818  C13 1PE A3006      60.788 -19.586  53.481  1.00 68.56           C  
HETATM 5819  C23 1PE A3006      60.955 -21.103  53.359  1.00 69.52           C  
HETATM 5820  OH4 1PE A3006      62.029 -19.021  53.906  1.00 71.78           O  
HETATM 5821  C14 1PE A3006      62.897 -17.162  55.161  1.00 85.00           C  
HETATM 5822  C24 1PE A3006      61.824 -17.640  54.189  1.00 78.95           C  
HETATM 5823  OH5 1PE A3006      62.820 -17.915  56.372  1.00 86.15           O  
HETATM 5824  C01 8NU B3001      14.061  -0.566  21.908  1.00 53.47           C  
HETATM 5825  C02 8NU B3001      13.042  -0.998  20.694  1.00 56.45           C  
HETATM 5826  C03 8NU B3001      12.908  -0.247  19.572  1.00 60.46           C  
HETATM 5827  C04 8NU B3001      13.679   1.087  19.269  1.00 66.35           C  
HETATM 5828  C05 8NU B3001      14.755   0.877  18.209  1.00 72.30           C  
HETATM 5829  C07 8NU B3001      17.070   0.985  17.782  1.00 79.93           C  
HETATM 5830  C08 8NU B3001      18.286   1.855  17.381  1.00 80.86           C  
HETATM 5831  C09 8NU B3001      17.882   3.176  16.681  1.00 81.05           C  
HETATM 5832  C10 8NU B3001      16.890   3.910  17.589  1.00 79.39           C  
HETATM 5833  C11 8NU B3001      15.675   3.075  17.987  1.00 78.54           C  
HETATM 5834  C12 8NU B3001      19.020   4.173  16.321  1.00 84.30           C  
HETATM 5835  C15 8NU B3001      21.058   5.096  15.669  1.00 81.46           C  
HETATM 5836  C16 8NU B3001      20.423   3.848  15.862  1.00 77.11           C  
HETATM 5837  C17 8NU B3001      21.198   2.673  15.603  1.00 62.86           C  
HETATM 5838  C18 8NU B3001      22.532   2.736  15.171  1.00 63.32           C  
HETATM 5839  C19 8NU B3001      23.156   4.021  14.982  1.00 74.98           C  
HETATM 5840  C21 8NU B3001      22.428   5.209  15.229  1.00 77.49           C  
HETATM 5841  C22 8NU B3001      11.945  -0.668  18.423  1.00 62.75           C  
HETATM 5842  C25 8NU B3001      10.121  -2.506  17.531  1.00 69.25           C  
HETATM 5843  C26 8NU B3001       9.565  -3.940  17.735  1.00 70.93           C  
HETATM 5844  C27 8NU B3001       9.228  -4.142  19.193  1.00 71.72           C  
HETATM 5845  C28 8NU B3001      10.514  -4.011  20.018  1.00 68.82           C  
HETATM 5846  C29 8NU B3001      11.413  -2.631  19.883  1.00 64.44           C  
HETATM 5847  F20 8NU B3001      24.418   4.065  14.574  1.00 83.51           F  
HETATM 5848  N06 8NU B3001      15.978   1.699  18.513  1.00 77.65           N  
HETATM 5849  N13 8NU B3001      18.935   5.510  16.363  1.00 89.91           N  
HETATM 5850  N24 8NU B3001      11.155  -1.963  18.637  1.00 65.56           N  
HETATM 5851  N30 8NU B3001      12.247  -2.235  20.829  1.00 59.66           N  
HETATM 5852  O14 8NU B3001      20.107   6.080  15.989  1.00 86.91           O  
HETATM 5853  O23 8NU B3001      11.774  -0.043  17.383  1.00 64.92           O  
HETATM 5854  C1  PLM B3002      37.691  -9.970  41.636  1.00 34.15           C  
HETATM 5855  O2  PLM B3002      38.686 -10.745  41.597  1.00 32.15           O  
HETATM 5856  C2  PLM B3002      36.375 -10.567  41.026  1.00 37.37           C  
HETATM 5857  C3  PLM B3002      35.117  -9.710  41.193  1.00 36.88           C  
HETATM 5858  C4  PLM B3002      33.808 -10.511  41.126  1.00 39.19           C  
HETATM 5859  C5  PLM B3002      32.540  -9.647  41.194  1.00 39.87           C  
HETATM 5860  C6  PLM B3002      31.297 -10.404  41.687  1.00 41.13           C  
HETATM 5861  C7  PLM B3002      29.965  -9.729  41.322  1.00 47.88           C  
HETATM 5862  C8  PLM B3002      28.736 -10.398  41.957  1.00 51.94           C  
HETATM 5863  C9  PLM B3002      27.397  -9.868  41.424  1.00 54.02           C  
HETATM 5864  C1  CLR B3003      35.144  -5.863  36.639  1.00 49.70           C  
HETATM 5865  C2  CLR B3003      36.630  -6.094  36.891  1.00 50.33           C  
HETATM 5866  C3  CLR B3003      37.154  -5.163  37.977  1.00 45.19           C  
HETATM 5867  C4  CLR B3003      36.411  -5.455  39.274  1.00 46.84           C  
HETATM 5868  C5  CLR B3003      34.933  -5.294  39.018  1.00 50.21           C  
HETATM 5869  C6  CLR B3003      34.235  -4.460  39.805  1.00 54.29           C  
HETATM 5870  C7  CLR B3003      32.755  -4.203  39.654  1.00 53.32           C  
HETATM 5871  C8  CLR B3003      32.080  -5.306  38.858  1.00 51.94           C  
HETATM 5872  C9  CLR B3003      32.877  -5.651  37.607  1.00 49.92           C  
HETATM 5873  C10 CLR B3003      34.310  -6.089  37.895  1.00 48.85           C  
HETATM 5874  C11 CLR B3003      32.142  -6.690  36.755  1.00 51.22           C  
HETATM 5875  C12 CLR B3003      30.727  -6.246  36.383  1.00 50.84           C  
HETATM 5876  C13 CLR B3003      29.939  -5.887  37.635  1.00 52.70           C  
HETATM 5877  C14 CLR B3003      30.713  -4.830  38.393  1.00 52.70           C  
HETATM 5878  C15 CLR B3003      29.743  -4.318  39.447  1.00 53.97           C  
HETATM 5879  C16 CLR B3003      28.394  -4.379  38.730  1.00 57.37           C  
HETATM 5880  C17 CLR B3003      28.599  -5.183  37.441  1.00 58.61           C  
HETATM 5881  C18 CLR B3003      29.740  -7.124  38.507  1.00 45.04           C  
HETATM 5882  C19 CLR B3003      34.347  -7.564  38.280  1.00 44.39           C  
HETATM 5883  C20 CLR B3003      27.391  -6.075  37.147  1.00 64.41           C  
HETATM 5884  C21 CLR B3003      27.372  -6.594  35.713  1.00 64.71           C  
HETATM 5885  C22 CLR B3003      26.099  -5.320  37.448  1.00 67.68           C  
HETATM 5886  C23 CLR B3003      24.864  -6.067  36.955  1.00 68.76           C  
HETATM 5887  C24 CLR B3003      23.586  -5.377  37.420  1.00 69.57           C  
HETATM 5888  C25 CLR B3003      23.398  -4.022  36.746  1.00 69.77           C  
HETATM 5889  C26 CLR B3003      22.255  -4.069  35.738  1.00 71.93           C  
HETATM 5890  C27 CLR B3003      23.171  -2.922  37.777  1.00 66.70           C  
HETATM 5891  O1  CLR B3003      38.555  -5.389  38.162  1.00 44.87           O  
CONECT  624 1257                                                                
CONECT  905 5784                                                                
CONECT  915 5784                                                                
CONECT 1257  624                                                                
CONECT 1556 5784                                                                
CONECT 2247 5784                                                                
CONECT 2248 5784                                                                
CONECT 2497 2527                                                                
CONECT 2527 2497                                                                
CONECT 3505 4074                                                                
CONECT 4074 3505                                                                
CONECT 5298 5328                                                                
CONECT 5328 5298                                                                
CONECT 5685 5854                                                                
CONECT 5726 5727                                                                
CONECT 5727 5726 5728 5753                                                      
CONECT 5728 5727 5729 5743                                                      
CONECT 5729 5728 5730                                                           
CONECT 5730 5729 5750                                                           
CONECT 5731 5732 5750                                                           
CONECT 5732 5731 5733                                                           
CONECT 5733 5732 5734 5736                                                      
CONECT 5734 5733 5735                                                           
CONECT 5735 5734 5750                                                           
CONECT 5736 5733 5738 5751                                                      
CONECT 5737 5738 5742 5754                                                      
CONECT 5738 5736 5737 5739                                                      
CONECT 5739 5738 5740                                                           
CONECT 5740 5739 5741                                                           
CONECT 5741 5740 5742 5749                                                      
CONECT 5742 5737 5741                                                           
CONECT 5743 5728 5752 5755                                                      
CONECT 5744 5745 5752                                                           
CONECT 5745 5744 5746                                                           
CONECT 5746 5745 5747                                                           
CONECT 5747 5746 5748                                                           
CONECT 5748 5747 5752 5753                                                      
CONECT 5749 5741                                                                
CONECT 5750 5730 5731 5735                                                      
CONECT 5751 5736 5754                                                           
CONECT 5752 5743 5744 5748                                                      
CONECT 5753 5727 5748                                                           
CONECT 5754 5737 5751                                                           
CONECT 5755 5743                                                                
CONECT 5756 5757 5765                                                           
CONECT 5757 5756 5758                                                           
CONECT 5758 5757 5759 5783                                                      
CONECT 5759 5758 5760                                                           
CONECT 5760 5759 5761 5765                                                      
CONECT 5761 5760 5762                                                           
CONECT 5762 5761 5763                                                           
CONECT 5763 5762 5764 5769                                                      
CONECT 5764 5763 5765 5766                                                      
CONECT 5765 5756 5760 5764 5774                                                 
CONECT 5766 5764 5767                                                           
CONECT 5767 5766 5768                                                           
CONECT 5768 5767 5769 5772 5773                                                 
CONECT 5769 5763 5768 5770                                                      
CONECT 5770 5769 5771                                                           
CONECT 5771 5770 5772                                                           
CONECT 5772 5768 5771 5775                                                      
CONECT 5773 5768                                                                
CONECT 5774 5765                                                                
CONECT 5775 5772 5776 5777                                                      
CONECT 5776 5775                                                                
CONECT 5777 5775 5778                                                           
CONECT 5778 5777 5779                                                           
CONECT 5779 5778 5780                                                           
CONECT 5780 5779 5781 5782                                                      
CONECT 5781 5780                                                                
CONECT 5782 5780                                                                
CONECT 5783 5758                                                                
CONECT 5784  905  915 1556 2247                                                 
CONECT 5784 2248                                                                
CONECT 5785 5787                                                                
CONECT 5786 5787 5788                                                           
CONECT 5787 5785 5786                                                           
CONECT 5788 5786 5790                                                           
CONECT 5789 5790 5791                                                           
CONECT 5790 5788 5789                                                           
CONECT 5791 5789 5793                                                           
CONECT 5792 5793 5794                                                           
CONECT 5793 5791 5792                                                           
CONECT 5794 5792 5796                                                           
CONECT 5795 5796 5797                                                           
CONECT 5796 5794 5795                                                           
CONECT 5797 5795                                                                
CONECT 5798 5799                                                                
CONECT 5799 5798 5800                                                           
CONECT 5800 5799 5801                                                           
CONECT 5801 5800 5803                                                           
CONECT 5802 5803 5804                                                           
CONECT 5803 5801 5802                                                           
CONECT 5804 5802 5806                                                           
CONECT 5805 5806 5807                                                           
CONECT 5806 5804 5805                                                           
CONECT 5807 5805 5809                                                           
CONECT 5808 5809 5810                                                           
CONECT 5809 5807 5808                                                           
CONECT 5810 5808 5812                                                           
CONECT 5811 5812 5813                                                           
CONECT 5812 5810 5811                                                           
CONECT 5813 5811                                                                
CONECT 5814 5815                                                                
CONECT 5815 5814 5816                                                           
CONECT 5816 5815 5817                                                           
CONECT 5817 5816 5819                                                           
CONECT 5818 5819 5820                                                           
CONECT 5819 5817 5818                                                           
CONECT 5820 5818 5822                                                           
CONECT 5821 5822 5823                                                           
CONECT 5822 5820 5821                                                           
CONECT 5823 5821                                                                
CONECT 5824 5825                                                                
CONECT 5825 5824 5826 5851                                                      
CONECT 5826 5825 5827 5841                                                      
CONECT 5827 5826 5828                                                           
CONECT 5828 5827 5848                                                           
CONECT 5829 5830 5848                                                           
CONECT 5830 5829 5831                                                           
CONECT 5831 5830 5832 5834                                                      
CONECT 5832 5831 5833                                                           
CONECT 5833 5832 5848                                                           
CONECT 5834 5831 5836 5849                                                      
CONECT 5835 5836 5840 5852                                                      
CONECT 5836 5834 5835 5837                                                      
CONECT 5837 5836 5838                                                           
CONECT 5838 5837 5839                                                           
CONECT 5839 5838 5840 5847                                                      
CONECT 5840 5835 5839                                                           
CONECT 5841 5826 5850 5853                                                      
CONECT 5842 5843 5850                                                           
CONECT 5843 5842 5844                                                           
CONECT 5844 5843 5845                                                           
CONECT 5845 5844 5846                                                           
CONECT 5846 5845 5850 5851                                                      
CONECT 5847 5839                                                                
CONECT 5848 5828 5829 5833                                                      
CONECT 5849 5834 5852                                                           
CONECT 5850 5841 5842 5846                                                      
CONECT 5851 5825 5846                                                           
CONECT 5852 5835 5849                                                           
CONECT 5853 5841                                                                
CONECT 5854 5685 5855 5856                                                      
CONECT 5855 5854                                                                
CONECT 5856 5854 5857                                                           
CONECT 5857 5856 5858                                                           
CONECT 5858 5857 5859                                                           
CONECT 5859 5858 5860                                                           
CONECT 5860 5859 5861                                                           
CONECT 5861 5860 5862                                                           
CONECT 5862 5861 5863                                                           
CONECT 5863 5862                                                                
CONECT 5864 5865 5873                                                           
CONECT 5865 5864 5866                                                           
CONECT 5866 5865 5867 5891                                                      
CONECT 5867 5866 5868                                                           
CONECT 5868 5867 5869 5873                                                      
CONECT 5869 5868 5870                                                           
CONECT 5870 5869 5871                                                           
CONECT 5871 5870 5872 5877                                                      
CONECT 5872 5871 5873 5874                                                      
CONECT 5873 5864 5868 5872 5882                                                 
CONECT 5874 5872 5875                                                           
CONECT 5875 5874 5876                                                           
CONECT 5876 5875 5877 5880 5881                                                 
CONECT 5877 5871 5876 5878                                                      
CONECT 5878 5877 5879                                                           
CONECT 5879 5878 5880                                                           
CONECT 5880 5876 5879 5883                                                      
CONECT 5881 5876                                                                
CONECT 5882 5873                                                                
CONECT 5883 5880 5884 5885                                                      
CONECT 5884 5883                                                                
CONECT 5885 5883 5886                                                           
CONECT 5886 5885 5887                                                           
CONECT 5887 5886 5888                                                           
CONECT 5888 5887 5889 5890                                                      
CONECT 5889 5888                                                                
CONECT 5890 5888                                                                
CONECT 5891 5866                                                                
MASTER      458    0    9   28    0    0   17    6 5889    2  181   58          
END