HEADER    MEMBRANE PROTEIN                        11-JUL-18   6A94              
TITLE     CRYSTAL STRUCTURE OF 5-HT2AR IN COMPLEX WITH ZOTEPINE                 
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    RECEPTOR, 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 6A94    1       JRNL                                     
REVDAT   1   13-FEB-19 6A94    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.    2.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.13_2998)                                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.82                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 2.040                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 86.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 21132                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.238                           
REMARK   3   R VALUE            (WORKING SET) : 0.236                           
REMARK   3   FREE R VALUE                     : 0.269                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.040                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1064                            
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 45.8281 -  5.7966    1.00     3022   167  0.2331 0.2775        
REMARK   3     2  5.7966 -  4.6023    1.00     2879   154  0.2316 0.2418        
REMARK   3     3  4.6023 -  4.0210    1.00     2907   154  0.2059 0.2194        
REMARK   3     4  4.0210 -  3.6535    1.00     2892   153  0.2276 0.2533        
REMARK   3     5  3.6535 -  3.3917    1.00     2870   146  0.2429 0.2917        
REMARK   3     6  3.3917 -  3.1918    0.91     2577   145  0.2691 0.3449        
REMARK   3     7  3.1918 -  3.0320    0.67     1900    99  0.2633 0.2683        
REMARK   3     8  3.0320 -  2.9000    0.35     1021    46  0.2683 0.3687        
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)     : 0.350            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.380           
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           5996                                  
REMARK   3   ANGLE     :  0.629           8141                                  
REMARK   3   CHIRALITY :  0.040            967                                  
REMARK   3   PLANARITY :  0.004            978                                  
REMARK   3   DIHEDRAL  : 12.124           3606                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 8                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 69 THROUGH 144 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  21.2272   4.1444  70.4427              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3780 T22:   1.4088                                     
REMARK   3      T33:   0.8934 T12:  -0.0245                                     
REMARK   3      T13:   0.1301 T23:  -0.5492                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.2709 L22:   0.9383                                     
REMARK   3      L33:   0.6822 L12:  -0.7377                                     
REMARK   3      L13:  -0.6509 L23:  -0.2668                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0612 S12:  -0.9135 S13:   0.2584                       
REMARK   3      S21:   0.2306 S22:   0.0327 S23:   0.0778                       
REMARK   3      S31:  -0.0590 S32:  -0.0080 S33:  -0.0892                       
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):  42.2713  -2.0175  52.9519              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2065 T22:  -0.0209                                     
REMARK   3      T33:   0.2395 T12:   0.0002                                     
REMARK   3      T13:   0.0585 T23:   0.0322                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5313 L22:   0.6859                                     
REMARK   3      L33:   0.9900 L12:   0.2828                                     
REMARK   3      L13:   0.1662 L23:  -0.0408                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0900 S12:  -0.1995 S13:   0.1264                       
REMARK   3      S21:   0.1806 S22:   0.0871 S23:   0.1949                       
REMARK   3      S31:  -0.0994 S32:  -0.5392 S33:   0.1145                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 349 THROUGH 399 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  24.9273  -3.4067  69.0742              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3325 T22:   1.2550                                     
REMARK   3      T33:   0.6197 T12:  -0.1530                                     
REMARK   3      T13:   0.1165 T23:  -0.0277                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.4240 L22:   3.2623                                     
REMARK   3      L33:   1.2416 L12:   0.3031                                     
REMARK   3      L13:  -1.7701 L23:  -0.3623                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0976 S12:  -0.9613 S13:   0.2700                       
REMARK   3      S21:   0.2463 S22:  -0.0433 S23:   0.3860                       
REMARK   3      S31:   0.0018 S32:   0.0369 S33:  -0.0303                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 72 THROUGH 144 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  25.1056  -2.2468  28.0341              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2686 T22:   0.7100                                     
REMARK   3      T33:   0.3050 T12:  -0.0933                                     
REMARK   3      T13:   0.0654 T23:   0.0153                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.5020 L22:   2.4249                                     
REMARK   3      L33:   1.4780 L12:  -0.7884                                     
REMARK   3      L13:  -0.7372 L23:   0.4001                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1830 S12:   0.6229 S13:   0.2863                       
REMARK   3      S21:  -0.0261 S22:   0.1932 S23:   0.1557                       
REMARK   3      S31:   0.2922 S32:  -0.3252 S33:   0.0400                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 145 THROUGH 216 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  27.6896  12.5949  19.7663              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4393 T22:   1.1694                                     
REMARK   3      T33:   0.9017 T12:   0.0116                                     
REMARK   3      T13:   0.0268 T23:   0.4164                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.7547 L22:   3.5089                                     
REMARK   3      L33:   2.8993 L12:   2.1441                                     
REMARK   3      L13:  -3.0565 L23:  -0.5954                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2257 S12:   0.5607 S13:   1.0591                       
REMARK   3      S21:  -0.1535 S22:  -0.0432 S23:   0.0299                       
REMARK   3      S31:  -0.3028 S32:  -0.1030 S33:  -0.1977                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'B' AND ((RESID 217 THROUGH 265 ) OR (RESID      
REMARK   3               1001 THROUGH 1018 ))                                   
REMARK   3    ORIGIN FOR THE GROUP (A):  36.3006   5.7324   6.7995              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5046 T22:   1.6629                                     
REMARK   3      T33:   0.8462 T12:  -0.0366                                     
REMARK   3      T13:   0.2037 T23:   0.3602                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0913 L22:   0.1008                                     
REMARK   3      L33:   0.2568 L12:   0.0108                                     
REMARK   3      L13:  -0.6450 L23:   0.0748                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0411 S12:   0.4215 S13:   0.0897                       
REMARK   3      S21:  -0.1100 S22:   0.2084 S23:   0.1475                       
REMARK   3      S31:  -0.0167 S32:  -0.1929 S33:  -0.0836                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 1019 THROUGH 1083 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  77.3313  11.2200   0.7620              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5063 T22:   1.6768                                     
REMARK   3      T33:   0.9104 T12:  -0.0012                                     
REMARK   3      T13:   0.2298 T23:  -0.1231                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.8327 L22:   7.2245                                     
REMARK   3      L33:   0.7784 L12:  -0.1414                                     
REMARK   3      L13:  -1.7013 L23:  -1.8451                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3407 S12:   0.1202 S13:   0.9797                       
REMARK   3      S21:  -0.1615 S22:   0.0117 S23:  -0.3207                       
REMARK   3      S31:  -0.0594 S32:  -0.0383 S33:  -0.3371                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND ((RESID 1084 THROUGH 1106 ) OR (RESID    
REMARK   3               313 THROUGH 401 ))                                     
REMARK   3    ORIGIN FOR THE GROUP (A):  38.7504  -2.3872  15.4287              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3458 T22:   1.4091                                     
REMARK   3      T33:   0.4792 T12:   0.0134                                     
REMARK   3      T13:   0.0589 T23:   0.0801                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0377 L22:   0.8300                                     
REMARK   3      L33:   0.2524 L12:   0.1764                                     
REMARK   3      L13:   0.0668 L23:   0.1941                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0512 S12:   0.8421 S13:   0.3274                       
REMARK   3      S21:  -0.2075 S22:  -0.0339 S23:  -0.1344                       
REMARK   3      S31:   0.0148 S32:  -0.3189 S33:   0.0929                       
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 6A94 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_1300008337.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-APR-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : 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   : 30115                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 45.822                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 86.7                               
REMARK 200  DATA REDUNDANCY                : 21.10                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.4800                             
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) : 2.86                     
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   (%): 61.80                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.22                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM MES, PH 6.0, OR HEPES, PH 7.0,    
REMARK 280  30% (V/V) PEG400, 100 MM LI-CHLORIDE, NA-ACETATE, OR 14 OTHER       
REMARK 280  VARIOUS SALTS FROM STOCKOPTIONS SALT (HAMPTON RESEARCH), LIPIDIC    
REMARK 280  CUBIC 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      139.59000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       21.11000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000      139.59000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       21.11000            
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  1062                                                      
REMARK 465     GLY B  1063                                                      
REMARK 465     SER B  1064                                                      
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   SG   CYS B   397     O2   PLM B  3002              1.84            
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    LEU A 105       47.09    -99.64                                   
REMARK 500    PHE A 243      -55.10   -126.17                                   
REMARK 500    LEU B 105       46.74   -100.40                                   
REMARK 500    PHE B 243      -55.40   -125.83                                   
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     PLM B 3002                                                       
REMARK 610     A6L B 3004                                                       
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 A3004  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 182   NE2                                                    
REMARK 620 2 HIS A 183   NE2 110.4                                              
REMARK 620 3 GLU A 264   OE2 105.9  87.5                                        
REMARK 620 4 GLU A 318   OE2 145.5  86.0 104.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZOT 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 1PE A 3003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 3004                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZOT B 3001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PLM B 3002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLR B 3003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue A6L B 3004                
DBREF  6A94 A   70   265  UNP    P28223   5HT2A_HUMAN     70    265             
DBREF  6A94 A 1001  1040  UNP    P0ABE7   C562_ECOLX      23     62             
DBREF  6A94 A 1066  1106  UNP    P0ABE7   C562_ECOLX      88    128             
DBREF  6A94 A  313   403  UNP    P28223   5HT2A_HUMAN    313    403             
DBREF  6A94 B   70   265  UNP    P28223   5HT2A_HUMAN     70    265             
DBREF  6A94 B 1001  1040  UNP    P0ABE7   C562_ECOLX      23     62             
DBREF  6A94 B 1066  1106  UNP    P0ABE7   C562_ECOLX      88    128             
DBREF  6A94 B  313   403  UNP    P28223   5HT2A_HUMAN    313    403             
SEQADV 6A94 GLY A   67  UNP  P28223              EXPRESSION TAG                 
SEQADV 6A94 GLY A   68  UNP  P28223              EXPRESSION TAG                 
SEQADV 6A94 THR A   69  UNP  P28223              EXPRESSION TAG                 
SEQADV 6A94 LYS A  162  UNP  P28223    SER   162 ENGINEERED MUTATION            
SEQADV 6A94 TRP A  164  UNP  P28223    MET   164 ENGINEERED MUTATION            
SEQADV 6A94 TRP A 1007  UNP  P0ABE7    MET    29 ENGINEERED MUTATION            
SEQADV 6A94 GLY A 1041  UNP  P0ABE7              LINKER                         
SEQADV 6A94 SER A 1042  UNP  P0ABE7              LINKER                         
SEQADV 6A94 GLY A 1043  UNP  P0ABE7              LINKER                         
SEQADV 6A94 SER A 1044  UNP  P0ABE7              LINKER                         
SEQADV 6A94 GLY A 1045  UNP  P0ABE7              LINKER                         
SEQADV 6A94 ILE A 1098  UNP  P0ABE7    ARG   120 ENGINEERED MUTATION            
SEQADV 6A94 ILE A 1102  UNP  P0ABE7    HIS   124 ENGINEERED MUTATION            
SEQADV 6A94 GLY A 1106  UNP  P0ABE7    ARG   128 ENGINEERED MUTATION            
SEQADV 6A94 GLY B   67  UNP  P28223              EXPRESSION TAG                 
SEQADV 6A94 GLY B   68  UNP  P28223              EXPRESSION TAG                 
SEQADV 6A94 THR B   69  UNP  P28223              EXPRESSION TAG                 
SEQADV 6A94 LYS B  162  UNP  P28223    SER   162 ENGINEERED MUTATION            
SEQADV 6A94 TRP B  164  UNP  P28223    MET   164 ENGINEERED MUTATION            
SEQADV 6A94 TRP B 1007  UNP  P0ABE7    MET    29 ENGINEERED MUTATION            
SEQADV 6A94 GLY B 1041  UNP  P0ABE7              LINKER                         
SEQADV 6A94 SER B 1062  UNP  P0ABE7              LINKER                         
SEQADV 6A94 GLY B 1063  UNP  P0ABE7              LINKER                         
SEQADV 6A94 SER B 1064  UNP  P0ABE7              LINKER                         
SEQADV 6A94 GLY B 1065  UNP  P0ABE7              LINKER                         
SEQADV 6A94 ILE B 1098  UNP  P0ABE7    ARG   120 ENGINEERED MUTATION            
SEQADV 6A94 ILE B 1102  UNP  P0ABE7    HIS   124 ENGINEERED MUTATION            
SEQADV 6A94 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    ZOT  A3001      22                                                       
HET    CLR  A3002      28                                                       
HET    1PE  A3003      16                                                       
HET     ZN  A3004       1                                                       
HET    ZOT  B3001      22                                                       
HET    PLM  B3002      10                                                       
HET    CLR  B3003      28                                                       
HET    A6L  B3004      20                                                       
HETNAM     ZOT 2-(3-CHLORANYLBENZO[B][1]BENZOTHIEPIN-5-YL)OXY-N,N-              
HETNAM   2 ZOT  DIMETHYL-ETHANAMINE                                             
HETNAM     CLR CHOLESTEROL                                                      
HETNAM     1PE PENTAETHYLENE GLYCOL                                             
HETNAM      ZN ZINC ION                                                         
HETNAM     PLM PALMITIC ACID                                                    
HETNAM     A6L 2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE                        
HETSYN     1PE PEG400                                                           
HETSYN     A6L MONOOLEIN                                                        
FORMUL   3  ZOT    2(C18 H18 CL N O S)                                          
FORMUL   4  CLR    2(C27 H46 O)                                                 
FORMUL   5  1PE    C10 H22 O6                                                   
FORMUL   6   ZN    ZN 2+                                                        
FORMUL   8  PLM    C16 H32 O2                                                   
FORMUL  10  A6L    C21 H40 O4                                                   
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 SER A  145  GLN A  178  1                                  34    
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  SER A 1042  1                                  21    
HELIX   11 AB2 ASP A 1066  GLU A 1081  1                                  16    
HELIX   12 AB3 LYS A 1083  CYS A  349  1                                  61    
HELIX   13 AB4 ASN A  354  ASN A  384  1                                  31    
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 LYS B  103  GLN B  106  5                                   4    
HELIX   17 AB8 ASN B  107  VAL B  127  1                                  21    
HELIX   18 AB9 VAL B  127  TYR B  137  1                                  11    
HELIX   19 AC1 PRO B  144  ASN B  179  1                                  36    
HELIX   20 AC2 ARG B  189  MET B  208  1                                  20    
HELIX   21 AC3 MET B  208  ASP B  217  1                                  10    
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 ASN B  354  ASN B  384  1                                  31    
HELIX   28 AD1 ASN B  384  GLN B  396  1                                  13    
SHEET    1 AA1 2 PHE A 222  LYS A 223  0                                        
SHEET    2 AA1 2 SER A 226  CYS A 227 -1  O  SER A 226   N  LYS A 223           
SHEET    1 AA2 2 PHE B 222  LYS B 223  0                                        
SHEET    2 AA2 2 SER B 226  CYS B 227 -1  O  SER B 226   N  LYS B 223           
SSBOND   1 CYS A  148    CYS A  227                          1555   1555  2.03  
SSBOND   2 CYS A  349    CYS A  353                          1555   1555  2.03  
SSBOND   3 CYS B  148    CYS B  227                          1555   1555  2.04  
SSBOND   4 CYS B  349    CYS B  353                          1555   1555  2.03  
LINK         NE2 HIS A 182                ZN    ZN A3004     1555   1555  2.11  
LINK         NE2 HIS A 183                ZN    ZN A3004     1555   1555  2.14  
LINK         OE2 GLU A 264                ZN    ZN A3004     1555   1555  1.88  
LINK         OE2 GLU A 318                ZN    ZN A3004     1555   1555  1.92  
LINK         SG  CYS B 397                 C1  PLM B3002     1555   1555  1.78  
SITE     1 AC1 10 ASP A 155  SER A 159  LEU A 229  VAL A 235                    
SITE     2 AC1 10 GLY A 238  SER A 242  TRP A 336  PHE A 339                    
SITE     3 AC1 10 PHE A 340  ASN A 343                                          
SITE     1 AC2  9 TYR A 111  MET A 114  ILE A 118  LEU A 122                    
SITE     2 AC2  9 TYR A 153  PHE A 193  ILE A 196  TRP A 200                    
SITE     3 AC2  9 VAL A 204                                                     
SITE     1 AC3  8 LEU A 261  GLN A 262  ALA A 265  ILE A 315                    
SITE     2 AC3  8 SER A 316  GLN A 319  GLU A1004  ASN A1080                    
SITE     1 AC4  4 HIS A 182  HIS A 183  GLU A 264  GLU A 318                    
SITE     1 AC5 10 ASP B 155  VAL B 156  SER B 159  THR B 160                    
SITE     2 AC5 10 LEU B 229  VAL B 235  GLY B 238  SER B 242                    
SITE     3 AC5 10 PHE B 339  PHE B 340                                          
SITE     1 AC6  4 ILE B 395  GLN B 396  CYS B 397  CLR B3003                    
SITE     1 AC7  4 ILE B  86  TYR B 394  TYR B 399  PLM B3002                    
SITE     1 AC8  3 THR A 253  LEU A 256  TYR B 399                               
CRYST1  279.180   42.220   91.710  90.00  92.16  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      0.003582  0.000000  0.000135        0.00000                         
SCALE2      0.000000  0.023685  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010912        0.00000                         
ATOM      1  N   THR A  69      -0.463  -8.626  82.541  1.00119.23           N  
ANISOU    1  N   THR A  69     7972  21524  15808    161   2912   -525       N  
ATOM      2  CA  THR A  69       0.586  -9.342  81.823  1.00125.06           C  
ANISOU    2  CA  THR A  69     8704  22037  16775     98   2834   -522       C  
ATOM      3  C   THR A  69       0.985  -8.577  80.566  1.00129.56           C  
ANISOU    3  C   THR A  69     9509  22367  17352     25   2670   -964       C  
ATOM      4  O   THR A  69       2.158  -8.544  80.191  1.00128.44           O  
ANISOU    4  O   THR A  69     9472  22188  17139      6   2575  -1102       O  
ATOM      5  CB  THR A  69       0.138 -10.765  81.441  1.00125.13           C  
ANISOU    5  CB  THR A  69     8461  21734  17351     31   2908   -211       C  
ATOM      6  OG1 THR A  69      -0.331 -11.447  82.610  1.00128.70           O  
ANISOU    6  OG1 THR A  69     8700  22390  17808     99   3065    218       O  
ATOM      7  CG2 THR A  69       1.296 -11.548  80.835  1.00123.52           C  
ANISOU    7  CG2 THR A  69     8227  21325  17379    -22   2840   -193       C  
ATOM      8  N   HIS A  70      -0.008  -7.964  79.919  1.00132.11           N  
ANISOU    8  N   HIS A  70     9910  22528  17756    -11   2638  -1171       N  
ATOM      9  CA  HIS A  70       0.263  -7.121  78.757  1.00136.98           C  
ANISOU    9  CA  HIS A  70    10761  22941  18344    -67   2484  -1575       C  
ATOM     10  C   HIS A  70       1.145  -5.939  79.139  1.00132.79           C  
ANISOU   10  C   HIS A  70    10439  22639  17378    -16   2422  -1837       C  
ATOM     11  O   HIS A  70       2.167  -5.669  78.491  1.00137.97           O  
ANISOU   11  O   HIS A  70    11242  23192  17988    -49   2308  -2052       O  
ATOM     12  CB  HIS A  70      -1.061  -6.649  78.151  1.00143.39           C  
ANISOU   12  CB  HIS A  70    11596  23592  19292    -97   2475  -1696       C  
ATOM     13  CG  HIS A  70      -0.906  -5.700  77.004  1.00145.07           C  
ANISOU   13  CG  HIS A  70    12039  23624  19456   -138   2330  -2077       C  
ATOM     14  ND1 HIS A  70      -0.007  -5.905  75.979  1.00144.07           N  
ANISOU   14  ND1 HIS A  70    12016  23291  19432   -198   2202  -2244       N  
ATOM     15  CD2 HIS A  70      -1.550  -4.545  76.712  1.00144.77           C  
ANISOU   15  CD2 HIS A  70    12135  23579  19294   -122   2299  -2301       C  
ATOM     16  CE1 HIS A  70      -0.097  -4.913  75.111  1.00142.49           C  
ANISOU   16  CE1 HIS A  70    12003  22981  19157   -214   2102  -2540       C  
ATOM     17  NE2 HIS A  70      -1.027  -4.074  75.532  1.00142.76           N  
ANISOU   17  NE2 HIS A  70    12053  23123  19067   -169   2159  -2573       N  
ATOM     18  N   LEU A  71       0.767  -5.227  80.205  1.00126.54           N  
ANISOU   18  N   LEU A  71     9650  22155  16274     65   2496  -1832       N  
ATOM     19  CA  LEU A  71       1.594  -4.134  80.703  1.00123.34           C  
ANISOU   19  CA  LEU A  71     9404  21985  15474    112   2439  -2090       C  
ATOM     20  C   LEU A  71       2.953  -4.641  81.169  1.00132.60           C  
ANISOU   20  C   LEU A  71    10551  23330  16501    131   2413  -1990       C  
ATOM     21  O   LEU A  71       3.975  -3.982  80.952  1.00129.97           O  
ANISOU   21  O   LEU A  71    10369  23016  15996    120   2310  -2250       O  
ATOM     22  CB  LEU A  71       0.872  -3.408  81.838  1.00117.84           C  
ANISOU   22  CB  LEU A  71     8677  21608  14489    198   2527  -2096       C  
ATOM     23  CG  LEU A  71       1.604  -2.222  82.465  1.00112.57           C  
ANISOU   23  CG  LEU A  71     8141  21201  13429    245   2467  -2398       C  
ATOM     24  CD1 LEU A  71       1.798  -1.111  81.444  1.00107.94           C  
ANISOU   24  CD1 LEU A  71     7760  20344  12907    188   2353  -2791       C  
ATOM     25  CD2 LEU A  71       0.852  -1.714  83.685  1.00111.46           C  
ANISOU   25  CD2 LEU A  71     7925  21409  13017    336   2562  -2372       C  
ATOM     26  N   GLN A  72       2.981  -5.812  81.810  1.00136.54           N  
ANISOU   26  N   GLN A  72    10846  23949  17086    162   2509  -1597       N  
ATOM     27  CA  GLN A  72       4.243  -6.416  82.228  1.00137.96           C  
ANISOU   27  CA  GLN A  72    10973  24283  17163    185   2491  -1445       C  
ATOM     28  C   GLN A  72       5.185  -6.608  81.045  1.00127.81           C  
ANISOU   28  C   GLN A  72     9797  22680  16084    103   2371  -1620       C  
ATOM     29  O   GLN A  72       6.358  -6.201  81.086  1.00129.51           O  
ANISOU   29  O   GLN A  72    10121  23000  16086    110   2286  -1785       O  
ATOM     30  CB  GLN A  72       3.952  -7.762  82.898  1.00146.72           C  
ANISOU   30  CB  GLN A  72    11821  25471  18453    222   2623   -944       C  
ATOM     31  CG  GLN A  72       5.160  -8.501  83.442  1.00151.86           C  
ANISOU   31  CG  GLN A  72    12380  26303  19017    263   2625   -699       C  
ATOM     32  CD  GLN A  72       4.805  -9.901  83.918  1.00153.89           C  
ANISOU   32  CD  GLN A  72    12369  26537  19564    288   2759   -177       C  
ATOM     33  OE1 GLN A  72       3.664 -10.347  83.775  1.00150.60           O  
ANISOU   33  OE1 GLN A  72    11833  25940  19449    261   2848    -20       O  
ATOM     34  NE2 GLN A  72       5.784 -10.604  84.475  1.00155.84           N  
ANISOU   34  NE2 GLN A  72    12514  26952  19747    338   2774    103       N  
ATOM     35  N   GLU A  73       4.674  -7.209  79.968  1.00118.92           N  
ANISOU   35  N   GLU A  73     8639  21173  15372     24   2357  -1604       N  
ATOM     36  CA  GLU A  73       5.502  -7.466  78.797  1.00113.06           C  
ANISOU   36  CA  GLU A  73     7991  20132  14836    -51   2242  -1771       C  
ATOM     37  C   GLU A  73       5.945  -6.174  78.126  1.00108.85           C  
ANISOU   37  C   GLU A  73     7719  19537  14101    -73   2115  -2195       C  
ATOM     38  O   GLU A  73       7.116  -6.041  77.750  1.00104.75           O  
ANISOU   38  O   GLU A  73     7305  18981  13517    -89   2027  -2336       O  
ATOM     39  CB  GLU A  73       4.754  -8.364  77.813  1.00114.66           C  
ANISOU   39  CB  GLU A  73     8087  19966  15511   -129   2244  -1696       C  
ATOM     40  CG  GLU A  73       4.498  -9.766  78.348  1.00122.79           C  
ANISOU   40  CG  GLU A  73     8828  20978  16850   -123   2369  -1268       C  
ATOM     41  CD  GLU A  73       3.755 -10.648  77.363  1.00128.17           C  
ANISOU   41  CD  GLU A  73     9383  21277  18037   -213   2359  -1236       C  
ATOM     42  OE1 GLU A  73       3.649 -10.264  76.180  1.00128.67           O  
ANISOU   42  OE1 GLU A  73     9606  21101  18180   -277   2232  -1557       O  
ATOM     43  OE2 GLU A  73       3.276 -11.727  77.775  1.00131.55           O  
ANISOU   43  OE2 GLU A  73     9547  21647  18791   -217   2475   -889       O  
ATOM     44  N   LYS A  74       5.038  -5.199  77.973  1.00106.29           N  
ANISOU   44  N   LYS A  74     7493  19197  13698    -70   2109  -2387       N  
ATOM     45  CA  LYS A  74       5.474  -3.970  77.318  1.00109.82           C  
ANISOU   45  CA  LYS A  74     8163  19557  14005    -89   1999  -2756       C  
ATOM     46  C   LYS A  74       6.478  -3.202  78.171  1.00111.59           C  
ANISOU   46  C   LYS A  74     8460  20063  13875    -41   1975  -2885       C  
ATOM     47  O   LYS A  74       7.415  -2.608  77.625  1.00122.79           O  
ANISOU   47  O   LYS A  74    10023  21394  15238    -67   1876  -3119       O  
ATOM     48  CB  LYS A  74       4.285  -3.065  76.979  1.00112.11           C  
ANISOU   48  CB  LYS A  74     8523  19759  14316    -90   2004  -2912       C  
ATOM     49  CG  LYS A  74       3.712  -2.308  78.164  1.00120.49           C  
ANISOU   49  CG  LYS A  74     9556  21110  15116    -20   2087  -2920       C  
ATOM     50  CD  LYS A  74       2.396  -1.629  77.838  1.00127.55           C  
ANISOU   50  CD  LYS A  74    10475  21893  16094    -18   2114  -3010       C  
ATOM     51  CE  LYS A  74       1.318  -2.626  77.481  1.00132.38           C  
ANISOU   51  CE  LYS A  74    10941  22360  16998    -46   2172  -2770       C  
ATOM     52  NZ  LYS A  74       0.007  -1.943  77.354  1.00133.32           N  
ANISOU   52  NZ  LYS A  74    11064  22429  17161    -31   2211  -2833       N  
ATOM     53  N   ASN A  75       6.347  -3.250  79.503  1.00102.43           N  
ANISOU   53  N   ASN A  75     7187  19255  12476     29   2060  -2732       N  
ATOM     54  CA  ASN A  75       7.276  -2.514  80.353  1.00 90.27           C  
ANISOU   54  CA  ASN A  75     5697  18019  10583     74   2023  -2887       C  
ATOM     55  C   ASN A  75       8.658  -3.154  80.355  1.00 97.14           C  
ANISOU   55  C   ASN A  75     6547  18941  11421     67   1971  -2802       C  
ATOM     56  O   ASN A  75       9.672  -2.449  80.274  1.00 97.67           O  
ANISOU   56  O   ASN A  75     6726  19048  11336     55   1879  -3048       O  
ATOM     57  CB  ASN A  75       6.721  -2.406  81.772  1.00 93.15           C  
ANISOU   57  CB  ASN A  75     5936  18786  10671    160   2118  -2754       C  
ATOM     58  CG  ASN A  75       5.508  -1.495  81.854  1.00107.21           C  
ANISOU   58  CG  ASN A  75     7758  20543  12432    174   2157  -2915       C  
ATOM     59  OD1 ASN A  75       5.198  -0.768  80.909  1.00106.19           O  
ANISOU   59  OD1 ASN A  75     7764  20122  12462    123   2102  -3154       O  
ATOM     60  ND2 ASN A  75       4.817  -1.528  82.990  1.00108.86           N  
ANISOU   60  ND2 ASN A  75     7843  21072  12446    251   2254  -2769       N  
ATOM     61  N   TRP A  76       8.728  -4.488  80.409  1.00100.60           N  
ANISOU   61  N   TRP A  76     6831  19353  12039     71   2031  -2453       N  
ATOM     62  CA  TRP A  76      10.048  -5.113  80.356  1.00106.69           C  
ANISOU   62  CA  TRP A  76     7576  20149  12812     66   1985  -2362       C  
ATOM     63  C   TRP A  76      10.676  -5.008  78.972  1.00 98.02           C  
ANISOU   63  C   TRP A  76     6628  18678  11936    -13   1877  -2586       C  
ATOM     64  O   TRP A  76      11.901  -4.863  78.864  1.00 94.84           O  
ANISOU   64  O   TRP A  76     6290  18310  11435    -19   1803  -2689       O  
ATOM     65  CB  TRP A  76       9.998  -6.563  80.836  1.00118.53           C  
ANISOU   65  CB  TRP A  76     8846  21711  14478     98   2086  -1904       C  
ATOM     66  CG  TRP A  76      10.006  -6.667  82.336  1.00129.03           C  
ANISOU   66  CG  TRP A  76    10035  23514  15478    199   2165  -1659       C  
ATOM     67  CD1 TRP A  76       9.284  -5.917  83.221  1.00132.45           C  
ANISOU   67  CD1 TRP A  76    10465  24244  15615    257   2206  -1725       C  
ATOM     68  CD2 TRP A  76      10.834  -7.532  83.127  1.00129.81           C  
ANISOU   68  CD2 TRP A  76     9973  23867  15481    261   2202  -1317       C  
ATOM     69  NE1 TRP A  76       9.588  -6.284  84.511  1.00133.36           N  
ANISOU   69  NE1 TRP A  76    10427  24806  15437    354   2261  -1450       N  
ATOM     70  CE2 TRP A  76      10.538  -7.272  84.480  1.00131.45           C  
ANISOU   70  CE2 TRP A  76    10087  24550  15309    361   2260  -1180       C  
ATOM     71  CE3 TRP A  76      11.785  -8.512  82.821  1.00125.53           C  
ANISOU   71  CE3 TRP A  76     9349  23202  15145    249   2192  -1104       C  
ATOM     72  CZ2 TRP A  76      11.158  -7.957  85.525  1.00129.55           C  
ANISOU   72  CZ2 TRP A  76     9677  24682  14865    452   2301   -818       C  
ATOM     73  CZ3 TRP A  76      12.399  -9.190  83.858  1.00123.43           C  
ANISOU   73  CZ3 TRP A  76     8913  23274  14710    336   2242   -736       C  
ATOM     74  CH2 TRP A  76      12.083  -8.909  85.194  1.00125.70           C  
ANISOU   74  CH2 TRP A  76     9113  24052  14595    439   2293   -586       C  
ATOM     75  N   SER A  77       9.871  -5.064  77.907  1.00 96.88           N  
ANISOU   75  N   SER A  77     6537  18198  12075    -69   1863  -2664       N  
ATOM     76  CA  SER A  77      10.423  -4.831  76.578  1.00 97.83           C  
ANISOU   76  CA  SER A  77     6812  18006  12355   -132   1754  -2898       C  
ATOM     77  C   SER A  77      10.974  -3.416  76.448  1.00 93.90           C  
ANISOU   77  C   SER A  77     6500  17550  11628   -132   1671  -3232       C  
ATOM     78  O   SER A  77      12.074  -3.217  75.916  1.00103.56           O  
ANISOU   78  O   SER A  77     7820  18688  12842   -154   1589  -3368       O  
ATOM     79  CB  SER A  77       9.352  -5.094  75.520  1.00 98.16           C  
ANISOU   79  CB  SER A  77     6861  17737  12697   -182   1747  -2927       C  
ATOM     80  OG  SER A  77       8.839  -6.409  75.641  1.00 98.74           O  
ANISOU   80  OG  SER A  77     6737  17742  13038   -193   1823  -2634       O  
ATOM     81  N   ALA A  78      10.243  -2.422  76.964  1.00 87.74           N  
ANISOU   81  N   ALA A  78     5757  16897  10685   -107   1697  -3360       N  
ATOM     82  CA  ALA A  78      10.738  -1.050  76.938  1.00 82.10           C  
ANISOU   82  CA  ALA A  78     5182  16208   9804   -110   1629  -3675       C  
ATOM     83  C   ALA A  78      12.009  -0.896  77.765  1.00 86.45           C  
ANISOU   83  C   ALA A  78     5714  17023  10108    -87   1594  -3724       C  
ATOM     84  O   ALA A  78      12.927  -0.167  77.373  1.00 85.56           O  
ANISOU   84  O   ALA A  78     5707  16837   9964   -114   1511  -3950       O  
ATOM     85  CB  ALA A  78       9.657  -0.093  77.438  1.00 82.21           C  
ANISOU   85  CB  ALA A  78     5204  16308   9724    -84   1675  -3791       C  
ATOM     86  N   LEU A  79      12.088  -1.581  78.908  1.00 92.52           N  
ANISOU   86  N   LEU A  79     6334  18116  10706    -34   1657  -3498       N  
ATOM     87  CA  LEU A  79      13.289  -1.497  79.735  1.00106.51           C  
ANISOU   87  CA  LEU A  79     8064  20189  12216     -4   1617  -3527       C  
ATOM     88  C   LEU A  79      14.499  -2.103  79.026  1.00105.99           C  
ANISOU   88  C   LEU A  79     8029  19965  12278    -37   1555  -3480       C  
ATOM     89  O   LEU A  79      15.594  -1.523  79.037  1.00101.08           O  
ANISOU   89  O   LEU A  79     7470  19401  11536    -50   1474  -3676       O  
ATOM     90  CB  LEU A  79      13.046  -2.179  81.082  1.00111.99           C  
ANISOU   90  CB  LEU A  79     8571  21291  12689     75   1703  -3239       C  
ATOM     91  CG  LEU A  79      14.274  -2.323  81.982  1.00119.88           C  
ANISOU   91  CG  LEU A  79     9490  22658  13402    119   1662  -3195       C  
ATOM     92  CD1 LEU A  79      14.836  -0.955  82.339  1.00121.99           C  
ANISOU   92  CD1 LEU A  79     9839  23083  13431    107   1567  -3605       C  
ATOM     93  CD2 LEU A  79      13.925  -3.106  83.235  1.00126.84           C  
ANISOU   93  CD2 LEU A  79    10169  23945  14078    210   1756  -2837       C  
ATOM     94  N   LEU A  80      14.327  -3.281  78.419  1.00104.19           N  
ANISOU   94  N   LEU A  80     7742  19531  12313    -52   1591  -3229       N  
ATOM     95  CA  LEU A  80      15.422  -3.885  77.664  1.00 94.04           C  
ANISOU   95  CA  LEU A  80     6484  18065  11183    -83   1534  -3197       C  
ATOM     96  C   LEU A  80      15.861  -2.982  76.518  1.00 90.17           C  
ANISOU   96  C   LEU A  80     6187  17298  10776   -137   1436  -3517       C  
ATOM     97  O   LEU A  80      17.065  -2.824  76.261  1.00 79.10           O  
ANISOU   97  O   LEU A  80     4839  15879   9335   -149   1368  -3614       O  
ATOM     98  CB  LEU A  80      15.007  -5.261  77.146  1.00 86.18           C  
ANISOU   98  CB  LEU A  80     5376  16854  10515    -97   1590  -2915       C  
ATOM     99  CG  LEU A  80      14.790  -6.321  78.226  1.00 85.75           C  
ANISOU   99  CG  LEU A  80     5094  17043  10444    -40   1697  -2522       C  
ATOM    100  CD1 LEU A  80      14.262  -7.610  77.624  1.00 85.78           C  
ANISOU  100  CD1 LEU A  80     4968  16765  10859    -70   1756  -2277       C  
ATOM    101  CD2 LEU A  80      16.086  -6.573  78.982  1.00 86.05           C  
ANISOU  101  CD2 LEU A  80     5061  17360  10275      6   1677  -2401       C  
ATOM    102  N   THR A  81      14.899  -2.373  75.818  1.00 88.21           N  
ANISOU  102  N   THR A  81     6033  16840  10645   -164   1433  -3661       N  
ATOM    103  CA  THR A  81      15.255  -1.462  74.737  1.00 88.44           C  
ANISOU  103  CA  THR A  81     6226  16625  10752   -203   1351  -3921       C  
ATOM    104  C   THR A  81      15.996  -0.240  75.266  1.00 88.51           C  
ANISOU  104  C   THR A  81     6292  16783  10555   -200   1304  -4158       C  
ATOM    105  O   THR A  81      16.907   0.273  74.608  1.00 91.46           O  
ANISOU  105  O   THR A  81     6758  17021  10972   -227   1234  -4312       O  
ATOM    106  CB  THR A  81      14.006  -1.040  73.968  1.00 89.68           C  
ANISOU  106  CB  THR A  81     6444  16570  11060   -221   1362  -3990       C  
ATOM    107  OG1 THR A  81      13.079  -0.420  74.865  1.00101.88           O  
ANISOU  107  OG1 THR A  81     7949  18289  12473   -194   1421  -4018       O  
ATOM    108  CG2 THR A  81      13.358  -2.248  73.314  1.00 87.12           C  
ANISOU  108  CG2 THR A  81     6052  16075  10972   -236   1388  -3803       C  
ATOM    109  N   ALA A  82      15.626   0.238  76.457  1.00 84.96           N  
ANISOU  109  N   ALA A  82     5775  16616   9892   -169   1341  -4199       N  
ATOM    110  CA  ALA A  82      16.351   1.355  77.054  1.00 83.55           C  
ANISOU  110  CA  ALA A  82     5614  16598   9533   -173   1289  -4458       C  
ATOM    111  C   ALA A  82      17.782   0.958  77.402  1.00 84.19           C  
ANISOU  111  C   ALA A  82     5652  16845   9490   -169   1238  -4432       C  
ATOM    112  O   ALA A  82      18.713   1.761  77.247  1.00 79.68           O  
ANISOU  112  O   ALA A  82     5131  16243   8900   -199   1167  -4658       O  
ATOM    113  CB  ALA A  82      15.613   1.860  78.292  1.00 81.91           C  
ANISOU  113  CB  ALA A  82     5321  16690   9111   -135   1335  -4519       C  
ATOM    114  N   VAL A  83      17.972  -0.273  77.882  1.00 87.74           N  
ANISOU  114  N   VAL A  83     5990  17468   9878   -132   1278  -4143       N  
ATOM    115  CA  VAL A  83      19.323  -0.781  78.127  1.00 85.55           C  
ANISOU  115  CA  VAL A  83     5660  17333   9510   -122   1235  -4068       C  
ATOM    116  C   VAL A  83      20.132  -0.782  76.834  1.00 83.95           C  
ANISOU  116  C   VAL A  83     5577  16788   9532   -169   1173  -4148       C  
ATOM    117  O   VAL A  83      21.300  -0.366  76.808  1.00 81.13           O  
ANISOU  117  O   VAL A  83     5244  16469   9112   -184   1106  -4287       O  
ATOM    118  CB  VAL A  83      19.258  -2.188  78.752  1.00 82.73           C  
ANISOU  118  CB  VAL A  83     5144  17171   9121    -68   1306  -3680       C  
ATOM    119  CG1 VAL A  83      20.640  -2.809  78.815  1.00 82.91           C  
ANISOU  119  CG1 VAL A  83     5110  17279   9111    -57   1263  -3564       C  
ATOM    120  CG2 VAL A  83      18.640  -2.127  80.133  1.00 89.74           C  
ANISOU  120  CG2 VAL A  83     5899  18470   9727     -6   1363  -3586       C  
ATOM    121  N   VAL A  84      19.522  -1.246  75.743  1.00 89.59           N  
ANISOU  121  N   VAL A  84     6356  17179  10506   -191   1193  -4067       N  
ATOM    122  CA  VAL A  84      20.209  -1.246  74.453  1.00 87.12           C  
ANISOU  122  CA  VAL A  84     6153  16560  10387   -225   1135  -4143       C  
ATOM    123  C   VAL A  84      20.563   0.178  74.034  1.00 86.64           C  
ANISOU  123  C   VAL A  84     6208  16395  10315   -255   1077  -4437       C  
ATOM    124  O   VAL A  84      21.667   0.442  73.540  1.00 97.84           O  
ANISOU  124  O   VAL A  84     7677  17728  11769   -272   1020  -4526       O  
ATOM    125  CB  VAL A  84      19.351  -1.955  73.389  1.00 82.99           C  
ANISOU  125  CB  VAL A  84     5661  15754  10119   -239   1159  -4036       C  
ATOM    126  CG1 VAL A  84      20.050  -1.933  72.039  1.00 80.45           C  
ANISOU  126  CG1 VAL A  84     5447  15159   9962   -263   1095  -4126       C  
ATOM    127  CG2 VAL A  84      19.062  -3.387  73.814  1.00 86.34           C  
ANISOU  127  CG2 VAL A  84     5936  16245  10625   -218   1223  -3743       C  
ATOM    128  N   ILE A  85      19.636   1.118  74.237  1.00 85.04           N  
ANISOU  128  N   ILE A  85     6032  16190  10091   -261   1096  -4577       N  
ATOM    129  CA  ILE A  85      19.871   2.510  73.855  1.00 74.44           C  
ANISOU  129  CA  ILE A  85     4767  14717   8801   -291   1056  -4835       C  
ATOM    130  C   ILE A  85      21.050   3.086  74.628  1.00 82.26           C  
ANISOU  130  C   ILE A  85     5708  15904   9643   -303   1008  -5003       C  
ATOM    131  O   ILE A  85      21.929   3.747  74.059  1.00 90.52           O  
ANISOU  131  O   ILE A  85     6803  16805  10787   -331    961  -5144       O  
ATOM    132  CB  ILE A  85      18.601   3.352  74.074  1.00 81.50           C  
ANISOU  132  CB  ILE A  85     5666  15587   9715   -289   1098  -4935       C  
ATOM    133  CG1 ILE A  85      17.501   2.944  73.094  1.00 85.61           C  
ANISOU  133  CG1 ILE A  85     6239  15881  10409   -284   1132  -4802       C  
ATOM    134  CG2 ILE A  85      18.918   4.832  73.935  1.00 78.21           C  
ANISOU  134  CG2 ILE A  85     5281  15063   9374   -318   1070  -5200       C  
ATOM    135  CD1 ILE A  85      16.152   3.572  73.380  1.00 74.51           C  
ANISOU  135  CD1 ILE A  85     4820  14474   9018   -273   1184  -4849       C  
ATOM    136  N   ILE A  86      21.073   2.864  75.944  1.00 84.80           N  
ANISOU  136  N   ILE A  86     5916  16578   9726   -277   1019  -4991       N  
ATOM    137  CA  ILE A  86      22.139   3.444  76.756  1.00 95.85           C  
ANISOU  137  CA  ILE A  86     7244  18216  10960   -289    962  -5185       C  
ATOM    138  C   ILE A  86      23.486   2.816  76.403  1.00 84.05           C  
ANISOU  138  C   ILE A  86     5751  16711   9475   -291    917  -5094       C  
ATOM    139  O   ILE A  86      24.505   3.516  76.323  1.00 81.83           O  
ANISOU  139  O   ILE A  86     5469  16411   9211   -324    858  -5291       O  
ATOM    140  CB  ILE A  86      21.809   3.339  78.261  1.00103.00           C  
ANISOU  140  CB  ILE A  86     8010  19561  11566   -249    978  -5188       C  
ATOM    141  CG1 ILE A  86      22.708   4.280  79.063  1.00103.58           C  
ANISOU  141  CG1 ILE A  86     7996  19873  11487   -273    902  -5496       C  
ATOM    142  CG2 ILE A  86      21.927   1.916  78.783  1.00103.27           C  
ANISOU  142  CG2 ILE A  86     7954  19837  11447   -191   1016  -4848       C  
ATOM    143  CD1 ILE A  86      22.535   5.737  78.696  1.00103.30           C  
ANISOU  143  CD1 ILE A  86     7999  19600  11649   -332    878  -5829       C  
ATOM    144  N   LEU A  87      23.515   1.501  76.159  1.00 77.63           N  
ANISOU  144  N   LEU A  87     4924  15886   8684   -260    948  -4798       N  
ATOM    145  CA  LEU A  87      24.761   0.873  75.732  1.00 76.92           C  
ANISOU  145  CA  LEU A  87     4835  15749   8641   -259    910  -4699       C  
ATOM    146  C   LEU A  87      25.250   1.481  74.425  1.00 83.44           C  
ANISOU  146  C   LEU A  87     5791  16219   9694   -299    872  -4833       C  
ATOM    147  O   LEU A  87      26.437   1.801  74.282  1.00 82.33           O  
ANISOU  147  O   LEU A  87     5652  16073   9558   -315    821  -4930       O  
ATOM    148  CB  LEU A  87      24.577  -0.637  75.580  1.00 79.04           C  
ANISOU  148  CB  LEU A  87     5053  16001   8978   -223    958  -4359       C  
ATOM    149  CG  LEU A  87      24.418  -1.477  76.844  1.00 84.78           C  
ANISOU  149  CG  LEU A  87     5614  17097   9502   -169   1003  -4123       C  
ATOM    150  CD1 LEU A  87      24.476  -2.958  76.497  1.00 78.69           C  
ANISOU  150  CD1 LEU A  87     4776  16221   8903   -143   1049  -3784       C  
ATOM    151  CD2 LEU A  87      25.492  -1.116  77.853  1.00 80.65           C  
ANISOU  151  CD2 LEU A  87     4995  16937   8709   -152    948  -4211       C  
ATOM    152  N   THR A  88      24.342   1.646  73.458  1.00 89.79           N  
ANISOU  152  N   THR A  88     6691  16742  10682   -309    899  -4825       N  
ATOM    153  CA  THR A  88      24.703   2.261  72.184  1.00 92.94           C  
ANISOU  153  CA  THR A  88     7198  16834  11279   -331    871  -4917       C  
ATOM    154  C   THR A  88      25.319   3.636  72.397  1.00 95.27           C  
ANISOU  154  C   THR A  88     7489  17129  11582   -364    839  -5174       C  
ATOM    155  O   THR A  88      26.416   3.928  71.898  1.00104.67           O  
ANISOU  155  O   THR A  88     8698  18221  12849   -377    805  -5229       O  
ATOM    156  CB  THR A  88      23.470   2.375  71.286  1.00 82.13           C  
ANISOU  156  CB  THR A  88     5905  15241  10061   -328    905  -4879       C  
ATOM    157  OG1 THR A  88      22.857   1.089  71.143  1.00 81.51           O  
ANISOU  157  OG1 THR A  88     5804  15160  10005   -307    934  -4672       O  
ATOM    158  CG2 THR A  88      23.854   2.909  69.915  1.00 81.35           C  
ANISOU  158  CG2 THR A  88     5898  14870  10142   -334    881  -4922       C  
ATOM    159  N   ILE A  89      24.614   4.497  73.131  1.00 73.83           N  
ANISOU  159  N   ILE A  89     4731  14508   8813   -378    856  -5337       N  
ATOM    160  CA  ILE A  89      25.071   5.871  73.309  1.00 80.76           C  
ANISOU  160  CA  ILE A  89     5578  15343   9765   -418    834  -5611       C  
ATOM    161  C   ILE A  89      26.444   5.894  73.969  1.00 94.98           C  
ANISOU  161  C   ILE A  89     7297  17346  11446   -434    778  -5725       C  
ATOM    162  O   ILE A  89      27.369   6.568  73.495  1.00 82.03           O  
ANISOU  162  O   ILE A  89     5661  15558   9949   -463    753  -5850       O  
ATOM    163  CB  ILE A  89      24.036   6.678  74.112  1.00 76.22           C  
ANISOU  163  CB  ILE A  89     4947  14863   9152   -428    861  -5778       C  
ATOM    164  CG1 ILE A  89      22.730   6.778  73.325  1.00 75.12           C  
ANISOU  164  CG1 ILE A  89     4888  14491   9162   -410    919  -5668       C  
ATOM    165  CG2 ILE A  89      24.571   8.059  74.430  1.00 77.64           C  
ANISOU  165  CG2 ILE A  89     5054  15008   9438   -476    839  -6094       C  
ATOM    166  CD1 ILE A  89      21.617   7.476  74.069  1.00 79.99           C  
ANISOU  166  CD1 ILE A  89     5453  15187   9752   -412    957  -5798       C  
ATOM    167  N   ALA A  90      26.606   5.134  75.057  1.00 94.75           N  
ANISOU  167  N   ALA A  90     7178  17668  11155   -410    761  -5661       N  
ATOM    168  CA  ALA A  90      27.867   5.153  75.794  1.00 91.43           C  
ANISOU  168  CA  ALA A  90     6656  17503  10581   -419    702  -5771       C  
ATOM    169  C   ALA A  90      29.020   4.633  74.939  1.00 85.76           C  
ANISOU  169  C   ALA A  90     5991  16624   9970   -415    681  -5639       C  
ATOM    170  O   ALA A  90      30.080   5.269  74.854  1.00 85.56           O  
ANISOU  170  O   ALA A  90     5936  16565  10006   -446    640  -5810       O  
ATOM    171  CB  ALA A  90      27.733   4.336  77.080  1.00 89.33           C  
ANISOU  171  CB  ALA A  90     6270  17678   9992   -373    699  -5658       C  
ATOM    172  N   GLY A  91      28.835   3.474  74.301  1.00 78.75           N  
ANISOU  172  N   GLY A  91     5167  15629   9123   -378    709  -5345       N  
ATOM    173  CA  GLY A  91      29.906   2.906  73.502  1.00 74.95           C  
ANISOU  173  CA  GLY A  91     4727  15007   8745   -369    688  -5215       C  
ATOM    174  C   GLY A  91      30.322   3.801  72.351  1.00 83.06           C  
ANISOU  174  C   GLY A  91     5843  15708  10010   -398    682  -5333       C  
ATOM    175  O   GLY A  91      31.517   3.989  72.097  1.00 73.09           O  
ANISOU  175  O   GLY A  91     4567  14406   8799   -407    650  -5375       O  
ATOM    176  N   ASN A  92      29.347   4.378  71.643  1.00 89.07           N  
ANISOU  176  N   ASN A  92     6680  16239  10922   -405    718  -5366       N  
ATOM    177  CA  ASN A  92      29.711   5.195  70.492  1.00 94.16           C  
ANISOU  177  CA  ASN A  92     7390  16590  11797   -415    726  -5418       C  
ATOM    178  C   ASN A  92      30.300   6.536  70.911  1.00 97.72           C  
ANISOU  178  C   ASN A  92     7769  17031  12329   -459    717  -5684       C  
ATOM    179  O   ASN A  92      31.190   7.055  70.226  1.00 99.20           O  
ANISOU  179  O   ASN A  92     7963  17047  12681   -466    716  -5712       O  
ATOM    180  CB  ASN A  92      28.504   5.384  69.579  1.00 96.72           C  
ANISOU  180  CB  ASN A  92     7797  16701  12253   -398    770  -5340       C  
ATOM    181  CG  ASN A  92      28.118   4.103  68.870  1.00 94.51           C  
ANISOU  181  CG  ASN A  92     7579  16374  11957   -360    775  -5111       C  
ATOM    182  OD1 ASN A  92      27.068   3.520  69.140  1.00103.18           O  
ANISOU  182  OD1 ASN A  92     8679  17531  12992   -349    796  -5035       O  
ATOM    183  ND2 ASN A  92      28.979   3.646  67.967  1.00 80.68           N  
ANISOU  183  ND2 ASN A  92     5865  14516  10275   -339    757  -5012       N  
ATOM    184  N   ILE A  93      29.855   7.097  72.040  1.00 96.06           N  
ANISOU  184  N   ILE A  93     7474  17008  12018   -488    711  -5890       N  
ATOM    185  CA  ILE A  93      30.517   8.288  72.565  1.00 94.37           C  
ANISOU  185  CA  ILE A  93     7158  16810  11887   -537    693  -6194       C  
ATOM    186  C   ILE A  93      31.968   7.976  72.912  1.00 84.40           C  
ANISOU  186  C   ILE A  93     5834  15703  10531   -544    640  -6232       C  
ATOM    187  O   ILE A  93      32.877   8.759  72.606  1.00 77.19           O  
ANISOU  187  O   ILE A  93     4885  14646   9799   -572    638  -6373       O  
ATOM    188  CB  ILE A  93      29.743   8.849  73.773  1.00 93.00           C  
ANISOU  188  CB  ILE A  93     6885  16856  11597   -565    686  -6431       C  
ATOM    189  CG1 ILE A  93      28.461   9.546  73.304  1.00 93.97           C  
ANISOU  189  CG1 ILE A  93     7054  16744  11907   -566    749  -6440       C  
ATOM    190  CG2 ILE A  93      30.609   9.818  74.568  1.00 83.83           C  
ANISOU  190  CG2 ILE A  93     5577  15813  10461   -621    644  -6788       C  
ATOM    191  CD1 ILE A  93      27.655  10.171  74.424  1.00 94.00           C  
ANISOU  191  CD1 ILE A  93     6952  16932  11831   -593    747  -6675       C  
ATOM    192  N   LEU A  94      32.211   6.823  73.544  1.00 85.86           N  
ANISOU  192  N   LEU A  94     5995  16177  10451   -513    605  -6084       N  
ATOM    193  CA  LEU A  94      33.582   6.435  73.863  1.00 83.34           C  
ANISOU  193  CA  LEU A  94     5612  16021  10034   -509    556  -6076       C  
ATOM    194  C   LEU A  94      34.426   6.289  72.603  1.00 81.29           C  
ANISOU  194  C   LEU A  94     5435  15464   9988   -498    566  -5921       C  
ATOM    195  O   LEU A  94      35.590   6.708  72.575  1.00 77.76           O  
ANISOU  195  O   LEU A  94     4936  14996   9613   -518    540  -6022       O  
ATOM    196  CB  LEU A  94      33.596   5.135  74.666  1.00 83.43           C  
ANISOU  196  CB  LEU A  94     5572  16375   9752   -463    532  -5866       C  
ATOM    197  CG  LEU A  94      33.190   5.226  76.135  1.00 80.31           C  
ANISOU  197  CG  LEU A  94     5043  16405   9067   -460    506  -6012       C  
ATOM    198  CD1 LEU A  94      33.315   3.863  76.799  1.00 80.85           C  
ANISOU  198  CD1 LEU A  94     5047  16796   8878   -399    498  -5716       C  
ATOM    199  CD2 LEU A  94      34.047   6.259  76.850  1.00 82.51           C  
ANISOU  199  CD2 LEU A  94     5197  16854   9299   -504    453  -6378       C  
ATOM    200  N   VAL A  95      33.864   5.681  71.555  1.00 81.22           N  
ANISOU  200  N   VAL A  95     5544  15240  10077   -465    601  -5681       N  
ATOM    201  CA  VAL A  95      34.616   5.528  70.309  1.00 80.76           C  
ANISOU  201  CA  VAL A  95     5554  14932  10198   -445    610  -5535       C  
ATOM    202  C   VAL A  95      34.944   6.892  69.712  1.00 75.76           C  
ANISOU  202  C   VAL A  95     4912  14056   9817   -474    638  -5690       C  
ATOM    203  O   VAL A  95      36.066   7.129  69.240  1.00 73.84           O  
ANISOU  203  O   VAL A  95     4649  13713   9694   -476    630  -5676       O  
ATOM    204  CB  VAL A  95      33.845   4.642  69.312  1.00 73.87           C  
ANISOU  204  CB  VAL A  95     4792  13911   9364   -400    640  -5294       C  
ATOM    205  CG1 VAL A  95      34.509   4.682  67.945  1.00 69.37           C  
ANISOU  205  CG1 VAL A  95     4284  13102   8973   -374    653  -5181       C  
ATOM    206  CG2 VAL A  95      33.777   3.214  69.824  1.00 72.34           C  
ANISOU  206  CG2 VAL A  95     4579  13911   8995   -371    624  -5115       C  
ATOM    207  N   ILE A  96      33.973   7.810  69.721  1.00 79.85           N  
ANISOU  207  N   ILE A  96     5430  14466  10444   -493    679  -5821       N  
ATOM    208  CA  ILE A  96      34.220   9.157  69.208  1.00 73.91           C  
ANISOU  208  CA  ILE A  96     4637  13464   9980   -516    724  -5952       C  
ATOM    209  C   ILE A  96      35.352   9.819  69.985  1.00 79.44           C  
ANISOU  209  C   ILE A  96     5214  14246  10724   -565    692  -6203       C  
ATOM    210  O   ILE A  96      36.257  10.432  69.403  1.00 77.44           O  
ANISOU  210  O   ILE A  96     4923  13802  10697   -573    712  -6211       O  
ATOM    211  CB  ILE A  96      32.931   9.995  69.258  1.00 74.20           C  
ANISOU  211  CB  ILE A  96     4672  13390  10129   -527    776  -6056       C  
ATOM    212  CG1 ILE A  96      31.892   9.428  68.286  1.00 75.88           C  
ANISOU  212  CG1 ILE A  96     5002  13494  10335   -473    810  -5796       C  
ATOM    213  CG2 ILE A  96      33.234  11.450  68.936  1.00 75.47           C  
ANISOU  213  CG2 ILE A  96     4751  13297  10628   -554    833  -6212       C  
ATOM    214  CD1 ILE A  96      30.494   9.985  68.470  1.00 72.78           C  
ANISOU  214  CD1 ILE A  96     4612  13051   9989   -476    854  -5860       C  
ATOM    215  N   MET A  97      35.319   9.695  71.316  1.00 86.15           N  
ANISOU  215  N   MET A  97     5983  15399  11349   -593    644  -6409       N  
ATOM    216  CA  MET A  97      36.370  10.279  72.146  1.00100.52           C  
ANISOU  216  CA  MET A  97     7671  17353  13170   -634    607  -6687       C  
ATOM    217  C   MET A  97      37.732   9.675  71.816  1.00 99.96           C  
ANISOU  217  C   MET A  97     7601  17303  13075   -617    570  -6529       C  
ATOM    218  O   MET A  97      38.728  10.398  71.680  1.00 95.29           O  
ANISOU  218  O   MET A  97     6937  16589  12681   -644    571  -6653       O  
ATOM    219  CB  MET A  97      36.048  10.074  73.630  1.00107.81           C  
ANISOU  219  CB  MET A  97     8501  18686  13778   -648    557  -6903       C  
ATOM    220  CG  MET A  97      34.748  10.716  74.113  1.00110.21           C  
ANISOU  220  CG  MET A  97     8776  19007  14093   -674    580  -7096       C  
ATOM    221  SD  MET A  97      34.808  12.509  74.297  1.00105.70           S  
ANISOU  221  SD  MET A  97     8075  18210  13878   -743    619  -7540       S  
ATOM    222  CE  MET A  97      33.129  12.849  74.817  1.00106.52           C  
ANISOU  222  CE  MET A  97     8158  18376  13940   -766    630  -7642       C  
ATOM    223  N   ALA A  98      37.788   8.349  71.669  1.00 98.40           N  
ANISOU  223  N   ALA A  98     7476  17243  12669   -572    540  -6247       N  
ATOM    224  CA  ALA A  98      39.059   7.680  71.412  1.00 97.27           C  
ANISOU  224  CA  ALA A  98     7325  17136  12496   -553    500  -6084       C  
ATOM    225  C   ALA A  98      39.637   8.081  70.061  1.00 88.19           C  
ANISOU  225  C   ALA A  98     6226  15640  11643   -545    540  -5956       C  
ATOM    226  O   ALA A  98      40.853   8.262  69.930  1.00 89.29           O  
ANISOU  226  O   ALA A  98     6309  15743  11874   -557    518  -5961       O  
ATOM    227  CB  ALA A  98      38.882   6.164  71.493  1.00 98.53           C  
ANISOU  227  CB  ALA A  98     7537  17477  12423   -503    475  -5802       C  
ATOM    228  N   VAL A  99      38.788   8.222  69.041  1.00 81.46           N  
ANISOU  228  N   VAL A  99     5468  14552  10932   -519    600  -5824       N  
ATOM    229  CA  VAL A  99      39.300   8.594  67.725  1.00 78.73           C  
ANISOU  229  CA  VAL A  99     5152  13925  10838   -494    646  -5670       C  
ATOM    230  C   VAL A  99      39.715  10.061  67.705  1.00 80.91           C  
ANISOU  230  C   VAL A  99     5323  14008  11411   -539    686  -5862       C  
ATOM    231  O   VAL A  99      40.700  10.430  67.055  1.00 77.62           O  
ANISOU  231  O   VAL A  99     4864  13437  11193   -535    704  -5784       O  
ATOM    232  CB  VAL A  99      38.268   8.281  66.628  1.00 83.34           C  
ANISOU  232  CB  VAL A  99     5849  14363  11454   -440    698  -5460       C  
ATOM    233  CG1 VAL A  99      38.787   8.731  65.268  1.00 71.30           C  
ANISOU  233  CG1 VAL A  99     4330  12601  10160   -399    753  -5289       C  
ATOM    234  CG2 VAL A  99      37.959   6.795  66.604  1.00 85.65           C  
ANISOU  234  CG2 VAL A  99     6226  14809  11510   -400    662  -5286       C  
ATOM    235  N   SER A 100      38.983  10.922  68.419  1.00 90.61           N  
ANISOU  235  N   SER A 100     6495  15234  12700   -581    705  -6118       N  
ATOM    236  CA  SER A 100      39.296  12.347  68.399  1.00 96.27           C  
ANISOU  236  CA  SER A 100     7094  15725  13760   -624    755  -6320       C  
ATOM    237  C   SER A 100      40.472  12.717  69.297  1.00101.40           C  
ANISOU  237  C   SER A 100     7614  16484  14431   -678    703  -6579       C  
ATOM    238  O   SER A 100      41.069  13.783  69.103  1.00 97.88           O  
ANISOU  238  O   SER A 100     7060  15810  14321   -712    743  -6702       O  
ATOM    239  CB  SER A 100      38.066  13.157  68.810  1.00 87.44           C  
ANISOU  239  CB  SER A 100     5948  14540  12733   -647    802  -6522       C  
ATOM    240  OG  SER A 100      37.581  12.729  70.069  1.00 82.41           O  
ANISOU  240  OG  SER A 100     5301  14220  11792   -670    743  -6733       O  
ATOM    241  N   LEU A 101      40.822  11.873  70.266  1.00105.87           N  
ANISOU  241  N   LEU A 101     8173  17393  14659   -681    621  -6650       N  
ATOM    242  CA  LEU A 101      41.888  12.179  71.212  1.00105.25           C  
ANISOU  242  CA  LEU A 101     7962  17480  14547   -720    567  -6904       C  
ATOM    243  C   LEU A 101      43.175  11.412  70.946  1.00109.68           C  
ANISOU  243  C   LEU A 101     8528  18115  15029   -704    510  -6693       C  
ATOM    244  O   LEU A 101      44.253  12.014  70.897  1.00112.52           O  
ANISOU  244  O   LEU A 101     8791  18368  15594   -736    502  -6783       O  
ATOM    245  CB  LEU A 101      41.406  11.903  72.642  1.00 96.82           C  
ANISOU  245  CB  LEU A 101     6843  16810  13136   -724    520  -7153       C  
ATOM    246  CG  LEU A 101      40.265  12.800  73.122  1.00 90.44           C  
ANISOU  246  CG  LEU A 101     5991  15964  12408   -748    570  -7450       C  
ATOM    247  CD1 LEU A 101      39.784  12.377  74.506  1.00 87.01           C  
ANISOU  247  CD1 LEU A 101     5500  15987  11575   -734    528  -7653       C  
ATOM    248  CD2 LEU A 101      40.704  14.255  73.109  1.00 97.12           C  
ANISOU  248  CD2 LEU A 101     6703  16538  13659   -796    622  -7763       C  
ATOM    249  N   GLU A 102      43.097  10.095  70.771  1.00108.52           N  
ANISOU  249  N   GLU A 102     8481  18134  14617   -655    475  -6413       N  
ATOM    250  CA  GLU A 102      44.297   9.274  70.644  1.00115.88           C  
ANISOU  250  CA  GLU A 102     9405  19167  15457   -635    419  -6221       C  
ATOM    251  C   GLU A 102      45.002   9.556  69.323  1.00121.30           C  
ANISOU  251  C   GLU A 102    10115  19531  16443   -623    464  -6026       C  
ATOM    252  O   GLU A 102      44.396   9.453  68.250  1.00123.17           O  
ANISOU  252  O   GLU A 102    10448  19568  16783   -583    527  -5828       O  
ATOM    253  CB  GLU A 102      43.940   7.795  70.754  1.00117.85           C  
ANISOU  253  CB  GLU A 102     9740  19636  15401   -581    387  -5968       C  
ATOM    254  CG  GLU A 102      43.344   7.401  72.094  1.00121.93           C  
ANISOU  254  CG  GLU A 102    10207  20522  15598   -581    345  -6095       C  
ATOM    255  CD  GLU A 102      44.323   7.575  73.238  1.00125.18           C  
ANISOU  255  CD  GLU A 102    10472  21230  15860   -605    273  -6282       C  
ATOM    256  OE1 GLU A 102      45.544   7.457  73.002  1.00122.73           O  
ANISOU  256  OE1 GLU A 102    10122  20886  15625   -610    237  -6200       O  
ATOM    257  OE2 GLU A 102      43.870   7.834  74.374  1.00128.12           O  
ANISOU  257  OE2 GLU A 102    10761  21888  16028   -614    256  -6514       O  
ATOM    258  N   LYS A 103      46.288   9.911  69.403  1.00120.84           N  
ANISOU  258  N   LYS A 103     9957  19444  16512   -653    433  -6075       N  
ATOM    259  CA  LYS A 103      47.063  10.228  68.211  1.00111.73           C  
ANISOU  259  CA  LYS A 103     8796  18011  15645   -639    480  -5883       C  
ATOM    260  C   LYS A 103      47.475   8.988  67.428  1.00103.42           C  
ANISOU  260  C   LYS A 103     7835  17001  14461   -571    471  -5546       C  
ATOM    261  O   LYS A 103      47.841   9.110  66.255  1.00109.36           O  
ANISOU  261  O   LYS A 103     8605  17543  15405   -534    530  -5343       O  
ATOM    262  CB  LYS A 103      48.307  11.035  68.591  1.00113.57           C  
ANISOU  262  CB  LYS A 103     8877  18193  16080   -698    450  -6054       C  
ATOM    263  CG  LYS A 103      47.995  12.360  69.269  1.00121.05           C  
ANISOU  263  CG  LYS A 103     9712  19047  17235   -763    472  -6423       C  
ATOM    264  CD  LYS A 103      47.015  13.187  68.448  1.00124.18           C  
ANISOU  264  CD  LYS A 103    10137  19129  17916   -755    579  -6390       C  
ATOM    265  CE  LYS A 103      46.651  14.486  69.156  1.00127.20           C  
ANISOU  265  CE  LYS A 103    10396  19397  18537   -817    610  -6777       C  
ATOM    266  NZ  LYS A 103      47.848  15.334  69.415  1.00134.20           N  
ANISOU  266  NZ  LYS A 103    11117  20159  19713   -874    598  -6963       N  
ATOM    267  N   LYS A 104      47.426   7.804  68.042  1.00 95.57           N  
ANISOU  267  N   LYS A 104     6881  16276  13156   -545    409  -5476       N  
ATOM    268  CA  LYS A 104      47.710   6.582  67.296  1.00 88.25           C  
ANISOU  268  CA  LYS A 104     6033  15363  12137   -475    412  -5177       C  
ATOM    269  C   LYS A 104      46.638   6.292  66.256  1.00 88.90           C  
ANISOU  269  C   LYS A 104     6242  15292  12245   -419    484  -5027       C  
ATOM    270  O   LYS A 104      46.940   5.725  65.200  1.00 84.47           O  
ANISOU  270  O   LYS A 104     5734  14634  11728   -358    519  -4812       O  
ATOM    271  CB  LYS A 104      47.816   5.387  68.243  1.00 82.17           C  
ANISOU  271  CB  LYS A 104     5252  14899  11069   -458    340  -5120       C  
ATOM    272  CG  LYS A 104      49.054   5.343  69.110  1.00 92.51           C  
ANISOU  272  CG  LYS A 104     6435  16406  12308   -488    260  -5178       C  
ATOM    273  CD  LYS A 104      49.081   4.035  69.888  1.00100.14           C  
ANISOU  273  CD  LYS A 104     7384  17674  12992   -449    204  -5032       C  
ATOM    274  CE  LYS A 104      50.377   3.852  70.655  1.00106.99           C  
ANISOU  274  CE  LYS A 104     8118  18760  13771   -463    122  -5029       C  
ATOM    275  NZ  LYS A 104      50.417   2.517  71.316  1.00109.05           N  
ANISOU  275  NZ  LYS A 104     8342  19304  13787   -411     81  -4819       N  
ATOM    276  N   LEU A 105      45.398   6.683  66.525  1.00 97.01           N  
ANISOU  276  N   LEU A 105     7310  16309  13240   -436    508  -5148       N  
ATOM    277  CA  LEU A 105      44.246   6.325  65.695  1.00101.99           C  
ANISOU  277  CA  LEU A 105     8058  16842  13852   -385    562  -5020       C  
ATOM    278  C   LEU A 105      43.851   7.454  64.751  1.00106.16           C  
ANISOU  278  C   LEU A 105     8588  17118  14631   -378    643  -5012       C  
ATOM    279  O   LEU A 105      42.677   7.799  64.632  1.00106.94           O  
ANISOU  279  O   LEU A 105     8734  17158  14741   -374    680  -5051       O  
ATOM    280  CB  LEU A 105      43.075   5.931  66.587  1.00 98.70           C  
ANISOU  280  CB  LEU A 105     7679  16591  13233   -400    540  -5115       C  
ATOM    281  CG  LEU A 105      43.358   4.806  67.584  1.00102.02           C  
ANISOU  281  CG  LEU A 105     8070  17288  13406   -396    473  -5076       C  
ATOM    282  CD1 LEU A 105      42.205   4.651  68.558  1.00105.60           C  
ANISOU  282  CD1 LEU A 105     8526  17922  13675   -412    462  -5179       C  
ATOM    283  CD2 LEU A 105      43.640   3.494  66.865  1.00102.88           C  
ANISOU  283  CD2 LEU A 105     8236  17380  13473   -330    478  -4821       C  
ATOM    284  N   GLN A 106      44.828   8.042  64.059  1.00106.49           N  
ANISOU  284  N   GLN A 106     8564  17012  14887   -369    677  -4934       N  
ATOM    285  CA  GLN A 106      44.581   9.168  63.169  1.00 97.29           C  
ANISOU  285  CA  GLN A 106     7361  15611  13993   -353    767  -4878       C  
ATOM    286  C   GLN A 106      44.645   8.780  61.693  1.00 87.39           C  
ANISOU  286  C   GLN A 106     6159  14284  12762   -254    829  -4590       C  
ATOM    287  O   GLN A 106      44.854   9.648  60.840  1.00 97.18           O  
ANISOU  287  O   GLN A 106     7330  15359  14235   -222    910  -4467       O  
ATOM    288  CB  GLN A 106      45.574  10.294  63.460  1.00101.94           C  
ANISOU  288  CB  GLN A 106     7802  16073  14858   -412    778  -4995       C  
ATOM    289  CG  GLN A 106      45.534  10.820  64.888  1.00102.64           C  
ANISOU  289  CG  GLN A 106     7816  16245  14936   -505    719  -5331       C  
ATOM    290  CD  GLN A 106      44.275  11.605  65.191  1.00103.89           C  
ANISOU  290  CD  GLN A 106     7978  16321  15176   -529    762  -5498       C  
ATOM    291  OE1 GLN A 106      43.553  12.018  64.283  1.00102.66           O  
ANISOU  291  OE1 GLN A 106     7850  15992  15163   -484    845  -5350       O  
ATOM    292  NE2 GLN A 106      44.008  11.823  66.475  1.00103.97           N  
ANISOU  292  NE2 GLN A 106     7945  16475  15086   -592    710  -5805       N  
ATOM    293  N   ASN A 107      44.466   7.501  61.371  1.00 70.71           N  
ANISOU  293  N   ASN A 107     4149  12298  10421   -200    799  -4480       N  
ATOM    294  CA  ASN A 107      44.440   7.068  59.983  1.00 69.56           C  
ANISOU  294  CA  ASN A 107     4049  12122  10259   -100    853  -4253       C  
ATOM    295  C   ASN A 107      43.027   7.194  59.414  1.00 68.92           C  
ANISOU  295  C   ASN A 107     4038  12014  10136    -58    894  -4214       C  
ATOM    296  O   ASN A 107      42.076   7.556  60.112  1.00 84.12           O  
ANISOU  296  O   ASN A 107     5982  13931  12050   -109    882  -4352       O  
ATOM    297  CB  ASN A 107      44.974   5.641  59.851  1.00 78.46           C  
ANISOU  297  CB  ASN A 107     5235  13377  11200    -59    805  -4181       C  
ATOM    298  CG  ASN A 107      44.260   4.659  60.759  1.00 89.47           C  
ANISOU  298  CG  ASN A 107     6701  14899  12395    -92    739  -4286       C  
ATOM    299  OD1 ASN A 107      43.067   4.391  60.599  1.00100.83           O  
ANISOU  299  OD1 ASN A 107     8213  16347  13750    -77    745  -4299       O  
ATOM    300  ND2 ASN A 107      44.996   4.103  61.715  1.00 86.24           N  
ANISOU  300  ND2 ASN A 107     6253  14601  11912   -131    677  -4338       N  
ATOM    301  N   ALA A 108      42.886   6.892  58.121  1.00 68.47           N  
ANISOU  301  N   ALA A 108     4010  11962  10043     40    942  -4027       N  
ATOM    302  CA  ALA A 108      41.593   7.043  57.457  1.00 68.96           C  
ANISOU  302  CA  ALA A 108     4119  12021  10061     91    980  -3970       C  
ATOM    303  C   ALA A 108      40.575   6.032  57.974  1.00 75.83           C  
ANISOU  303  C   ALA A 108     5099  12987  10726     65    913  -4086       C  
ATOM    304  O   ALA A 108      39.392   6.362  58.139  1.00 80.29           O  
ANISOU  304  O   ALA A 108     5693  13534  11280     50    921  -4136       O  
ATOM    305  CB  ALA A 108      41.761   6.901  55.945  1.00 68.18           C  
ANISOU  305  CB  ALA A 108     4006  11962   9937    213   1041  -3751       C  
ATOM    306  N   THR A 109      41.014   4.796  58.229  1.00 72.91           N  
ANISOU  306  N   THR A 109     4777  12710  10217     62    854  -4114       N  
ATOM    307  CA  THR A 109      40.098   3.764  58.701  1.00 65.72           C  
ANISOU  307  CA  THR A 109     3944  11875   9151     42    802  -4196       C  
ATOM    308  C   THR A 109      39.446   4.158  60.018  1.00 65.89           C  
ANISOU  308  C   THR A 109     3962  11910   9164    -45    775  -4341       C  
ATOM    309  O   THR A 109      38.234   3.990  60.192  1.00 65.53           O  
ANISOU  309  O   THR A 109     3963  11882   9052    -55    769  -4385       O  
ATOM    310  CB  THR A 109      40.835   2.433  58.853  1.00 65.45           C  
ANISOU  310  CB  THR A 109     3924  11913   9032     54    759  -4183       C  
ATOM    311  OG1 THR A 109      41.348   2.016  57.581  1.00 71.48           O  
ANISOU  311  OG1 THR A 109     4691  12678   9790    142    786  -4076       O  
ATOM    312  CG2 THR A 109      39.901   1.367  59.392  1.00 64.98           C  
ANISOU  312  CG2 THR A 109     3914  11912   8866     34    720  -4245       C  
ATOM    313  N   ASN A 110      40.222   4.710  60.951  1.00 66.64           N  
ANISOU  313  N   ASN A 110     3990  12011   9319   -106    759  -4429       N  
ATOM    314  CA  ASN A 110      39.635   5.132  62.219  1.00 69.09           C  
ANISOU  314  CA  ASN A 110     4281  12372   9599   -181    734  -4597       C  
ATOM    315  C   ASN A 110      38.727   6.342  62.050  1.00 68.82           C  
ANISOU  315  C   ASN A 110     4234  12224   9691   -192    786  -4653       C  
ATOM    316  O   ASN A 110      37.763   6.496  62.807  1.00 68.95           O  
ANISOU  316  O   ASN A 110     4265  12283   9651   -231    776  -4771       O  
ATOM    317  CB  ASN A 110      40.728   5.414  63.244  1.00 80.71           C  
ANISOU  317  CB  ASN A 110     5666  13913  11086   -239    695  -4708       C  
ATOM    318  CG  ASN A 110      41.378   4.146  63.752  1.00 88.12           C  
ANISOU  318  CG  ASN A 110     6604  15007  11872   -232    639  -4655       C  
ATOM    319  OD1 ASN A 110      40.765   3.376  64.494  1.00 91.57           O  
ANISOU  319  OD1 ASN A 110     7059  15576  12159   -242    610  -4672       O  
ATOM    320  ND2 ASN A 110      42.622   3.917  63.355  1.00 91.82           N  
ANISOU  320  ND2 ASN A 110     7035  15458  12394   -209    633  -4567       N  
ATOM    321  N   TYR A 111      39.004   7.206  61.073  1.00 74.99           N  
ANISOU  321  N   TYR A 111     4975  12866  10653   -151    850  -4551       N  
ATOM    322  CA  TYR A 111      38.080   8.301  60.793  1.00 83.74           C  
ANISOU  322  CA  TYR A 111     6056  13853  11908   -145    915  -4555       C  
ATOM    323  C   TYR A 111      36.743   7.763  60.302  1.00 76.73           C  
ANISOU  323  C   TYR A 111     5254  13011  10888   -101    917  -4488       C  
ATOM    324  O   TYR A 111      35.678   8.228  60.730  1.00 71.73           O  
ANISOU  324  O   TYR A 111     4628  12353  10274   -126    932  -4571       O  
ATOM    325  CB  TYR A 111      38.690   9.257  59.768  1.00 95.72           C  
ANISOU  325  CB  TYR A 111     7485  15227  13658    -91    998  -4396       C  
ATOM    326  CG  TYR A 111      39.860  10.048  60.308  1.00104.84           C  
ANISOU  326  CG  TYR A 111     8528  16291  15017   -149   1006  -4486       C  
ATOM    327  CD1 TYR A 111      39.899  10.449  61.638  1.00107.10           C  
ANISOU  327  CD1 TYR A 111     8774  16585  15335   -245    964  -4750       C  
ATOM    328  CD2 TYR A 111      40.935  10.379  59.493  1.00111.62           C  
ANISOU  328  CD2 TYR A 111     9307  17074  16029   -104   1055  -4318       C  
ATOM    329  CE1 TYR A 111      40.971  11.166  62.138  1.00116.79           C  
ANISOU  329  CE1 TYR A 111     9886  17737  16754   -303    961  -4869       C  
ATOM    330  CE2 TYR A 111      42.013  11.092  59.984  1.00114.73           C  
ANISOU  330  CE2 TYR A 111     9588  17373  16633   -163   1058  -4405       C  
ATOM    331  CZ  TYR A 111      42.027  11.485  61.305  1.00120.22           C  
ANISOU  331  CZ  TYR A 111    10245  18066  17367   -266   1007  -4693       C  
ATOM    332  OH  TYR A 111      43.102  12.197  61.792  1.00122.69           O  
ANISOU  332  OH  TYR A 111    10433  18289  17895   -328   1002  -4813       O  
ATOM    333  N   PHE A 112      36.781   6.764  59.417  1.00 77.43           N  
ANISOU  333  N   PHE A 112     5402  13169  10847    -36    900  -4357       N  
ATOM    334  CA  PHE A 112      35.546   6.121  58.982  1.00 75.76           C  
ANISOU  334  CA  PHE A 112     5263  13015  10507     -2    888  -4326       C  
ATOM    335  C   PHE A 112      34.842   5.431  60.147  1.00 70.72           C  
ANISOU  335  C   PHE A 112     4672  12453   9746    -69    832  -4465       C  
ATOM    336  O   PHE A 112      33.610   5.446  60.235  1.00 67.40           O  
ANISOU  336  O   PHE A 112     4281  12040   9288    -74    836  -4491       O  
ATOM    337  CB  PHE A 112      35.841   5.112  57.875  1.00 65.34           C  
ANISOU  337  CB  PHE A 112     3979  11766   9081     74    872  -4213       C  
ATOM    338  CG  PHE A 112      35.867   5.700  56.492  1.00 65.81           C  
ANISOU  338  CG  PHE A 112     3995  11816   9193    171    935  -4046       C  
ATOM    339  CD1 PHE A 112      37.053   6.142  55.932  1.00 66.40           C  
ANISOU  339  CD1 PHE A 112     4004  11863   9363    215    980  -3929       C  
ATOM    340  CD2 PHE A 112      34.705   5.786  55.742  1.00 65.84           C  
ANISOU  340  CD2 PHE A 112     4009  11862   9145    226    953  -3987       C  
ATOM    341  CE1 PHE A 112      37.076   6.671  54.651  1.00 72.37           C  
ANISOU  341  CE1 PHE A 112     4697  12646  10156    321   1051  -3739       C  
ATOM    342  CE2 PHE A 112      34.721   6.314  54.461  1.00 66.56           C  
ANISOU  342  CE2 PHE A 112     4038  11994   9259    332   1016  -3807       C  
ATOM    343  CZ  PHE A 112      35.905   6.757  53.916  1.00 67.23           C  
ANISOU  343  CZ  PHE A 112     4050  12063   9433    383   1070  -3673       C  
ATOM    344  N   LEU A 113      35.607   4.830  61.061  1.00 65.52           N  
ANISOU  344  N   LEU A 113     4004  11867   9022   -115    787  -4536       N  
ATOM    345  CA  LEU A 113      34.992   4.180  62.214  1.00 65.47           C  
ANISOU  345  CA  LEU A 113     4014  11968   8894   -165    748  -4629       C  
ATOM    346  C   LEU A 113      34.338   5.196  63.141  1.00 82.31           C  
ANISOU  346  C   LEU A 113     6113  14100  11061   -219    764  -4770       C  
ATOM    347  O   LEU A 113      33.287   4.918  63.729  1.00 81.43           O  
ANISOU  347  O   LEU A 113     6022  14054  10863   -239    757  -4816       O  
ATOM    348  CB  LEU A 113      36.028   3.354  62.975  1.00 65.68           C  
ANISOU  348  CB  LEU A 113     4009  12104   8842   -186    704  -4637       C  
ATOM    349  CG  LEU A 113      36.625   2.151  62.242  1.00 76.14           C  
ANISOU  349  CG  LEU A 113     5356  13432  10140   -134    690  -4517       C  
ATOM    350  CD1 LEU A 113      37.489   1.308  63.175  1.00 70.11           C  
ANISOU  350  CD1 LEU A 113     4543  12787   9311   -153    655  -4503       C  
ATOM    351  CD2 LEU A 113      35.541   1.308  61.588  1.00 64.71           C  
ANISOU  351  CD2 LEU A 113     3963  11967   8658   -100    693  -4474       C  
ATOM    352  N   MET A 114      34.932   6.383  63.279  1.00 73.98           N  
ANISOU  352  N   MET A 114     4994  12964  10152   -242    791  -4847       N  
ATOM    353  CA  MET A 114      34.298   7.424  64.085  1.00 76.58           C  
ANISOU  353  CA  MET A 114     5275  13269  10552   -291    814  -5016       C  
ATOM    354  C   MET A 114      33.055   7.971  63.397  1.00 70.89           C  
ANISOU  354  C   MET A 114     4582  12435   9918   -257    869  -4954       C  
ATOM    355  O   MET A 114      32.076   8.321  64.063  1.00 76.29           O  
ANISOU  355  O   MET A 114     5261  13140  10587   -286    879  -5063       O  
ATOM    356  CB  MET A 114      35.283   8.549  64.392  1.00 86.45           C  
ANISOU  356  CB  MET A 114     6426  14434  11986   -329    833  -5142       C  
ATOM    357  CG  MET A 114      34.662   9.695  65.177  1.00 88.02           C  
ANISOU  357  CG  MET A 114     6557  14583  12304   -379    864  -5358       C  
ATOM    358  SD  MET A 114      35.850  10.959  65.656  1.00104.89           S  
ANISOU  358  SD  MET A 114     8549  16610  14694   -436    881  -5568       S  
ATOM    359  CE  MET A 114      36.402  11.548  64.058  1.00106.83           C  
ANISOU  359  CE  MET A 114     8770  16599  15220   -371    963  -5305       C  
ATOM    360  N   SER A 115      33.077   8.063  62.066  1.00 71.03           N  
ANISOU  360  N   SER A 115     4615  12355  10016   -188    907  -4773       N  
ATOM    361  CA  SER A 115      31.852   8.396  61.344  1.00 72.13           C  
ANISOU  361  CA  SER A 115     4773  12436  10195   -141    953  -4680       C  
ATOM    362  C   SER A 115      30.772   7.353  61.605  1.00 70.46           C  
ANISOU  362  C   SER A 115     4639  12340   9794   -147    908  -4691       C  
ATOM    363  O   SER A 115      29.601   7.692  61.825  1.00 67.97           O  
ANISOU  363  O   SER A 115     4328  12011   9489   -153    930  -4723       O  
ATOM    364  CB  SER A 115      32.139   8.512  59.847  1.00 71.87           C  
ANISOU  364  CB  SER A 115     4727  12353  10226    -50    995  -4467       C  
ATOM    365  OG  SER A 115      30.963   8.816  59.117  1.00 67.05           O  
ANISOU  365  OG  SER A 115     4117  11726   9633      8   1037  -4363       O  
ATOM    366  N   LEU A 116      31.155   6.074  61.589  1.00 69.80           N  
ANISOU  366  N   LEU A 116     4602  12357   9563   -145    851  -4659       N  
ATOM    367  CA  LEU A 116      30.229   4.998  61.925  1.00 68.35           C  
ANISOU  367  CA  LEU A 116     4464  12265   9240   -156    815  -4666       C  
ATOM    368  C   LEU A 116      29.690   5.159  63.341  1.00 67.37           C  
ANISOU  368  C   LEU A 116     4319  12216   9062   -218    811  -4795       C  
ATOM    369  O   LEU A 116      28.502   4.931  63.596  1.00 65.57           O  
ANISOU  369  O   LEU A 116     4108  12020   8787   -224    816  -4801       O  
ATOM    370  CB  LEU A 116      30.934   3.650  61.769  1.00 69.15           C  
ANISOU  370  CB  LEU A 116     4587  12434   9252   -144    771  -4616       C  
ATOM    371  CG  LEU A 116      30.146   2.356  61.981  1.00 67.80           C  
ANISOU  371  CG  LEU A 116     4437  12329   8994   -149    745  -4602       C  
ATOM    372  CD1 LEU A 116      29.257   2.087  60.794  1.00 63.92           C  
ANISOU  372  CD1 LEU A 116     3973  11800   8514   -103    746  -4554       C  
ATOM    373  CD2 LEU A 116      31.085   1.178  62.213  1.00 73.18           C  
ANISOU  373  CD2 LEU A 116     5103  13062   9639   -148    717  -4567       C  
ATOM    374  N   ALA A 117      30.553   5.561  64.274  1.00 70.79           N  
ANISOU  374  N   ALA A 117     4703  12700   9495   -261    800  -4905       N  
ATOM    375  CA  ALA A 117      30.128   5.755  65.656  1.00 79.94           C  
ANISOU  375  CA  ALA A 117     5820  13984  10568   -312    793  -5049       C  
ATOM    376  C   ALA A 117      29.158   6.923  65.779  1.00 82.48           C  
ANISOU  376  C   ALA A 117     6122  14220  10997   -324    840  -5146       C  
ATOM    377  O   ALA A 117      28.201   6.863  66.556  1.00 73.24           O  
ANISOU  377  O   ALA A 117     4943  13141   9743   -344    844  -5210       O  
ATOM    378  CB  ALA A 117      31.345   5.975  66.551  1.00 85.70           C  
ANISOU  378  CB  ALA A 117     6480  14818  11262   -350    763  -5171       C  
ATOM    379  N   ILE A 118      29.396   7.997  65.025  1.00 81.72           N  
ANISOU  379  N   ILE A 118     6003  13947  11100   -306    886  -5141       N  
ATOM    380  CA  ILE A 118      28.465   9.123  65.020  1.00 79.26           C  
ANISOU  380  CA  ILE A 118     5658  13521  10938   -306    946  -5204       C  
ATOM    381  C   ILE A 118      27.122   8.697  64.447  1.00 76.71           C  
ANISOU  381  C   ILE A 118     5392  13193  10563   -265    961  -5073       C  
ATOM    382  O   ILE A 118      26.063   9.080  64.958  1.00 78.52           O  
ANISOU  382  O   ILE A 118     5608  13428  10800   -277    987  -5142       O  
ATOM    383  CB  ILE A 118      29.061  10.310  64.243  1.00 81.45           C  
ANISOU  383  CB  ILE A 118     5873  13595  11481   -281   1010  -5174       C  
ATOM    384  CG1 ILE A 118      30.231  10.917  65.016  1.00 94.49           C  
ANISOU  384  CG1 ILE A 118     7441  15235  13226   -339   1000  -5367       C  
ATOM    385  CG2 ILE A 118      28.002  11.363  63.987  1.00 76.23           C  
ANISOU  385  CG2 ILE A 118     5170  12789  11004   -257   1090  -5169       C  
ATOM    386  CD1 ILE A 118      30.832  12.133  64.349  1.00103.03           C  
ANISOU  386  CD1 ILE A 118     8433  16090  14623   -321   1075  -5339       C  
ATOM    387  N   ALA A 119      27.142   7.901  63.374  1.00 80.05           N  
ANISOU  387  N   ALA A 119     5868  13615  10933   -214    943  -4898       N  
ATOM    388  CA  ALA A 119      25.894   7.393  62.812  1.00 75.83           C  
ANISOU  388  CA  ALA A 119     5373  13098  10339   -179    944  -4799       C  
ATOM    389  C   ALA A 119      25.145   6.541  63.828  1.00 78.80           C  
ANISOU  389  C   ALA A 119     5770  13604  10568   -221    912  -4861       C  
ATOM    390  O   ALA A 119      23.924   6.665  63.974  1.00 86.01           O  
ANISOU  390  O   ALA A 119     6682  14520  11478   -218    935  -4861       O  
ATOM    391  CB  ALA A 119      26.170   6.592  61.541  1.00 72.30           C  
ANISOU  391  CB  ALA A 119     4961  12662   9846   -122    917  -4652       C  
ATOM    392  N   ASP A 120      25.865   5.679  64.549  1.00 72.92           N  
ANISOU  392  N   ASP A 120     5027  12973   9707   -252    869  -4894       N  
ATOM    393  CA  ASP A 120      25.234   4.849  65.570  1.00 66.54           C  
ANISOU  393  CA  ASP A 120     4209  12309   8764   -280    856  -4912       C  
ATOM    394  C   ASP A 120      24.689   5.692  66.717  1.00 67.67           C  
ANISOU  394  C   ASP A 120     4304  12520   8887   -314    883  -5052       C  
ATOM    395  O   ASP A 120      23.627   5.387  67.271  1.00 67.97           O  
ANISOU  395  O   ASP A 120     4333  12637   8855   -318    899  -5044       O  
ATOM    396  CB  ASP A 120      26.228   3.814  66.088  1.00 66.51           C  
ANISOU  396  CB  ASP A 120     4189  12424   8656   -291    819  -4883       C  
ATOM    397  CG  ASP A 120      26.232   2.550  65.259  1.00 74.69           C  
ANISOU  397  CG  ASP A 120     5255  13428   9696   -262    799  -4753       C  
ATOM    398  OD1 ASP A 120      25.140   2.136  64.821  1.00 65.43           O  
ANISOU  398  OD1 ASP A 120     4096  12220   8543   -249    809  -4705       O  
ATOM    399  OD2 ASP A 120      27.323   1.977  65.041  1.00 88.50           O  
ANISOU  399  OD2 ASP A 120     7001  15183  11441   -252    775  -4713       O  
ATOM    400  N   MET A 121      25.404   6.749  67.097  1.00 71.22           N  
ANISOU  400  N   MET A 121     4711  12942   9407   -338    892  -5195       N  
ATOM    401  CA  MET A 121      24.918   7.614  68.165  1.00 83.18           C  
ANISOU  401  CA  MET A 121     6164  14523  10919   -371    915  -5376       C  
ATOM    402  C   MET A 121      23.662   8.356  67.734  1.00 88.24           C  
ANISOU  402  C   MET A 121     6813  15026  11689   -350    972  -5363       C  
ATOM    403  O   MET A 121      22.720   8.502  68.520  1.00108.63           O  
ANISOU  403  O   MET A 121     9368  17694  14213   -362    993  -5434       O  
ATOM    404  CB  MET A 121      26.007   8.599  68.584  1.00 87.69           C  
ANISOU  404  CB  MET A 121     6665  15072  11583   -407    910  -5568       C  
ATOM    405  CG  MET A 121      25.643   9.436  69.795  1.00 84.63           C  
ANISOU  405  CG  MET A 121     6188  14787  11180   -448    921  -5815       C  
ATOM    406  SD  MET A 121      26.928  10.620  70.237  1.00 85.17           S  
ANISOU  406  SD  MET A 121     6146  14810  11405   -500    913  -6095       S  
ATOM    407  CE  MET A 121      26.972  11.631  68.757  1.00 82.96           C  
ANISOU  407  CE  MET A 121     5886  14148  11488   -467    993  -5989       C  
ATOM    408  N   LEU A 122      23.626   8.830  66.488  1.00 74.07           N  
ANISOU  408  N   LEU A 122     5043  13038  10063   -310   1004  -5256       N  
ATOM    409  CA  LEU A 122      22.411   9.458  65.978  1.00 79.87           C  
ANISOU  409  CA  LEU A 122     5774  13658  10915   -275   1062  -5201       C  
ATOM    410  C   LEU A 122      21.266   8.457  65.895  1.00 78.09           C  
ANISOU  410  C   LEU A 122     5593  13523  10554   -259   1046  -5089       C  
ATOM    411  O   LEU A 122      20.105   8.809  66.131  1.00 77.85           O  
ANISOU  411  O   LEU A 122     5545  13483  10550   -250   1086  -5101       O  
ATOM    412  CB  LEU A 122      22.675  10.090  64.613  1.00 74.57           C  
ANISOU  412  CB  LEU A 122     5096  12809  10429   -217   1104  -5064       C  
ATOM    413  CG  LEU A 122      23.606  11.300  64.630  1.00 76.61           C  
ANISOU  413  CG  LEU A 122     5281  12924  10905   -226   1151  -5157       C  
ATOM    414  CD1 LEU A 122      23.830  11.812  63.221  1.00 74.50           C  
ANISOU  414  CD1 LEU A 122     4987  12509  10808   -150   1204  -4954       C  
ATOM    415  CD2 LEU A 122      23.045  12.394  65.522  1.00 72.04           C  
ANISOU  415  CD2 LEU A 122     4626  12278  10467   -258   1207  -5351       C  
ATOM    416  N   LEU A 123      21.573   7.203  65.564  1.00 74.81           N  
ANISOU  416  N   LEU A 123     5222  13185  10018   -255    994  -4986       N  
ATOM    417  CA  LEU A 123      20.544   6.169  65.541  1.00 68.57           C  
ANISOU  417  CA  LEU A 123     4451  12468   9135   -248    981  -4898       C  
ATOM    418  C   LEU A 123      19.994   5.909  66.940  1.00 68.24           C  
ANISOU  418  C   LEU A 123     4373  12577   8979   -281    995  -4968       C  
ATOM    419  O   LEU A 123      18.782   5.733  67.118  1.00 68.47           O  
ANISOU  419  O   LEU A 123     4390  12631   8993   -274   1022  -4932       O  
ATOM    420  CB  LEU A 123      21.121   4.888  64.936  1.00 66.50           C  
ANISOU  420  CB  LEU A 123     4220  12235   8812   -239    930  -4803       C  
ATOM    421  CG  LEU A 123      20.164   3.774  64.528  1.00 69.00           C  
ANISOU  421  CG  LEU A 123     4539  12576   9102   -229    916  -4717       C  
ATOM    422  CD1 LEU A 123      19.215   4.269  63.447  1.00 74.77           C  
ANISOU  422  CD1 LEU A 123     5273  13227   9909   -188    929  -4671       C  
ATOM    423  CD2 LEU A 123      20.942   2.555  64.058  1.00 65.61           C  
ANISOU  423  CD2 LEU A 123     4120  12159   8649   -226    872  -4667       C  
ATOM    424  N   GLY A 124      20.871   5.885  67.945  1.00 68.89           N  
ANISOU  424  N   GLY A 124     4424  12784   8967   -312    977  -5063       N  
ATOM    425  CA  GLY A 124      20.445   5.678  69.318  1.00 79.29           C  
ANISOU  425  CA  GLY A 124     5685  14302  10139   -330    992  -5122       C  
ATOM    426  C   GLY A 124      19.778   6.881  69.955  1.00 81.34           C  
ANISOU  426  C   GLY A 124     5902  14565  10439   -340   1033  -5280       C  
ATOM    427  O   GLY A 124      19.077   6.729  70.961  1.00 72.33           O  
ANISOU  427  O   GLY A 124     4713  13593   9175   -342   1056  -5310       O  
ATOM    428  N   PHE A 125      20.008   8.076  69.413  1.00 75.09           N  
ANISOU  428  N   PHE A 125     5111  13592   9828   -342   1052  -5376       N  
ATOM    429  CA  PHE A 125      19.386   9.284  69.941  1.00 82.62           C  
ANISOU  429  CA  PHE A 125     6009  14504  10879   -350   1103  -5541       C  
ATOM    430  C   PHE A 125      18.064   9.622  69.258  1.00 89.01           C  
ANISOU  430  C   PHE A 125     6837  15170  11811   -311   1160  -5440       C  
ATOM    431  O   PHE A 125      17.131  10.089  69.919  1.00 86.66           O  
ANISOU  431  O   PHE A 125     6498  14912  11515   -309   1205  -5520       O  
ATOM    432  CB  PHE A 125      20.347  10.469  69.812  1.00 85.03           C  
ANISOU  432  CB  PHE A 125     6269  14670  11369   -372   1112  -5709       C  
ATOM    433  CG  PHE A 125      21.179  10.712  71.041  1.00101.09           C  
ANISOU  433  CG  PHE A 125     8221  16887  13300   -422   1074  -5945       C  
ATOM    434  CD1 PHE A 125      20.634  11.338  72.151  1.00110.63           C  
ANISOU  434  CD1 PHE A 125     9344  18219  14472   -445   1092  -6155       C  
ATOM    435  CD2 PHE A 125      22.509  10.323  71.084  1.00105.05           C  
ANISOU  435  CD2 PHE A 125     8718  17460  13736   -444   1016  -5965       C  
ATOM    436  CE1 PHE A 125      21.398  11.567  73.283  1.00116.90           C  
ANISOU  436  CE1 PHE A 125    10037  19228  15150   -489   1044  -6395       C  
ATOM    437  CE2 PHE A 125      23.280  10.550  72.212  1.00106.89           C  
ANISOU  437  CE2 PHE A 125     8856  17897  13859   -487    972  -6191       C  
ATOM    438  CZ  PHE A 125      22.724  11.173  73.312  1.00113.93           C  
ANISOU  438  CZ  PHE A 125     9651  18936  14701   -511    981  -6413       C  
ATOM    439  N   LEU A 126      17.959   9.404  67.946  1.00 92.31           N  
ANISOU  439  N   LEU A 126     7306  15445  12322   -273   1160  -5267       N  
ATOM    440  CA  LEU A 126      16.826   9.898  67.177  1.00 91.78           C  
ANISOU  440  CA  LEU A 126     7235  15248  12388   -227   1214  -5170       C  
ATOM    441  C   LEU A 126      15.845   8.821  66.748  1.00 93.35           C  
ANISOU  441  C   LEU A 126     7467  15513  12488   -206   1195  -5010       C  
ATOM    442  O   LEU A 126      14.681   9.143  66.491  1.00109.67           O  
ANISOU  442  O   LEU A 126     9513  17536  14621   -175   1239  -4957       O  
ATOM    443  CB  LEU A 126      17.314  10.641  65.924  1.00 86.52           C  
ANISOU  443  CB  LEU A 126     6563  14394  11915   -183   1240  -5083       C  
ATOM    444  CG  LEU A 126      18.326  11.764  66.153  1.00 82.76           C  
ANISOU  444  CG  LEU A 126     6034  13801  11609   -201   1274  -5224       C  
ATOM    445  CD1 LEU A 126      18.616  12.489  64.849  1.00 85.11           C  
ANISOU  445  CD1 LEU A 126     6303  13917  12119   -137   1324  -5073       C  
ATOM    446  CD2 LEU A 126      17.830  12.735  67.213  1.00 79.69           C  
ANISOU  446  CD2 LEU A 126     5574  13391  11315   -228   1329  -5431       C  
ATOM    447  N   VAL A 127      16.268   7.567  66.662  1.00 84.87           N  
ANISOU  447  N   VAL A 127     6429  14534  11284   -222   1135  -4940       N  
ATOM    448  CA  VAL A 127      15.434   6.493  66.142  1.00 81.33           C  
ANISOU  448  CA  VAL A 127     5992  14120  10789   -209   1115  -4811       C  
ATOM    449  C   VAL A 127      15.019   5.525  67.242  1.00 78.92           C  
ANISOU  449  C   VAL A 127     5661  13972  10354   -238   1118  -4803       C  
ATOM    450  O   VAL A 127      13.835   5.226  67.403  1.00 81.00           O  
ANISOU  450  O   VAL A 127     5894  14266  10616   -231   1148  -4749       O  
ATOM    451  CB  VAL A 127      16.147   5.750  64.989  1.00 70.99           C  
ANISOU  451  CB  VAL A 127     4718  12771   9482   -195   1056  -4728       C  
ATOM    452  CG1 VAL A 127      15.312   4.575  64.527  1.00 67.44           C  
ANISOU  452  CG1 VAL A 127     4259  12360   9007   -193   1030  -4645       C  
ATOM    453  CG2 VAL A 127      16.410   6.703  63.834  1.00 67.62           C  
ANISOU  453  CG2 VAL A 127     4295  12225   9173   -146   1068  -4688       C  
ATOM    454  N   MET A 128      15.984   5.027  68.011  1.00 77.69           N  
ANISOU  454  N   MET A 128     5498  13927  10091   -264   1095  -4836       N  
ATOM    455  CA  MET A 128      15.683   3.995  69.000  1.00 83.92           C  
ANISOU  455  CA  MET A 128     6238  14888  10759   -276   1111  -4772       C  
ATOM    456  C   MET A 128      14.744   4.456  70.113  1.00 85.23           C  
ANISOU  456  C   MET A 128     6349  15179  10853   -271   1169  -4818       C  
ATOM    457  O   MET A 128      13.839   3.681  70.472  1.00102.56           O  
ANISOU  457  O   MET A 128     8497  17454  13017   -264   1205  -4706       O  
ATOM    458  CB  MET A 128      16.995   3.442  69.567  1.00 92.98           C  
ANISOU  458  CB  MET A 128     7372  16153  11802   -291   1079  -4777       C  
ATOM    459  CG  MET A 128      17.860   2.772  68.508  1.00 90.39           C  
ANISOU  459  CG  MET A 128     7088  15712  11544   -290   1028  -4714       C  
ATOM    460  SD  MET A 128      19.484   2.238  69.077  1.00 83.16           S  
ANISOU  460  SD  MET A 128     6153  14913  10530   -302    993  -4714       S  
ATOM    461  CE  MET A 128      19.043   1.141  70.420  1.00 77.56           C  
ANISOU  461  CE  MET A 128     5336  14441   9693   -296   1039  -4581       C  
ATOM    462  N   PRO A 129      14.887   5.650  70.702  1.00 78.71           N  
ANISOU  462  N   PRO A 129     5512  14378  10016   -275   1187  -4981       N  
ATOM    463  CA  PRO A 129      13.896   6.055  71.717  1.00 85.41           C  
ANISOU  463  CA  PRO A 129     6302  15355  10795   -264   1245  -5036       C  
ATOM    464  C   PRO A 129      12.500   6.255  71.148  1.00 88.46           C  
ANISOU  464  C   PRO A 129     6692  15619  11300   -240   1291  -4962       C  
ATOM    465  O   PRO A 129      11.513   5.932  71.819  1.00 74.41           O  
ANISOU  465  O   PRO A 129     4862  13958   9454   -225   1341  -4906       O  
ATOM    466  CB  PRO A 129      14.482   7.359  72.277  1.00 79.86           C  
ANISOU  466  CB  PRO A 129     5576  14661  10104   -279   1244  -5269       C  
ATOM    467  CG  PRO A 129      15.366   7.867  71.203  1.00 73.73           C  
ANISOU  467  CG  PRO A 129     4854  13671   9490   -290   1209  -5299       C  
ATOM    468  CD  PRO A 129      15.958   6.652  70.565  1.00 72.31           C  
ANISOU  468  CD  PRO A 129     4720  13491   9266   -291   1160  -5136       C  
ATOM    469  N   VAL A 130      12.388   6.771  69.921  1.00 88.13           N  
ANISOU  469  N   VAL A 130     6696  15364  11426   -229   1280  -4945       N  
ATOM    470  CA  VAL A 130      11.082   6.880  69.276  1.00 79.78           C  
ANISOU  470  CA  VAL A 130     5628  14213  10472   -200   1315  -4855       C  
ATOM    471  C   VAL A 130      10.496   5.495  69.031  1.00 77.41           C  
ANISOU  471  C   VAL A 130     5311  13966  10135   -205   1299  -4699       C  
ATOM    472  O   VAL A 130       9.280   5.293  69.128  1.00 82.14           O  
ANISOU  472  O   VAL A 130     5866  14584  10759   -192   1339  -4630       O  
ATOM    473  CB  VAL A 130      11.193   7.696  67.973  1.00 80.37           C  
ANISOU  473  CB  VAL A 130     5733  14089  10715   -172   1307  -4841       C  
ATOM    474  CG1 VAL A 130       9.844   7.798  67.282  1.00 76.78           C  
ANISOU  474  CG1 VAL A 130     5250  13573  10351   -134   1338  -4737       C  
ATOM    475  CG2 VAL A 130      11.746   9.084  68.260  1.00 76.84           C  
ANISOU  475  CG2 VAL A 130     5272  13556  10366   -169   1343  -4989       C  
ATOM    476  N   SER A 131      11.348   4.515  68.721  1.00 71.17           N  
ANISOU  476  N   SER A 131     4541  13191   9310   -226   1245  -4646       N  
ATOM    477  CA  SER A 131      10.865   3.145  68.576  1.00 71.05           C  
ANISOU  477  CA  SER A 131     4482  13208   9306   -237   1238  -4514       C  
ATOM    478  C   SER A 131      10.359   2.598  69.906  1.00 72.32           C  
ANISOU  478  C   SER A 131     4562  13544   9372   -240   1301  -4446       C  
ATOM    479  O   SER A 131       9.332   1.910  69.952  1.00 72.78           O  
ANISOU  479  O   SER A 131     4553  13614   9486   -240   1335  -4334       O  
ATOM    480  CB  SER A 131      11.968   2.253  68.009  1.00 70.20           C  
ANISOU  480  CB  SER A 131     4400  13065   9209   -255   1176  -4486       C  
ATOM    481  OG  SER A 131      11.482   0.946  67.754  1.00 80.07           O  
ANISOU  481  OG  SER A 131     5589  14304  10532   -270   1171  -4378       O  
ATOM    482  N   MET A 132      11.062   2.900  71.001  1.00 73.96           N  
ANISOU  482  N   MET A 132     4758  13908   9434   -238   1318  -4506       N  
ATOM    483  CA  MET A 132      10.572   2.499  72.318  1.00 79.59           C  
ANISOU  483  CA  MET A 132     5378  14843  10018   -222   1386  -4429       C  
ATOM    484  C   MET A 132       9.232   3.158  72.631  1.00 90.85           C  
ANISOU  484  C   MET A 132     6776  16283  11462   -199   1449  -4450       C  
ATOM    485  O   MET A 132       8.325   2.517  73.178  1.00 93.24           O  
ANISOU  485  O   MET A 132     6991  16688  11747   -185   1512  -4311       O  
ATOM    486  CB  MET A 132      11.601   2.847  73.392  1.00 78.25           C  
ANISOU  486  CB  MET A 132     5194  14881   9658   -217   1379  -4524       C  
ATOM    487  CG  MET A 132      11.183   2.427  74.790  1.00 87.56           C  
ANISOU  487  CG  MET A 132     6261  16352  10656   -185   1448  -4430       C  
ATOM    488  SD  MET A 132      12.372   2.900  76.058  1.00101.65           S  
ANISOU  488  SD  MET A 132     8005  18442  12174   -173   1423  -4573       S  
ATOM    489  CE  MET A 132      12.135   4.676  76.101  1.00 96.75           C  
ANISOU  489  CE  MET A 132     7437  17737  11587   -183   1409  -4892       C  
ATOM    490  N   LEU A 133       9.096   4.443  72.293  1.00 87.88           N  
ANISOU  490  N   LEU A 133     6455  15796  11141   -193   1443  -4608       N  
ATOM    491  CA  LEU A 133       7.832   5.146  72.499  1.00 83.35           C  
ANISOU  491  CA  LEU A 133     5850  15207  10612   -166   1507  -4632       C  
ATOM    492  C   LEU A 133       6.711   4.506  71.691  1.00 84.83           C  
ANISOU  492  C   LEU A 133     6011  15287  10933   -163   1519  -4478       C  
ATOM    493  O   LEU A 133       5.586   4.356  72.182  1.00 76.67           O  
ANISOU  493  O   LEU A 133     4909  14326   9898   -143   1585  -4402       O  
ATOM    494  CB  LEU A 133       7.988   6.620  72.122  1.00 76.18           C  
ANISOU  494  CB  LEU A 133     4989  14153   9803   -158   1504  -4810       C  
ATOM    495  CG  LEU A 133       6.734   7.491  72.218  1.00 77.64           C  
ANISOU  495  CG  LEU A 133     5139  14286  10077   -123   1576  -4843       C  
ATOM    496  CD1 LEU A 133       6.322   7.649  73.669  1.00 79.05           C  
ANISOU  496  CD1 LEU A 133     5248  14687  10100   -105   1640  -4913       C  
ATOM    497  CD2 LEU A 133       6.947   8.849  71.562  1.00 77.04           C  
ANISOU  497  CD2 LEU A 133     5093  14008  10173   -111   1581  -4969       C  
ATOM    498  N   THR A 134       7.002   4.131  70.443  1.00 87.22           N  
ANISOU  498  N   THR A 134     6358  15432  11350   -180   1453  -4441       N  
ATOM    499  CA  THR A 134       6.029   3.408  69.632  1.00 91.22           C  
ANISOU  499  CA  THR A 134     6823  15859  11980   -186   1443  -4324       C  
ATOM    500  C   THR A 134       5.640   2.094  70.295  1.00 96.00           C  
ANISOU  500  C   THR A 134     7330  16569  12575   -204   1478  -4176       C  
ATOM    501  O   THR A 134       4.464   1.710  70.290  1.00109.27           O  
ANISOU  501  O   THR A 134     8932  18248  14340   -203   1517  -4080       O  
ATOM    502  CB  THR A 134       6.601   3.159  68.232  1.00 84.09           C  
ANISOU  502  CB  THR A 134     5972  14815  11163   -198   1355  -4338       C  
ATOM    503  OG1 THR A 134       6.838   4.413  67.579  1.00 85.96           O  
ANISOU  503  OG1 THR A 134     6269  14957  11434   -169   1341  -4423       O  
ATOM    504  CG2 THR A 134       5.643   2.342  67.392  1.00 85.12           C  
ANISOU  504  CG2 THR A 134     6041  14890  11413   -209   1328  -4256       C  
ATOM    505  N   ILE A 135       6.614   1.402  70.890  1.00 85.26           N  
ANISOU  505  N   ILE A 135     5957  15306  11133   -218   1473  -4136       N  
ATOM    506  CA  ILE A 135       6.316   0.172  71.620  1.00 81.50           C  
ANISOU  506  CA  ILE A 135     5357  14938  10672   -226   1527  -3952       C  
ATOM    507  C   ILE A 135       5.363   0.455  72.774  1.00 89.84           C  
ANISOU  507  C   ILE A 135     6332  16167  11634   -191   1627  -3883       C  
ATOM    508  O   ILE A 135       4.396  -0.285  72.999  1.00 91.31           O  
ANISOU  508  O   ILE A 135     6403  16373  11917   -192   1686  -3718       O  
ATOM    509  CB  ILE A 135       7.619  -0.489  72.109  1.00 82.41           C  
ANISOU  509  CB  ILE A 135     5461  15147  10703   -234   1512  -3904       C  
ATOM    510  CG1 ILE A 135       8.394  -1.082  70.930  1.00 89.47           C  
ANISOU  510  CG1 ILE A 135     6404  15859  11732   -268   1425  -3935       C  
ATOM    511  CG2 ILE A 135       7.323  -1.566  73.138  1.00 80.73           C  
ANISOU  511  CG2 ILE A 135     5092  15097  10486   -223   1596  -3672       C  
ATOM    512  CD1 ILE A 135       9.603  -1.897  71.337  1.00 82.21           C  
ANISOU  512  CD1 ILE A 135     5451  15009  10778   -275   1416  -3856       C  
ATOM    513  N   LEU A 136       5.605   1.545  73.508  1.00 90.22           N  
ANISOU  513  N   LEU A 136     6428  16340  11510   -159   1649  -4018       N  
ATOM    514  CA  LEU A 136       4.776   1.865  74.668  1.00 97.94           C  
ANISOU  514  CA  LEU A 136     7328  17516  12368   -116   1744  -3981       C  
ATOM    515  C   LEU A 136       3.329   2.144  74.279  1.00102.38           C  
ANISOU  515  C   LEU A 136     7859  17973  13066   -105   1788  -3947       C  
ATOM    516  O   LEU A 136       2.411   1.865  75.059  1.00 95.11           O  
ANISOU  516  O   LEU A 136     6835  17190  12114    -76   1877  -3819       O  
ATOM    517  CB  LEU A 136       5.360   3.065  75.413  1.00 95.82           C  
ANISOU  517  CB  LEU A 136     7114  17378  11914    -91   1741  -4195       C  
ATOM    518  CG  LEU A 136       6.642   2.802  76.202  1.00 90.00           C  
ANISOU  518  CG  LEU A 136     6365  16849  10983    -89   1714  -4219       C  
ATOM    519  CD1 LEU A 136       7.099   4.070  76.899  1.00 87.98           C  
ANISOU  519  CD1 LEU A 136     6141  16713  10575    -73   1700  -4478       C  
ATOM    520  CD2 LEU A 136       6.427   1.679  77.203  1.00 89.57           C  
ANISOU  520  CD2 LEU A 136     6171  17051  10810    -57   1788  -3971       C  
ATOM    521  N   TYR A 137       3.103   2.699  73.086  1.00100.34           N  
ANISOU  521  N   TYR A 137     7678  17494  12953   -122   1730  -4041       N  
ATOM    522  CA  TYR A 137       1.765   3.030  72.613  1.00 86.00           C  
ANISOU  522  CA  TYR A 137     5827  15582  11266   -107   1761  -4010       C  
ATOM    523  C   TYR A 137       1.147   1.925  71.767  1.00 78.67           C  
ANISOU  523  C   TYR A 137     4829  14542  10518   -144   1730  -3868       C  
ATOM    524  O   TYR A 137       0.325   2.215  70.888  1.00 78.33           O  
ANISOU  524  O   TYR A 137     4783  14379  10602   -143   1706  -3880       O  
ATOM    525  CB  TYR A 137       1.794   4.344  71.831  1.00 85.85           C  
ANISOU  525  CB  TYR A 137     5900  15413  11306    -91   1727  -4171       C  
ATOM    526  CG  TYR A 137       1.780   5.580  72.704  1.00 88.33           C  
ANISOU  526  CG  TYR A 137     6230  15801  11530    -51   1788  -4317       C  
ATOM    527  CD1 TYR A 137       0.623   6.337  72.846  1.00 94.31           C  
ANISOU  527  CD1 TYR A 137     6946  16536  12351    -10   1859  -4329       C  
ATOM    528  CD2 TYR A 137       2.918   5.989  73.385  1.00 88.93           C  
ANISOU  528  CD2 TYR A 137     6349  15969  11470    -56   1771  -4457       C  
ATOM    529  CE1 TYR A 137       0.602   7.468  73.641  1.00 99.80           C  
ANISOU  529  CE1 TYR A 137     7642  17285  12992     25   1917  -4490       C  
ATOM    530  CE2 TYR A 137       2.905   7.117  74.183  1.00 91.21           C  
ANISOU  530  CE2 TYR A 137     6634  16325  11698    -27   1818  -4630       C  
ATOM    531  CZ  TYR A 137       1.747   7.853  74.307  1.00 98.75           C  
ANISOU  531  CZ  TYR A 137     7546  17241  12732     13   1893  -4653       C  
ATOM    532  OH  TYR A 137       1.735   8.976  75.102  1.00101.81           O  
ANISOU  532  OH  TYR A 137     7916  17683  13084     40   1943  -4852       O  
ATOM    533  N   GLY A 138       1.511   0.669  72.011  1.00 78.94           N  
ANISOU  533  N   GLY A 138     4792  14618  10585   -175   1730  -3735       N  
ATOM    534  CA  GLY A 138       0.926  -0.432  71.264  1.00 78.97           C  
ANISOU  534  CA  GLY A 138     4703  14498  10803   -220   1699  -3624       C  
ATOM    535  C   GLY A 138       1.188  -0.377  69.778  1.00 77.54           C  
ANISOU  535  C   GLY A 138     4597  14138  10727   -249   1582  -3747       C  
ATOM    536  O   GLY A 138       0.346  -0.815  68.986  1.00 77.73           O  
ANISOU  536  O   GLY A 138     4555  14066  10912   -274   1546  -3726       O  
ATOM    537  N   TYR A 139       2.338   0.163  69.377  1.00 76.31           N  
ANISOU  537  N   TYR A 139     4567  13954  10475   -242   1521  -3877       N  
ATOM    538  CA  TYR A 139       2.753   0.273  67.981  1.00 75.09           C  
ANISOU  538  CA  TYR A 139     4484  13668  10380   -254   1416  -3985       C  
ATOM    539  C   TYR A 139       1.834   1.172  67.160  1.00 74.98           C  
ANISOU  539  C   TYR A 139     4481  13603  10406   -223   1399  -4032       C  
ATOM    540  O   TYR A 139       1.769   1.044  65.935  1.00 74.51           O  
ANISOU  540  O   TYR A 139     4425  13473  10412   -228   1317  -4079       O  
ATOM    541  CB  TYR A 139       2.862  -1.110  67.328  1.00 76.08           C  
ANISOU  541  CB  TYR A 139     4538  13710  10661   -305   1356  -3951       C  
ATOM    542  CG  TYR A 139       3.877  -2.003  68.000  1.00 76.52           C  
ANISOU  542  CG  TYR A 139     4570  13794  10711   -329   1373  -3885       C  
ATOM    543  CD1 TYR A 139       5.230  -1.705  67.948  1.00 75.50           C  
ANISOU  543  CD1 TYR A 139     4546  13677  10463   -319   1336  -3963       C  
ATOM    544  CD2 TYR A 139       3.481  -3.146  68.682  1.00 80.25           C  
ANISOU  544  CD2 TYR A 139     4896  14280  11317   -357   1431  -3719       C  
ATOM    545  CE1 TYR A 139       6.163  -2.515  68.559  1.00 75.50           C  
ANISOU  545  CE1 TYR A 139     4512  13716  10458   -334   1353  -3887       C  
ATOM    546  CE2 TYR A 139       4.409  -3.966  69.296  1.00 79.73           C  
ANISOU  546  CE2 TYR A 139     4783  14248  11264   -369   1457  -3620       C  
ATOM    547  CZ  TYR A 139       5.748  -3.643  69.231  1.00 78.01           C  
ANISOU  547  CZ  TYR A 139     4678  14055  10907   -356   1415  -3709       C  
ATOM    548  OH  TYR A 139       6.679  -4.450  69.839  1.00 85.20           O  
ANISOU  548  OH  TYR A 139     5532  15012  11830   -361   1441  -3596       O  
ATOM    549  N   ARG A 140       1.129   2.093  67.807  1.00 75.61           N  
ANISOU  549  N   ARG A 140     4554  13733  10443   -185   1477  -4018       N  
ATOM    550  CA  ARG A 140       0.371   3.129  67.120  1.00 75.63           C  
ANISOU  550  CA  ARG A 140     4563  13686  10488   -141   1478  -4046       C  
ATOM    551  C   ARG A 140       1.148   4.434  67.209  1.00 83.99           C  
ANISOU  551  C   ARG A 140     5719  14718  11477   -101   1495  -4140       C  
ATOM    552  O   ARG A 140       1.623   4.803  68.287  1.00 88.22           O  
ANISOU  552  O   ARG A 140     6285  15314  11922    -97   1551  -4189       O  
ATOM    553  CB  ARG A 140      -1.022   3.299  67.727  1.00 76.89           C  
ANISOU  553  CB  ARG A 140     4629  13891  10694   -121   1562  -3964       C  
ATOM    554  CG  ARG A 140      -1.853   4.393  67.068  1.00 77.69           C  
ANISOU  554  CG  ARG A 140     4719  13944  10857    -68   1575  -3970       C  
ATOM    555  CD  ARG A 140      -3.117   4.688  67.863  1.00 78.44           C  
ANISOU  555  CD  ARG A 140     4730  14090  10985    -40   1676  -3900       C  
ATOM    556  NE  ARG A 140      -2.808   5.110  69.227  1.00 79.89           N  
ANISOU  556  NE  ARG A 140     4941  14355  11059    -22   1768  -3940       N  
ATOM    557  CZ  ARG A 140      -2.607   6.372  69.593  1.00 79.40           C  
ANISOU  557  CZ  ARG A 140     4929  14275  10966     25   1821  -4039       C  
ATOM    558  NH1 ARG A 140      -2.325   6.660  70.856  1.00 80.29           N  
ANISOU  558  NH1 ARG A 140     5051  14493  10960     37   1892  -4107       N  
ATOM    559  NH2 ARG A 140      -2.687   7.346  68.696  1.00 79.10           N  
ANISOU  559  NH2 ARG A 140     4912  14120  11023     64   1807  -4069       N  
ATOM    560  N   TRP A 141       1.289   5.111  66.081  1.00 77.02           N  
ANISOU  560  N   TRP A 141     4864  13755  10643    -69   1450  -4163       N  
ATOM    561  CA  TRP A 141       2.131   6.298  65.984  1.00 82.75           C  
ANISOU  561  CA  TRP A 141     5662  14419  11359    -34   1466  -4234       C  
ATOM    562  C   TRP A 141       1.568   7.436  66.833  1.00 81.65           C  
ANISOU  562  C   TRP A 141     5502  14269  11252      5   1570  -4269       C  
ATOM    563  O   TRP A 141       0.506   7.977  66.496  1.00 76.05           O  
ANISOU  563  O   TRP A 141     4731  13528  10636     49   1612  -4207       O  
ATOM    564  CB  TRP A 141       2.255   6.719  64.519  1.00 84.67           C  
ANISOU  564  CB  TRP A 141     5903  14601  11666      7   1411  -4197       C  
ATOM    565  CG  TRP A 141       3.327   7.730  64.272  1.00 90.21           C  
ANISOU  565  CG  TRP A 141     6663  15224  12387     38   1423  -4240       C  
ATOM    566  CD1 TRP A 141       3.161   9.012  63.839  1.00 88.22           C  
ANISOU  566  CD1 TRP A 141     6380  14890  12248    106   1481  -4201       C  
ATOM    567  CD2 TRP A 141       4.738   7.545  64.448  1.00 94.88           C  
ANISOU  567  CD2 TRP A 141     7333  15803  12913      5   1385  -4317       C  
ATOM    568  NE1 TRP A 141       4.380   9.636  63.731  1.00 95.40           N  
ANISOU  568  NE1 TRP A 141     7340  15725  13181    114   1484  -4251       N  
ATOM    569  CE2 TRP A 141       5.364   8.757  64.099  1.00 91.00           C  
ANISOU  569  CE2 TRP A 141     6855  15215  12505     50   1420  -4329       C  
ATOM    570  CE3 TRP A 141       5.531   6.472  64.867  1.00 85.73           C  
ANISOU  570  CE3 TRP A 141     6219  14700  11653    -54   1332  -4362       C  
ATOM    571  CZ2 TRP A 141       6.744   8.928  64.157  1.00 86.40           C  
ANISOU  571  CZ2 TRP A 141     6334  14594  11899     31   1397  -4398       C  
ATOM    572  CZ3 TRP A 141       6.900   6.643  64.921  1.00 86.04           C  
ANISOU  572  CZ3 TRP A 141     6325  14714  11655    -67   1307  -4427       C  
ATOM    573  CH2 TRP A 141       7.493   7.861  64.567  1.00 86.18           C  
ANISOU  573  CH2 TRP A 141     6359  14637  11747    -29   1335  -4451       C  
ATOM    574  N   PRO A 142       2.234   7.832  67.928  1.00 78.27           N  
ANISOU  574  N   PRO A 142     5113  13875  10752     -7   1612  -4377       N  
ATOM    575  CA  PRO A 142       1.680   8.886  68.788  1.00 86.82           C  
ANISOU  575  CA  PRO A 142     6163  14957  11867     29   1710  -4451       C  
ATOM    576  C   PRO A 142       1.961  10.280  68.253  1.00 93.30           C  
ANISOU  576  C   PRO A 142     6990  15623  12838     74   1744  -4509       C  
ATOM    577  O   PRO A 142       1.156  11.200  68.430  1.00118.03           O  
ANISOU  577  O   PRO A 142    10066  18697  16082    122   1827  -4520       O  
ATOM    578  CB  PRO A 142       2.390   8.654  70.132  1.00 80.56           C  
ANISOU  578  CB  PRO A 142     5391  14300  10916     -4   1724  -4564       C  
ATOM    579  CG  PRO A 142       3.202   7.374  69.962  1.00 76.52           C  
ANISOU  579  CG  PRO A 142     4915  13855  10306    -53   1644  -4503       C  
ATOM    580  CD  PRO A 142       3.460   7.259  68.501  1.00 75.24           C  
ANISOU  580  CD  PRO A 142     4784  13559  10245    -53   1571  -4444       C  
ATOM    581  N   LEU A 143       3.106  10.442  67.599  1.00 84.06           N  
ANISOU  581  N   LEU A 143     5872  14377  11689     64   1689  -4533       N  
ATOM    582  CA  LEU A 143       3.524  11.726  67.070  1.00 76.91           C  
ANISOU  582  CA  LEU A 143     4953  13314  10955    109   1731  -4563       C  
ATOM    583  C   LEU A 143       2.636  12.101  65.884  1.00 84.17           C  
ANISOU  583  C   LEU A 143     5805  14162  12013    179   1753  -4387       C  
ATOM    584  O   LEU A 143       1.812  11.298  65.435  1.00 76.70           O  
ANISOU  584  O   LEU A 143     4833  13299  11011    180   1714  -4273       O  
ATOM    585  CB  LEU A 143       4.998  11.662  66.668  1.00 79.26           C  
ANISOU  585  CB  LEU A 143     5313  13571  11232     81   1668  -4607       C  
ATOM    586  CG  LEU A 143       5.966  11.189  67.753  1.00 78.27           C  
ANISOU  586  CG  LEU A 143     5241  13545  10952     13   1631  -4761       C  
ATOM    587  CD1 LEU A 143       7.393  11.198  67.229  1.00 74.90           C  
ANISOU  587  CD1 LEU A 143     4865  13061  10531     -7   1572  -4788       C  
ATOM    588  CD2 LEU A 143       5.836  12.045  69.005  1.00 82.21           C  
ANISOU  588  CD2 LEU A 143     5704  14061  11472      8   1704  -4946       C  
ATOM    589  N   PRO A 144       2.759  13.330  65.369  1.00 87.85           N  
ANISOU  589  N   PRO A 144     6220  14483  12677    242   1821  -4354       N  
ATOM    590  CA  PRO A 144       2.023  13.684  64.148  1.00 94.19           C  
ANISOU  590  CA  PRO A 144     6937  15254  13598    325   1842  -4145       C  
ATOM    591  C   PRO A 144       2.344  12.724  63.011  1.00 95.97           C  
ANISOU  591  C   PRO A 144     7183  15581  13701    320   1729  -4027       C  
ATOM    592  O   PRO A 144       3.429  12.141  62.948  1.00102.12           O  
ANISOU  592  O   PRO A 144     8041  16386  14373    271   1656  -4092       O  
ATOM    593  CB  PRO A 144       2.509  15.103  63.837  1.00 94.55           C  
ANISOU  593  CB  PRO A 144     6920  15120  13884    391   1936  -4122       C  
ATOM    594  CG  PRO A 144       2.901  15.662  65.161  1.00 92.81           C  
ANISOU  594  CG  PRO A 144     6729  14823  13711    342   1992  -4365       C  
ATOM    595  CD  PRO A 144       3.364  14.514  66.014  1.00 86.64           C  
ANISOU  595  CD  PRO A 144     6052  14195  12672    247   1901  -4508       C  
ATOM    596  N   SER A 145       1.380  12.572  62.099  1.00 89.45           N  
ANISOU  596  N   SER A 145     7216  14319  12450   2766   2769    359       N  
ATOM    597  CA  SER A 145       1.514  11.582  61.034  1.00 90.16           C  
ANISOU  597  CA  SER A 145     7286  14437  12534   2629   2636    497       C  
ATOM    598  C   SER A 145       2.648  11.912  60.071  1.00 87.32           C  
ANISOU  598  C   SER A 145     7102  13868  12207   2653   2510    516       C  
ATOM    599  O   SER A 145       3.244  10.999  59.488  1.00 91.26           O  
ANISOU  599  O   SER A 145     7660  14345  12669   2509   2420    603       O  
ATOM    600  CB  SER A 145       0.194  11.454  60.275  1.00102.70           C  
ANISOU  600  CB  SER A 145     8651  16181  14189   2657   2593    586       C  
ATOM    601  OG  SER A 145      -0.296  12.724  59.884  1.00111.69           O  
ANISOU  601  OG  SER A 145     9740  17264  15434   2865   2589    538       O  
ATOM    602  N   LYS A 146       2.966  13.196  59.891  1.00 88.45           N  
ANISOU  602  N   LYS A 146     7333  13854  12420   2827   2502    435       N  
ATOM    603  CA  LYS A 146       4.054  13.576  58.994  1.00 87.91           C  
ANISOU  603  CA  LYS A 146     7438  13581  12383   2851   2386    449       C  
ATOM    604  C   LYS A 146       5.428  13.198  59.536  1.00 86.61           C  
ANISOU  604  C   LYS A 146     7479  13292  12135   2749   2395    407       C  
ATOM    605  O   LYS A 146       6.396  13.168  58.767  1.00 72.09           O  
ANISOU  605  O   LYS A 146     5781  11306  10306   2718   2293    441       O  
ATOM    606  CB  LYS A 146       3.992  15.074  58.697  1.00 88.24           C  
ANISOU  606  CB  LYS A 146     7522  13487  12520   3058   2373    372       C  
ATOM    607  CG  LYS A 146       2.740  15.481  57.936  1.00 89.20           C  
ANISOU  607  CG  LYS A 146     7452  13704  12735   3164   2336    425       C  
ATOM    608  CD  LYS A 146       2.667  14.764  56.595  1.00 89.71           C  
ANISOU  608  CD  LYS A 146     7470  13796  12820   3074   2195    568       C  
ATOM    609  CE  LYS A 146       1.431  15.171  55.807  1.00 92.69           C  
ANISOU  609  CE  LYS A 146     7659  14269  13290   3178   2150    624       C  
ATOM    610  NZ  LYS A 146       1.309  14.409  54.531  1.00 86.51           N  
ANISOU  610  NZ  LYS A 146     6825  13528  12518   3075   2015    765       N  
ATOM    611  N   LEU A 147       5.542  12.919  60.837  1.00 90.94           N  
ANISOU  611  N   LEU A 147     8052  13898  12603   2696   2515    335       N  
ATOM    612  CA  LEU A 147       6.825  12.561  61.428  1.00 95.69           C  
ANISOU  612  CA  LEU A 147     8845  14389  13122   2600   2528    292       C  
ATOM    613  C   LEU A 147       7.166  11.086  61.263  1.00 96.25           C  
ANISOU  613  C   LEU A 147     8916  14534  13121   2392   2482    395       C  
ATOM    614  O   LEU A 147       8.325  10.711  61.469  1.00102.75           O  
ANISOU  614  O   LEU A 147     9902  15249  13889   2307   2461    383       O  
ATOM    615  CB  LEU A 147       6.849  12.928  62.915  1.00 99.68           C  
ANISOU  615  CB  LEU A 147     9391  14917  13567   2629   2674    166       C  
ATOM    616  CG  LEU A 147       6.824  14.421  63.248  1.00102.08           C  
ANISOU  616  CG  LEU A 147     9750  15108  13928   2822   2722     41       C  
ATOM    617  CD1 LEU A 147       6.935  14.632  64.750  1.00108.38           C  
ANISOU  617  CD1 LEU A 147    10598  15931  14650   2823   2865    -80       C  
ATOM    618  CD2 LEU A 147       7.935  15.161  62.515  1.00 96.57           C  
ANISOU  618  CD2 LEU A 147     9241  14178  13274   2885   2616     21       C  
ATOM    619  N   CYS A 148       6.199  10.246  60.888  1.00 93.68           N  
ANISOU  619  N   CYS A 148     8414  14384  12796   2307   2462    497       N  
ATOM    620  CA  CYS A 148       6.499   8.839  60.641  1.00 93.76           C  
ANISOU  620  CA  CYS A 148     8425  14457  12742   2103   2404    600       C  
ATOM    621  C   CYS A 148       7.455   8.681  59.465  1.00 95.27           C  
ANISOU  621  C   CYS A 148     8735  14496  12966   2070   2265    665       C  
ATOM    622  O   CYS A 148       8.414   7.897  59.529  1.00 88.99           O  
ANISOU  622  O   CYS A 148     8058  13641  12113   1938   2232    691       O  
ATOM    623  CB  CYS A 148       5.202   8.072  60.386  1.00 87.37           C  
ANISOU  623  CB  CYS A 148     7402  13860  11935   2024   2397    695       C  
ATOM    624  SG  CYS A 148       5.410   6.436  59.643  1.00 77.30           S  
ANISOU  624  SG  CYS A 148     6113  12648  10609   1784   2281    843       S  
ATOM    625  N   ALA A 149       7.200   9.414  58.378  1.00 89.96           N  
ANISOU  625  N   ALA A 149     8033  13760  12386   2188   2184    693       N  
ATOM    626  CA  ALA A 149       8.105   9.381  57.237  1.00 79.22           C  
ANISOU  626  CA  ALA A 149     6792  12248  11060   2168   2057    748       C  
ATOM    627  C   ALA A 149       9.493   9.863  57.630  1.00 71.08           C  
ANISOU  627  C   ALA A 149     5982  11018  10008   2196   2069    662       C  
ATOM    628  O   ALA A 149      10.498   9.291  57.196  1.00 77.13           O  
ANISOU  628  O   ALA A 149     6868  11687  10752   2097   1999    703       O  
ATOM    629  CB  ALA A 149       7.545  10.226  56.092  1.00 79.88           C  
ANISOU  629  CB  ALA A 149     6811  12295  11246   2302   1978    781       C  
ATOM    630  N   VAL A 150       9.570  10.903  58.464  1.00 70.46           N  
ANISOU  630  N   VAL A 150     5961  10876   9933   2325   2155    540       N  
ATOM    631  CA  VAL A 150      10.866  11.419  58.898  1.00 76.11           C  
ANISOU  631  CA  VAL A 150     6890  11402  10624   2350   2165    451       C  
ATOM    632  C   VAL A 150      11.598  10.390  59.753  1.00 71.83           C  
ANISOU  632  C   VAL A 150     6427  10885   9982   2193   2209    448       C  
ATOM    633  O   VAL A 150      12.822  10.230  59.649  1.00 70.65           O  
ANISOU  633  O   VAL A 150     6445  10591   9809   2141   2165    439       O  
ATOM    634  CB  VAL A 150      10.683  12.752  59.647  1.00 79.79           C  
ANISOU  634  CB  VAL A 150     7393  11810  11115   2515   2246    320       C  
ATOM    635  CG1 VAL A 150      12.018  13.256  60.181  1.00 80.02           C  
ANISOU  635  CG1 VAL A 150     7646  11650  11108   2525   2255    225       C  
ATOM    636  CG2 VAL A 150      10.042  13.788  58.735  1.00 79.35           C  
ANISOU  636  CG2 VAL A 150     7275  11712  11164   2670   2190    326       C  
ATOM    637  N   TRP A 151      10.860   9.670  60.599  1.00 67.07           N  
ANISOU  637  N   TRP A 151     5704  10463   9317   2111   2295    456       N  
ATOM    638  CA  TRP A 151      11.464   8.640  61.438  1.00 63.30           C  
ANISOU  638  CA  TRP A 151     5292  10021   8738   1951   2337    459       C  
ATOM    639  C   TRP A 151      12.032   7.506  60.593  1.00 63.82           C  
ANISOU  639  C   TRP A 151     5387  10069   8794   1797   2230    574       C  
ATOM    640  O   TRP A 151      13.191   7.099  60.764  1.00 64.95           O  
ANISOU  640  O   TRP A 151     5681  10103   8894   1717   2209    566       O  
ATOM    641  CB  TRP A 151      10.418   8.117  62.421  1.00 62.51           C  
ANISOU  641  CB  TRP A 151     5046  10128   8579   1889   2445    453       C  
ATOM    642  CG  TRP A 151      10.894   7.030  63.324  1.00 60.68           C  
ANISOU  642  CG  TRP A 151     4870   9950   8237   1714   2490    461       C  
ATOM    643  CD1 TRP A 151      11.797   7.142  64.339  1.00 56.42           C  
ANISOU  643  CD1 TRP A 151     4483   9330   7625   1693   2554    374       C  
ATOM    644  CD2 TRP A 151      10.477   5.658  63.304  1.00 70.19           C  
ANISOU  644  CD2 TRP A 151     5983  11298   9387   1527   2468    563       C  
ATOM    645  NE1 TRP A 151      11.972   5.923  64.952  1.00 60.22           N  
ANISOU  645  NE1 TRP A 151     4973   9896   8011   1507   2576    417       N  
ATOM    646  CE2 TRP A 151      11.173   4.996  64.335  1.00 68.47           C  
ANISOU  646  CE2 TRP A 151     5873  11076   9066   1400   2523    533       C  
ATOM    647  CE3 TRP A 151       9.585   4.926  62.513  1.00 76.22           C  
ANISOU  647  CE3 TRP A 151     6593  12191  10178   1448   2402    677       C  
ATOM    648  CZ2 TRP A 151      11.006   3.634  64.595  1.00 73.96           C  
ANISOU  648  CZ2 TRP A 151     6531  11884   9687   1196   2511    613       C  
ATOM    649  CZ3 TRP A 151       9.419   3.574  62.773  1.00 80.03           C  
ANISOU  649  CZ3 TRP A 151     7039  12785  10585   1244   2389    754       C  
ATOM    650  CH2 TRP A 151      10.128   2.942  63.805  1.00 79.12           C  
ANISOU  650  CH2 TRP A 151     7037  12654  10369   1120   2442    722       C  
ATOM    651  N   ILE A 152      11.225   6.988  59.664  1.00 70.95           N  
ANISOU  651  N   ILE A 152     6147  11075   9736   1752   2159    681       N  
ATOM    652  CA  ILE A 152      11.703   5.931  58.775  1.00 70.83           C  
ANISOU  652  CA  ILE A 152     6154  11042   9716   1605   2050    791       C  
ATOM    653  C   ILE A 152      12.888   6.421  57.951  1.00 70.05           C  
ANISOU  653  C   ILE A 152     6219  10730   9668   1659   1966    784       C  
ATOM    654  O   ILE A 152      13.857   5.683  57.731  1.00 73.03           O  
ANISOU  654  O   ILE A 152     6701  11029  10019   1543   1915    822       O  
ATOM    655  CB  ILE A 152      10.556   5.423  57.881  1.00 63.04           C  
ANISOU  655  CB  ILE A 152     4986  10201   8767   1559   1984    901       C  
ATOM    656  CG1 ILE A 152       9.457   4.787  58.736  1.00 55.06           C  
ANISOU  656  CG1 ILE A 152     3824   9400   7697   1477   2064    913       C  
ATOM    657  CG2 ILE A 152      11.078   4.425  56.859  1.00 55.95           C  
ANISOU  657  CG2 ILE A 152     4123   9266   7871   1414   1860   1009       C  
ATOM    658  CD1 ILE A 152       8.324   4.197  57.928  1.00 54.74           C  
ANISOU  658  CD1 ILE A 152     3607   9508   7682   1414   1997   1021       C  
ATOM    659  N   TYR A 153      12.841   7.678  57.497  1.00 61.70           N  
ANISOU  659  N   TYR A 153     5189   9570   8684   1830   1951    734       N  
ATOM    660  CA  TYR A 153      13.928   8.224  56.693  1.00 60.06           C  
ANISOU  660  CA  TYR A 153     5141   9155   8524   1881   1870    724       C  
ATOM    661  C   TYR A 153      15.224   8.289  57.483  1.00 56.19           C  
ANISOU  661  C   TYR A 153     4842   8526   7984   1855   1909    643       C  
ATOM    662  O   TYR A 153      16.284   7.914  56.980  1.00 56.77           O  
ANISOU  662  O   TYR A 153     5037   8473   8060   1787   1842    672       O  
ATOM    663  CB  TYR A 153      13.565   9.614  56.185  1.00 65.26           C  
ANISOU  663  CB  TYR A 153     5799   9734   9263   2063   1851    676       C  
ATOM    664  CG  TYR A 153      14.775  10.428  55.771  1.00 73.93           C  
ANISOU  664  CG  TYR A 153     7096  10600  10392   2126   1797    622       C  
ATOM    665  CD1 TYR A 153      15.448  10.154  54.584  1.00 70.17           C  
ANISOU  665  CD1 TYR A 153     6692  10019   9952   2073   1686    694       C  
ATOM    666  CD2 TYR A 153      15.248  11.466  56.568  1.00 80.54           C  
ANISOU  666  CD2 TYR A 153     8054  11325  11220   2227   1855    498       C  
ATOM    667  CE1 TYR A 153      16.552  10.897  54.198  1.00 71.14           C  
ANISOU  667  CE1 TYR A 153     6999   9932  10100   2119   1635    643       C  
ATOM    668  CE2 TYR A 153      16.355  12.212  56.191  1.00 78.36           C  
ANISOU  668  CE2 TYR A 153     7966  10840  10969   2267   1798    449       C  
ATOM    669  CZ  TYR A 153      17.002  11.922  55.005  1.00 75.81           C  
ANISOU  669  CZ  TYR A 153     7708  10417  10680   2211   1688    521       C  
ATOM    670  OH  TYR A 153      18.103  12.657  54.621  1.00 73.99           O  
ANISOU  670  OH  TYR A 153     7663   9982  10469   2238   1629    471       O  
ATOM    671  N   LEU A 154      15.164   8.790  58.716  1.00 60.15           N  
ANISOU  671  N   LEU A 154     5372   9042   8439   1911   2015    539       N  
ATOM    672  CA  LEU A 154      16.375   8.882  59.523  1.00 63.39           C  
ANISOU  672  CA  LEU A 154     5966   9324   8796   1885   2050    459       C  
ATOM    673  C   LEU A 154      16.927   7.499  59.837  1.00 60.92           C  
ANISOU  673  C   LEU A 154     5678   9057   8412   1703   2049    518       C  
ATOM    674  O   LEU A 154      18.145   7.282  59.776  1.00 67.95           O  
ANISOU  674  O   LEU A 154     6724   9806   9289   1652   2013    510       O  
ATOM    675  CB  LEU A 154      16.095   9.658  60.808  1.00 82.46           C  
ANISOU  675  CB  LEU A 154     8396  11766  11170   1972   2165    338       C  
ATOM    676  CG  LEU A 154      15.877  11.162  60.614  1.00 89.41           C  
ANISOU  676  CG  LEU A 154     9306  12549  12118   2152   2162    257       C  
ATOM    677  CD1 LEU A 154      15.788  11.873  61.957  1.00 87.47           C  
ANISOU  677  CD1 LEU A 154     9100  12310  11824   2222   2275    129       C  
ATOM    678  CD2 LEU A 154      16.978  11.765  59.744  1.00 84.45           C  
ANISOU  678  CD2 LEU A 154     8846  11701  11541   2188   2060    249       C  
ATOM    679  N   ASP A 155      16.045   6.545  60.150  1.00 61.31           N  
ANISOU  679  N   ASP A 155     5579   9300   8417   1597   2082    580       N  
ATOM    680  CA  ASP A 155      16.492   5.179  60.410  1.00 52.34           C  
ANISOU  680  CA  ASP A 155     4463   8213   7212   1407   2069    644       C  
ATOM    681  C   ASP A 155      17.206   4.592  59.196  1.00 42.20           C  
ANISOU  681  C   ASP A 155     3229   6830   5974   1331   1949    734       C  
ATOM    682  O   ASP A 155      18.343   4.103  59.297  1.00 47.09           O  
ANISOU  682  O   ASP A 155     3983   7340   6568   1249   1926    735       O  
ATOM    683  CB  ASP A 155      15.292   4.316  60.805  1.00 54.58           C  
ANISOU  683  CB  ASP A 155     4573   8720   7447   1301   2107    701       C  
ATOM    684  CG  ASP A 155      15.699   3.021  61.477  1.00 68.11           C  
ANISOU  684  CG  ASP A 155     6325  10489   9065   1102   2118    737       C  
ATOM    685  OD1 ASP A 155      16.915   2.729  61.530  1.00 66.02           O  
ANISOU  685  OD1 ASP A 155     6212  10092   8779   1045   2089    730       O  
ATOM    686  OD2 ASP A 155      14.799   2.297  61.960  1.00 71.95           O  
ANISOU  686  OD2 ASP A 155     6694  11146   9497    998   2153    774       O  
ATOM    687  N   VAL A 156      16.553   4.647  58.031  1.00 51.36           N  
ANISOU  687  N   VAL A 156     4285   8026   7205   1359   1870    810       N  
ATOM    688  CA  VAL A 156      17.131   4.085  56.814  1.00 53.86           C  
ANISOU  688  CA  VAL A 156     4637   8259   7567   1283   1754    898       C  
ATOM    689  C   VAL A 156      18.425   4.801  56.453  1.00 59.10           C  
ANISOU  689  C   VAL A 156     5484   8695   8274   1361   1723    845       C  
ATOM    690  O   VAL A 156      19.401   4.172  56.032  1.00 57.73           O  
ANISOU  690  O   VAL A 156     5406   8422   8107   1267   1666    882       O  
ATOM    691  CB  VAL A 156      16.107   4.149  55.664  1.00 45.37           C  
ANISOU  691  CB  VAL A 156     3416   7268   6555   1310   1679    981       C  
ATOM    692  CG1 VAL A 156      16.782   3.833  54.335  1.00 40.02           C  
ANISOU  692  CG1 VAL A 156     2796   6476   5933   1261   1559   1056       C  
ATOM    693  CG2 VAL A 156      14.956   3.190  55.927  1.00 43.05           C  
ANISOU  693  CG2 VAL A 156     2954   7189   6212   1190   1690   1048       C  
ATOM    694  N   LEU A 157      18.462   6.123  56.637  1.00 62.06           N  
ANISOU  694  N   LEU A 157     5919   8981   8680   1526   1756    752       N  
ATOM    695  CA  LEU A 157      19.644   6.902  56.293  1.00 58.51           C  
ANISOU  695  CA  LEU A 157     5653   8310   8268   1595   1717    693       C  
ATOM    696  C   LEU A 157      20.833   6.495  57.146  1.00 63.63           C  
ANISOU  696  C   LEU A 157     6454   8864   8859   1520   1755    642       C  
ATOM    697  O   LEU A 157      21.936   6.279  56.632  1.00 64.89           O  
ANISOU  697  O   LEU A 157     6739   8874   9043   1473   1696    653       O  
ATOM    698  CB  LEU A 157      19.346   8.391  56.458  1.00 39.86           C  
ANISOU  698  CB  LEU A 157     3322   5885   5937   1767   1742    599       C  
ATOM    699  CG  LEU A 157      20.531   9.351  56.356  1.00 45.06           C  
ANISOU  699  CG  LEU A 157     4185   6319   6616   1831   1708    514       C  
ATOM    700  CD1 LEU A 157      21.112   9.328  54.957  1.00 37.76           C  
ANISOU  700  CD1 LEU A 157     3321   5273   5754   1807   1592    576       C  
ATOM    701  CD2 LEU A 157      20.131  10.770  56.748  1.00 47.74           C  
ANISOU  701  CD2 LEU A 157     4545   6622   6973   1983   1743    414       C  
ATOM    702  N   PHE A 158      20.628   6.387  58.460  1.00 58.22           N  
ANISOU  702  N   PHE A 158     5760   8264   8097   1504   1854    583       N  
ATOM    703  CA  PHE A 158      21.736   6.019  59.333  1.00 59.48           C  
ANISOU  703  CA  PHE A 158     6068   8337   8194   1432   1892    532       C  
ATOM    704  C   PHE A 158      22.215   4.600  59.049  1.00 70.27           C  
ANISOU  704  C   PHE A 158     7432   9726   9542   1258   1851    627       C  
ATOM    705  O   PHE A 158      23.426   4.347  58.998  1.00 80.35           O  
ANISOU  705  O   PHE A 158     8853  10854  10822   1207   1825    613       O  
ATOM    706  CB  PHE A 158      21.329   6.187  60.796  1.00 67.25           C  
ANISOU  706  CB  PHE A 158     7038   9423   9092   1445   2005    453       C  
ATOM    707  CG  PHE A 158      21.003   7.610  61.171  1.00 78.40           C  
ANISOU  707  CG  PHE A 158     8474  10793  10523   1609   2046    347       C  
ATOM    708  CD1 PHE A 158      21.511   8.671  60.433  1.00 71.25           C  
ANISOU  708  CD1 PHE A 158     7667   9715   9688   1716   1979    308       C  
ATOM    709  CD2 PHE A 158      20.191   7.886  62.261  1.00 79.35           C  
ANISOU  709  CD2 PHE A 158     8519  11042  10586   1647   2148    286       C  
ATOM    710  CE1 PHE A 158      21.214   9.979  60.771  1.00 65.48           C  
ANISOU  710  CE1 PHE A 158     6963   8943   8975   1854   2007    213       C  
ATOM    711  CE2 PHE A 158      19.892   9.192  62.604  1.00 78.76           C  
ANISOU  711  CE2 PHE A 158     8466  10925  10534   1795   2185    187       C  
ATOM    712  CZ  PHE A 158      20.405  10.240  61.859  1.00 73.66           C  
ANISOU  712  CZ  PHE A 158     7920  10106   9960   1897   2112    151       C  
ATOM    713  N   SER A 159      21.287   3.664  58.832  1.00 71.98           N  
ANISOU  713  N   SER A 159     7488  10120   9741   1156   1837    721       N  
ATOM    714  CA  SER A 159      21.707   2.292  58.558  1.00 70.83           C  
ANISOU  714  CA  SER A 159     7344   9994   9573    969   1784    812       C  
ATOM    715  C   SER A 159      22.444   2.188  57.224  1.00 65.73           C  
ANISOU  715  C   SER A 159     6755   9205   9015    958   1680    866       C  
ATOM    716  O   SER A 159      23.441   1.459  57.108  1.00 76.24           O  
ANISOU  716  O   SER A 159     8183  10441  10344    846   1646    890       O  
ATOM    717  CB  SER A 159      20.495   1.364  58.584  1.00 77.05           C  
ANISOU  717  CB  SER A 159     7960  10997  10318    850   1773    895       C  
ATOM    718  OG  SER A 159      19.881   1.359  59.863  1.00 78.38           O  
ANISOU  718  OG  SER A 159     8084  11296  10401    841   1873    844       O  
ATOM    719  N   THR A 160      21.978   2.921  56.209  1.00 58.39           N  
ANISOU  719  N   THR A 160     5769   8253   8162   1068   1627    883       N  
ATOM    720  CA  THR A 160      22.647   2.912  54.914  1.00 52.47           C  
ANISOU  720  CA  THR A 160     5076   7366   7494   1062   1528    929       C  
ATOM    721  C   THR A 160      24.029   3.542  55.011  1.00 53.35           C  
ANISOU  721  C   THR A 160     5387   7254   7631   1122   1532    843       C  
ATOM    722  O   THR A 160      24.993   3.037  54.420  1.00 52.75           O  
ANISOU  722  O   THR A 160     5396   7055   7590   1045   1472    869       O  
ATOM    723  CB  THR A 160      21.790   3.644  53.877  1.00 41.90           C  
ANISOU  723  CB  THR A 160     3644   6058   6220   1168   1473    961       C  
ATOM    724  OG1 THR A 160      20.473   3.081  53.857  1.00 48.93           O  
ANISOU  724  OG1 THR A 160     4350   7158   7083   1113   1471   1032       O  
ATOM    725  CG2 THR A 160      22.388   3.517  52.496  1.00 31.75           C  
ANISOU  725  CG2 THR A 160     2405   4650   5008   1141   1364   1020       C  
ATOM    726  N   ALA A 161      24.147   4.642  55.756  1.00 43.41           N  
ANISOU  726  N   ALA A 161     4209   5934   6350   1247   1590    734       N  
ATOM    727  CA  ALA A 161      25.456   5.234  55.992  1.00 37.17           C  
ANISOU  727  CA  ALA A 161     3621   4937   5564   1281   1584    642       C  
ATOM    728  C   ALA A 161      26.392   4.242  56.668  1.00 35.55           C  
ANISOU  728  C   ALA A 161     3500   4692   5317   1155   1616    640       C  
ATOM    729  O   ALA A 161      27.561   4.133  56.290  1.00 28.36           O  
ANISOU  729  O   ALA A 161     2730   3611   4436   1114   1561    618       O  
ATOM    730  CB  ALA A 161      25.316   6.505  56.828  1.00 31.49           C  
ANISOU  730  CB  ALA A 161     2965   4188   4812   1408   1638    528       C  
ATOM    731  N   LYS A 162      25.894   3.495  57.657  1.00 35.12           N  
ANISOU  731  N   LYS A 162     3370   4791   5184   1074   1690    658       N  
ATOM    732  CA  LYS A 162      26.730   2.492  58.317  1.00 30.38           C  
ANISOU  732  CA  LYS A 162     2885   4148   4509    902   1661    647       C  
ATOM    733  C   LYS A 162      27.240   1.449  57.328  1.00 41.54           C  
ANISOU  733  C   LYS A 162     4336   5499   5947    743   1520    718       C  
ATOM    734  O   LYS A 162      28.453   1.192  57.231  1.00 25.91           O  
ANISOU  734  O   LYS A 162     2519   3356   3969    674   1451    681       O  
ATOM    735  CB  LYS A 162      25.940   1.803  59.427  1.00 32.80           C  
ANISOU  735  CB  LYS A 162     3096   4648   4717    819   1741    670       C  
ATOM    736  CG  LYS A 162      25.652   2.662  60.626  1.00 51.53           C  
ANISOU  736  CG  LYS A 162     5470   7070   7038    943   1881    582       C  
ATOM    737  CD  LYS A 162      25.019   1.820  61.711  1.00 71.13           C  
ANISOU  737  CD  LYS A 162     7880   9735   9411    824   1944    607       C  
ATOM    738  CE  LYS A 162      25.931   0.664  62.106  1.00 67.76           C  
ANISOU  738  CE  LYS A 162     7585   9243   8918    624   1872    623       C  
ATOM    739  NZ  LYS A 162      25.293  -0.226  63.119  1.00 78.50           N  
ANISOU  739  NZ  LYS A 162     8875  10783  10167    493   1928    660       N  
ATOM    740  N   ILE A 163      26.315   0.826  56.593  1.00 42.49           N  
ANISOU  740  N   ILE A 163     4305   5753   6087    682   1476    820       N  
ATOM    741  CA  ILE A 163      26.692  -0.293  55.735  1.00 38.89           C  
ANISOU  741  CA  ILE A 163     3878   5258   5642    515   1348    890       C  
ATOM    742  C   ILE A 163      27.620   0.175  54.615  1.00 43.86           C  
ANISOU  742  C   ILE A 163     4619   5693   6353    561   1261    868       C  
ATOM    743  O   ILE A 163      28.604  -0.501  54.282  1.00 44.57           O  
ANISOU  743  O   ILE A 163     4833   5661   6442    445   1173    864       O  
ATOM    744  CB  ILE A 163      25.429  -0.996  55.200  1.00 31.42           C  
ANISOU  744  CB  ILE A 163     2740   4503   4694    443   1323   1004       C  
ATOM    745  CG1 ILE A 163      25.794  -2.273  54.446  1.00 27.01           C  
ANISOU  745  CG1 ILE A 163     2221   3910   4131    251   1194   1073       C  
ATOM    746  CG2 ILE A 163      24.596  -0.060  54.342  1.00 39.22           C  
ANISOU  746  CG2 ILE A 163     3595   5544   5762    599   1337   1034       C  
ATOM    747  CD1 ILE A 163      26.257  -3.385  55.355  1.00 36.16           C  
ANISOU  747  CD1 ILE A 163     3463   5072   5203     82   1182   1070       C  
ATOM    748  N   TRP A 164      27.358   1.359  54.046  1.00 40.99           N  
ANISOU  748  N   TRP A 164     4220   5294   6060    733   1287    850       N  
ATOM    749  CA  TRP A 164      28.224   1.866  52.993  1.00 40.85           C  
ANISOU  749  CA  TRP A 164     4310   5097   6116    776   1210    830       C  
ATOM    750  C   TRP A 164      29.538   2.417  53.526  1.00 42.49           C  
ANISOU  750  C   TRP A 164     4708   5117   6318    812   1227    723       C  
ATOM    751  O   TRP A 164      30.523   2.429  52.787  1.00 43.93           O  
ANISOU  751  O   TRP A 164     5007   5144   6541    781   1149    706       O  
ATOM    752  CB  TRP A 164      27.491   2.915  52.158  1.00 49.32           C  
ANISOU  752  CB  TRP A 164     5285   6191   7265    939   1222    856       C  
ATOM    753  CG  TRP A 164      26.569   2.295  51.152  1.00 50.61           C  
ANISOU  753  CG  TRP A 164     5299   6478   7453    875   1153    969       C  
ATOM    754  CD1 TRP A 164      25.213   2.353  51.147  1.00 55.29           C  
ANISOU  754  CD1 TRP A 164     5698   7261   8050    924   1193   1034       C  
ATOM    755  CD2 TRP A 164      26.942   1.521  50.002  1.00 51.23           C  
ANISOU  755  CD2 TRP A 164     5409   6502   7553    748   1029   1028       C  
ATOM    756  NE1 TRP A 164      24.709   1.664  50.069  1.00 59.68           N  
ANISOU  756  NE1 TRP A 164     6163   7885   8627    831   1098   1134       N  
ATOM    757  CE2 TRP A 164      25.750   1.142  49.349  1.00 47.15           C  
ANISOU  757  CE2 TRP A 164     4716   6148   7050    721    998   1130       C  
ATOM    758  CE3 TRP A 164      28.168   1.110  49.463  1.00 42.58           C  
ANISOU  758  CE3 TRP A 164     4472   5240   6468    654    945   1003       C  
ATOM    759  CZ2 TRP A 164      25.743   0.375  48.184  1.00 35.49           C  
ANISOU  759  CZ2 TRP A 164     3226   4668   5591    600    883   1206       C  
ATOM    760  CZ3 TRP A 164      28.160   0.342  48.305  1.00 40.36           C  
ANISOU  760  CZ3 TRP A 164     4175   4955   6205    539    836   1075       C  
ATOM    761  CH2 TRP A 164      26.953  -0.018  47.681  1.00 36.81           C  
ANISOU  761  CH2 TRP A 164     3557   4666   5763    512    806   1175       C  
ATOM    762  N   HIS A 165      29.596   2.846  54.788  1.00 39.39           N  
ANISOU  762  N   HIS A 165     4351   4740   5874    869   1326    651       N  
ATOM    763  CA  HIS A 165      30.890   3.145  55.386  1.00 37.64           C  
ANISOU  763  CA  HIS A 165     4315   4353   5634    866   1329    556       C  
ATOM    764  C   HIS A 165      31.727   1.879  55.504  1.00 39.00           C  
ANISOU  764  C   HIS A 165     4575   4479   5764    677   1248    570       C  
ATOM    765  O   HIS A 165      32.928   1.894  55.220  1.00 37.86           O  
ANISOU  765  O   HIS A 165     4572   4171   5644    644   1188    526       O  
ATOM    766  CB  HIS A 165      30.711   3.798  56.758  1.00 43.39           C  
ANISOU  766  CB  HIS A 165     5060   5119   6305    955   1452    477       C  
ATOM    767  CG  HIS A 165      30.604   5.291  56.716  1.00 49.99           C  
ANISOU  767  CG  HIS A 165     5929   5896   7169   1122   1483    410       C  
ATOM    768  ND1 HIS A 165      29.563   5.949  56.096  1.00 56.24           N  
ANISOU  768  ND1 HIS A 165     6608   6772   7989   1211   1469    442       N  
ATOM    769  CD2 HIS A 165      31.404   6.255  57.230  1.00 53.33           C  
ANISOU  769  CD2 HIS A 165     6506   6205   7552   1148   1456    305       C  
ATOM    770  CE1 HIS A 165      29.731   7.254  56.224  1.00 56.85           C  
ANISOU  770  CE1 HIS A 165     6769   6780   8050   1291   1443    358       C  
ATOM    771  NE2 HIS A 165      30.841   7.467  56.907  1.00 52.31           N  
ANISOU  771  NE2 HIS A 165     6351   6093   7432   1249   1432    277       N  
ATOM    772  N   LEU A 166      31.112   0.769  55.917  1.00 35.53           N  
ANISOU  772  N   LEU A 166     4053   4182   5264    551   1243    632       N  
ATOM    773  CA  LEU A 166      31.867  -0.483  55.968  1.00 33.45           C  
ANISOU  773  CA  LEU A 166     3873   3870   4966    372   1157    653       C  
ATOM    774  C   LEU A 166      32.351  -0.887  54.580  1.00 30.81           C  
ANISOU  774  C   LEU A 166     3568   3441   4699    314   1042    694       C  
ATOM    775  O   LEU A 166      33.519  -1.273  54.400  1.00 33.57           O  
ANISOU  775  O   LEU A 166     4050   3649   5058    243    973    661       O  
ATOM    776  CB  LEU A 166      31.021  -1.596  56.586  1.00 33.91           C  
ANISOU  776  CB  LEU A 166     3833   4103   4949    244   1170    722       C  
ATOM    777  CG  LEU A 166      30.598  -1.406  58.044  1.00 44.61           C  
ANISOU  777  CG  LEU A 166     5169   5561   6220    268   1282    684       C  
ATOM    778  CD1 LEU A 166      29.775  -2.591  58.525  1.00 53.32           C  
ANISOU  778  CD1 LEU A 166     6175   6837   7249    121   1283    763       C  
ATOM    779  CD2 LEU A 166      31.819  -1.210  58.928  1.00 43.32           C  
ANISOU  779  CD2 LEU A 166     5181   5259   6020    261   1291    592       C  
ATOM    780  N   CYS A 167      31.470  -0.794  53.583  1.00 28.10           N  
ANISOU  780  N   CYS A 167     3101   3176   4402    345   1020    764       N  
ATOM    781  CA  CYS A 167      31.864  -1.133  52.218  1.00 33.93           C  
ANISOU  781  CA  CYS A 167     3864   3830   5197    292    913    804       C  
ATOM    782  C   CYS A 167      32.980  -0.219  51.716  1.00 24.18           C  
ANISOU  782  C   CYS A 167     2761   2405   4021    380    894    731       C  
ATOM    783  O   CYS A 167      33.922  -0.678  51.051  1.00 25.32           O  
ANISOU  783  O   CYS A 167     3003   2430   4190    301    811    723       O  
ATOM    784  CB  CYS A 167      30.649  -1.071  51.296  1.00 41.18           C  
ANISOU  784  CB  CYS A 167     4621   4876   6151    321    898    892       C  
ATOM    785  SG  CYS A 167      31.021  -1.456  49.576  1.00 52.61           S  
ANISOU  785  SG  CYS A 167     6094   6234   7660    255    770    944       S  
ATOM    786  N   ALA A 168      32.895   1.077  52.031  1.00 24.31           N  
ANISOU  786  N   ALA A 168     2786   2391   4061    541    972    675       N  
ATOM    787  CA  ALA A 168      33.922   2.022  51.608  1.00 28.07           C  
ANISOU  787  CA  ALA A 168     3388   2687   4588    624    958    606       C  
ATOM    788  C   ALA A 168      35.248   1.736  52.293  1.00 30.60           C  
ANISOU  788  C   ALA A 168     3861   2905   4859    541    931    522       C  
ATOM    789  O   ALA A 168      36.304   1.848  51.669  1.00 38.15           O  
ANISOU  789  O   ALA A 168     4895   3854   5747    457    808    445       O  
ATOM    790  CB  ALA A 168      33.476   3.454  51.894  1.00 27.41           C  
ANISOU  790  CB  ALA A 168     3285   2624   4506    785   1030    555       C  
ATOM    791  N   ILE A 169      35.214   1.375  53.575  1.00 36.13           N  
ANISOU  791  N   ILE A 169     4579   3640   5511    517    995    502       N  
ATOM    792  CA  ILE A 169      36.435   0.978  54.270  1.00 28.62           C  
ANISOU  792  CA  ILE A 169     3764   2593   4515    433    964    436       C  
ATOM    793  C   ILE A 169      37.084  -0.193  53.553  1.00 28.46           C  
ANISOU  793  C   ILE A 169     3762   2595   4458    273    820    445       C  
ATOM    794  O   ILE A 169      38.291  -0.187  53.277  1.00 21.32           O  
ANISOU  794  O   ILE A 169     2922   1709   3468    217    691    350       O  
ATOM    795  CB  ILE A 169      36.133   0.629  55.737  1.00 29.20           C  
ANISOU  795  CB  ILE A 169     3835   2747   4511    404   1037    421       C  
ATOM    796  CG1 ILE A 169      35.758   1.874  56.527  1.00 30.41           C  
ANISOU  796  CG1 ILE A 169     3983   2920   4649    555   1149    358       C  
ATOM    797  CG2 ILE A 169      37.323  -0.052  56.377  1.00 34.39           C  
ANISOU  797  CG2 ILE A 169     4626   3310   5132    296    989    379       C  
ATOM    798  CD1 ILE A 169      35.370   1.571  57.946  1.00 41.73           C  
ANISOU  798  CD1 ILE A 169     5404   4461   5991    523   1224    340       C  
ATOM    799  N   SER A 170      36.289  -1.220  53.246  1.00 28.89           N  
ANISOU  799  N   SER A 170     3744   2681   4552    195    824    563       N  
ATOM    800  CA  SER A 170      36.846  -2.387  52.567  1.00 30.17           C  
ANISOU  800  CA  SER A 170     3922   2897   4646     57    666    540       C  
ATOM    801  C   SER A 170      37.510  -1.990  51.254  1.00 30.06           C  
ANISOU  801  C   SER A 170     3928   2890   4604     76    551    471       C  
ATOM    802  O   SER A 170      38.700  -2.265  51.038  1.00 33.12           O  
ANISOU  802  O   SER A 170     4393   3296   4895     26    428    381       O  
ATOM    803  CB  SER A 170      35.754  -3.423  52.325  1.00 30.36           C  
ANISOU  803  CB  SER A 170     3844   3002   4688    -39    670    668       C  
ATOM    804  OG  SER A 170      35.137  -3.781  53.546  1.00 52.08           O  
ANISOU  804  OG  SER A 170     6554   5837   7396    -79    752    710       O  
ATOM    805  N   LEU A 171      36.762  -1.303  50.383  1.00 26.71           N  
ANISOU  805  N   LEU A 171     3433   2463   4253    149    589    523       N  
ATOM    806  CA  LEU A 171      37.303  -0.930  49.077  1.00 20.13           C  
ANISOU  806  CA  LEU A 171     2623   1646   3380    149    488    468       C  
ATOM    807  C   LEU A 171      38.529  -0.041  49.215  1.00 21.78           C  
ANISOU  807  C   LEU A 171     2921   1849   3506    173    434    353       C  
ATOM    808  O   LEU A 171      39.523  -0.227  48.503  1.00 13.27           O  
ANISOU  808  O   LEU A 171     1892    795   2357    125    333    298       O  
ATOM    809  CB  LEU A 171      36.239  -0.218  48.244  1.00 20.59           C  
ANISOU  809  CB  LEU A 171     2588   1703   3531    232    540    550       C  
ATOM    810  CG  LEU A 171      35.104  -1.074  47.696  1.00 29.85           C  
ANISOU  810  CG  LEU A 171     3651   2914   4776    189    544    688       C  
ATOM    811  CD1 LEU A 171      34.034  -0.196  47.087  1.00 44.56           C  
ANISOU  811  CD1 LEU A 171     5410   4786   6737    306    600    784       C  
ATOM    812  CD2 LEU A 171      35.651  -2.039  46.668  1.00 38.90           C  
ANISOU  812  CD2 LEU A 171     4840   4097   5843     72    409    645       C  
ATOM    813  N   ASP A 172      38.475   0.927  50.131  1.00 30.85           N  
ANISOU  813  N   ASP A 172     4081   2969   4671    251    517    329       N  
ATOM    814  CA  ASP A 172      39.557   1.888  50.287  1.00 27.57           C  
ANISOU  814  CA  ASP A 172     3736   2559   4182    266    454    238       C  
ATOM    815  C   ASP A 172      40.831   1.203  50.750  1.00 25.45           C  
ANISOU  815  C   ASP A 172     3513   2297   3860    192    407    194       C  
ATOM    816  O   ASP A 172      41.903   1.428  50.179  1.00 20.33           O  
ANISOU  816  O   ASP A 172     2884   1652   3190    172    373    160       O  
ATOM    817  CB  ASP A 172      39.134   2.975  51.273  1.00 28.65           C  
ANISOU  817  CB  ASP A 172     3875   2665   4345    360    561    226       C  
ATOM    818  CG  ASP A 172      40.161   4.063  51.412  1.00 42.33           C  
ANISOU  818  CG  ASP A 172     5664   4392   6026    372    516    153       C  
ATOM    819  OD1 ASP A 172      40.195   4.949  50.533  1.00 62.96           O  
ANISOU  819  OD1 ASP A 172     8273   6996   8653    406    506    151       O  
ATOM    820  OD2 ASP A 172      40.929   4.035  52.397  1.00 50.90           O  
ANISOU  820  OD2 ASP A 172     6793   5469   7077    349    525    114       O  
ATOM    821  N   ARG A 173      40.730   0.346  51.771  1.00 24.05           N  
ANISOU  821  N   ARG A 173     3350   2120   3666    153    411    202       N  
ATOM    822  CA  ARG A 173      41.910  -0.361  52.259  1.00 23.25           C  
ANISOU  822  CA  ARG A 173     3288   2026   3521     93    368    166       C  
ATOM    823  C   ARG A 173      42.475  -1.292  51.194  1.00 24.90           C  
ANISOU  823  C   ARG A 173     3487   2258   3715     34    293    172       C  
ATOM    824  O   ARG A 173      43.699  -1.409  51.047  1.00 30.73           O  
ANISOU  824  O   ARG A 173     4247   3003   4425     15    254    135       O  
ATOM    825  CB  ARG A 173      41.570  -1.136  53.528  1.00 23.42           C  
ANISOU  825  CB  ARG A 173     3329   2042   3528     57    380    182       C  
ATOM    826  CG  ARG A 173      41.332  -0.267  54.749  1.00 24.67           C  
ANISOU  826  CG  ARG A 173     3512   2166   3695    117    480    161       C  
ATOM    827  CD  ARG A 173      41.000  -1.126  55.957  1.00 33.79           C  
ANISOU  827  CD  ARG A 173     4694   3295   4851     73    553    189       C  
ATOM    828  NE  ARG A 173      42.062  -2.086  56.238  1.00 52.67           N  
ANISOU  828  NE  ARG A 173     7112   5721   7178    -11    412    165       N  
ATOM    829  CZ  ARG A 173      43.105  -1.832  57.019  1.00 63.70           C  
ANISOU  829  CZ  ARG A 173     8549   7114   8541     -9    392    113       C  
ATOM    830  NH1 ARG A 173      43.226  -0.641  57.595  1.00 64.53           N  
ANISOU  830  NH1 ARG A 173     8678   7199   8641     55    453     72       N  
ATOM    831  NH2 ARG A 173      44.029  -2.764  57.217  1.00 64.23           N  
ANISOU  831  NH2 ARG A 173     8631   7192   8581    -67    325    106       N  
ATOM    832  N   TYR A 174      41.598  -1.951  50.431  1.00 19.97           N  
ANISOU  832  N   TYR A 174     2832   1648   3107      7    274    221       N  
ATOM    833  CA  TYR A 174      42.067  -2.841  49.372  1.00 17.83           C  
ANISOU  833  CA  TYR A 174     2562   1398   2815    -44    207    223       C  
ATOM    834  C   TYR A 174      42.834  -2.060  48.309  1.00 31.24           C  
ANISOU  834  C   TYR A 174     4257   3097   4516    -13    198    191       C  
ATOM    835  O   TYR A 174      43.998  -2.368  48.004  1.00 39.28           O  
ANISOU  835  O   TYR A 174     5298   4124   5502    -35    157    158       O  
ATOM    836  CB  TYR A 174      40.873  -3.584  48.763  1.00 11.43           C  
ANISOU  836  CB  TYR A 174     1720    605   2017    -83    197    286       C  
ATOM    837  CG  TYR A 174      41.222  -4.517  47.633  1.00 18.90           C  
ANISOU  837  CG  TYR A 174     2673   1571   2936   -133    140    286       C  
ATOM    838  CD1 TYR A 174      41.904  -5.702  47.877  1.00 22.62           C  
ANISOU  838  CD1 TYR A 174     3189   2052   3356   -192     96    269       C  
ATOM    839  CD2 TYR A 174      40.860  -4.221  46.318  1.00 34.01           C  
ANISOU  839  CD2 TYR A 174     4555   3494   4874   -119    135    302       C  
ATOM    840  CE1 TYR A 174      42.227  -6.568  46.847  1.00 19.15           C  
ANISOU  840  CE1 TYR A 174     2761   1627   2888   -228     67    262       C  
ATOM    841  CE2 TYR A 174      41.179  -5.084  45.275  1.00 29.32           C  
ANISOU  841  CE2 TYR A 174     3970   2917   4254   -161     94    298       C  
ATOM    842  CZ  TYR A 174      41.862  -6.257  45.551  1.00 21.08           C  
ANISOU  842  CZ  TYR A 174     2969   1881   3160   -212     66    276       C  
ATOM    843  OH  TYR A 174      42.192  -7.126  44.536  1.00 22.57           O  
ANISOU  843  OH  TYR A 174     3161   2085   3331   -242     44    267       O  
ATOM    844  N   VAL A 175      42.206  -1.017  47.756  1.00 11.40           N  
ANISOU  844  N   VAL A 175     1719    575   2039     38    234    205       N  
ATOM    845  CA  VAL A 175      42.872  -0.213  46.737  1.00 22.01           C  
ANISOU  845  CA  VAL A 175     3065   1916   3382     59    223    181       C  
ATOM    846  C   VAL A 175      44.151   0.391  47.296  1.00 22.75           C  
ANISOU  846  C   VAL A 175     3193   2002   3449     68    226    130       C  
ATOM    847  O   VAL A 175      45.156   0.517  46.582  1.00 19.59           O  
ANISOU  847  O   VAL A 175     2805   1608   3029     55    196    108       O  
ATOM    848  CB  VAL A 175      41.912   0.869  46.201  1.00 22.02           C  
ANISOU  848  CB  VAL A 175     3040   1901   3425    117    259    208       C  
ATOM    849  CG1 VAL A 175      42.631   1.797  45.240  1.00 11.84           C  
ANISOU  849  CG1 VAL A 175     1766    603   2131    134    246    184       C  
ATOM    850  CG2 VAL A 175      40.729   0.231  45.516  1.00 11.88           C  
ANISOU  850  CG2 VAL A 175     1714    630   2169    103    247    268       C  
ATOM    851  N   ALA A 176      44.163   0.700  48.595  1.00 13.26           N  
ANISOU  851  N   ALA A 176     2009    787   2243     87    262    116       N  
ATOM    852  CA  ALA A 176      45.344   1.288  49.208  1.00 11.51           C  
ANISOU  852  CA  ALA A 176     1820    558   1997     92    265     74       C  
ATOM    853  C   ALA A 176      46.497   0.302  49.210  1.00 36.88           C  
ANISOU  853  C   ALA A 176     5045   3790   5177     43    210     56       C  
ATOM    854  O   ALA A 176      47.601   0.630  48.764  1.00 46.23           O  
ANISOU  854  O   ALA A 176     6239   4978   6347     39    188     34       O  
ATOM    855  CB  ALA A 176      45.018   1.744  50.627  1.00 11.90           C  
ANISOU  855  CB  ALA A 176     1890    587   2045    121    316     63       C  
ATOM    856  N   ILE A 177      46.248  -0.929  49.668  1.00 41.29           N  
ANISOU  856  N   ILE A 177     5604   4359   5727      7    184     71       N  
ATOM    857  CA  ILE A 177      47.329  -1.910  49.722  1.00 34.91           C  
ANISOU  857  CA  ILE A 177     4810   3564   4889    -33    126     58       C  
ATOM    858  C   ILE A 177      47.759  -2.325  48.318  1.00 40.85           C  
ANISOU  858  C   ILE A 177     5555   4333   5632    -50     85     61       C  
ATOM    859  O   ILE A 177      48.856  -2.868  48.143  1.00 51.28           O  
ANISOU  859  O   ILE A 177     6890   5663   6930    -70     43     46       O  
ATOM    860  CB  ILE A 177      46.949  -3.136  50.578  1.00 10.90           C  
ANISOU  860  CB  ILE A 177     1780    523   1838    -72    100     76       C  
ATOM    861  CG1 ILE A 177      45.899  -3.996  49.873  1.00 16.44           C  
ANISOU  861  CG1 ILE A 177     2471   1234   2542   -102     82    116       C  
ATOM    862  CG2 ILE A 177      46.477  -2.699  51.943  1.00 10.84           C  
ANISOU  862  CG2 ILE A 177     1784    498   1837    -55    150     74       C  
ATOM    863  CD1 ILE A 177      45.743  -5.363  50.473  1.00 10.51           C  
ANISOU  863  CD1 ILE A 177     1742    483   1767   -159     36    139       C  
ATOM    864  N   GLN A 178      46.923  -2.074  47.305  1.00 27.17           N  
ANISOU  864  N   GLN A 178     3803   2603   3916    -41     98     82       N  
ATOM    865  CA  GLN A 178      47.346  -2.324  45.920  1.00 26.81           C  
ANISOU  865  CA  GLN A 178     3757   2572   3860    -55     69     82       C  
ATOM    866  C   GLN A 178      48.413  -1.303  45.407  1.00 38.88           C  
ANISOU  866  C   GLN A 178     5289   4098   5387    -34     74     55       C  
ATOM    867  O   GLN A 178      48.743  -1.328  44.212  1.00 51.90           O  
ANISOU  867  O   GLN A 178     6937   5755   7029    -41     57     55       O  
ATOM    868  CB  GLN A 178      46.128  -2.292  44.994  1.00 17.56           C  
ANISOU  868  CB  GLN A 178     2561   1401   2712    -53     81    114       C  
ATOM    869  CG  GLN A 178      46.058  -3.442  44.009  1.00 11.78           C  
ANISOU  869  CG  GLN A 178     1835    685   1957    -93     48    128       C  
ATOM    870  CD  GLN A 178      45.648  -4.754  44.665  1.00 28.59           C  
ANISOU  870  CD  GLN A 178     3979   2819   4064   -135     35    144       C  
ATOM    871  OE1 GLN A 178      45.086  -4.771  45.771  1.00 11.67           O  
ANISOU  871  OE1 GLN A 178     1835    668   1932   -135     46    157       O  
ATOM    872  NE2 GLN A 178      45.924  -5.866  43.982  1.00 39.41           N  
ANISOU  872  NE2 GLN A 178     5365   4204   5407   -170     22    142       N  
ATOM    873  N   ASN A 179      48.974  -0.451  46.266  1.00 24.93           N  
ANISOU  873  N   ASN A 179     3530   2318   3623    -12     96     33       N  
ATOM    874  CA  ASN A 179      49.865   0.640  45.878  1.00 10.54           C  
ANISOU  874  CA  ASN A 179     1715    488   1802      6    105     12       C  
ATOM    875  C   ASN A 179      51.270   0.382  46.406  1.00 10.18           C  
ANISOU  875  C   ASN A 179     1684    449   1736     -9     81    -12       C  
ATOM    876  O   ASN A 179      51.439   0.244  47.627  1.00 23.58           O  
ANISOU  876  O   ASN A 179     3391   2140   3430     -9     86    -20       O  
ATOM    877  CB  ASN A 179      49.314   1.960  46.418  1.00 21.31           C  
ANISOU  877  CB  ASN A 179     3086   1826   3185     45    154     10       C  
ATOM    878  CG  ASN A 179      50.135   3.162  46.004  1.00 30.54           C  
ANISOU  878  CG  ASN A 179     4270   2979   4354     61    162     -8       C  
ATOM    879  OD1 ASN A 179      51.023   3.066  45.166  1.00 20.51           O  
ANISOU  879  OD1 ASN A 179     2999   1719   3074     43    135    -16       O  
ATOM    880  ND2 ASN A 179      49.836   4.313  46.601  1.00 48.83           N  
ANISOU  880  ND2 ASN A 179     6604   5267   6682     95    201    -15       N  
ATOM    881  N   PRO A 180      52.297   0.312  45.547  1.00 15.47           N  
ANISOU  881  N   PRO A 180     2354   1128   2395    -20     56    -21       N  
ATOM    882  CA  PRO A 180      53.616  -0.179  45.997  1.00 13.02           C  
ANISOU  882  CA  PRO A 180     2052    825   2070    -35     27    -38       C  
ATOM    883  C   PRO A 180      54.241   0.573  47.160  1.00 17.46           C  
ANISOU  883  C   PRO A 180     2626   1371   2637    -23     43    -57       C  
ATOM    884  O   PRO A 180      55.102  -0.004  47.833  1.00 18.27           O  
ANISOU  884  O   PRO A 180     2732   1475   2733    -35     15    -67       O  
ATOM    885  CB  PRO A 180      54.486  -0.037  44.740  1.00  9.75           C  
ANISOU  885  CB  PRO A 180     1637    418   1648    -41     14    -43       C  
ATOM    886  CG  PRO A 180      53.549  -0.130  43.636  1.00 14.37           C  
ANISOU  886  CG  PRO A 180     2215   1008   2236    -42     19    -25       C  
ATOM    887  CD  PRO A 180      52.295   0.567  44.097  1.00 12.04           C  
ANISOU  887  CD  PRO A 180     1914    698   1962    -21     51    -14       C  
ATOM    888  N   ILE A 181      53.876   1.828  47.417  1.00 23.22           N  
ANISOU  888  N   ILE A 181     3365   2082   3378      1     84    -63       N  
ATOM    889  CA  ILE A 181      54.473   2.525  48.554  1.00 27.84           C  
ANISOU  889  CA  ILE A 181     3969   2648   3961     10    100    -82       C  
ATOM    890  C   ILE A 181      53.436   2.734  49.645  1.00 25.45           C  
ANISOU  890  C   ILE A 181     3680   2331   3660     26    137    -79       C  
ATOM    891  O   ILE A 181      53.507   3.708  50.402  1.00 15.21           O  
ANISOU  891  O   ILE A 181     2408   1010   2361     45    169    -93       O  
ATOM    892  CB  ILE A 181      55.097   3.874  48.152  1.00 29.02           C  
ANISOU  892  CB  ILE A 181     4134   2779   4115     24    119    -96       C  
ATOM    893  CG1 ILE A 181      54.080   4.759  47.432  1.00 31.15           C  
ANISOU  893  CG1 ILE A 181     4406   3032   4397     48    149    -84       C  
ATOM    894  CG2 ILE A 181      56.310   3.661  47.309  1.00 10.81           C  
ANISOU  894  CG2 ILE A 181     1818    483   1805      7     87   -102       C  
ATOM    895  CD1 ILE A 181      54.495   6.213  47.396  1.00 36.12           C  
ANISOU  895  CD1 ILE A 181     5063   3630   5032     67    172    -98       C  
ATOM    896  N   HIS A 182      52.480   1.815  49.754  1.00 21.41           N  
ANISOU  896  N   HIS A 182     3155   1831   3150     19    133    -61       N  
ATOM    897  CA  HIS A 182      51.398   2.036  50.701  1.00 17.47           C  
ANISOU  897  CA  HIS A 182     2667   1317   2655     36    174    -56       C  
ATOM    898  C   HIS A 182      51.811   1.795  52.146  1.00 11.24           C  
ANISOU  898  C   HIS A 182     1901    519   1850     28    178    -70       C  
ATOM    899  O   HIS A 182      50.949   1.852  53.026  1.00 21.27           O  
ANISOU  899  O   HIS A 182     3186   1777   3119     40    214    -67       O  
ATOM    900  CB  HIS A 182      50.202   1.158  50.344  1.00 14.88           C  
ANISOU  900  CB  HIS A 182     2317   1000   2337     28    171    -28       C  
ATOM    901  CG  HIS A 182      50.435  -0.297  50.578  1.00 16.56           C  
ANISOU  901  CG  HIS A 182     2525   1230   2539     -8    123    -20       C  
ATOM    902  ND1 HIS A 182      50.963  -1.128  49.615  1.00 22.46           N  
ANISOU  902  ND1 HIS A 182     3260   1995   3279    -32     73    -14       N  
ATOM    903  CD2 HIS A 182      50.216  -1.072  51.667  1.00 22.61           C  
ANISOU  903  CD2 HIS A 182     3301   1993   3299    -25    117    -16       C  
ATOM    904  CE1 HIS A 182      51.059  -2.354  50.099  1.00 30.68           C  
ANISOU  904  CE1 HIS A 182     4303   3040   4312    -60     33     -6       C  
ATOM    905  NE2 HIS A 182      50.609  -2.348  51.342  1.00 30.33           N  
ANISOU  905  NE2 HIS A 182     4269   2984   4272    -58     56     -5       N  
ATOM    906  N   HIS A 183      53.085   1.529  52.421  1.00 11.12           N  
ANISOU  906  N   HIS A 183     1891    507   1826     10    143    -86       N  
ATOM    907  CA  HIS A 183      53.583   1.533  53.790  1.00 18.90           C  
ANISOU  907  CA  HIS A 183     2903   1479   2798      5    148   -102       C  
ATOM    908  C   HIS A 183      54.310   2.827  54.134  1.00 21.17           C  
ANISOU  908  C   HIS A 183     3219   1745   3079     22    172   -125       C  
ATOM    909  O   HIS A 183      54.960   2.905  55.179  1.00 30.04           O  
ANISOU  909  O   HIS A 183     4368   2856   4191     15    170   -141       O  
ATOM    910  CB  HIS A 183      54.484   0.321  54.030  1.00 14.04           C  
ANISOU  910  CB  HIS A 183     2273    876   2185    -25     92   -102       C  
ATOM    911  CG  HIS A 183      53.721  -0.944  54.263  1.00 34.59           C  
ANISOU  911  CG  HIS A 183     4863   3488   4792    -44     74    -81       C  
ATOM    912  ND1 HIS A 183      53.255  -1.311  55.508  1.00 34.33           N  
ANISOU  912  ND1 HIS A 183     4853   3444   4747    -53     91    -79       N  
ATOM    913  CD2 HIS A 183      53.311  -1.911  53.409  1.00 35.93           C  
ANISOU  913  CD2 HIS A 183     5005   3674   4973    -59     39    -60       C  
ATOM    914  CE1 HIS A 183      52.604  -2.455  55.413  1.00 27.92           C  
ANISOU  914  CE1 HIS A 183     4023   2640   3944    -75     67    -56       C  
ATOM    915  NE2 HIS A 183      52.620  -2.840  54.150  1.00 35.05           N  
ANISOU  915  NE2 HIS A 183     4895   3559   4864    -79     34    -44       N  
ATOM    916  N   SER A 184      54.205   3.841  53.279  1.00 12.63           N  
ANISOU  916  N   SER A 184     2137    655   2007     42    191   -126       N  
ATOM    917  CA  SER A 184      54.746   5.161  53.561  1.00 22.44           C  
ANISOU  917  CA  SER A 184     3411   1868   3245     60    215   -147       C  
ATOM    918  C   SER A 184      54.019   5.800  54.740  1.00 30.20           C  
ANISOU  918  C   SER A 184     4435   2824   4216     84    264   -156       C  
ATOM    919  O   SER A 184      52.899   5.424  55.094  1.00 38.28           O  
ANISOU  919  O   SER A 184     5455   3849   5239     94    290   -145       O  
ATOM    920  CB  SER A 184      54.630   6.055  52.322  1.00 29.85           C  
ANISOU  920  CB  SER A 184     4343   2800   4199     76    223   -142       C  
ATOM    921  OG  SER A 184      54.696   7.435  52.642  1.00 31.75           O  
ANISOU  921  OG  SER A 184     4622   3004   4438    102    255   -158       O  
ATOM    922  N   ARG A 185      54.667   6.798  55.336  1.00 35.19           N  
ANISOU  922  N   ARG A 185     5106   3428   4838     93    278   -179       N  
ATOM    923  CA  ARG A 185      54.126   7.516  56.482  1.00 30.51           C  
ANISOU  923  CA  ARG A 185     4561   2803   4229    118    325   -195       C  
ATOM    924  C   ARG A 185      53.308   8.744  56.096  1.00 14.53           C  
ANISOU  924  C   ARG A 185     2553    748   2218    164    367   -197       C  
ATOM    925  O   ARG A 185      52.947   9.529  56.974  1.00 21.95           O  
ANISOU  925  O   ARG A 185     3538   1655   3147    193    406   -214       O  
ATOM    926  CB  ARG A 185      55.262   7.936  57.421  1.00 44.72           C  
ANISOU  926  CB  ARG A 185     6401   4583   6009    105    316   -220       C  
ATOM    927  CG  ARG A 185      56.262   8.896  56.800  1.00 58.52           C  
ANISOU  927  CG  ARG A 185     8156   6312   7765    105    300   -233       C  
ATOM    928  CD  ARG A 185      57.452   9.129  57.726  1.00 69.73           C  
ANISOU  928  CD  ARG A 185     9610   7715   9168     85    284   -256       C  
ATOM    929  NE  ARG A 185      58.383  10.117  57.185  1.00 77.13           N  
ANISOU  929  NE  ARG A 185    10559   8630  10115     85    274   -269       N  
ATOM    930  CZ  ARG A 185      58.317  11.421  57.439  1.00 84.44           C  
ANISOU  930  CZ  ARG A 185    11535   9513  11036    108    304   -288       C  
ATOM    931  NH1 ARG A 185      57.364  11.898  58.230  1.00 84.52           N  
ANISOU  931  NH1 ARG A 185    11584   9497  11031    138    348   -297       N  
ATOM    932  NH2 ARG A 185      59.205  12.249  56.903  1.00 87.32           N  
ANISOU  932  NH2 ARG A 185    11910   9857  11411    102    291   -298       N  
ATOM    933  N   PHE A 186      53.004   8.935  54.821  1.00 36.18           N  
ANISOU  933  N   PHE A 186     5265   3498   4984    173    358   -180       N  
ATOM    934  CA  PHE A 186      52.294  10.128  54.360  1.00 37.13           C  
ANISOU  934  CA  PHE A 186     5402   3585   5122    219    389   -180       C  
ATOM    935  C   PHE A 186      50.896   9.706  53.923  1.00 43.85           C  
ANISOU  935  C   PHE A 186     6220   4447   5993    244    409   -155       C  
ATOM    936  O   PHE A 186      50.682   9.314  52.776  1.00 25.23           O  
ANISOU  936  O   PHE A 186     3824   2111   3653    234    386   -133       O  
ATOM    937  CB  PHE A 186      53.050  10.826  53.232  1.00 30.55           C  
ANISOU  937  CB  PHE A 186     4566   2742   4301    213    364   -181       C  
ATOM    938  CG  PHE A 186      54.452  11.215  53.598  1.00 32.73           C  
ANISOU  938  CG  PHE A 186     4868   3006   4562    188    345   -204       C  
ATOM    939  CD1 PHE A 186      54.689  12.284  54.450  1.00 38.30           C  
ANISOU  939  CD1 PHE A 186     5628   3667   5256    209    369   -229       C  
ATOM    940  CD2 PHE A 186      55.535  10.510  53.097  1.00 37.37           C  
ANISOU  940  CD2 PHE A 186     5427   3623   5147    147    301   -200       C  
ATOM    941  CE1 PHE A 186      55.985  12.646  54.796  1.00 30.35           C  
ANISOU  941  CE1 PHE A 186     4648   2648   4238    184    350   -249       C  
ATOM    942  CE2 PHE A 186      56.833  10.866  53.437  1.00 45.80           C  
ANISOU  942  CE2 PHE A 186     6516   4680   6207    126    283   -220       C  
ATOM    943  CZ  PHE A 186      57.057  11.939  54.289  1.00 28.45           C  
ANISOU  943  CZ  PHE A 186     4373   2439   3999    143    307   -244       C  
ATOM    944  N   ASN A 187      49.948   9.788  54.855  1.00 68.89           N  
ANISOU  944  N   ASN A 187     9408   7606   9163    277    452   -159       N  
ATOM    945  CA  ASN A 187      48.549   9.471  54.602  1.00 84.02           C  
ANISOU  945  CA  ASN A 187    11294   9530  11101    310    478   -136       C  
ATOM    946  C   ASN A 187      47.716  10.722  54.847  1.00 90.14           C  
ANISOU  946  C   ASN A 187    12094  10262  11891    383    524   -148       C  
ATOM    947  O   ASN A 187      47.797  11.323  55.924  1.00 89.05           O  
ANISOU  947  O   ASN A 187    12001  10099  11737    407    555   -176       O  
ATOM    948  CB  ASN A 187      48.075   8.317  55.493  1.00 89.44           C  
ANISOU  948  CB  ASN A 187    11969  10239  11774    290    491   -129       C  
ATOM    949  CG  ASN A 187      48.918   7.055  55.319  1.00 91.90           C  
ANISOU  949  CG  ASN A 187    12259  10587  12071    224    440   -120       C  
ATOM    950  OD1 ASN A 187      49.417   6.492  56.293  1.00 95.56           O  
ANISOU  950  OD1 ASN A 187    12743  11057  12510    196    433   -132       O  
ATOM    951  ND2 ASN A 187      49.078   6.610  54.077  1.00 86.57           N  
ANISOU  951  ND2 ASN A 187    11545   9936  11412    203    401   -101       N  
ATOM    952  N   SER A 188      46.921  11.109  53.850  1.00 89.29           N  
ANISOU  952  N   SER A 188    11960  10149  11817    421    525   -127       N  
ATOM    953  CA  SER A 188      46.182  12.367  53.895  1.00 78.67           C  
ANISOU  953  CA  SER A 188    10635   8763  10492    500    560   -139       C  
ATOM    954  C   SER A 188      44.926  12.224  54.748  1.00 87.31           C  
ANISOU  954  C   SER A 188    11717   9860  11595    558    612   -140       C  
ATOM    955  O   SER A 188      44.072  11.371  54.478  1.00 93.30           O  
ANISOU  955  O   SER A 188    12428  10652  12371    560    616   -110       O  
ATOM    956  CB  SER A 188      45.814  12.820  52.485  1.00 65.69           C  
ANISOU  956  CB  SER A 188     8966   7110   8882    523    537   -115       C  
ATOM    957  OG  SER A 188      44.989  13.970  52.532  1.00 57.10           O  
ANISOU  957  OG  SER A 188     7894   5983   7819    608    567   -124       O  
ATOM    958  N   ARG A 189      44.813  13.071  55.771  1.00 81.26           N  
ANISOU  958  N   ARG A 189    10994   9063  10817    608    652   -176       N  
ATOM    959  CA  ARG A 189      43.641  13.072  56.639  1.00 79.88           C  
ANISOU  959  CA  ARG A 189    10808   8895  10649    676    708   -188       C  
ATOM    960  C   ARG A 189      42.438  13.725  55.962  1.00 82.11           C  
ANISOU  960  C   ARG A 189    11051   9173  10975    766    727   -176       C  
ATOM    961  O   ARG A 189      41.303  13.261  56.123  1.00 87.19           O  
ANISOU  961  O   ARG A 189    11643   9850  11635    813    758   -162       O  
ATOM    962  CB  ARG A 189      43.979  13.763  57.963  1.00 79.38           C  
ANISOU  962  CB  ARG A 189    10805   8802  10553    699    745   -239       C  
ATOM    963  CG  ARG A 189      42.783  14.258  58.755  1.00 80.55           C  
ANISOU  963  CG  ARG A 189    10945   8950  10709    796    809   -267       C  
ATOM    964  CD  ARG A 189      43.220  15.025  59.995  1.00 86.32           C  
ANISOU  964  CD  ARG A 189    11745   9648  11406    816    842   -323       C  
ATOM    965  NE  ARG A 189      42.121  15.788  60.581  1.00 99.81           N  
ANISOU  965  NE  ARG A 189    13444  11353  13124    924    904   -362       N  
ATOM    966  CZ  ARG A 189      42.136  16.304  61.806  1.00 99.30           C  
ANISOU  966  CZ  ARG A 189    13428  11274  13028    957    950   -417       C  
ATOM    967  NH1 ARG A 189      43.194  16.132  62.589  1.00 90.35           N  
ANISOU  967  NH1 ARG A 189    12358  10122  11850    887    938   -435       N  
ATOM    968  NH2 ARG A 189      41.087  16.985  62.253  1.00102.14           N  
ANISOU  968  NH2 ARG A 189    13768  11642  13398   1062   1009   -456       N  
ATOM    969  N   THR A 190      42.670  14.798  55.200  1.00 75.62           N  
ANISOU  969  N   THR A 190    10249   8312  10172    795    707   -180       N  
ATOM    970  CA  THR A 190      41.573  15.533  54.574  1.00 71.12           C  
ANISOU  970  CA  THR A 190     9646   7731   9646    888    720   -170       C  
ATOM    971  C   THR A 190      40.812  14.678  53.566  1.00 63.35           C  
ANISOU  971  C   THR A 190     8590   6789   8691    882    698   -118       C  
ATOM    972  O   THR A 190      39.576  14.747  53.489  1.00 73.59           O  
ANISOU  972  O   THR A 190     9834   8109  10019    963    725   -105       O  
ATOM    973  CB  THR A 190      42.120  16.790  53.897  1.00 81.40           C  
ANISOU  973  CB  THR A 190    10991   8976  10961    906    694   -182       C  
ATOM    974  OG1 THR A 190      42.717  17.640  54.885  1.00 95.59           O  
ANISOU  974  OG1 THR A 190    12855  10731  12734    920    718   -232       O  
ATOM    975  CG2 THR A 190      41.010  17.552  53.179  1.00 80.49           C  
ANISOU  975  CG2 THR A 190    10842   8845  10894   1004    699   -170       C  
ATOM    976  N   LYS A 191      41.528  13.861  52.788  1.00 59.11           N  
ANISOU  976  N   LYS A 191     8046   6268   8144    791    650    -88       N  
ATOM    977  CA  LYS A 191      40.869  13.021  51.789  1.00 61.22           C  
ANISOU  977  CA  LYS A 191     8251   6572   8437    778    626    -38       C  
ATOM    978  C   LYS A 191      39.902  12.032  52.432  1.00 59.82           C  
ANISOU  978  C   LYS A 191     8021   6442   8265    795    661    -21       C  
ATOM    979  O   LYS A 191      38.847  11.725  51.861  1.00 52.14           O  
ANISOU  979  O   LYS A 191     6986   5499   7326    836    663     16       O  
ATOM    980  CB  LYS A 191      41.914  12.287  50.951  1.00 67.34           C  
ANISOU  980  CB  LYS A 191     9033   7359   9196    675    572    -21       C  
ATOM    981  CG  LYS A 191      41.359  11.704  49.663  1.00 69.15           C  
ANISOU  981  CG  LYS A 191     9212   7612   9452    662    539     27       C  
ATOM    982  CD  LYS A 191      40.442  12.688  48.955  1.00 65.55           C  
ANISOU  982  CD  LYS A 191     8737   7132   9035    750    540     42       C  
ATOM    983  CE  LYS A 191      39.819  12.058  47.722  1.00 77.05           C  
ANISOU  983  CE  LYS A 191    10142   8615  10517    738    506     94       C  
ATOM    984  NZ  LYS A 191      38.775  12.929  47.118  1.00 90.09           N  
ANISOU  984  NZ  LYS A 191    11767  10252  12212    834    507    115       N  
ATOM    985  N   ALA A 192      40.241  11.526  53.620  1.00 71.60           N  
ANISOU  985  N   ALA A 192     9536   7944   9724    764    688    -46       N  
ATOM    986  CA  ALA A 192      39.330  10.627  54.323  1.00 74.45           C  
ANISOU  986  CA  ALA A 192     9850   8349  10088    784    727    -35       C  
ATOM    987  C   ALA A 192      38.036  11.339  54.696  1.00 78.39           C  
ANISOU  987  C   ALA A 192    10302   8870  10612    906    782    -49       C  
ATOM    988  O   ALA A 192      36.941  10.790  54.520  1.00 70.59           O  
ANISOU  988  O   ALA A 192     9241   7923   9655    953    835     -2       O  
ATOM    989  CB  ALA A 192      40.009  10.067  55.572  1.00 73.98           C  
ANISOU  989  CB  ALA A 192     9834   8289   9984    730    745    -65       C  
ATOM    990  N   PHE A 193      38.145  12.567  55.210  1.00 77.64           N  
ANISOU  990  N   PHE A 193    10247   8741  10510    968    808    -96       N  
ATOM    991  CA  PHE A 193      36.952  13.341  55.532  1.00 70.49           C  
ANISOU  991  CA  PHE A 193     9293   7862   9630   1092    860   -117       C  
ATOM    992  C   PHE A 193      36.115  13.600  54.285  1.00 61.39           C  
ANISOU  992  C   PHE A 193     8074   6724   8528   1147    835    -74       C  
ATOM    993  O   PHE A 193      34.880  13.523  54.328  1.00 69.65           O  
ANISOU  993  O   PHE A 193     9038   7822   9603   1236    901    -46       O  
ATOM    994  CB  PHE A 193      37.352  14.656  56.205  1.00 77.16           C  
ANISOU  994  CB  PHE A 193    10204   8652  10460   1141    884   -177       C  
ATOM    995  CG  PHE A 193      37.873  14.492  57.613  1.00 84.31           C  
ANISOU  995  CG  PHE A 193    11162   9555  11316   1113    922   -225       C  
ATOM    996  CD1 PHE A 193      37.791  13.272  58.267  1.00 89.90           C  
ANISOU  996  CD1 PHE A 193    11848  10314  11998   1063    941   -218       C  
ATOM    997  CD2 PHE A 193      38.446  15.564  58.282  1.00 83.51           C  
ANISOU  997  CD2 PHE A 193    11135   9399  11194   1135    938   -278       C  
ATOM    998  CE1 PHE A 193      38.272  13.125  59.563  1.00 90.54           C  
ANISOU  998  CE1 PHE A 193    11981  10391  12029   1036    974   -263       C  
ATOM    999  CE2 PHE A 193      38.927  15.424  59.575  1.00 84.03           C  
ANISOU  999  CE2 PHE A 193    11252   9463  11212   1108    971   -322       C  
ATOM   1000  CZ  PHE A 193      38.840  14.202  60.216  1.00 81.82           C  
ANISOU 1000  CZ  PHE A 193    10950   9234  10903   1058    988   -315       C  
ATOM   1001  N   LEU A 194      36.772  13.883  53.156  1.00 45.82           N  
ANISOU 1001  N   LEU A 194     6138   4704   6568   1101    775    -47       N  
ATOM   1002  CA  LEU A 194      36.041  14.098  51.909  1.00 46.61           C  
ANISOU 1002  CA  LEU A 194     6183   4814   6713   1145    743     -3       C  
ATOM   1003  C   LEU A 194      35.282  12.843  51.494  1.00 56.58           C  
ANISOU 1003  C   LEU A 194     7360   6146   7991   1125    736     52       C  
ATOM   1004  O   LEU A 194      34.109  12.909  51.104  1.00 65.33           O  
ANISOU 1004  O   LEU A 194     8386   7292   9143   1211    781    101       O  
ATOM   1005  CB  LEU A 194      37.008  14.516  50.804  1.00 50.19           C  
ANISOU 1005  CB  LEU A 194     6695   5208   7166   1085    681     11       C  
ATOM   1006  CG  LEU A 194      37.769  15.825  50.996  1.00 43.90           C  
ANISOU 1006  CG  LEU A 194     5977   4342   6361   1104    679    -35       C  
ATOM   1007  CD1 LEU A 194      38.697  16.058  49.806  1.00 28.03           C  
ANISOU 1007  CD1 LEU A 194     4008   2293   4350   1037    618    -17       C  
ATOM   1008  CD2 LEU A 194      36.803  16.989  51.192  1.00 46.64           C  
ANISOU 1008  CD2 LEU A 194     6303   4674   6744   1235    711    -57       C  
ATOM   1009  N   LYS A 195      35.942  11.683  51.572  1.00 54.33           N  
ANISOU 1009  N   LYS A 195     7095   5867   7681   1020    722     72       N  
ATOM   1010  CA  LYS A 195      35.272  10.428  51.242  1.00 56.79           C  
ANISOU 1010  CA  LYS A 195     7335   6219   8025   1002    772    156       C  
ATOM   1011  C   LYS A 195      34.089  10.171  52.169  1.00 59.39           C  
ANISOU 1011  C   LYS A 195     7581   6605   8381   1095    901    190       C  
ATOM   1012  O   LYS A 195      33.034   9.698  51.726  1.00 53.49           O  
ANISOU 1012  O   LYS A 195     6726   5916   7681   1142    946    269       O  
ATOM   1013  CB  LYS A 195      36.270   9.270  51.297  1.00 51.39           C  
ANISOU 1013  CB  LYS A 195     6693   5522   7309    872    733    159       C  
ATOM   1014  CG  LYS A 195      37.318   9.335  50.194  1.00 53.95           C  
ANISOU 1014  CG  LYS A 195     7068   5823   7609    784    617    142       C  
ATOM   1015  CD  LYS A 195      38.429   8.316  50.375  1.00 38.39           C  
ANISOU 1015  CD  LYS A 195     5137   3846   5602    667    589    135       C  
ATOM   1016  CE  LYS A 195      39.492   8.500  49.304  1.00 38.16           C  
ANISOU 1016  CE  LYS A 195     5145   3795   5560    602    534    130       C  
ATOM   1017  NZ  LYS A 195      40.689   7.662  49.558  1.00 47.14           N  
ANISOU 1017  NZ  LYS A 195     6314   4939   6659    504    508    110       N  
ATOM   1018  N   ILE A 196      34.238  10.498  53.456  1.00 55.79           N  
ANISOU 1018  N   ILE A 196     7163   6148   7889   1123    959    132       N  
ATOM   1019  CA  ILE A 196      33.146  10.295  54.404  1.00 47.43           C  
ANISOU 1019  CA  ILE A 196     6021   5163   6836   1211   1084    150       C  
ATOM   1020  C   ILE A 196      31.960  11.181  54.048  1.00 47.86           C  
ANISOU 1020  C   ILE A 196     5984   5273   6927   1339   1108    161       C  
ATOM   1021  O   ILE A 196      30.801  10.744  54.087  1.00 52.42           O  
ANISOU 1021  O   ILE A 196     6434   5951   7533   1401   1180    222       O  
ATOM   1022  CB  ILE A 196      33.636  10.542  55.843  1.00 49.38           C  
ANISOU 1022  CB  ILE A 196     6341   5394   7026   1210   1134     73       C  
ATOM   1023  CG1 ILE A 196      34.644   9.462  56.248  1.00 44.81           C  
ANISOU 1023  CG1 ILE A 196     5832   4776   6417   1087   1120     76       C  
ATOM   1024  CG2 ILE A 196      32.463  10.575  56.814  1.00 51.50           C  
ANISOU 1024  CG2 ILE A 196     6522   5759   7288   1311   1260     72       C  
ATOM   1025  CD1 ILE A 196      35.246   9.659  57.622  1.00 45.94           C  
ANISOU 1025  CD1 ILE A 196     6058   4899   6500   1071   1156      4       C  
ATOM   1026  N   ILE A 197      32.230  12.438  53.690  1.00 57.42           N  
ANISOU 1026  N   ILE A 197     7249   6428   8138   1377   1044    105       N  
ATOM   1027  CA  ILE A 197      31.149  13.341  53.294  1.00 73.81           C  
ANISOU 1027  CA  ILE A 197     9248   8542  10256   1500   1057    111       C  
ATOM   1028  C   ILE A 197      30.464  12.834  52.028  1.00 68.43           C  
ANISOU 1028  C   ILE A 197     8472   7903   9625   1504   1027    206       C  
ATOM   1029  O   ILE A 197      29.236  12.917  51.889  1.00 67.98           O  
ANISOU 1029  O   ILE A 197     8292   7934   9604   1597   1073    251       O  
ATOM   1030  CB  ILE A 197      31.686  14.775  53.121  1.00 70.35           C  
ANISOU 1030  CB  ILE A 197     8895   8020   9815   1529    987     32       C  
ATOM   1031  CG1 ILE A 197      32.182  15.324  54.462  1.00 67.48           C  
ANISOU 1031  CG1 ILE A 197     8602   7629   9407   1539   1026    -56       C  
ATOM   1032  CG2 ILE A 197      30.616  15.686  52.542  1.00 67.29           C  
ANISOU 1032  CG2 ILE A 197     8432   7656   9480   1652    987     43       C  
ATOM   1033  CD1 ILE A 197      32.807  16.703  54.365  1.00 65.10           C  
ANISOU 1033  CD1 ILE A 197     8380   7245   9110   1556    955   -131       C  
ATOM   1034  N   ALA A 198      31.239  12.275  51.097  1.00 67.00           N  
ANISOU 1034  N   ALA A 198     8341   7671   9445   1399    947    238       N  
ATOM   1035  CA  ALA A 198      30.643  11.734  49.878  1.00 79.30           C  
ANISOU 1035  CA  ALA A 198     9814   9266  11050   1392    914    332       C  
ATOM   1036  C   ALA A 198      29.753  10.530  50.178  1.00 74.56           C  
ANISOU 1036  C   ALA A 198     9080   8773  10476   1395    994    421       C  
ATOM   1037  O   ALA A 198      28.688  10.366  49.564  1.00 85.27           O  
ANISOU 1037  O   ALA A 198    10307  10214  11876   1446   1000    500       O  
ATOM   1038  CB  ALA A 198      31.738  11.358  48.880  1.00 87.83           C  
ANISOU 1038  CB  ALA A 198    10983  10273  12117   1269    814    335       C  
ATOM   1039  N   VAL A 199      30.173   9.675  51.114  1.00 63.77           N  
ANISOU 1039  N   VAL A 199     7733   7413   9081   1336   1049    414       N  
ATOM   1040  CA  VAL A 199      29.342   8.534  51.492  1.00 52.36           C  
ANISOU 1040  CA  VAL A 199     6150   6086   7658   1332   1127    498       C  
ATOM   1041  C   VAL A 199      28.057   9.007  52.167  1.00 54.27           C  
ANISOU 1041  C   VAL A 199     6265   6460   7896   1449   1211    497       C  
ATOM   1042  O   VAL A 199      26.971   8.466  51.917  1.00 37.83           O  
ANISOU 1042  O   VAL A 199     4019   4515   5840   1468   1238    582       O  
ATOM   1043  CB  VAL A 199      30.130   7.561  52.386  1.00 45.77           C  
ANISOU 1043  CB  VAL A 199     5376   5222   6794   1242   1170    483       C  
ATOM   1044  CG1 VAL A 199      29.211   6.465  52.902  1.00 40.52           C  
ANISOU 1044  CG1 VAL A 199     4551   4706   6140   1235   1258    564       C  
ATOM   1045  CG2 VAL A 199      31.283   6.954  51.603  1.00 41.76           C  
ANISOU 1045  CG2 VAL A 199     4969   4602   6297   1120   1079    492       C  
ATOM   1046  N   TRP A 200      28.155  10.018  53.032  1.00 52.75           N  
ANISOU 1046  N   TRP A 200     6138   6239   7666   1518   1245    399       N  
ATOM   1047  CA  TRP A 200      26.946  10.579  53.629  1.00 50.96           C  
ANISOU 1047  CA  TRP A 200     5796   6131   7436   1633   1319    385       C  
ATOM   1048  C   TRP A 200      26.011  11.130  52.559  1.00 59.24           C  
ANISOU 1048  C   TRP A 200     6744   7223   8539   1710   1273    434       C  
ATOM   1049  O   TRP A 200      24.787  10.955  52.638  1.00 60.27           O  
ANISOU 1049  O   TRP A 200     6713   7500   8685   1767   1320    483       O  
ATOM   1050  CB  TRP A 200      27.313  11.658  54.644  1.00 44.81           C  
ANISOU 1050  CB  TRP A 200     5118   5291   6616   1692   1351    266       C  
ATOM   1051  CG  TRP A 200      27.651  11.100  55.989  1.00 47.63           C  
ANISOU 1051  CG  TRP A 200     5509   5676   6911   1649   1435    225       C  
ATOM   1052  CD1 TRP A 200      28.889  11.008  56.551  1.00 52.94           C  
ANISOU 1052  CD1 TRP A 200     6332   6241   7542   1573   1419    168       C  
ATOM   1053  CD2 TRP A 200      26.734  10.541  56.940  1.00 42.54           C  
ANISOU 1053  CD2 TRP A 200     4742   5188   6233   1671   1545    239       C  
ATOM   1054  NE1 TRP A 200      28.801  10.430  57.798  1.00 56.18           N  
ANISOU 1054  NE1 TRP A 200     6730   6720   7897   1553   1514    146       N  
ATOM   1055  CE2 TRP A 200      27.489  10.135  58.059  1.00 48.33           C  
ANISOU 1055  CE2 TRP A 200     5569   5891   6902   1608   1595    187       C  
ATOM   1056  CE3 TRP A 200      25.350  10.345  56.952  1.00 40.89           C  
ANISOU 1056  CE3 TRP A 200     4350   5151   6036   1727   1600    290       C  
ATOM   1057  CZ2 TRP A 200      26.906   9.547  59.181  1.00 51.20           C  
ANISOU 1057  CZ2 TRP A 200     5855   6392   7207   1597   1703    183       C  
ATOM   1058  CZ3 TRP A 200      24.771   9.762  58.070  1.00 50.06           C  
ANISOU 1058  CZ3 TRP A 200     5425   6455   7139   1709   1704    284       C  
ATOM   1059  CH2 TRP A 200      25.550   9.369  59.168  1.00 51.84           C  
ANISOU 1059  CH2 TRP A 200     5754   6648   7295   1643   1756    231       C  
ATOM   1060  N   THR A 201      26.573  11.783  51.538  1.00 66.58           N  
ANISOU 1060  N   THR A 201     7765   8036   9495   1705   1177    424       N  
ATOM   1061  CA  THR A 201      25.748  12.327  50.463  1.00 79.82           C  
ANISOU 1061  CA  THR A 201     9360   9743  11224   1775   1126    471       C  
ATOM   1062  C   THR A 201      25.038  11.220  49.691  1.00 80.99           C  
ANISOU 1062  C   THR A 201     9365  10002  11405   1730   1111    597       C  
ATOM   1063  O   THR A 201      23.840  11.329  49.395  1.00 90.42           O  
ANISOU 1063  O   THR A 201    10413  11314  12631   1799   1121    650       O  
ATOM   1064  CB  THR A 201      26.604  13.173  49.517  1.00 79.98           C  
ANISOU 1064  CB  THR A 201     9516   9619  11255   1757   1023    433       C  
ATOM   1065  OG1 THR A 201      27.092  14.327  50.214  1.00 83.41           O  
ANISOU 1065  OG1 THR A 201    10056   9972  11665   1806   1028    323       O  
ATOM   1066  CG2 THR A 201      25.791  13.619  48.312  1.00 72.92           C  
ANISOU 1066  CG2 THR A 201     8543   8751  10413   1819    964    493       C  
ATOM   1067  N   ILE A 202      25.754  10.144  49.357  1.00 74.85           N  
ANISOU 1067  N   ILE A 202     8623   9192  10625   1608   1082    646       N  
ATOM   1068  CA  ILE A 202      25.095   9.072  48.615  1.00 75.77           C  
ANISOU 1068  CA  ILE A 202     8598   9416  10775   1553   1059    770       C  
ATOM   1069  C   ILE A 202      24.061   8.373  49.493  1.00 76.06           C  
ANISOU 1069  C   ILE A 202     8466   9639  10796   1560   1145    813       C  
ATOM   1070  O   ILE A 202      23.030   7.907  48.993  1.00 90.64           O  
ANISOU 1070  O   ILE A 202    10151  11625  12665   1553   1129    905       O  
ATOM   1071  CB  ILE A 202      26.117   8.078  48.026  1.00 73.34           C  
ANISOU 1071  CB  ILE A 202     8366   9024  10477   1418   1002    811       C  
ATOM   1072  CG1 ILE A 202      25.432   7.124  47.043  1.00 68.56           C  
ANISOU 1072  CG1 ILE A 202     7618   8519   9914   1357    952    942       C  
ATOM   1073  CG2 ILE A 202      26.778   7.260  49.110  1.00 79.56           C  
ANISOU 1073  CG2 ILE A 202     9197   9800  11232   1348   1065    784       C  
ATOM   1074  CD1 ILE A 202      24.708   7.818  45.905  1.00 67.40           C  
ANISOU 1074  CD1 ILE A 202     7416   8394   9798   1419    885    982       C  
ATOM   1075  N   SER A 203      24.283   8.319  50.809  1.00 58.09           N  
ANISOU 1075  N   SER A 203     6222   7377   8471   1565   1232    746       N  
ATOM   1076  CA  SER A 203      23.260   7.760  51.686  1.00 49.04           C  
ANISOU 1076  CA  SER A 203     4918   6420   7293   1566   1317    774       C  
ATOM   1077  C   SER A 203      22.004   8.621  51.679  1.00 59.17           C  
ANISOU 1077  C   SER A 203     6084   7808   8591   1688   1339    764       C  
ATOM   1078  O   SER A 203      20.882   8.098  51.621  1.00 59.12           O  
ANISOU 1078  O   SER A 203     5901   7977   8584   1675   1354    835       O  
ATOM   1079  CB  SER A 203      23.801   7.615  53.107  1.00 56.04           C  
ANISOU 1079  CB  SER A 203     5881   7294   8117   1546   1408    694       C  
ATOM   1080  OG  SER A 203      24.926   6.758  53.141  1.00 65.63           O  
ANISOU 1080  OG  SER A 203     7196   8417   9323   1433   1390    705       O  
ATOM   1081  N   VAL A 204      22.174   9.945  51.737  1.00 63.35           N  
ANISOU 1081  N   VAL A 204     6705   8232   9131   1800   1334    675       N  
ATOM   1082  CA  VAL A 204      21.025  10.845  51.675  1.00 61.01           C  
ANISOU 1082  CA  VAL A 204     6303   8014   8863   1926   1350    661       C  
ATOM   1083  C   VAL A 204      20.284  10.669  50.356  1.00 67.13           C  
ANISOU 1083  C   VAL A 204     6965   8850   9692   1927   1270    765       C  
ATOM   1084  O   VAL A 204      19.047  10.666  50.314  1.00 83.88           O  
ANISOU 1084  O   VAL A 204     8919  11122  11829   1976   1289    807       O  
ATOM   1085  CB  VAL A 204      21.476  12.302  51.883  1.00 54.11           C  
ANISOU 1085  CB  VAL A 204     5565   6996   7997   2031   1344    548       C  
ATOM   1086  CG1 VAL A 204      20.324  13.259  51.628  1.00 50.97           C  
ANISOU 1086  CG1 VAL A 204     5061   6661   7646   2166   1346    540       C  
ATOM   1087  CG2 VAL A 204      22.024  12.489  53.288  1.00 59.27           C  
ANISOU 1087  CG2 VAL A 204     6309   7617   8592   2033   1427    447       C  
ATOM   1088  N   GLY A 205      21.028  10.517  49.260  1.00 66.14           N  
ANISOU 1088  N   GLY A 205     6926   8611   9592   1867   1177    806       N  
ATOM   1089  CA  GLY A 205      20.395  10.294  47.971  1.00 63.33           C  
ANISOU 1089  CA  GLY A 205     6473   8308   9282   1854   1095    908       C  
ATOM   1090  C   GLY A 205      19.650   8.976  47.890  1.00 73.39           C  
ANISOU 1090  C   GLY A 205     7577   9760  10546   1756   1098   1017       C  
ATOM   1091  O   GLY A 205      18.615   8.884  47.223  1.00 82.78           O  
ANISOU 1091  O   GLY A 205     8625  11065  11762   1770   1059   1093       O  
ATOM   1092  N   ILE A 206      20.163   7.940  48.556  1.00 72.51           N  
ANISOU 1092  N   ILE A 206     7481   9676  10396   1646   1137   1027       N  
ATOM   1093  CA  ILE A 206      19.471   6.655  48.583  1.00 70.84           C  
ANISOU 1093  CA  ILE A 206     7112   9641  10163   1528   1136   1125       C  
ATOM   1094  C   ILE A 206      18.204   6.747  49.424  1.00 62.16           C  
ANISOU 1094  C   ILE A 206     5857   8727   9035   1579   1213   1115       C  
ATOM   1095  O   ILE A 206      17.184   6.123  49.106  1.00 58.12           O  
ANISOU 1095  O   ILE A 206     5185   8379   8520   1523   1189   1198       O  
ATOM   1096  CB  ILE A 206      20.415   5.552  49.100  1.00 77.01           C  
ANISOU 1096  CB  ILE A 206     7961  10392  10909   1390   1154   1133       C  
ATOM   1097  CG1 ILE A 206      21.534   5.286  48.097  1.00 81.45           C  
ANISOU 1097  CG1 ILE A 206     8646  10792  11510   1324   1066   1161       C  
ATOM   1098  CG2 ILE A 206      19.658   4.262  49.380  1.00 71.54           C  
ANISOU 1098  CG2 ILE A 206     7115   9893  10174   1253   1161   1216       C  
ATOM   1099  CD1 ILE A 206      22.538   4.269  48.580  1.00 81.25           C  
ANISOU 1099  CD1 ILE A 206     8694  10716  11464   1197   1082   1161       C  
ATOM   1100  N   SER A 207      18.242   7.522  50.506  1.00 67.41           N  
ANISOU 1100  N   SER A 207     6568   9368   9677   1677   1304   1010       N  
ATOM   1101  CA  SER A 207      17.122   7.548  51.440  1.00 78.82           C  
ANISOU 1101  CA  SER A 207     7872  10986  11089   1716   1390    989       C  
ATOM   1102  C   SER A 207      16.020   8.528  51.050  1.00 82.77           C  
ANISOU 1102  C   SER A 207     8268  11542  11638   1854   1383    983       C  
ATOM   1103  O   SER A 207      14.862   8.311  51.422  1.00 86.95           O  
ANISOU 1103  O   SER A 207     8634  12248  12156   1861   1426   1006       O  
ATOM   1104  CB  SER A 207      17.619   7.875  52.851  1.00 77.23           C  
ANISOU 1104  CB  SER A 207     7761  10747  10835   1749   1496    877       C  
ATOM   1105  OG  SER A 207      18.481   6.858  53.332  1.00 72.17           O  
ANISOU 1105  OG  SER A 207     7193  10086  10145   1614   1511    889       O  
ATOM   1106  N   MET A 208      16.346   9.588  50.309  1.00 80.30           N  
ANISOU 1106  N   MET A 208     8047  11085  11380   1958   1328    952       N  
ATOM   1107  CA  MET A 208      15.365  10.623  49.975  1.00 85.10           C  
ANISOU 1107  CA  MET A 208     8569  11727  12039   2099   1321    938       C  
ATOM   1108  C   MET A 208      14.061  10.120  49.349  1.00 79.98           C  
ANISOU 1108  C   MET A 208     7716  11259  11412   2077   1285   1041       C  
ATOM   1109  O   MET A 208      13.008  10.726  49.627  1.00 91.34           O  
ANISOU 1109  O   MET A 208     9036  12793  12875   2184   1326   1018       O  
ATOM   1110  CB  MET A 208      16.026  11.656  49.049  1.00 95.63           C  
ANISOU 1110  CB  MET A 208    10043  12869  13422   2175   1241    910       C  
ATOM   1111  CG  MET A 208      15.118  12.807  48.646  1.00102.49           C  
ANISOU 1111  CG  MET A 208    10843  13749  14351   2325   1224    892       C  
ATOM   1112  SD  MET A 208      15.888  13.918  47.454  1.00109.41           S  
ANISOU 1112  SD  MET A 208    11883  14409  15277   2386   1116    871       S  
ATOM   1113  CE  MET A 208      14.669  15.230  47.372  1.00113.47           C  
ANISOU 1113  CE  MET A 208    12292  14962  15858   2572   1123    837       C  
ATOM   1114  N   PRO A 209      14.042   9.084  48.499  1.00 65.48           N  
ANISOU 1114  N   PRO A 209     5830   9477   9572   1946   1207   1151       N  
ATOM   1115  CA  PRO A 209      12.747   8.609  47.981  1.00 66.42           C  
ANISOU 1115  CA  PRO A 209     5754   9780   9705   1916   1171   1245       C  
ATOM   1116  C   PRO A 209      11.746   8.250  49.065  1.00 71.38           C  
ANISOU 1116  C   PRO A 209     6231  10597  10295   1908   1267   1230       C  
ATOM   1117  O   PRO A 209      10.535   8.398  48.843  1.00 71.00           O  
ANISOU 1117  O   PRO A 209     6022  10684  10272   1953   1262   1267       O  
ATOM   1118  CB  PRO A 209      13.136   7.384  47.145  1.00 61.52           C  
ANISOU 1118  CB  PRO A 209     5137   9171   9065   1741   1082   1351       C  
ATOM   1119  CG  PRO A 209      14.496   7.693  46.669  1.00 66.79           C  
ANISOU 1119  CG  PRO A 209     5999   9629   9749   1741   1038   1321       C  
ATOM   1120  CD  PRO A 209      15.168   8.447  47.787  1.00 65.46           C  
ANISOU 1120  CD  PRO A 209     5951   9356   9564   1831   1132   1196       C  
ATOM   1121  N   ILE A 210      12.205   7.803  50.237  1.00 64.17           N  
ANISOU 1121  N   ILE A 210     5365   9698   9320   1850   1354   1174       N  
ATOM   1122  CA  ILE A 210      11.271   7.456  51.309  1.00 77.24           C  
ANISOU 1122  CA  ILE A 210     6884  11533  10931   1833   1449   1155       C  
ATOM   1123  C   ILE A 210      10.489   8.674  51.789  1.00 88.45           C  
ANISOU 1123  C   ILE A 210     8240  12978  12390   2014   1520   1075       C  
ATOM   1124  O   ILE A 210       9.249   8.617  51.792  1.00 93.69           O  
ANISOU 1124  O   ILE A 210     8727  13803  13067   2036   1537   1109       O  
ATOM   1125  CB  ILE A 210      12.007   6.721  52.443  1.00 82.21           C  
ANISOU 1125  CB  ILE A 210     7594  12162  11481   1725   1523   1112       C  
ATOM   1126  CG1 ILE A 210      12.484   5.349  51.966  1.00 75.46           C  
ANISOU 1126  CG1 ILE A 210     6758  11326  10589   1528   1449   1207       C  
ATOM   1127  CG2 ILE A 210      11.107   6.586  53.665  1.00 80.25           C  
ANISOU 1127  CG2 ILE A 210     7227  12080  11184   1727   1636   1069       C  
ATOM   1128  CD1 ILE A 210      13.227   4.571  53.024  1.00 71.24           C  
ANISOU 1128  CD1 ILE A 210     6305  10786   9976   1411   1510   1172       C  
ATOM   1129  N   PRO A 211      11.118   9.792  52.186  1.00 87.25           N  
ANISOU 1129  N   PRO A 211     8219  12673  12258   2145   1560    968       N  
ATOM   1130  CA  PRO A 211      10.305  10.984  52.480  1.00 88.62           C  
ANISOU 1130  CA  PRO A 211     8326  12865  12482   2319   1611    899       C  
ATOM   1131  C   PRO A 211       9.541  11.491  51.275  1.00 94.33           C  
ANISOU 1131  C   PRO A 211     8956  13602  13283   2399   1523    963       C  
ATOM   1132  O   PRO A 211       8.396  11.940  51.428  1.00106.13           O  
ANISOU 1132  O   PRO A 211    10301  15210  14813   2493   1558    955       O  
ATOM   1133  CB  PRO A 211      11.336  12.017  52.952  1.00 77.49           C  
ANISOU 1133  CB  PRO A 211     7110  11257  11076   2415   1642    781       C  
ATOM   1134  CG  PRO A 211      12.478  11.249  53.385  1.00 71.14           C  
ANISOU 1134  CG  PRO A 211     6438  10386  10205   2288   1652    773       C  
ATOM   1135  CD  PRO A 211      12.530  10.016  52.542  1.00 79.01           C  
ANISOU 1135  CD  PRO A 211     7385  11446  11190   2135   1570    898       C  
ATOM   1136  N   VAL A 212      10.137  11.419  50.078  1.00 88.65           N  
ANISOU 1136  N   VAL A 212     8318  12773  12590   2362   1409   1026       N  
ATOM   1137  CA  VAL A 212       9.458  11.918  48.881  1.00 97.08           C  
ANISOU 1137  CA  VAL A 212     9309  13847  13729   2434   1317   1089       C  
ATOM   1138  C   VAL A 212       8.089  11.264  48.730  1.00101.41           C  
ANISOU 1138  C   VAL A 212     9633  14619  14281   2392   1315   1174       C  
ATOM   1139  O   VAL A 212       7.063  11.944  48.611  1.00104.19           O  
ANISOU 1139  O   VAL A 212     9860  15040  14686   2512   1323   1169       O  
ATOM   1140  CB  VAL A 212      10.329  11.698  47.632  1.00 95.20           C  
ANISOU 1140  CB  VAL A 212     9191  13478  13505   2363   1197   1155       C  
ATOM   1141  CG1 VAL A 212       9.497  11.873  46.369  1.00 86.68           C  
ANISOU 1141  CG1 VAL A 212     8003  12449  12481   2394   1097   1246       C  
ATOM   1142  CG2 VAL A 212      11.496  12.671  47.628  1.00100.10           C  
ANISOU 1142  CG2 VAL A 212    10021  13872  14139   2437   1188   1066       C  
ATOM   1143  N   PHE A 213       8.054   9.935  48.724  1.00101.59           N  
ANISOU 1143  N   PHE A 213     9602  14752  14248   2218   1299   1252       N  
ATOM   1144  CA  PHE A 213       6.807   9.209  48.523  1.00101.48           C  
ANISOU 1144  CA  PHE A 213     9384  14947  14227   2150   1284   1338       C  
ATOM   1145  C   PHE A 213       6.035   8.954  49.815  1.00 97.08           C  
ANISOU 1145  C   PHE A 213     8705  14550  13629   2146   1406   1292       C  
ATOM   1146  O   PHE A 213       4.916   8.434  49.752  1.00 92.18           O  
ANISOU 1146  O   PHE A 213     7908  14111  13004   2097   1404   1355       O  
ATOM   1147  CB  PHE A 213       7.083   7.882  47.808  1.00104.78           C  
ANISOU 1147  CB  PHE A 213     9804  15406  14602   1950   1194   1449       C  
ATOM   1148  CG  PHE A 213       7.510   8.045  46.372  1.00106.99           C  
ANISOU 1148  CG  PHE A 213    10154  15572  14924   1944   1066   1515       C  
ATOM   1149  CD1 PHE A 213       6.592   7.910  45.344  1.00110.15           C  
ANISOU 1149  CD1 PHE A 213    10427  16066  15357   1930    977   1610       C  
ATOM   1150  CD2 PHE A 213       8.824   8.347  46.052  1.00102.86           C  
ANISOU 1150  CD2 PHE A 213     9826  14849  14407   1950   1034   1482       C  
ATOM   1151  CE1 PHE A 213       6.978   8.062  44.024  1.00105.65           C  
ANISOU 1151  CE1 PHE A 213     9927  15394  14822   1920    860   1670       C  
ATOM   1152  CE2 PHE A 213       9.215   8.502  44.734  1.00 96.10           C  
ANISOU 1152  CE2 PHE A 213     9037  13890  13587   1940    919   1541       C  
ATOM   1153  CZ  PHE A 213       8.291   8.358  43.720  1.00 98.07           C  
ANISOU 1153  CZ  PHE A 213     9161  14236  13866   1924    833   1635       C  
ATOM   1154  N   GLY A 214       6.589   9.306  50.976  1.00 95.13           N  
ANISOU 1154  N   GLY A 214     8550  14245  13351   2190   1511   1185       N  
ATOM   1155  CA  GLY A 214       5.863   9.175  52.224  1.00 92.96           C  
ANISOU 1155  CA  GLY A 214     8167  14115  13038   2196   1634   1132       C  
ATOM   1156  C   GLY A 214       5.098  10.408  52.651  1.00 87.80           C  
ANISOU 1156  C   GLY A 214     7439  13477  12444   2391   1706   1049       C  
ATOM   1157  O   GLY A 214       4.023  10.299  53.248  1.00 95.33           O  
ANISOU 1157  O   GLY A 214     8229  14598  13393   2406   1780   1043       O  
ATOM   1158  N   LEU A 215       5.642  11.591  52.363  1.00 81.30           N  
ANISOU 1158  N   LEU A 215     6735  12477  11677   2537   1686    983       N  
ATOM   1159  CA  LEU A 215       4.908  12.811  52.675  1.00 86.16           C  
ANISOU 1159  CA  LEU A 215     7284  13095  12359   2727   1742    906       C  
ATOM   1160  C   LEU A 215       3.727  13.006  51.734  1.00 98.40           C  
ANISOU 1160  C   LEU A 215     8657  14748  13981   2788   1675    986       C  
ATOM   1161  O   LEU A 215       2.691  13.542  52.145  1.00 94.95           O  
ANISOU 1161  O   LEU A 215     8078  14413  13586   2899   1739    951       O  
ATOM   1162  CB  LEU A 215       5.846  14.018  52.624  1.00 83.22           C  
ANISOU 1162  CB  LEU A 215     7101  12495  12024   2854   1731    813       C  
ATOM   1163  CG  LEU A 215       7.016  13.994  53.615  1.00 75.16           C  
ANISOU 1163  CG  LEU A 215     6261  11362  10936   2812   1800    721       C  
ATOM   1164  CD1 LEU A 215       7.840  15.272  53.526  1.00 64.32           C  
ANISOU 1164  CD1 LEU A 215     5067   9769   9604   2938   1780    628       C  
ATOM   1165  CD2 LEU A 215       6.515  13.772  55.035  1.00 77.78           C  
ANISOU 1165  CD2 LEU A 215     6514  11826  11214   2804   1942    651       C  
ATOM   1166  N   GLN A 216       3.858  12.569  50.479  1.00104.23           N  
ANISOU 1166  N   GLN A 216     9401  15465  14735   2716   1547   1093       N  
ATOM   1167  CA  GLN A 216       2.744  12.655  49.539  1.00107.48           C  
ANISOU 1167  CA  GLN A 216     9645  15983  15209   2756   1473   1178       C  
ATOM   1168  C   GLN A 216       1.665  11.627  49.865  1.00102.69           C  
ANISOU 1168  C   GLN A 216     8838  15615  14564   2646   1507   1245       C  
ATOM   1169  O   GLN A 216       0.477  11.962  49.942  1.00114.57           O  
ANISOU 1169  O   GLN A 216    10166  17250  16115   2731   1536   1250       O  
ATOM   1170  CB  GLN A 216       3.250  12.470  48.106  1.00105.92           C  
ANISOU 1170  CB  GLN A 216     9525  15689  15031   2699   1326   1271       C  
ATOM   1171  CG  GLN A 216       4.089  13.627  47.581  1.00105.59           C  
ANISOU 1171  CG  GLN A 216     9656  15422  15041   2823   1276   1216       C  
ATOM   1172  CD  GLN A 216       4.477  13.454  46.121  1.00106.35           C  
ANISOU 1172  CD  GLN A 216     9813  15438  15157   2766   1132   1311       C  
ATOM   1173  OE1 GLN A 216       4.129  12.457  45.487  1.00106.06           O  
ANISOU 1173  OE1 GLN A 216     9691  15511  15095   2633   1068   1418       O  
ATOM   1174  NE2 GLN A 216       5.202  14.429  45.580  1.00101.41           N  
ANISOU 1174  NE2 GLN A 216     9341  14618  14574   2860   1080   1270       N  
ATOM   1175  N   ASP A 217       2.059  10.371  50.065  1.00 93.50           N  
ANISOU 1175  N   ASP A 217     7699  14509  13317   2453   1503   1295       N  
ATOM   1176  CA  ASP A 217       1.131   9.272  50.304  1.00 87.25           C  
ANISOU 1176  CA  ASP A 217     6738  13933  12479   2316   1519   1367       C  
ATOM   1177  C   ASP A 217       1.397   8.684  51.683  1.00 95.17           C  
ANISOU 1177  C   ASP A 217     7768  14992  13398   2229   1640   1306       C  
ATOM   1178  O   ASP A 217       2.526   8.280  51.983  1.00 94.67           O  
ANISOU 1178  O   ASP A 217     7867  14823  13280   2143   1644   1282       O  
ATOM   1179  CB  ASP A 217       1.266   8.196  49.223  1.00 83.42           C  
ANISOU 1179  CB  ASP A 217     6254  13476  11965   2141   1391   1495       C  
ATOM   1180  CG  ASP A 217       0.123   7.197  49.240  1.00 88.60           C  
ANISOU 1180  CG  ASP A 217     6722  14355  12587   2012   1383   1580       C  
ATOM   1181  OD1 ASP A 217      -0.407   6.902  50.331  1.00 91.36           O  
ANISOU 1181  OD1 ASP A 217     6984  14832  12897   1985   1491   1541       O  
ATOM   1182  OD2 ASP A 217      -0.250   6.702  48.157  1.00 93.06           O  
ANISOU 1182  OD2 ASP A 217     7229  14968  13162   1932   1269   1685       O  
ATOM   1183  N   ASP A 218       0.353   8.627  52.511  1.00100.20           N  
ANISOU 1183  N   ASP A 218     8245  15799  14026   2248   1736   1281       N  
ATOM   1184  CA  ASP A 218       0.455   8.083  53.858  1.00103.43           C  
ANISOU 1184  CA  ASP A 218     8664  16282  14354   2164   1857   1224       C  
ATOM   1185  C   ASP A 218       0.388   6.561  53.896  1.00 99.87           C  
ANISOU 1185  C   ASP A 218     8179  15949  13816   1929   1825   1314       C  
ATOM   1186  O   ASP A 218       0.711   5.973  54.933  1.00100.07           O  
ANISOU 1186  O   ASP A 218     8252  16008  13763   1829   1906   1276       O  
ATOM   1187  CB  ASP A 218      -0.658   8.654  54.742  1.00112.37           C  
ANISOU 1187  CB  ASP A 218     9636  17548  15510   2279   1980   1159       C  
ATOM   1188  CG  ASP A 218      -0.648  10.169  54.788  1.00117.59           C  
ANISOU 1188  CG  ASP A 218    10329  18092  16257   2512   2017   1061       C  
ATOM   1189  OD1 ASP A 218       0.403  10.766  54.469  1.00116.51           O  
ANISOU 1189  OD1 ASP A 218    10371  17758  16141   2574   1975   1020       O  
ATOM   1190  OD2 ASP A 218      -1.691  10.762  55.142  1.00117.17           O  
ANISOU 1190  OD2 ASP A 218    10124  18143  16254   2632   2087   1025       O  
ATOM   1191  N   SER A 219      -0.016   5.911  52.802  1.00 92.00           N  
ANISOU 1191  N   SER A 219     7113  15013  12830   1832   1705   1431       N  
ATOM   1192  CA  SER A 219      -0.175   4.462  52.814  1.00 87.45           C  
ANISOU 1192  CA  SER A 219     6503  14551  12173   1604   1666   1517       C  
ATOM   1193  C   SER A 219       1.145   3.710  52.688  1.00 85.49           C  
ANISOU 1193  C   SER A 219     6447  14170  11865   1462   1611   1533       C  
ATOM   1194  O   SER A 219       1.212   2.541  53.085  1.00 89.75           O  
ANISOU 1194  O   SER A 219     6997  14781  12323   1274   1610   1572       O  
ATOM   1195  CB  SER A 219      -1.121   4.027  51.692  1.00 84.45           C  
ANISOU 1195  CB  SER A 219     5980  14284  11821   1546   1555   1635       C  
ATOM   1196  OG  SER A 219      -0.576   4.336  50.421  1.00 85.81           O  
ANISOU 1196  OG  SER A 219     6236  14323  12044   1580   1432   1681       O  
ATOM   1197  N   LYS A 220       2.194   4.342  52.154  1.00 78.67           N  
ANISOU 1197  N   LYS A 220     5737  13114  11041   1544   1565   1504       N  
ATOM   1198  CA  LYS A 220       3.477   3.663  51.999  1.00 73.54           C  
ANISOU 1198  CA  LYS A 220     5265  12333  10342   1417   1512   1518       C  
ATOM   1199  C   LYS A 220       4.292   3.630  53.285  1.00 76.24           C  
ANISOU 1199  C   LYS A 220     5726  12617  10626   1403   1620   1423       C  
ATOM   1200  O   LYS A 220       5.268   2.876  53.362  1.00 72.95           O  
ANISOU 1200  O   LYS A 220     5441  12121  10156   1271   1590   1436       O  
ATOM   1201  CB  LYS A 220       4.296   4.317  50.883  1.00 63.38           C  
ANISOU 1201  CB  LYS A 220     4098  10864   9120   1501   1418   1529       C  
ATOM   1202  CG  LYS A 220       3.683   4.143  49.502  1.00 70.30           C  
ANISOU 1202  CG  LYS A 220     4889  11783  10040   1475   1292   1636       C  
ATOM   1203  CD  LYS A 220       4.436   4.926  48.438  1.00 67.71           C  
ANISOU 1203  CD  LYS A 220     4677  11274   9777   1574   1208   1639       C  
ATOM   1204  CE  LYS A 220       3.718   4.838  47.098  1.00 71.92           C  
ANISOU 1204  CE  LYS A 220     5114  11860  10352   1557   1088   1742       C  
ATOM   1205  NZ  LYS A 220       4.413   5.594  46.023  1.00 67.64           N  
ANISOU 1205  NZ  LYS A 220     4685  11144   9870   1646   1004   1749       N  
ATOM   1206  N   VAL A 221       3.917   4.416  54.291  1.00 75.79           N  
ANISOU 1206  N   VAL A 221     5627  12594  10575   1530   1745   1328       N  
ATOM   1207  CA  VAL A 221       4.596   4.399  55.581  1.00 66.54           C  
ANISOU 1207  CA  VAL A 221     4560  11381   9341   1515   1854   1235       C  
ATOM   1208  C   VAL A 221       3.683   3.985  56.725  1.00 75.08           C  
ANISOU 1208  C   VAL A 221     5518  12644  10364   1460   1966   1213       C  
ATOM   1209  O   VAL A 221       4.172   3.815  57.853  1.00 80.19           O  
ANISOU 1209  O   VAL A 221     6246  13278  10946   1419   2059   1144       O  
ATOM   1210  CB  VAL A 221       5.242   5.766  55.894  1.00 65.72           C  
ANISOU 1210  CB  VAL A 221     4569  11117   9284   1712   1912   1120       C  
ATOM   1211  CG1 VAL A 221       6.232   6.138  54.808  1.00 64.17           C  
ANISOU 1211  CG1 VAL A 221     4512  10733   9138   1752   1803   1142       C  
ATOM   1212  CG2 VAL A 221       4.171   6.842  56.048  1.00 64.02           C  
ANISOU 1212  CG2 VAL A 221     4218  10971   9134   1893   1974   1071       C  
ATOM   1213  N   PHE A 222       2.384   3.814  56.485  1.00 72.61           N  
ANISOU 1213  N   PHE A 222     5014  12500  10072   1454   1962   1268       N  
ATOM   1214  CA  PHE A 222       1.440   3.409  57.516  1.00 65.98           C  
ANISOU 1214  CA  PHE A 222     4046  11843   9181   1399   2067   1254       C  
ATOM   1215  C   PHE A 222       0.760   2.112  57.107  1.00 67.41           C  
ANISOU 1215  C   PHE A 222     4126  12171   9317   1202   1993   1372       C  
ATOM   1216  O   PHE A 222       0.459   1.901  55.928  1.00 71.80           O  
ANISOU 1216  O   PHE A 222     4629  12737   9914   1177   1875   1460       O  
ATOM   1217  CB  PHE A 222       0.379   4.485  57.767  1.00 68.59           C  
ANISOU 1217  CB  PHE A 222     4224  12257   9579   1587   2150   1199       C  
ATOM   1218  CG  PHE A 222       0.875   5.657  58.564  1.00 68.80           C  
ANISOU 1218  CG  PHE A 222     4342  12171   9628   1760   2257   1064       C  
ATOM   1219  CD1 PHE A 222       1.171   5.520  59.913  1.00 68.97           C  
ANISOU 1219  CD1 PHE A 222     4423  12209   9573   1721   2382    982       C  
ATOM   1220  CD2 PHE A 222       1.028   6.902  57.971  1.00 68.93           C  
ANISOU 1220  CD2 PHE A 222     4389  12063   9737   1957   2229   1019       C  
ATOM   1221  CE1 PHE A 222       1.625   6.599  60.653  1.00 69.23           C  
ANISOU 1221  CE1 PHE A 222     4546  12136   9621   1874   2478    855       C  
ATOM   1222  CE2 PHE A 222       1.479   7.985  58.704  1.00 69.20           C  
ANISOU 1222  CE2 PHE A 222     4517  11986   9790   2110   2321    892       C  
ATOM   1223  CZ  PHE A 222       1.777   7.833  60.048  1.00 69.35           C  
ANISOU 1223  CZ  PHE A 222     4595  12024   9731   2068   2446    809       C  
ATOM   1224  N   LYS A 223       0.523   1.245  58.090  1.00 66.82           N  
ANISOU 1224  N   LYS A 223     4031  12205   9154   1057   2061   1372       N  
ATOM   1225  CA  LYS A 223      -0.218   0.000  57.885  1.00 67.48           C  
ANISOU 1225  CA  LYS A 223     4018  12438   9185    864   2004   1474       C  
ATOM   1226  C   LYS A 223      -1.076  -0.223  59.127  1.00 69.68           C  
ANISOU 1226  C   LYS A 223     4186  12883   9407    827   2135   1440       C  
ATOM   1227  O   LYS A 223      -0.584  -0.731  60.139  1.00 69.15           O  
ANISOU 1227  O   LYS A 223     4211  12805   9256    728   2203   1402       O  
ATOM   1228  CB  LYS A 223       0.717  -1.175  57.620  1.00 65.12           C  
ANISOU 1228  CB  LYS A 223     3870  12055   8818    662   1908   1531       C  
ATOM   1229  CG  LYS A 223       0.004  -2.506  57.405  1.00 65.76           C  
ANISOU 1229  CG  LYS A 223     3874  12272   8838    452   1839   1635       C  
ATOM   1230  CD  LYS A 223       0.997  -3.650  57.255  1.00 66.76           C  
ANISOU 1230  CD  LYS A 223     4170  12298   8897    258   1749   1676       C  
ATOM   1231  CE  LYS A 223       1.831  -3.490  55.993  1.00 66.57           C  
ANISOU 1231  CE  LYS A 223     4249  12116   8928    284   1624   1709       C  
ATOM   1232  NZ  LYS A 223       2.823  -4.589  55.822  1.00 63.28           N  
ANISOU 1232  NZ  LYS A 223     4000  11592   8451    101   1536   1744       N  
ATOM   1233  N   GLU A 224      -2.349   0.178  59.048  1.00 72.69           N  
ANISOU 1233  N   GLU A 224     4370  13415   9835    910   2173   1454       N  
ATOM   1234  CA  GLU A 224      -3.317   0.011  60.137  1.00 74.65           C  
ANISOU 1234  CA  GLU A 224     4485  13839  10038    884   2299   1427       C  
ATOM   1235  C   GLU A 224      -2.897   0.797  61.378  1.00 78.18           C  
ANISOU 1235  C   GLU A 224     5003  14235  10469    998   2453   1297       C  
ATOM   1236  O   GLU A 224      -2.813   0.259  62.485  1.00 75.28           O  
ANISOU 1236  O   GLU A 224     4672  13918  10013    893   2542   1268       O  
ATOM   1237  CB  GLU A 224      -3.519  -1.467  60.485  1.00 74.58           C  
ANISOU 1237  CB  GLU A 224     4478  13934   9926    634   2271   1504       C  
ATOM   1238  CG  GLU A 224      -3.856  -2.369  59.315  1.00 80.35           C  
ANISOU 1238  CG  GLU A 224     5165  14705  10657    496   2115   1629       C  
ATOM   1239  CD  GLU A 224      -3.834  -3.837  59.702  1.00 79.30           C  
ANISOU 1239  CD  GLU A 224     5082  14634  10416    245   2079   1694       C  
ATOM   1240  OE1 GLU A 224      -3.909  -4.137  60.914  1.00 75.12           O  
ANISOU 1240  OE1 GLU A 224     4564  14166   9814    183   2187   1651       O  
ATOM   1241  OE2 GLU A 224      -3.735  -4.691  58.796  1.00 77.32           O  
ANISOU 1241  OE2 GLU A 224     4864  14363  10149    109   1941   1785       O  
ATOM   1242  N   GLY A 225      -2.631   2.090  61.184  1.00 78.30           N  
ANISOU 1242  N   GLY A 225     5043  14142  10568   1213   2481   1219       N  
ATOM   1243  CA  GLY A 225      -2.253   2.969  62.269  1.00 85.26           C  
ANISOU 1243  CA  GLY A 225     5994  14961  11442   1340   2621   1088       C  
ATOM   1244  C   GLY A 225      -0.801   2.903  62.688  1.00 90.27           C  
ANISOU 1244  C   GLY A 225     6857  15418  12022   1299   2623   1033       C  
ATOM   1245  O   GLY A 225      -0.296   3.872  63.267  1.00101.11           O  
ANISOU 1245  O   GLY A 225     8317  16688  13412   1441   2707    922       O  
ATOM   1246  N   SER A 226      -0.112   1.799  62.417  1.00 89.14           N  
ANISOU 1246  N   SER A 226     6820  15234  11817   1112   2532   1105       N  
ATOM   1247  CA  SER A 226       1.289   1.657  62.773  1.00 68.47           C  
ANISOU 1247  CA  SER A 226     4417  12451   9148   1063   2526   1061       C  
ATOM   1248  C   SER A 226       2.183   2.307  61.721  1.00 66.51           C  
ANISOU 1248  C   SER A 226     4278  12016   8975   1170   2425   1058       C  
ATOM   1249  O   SER A 226       1.806   2.472  60.559  1.00 66.55           O  
ANISOU 1249  O   SER A 226     4208  12023   9053   1216   2325   1123       O  
ATOM   1250  CB  SER A 226       1.650   0.180  62.937  1.00 74.56           C  
ANISOU 1250  CB  SER A 226     5257  13250   9823    816   2468   1139       C  
ATOM   1251  OG  SER A 226       1.304  -0.565  61.784  1.00 82.33           O  
ANISOU 1251  OG  SER A 226     6179  14273  10830    714   2329   1256       O  
ATOM   1252  N   CYS A 227       3.385   2.683  62.149  1.00 68.91           N  
ANISOU 1252  N   CYS A 227     4764  12160   9258   1206   2451    981       N  
ATOM   1253  CA  CYS A 227       4.360   3.350  61.292  1.00 69.12           C  
ANISOU 1253  CA  CYS A 227     4917  11997   9349   1308   2368    965       C  
ATOM   1254  C   CYS A 227       5.447   2.351  60.919  1.00 71.35           C  
ANISOU 1254  C   CYS A 227     5344  12183   9582   1140   2271   1025       C  
ATOM   1255  O   CYS A 227       6.270   1.976  61.763  1.00 73.44           O  
ANISOU 1255  O   CYS A 227     5739  12393   9773   1059   2316    982       O  
ATOM   1256  CB  CYS A 227       4.956   4.569  61.991  1.00 70.58           C  
ANISOU 1256  CB  CYS A 227     5208  12058   9550   1479   2462    831       C  
ATOM   1257  SG  CYS A 227       6.318   5.344  61.091  1.00 72.30           S  
ANISOU 1257  SG  CYS A 227     5615  12024   9831   1586   2366    805       S  
ATOM   1258  N   LEU A 228       5.451   1.932  59.656  1.00 66.69           N  
ANISOU 1258  N   LEU A 228     4734  11572   9035   1089   2136   1123       N  
ATOM   1259  CA  LEU A 228       6.453   1.013  59.132  1.00 72.48           C  
ANISOU 1259  CA  LEU A 228     5597  12206   9736    937   2031   1183       C  
ATOM   1260  C   LEU A 228       6.362   1.025  57.614  1.00 82.32           C  
ANISOU 1260  C   LEU A 228     6810  13411  11056    953   1895   1269       C  
ATOM   1261  O   LEU A 228       5.343   1.422  57.042  1.00 92.74           O  
ANISOU 1261  O   LEU A 228     7984  14821  12433   1032   1876   1303       O  
ATOM   1262  CB  LEU A 228       6.264  -0.408  59.679  1.00 65.73           C  
ANISOU 1262  CB  LEU A 228     4733  11456   8784    709   2026   1240       C  
ATOM   1263  CG  LEU A 228       4.878  -1.048  59.587  1.00 64.76           C  
ANISOU 1263  CG  LEU A 228     4429  11532   8647    623   2017   1315       C  
ATOM   1264  CD1 LEU A 228       4.702  -1.805  58.284  1.00 59.69           C  
ANISOU 1264  CD1 LEU A 228     3756  10895   8028    516   1865   1429       C  
ATOM   1265  CD2 LEU A 228       4.653  -1.968  60.773  1.00 79.16           C  
ANISOU 1265  CD2 LEU A 228     6254  13456  10365    464   2088   1311       C  
ATOM   1266  N   LEU A 229       7.443   0.591  56.969  1.00 82.28           N  
ANISOU 1266  N   LEU A 229     6944  13269  11051    877   1800   1303       N  
ATOM   1267  CA  LEU A 229       7.460   0.521  55.514  1.00 82.68           C  
ANISOU 1267  CA  LEU A 229     6982  13270  11163    874   1667   1387       C  
ATOM   1268  C   LEU A 229       6.409  -0.470  55.029  1.00 92.69           C  
ANISOU 1268  C   LEU A 229     8113  14697  12409    731   1599   1490       C  
ATOM   1269  O   LEU A 229       6.461  -1.659  55.361  1.00 96.20           O  
ANISOU 1269  O   LEU A 229     8583  15192  12778    541   1577   1530       O  
ATOM   1270  CB  LEU A 229       8.848   0.115  55.020  1.00 72.25           C  
ANISOU 1270  CB  LEU A 229     5839  11777   9837    798   1588   1401       C  
ATOM   1271  CG  LEU A 229       9.932   1.194  55.064  1.00 66.61           C  
ANISOU 1271  CG  LEU A 229     5264  10879   9167    953   1618   1318       C  
ATOM   1272  CD1 LEU A 229      11.309   0.579  54.898  1.00 69.53           C  
ANISOU 1272  CD1 LEU A 229     5805  11101   9511    845   1563   1327       C  
ATOM   1273  CD2 LEU A 229       9.685   2.232  53.987  1.00 55.43           C  
ANISOU 1273  CD2 LEU A 229     3812   9402   7847   1116   1565   1328       C  
ATOM   1274  N   ALA A 230       5.454   0.024  54.238  1.00 89.24           N  
ANISOU 1274  N   ALA A 230     7538  14332  12035    820   1562   1531       N  
ATOM   1275  CA  ALA A 230       4.378  -0.806  53.722  1.00 93.84           C  
ANISOU 1275  CA  ALA A 230     7984  15070  12602    700   1496   1628       C  
ATOM   1276  C   ALA A 230       4.472  -1.072  52.227  1.00 92.50           C  
ANISOU 1276  C   ALA A 230     7825  14847  12473    656   1349   1719       C  
ATOM   1277  O   ALA A 230       3.912  -2.069  51.761  1.00 97.87           O  
ANISOU 1277  O   ALA A 230     8449  15620  13119    501   1271   1805       O  
ATOM   1278  CB  ALA A 230       3.015  -0.165  54.027  1.00 98.66           C  
ANISOU 1278  CB  ALA A 230     8402  15840  13246    816   1571   1615       C  
ATOM   1279  N   ASP A 231       5.158  -0.217  51.472  1.00 83.89           N  
ANISOU 1279  N   ASP A 231     6814  13608  11451    783   1307   1702       N  
ATOM   1280  CA  ASP A 231       5.275  -0.415  50.034  1.00 88.07           C  
ANISOU 1280  CA  ASP A 231     7361  14082  12019    744   1170   1786       C  
ATOM   1281  C   ASP A 231       6.202  -1.587  49.736  1.00 86.76           C  
ANISOU 1281  C   ASP A 231     7333  13834  11797    549   1087   1828       C  
ATOM   1282  O   ASP A 231       7.318  -1.657  50.259  1.00 80.61           O  
ANISOU 1282  O   ASP A 231     6697  12934  10996    531   1119   1774       O  
ATOM   1283  CB  ASP A 231       5.796   0.857  49.364  1.00 84.91           C  
ANISOU 1283  CB  ASP A 231     7021  13537  11705    934   1153   1751       C  
ATOM   1284  CG  ASP A 231       5.693   0.805  47.850  1.00 87.01           C  
ANISOU 1284  CG  ASP A 231     7278  13767  12016    914   1018   1839       C  
ATOM   1285  OD1 ASP A 231       4.569   0.944  47.319  1.00 93.11           O  
ANISOU 1285  OD1 ASP A 231     7903  14658  12816    943    984   1893       O  
ATOM   1286  OD2 ASP A 231       6.738   0.622  47.190  1.00 81.72           O  
ANISOU 1286  OD2 ASP A 231     6747  12950  11351    867    946   1855       O  
ATOM   1287  N   ASP A 232       5.741  -2.509  48.887  1.00 89.39           N  
ANISOU 1287  N   ASP A 232     7627  14228  12108    403    979   1922       N  
ATOM   1288  CA  ASP A 232       6.543  -3.688  48.576  1.00 98.64           C  
ANISOU 1288  CA  ASP A 232     8932  15321  13226    210    893   1960       C  
ATOM   1289  C   ASP A 232       7.779  -3.307  47.770  1.00 98.09           C  
ANISOU 1289  C   ASP A 232     9009  15057  13202    254    832   1950       C  
ATOM   1290  O   ASP A 232       8.889  -3.777  48.053  1.00100.74           O  
ANISOU 1290  O   ASP A 232     9493  15275  13509    176    826   1921       O  
ATOM   1291  CB  ASP A 232       5.701  -4.716  47.817  1.00108.11           C  
ANISOU 1291  CB  ASP A 232    10061  16626  14389     51    789   2058       C  
ATOM   1292  CG  ASP A 232       4.436  -5.093  48.557  1.00119.65           C  
ANISOU 1292  CG  ASP A 232    11369  18284  15807      5    846   2074       C  
ATOM   1293  OD1 ASP A 232       4.149  -4.469  49.600  1.00127.60           O  
ANISOU 1293  OD1 ASP A 232    12312  19350  16819    111    968   2008       O  
ATOM   1294  OD2 ASP A 232       3.727  -6.013  48.097  1.00121.85           O  
ANISOU 1294  OD2 ASP A 232    11594  18657  16046   -137    769   2149       O  
ATOM   1295  N   ASN A 233       7.601  -2.461  46.752  1.00 93.32           N  
ANISOU 1295  N   ASN A 233     8369  14416  12672    376    784   1976       N  
ATOM   1296  CA  ASN A 233       8.738  -2.009  45.960  1.00 81.19           C  
ANISOU 1296  CA  ASN A 233     6968  12695  11185    427    729   1968       C  
ATOM   1297  C   ASN A 233       9.745  -1.266  46.827  1.00 75.66           C  
ANISOU 1297  C   ASN A 233     6373  11872  10501    542    826   1869       C  
ATOM   1298  O   ASN A 233      10.960  -1.406  46.640  1.00 82.85           O  
ANISOU 1298  O   ASN A 233     7433  12630  11417    508    798   1850       O  
ATOM   1299  CB  ASN A 233       8.256  -1.124  44.809  1.00 87.60           C  
ANISOU 1299  CB  ASN A 233     7715  13497  12070    551    670   2008       C  
ATOM   1300  CG  ASN A 233       7.394  -1.881  43.813  1.00 96.11           C  
ANISOU 1300  CG  ASN A 233     8710  14678  13130    427    561   2110       C  
ATOM   1301  OD1 ASN A 233       7.559  -3.087  43.618  1.00 88.84           O  
ANISOU 1301  OD1 ASN A 233     7839  13767  12149    238    496   2154       O  
ATOM   1302  ND2 ASN A 233       6.468  -1.173  43.175  1.00107.03           N  
ANISOU 1302  ND2 ASN A 233     9972  16131  14564    533    538   2146       N  
ATOM   1303  N   PHE A 234       9.258  -0.476  47.787  1.00 70.13           N  
ANISOU 1303  N   PHE A 234     5603  11234   9811    678    940   1802       N  
ATOM   1304  CA  PHE A 234      10.155   0.171  48.740  1.00 60.65           C  
ANISOU 1304  CA  PHE A 234     4507   9926   8612    777   1039   1701       C  
ATOM   1305  C   PHE A 234      10.998  -0.859  49.475  1.00 56.58           C  
ANISOU 1305  C   PHE A 234     4099   9373   8024    617   1055   1685       C  
ATOM   1306  O   PHE A 234      12.224  -0.735  49.547  1.00 51.61           O  
ANISOU 1306  O   PHE A 234     3617   8590   7404    625   1057   1645       O  
ATOM   1307  CB  PHE A 234       9.356   1.010  49.737  1.00 72.84           C  
ANISOU 1307  CB  PHE A 234     5950  11565  10161    921   1160   1631       C  
ATOM   1308  CG  PHE A 234       9.323   2.476  49.415  1.00 82.02           C  
ANISOU 1308  CG  PHE A 234     7116  12643  11403   1141   1182   1580       C  
ATOM   1309  CD1 PHE A 234      10.222   3.022  48.514  1.00 79.92           C  
ANISOU 1309  CD1 PHE A 234     6971  12203  11190   1203   1116   1580       C  
ATOM   1310  CD2 PHE A 234       8.397   3.310  50.021  1.00 84.75           C  
ANISOU 1310  CD2 PHE A 234     7351  13079  11771   1283   1269   1528       C  
ATOM   1311  CE1 PHE A 234      10.192   4.375  48.219  1.00 81.50           C  
ANISOU 1311  CE1 PHE A 234     7191  12315  11459   1398   1128   1530       C  
ATOM   1312  CE2 PHE A 234       8.365   4.662  49.730  1.00 83.31           C  
ANISOU 1312  CE2 PHE A 234     7185  12809  11662   1482   1281   1475       C  
ATOM   1313  CZ  PHE A 234       9.264   5.194  48.828  1.00 80.82           C  
ANISOU 1313  CZ  PHE A 234     6999  12314  11394   1537   1209   1477       C  
ATOM   1314  N   VAL A 235      10.354  -1.893  50.021  1.00 52.23           N  
ANISOU 1314  N   VAL A 235     3484   8960   7402    467   1062   1716       N  
ATOM   1315  CA  VAL A 235      11.082  -2.895  50.794  1.00 44.86           C  
ANISOU 1315  CA  VAL A 235     2656   7994   6394    310   1074   1697       C  
ATOM   1316  C   VAL A 235      12.109  -3.603  49.922  1.00 50.21           C  
ANISOU 1316  C   VAL A 235     3470   8533   7074    190    961   1737       C  
ATOM   1317  O   VAL A 235      13.260  -3.793  50.331  1.00 64.95           O  
ANISOU 1317  O   VAL A 235     5477  10275   8925    154    975   1694       O  
ATOM   1318  CB  VAL A 235      10.104  -3.893  51.440  1.00 45.53           C  
ANISOU 1318  CB  VAL A 235     2650   8249   6402    166   1090   1729       C  
ATOM   1319  CG1 VAL A 235      10.869  -5.035  52.094  1.00 44.31           C  
ANISOU 1319  CG1 VAL A 235     2624   8044   6169    -13   1078   1718       C  
ATOM   1320  CG2 VAL A 235       9.225  -3.189  52.462  1.00 47.91           C  
ANISOU 1320  CG2 VAL A 235     2830   8678   6698    283   1218   1675       C  
ATOM   1321  N   LEU A 236      11.721  -3.986  48.703  1.00 52.86           N  
ANISOU 1321  N   LEU A 236     3771   8884   7430    128    847   1817       N  
ATOM   1322  CA  LEU A 236      12.637  -4.726  47.835  1.00 55.47           C  
ANISOU 1322  CA  LEU A 236     4233   9085   7759      4    736   1852       C  
ATOM   1323  C   LEU A 236      13.829  -3.872  47.416  1.00 60.67           C  
ANISOU 1323  C   LEU A 236     5001   9564   8486    118    737   1814       C  
ATOM   1324  O   LEU A 236      14.990  -4.284  47.565  1.00 65.76           O  
ANISOU 1324  O   LEU A 236     5789  10078   9120     49    722   1785       O  
ATOM   1325  CB  LEU A 236      11.891  -5.237  46.604  1.00 53.88           C  
ANISOU 1325  CB  LEU A 236     3968   8944   7561    -78    618   1942       C  
ATOM   1326  CG  LEU A 236      10.774  -6.246  46.866  1.00 70.64           C  
ANISOU 1326  CG  LEU A 236     5999  11228   9612   -217    596   1989       C  
ATOM   1327  CD1 LEU A 236      10.181  -6.726  45.553  1.00 77.31           C  
ANISOU 1327  CD1 LEU A 236     6805  12108  10460   -296    473   2075       C  
ATOM   1328  CD2 LEU A 236      11.285  -7.422  47.691  1.00 74.18           C  
ANISOU 1328  CD2 LEU A 236     6557  11648   9979   -383    596   1963       C  
ATOM   1329  N   ILE A 237      13.562  -2.676  46.885  1.00 55.14           N  
ANISOU 1329  N   ILE A 237     4243   8848   7859    295    752   1811       N  
ATOM   1330  CA  ILE A 237      14.641  -1.808  46.433  1.00 46.89           C  
ANISOU 1330  CA  ILE A 237     3308   7626   6882    412    749   1775       C  
ATOM   1331  C   ILE A 237      15.541  -1.430  47.597  1.00 43.22           C  
ANISOU 1331  C   ILE A 237     2938   7075   6407    474    855   1682       C  
ATOM   1332  O   ILE A 237      16.765  -1.376  47.453  1.00 41.87           O  
ANISOU 1332  O   ILE A 237     2902   6744   6260    469    842   1655       O  
ATOM   1333  CB  ILE A 237      14.064  -0.565  45.730  1.00 65.41           C  
ANISOU 1333  CB  ILE A 237     5581   9971   9299    594    746   1781       C  
ATOM   1334  CG1 ILE A 237      13.306  -0.980  44.463  1.00 62.22           C  
ANISOU 1334  CG1 ILE A 237     5100   9636   8905    520    630   1878       C  
ATOM   1335  CG2 ILE A 237      15.171   0.451  45.419  1.00 50.21           C  
ANISOU 1335  CG2 ILE A 237     3784   7852   7440    730    756   1727       C  
ATOM   1336  CD1 ILE A 237      12.667   0.173  43.718  1.00 55.73           C  
ANISOU 1336  CD1 ILE A 237     4206   8821   8149    685    614   1891       C  
ATOM   1337  N   GLY A 238      14.959  -1.185  48.775  1.00 46.14           N  
ANISOU 1337  N   GLY A 238     3243   7549   6740    527    961   1632       N  
ATOM   1338  CA  GLY A 238      15.774  -0.846  49.927  1.00 38.25           C  
ANISOU 1338  CA  GLY A 238     2339   6474   5719    579   1063   1542       C  
ATOM   1339  C   GLY A 238      16.636  -2.002  50.384  1.00 36.31           C  
ANISOU 1339  C   GLY A 238     2201   6180   5414    398   1044   1544       C  
ATOM   1340  O   GLY A 238      17.823  -1.824  50.669  1.00 35.90           O  
ANISOU 1340  O   GLY A 238     2283   5985   5375    416   1068   1495       O  
ATOM   1341  N   SER A 239      16.062  -3.209  50.435  1.00 36.73           N  
ANISOU 1341  N   SER A 239     2210   6344   5404    220    993   1598       N  
ATOM   1342  CA  SER A 239      16.818  -4.377  50.865  1.00 37.67           C  
ANISOU 1342  CA  SER A 239     2446   6408   5458     38    960   1596       C  
ATOM   1343  C   SER A 239      17.957  -4.680  49.907  1.00 51.54           C  
ANISOU 1343  C   SER A 239     4334   7994   7255    -21    863   1614       C  
ATOM   1344  O   SER A 239      19.005  -5.188  50.323  1.00 49.94           O  
ANISOU 1344  O   SER A 239     4269   7680   7027   -104    858   1580       O  
ATOM   1345  CB  SER A 239      15.886  -5.578  50.980  1.00 36.54           C  
ANISOU 1345  CB  SER A 239     2240   6403   5242   -133    910   1647       C  
ATOM   1346  OG  SER A 239      14.816  -5.296  51.862  1.00 48.47           O  
ANISOU 1346  OG  SER A 239     3622   8075   6719    -81   1004   1631       O  
ATOM   1347  N   PHE A 240      17.778  -4.370  48.626  1.00 53.37           N  
ANISOU 1347  N   PHE A 240     4532   8199   7549     19    784   1664       N  
ATOM   1348  CA  PHE A 240      18.862  -4.618  47.685  1.00 55.68           C  
ANISOU 1348  CA  PHE A 240     4948   8325   7881    -35    695   1677       C  
ATOM   1349  C   PHE A 240      19.906  -3.506  47.725  1.00 51.85           C  
ANISOU 1349  C   PHE A 240     4540   7688   7472    119    755   1622       C  
ATOM   1350  O   PHE A 240      21.106  -3.781  47.821  1.00 61.03           O  
ANISOU 1350  O   PHE A 240     5841   8706   8643     64    745   1590       O  
ATOM   1351  CB  PHE A 240      18.303  -4.816  46.277  1.00 62.91           C  
ANISOU 1351  CB  PHE A 240     5812   9267   8824    -72    581   1753       C  
ATOM   1352  CG  PHE A 240      18.029  -6.257  45.947  1.00 75.81           C  
ANISOU 1352  CG  PHE A 240     7481  10938  10385   -276    480   1793       C  
ATOM   1353  CD1 PHE A 240      16.812  -6.837  46.269  1.00 82.61           C  
ANISOU 1353  CD1 PHE A 240     8235  11966  11185   -344    478   1827       C  
ATOM   1354  CD2 PHE A 240      18.999  -7.042  45.347  1.00 74.42           C  
ANISOU 1354  CD2 PHE A 240     7459  10621  10199   -396    386   1784       C  
ATOM   1355  CE1 PHE A 240      16.563  -8.165  45.979  1.00 83.10           C  
ANISOU 1355  CE1 PHE A 240     8344  12050  11179   -522    385   1856       C  
ATOM   1356  CE2 PHE A 240      18.756  -8.370  45.056  1.00 69.18           C  
ANISOU 1356  CE2 PHE A 240     6849   9975   9462   -565    292   1801       C  
ATOM   1357  CZ  PHE A 240      17.537  -8.932  45.371  1.00 78.17           C  
ANISOU 1357  CZ  PHE A 240     7882  11278  10542   -627    291   1840       C  
ATOM   1358  N   VAL A 241      19.469  -2.245  47.680  1.00 44.19           N  
ANISOU 1358  N   VAL A 241     3497   6737   6555    314    816   1601       N  
ATOM   1359  CA  VAL A 241      20.398  -1.124  47.565  1.00 41.04           C  
ANISOU 1359  CA  VAL A 241     3189   6175   6230    474    857   1543       C  
ATOM   1360  C   VAL A 241      21.184  -0.928  48.856  1.00 47.78           C  
ANISOU 1360  C   VAL A 241     4135   6963   7056    508    964   1456       C  
ATOM   1361  O   VAL A 241      22.368  -0.568  48.827  1.00 52.09           O  
ANISOU 1361  O   VAL A 241     4833   7327   7632    545    965   1395       O  
ATOM   1362  CB  VAL A 241      19.628   0.149  47.163  1.00 35.25           C  
ANISOU 1362  CB  VAL A 241     2380   5469   5545    667    876   1532       C  
ATOM   1363  CG1 VAL A 241      20.512   1.383  47.255  1.00 31.78           C  
ANISOU 1363  CG1 VAL A 241     2063   4852   5159    837    924   1446       C  
ATOM   1364  CG2 VAL A 241      19.091   0.000  45.754  1.00 49.02           C  
ANISOU 1364  CG2 VAL A 241     4062   7241   7322    630    761   1619       C  
ATOM   1365  N   SER A 242      20.553  -1.165  50.004  1.00 43.75           N  
ANISOU 1365  N   SER A 242     3567   6583   6472    487   1041   1431       N  
ATOM   1366  CA  SER A 242      21.168  -0.866  51.288  1.00 45.83           C  
ANISOU 1366  CA  SER A 242     3913   6799   6700    533   1149   1345       C  
ATOM   1367  C   SER A 242      21.655  -2.089  52.055  1.00 45.86           C  
ANISOU 1367  C   SER A 242     3985   6815   6625    343   1147   1350       C  
ATOM   1368  O   SER A 242      22.340  -1.918  53.067  1.00 60.30           O  
ANISOU 1368  O   SER A 242     5908   8583   8422    363   1227   1281       O  
ATOM   1369  CB  SER A 242      20.192  -0.074  52.170  1.00 66.35           C  
ANISOU 1369  CB  SER A 242     6422   9519   9269    665   1250   1292       C  
ATOM   1370  OG  SER A 242      19.885   1.181  51.587  1.00 73.49           O  
ANISOU 1370  OG  SER A 242     7305  10377  10241    851   1252   1266       O  
ATOM   1371  N   PHE A 243      21.305  -3.309  51.643  1.00 43.09           N  
ANISOU 1371  N   PHE A 243     3609   6530   6232    158   1052   1420       N  
ATOM   1372  CA  PHE A 243      21.773  -4.470  52.399  1.00 48.23           C  
ANISOU 1372  CA  PHE A 243     4355   7172   6800    -22   1033   1412       C  
ATOM   1373  C   PHE A 243      22.501  -5.505  51.548  1.00 58.50           C  
ANISOU 1373  C   PHE A 243     5769   8358   8102   -184    899   1445       C  
ATOM   1374  O   PHE A 243      23.637  -5.878  51.857  1.00 59.49           O  
ANISOU 1374  O   PHE A 243     6046   8344   8215   -250    882   1407       O  
ATOM   1375  CB  PHE A 243      20.606  -5.134  53.125  1.00 38.89           C  
ANISOU 1375  CB  PHE A 243     3072   6177   5529   -109   1053   1430       C  
ATOM   1376  CG  PHE A 243      21.027  -6.204  54.092  1.00 39.54           C  
ANISOU 1376  CG  PHE A 243     3256   6248   5519   -272   1047   1409       C  
ATOM   1377  CD1 PHE A 243      21.648  -5.875  55.284  1.00 30.82           C  
ANISOU 1377  CD1 PHE A 243     2226   5108   4378   -236   1146   1345       C  
ATOM   1378  CD2 PHE A 243      20.784  -7.541  53.815  1.00 43.86           C  
ANISOU 1378  CD2 PHE A 243     3835   6815   6013   -456    940   1447       C  
ATOM   1379  CE1 PHE A 243      22.028  -6.862  56.180  1.00 30.58           C  
ANISOU 1379  CE1 PHE A 243     2295   5064   4259   -387   1134   1328       C  
ATOM   1380  CE2 PHE A 243      21.160  -8.528  54.706  1.00 34.68           C  
ANISOU 1380  CE2 PHE A 243     2779   5630   4768   -595    928   1422       C  
ATOM   1381  CZ  PHE A 243      21.782  -8.187  55.891  1.00 30.52           C  
ANISOU 1381  CZ  PHE A 243     2320   5071   4206   -564   1023   1366       C  
ATOM   1382  N   PHE A 244      21.858  -5.988  50.485  1.00 53.41           N  
ANISOU 1382  N   PHE A 244     5065   7762   7467   -248    797   1506       N  
ATOM   1383  CA  PHE A 244      22.402  -7.121  49.744  1.00 43.73           C  
ANISOU 1383  CA  PHE A 244     3958   6439   6219   -408    663   1519       C  
ATOM   1384  C   PHE A 244      23.635  -6.721  48.942  1.00 47.53           C  
ANISOU 1384  C   PHE A 244     4559   6725   6774   -370    621   1498       C  
ATOM   1385  O   PHE A 244      24.682  -7.381  49.016  1.00 60.96           O  
ANISOU 1385  O   PHE A 244     6426   8287   8450   -459    565   1449       O  
ATOM   1386  CB  PHE A 244      21.328  -7.706  48.828  1.00 50.43           C  
ANISOU 1386  CB  PHE A 244     4714   7395   7051   -477    573   1585       C  
ATOM   1387  CG  PHE A 244      20.193  -8.373  49.559  1.00 58.26           C  
ANISOU 1387  CG  PHE A 244     5615   8557   7964   -552    594   1605       C  
ATOM   1388  CD1 PHE A 244      20.425  -9.096  50.720  1.00 54.37           C  
ANISOU 1388  CD1 PHE A 244     5195   8068   7395   -644    625   1563       C  
ATOM   1389  CD2 PHE A 244      18.895  -8.285  49.080  1.00 58.47           C  
ANISOU 1389  CD2 PHE A 244     5487   8736   7992   -535    580   1666       C  
ATOM   1390  CE1 PHE A 244      19.383  -9.719  51.392  1.00 37.35           C  
ANISOU 1390  CE1 PHE A 244     2958   6064   5170   -718    646   1584       C  
ATOM   1391  CE2 PHE A 244      17.850  -8.904  49.749  1.00 60.40           C  
ANISOU 1391  CE2 PHE A 244     5647   9133   8167   -608    601   1685       C  
ATOM   1392  CZ  PHE A 244      18.097  -9.621  50.907  1.00 46.27           C  
ANISOU 1392  CZ  PHE A 244     3931   7344   6305   -700    636   1644       C  
ATOM   1393  N   ILE A 245      23.527  -5.648  48.158  1.00 41.08           N  
ANISOU 1393  N   ILE A 245     3668   5892   6048   -232    642   1525       N  
ATOM   1394  CA  ILE A 245      24.640  -5.239  47.299  1.00 46.85           C  
ANISOU 1394  CA  ILE A 245     4524   6430   6847   -194    593   1496       C  
ATOM   1395  C   ILE A 245      25.899  -4.919  48.101  1.00 53.98           C  
ANISOU 1395  C   ILE A 245     5602   7167   7739   -151    637   1388       C  
ATOM   1396  O   ILE A 245      26.968  -5.466  47.772  1.00 65.81           O  
ANISOU 1396  O   ILE A 245     7250   8516   9237   -237    567   1357       O  
ATOM   1397  CB  ILE A 245      24.205  -4.080  46.389  1.00 38.43           C  
ANISOU 1397  CB  ILE A 245     3382   5365   5855    -33    592   1511       C  
ATOM   1398  CG1 ILE A 245      23.084  -4.531  45.453  1.00 36.56           C  
ANISOU 1398  CG1 ILE A 245     2987   5277   5627   -100    524   1623       C  
ATOM   1399  CG2 ILE A 245      25.382  -3.562  45.588  1.00 44.09           C  
ANISOU 1399  CG2 ILE A 245     4261   5870   6622     18    540   1454       C  
ATOM   1400  CD1 ILE A 245      22.593  -3.443  44.537  1.00 34.49           C  
ANISOU 1400  CD1 ILE A 245     2643   5025   5437     53    512   1650       C  
ATOM   1401  N   PRO A 246      25.861  -4.070  49.136  1.00 43.74           N  
ANISOU 1401  N   PRO A 246     4299   5887   6434    -22    746   1326       N  
ATOM   1402  CA  PRO A 246      27.087  -3.842  49.916  1.00 36.06           C  
ANISOU 1402  CA  PRO A 246     3497   4758   5444      1    778   1226       C  
ATOM   1403  C   PRO A 246      27.607  -5.102  50.580  1.00 36.85           C  
ANISOU 1403  C   PRO A 246     3683   4841   5476   -175    746   1226       C  
ATOM   1404  O   PRO A 246      28.824  -5.269  50.694  1.00 44.33           O  
ANISOU 1404  O   PRO A 246     4792   5626   6425   -206    712   1164       O  
ATOM   1405  CB  PRO A 246      26.659  -2.797  50.956  1.00 40.67           C  
ANISOU 1405  CB  PRO A 246     4028   5407   6019    157    907   1174       C  
ATOM   1406  CG  PRO A 246      25.415  -2.187  50.411  1.00 45.61           C  
ANISOU 1406  CG  PRO A 246     4473   6171   6684    261    932   1234       C  
ATOM   1407  CD  PRO A 246      24.733  -3.281  49.664  1.00 40.70           C  
ANISOU 1407  CD  PRO A 246     3752   5660   6050    108    846   1340       C  
ATOM   1408  N   LEU A 247      26.724  -6.004  51.004  1.00 37.72           N  
ANISOU 1408  N   LEU A 247     3690   5115   5530   -293    750   1296       N  
ATOM   1409  CA  LEU A 247      27.168  -7.262  51.594  1.00 43.38           C  
ANISOU 1409  CA  LEU A 247     4506   5809   6170   -460    698   1286       C  
ATOM   1410  C   LEU A 247      27.994  -8.068  50.600  1.00 41.24           C  
ANISOU 1410  C   LEU A 247     4380   5394   5897   -546    551   1246       C  
ATOM   1411  O   LEU A 247      29.081  -8.561  50.931  1.00 41.91           O  
ANISOU 1411  O   LEU A 247     4626   5349   5947   -593    506   1167       O  
ATOM   1412  CB  LEU A 247      25.957  -8.066  52.074  1.00 52.73           C  
ANISOU 1412  CB  LEU A 247     5587   7180   7270   -551    693   1322       C  
ATOM   1413  CG  LEU A 247      26.126  -9.575  52.267  1.00 57.82           C  
ANISOU 1413  CG  LEU A 247     6341   7800   7827   -717    591   1293       C  
ATOM   1414  CD1 LEU A 247      27.145  -9.889  53.352  1.00 66.24           C  
ANISOU 1414  CD1 LEU A 247     7555   8767   8847   -758    611   1225       C  
ATOM   1415  CD2 LEU A 247      24.789 -10.218  52.587  1.00 54.79           C  
ANISOU 1415  CD2 LEU A 247     5838   7598   7381   -788    596   1341       C  
ATOM   1416  N   THR A 248      27.486  -8.218  49.374  1.00 43.26           N  
ANISOU 1416  N   THR A 248     4580   5678   6179   -557    476   1287       N  
ATOM   1417  CA  THR A 248      28.222  -8.969  48.359  1.00 41.60           C  
ANISOU 1417  CA  THR A 248     4505   5347   5953   -618    348   1231       C  
ATOM   1418  C   THR A 248      29.559  -8.304  48.048  1.00 31.81           C  
ANISOU 1418  C   THR A 248     3395   3927   4765   -543    342   1157       C  
ATOM   1419  O   THR A 248      30.600  -8.978  47.966  1.00 29.88           O  
ANISOU 1419  O   THR A 248     3309   3575   4469   -584    275   1054       O  
ATOM   1420  CB  THR A 248      27.374  -9.095  47.091  1.00 31.43           C  
ANISOU 1420  CB  THR A 248     3124   4130   4686   -631    282   1296       C  
ATOM   1421  OG1 THR A 248      26.128  -9.729  47.410  1.00 27.55           O  
ANISOU 1421  OG1 THR A 248     2519   3808   4141   -700    284   1355       O  
ATOM   1422  CG2 THR A 248      28.094  -9.924  46.040  1.00 29.45           C  
ANISOU 1422  CG2 THR A 248     3012   3772   4407   -685    165   1226       C  
ATOM   1423  N   ILE A 249      29.550  -6.976  47.899  1.00 25.75           N  
ANISOU 1423  N   ILE A 249     2563   3128   4093   -418    422   1198       N  
ATOM   1424  CA  ILE A 249      30.782  -6.254  47.603  1.00 18.09           C  
ANISOU 1424  CA  ILE A 249     1723   1980   3172   -337    419   1120       C  
ATOM   1425  C   ILE A 249      31.796  -6.453  48.720  1.00 17.43           C  
ANISOU 1425  C   ILE A 249     1772   1813   3037   -351    438   1024       C  
ATOM   1426  O   ILE A 249      32.991  -6.659  48.466  1.00 16.24           O  
ANISOU 1426  O   ILE A 249     1771   1554   2847   -355    366    908       O  
ATOM   1427  CB  ILE A 249      30.480  -4.762  47.368  1.00 18.57           C  
ANISOU 1427  CB  ILE A 249     1709   2025   3324   -174    506   1150       C  
ATOM   1428  CG1 ILE A 249      29.553  -4.588  46.163  1.00 19.20           C  
ANISOU 1428  CG1 ILE A 249     1668   2187   3440   -156    462   1231       C  
ATOM   1429  CG2 ILE A 249      31.766  -3.977  47.158  1.00 17.45           C  
ANISOU 1429  CG2 ILE A 249     1716   1691   3225    -90    506   1061       C  
ATOM   1430  CD1 ILE A 249      29.264  -3.147  45.830  1.00 19.72           C  
ANISOU 1430  CD1 ILE A 249     1688   2242   3561     29    511   1214       C  
ATOM   1431  N   MET A 250      31.337  -6.414  49.973  1.00 21.42           N  
ANISOU 1431  N   MET A 250     2219   2395   3525   -358    535   1062       N  
ATOM   1432  CA  MET A 250      32.241  -6.586  51.106  1.00 32.93           C  
ANISOU 1432  CA  MET A 250     3798   3779   4933   -376    555    983       C  
ATOM   1433  C   MET A 250      32.827  -7.989  51.149  1.00 40.41           C  
ANISOU 1433  C   MET A 250     4866   4714   5774   -504    433    907       C  
ATOM   1434  O   MET A 250      34.022  -8.151  51.417  1.00 51.34           O  
ANISOU 1434  O   MET A 250     6394   5998   7115   -505    388    805       O  
ATOM   1435  CB  MET A 250      31.521  -6.252  52.411  1.00 22.58           C  
ANISOU 1435  CB  MET A 250     2402   2583   3595   -347    683   1016       C  
ATOM   1436  CG  MET A 250      31.416  -4.756  52.665  1.00 28.47           C  
ANISOU 1436  CG  MET A 250     3126   3318   4372   -157    776    955       C  
ATOM   1437  SD  MET A 250      30.604  -4.344  54.218  1.00 41.64           S  
ANISOU 1437  SD  MET A 250     4717   5138   5967    -98    909    936       S  
ATOM   1438  CE  MET A 250      29.006  -5.142  53.989  1.00 27.35           C  
ANISOU 1438  CE  MET A 250     2706   3559   4125   -188    908   1056       C  
ATOM   1439  N   VAL A 251      32.010  -9.015  50.895  1.00 23.49           N  
ANISOU 1439  N   VAL A 251     2670   2676   3580   -600    387    946       N  
ATOM   1440  CA  VAL A 251      32.542 -10.379  50.871  1.00 37.12           C  
ANISOU 1440  CA  VAL A 251     4514   4370   5219   -690    306    866       C  
ATOM   1441  C   VAL A 251      33.636 -10.504  49.813  1.00 41.55           C  
ANISOU 1441  C   VAL A 251     5192   4824   5770   -651    238    763       C  
ATOM   1442  O   VAL A 251      34.753 -10.984  50.085  1.00 57.89           O  
ANISOU 1442  O   VAL A 251     7390   6820   7786   -648    225    660       O  
ATOM   1443  CB  VAL A 251      31.411 -11.395  50.626  1.00 17.95           C  
ANISOU 1443  CB  VAL A 251     2002   2058   2760   -774    276    925       C  
ATOM   1444  CG1 VAL A 251      31.991 -12.773  50.371  1.00 20.84           C  
ANISOU 1444  CG1 VAL A 251     2475   2369   3075   -820    207    846       C  
ATOM   1445  CG2 VAL A 251      30.478 -11.438  51.806  1.00 19.22           C  
ANISOU 1445  CG2 VAL A 251     2066   2344   2893   -820    348    997       C  
ATOM   1446  N   ILE A 252      33.333 -10.052  48.592  1.00 26.89           N  
ANISOU 1446  N   ILE A 252     3283   2974   3962   -611    208    791       N  
ATOM   1447  CA  ILE A 252      34.297 -10.168  47.502  1.00 33.09           C  
ANISOU 1447  CA  ILE A 252     4165   3686   4721   -576    157    695       C  
ATOM   1448  C   ILE A 252      35.583  -9.421  47.849  1.00 35.93           C  
ANISOU 1448  C   ILE A 252     4634   3961   5057   -509    170    603       C  
ATOM   1449  O   ILE A 252      36.691  -9.963  47.715  1.00 26.49           O  
ANISOU 1449  O   ILE A 252     3515   2722   3827   -503    139    530       O  
ATOM   1450  CB  ILE A 252      33.677  -9.661  46.188  1.00 33.76           C  
ANISOU 1450  CB  ILE A 252     4167   3795   4864   -546    127    753       C  
ATOM   1451  CG1 ILE A 252      32.446 -10.493  45.825  1.00 23.00           C  
ANISOU 1451  CG1 ILE A 252     2705   2533   3500   -621     95    839       C  
ATOM   1452  CG2 ILE A 252      34.691  -9.724  45.058  1.00 32.17           C  
ANISOU 1452  CG2 ILE A 252     4065   3535   4623   -510     89    651       C  
ATOM   1453  CD1 ILE A 252      31.802 -10.097  44.504  1.00 27.90           C  
ANISOU 1453  CD1 ILE A 252     3244   3187   4170   -602     56    903       C  
ATOM   1454  N   THR A 253      35.450  -8.174  48.326  1.00 29.37           N  
ANISOU 1454  N   THR A 253     3753   3106   4302   -442    211    648       N  
ATOM   1455  CA  THR A 253      36.618  -7.355  48.644  1.00 25.10           C  
ANISOU 1455  CA  THR A 253     3301   2493   3744   -371    209    563       C  
ATOM   1456  C   THR A 253      37.436  -7.973  49.771  1.00 21.04           C  
ANISOU 1456  C   THR A 253     2891   1966   3138   -418    192    502       C  
ATOM   1457  O   THR A 253      38.666  -7.893  49.765  1.00 28.05           O  
ANISOU 1457  O   THR A 253     3843   2811   4003   -386    154    434       O  
ATOM   1458  CB  THR A 253      36.184  -5.930  49.008  1.00 22.99           C  
ANISOU 1458  CB  THR A 253     2948   2190   3599   -264    300    618       C  
ATOM   1459  OG1 THR A 253      35.372  -5.388  47.962  1.00 34.92           O  
ANISOU 1459  OG1 THR A 253     4360   3715   5192   -217    318    689       O  
ATOM   1460  CG2 THR A 253      37.387  -5.024  49.166  1.00 28.23           C  
ANISOU 1460  CG2 THR A 253     3699   2790   4237   -186    288    514       C  
ATOM   1461  N   TYR A 254      36.773  -8.614  50.735  1.00 30.99           N  
ANISOU 1461  N   TYR A 254     4117   3263   4397   -487    230    557       N  
ATOM   1462  CA  TYR A 254      37.480  -9.266  51.834  1.00 29.62           C  
ANISOU 1462  CA  TYR A 254     4045   3074   4136   -538    220    505       C  
ATOM   1463  C   TYR A 254      38.360 -10.398  51.324  1.00 26.62           C  
ANISOU 1463  C   TYR A 254     3706   2671   3737   -538    201    438       C  
ATOM   1464  O   TYR A 254      39.541 -10.514  51.699  1.00 28.13           O  
ANISOU 1464  O   TYR A 254     3946   2833   3911   -501    186    377       O  
ATOM   1465  CB  TYR A 254      36.465  -9.794  52.849  1.00 28.01           C  
ANISOU 1465  CB  TYR A 254     3771   2927   3946   -612    283    585       C  
ATOM   1466  CG  TYR A 254      37.076 -10.442  54.070  1.00 23.35           C  
ANISOU 1466  CG  TYR A 254     3265   2322   3284   -649    293    533       C  
ATOM   1467  CD1 TYR A 254      37.512  -9.671  55.146  1.00 16.62           C  
ANISOU 1467  CD1 TYR A 254     2425   1450   2440   -638    270    559       C  
ATOM   1468  CD2 TYR A 254      37.195 -11.827  54.160  1.00 16.10           C  
ANISOU 1468  CD2 TYR A 254     2329   1400   2386   -644    330    496       C  
ATOM   1469  CE1 TYR A 254      38.067 -10.260  56.272  1.00 18.60           C  
ANISOU 1469  CE1 TYR A 254     2722   1719   2627   -672    219    535       C  
ATOM   1470  CE2 TYR A 254      37.745 -12.424  55.280  1.00 23.83           C  
ANISOU 1470  CE2 TYR A 254     3295   2355   3403   -631    342    498       C  
ATOM   1471  CZ  TYR A 254      38.182 -11.637  56.334  1.00 27.50           C  
ANISOU 1471  CZ  TYR A 254     3775   2796   3880   -581    390    480       C  
ATOM   1472  OH  TYR A 254      38.736 -12.230  57.452  1.00 22.17           O  
ANISOU 1472  OH  TYR A 254     3046   2116   3263   -580    337    526       O  
ATOM   1473  N   PHE A 255      37.808 -11.239  50.450  1.00 21.00           N  
ANISOU 1473  N   PHE A 255     2933   1985   3061   -565    192    469       N  
ATOM   1474  CA  PHE A 255      38.631 -12.334  49.940  1.00 25.52           C  
ANISOU 1474  CA  PHE A 255     3497   2545   3654   -558    137    441       C  
ATOM   1475  C   PHE A 255      39.759 -11.808  49.048  1.00 33.78           C  
ANISOU 1475  C   PHE A 255     4575   3557   4704   -495    111    385       C  
ATOM   1476  O   PHE A 255      40.913 -12.259  49.153  1.00 31.73           O  
ANISOU 1476  O   PHE A 255     4333   3277   4447   -472     88    343       O  
ATOM   1477  CB  PHE A 255      37.754 -13.353  49.214  1.00 14.58           C  
ANISOU 1477  CB  PHE A 255     2050   1216   2275   -612     80    496       C  
ATOM   1478  CG  PHE A 255      37.020 -14.283  50.149  1.00 18.55           C  
ANISOU 1478  CG  PHE A 255     2528   1763   2760   -683     77    545       C  
ATOM   1479  CD1 PHE A 255      37.696 -15.297  50.813  1.00 29.17           C  
ANISOU 1479  CD1 PHE A 255     3905   3097   4082   -705     28    532       C  
ATOM   1480  CD2 PHE A 255      35.661 -14.131  50.381  1.00 32.41           C  
ANISOU 1480  CD2 PHE A 255     4223   3581   4509   -730    118    607       C  
ATOM   1481  CE1 PHE A 255      37.028 -16.148  51.683  1.00 28.50           C  
ANISOU 1481  CE1 PHE A 255     3805   3056   3966   -776     15    579       C  
ATOM   1482  CE2 PHE A 255      34.989 -14.978  51.251  1.00 31.16           C  
ANISOU 1482  CE2 PHE A 255     4039   3476   4326   -799    117    653       C  
ATOM   1483  CZ  PHE A 255      35.674 -15.989  51.902  1.00 26.14           C  
ANISOU 1483  CZ  PHE A 255     3447   2821   3663   -824     63    639       C  
ATOM   1484  N   LEU A 256      39.461 -10.814  48.203  1.00 14.36           N  
ANISOU 1484  N   LEU A 256     2109   1099   2249   -465    107    391       N  
ATOM   1485  CA  LEU A 256      40.516 -10.215  47.395  1.00 16.48           C  
ANISOU 1485  CA  LEU A 256     2401   1343   2518   -407     84    342       C  
ATOM   1486  C   LEU A 256      41.609  -9.608  48.268  1.00 28.25           C  
ANISOU 1486  C   LEU A 256     3954   2805   3975   -372     92    291       C  
ATOM   1487  O   LEU A 256      42.794  -9.647  47.902  1.00 12.96           O  
ANISOU 1487  O   LEU A 256     2029    864   2030   -340     81    244       O  
ATOM   1488  CB  LEU A 256      39.927  -9.164  46.461  1.00 16.96           C  
ANISOU 1488  CB  LEU A 256     2425   1410   2608   -373     75    367       C  
ATOM   1489  CG  LEU A 256      38.971  -9.693  45.397  1.00 14.31           C  
ANISOU 1489  CG  LEU A 256     2026   1110   2300   -404     53    416       C  
ATOM   1490  CD1 LEU A 256      38.539  -8.563  44.487  1.00 23.55           C  
ANISOU 1490  CD1 LEU A 256     3160   2280   3507   -358     53    438       C  
ATOM   1491  CD2 LEU A 256      39.609 -10.806  44.597  1.00 11.76           C  
ANISOU 1491  CD2 LEU A 256     1703    796   1969   -424      6    393       C  
ATOM   1492  N   THR A 257      41.232  -9.062  49.430  1.00 22.38           N  
ANISOU 1492  N   THR A 257     3230   2058   3215   -377     95    308       N  
ATOM   1493  CA  THR A 257      42.209  -8.463  50.329  1.00 24.27           C  
ANISOU 1493  CA  THR A 257     3501   2282   3440   -342     61    275       C  
ATOM   1494  C   THR A 257      43.117  -9.517  50.946  1.00 24.98           C  
ANISOU 1494  C   THR A 257     3633   2382   3476   -360     88    229       C  
ATOM   1495  O   THR A 257      44.337  -9.310  51.040  1.00 21.23           O  
ANISOU 1495  O   THR A 257     3182   1904   2980   -328     68    188       O  
ATOM   1496  CB  THR A 257      41.502  -7.665  51.423  1.00 15.84           C  
ANISOU 1496  CB  THR A 257     2413   1194   2413   -336     77    315       C  
ATOM   1497  OG1 THR A 257      40.808  -6.561  50.832  1.00 34.72           O  
ANISOU 1497  OG1 THR A 257     4749   3582   4860   -274    127    329       O  
ATOM   1498  CG2 THR A 257      42.508  -7.134  52.434  1.00 11.43           C  
ANISOU 1498  CG2 THR A 257     1864    607   1873   -295     63    277       C  
ATOM   1499  N   ILE A 258      42.556 -10.651  51.374  1.00 11.60           N  
ANISOU 1499  N   ILE A 258     1880    688   1841   -387    167    249       N  
ATOM   1500  CA  ILE A 258      43.439 -11.675  51.933  1.00 27.85           C  
ANISOU 1500  CA  ILE A 258     3883   2732   3969   -386    140    248       C  
ATOM   1501  C   ILE A 258      44.397 -12.181  50.859  1.00 21.09           C  
ANISOU 1501  C   ILE A 258     3031   1873   3109   -381     81    225       C  
ATOM   1502  O   ILE A 258      45.576 -12.455  51.137  1.00 20.76           O  
ANISOU 1502  O   ILE A 258     2997   1824   3066   -367     48    198       O  
ATOM   1503  CB  ILE A 258      42.647 -12.825  52.594  1.00 43.48           C  
ANISOU 1503  CB  ILE A 258     5855   4715   5951   -460    116    303       C  
ATOM   1504  CG1 ILE A 258      41.964 -13.716  51.564  1.00 51.22           C  
ANISOU 1504  CG1 ILE A 258     6821   5731   6909   -506     59    335       C  
ATOM   1505  CG2 ILE A 258      41.641 -12.290  53.606  1.00 60.97           C  
ANISOU 1505  CG2 ILE A 258     8053   6941   8170   -468    183    335       C  
ATOM   1506  CD1 ILE A 258      41.238 -14.878  52.179  1.00 61.42           C  
ANISOU 1506  CD1 ILE A 258     8107   7057   8173   -580     17    385       C  
ATOM   1507  N   LYS A 259      43.929 -12.257  49.604  1.00 21.38           N  
ANISOU 1507  N   LYS A 259     3062   1923   3139   -391     63    237       N  
ATOM   1508  CA  LYS A 259      44.831 -12.668  48.522  1.00 27.49           C  
ANISOU 1508  CA  LYS A 259     3829   2712   3905   -376      6    215       C  
ATOM   1509  C   LYS A 259      45.953 -11.652  48.303  1.00 24.78           C  
ANISOU 1509  C   LYS A 259     3500   2353   3562   -324     39    168       C  
ATOM   1510  O   LYS A 259      47.123 -12.028  48.129  1.00 25.99           O  
ANISOU 1510  O   LYS A 259     3652   2514   3711   -311      3    145       O  
ATOM   1511  CB  LYS A 259      44.049 -12.896  47.227  1.00 24.44           C  
ANISOU 1511  CB  LYS A 259     3421   2346   3519   -394    -24    241       C  
ATOM   1512  CG  LYS A 259      43.381 -14.263  47.159  1.00 35.63           C  
ANISOU 1512  CG  LYS A 259     4828   3789   4922   -452    -89    282       C  
ATOM   1513  CD  LYS A 259      42.446 -14.393  45.963  1.00 45.92           C  
ANISOU 1513  CD  LYS A 259     6103   5115   6231   -474   -114    316       C  
ATOM   1514  CE  LYS A 259      41.749 -15.752  45.964  1.00 62.18           C  
ANISOU 1514  CE  LYS A 259     8159   7203   8265   -540   -179    361       C  
ATOM   1515  NZ  LYS A 259      40.777 -15.917  44.842  1.00 69.39           N  
ANISOU 1515  NZ  LYS A 259     9041   8144   9181   -570   -208    400       N  
ATOM   1516  N   SER A 260      45.620 -10.360  48.305  1.00 22.89           N  
ANISOU 1516  N   SER A 260     3283   2119   3296   -294     83    158       N  
ATOM   1517  CA  SER A 260      46.653  -9.345  48.115  1.00 17.81           C  
ANISOU 1517  CA  SER A 260     2671   1481   2617   -254     86    121       C  
ATOM   1518  C   SER A 260      47.675  -9.378  49.244  1.00 32.17           C  
ANISOU 1518  C   SER A 260     4473   3295   4456   -236    113     95       C  
ATOM   1519  O   SER A 260      48.879  -9.224  49.006  1.00 44.74           O  
ANISOU 1519  O   SER A 260     6049   4890   6058   -216    104     70       O  
ATOM   1520  CB  SER A 260      46.022  -7.961  48.008  1.00 21.75           C  
ANISOU 1520  CB  SER A 260     3202   1972   3089   -238     28    139       C  
ATOM   1521  OG  SER A 260      45.160  -7.893  46.890  1.00 46.94           O  
ANISOU 1521  OG  SER A 260     6362   5161   6313   -242     37    164       O  
ATOM   1522  N   LEU A 261      47.219  -9.580  50.481  1.00 16.70           N  
ANISOU 1522  N   LEU A 261     2485   1325   2536   -241    136    108       N  
ATOM   1523  CA  LEU A 261      48.161  -9.633  51.594  1.00 15.82           C  
ANISOU 1523  CA  LEU A 261     2322   1201   2488   -228     98    102       C  
ATOM   1524  C   LEU A 261      49.061 -10.863  51.493  1.00 45.01           C  
ANISOU 1524  C   LEU A 261     6066   4889   6146   -261     47     94       C  
ATOM   1525  O   LEU A 261      50.256 -10.799  51.826  1.00 59.03           O  
ANISOU 1525  O   LEU A 261     7852   6660   7916   -249     28     71       O  
ATOM   1526  CB  LEU A 261      47.407  -9.604  52.919  1.00 15.82           C  
ANISOU 1526  CB  LEU A 261     2296   1185   2528   -242     62    137       C  
ATOM   1527  CG  LEU A 261      46.664  -8.298  53.220  1.00 26.69           C  
ANISOU 1527  CG  LEU A 261     3728   2558   3856   -246    -57    167       C  
ATOM   1528  CD1 LEU A 261      45.946  -8.386  54.557  1.00 34.50           C  
ANISOU 1528  CD1 LEU A 261     4735   3526   4848   -273    -22    192       C  
ATOM   1529  CD2 LEU A 261      47.608  -7.103  53.205  1.00 10.62           C  
ANISOU 1529  CD2 LEU A 261     1737    504   1794   -204    -39    119       C  
ATOM   1530  N   GLN A 262      48.512 -11.995  51.037  1.00 29.51           N  
ANISOU 1530  N   GLN A 262     4120   2930   4164   -300     10    119       N  
ATOM   1531  CA  GLN A 262      49.361 -13.160  50.808  1.00 22.62           C  
ANISOU 1531  CA  GLN A 262     3266   2074   3254   -317    -66    117       C  
ATOM   1532  C   GLN A 262      50.433 -12.856  49.766  1.00 28.14           C  
ANISOU 1532  C   GLN A 262     3956   2782   3953   -287    -73     89       C  
ATOM   1533  O   GLN A 262      51.611 -13.201  49.948  1.00 26.78           O  
ANISOU 1533  O   GLN A 262     3797   2612   3768   -279   -107     74       O  
ATOM   1534  CB  GLN A 262      48.512 -14.355  50.378  1.00 26.24           C  
ANISOU 1534  CB  GLN A 262     3730   2548   3692   -360   -117    151       C  
ATOM   1535  CG  GLN A 262      47.638 -14.913  51.490  1.00 55.71           C  
ANISOU 1535  CG  GLN A 262     7479   6278   7411   -404   -125    184       C  
ATOM   1536  CD  GLN A 262      46.749 -16.052  51.024  1.00 69.40           C  
ANISOU 1536  CD  GLN A 262     9215   8030   9122   -454   -176    223       C  
ATOM   1537  OE1 GLN A 262      46.649 -16.327  49.827  1.00 79.50           O  
ANISOU 1537  OE1 GLN A 262    10482   9321  10401   -454   -200    226       O  
ATOM   1538  NE2 GLN A 262      46.097 -16.723  51.974  1.00 54.58           N  
ANISOU 1538  NE2 GLN A 262     7358   6159   7222   -504   -194    255       N  
ATOM   1539  N   LYS A 263      50.043 -12.196  48.673  1.00 29.54           N  
ANISOU 1539  N   LYS A 263     4116   2964   4145   -272    -40     86       N  
ATOM   1540  CA  LYS A 263      51.017 -11.822  47.649  1.00 23.07           C  
ANISOU 1540  CA  LYS A 263     3289   2152   3323   -249    -41     63       C  
ATOM   1541  C   LYS A 263      52.084 -10.898  48.228  1.00 21.17           C  
ANISOU 1541  C   LYS A 263     3053   1902   3089   -222     -7     34       C  
ATOM   1542  O   LYS A 263      53.270 -10.992  47.878  1.00 10.91           O  
ANISOU 1542  O   LYS A 263     1754    610   1783   -212    -28     18       O  
ATOM   1543  CB  LYS A 263      50.298 -11.163  46.474  1.00 14.75           C  
ANISOU 1543  CB  LYS A 263     2228   1103   2274   -242    -12     67       C  
ATOM   1544  CG  LYS A 263      51.209 -10.626  45.400  1.00 13.58           C  
ANISOU 1544  CG  LYS A 263     2077    962   2121   -222     -7     46       C  
ATOM   1545  CD  LYS A 263      51.889 -11.750  44.663  1.00 30.48           C  
ANISOU 1545  CD  LYS A 263     4209   3115   4256   -232    -64     46       C  
ATOM   1546  CE  LYS A 263      52.734 -11.206  43.526  1.00 49.92           C  
ANISOU 1546  CE  LYS A 263     6667   5583   6718   -215    -52     27       C  
ATOM   1547  NZ  LYS A 263      53.204 -12.292  42.624  1.00 65.91           N  
ANISOU 1547  NZ  LYS A 263     8688   7615   8740   -226    -99     29       N  
ATOM   1548  N   GLU A 264      51.674  -9.996  49.119  1.00 16.17           N  
ANISOU 1548  N   GLU A 264     2414   1266   2464   -208     37     32       N  
ATOM   1549  CA  GLU A 264      52.623  -9.097  49.763  1.00 10.56           C  
ANISOU 1549  CA  GLU A 264     1695    556   1761   -183     57      9       C  
ATOM   1550  C   GLU A 264      53.667  -9.884  50.555  1.00 13.71           C  
ANISOU 1550  C   GLU A 264     2115    938   2157   -196     13      2       C  
ATOM   1551  O   GLU A 264      54.878  -9.647  50.427  1.00 21.11           O  
ANISOU 1551  O   GLU A 264     3055   1876   3089   -185      5    -17       O  
ATOM   1552  CB  GLU A 264      51.854  -8.118  50.659  1.00  9.86           C  
ANISOU 1552  CB  GLU A 264     1556    463   1726   -162     78     15       C  
ATOM   1553  CG  GLU A 264      52.617  -6.888  51.091  1.00  9.86           C  
ANISOU 1553  CG  GLU A 264     1521    458   1765   -134    -21      7       C  
ATOM   1554  CD  GLU A 264      51.704  -5.760  51.547  1.00 13.18           C  
ANISOU 1554  CD  GLU A 264     2036    857   2113   -130    -72     19       C  
ATOM   1555  OE1 GLU A 264      50.547  -5.689  51.073  1.00 10.01           O  
ANISOU 1555  OE1 GLU A 264     1660    454   1688   -136    -65     39       O  
ATOM   1556  OE2 GLU A 264      52.146  -4.937  52.373  1.00 20.34           O  
ANISOU 1556  OE2 GLU A 264     2967   1743   3019   -115    -44     -2       O  
ATOM   1557  N   ALA A 265      53.211 -10.854  51.354  1.00 11.78           N  
ANISOU 1557  N   ALA A 265     1888    686   1901   -222    -22     21       N  
ATOM   1558  CA  ALA A 265      54.144 -11.655  52.147  1.00 24.41           C  
ANISOU 1558  CA  ALA A 265     3516   2286   3474   -232    -77     19       C  
ATOM   1559  C   ALA A 265      55.067 -12.486  51.258  1.00 27.88           C  
ANISOU 1559  C   ALA A 265     3956   2739   3899   -232   -127     17       C  
ATOM   1560  O   ALA A 265      56.254 -12.673  51.571  1.00 29.39           O  
ANISOU 1560  O   ALA A 265     4156   2927   4083   -224   -157      5       O  
ATOM   1561  CB  ALA A 265      53.378 -12.554  53.113  1.00 30.09           C  
ANISOU 1561  CB  ALA A 265     4262   3000   4171   -265   -109     45       C  
ATOM   1562  N   ALA A1001      54.535 -13.003  50.148  1.00 11.42           N  
ANISOU 1562  N   ALA A1001     1861    666   1814   -240   -139     28       N  
ATOM   1563  CA  ALA A1001      55.360 -13.779  49.226  1.00 10.20           C  
ANISOU 1563  CA  ALA A1001     1703    519   1655   -237   -184     25       C  
ATOM   1564  C   ALA A1001      56.467 -12.923  48.628  1.00 36.52           C  
ANISOU 1564  C   ALA A1001     5020   3855   5003   -211   -155     -1       C  
ATOM   1565  O   ALA A1001      57.637 -13.332  48.578  1.00 35.92           O  
ANISOU 1565  O   ALA A1001     4944   3776   4927   -204   -187    -11       O  
ATOM   1566  CB  ALA A1001      54.486 -14.375  48.120  1.00 10.21           C  
ANISOU 1566  CB  ALA A1001     1696    529   1654   -252   -197     42       C  
ATOM   1567  N   ASP A1002      56.112 -11.719  48.171  1.00 19.44           N  
ANISOU 1567  N   ASP A1002     2843   1694   2851   -198    -96    -12       N  
ATOM   1568  CA  ASP A1002      57.117 -10.827  47.609  1.00 20.76           C  
ANISOU 1568  CA  ASP A1002     3001   1861   3023   -180    -67    -34       C  
ATOM   1569  C   ASP A1002      58.165 -10.462  48.649  1.00 15.72           C  
ANISOU 1569  C   ASP A1002     2372   1214   2387   -172    -69    -48       C  
ATOM   1570  O   ASP A1002      59.364 -10.400  48.338  1.00  9.88           O  
ANISOU 1570  O   ASP A1002     1629    475   1651   -164    -81    -61       O  
ATOM   1571  CB  ASP A1002      56.452  -9.576  47.045  1.00 16.47           C  
ANISOU 1571  CB  ASP A1002     2459   1318   2483   -171     -6    -38       C  
ATOM   1572  CG  ASP A1002      55.517  -9.887  45.902  1.00 33.70           C  
ANISOU 1572  CG  ASP A1002     4633   3509   4661   -178    -10    -24       C  
ATOM   1573  OD1 ASP A1002      55.419 -11.075  45.527  1.00 22.66           O  
ANISOU 1573  OD1 ASP A1002     3228   2119   3264   -192    -57    -12       O  
ATOM   1574  OD2 ASP A1002      54.887  -8.942  45.376  1.00 42.87           O  
ANISOU 1574  OD2 ASP A1002     5797   4681   5809   -169     22    -21       O  
ATOM   1575  N   LEU A1003      57.736 -10.245  49.897  1.00  9.81           N  
ANISOU 1575  N   LEU A1003     1634    454   1639   -175    -60    -44       N  
ATOM   1576  CA  LEU A1003      58.698  -9.937  50.949  1.00 16.06           C  
ANISOU 1576  CA  LEU A1003     2437   1234   2430   -170    -69    -57       C  
ATOM   1577  C   LEU A1003      59.686 -11.080  51.147  1.00 12.95           C  
ANISOU 1577  C   LEU A1003     2052    841   2027   -175   -138    -53       C  
ATOM   1578  O   LEU A1003      60.899 -10.850  51.259  1.00 27.76           O  
ANISOU 1578  O   LEU A1003     3926   2713   3909   -166   -150    -67       O  
ATOM   1579  CB  LEU A1003      57.970  -9.636  52.255  1.00 18.78           C  
ANISOU 1579  CB  LEU A1003     2794   1565   2777   -175    -55    -51       C  
ATOM   1580  CG  LEU A1003      58.885  -9.282  53.424  1.00 22.59           C  
ANISOU 1580  CG  LEU A1003     3294   2034   3256   -172    -68    -63       C  
ATOM   1581  CD1 LEU A1003      59.616  -7.977  53.159  1.00 20.88           C  
ANISOU 1581  CD1 LEU A1003     3062   1810   3060   -155    -26    -87       C  
ATOM   1582  CD2 LEU A1003      58.082  -9.194  54.697  1.00 20.72           C  
ANISOU 1582  CD2 LEU A1003     3076   1783   3014   -182    -65    -55       C  
ATOM   1583  N   GLU A1004      59.191 -12.319  51.189  1.00 14.64           N  
ANISOU 1583  N   GLU A1004     2276   1058   2229   -190   -186    -33       N  
ATOM   1584  CA  GLU A1004      60.097 -13.458  51.314  1.00 13.70           C  
ANISOU 1584  CA  GLU A1004     2166    933   2107   -194   -254    -28       C  
ATOM   1585  C   GLU A1004      61.077 -13.496  50.150  1.00 14.74           C  
ANISOU 1585  C   GLU A1004     2273   1070   2259   -179   -257    -42       C  
ATOM   1586  O   GLU A1004      62.265 -13.796  50.333  1.00 14.20           O  
ANISOU 1586  O   GLU A1004     2201    992   2202   -170   -292    -51       O  
ATOM   1587  CB  GLU A1004      59.303 -14.765  51.399  1.00 27.93           C  
ANISOU 1587  CB  GLU A1004     3987   2733   3891   -216   -303     -2       C  
ATOM   1588  CG  GLU A1004      60.165 -16.031  51.438  1.00 36.09           C  
ANISOU 1588  CG  GLU A1004     5033   3756   4925   -219   -377      6       C  
ATOM   1589  CD  GLU A1004      59.406 -17.270  51.912  1.00 45.31           C  
ANISOU 1589  CD  GLU A1004     6234   4915   6066   -247   -431     35       C  
ATOM   1590  OE1 GLU A1004      58.715 -17.202  52.951  1.00 46.48           O  
ANISOU 1590  OE1 GLU A1004     6409   5061   6191   -266   -430     49       O  
ATOM   1591  OE2 GLU A1004      59.503 -18.319  51.241  1.00 55.29           O  
ANISOU 1591  OE2 GLU A1004     7501   6172   7332   -254   -474     45       O  
ATOM   1592  N   ASP A1005      60.597 -13.181  48.944  1.00 17.51           N  
ANISOU 1592  N   ASP A1005     2606   1432   2616   -177   -222    -45       N  
ATOM   1593  CA  ASP A1005      61.477 -13.188  47.776  1.00 19.91           C  
ANISOU 1593  CA  ASP A1005     2890   1738   2936   -166   -219    -59       C  
ATOM   1594  C   ASP A1005      62.601 -12.171  47.927  1.00 29.76           C  
ANISOU 1594  C   ASP A1005     4129   2983   4194   -152   -194    -80       C  
ATOM   1595  O   ASP A1005      63.772 -12.466  47.637  1.00 49.29           O  
ANISOU 1595  O   ASP A1005     6592   5451   6687   -145   -218    -92       O  
ATOM   1596  CB  ASP A1005      60.660 -12.910  46.517  1.00 31.28           C  
ANISOU 1596  CB  ASP A1005     4320   3190   4373   -169   -184    -57       C  
ATOM   1597  CG  ASP A1005      61.491 -12.956  45.265  1.00 41.83           C  
ANISOU 1597  CG  ASP A1005     5643   4527   5724   -163   -178    -71       C  
ATOM   1598  OD1 ASP A1005      61.885 -14.065  44.860  1.00 52.36           O  
ANISOU 1598  OD1 ASP A1005     6976   5853   7067   -166   -218    -69       O  
ATOM   1599  OD2 ASP A1005      61.747 -11.883  44.685  1.00 51.79           O  
ANISOU 1599  OD2 ASP A1005     6900   5794   6985   -156   -134    -83       O  
ATOM   1600  N   ASN A1006      62.262 -10.965  48.382  1.00 34.86           N  
ANISOU 1600  N   ASN A1006     4783   3630   4832   -150   -146    -86       N  
ATOM   1601  CA  ASN A1006      63.282  -9.939  48.574  1.00 20.76           C  
ANISOU 1601  CA  ASN A1006     2997   1838   3052   -141   -123   -104       C  
ATOM   1602  C   ASN A1006      64.287 -10.368  49.630  1.00 28.55           C  
ANISOU 1602  C   ASN A1006     3986   2812   4048   -138   -170   -108       C  
ATOM   1603  O   ASN A1006      65.492 -10.122  49.492  1.00 36.59           O  
ANISOU 1603  O   ASN A1006     4994   3826   5083   -131   -179   -123       O  
ATOM   1604  CB  ASN A1006      62.631  -8.617  48.972  1.00 16.63           C  
ANISOU 1604  CB  ASN A1006     2490   1312   2517   -140    -65   -108       C  
ATOM   1605  CG  ASN A1006      61.802  -8.020  47.857  1.00 32.71           C  
ANISOU 1605  CG  ASN A1006     4529   3357   4543   -140    -22   -105       C  
ATOM   1606  OD1 ASN A1006      62.121  -8.189  46.678  1.00 35.70           O  
ANISOU 1606  OD1 ASN A1006     4899   3744   4921   -139    -29   -106       O  
ATOM   1607  ND2 ASN A1006      60.719  -7.323  48.222  1.00 12.27           N  
ANISOU 1607  ND2 ASN A1006     1946    775   1942   -137     14    -98       N  
ATOM   1608  N   TRP A1007      63.812 -11.025  50.690  1.00 26.26           N  
ANISOU 1608  N   TRP A1007     3714   2517   3748   -146   -203    -95       N  
ATOM   1609  CA  TRP A1007      64.741 -11.502  51.710  1.00 33.99           C  
ANISOU 1609  CA  TRP A1007     4702   3481   4732   -144   -257    -95       C  
ATOM   1610  C   TRP A1007      65.697 -12.536  51.133  1.00 37.66           C  
ANISOU 1610  C   TRP A1007     5148   3942   5220   -137   -310    -97       C  
ATOM   1611  O   TRP A1007      66.898 -12.523  51.441  1.00 41.86           O  
ANISOU 1611  O   TRP A1007     5670   4462   5772   -128   -339   -108       O  
ATOM   1612  CB  TRP A1007      63.989 -12.096  52.897  1.00 32.51           C  
ANISOU 1612  CB  TRP A1007     4545   3287   4521   -157   -287    -77       C  
ATOM   1613  CG  TRP A1007      64.915 -12.780  53.857  1.00 35.33           C  
ANISOU 1613  CG  TRP A1007     4919   3628   4879   -157   -355    -73       C  
ATOM   1614  CD1 TRP A1007      65.677 -12.189  54.820  1.00 31.50           C  
ANISOU 1614  CD1 TRP A1007     4446   3130   4394   -154   -363    -82       C  
ATOM   1615  CD2 TRP A1007      65.216 -14.180  53.910  1.00 60.26           C  
ANISOU 1615  CD2 TRP A1007     8081   6775   8039   -161   -429    -58       C  
ATOM   1616  NE1 TRP A1007      66.412 -13.135  55.490  1.00 46.93           N  
ANISOU 1616  NE1 TRP A1007     6412   5068   6350   -155   -440    -73       N  
ATOM   1617  CE2 TRP A1007      66.151 -14.367  54.948  1.00 63.03           C  
ANISOU 1617  CE2 TRP A1007     8448   7108   8393   -158   -481    -58       C  
ATOM   1618  CE3 TRP A1007      64.779 -15.296  53.185  1.00 66.48           C  
ANISOU 1618  CE3 TRP A1007     8866   7564   8829   -167   -458    -44       C  
ATOM   1619  CZ2 TRP A1007      66.658 -15.625  55.282  1.00 63.79           C  
ANISOU 1619  CZ2 TRP A1007     8555   7186   8495   -160   -563    -44       C  
ATOM   1620  CZ3 TRP A1007      65.279 -16.545  53.519  1.00 62.13           C  
ANISOU 1620  CZ3 TRP A1007     8329   6995   8283   -169   -535    -31       C  
ATOM   1621  CH2 TRP A1007      66.209 -16.698  54.558  1.00 68.65           C  
ANISOU 1621  CH2 TRP A1007     9169   7802   9114   -165   -588    -32       C  
ATOM   1622  N   GLU A1008      65.177 -13.449  50.306  1.00 26.27           N  
ANISOU 1622  N   GLU A1008     3700   2504   3779   -142   -325    -86       N  
ATOM   1623  CA  GLU A1008      66.040 -14.432  49.655  1.00 25.35           C  
ANISOU 1623  CA  GLU A1008     3566   2378   3689   -134   -369    -91       C  
ATOM   1624  C   GLU A1008      67.120 -13.751  48.825  1.00 32.02           C  
ANISOU 1624  C   GLU A1008     4381   3224   4562   -121   -341   -115       C  
ATOM   1625  O   GLU A1008      68.292 -14.151  48.864  1.00 41.56           O  
ANISOU 1625  O   GLU A1008     5571   4418   5801   -111   -378   -126       O  
ATOM   1626  CB  GLU A1008      65.214 -15.362  48.765  1.00 23.84           C  
ANISOU 1626  CB  GLU A1008     3377   2189   3491   -144   -377    -78       C  
ATOM   1627  CG  GLU A1008      64.412 -16.413  49.500  1.00 24.82           C  
ANISOU 1627  CG  GLU A1008     3533   2306   3594   -159   -427    -53       C  
ATOM   1628  CD  GLU A1008      65.154 -17.718  49.613  1.00 27.95           C  
ANISOU 1628  CD  GLU A1008     3935   2677   4007   -157   -499    -49       C  
ATOM   1629  OE1 GLU A1008      66.400 -17.707  49.502  1.00 33.18           O  
ANISOU 1629  OE1 GLU A1008     4576   3327   4702   -140   -515    -67       O  
ATOM   1630  OE2 GLU A1008      64.491 -18.757  49.805  1.00 35.83           O  
ANISOU 1630  OE2 GLU A1008     4961   3666   4988   -173   -541    -27       O  
ATOM   1631  N   THR A1009      66.742 -12.722  48.065  1.00 43.83           N  
ANISOU 1631  N   THR A1009     5871   4735   6048   -123   -278   -122       N  
ATOM   1632  CA  THR A1009      67.731 -12.008  47.260  1.00 45.24           C  
ANISOU 1632  CA  THR A1009     6028   4915   6247   -115   -251   -142       C  
ATOM   1633  C   THR A1009      68.799 -11.361  48.144  1.00 10.90           C  
ANISOU 1633  C   THR A1009     1674    555   1912   -108   -262   -155       C  
ATOM   1634  O   THR A1009      70.005 -11.446  47.860  1.00 11.11           O  
ANISOU 1634  O   THR A1009     1675    573   1972   -100   -279   -171       O  
ATOM   1635  CB  THR A1009      67.038 -10.969  46.379  1.00 35.82           C  
ANISOU 1635  CB  THR A1009     4842   3736   5032   -120   -188   -143       C  
ATOM   1636  OG1 THR A1009      66.272 -11.638  45.370  1.00 34.03           O  
ANISOU 1636  OG1 THR A1009     4616   3516   4799   -126   -184   -135       O  
ATOM   1637  CG2 THR A1009      68.056 -10.074  45.706  1.00 10.40           C  
ANISOU 1637  CG2 THR A1009     1610    516   1825   -116   -163   -162       C  
ATOM   1638  N   LEU A1010      68.370 -10.714  49.228  1.00 10.85           N  
ANISOU 1638  N   LEU A1010     1692    548   1883   -113   -250   -150       N  
ATOM   1639  CA  LEU A1010      69.318 -10.074  50.135  1.00 31.30           C  
ANISOU 1639  CA  LEU A1010     4284   3125   4482   -109   -261   -161       C  
ATOM   1640  C   LEU A1010      70.302 -11.081  50.707  1.00 23.62           C  
ANISOU 1640  C   LEU A1010     3297   2137   3540   -101   -333   -163       C  
ATOM   1641  O   LEU A1010      71.508 -10.813  50.775  1.00 11.67           O  
ANISOU 1641  O   LEU A1010     1763    614   2057    -93   -349   -179       O  
ATOM   1642  CB  LEU A1010      68.575  -9.363  51.263  1.00 11.00           C  
ANISOU 1642  CB  LEU A1010     1748    551   1881   -117   -238   -155       C  
ATOM   1643  CG  LEU A1010      67.923  -8.044  50.867  1.00 10.74           C  
ANISOU 1643  CG  LEU A1010     1731    524   1827   -122   -165   -160       C  
ATOM   1644  CD1 LEU A1010      67.025  -7.568  51.976  1.00 10.74           C  
ANISOU 1644  CD1 LEU A1010     1760    516   1805   -128   -142   -155       C  
ATOM   1645  CD2 LEU A1010      68.989  -7.004  50.554  1.00 16.33           C  
ANISOU 1645  CD2 LEU A1010     2436   1225   2545   -119   -144   -179       C  
ATOM   1646  N   ASN A1011      69.807 -12.248  51.121  1.00 19.49           N  
ANISOU 1646  N   ASN A1011     2785   1609   3010   -103   -380   -146       N  
ATOM   1647  CA  ASN A1011      70.691 -13.245  51.715  1.00 28.41           C  
ANISOU 1647  CA  ASN A1011     3908   2719   4167    -95   -456   -144       C  
ATOM   1648  C   ASN A1011      71.672 -13.799  50.690  1.00 21.59           C  
ANISOU 1648  C   ASN A1011     3004   1849   3352    -82   -473   -161       C  
ATOM   1649  O   ASN A1011      72.878 -13.923  50.970  1.00 13.53           O  
ANISOU 1649  O   ASN A1011     1959    812   2370    -70   -512   -175       O  
ATOM   1650  CB  ASN A1011      69.870 -14.378  52.326  1.00 42.93           C  
ANISOU 1650  CB  ASN A1011     5777   4551   5982   -104   -504   -119       C  
ATOM   1651  CG  ASN A1011      70.161 -14.576  53.797  1.00 57.62           C  
ANISOU 1651  CG  ASN A1011     7666   6394   7831   -107   -560   -109       C  
ATOM   1652  OD1 ASN A1011      70.546 -13.637  54.497  1.00 62.05           O  
ANISOU 1652  OD1 ASN A1011     8236   6953   8387   -107   -544   -118       O  
ATOM   1653  ND2 ASN A1011      69.983 -15.804  54.278  1.00 54.17           N  
ANISOU 1653  ND2 ASN A1011     7251   5942   7388   -112   -627    -90       N  
ATOM   1654  N   ASP A1012      71.176 -14.130  49.494  1.00 13.89           N  
ANISOU 1654  N   ASP A1012     2018    882   2375    -84   -444   -161       N  
ATOM   1655  CA  ASP A1012      72.058 -14.665  48.464  1.00 30.03           C  
ANISOU 1655  CA  ASP A1012     4028   2918   4465    -74   -453   -180       C  
ATOM   1656  C   ASP A1012      73.194 -13.705  48.179  1.00 42.28           C  
ANISOU 1656  C   ASP A1012     5547   4470   6047    -66   -427   -204       C  
ATOM   1657  O   ASP A1012      74.376 -14.085  48.189  1.00 53.82           O  
ANISOU 1657  O   ASP A1012     6977   5915   7559    -53   -463   -222       O  
ATOM   1658  CB  ASP A1012      71.278 -14.940  47.180  1.00 28.41           C  
ANISOU 1658  CB  ASP A1012     3826   2723   4246    -81   -414   -177       C  
ATOM   1659  CG  ASP A1012      70.373 -16.129  47.298  1.00 31.57           C  
ANISOU 1659  CG  ASP A1012     4252   3115   4627    -89   -450   -156       C  
ATOM   1660  OD1 ASP A1012      70.347 -16.754  48.384  1.00 32.78           O  
ANISOU 1660  OD1 ASP A1012     4424   3256   4777    -88   -506   -142       O  
ATOM   1661  OD2 ASP A1012      69.698 -16.440  46.294  1.00 33.74           O  
ANISOU 1661  OD2 ASP A1012     4534   3395   4890    -96   -424   -153       O  
ATOM   1662  N   ASN A1013      72.856 -12.439  47.954  1.00 38.59           N  
ANISOU 1662  N   ASN A1013     5089   4020   5553    -74   -367   -206       N  
ATOM   1663  CA  ASN A1013      73.903 -11.514  47.568  1.00 13.35           C  
ANISOU 1663  CA  ASN A1013     1866    822   2383    -71   -340   -229       C  
ATOM   1664  C   ASN A1013      74.800 -11.155  48.744  1.00 12.22           C  
ANISOU 1664  C   ASN A1013     1718    666   2259    -66   -375   -236       C  
ATOM   1665  O   ASN A1013      75.985 -10.887  48.536  1.00 12.46           O  
ANISOU 1665  O   ASN A1013     1714    688   2333    -59   -381   -258       O  
ATOM   1666  CB  ASN A1013      73.280 -10.297  46.904  1.00 15.61           C  
ANISOU 1666  CB  ASN A1013     2171   1127   2633    -83   -272   -227       C  
ATOM   1667  CG  ASN A1013      72.780 -10.612  45.500  1.00 20.66           C  
ANISOU 1667  CG  ASN A1013     2806   1776   3266    -87   -241   -227       C  
ATOM   1668  OD1 ASN A1013      73.565 -10.666  44.553  1.00 24.15           O  
ANISOU 1668  OD1 ASN A1013     3221   2215   3741    -84   -231   -244       O  
ATOM   1669  ND2 ASN A1013      71.479 -10.859  45.366  1.00 17.16           N  
ANISOU 1669  ND2 ASN A1013     2391   1343   2785    -94   -228   -207       N  
ATOM   1670  N   LEU A1014      74.292 -11.208  49.982  1.00 13.67           N  
ANISOU 1670  N   LEU A1014     1935    845   2414    -69   -402   -220       N  
ATOM   1671  CA  LEU A1014      75.175 -11.060  51.139  1.00 12.58           C  
ANISOU 1671  CA  LEU A1014     1796    689   2294    -64   -447   -226       C  
ATOM   1672  C   LEU A1014      76.257 -12.132  51.145  1.00 26.36           C  
ANISOU 1672  C   LEU A1014     3502   2415   4098    -47   -515   -236       C  
ATOM   1673  O   LEU A1014      77.440 -11.838  51.365  1.00 13.34           O  
ANISOU 1673  O   LEU A1014     1824    753   2491    -39   -536   -256       O  
ATOM   1674  CB  LEU A1014      74.368 -11.122  52.437  1.00 25.55           C  
ANISOU 1674  CB  LEU A1014     3487   2328   3894    -73   -468   -204       C  
ATOM   1675  CG  LEU A1014      73.884  -9.815  53.070  1.00 32.87           C  
ANISOU 1675  CG  LEU A1014     4451   3258   4779    -86   -418   -204       C  
ATOM   1676  CD1 LEU A1014      73.224 -10.097  54.415  1.00 26.65           C  
ANISOU 1676  CD1 LEU A1014     3708   2463   3957    -94   -449   -186       C  
ATOM   1677  CD2 LEU A1014      75.026  -8.806  53.231  1.00 17.45           C  
ANISOU 1677  CD2 LEU A1014     2486   1293   2849    -85   -408   -226       C  
ATOM   1678  N   LYS A1015      75.872 -13.389  50.900  1.00 30.27           N  
ANISOU 1678  N   LYS A1015     3998   2905   4599    -43   -551   -226       N  
ATOM   1679  CA  LYS A1015      76.877 -14.452  50.854  1.00 26.79           C  
ANISOU 1679  CA  LYS A1015     3522   2441   4217    -25   -617   -238       C  
ATOM   1680  C   LYS A1015      77.864 -14.237  49.708  1.00 18.51           C  
ANISOU 1680  C   LYS A1015     2419   1391   3224    -16   -587   -270       C  
ATOM   1681  O   LYS A1015      79.086 -14.403  49.878  1.00 21.56           O  
ANISOU 1681  O   LYS A1015     2764   1758   3668     -2   -625   -291       O  
ATOM   1682  CB  LYS A1015      76.200 -15.813  50.727  1.00 22.14           C  
ANISOU 1682  CB  LYS A1015     2952   1842   3619    -25   -656   -221       C  
ATOM   1683  CG  LYS A1015      75.375 -16.224  51.940  1.00 22.84           C  
ANISOU 1683  CG  LYS A1015     3092   1926   3662    -35   -700   -190       C  
ATOM   1684  CD  LYS A1015      74.759 -17.597  51.722  1.00 33.13           C  
ANISOU 1684  CD  LYS A1015     4416   3215   4958    -37   -740   -174       C  
ATOM   1685  CE  LYS A1015      73.746 -17.945  52.802  1.00 44.69           C  
ANISOU 1685  CE  LYS A1015     5935   4678   6366    -53   -772   -141       C  
ATOM   1686  NZ  LYS A1015      73.068 -19.261  52.547  1.00 42.21           N  
ANISOU 1686  NZ  LYS A1015     5647   4350   6042    -60   -810   -123       N  
ATOM   1687  N   VAL A1016      77.353 -13.844  48.537  1.00 37.20           N  
ANISOU 1687  N   VAL A1016     4784   3777   5572    -25   -519   -273       N  
ATOM   1688  CA  VAL A1016      78.234 -13.566  47.404  1.00 13.50           C  
ANISOU 1688  CA  VAL A1016     1736    775   2616    -21   -484   -303       C  
ATOM   1689  C   VAL A1016      79.247 -12.486  47.764  1.00 28.17           C  
ANISOU 1689  C   VAL A1016     3570   2633   4501    -20   -473   -322       C  
ATOM   1690  O   VAL A1016      80.432 -12.586  47.423  1.00 30.88           O  
ANISOU 1690  O   VAL A1016     3862   2963   4907     -9   -485   -351       O  
ATOM   1691  CB  VAL A1016      77.416 -13.172  46.163  1.00 13.08           C  
ANISOU 1691  CB  VAL A1016     1699    743   2528    -35   -413   -300       C  
ATOM   1692  CG1 VAL A1016      78.339 -12.673  45.083  1.00 13.19           C  
ANISOU 1692  CG1 VAL A1016     1671    758   2582    -34   -372   -329       C  
ATOM   1693  CG2 VAL A1016      76.616 -14.349  45.666  1.00 39.92           C  
ANISOU 1693  CG2 VAL A1016     5117   4138   5914    -35   -426   -287       C  
ATOM   1694  N   ILE A1017      78.801 -11.435  48.451  1.00 24.65           N  
ANISOU 1694  N   ILE A1017     3160   2198   4009    -32   -450   -308       N  
ATOM   1695  CA  ILE A1017      79.734 -10.402  48.885  1.00 27.60           C  
ANISOU 1695  CA  ILE A1017     3521   2565   4402    -34   -443   -325       C  
ATOM   1696  C   ILE A1017      80.758 -10.993  49.841  1.00 38.22           C  
ANISOU 1696  C   ILE A1017     4839   3885   5798    -18   -520   -335       C  
ATOM   1697  O   ILE A1017      81.959 -10.704  49.749  1.00 29.56           O  
ANISOU 1697  O   ILE A1017     3697   2777   4756    -12   -528   -362       O  
ATOM   1698  CB  ILE A1017      78.980  -9.224  49.525  1.00 13.18           C  
ANISOU 1698  CB  ILE A1017     1749    748   2512    -51   -406   -309       C  
ATOM   1699  CG1 ILE A1017      78.097  -8.528  48.493  1.00 12.95           C  
ANISOU 1699  CG1 ILE A1017     1741    739   2440    -65   -334   -303       C  
ATOM   1700  CG2 ILE A1017      79.962  -8.237  50.116  1.00 13.44           C  
ANISOU 1700  CG2 ILE A1017     1777    767   2563    -55   -407   -326       C  
ATOM   1701  CD1 ILE A1017      77.235  -7.424  49.076  1.00 19.02           C  
ANISOU 1701  CD1 ILE A1017     2566   1513   3148    -80   -296   -289       C  
ATOM   1702  N   GLU A1018      80.300 -11.852  50.759  1.00 43.57           N  
ANISOU 1702  N   GLU A1018     5542   4553   6458    -13   -579   -314       N  
ATOM   1703  CA  GLU A1018      81.214 -12.463  51.721  1.00 32.78           C  
ANISOU 1703  CA  GLU A1018     4157   3160   5137      3   -662   -319       C  
ATOM   1704  C   GLU A1018      82.353 -13.174  51.015  1.00 28.19           C  
ANISOU 1704  C   GLU A1018     3508   2563   4638     22   -689   -349       C  
ATOM   1705  O   GLU A1018      83.475 -13.216  51.532  1.00 19.51           O  
ANISOU 1705  O   GLU A1018     2375   1444   3595     35   -739   -367       O  
ATOM   1706  CB  GLU A1018      80.466 -13.441  52.627  1.00 33.37           C  
ANISOU 1706  CB  GLU A1018     4275   3226   5179      4   -723   -289       C  
ATOM   1707  CG  GLU A1018      81.348 -14.156  53.638  1.00 46.65           C  
ANISOU 1707  CG  GLU A1018     5945   4876   6903     19   -819   -290       C  
ATOM   1708  CD  GLU A1018      80.600 -15.231  54.412  1.00 72.73           C  
ANISOU 1708  CD  GLU A1018     9295   8168  10173     18   -882   -259       C  
ATOM   1709  OE1 GLU A1018      79.348 -15.216  54.401  1.00 79.20           O  
ANISOU 1709  OE1 GLU A1018    10160   9005  10929      2   -847   -236       O  
ATOM   1710  OE2 GLU A1018      81.267 -16.100  55.019  1.00 72.33           O  
ANISOU 1710  OE2 GLU A1018     9234   8088  10160     32   -970   -259       O  
ATOM   1711  N   LYS A1019      82.099 -13.724  49.831  1.00 37.45           N  
ANISOU 1711  N   LYS A1019     4662   3743   5823     24   -658   -358       N  
ATOM   1712  CA  LYS A1019      83.196 -14.423  49.163  1.00 36.79           C  
ANISOU 1712  CA  LYS A1019     4515   3641   5823     41   -680   -392       C  
ATOM   1713  C   LYS A1019      83.495 -13.866  47.772  1.00 46.26           C  
ANISOU 1713  C   LYS A1019     5680   4856   7043     34   -601   -418       C  
ATOM   1714  O   LYS A1019      83.383 -14.589  46.779  1.00 62.56           O  
ANISOU 1714  O   LYS A1019     7729   6916   9124     37   -584   -430       O  
ATOM   1715  CB  LYS A1019      82.881 -15.920  49.087  1.00 20.01           C  
ANISOU 1715  CB  LYS A1019     2398   1496   3710     53   -734   -385       C  
ATOM   1716  CG  LYS A1019      82.754 -16.570  50.454  1.00 22.29           C  
ANISOU 1716  CG  LYS A1019     2718   1764   3987     60   -822   -360       C  
ATOM   1717  CD  LYS A1019      82.212 -17.983  50.375  1.00 43.62           C  
ANISOU 1717  CD  LYS A1019     5444   4446   6685     66   -870   -347       C  
ATOM   1718  CE  LYS A1019      81.973 -18.552  51.770  1.00 63.71           C  
ANISOU 1718  CE  LYS A1019     8031   6970   9205     68   -956   -318       C  
ATOM   1719  NZ  LYS A1019      81.437 -19.946  51.744  1.00 71.23           N  
ANISOU 1719  NZ  LYS A1019     9014   7898  10150     70  -1008   -303       N  
ATOM   1720  N   ALA A1020      83.938 -12.611  47.687  1.00 45.05           N  
ANISOU 1720  N   ALA A1020     5514   4713   6888     23   -555   -430       N  
ATOM   1721  CA  ALA A1020      84.176 -11.951  46.410  1.00 28.94           C  
ANISOU 1721  CA  ALA A1020     3450   2688   4858     12   -479   -452       C  
ATOM   1722  C   ALA A1020      85.632 -11.531  46.254  1.00 25.86           C  
ANISOU 1722  C   ALA A1020     2995   2286   4544     18   -477   -493       C  
ATOM   1723  O   ALA A1020      86.308 -11.182  47.226  1.00 26.87           O  
ANISOU 1723  O   ALA A1020     3113   2401   4695     23   -518   -498       O  
ATOM   1724  CB  ALA A1020      83.281 -10.718  46.249  1.00 14.51           C  
ANISOU 1724  CB  ALA A1020     1674    884   2954    -11   -414   -430       C  
ATOM   1725  N   ASP A1021      86.094 -11.530  45.001  1.00 31.78           N  
ANISOU 1725  N   ASP A1021     3704   3040   5331     14   -427   -523       N  
ATOM   1726  CA  ASP A1021      87.469 -11.194  44.643  1.00 37.00           C  
ANISOU 1726  CA  ASP A1021     4296   3691   6070     17   -414   -568       C  
ATOM   1727  C   ASP A1021      87.649  -9.713  44.337  1.00 37.38           C  
ANISOU 1727  C   ASP A1021     4356   3754   6093     -6   -348   -573       C  
ATOM   1728  O   ASP A1021      88.556  -9.075  44.874  1.00 38.94           O  
ANISOU 1728  O   ASP A1021     4529   3942   6326     -7   -360   -591       O  
ATOM   1729  CB  ASP A1021      87.924 -12.006  43.425  1.00 46.89           C  
ANISOU 1729  CB  ASP A1021     5498   4938   7379     23   -389   -604       C  
ATOM   1730  CG  ASP A1021      88.491 -13.349  43.796  1.00 59.84           C  
ANISOU 1730  CG  ASP A1021     7099   6550   9087     50   -464   -623       C  
ATOM   1731  OD1 ASP A1021      89.241 -13.411  44.792  1.00 64.66           O  
ANISOU 1731  OD1 ASP A1021     7681   7144   9743     66   -527   -631       O  
ATOM   1732  OD2 ASP A1021      88.204 -14.334  43.080  1.00 73.66           O  
ANISOU 1732  OD2 ASP A1021     8850   8292  10846     56   -462   -630       O  
ATOM   1733  N   ASN A1022      86.810  -9.164  43.468  1.00 39.22           N  
ANISOU 1733  N   ASN A1022     4628   4007   6266    -26   -282   -557       N  
ATOM   1734  CA  ASN A1022      87.001  -7.845  42.884  1.00 43.28           C  
ANISOU 1734  CA  ASN A1022     5153   4532   6759    -50   -215   -566       C  
ATOM   1735  C   ASN A1022      85.827  -6.930  43.222  1.00 36.90           C  
ANISOU 1735  C   ASN A1022     4425   3737   5858    -67   -194   -525       C  
ATOM   1736  O   ASN A1022      84.825  -7.351  43.805  1.00 40.35           O  
ANISOU 1736  O   ASN A1022     4905   4178   6247    -61   -223   -492       O  
ATOM   1737  CB  ASN A1022      87.165  -7.972  41.369  1.00 47.61           C  
ANISOU 1737  CB  ASN A1022     5673   5088   7327    -60   -153   -591       C  
ATOM   1738  CG  ASN A1022      86.096  -8.852  40.749  1.00 36.37           C  
ANISOU 1738  CG  ASN A1022     4279   3674   5866    -57   -149   -569       C  
ATOM   1739  OD1 ASN A1022      85.045  -8.368  40.332  1.00 51.31           O  
ANISOU 1739  OD1 ASN A1022     6226   5581   7687    -71   -115   -540       O  
ATOM   1740  ND2 ASN A1022      86.349 -10.154  40.707  1.00 21.17           N  
ANISOU 1740  ND2 ASN A1022     2319   1735   3988    -37   -188   -584       N  
ATOM   1741  N   ALA A1023      85.950  -5.664  42.813  1.00 24.40           N  
ANISOU 1741  N   ALA A1023     2864   2158   4250    -90   -142   -530       N  
ATOM   1742  CA  ALA A1023      84.912  -4.680  43.095  1.00 21.92           C  
ANISOU 1742  CA  ALA A1023     2625   1851   3852   -107   -121   -496       C  
ATOM   1743  C   ALA A1023      83.683  -4.845  42.207  1.00 35.12           C  
ANISOU 1743  C   ALA A1023     4331   3542   5470   -111    -88   -472       C  
ATOM   1744  O   ALA A1023      82.586  -4.434  42.605  1.00 26.94           O  
ANISOU 1744  O   ALA A1023     3355   2513   4368   -116    -87   -440       O  
ATOM   1745  CB  ALA A1023      85.467  -3.265  42.939  1.00 32.99           C  
ANISOU 1745  CB  ALA A1023     4045   3244   5245   -131    -82   -510       C  
ATOM   1746  N   ALA A1024      83.832  -5.427  41.012  1.00 25.41           N  
ANISOU 1746  N   ALA A1024     3068   2319   4268   -110    -60   -488       N  
ATOM   1747  CA  ALA A1024      82.681  -5.566  40.123  1.00 17.21           C  
ANISOU 1747  CA  ALA A1024     2065   1296   3177   -116    -31   -465       C  
ATOM   1748  C   ALA A1024      81.665  -6.543  40.692  1.00 35.30           C  
ANISOU 1748  C   ALA A1024     4382   3592   5439   -102    -72   -437       C  
ATOM   1749  O   ALA A1024      80.455  -6.282  40.661  1.00 41.38           O  
ANISOU 1749  O   ALA A1024     5204   4373   6145   -107    -63   -407       O  
ATOM   1750  CB  ALA A1024      83.129  -6.010  38.733  1.00 13.73           C  
ANISOU 1750  CB  ALA A1024     1587    857   2772   -121      9   -492       C  
ATOM   1751  N   GLN A1025      82.144  -7.674  41.214  1.00 34.05           N  
ANISOU 1751  N   GLN A1025     4187   3422   5327    -83   -121   -448       N  
ATOM   1752  CA  GLN A1025      81.258  -8.642  41.848  1.00 34.46           C  
ANISOU 1752  CA  GLN A1025     4265   3475   5354    -71   -165   -422       C  
ATOM   1753  C   GLN A1025      80.522  -8.012  43.024  1.00 29.86           C  
ANISOU 1753  C   GLN A1025     3732   2896   4717    -74   -182   -393       C  
ATOM   1754  O   GLN A1025      79.298  -8.158  43.164  1.00 31.48           O  
ANISOU 1754  O   GLN A1025     3982   3111   4867    -77   -181   -364       O  
ATOM   1755  CB  GLN A1025      82.079  -9.852  42.306  1.00 45.74           C  
ANISOU 1755  CB  GLN A1025     5646   4884   6849    -51   -221   -441       C  
ATOM   1756  CG  GLN A1025      81.294 -10.936  43.024  1.00 52.66           C  
ANISOU 1756  CG  GLN A1025     6549   5755   7704    -39   -275   -416       C  
ATOM   1757  CD  GLN A1025      80.381 -11.701  42.091  1.00 54.15           C  
ANISOU 1757  CD  GLN A1025     6763   5948   7864    -43   -257   -405       C  
ATOM   1758  OE1 GLN A1025      80.836 -12.529  41.301  1.00 70.64           O  
ANISOU 1758  OE1 GLN A1025     8823   8024   9994    -37   -257   -428       O  
ATOM   1759  NE2 GLN A1025      79.086 -11.419  42.167  1.00 42.09           N  
ANISOU 1759  NE2 GLN A1025     5289   4436   6266    -53   -241   -373       N  
ATOM   1760  N   VAL A1026      81.258  -7.283  43.868  1.00 14.97           N  
ANISOU 1760  N   VAL A1026     1840   1000   2847    -76   -195   -402       N  
ATOM   1761  CA  VAL A1026      80.652  -6.632  45.024  1.00 15.36           C  
ANISOU 1761  CA  VAL A1026     1942   1050   2847    -81   -207   -380       C  
ATOM   1762  C   VAL A1026      79.592  -5.635  44.581  1.00 26.42           C  
ANISOU 1762  C   VAL A1026     3396   2463   4180    -97   -157   -360       C  
ATOM   1763  O   VAL A1026      78.505  -5.562  45.170  1.00 23.38           O  
ANISOU 1763  O   VAL A1026     3057   2083   3742    -99   -160   -335       O  
ATOM   1764  CB  VAL A1026      81.735  -5.958  45.882  1.00 13.43           C  
ANISOU 1764  CB  VAL A1026     1685    787   2631    -83   -226   -397       C  
ATOM   1765  CG1 VAL A1026      81.102  -5.277  47.083  1.00 13.29           C  
ANISOU 1765  CG1 VAL A1026     1728    764   2559    -91   -235   -377       C  
ATOM   1766  CG2 VAL A1026      82.774  -6.983  46.317  1.00 15.63           C  
ANISOU 1766  CG2 VAL A1026     1906   1050   2982    -63   -284   -417       C  
ATOM   1767  N   LYS A1027      79.887  -4.852  43.540  1.00 17.28           N  
ANISOU 1767  N   LYS A1027     2232   1308   3024   -109   -111   -372       N  
ATOM   1768  CA  LYS A1027      78.916  -3.872  43.075  1.00 12.71           C  
ANISOU 1768  CA  LYS A1027     1705    739   2386   -123    -71   -354       C  
ATOM   1769  C   LYS A1027      77.676  -4.554  42.523  1.00 26.86           C  
ANISOU 1769  C   LYS A1027     3515   2547   4144   -119    -67   -332       C  
ATOM   1770  O   LYS A1027      76.556  -4.082  42.743  1.00 26.63           O  
ANISOU 1770  O   LYS A1027     3533   2523   4060   -122    -57   -309       O  
ATOM   1771  CB  LYS A1027      79.533  -2.952  42.021  1.00 14.32           C  
ANISOU 1771  CB  LYS A1027     1898    939   2602   -137    -29   -372       C  
ATOM   1772  CG  LYS A1027      78.510  -2.010  41.399  1.00 29.46           C  
ANISOU 1772  CG  LYS A1027     3867   2864   4463   -148      4   -352       C  
ATOM   1773  CD  LYS A1027      79.124  -0.968  40.483  1.00 48.50           C  
ANISOU 1773  CD  LYS A1027     6276   5268   6883   -165     43   -368       C  
ATOM   1774  CE  LYS A1027      78.035  -0.043  39.935  1.00 53.81           C  
ANISOU 1774  CE  LYS A1027     6999   5943   7501   -172     64   -346       C  
ATOM   1775  NZ  LYS A1027      78.564   1.124  39.170  1.00 46.61           N  
ANISOU 1775  NZ  LYS A1027     6097   5020   6593   -191     97   -358       N  
ATOM   1776  N   ASP A1028      77.850  -5.667  41.808  1.00 22.32           N  
ANISOU 1776  N   ASP A1028     2904   1976   3600   -111    -74   -340       N  
ATOM   1777  CA  ASP A1028      76.697  -6.361  41.243  1.00 19.31           C  
ANISOU 1777  CA  ASP A1028     2544   1607   3186   -110    -71   -320       C  
ATOM   1778  C   ASP A1028      75.795  -6.908  42.344  1.00 22.25           C  
ANISOU 1778  C   ASP A1028     2945   1981   3529   -104   -104   -297       C  
ATOM   1779  O   ASP A1028      74.564  -6.718  42.324  1.00 25.17           O  
ANISOU 1779  O   ASP A1028     3354   2361   3849   -108    -92   -275       O  
ATOM   1780  CB  ASP A1028      77.175  -7.477  40.318  1.00 12.53           C  
ANISOU 1780  CB  ASP A1028     1648    745   2369   -105    -74   -337       C  
ATOM   1781  CG  ASP A1028      76.040  -8.235  39.696  1.00 20.06           C  
ANISOU 1781  CG  ASP A1028     2628   1705   3288   -107    -72   -319       C  
ATOM   1782  OD1 ASP A1028      75.194  -7.597  39.038  1.00 41.63           O  
ANISOU 1782  OD1 ASP A1028     5392   4448   5976   -117    -43   -304       O  
ATOM   1783  OD2 ASP A1028      75.997  -9.468  39.854  1.00 27.99           O  
ANISOU 1783  OD2 ASP A1028     3623   2702   4310    -98   -104   -319       O  
ATOM   1784  N   ALA A1029      76.401  -7.572  43.332  1.00 21.33           N  
ANISOU 1784  N   ALA A1029     2806   1853   3444    -93   -147   -304       N  
ATOM   1785  CA  ALA A1029      75.626  -8.090  44.455  1.00 29.78           C  
ANISOU 1785  CA  ALA A1029     3903   2923   4489    -89   -179   -283       C  
ATOM   1786  C   ALA A1029      74.949  -6.959  45.227  1.00 41.84           C  
ANISOU 1786  C   ALA A1029     5476   4453   5967    -98   -159   -270       C  
ATOM   1787  O   ALA A1029      73.790  -7.091  45.647  1.00 30.38           O  
ANISOU 1787  O   ALA A1029     4059   3009   4476   -100   -156   -249       O  
ATOM   1788  CB  ALA A1029      76.523  -8.913  45.374  1.00 12.09           C  
ANISOU 1788  CB  ALA A1029     1633    667   2295    -76   -236   -294       C  
ATOM   1789  N   LEU A1030      75.641  -5.826  45.398  1.00 22.06           N  
ANISOU 1789  N   LEU A1030     2975   1940   3466   -104   -141   -282       N  
ATOM   1790  CA  LEU A1030      75.033  -4.705  46.101  1.00 12.13           C  
ANISOU 1790  CA  LEU A1030     1769    678   2162   -113   -119   -272       C  
ATOM   1791  C   LEU A1030      73.898  -4.077  45.301  1.00 13.19           C  
ANISOU 1791  C   LEU A1030     1937    823   2250   -119    -81   -257       C  
ATOM   1792  O   LEU A1030      72.912  -3.622  45.889  1.00 11.49           O  
ANISOU 1792  O   LEU A1030     1766    608   1993   -122    -69   -243       O  
ATOM   1793  CB  LEU A1030      76.087  -3.656  46.442  1.00 14.27           C  
ANISOU 1793  CB  LEU A1030     2043    932   2447   -120   -113   -290       C  
ATOM   1794  CG  LEU A1030      76.946  -3.935  47.675  1.00 25.05           C  
ANISOU 1794  CG  LEU A1030     3396   2280   3841   -116   -153   -301       C  
ATOM   1795  CD1 LEU A1030      78.053  -2.887  47.838  1.00 14.71           C  
ANISOU 1795  CD1 LEU A1030     2088    952   2549   -126   -145   -322       C  
ATOM   1796  CD2 LEU A1030      76.067  -3.979  48.909  1.00 28.43           C  
ANISOU 1796  CD2 LEU A1030     3869   2705   4230   -117   -163   -284       C  
ATOM   1797  N   THR A1031      74.004  -4.049  43.973  1.00 11.38           N  
ANISOU 1797  N   THR A1031     1689    603   2031   -121    -63   -261       N  
ATOM   1798  CA  THR A1031      72.912  -3.533  43.151  1.00 18.63           C  
ANISOU 1798  CA  THR A1031     2636   1531   2911   -125    -38   -246       C  
ATOM   1799  C   THR A1031      71.662  -4.387  43.320  1.00 37.20           C  
ANISOU 1799  C   THR A1031     5002   3895   5237   -121    -46   -226       C  
ATOM   1800  O   THR A1031      70.546  -3.867  43.517  1.00 29.21           O  
ANISOU 1800  O   THR A1031     4027   2885   4185   -123    -34   -210       O  
ATOM   1801  CB  THR A1031      73.344  -3.500  41.684  1.00 15.34           C  
ANISOU 1801  CB  THR A1031     2192   1120   2515   -129    -20   -256       C  
ATOM   1802  OG1 THR A1031      74.543  -2.726  41.551  1.00 18.38           O  
ANISOU 1802  OG1 THR A1031     2561   1494   2929   -134     -8   -276       O  
ATOM   1803  CG2 THR A1031      72.261  -2.905  40.826  1.00 10.69           C  
ANISOU 1803  CG2 THR A1031     1631    540   1891   -132     -1   -240       C  
ATOM   1804  N   LYS A1032      71.839  -5.711  43.258  1.00 30.83           N  
ANISOU 1804  N   LYS A1032     4166   3092   4455   -117    -68   -228       N  
ATOM   1805  CA  LYS A1032      70.712  -6.606  43.494  1.00 19.44           C  
ANISOU 1805  CA  LYS A1032     2736   1657   2992   -116    -78   -210       C  
ATOM   1806  C   LYS A1032      70.128  -6.388  44.884  1.00 20.87           C  
ANISOU 1806  C   LYS A1032     2945   1835   3151   -116    -83   -200       C  
ATOM   1807  O   LYS A1032      68.902  -6.302  45.045  1.00 10.23           O  
ANISOU 1807  O   LYS A1032     1623    493   1771   -119    -68   -185       O  
ATOM   1808  CB  LYS A1032      71.156  -8.055  43.320  1.00 16.08           C  
ANISOU 1808  CB  LYS A1032     2280   1229   2602   -110   -111   -216       C  
ATOM   1809  CG  LYS A1032      71.479  -8.440  41.886  1.00 10.69           C  
ANISOU 1809  CG  LYS A1032     1578    547   1936   -112   -100   -225       C  
ATOM   1810  CD  LYS A1032      71.932  -9.877  41.803  1.00 13.66           C  
ANISOU 1810  CD  LYS A1032     1930    913   2347   -106   -134   -233       C  
ATOM   1811  CE  LYS A1032      72.172 -10.287  40.370  1.00 28.11           C  
ANISOU 1811  CE  LYS A1032     3750   2741   4190   -110   -117   -244       C  
ATOM   1812  NZ  LYS A1032      73.117  -9.361  39.705  1.00 39.34           N  
ANISOU 1812  NZ  LYS A1032     5152   4163   5633   -112    -89   -263       N  
ATOM   1813  N   MET A1033      70.999  -6.254  45.893  1.00 31.31           N  
ANISOU 1813  N   MET A1033     4260   3144   4492   -113   -102   -211       N  
ATOM   1814  CA  MET A1033      70.544  -6.025  47.260  1.00 24.74           C  
ANISOU 1814  CA  MET A1033     3456   2304   3640   -115   -105   -204       C  
ATOM   1815  C   MET A1033      69.759  -4.732  47.373  1.00 12.30           C  
ANISOU 1815  C   MET A1033     1926    725   2023   -121    -61   -199       C  
ATOM   1816  O   MET A1033      68.755  -4.667  48.092  1.00 10.47           O  
ANISOU 1816  O   MET A1033     1720    492   1767   -123    -46   -188       O  
ATOM   1817  CB  MET A1033      71.734  -5.980  48.218  1.00 18.48           C  
ANISOU 1817  CB  MET A1033     2652   1496   2875   -112   -135   -218       C  
ATOM   1818  CG  MET A1033      72.341  -7.331  48.518  1.00 29.48           C  
ANISOU 1818  CG  MET A1033     4010   2885   4306   -103   -192   -219       C  
ATOM   1819  SD  MET A1033      73.749  -7.233  49.643  1.00 45.10           S  
ANISOU 1819  SD  MET A1033     5975   4843   6319    -98   -236   -235       S  
ATOM   1820  CE  MET A1033      72.935  -6.519  51.068  1.00 11.63           C  
ANISOU 1820  CE  MET A1033     1790    595   2035   -108   -221   -225       C  
ATOM   1821  N   ARG A1034      70.221  -3.684  46.696  1.00 10.61           N  
ANISOU 1821  N   ARG A1034     1722    505   1803   -123    -45   -207       N  
ATOM   1822  CA  ARG A1034      69.550  -2.394  46.794  1.00 10.57           C  
ANISOU 1822  CA  ARG A1034     1768    491   1758   -125    -21   -201       C  
ATOM   1823  C   ARG A1034      68.147  -2.486  46.229  1.00 16.34           C  
ANISOU 1823  C   ARG A1034     2506   1241   2462   -120    -14   -182       C  
ATOM   1824  O   ARG A1034      67.180  -2.047  46.863  1.00 10.26           O  
ANISOU 1824  O   ARG A1034     1761    477   1660   -115     -8   -170       O  
ATOM   1825  CB  ARG A1034      70.358  -1.328  46.060  1.00 10.73           C  
ANISOU 1825  CB  ARG A1034     1788    501   1786   -126    -21   -212       C  
ATOM   1826  CG  ARG A1034      70.004   0.087  46.428  1.00 24.12           C  
ANISOU 1826  CG  ARG A1034     3523   2187   3453   -122    -22   -208       C  
ATOM   1827  CD  ARG A1034      70.458   1.065  45.354  1.00 22.51           C  
ANISOU 1827  CD  ARG A1034     3311   1972   3268   -123    -23   -216       C  
ATOM   1828  NE  ARG A1034      70.228   2.447  45.765  1.00 16.48           N  
ANISOU 1828  NE  ARG A1034     2571   1193   2499   -116    -35   -217       N  
ATOM   1829  CZ  ARG A1034      69.130   3.135  45.473  1.00 17.87           C  
ANISOU 1829  CZ  ARG A1034     2742   1368   2678   -104    -39   -208       C  
ATOM   1830  NH1 ARG A1034      68.165   2.568  44.764  1.00 24.52           N  
ANISOU 1830  NH1 ARG A1034     3568   2231   3518    -99    -32   -195       N  
ATOM   1831  NH2 ARG A1034      68.999   4.385  45.887  1.00 27.99           N  
ANISOU 1831  NH2 ARG A1034     4032   2627   3978    -97    -43   -217       N  
ATOM   1832  N   ALA A1035      68.013  -3.105  45.053  1.00 19.96           N  
ANISOU 1832  N   ALA A1035     2941   1710   2934   -121    -18   -179       N  
ATOM   1833  CA  ALA A1035      66.683  -3.270  44.479  1.00  9.91           C  
ANISOU 1833  CA  ALA A1035     1672    454   1639   -118    -14   -161       C  
ATOM   1834  C   ALA A1035      65.784  -4.077  45.409  1.00 23.69           C  
ANISOU 1834  C   ALA A1035     3421   2206   3373   -120     -8   -151       C  
ATOM   1835  O   ALA A1035      64.624  -3.710  45.646  1.00  9.73           O  
ANISOU 1835  O   ALA A1035     1670    447   1578   -115     -1   -137       O  
ATOM   1836  CB  ALA A1035      66.779  -3.928  43.108  1.00  9.81           C  
ANISOU 1836  CB  ALA A1035     1634    450   1643   -122    -17   -161       C  
ATOM   1837  N   ALA A1036      66.316  -5.161  45.976  1.00 17.01           N  
ANISOU 1837  N   ALA A1036     2555   1352   2555   -124    -19   -158       N  
ATOM   1838  CA  ALA A1036      65.515  -5.998  46.861  1.00 12.96           C  
ANISOU 1838  CA  ALA A1036     2038    841   2045   -126    -22   -148       C  
ATOM   1839  C   ALA A1036      65.063  -5.227  48.098  1.00 17.04           C  
ANISOU 1839  C   ALA A1036     2577   1353   2546   -125      2   -147       C  
ATOM   1840  O   ALA A1036      63.887  -5.268  48.470  1.00 17.90           O  
ANISOU 1840  O   ALA A1036     2688   1470   2642   -125     20   -136       O  
ATOM   1841  CB  ALA A1036      66.312  -7.240  47.266  1.00 23.33           C  
ANISOU 1841  CB  ALA A1036     3319   2154   3391   -125    -69   -152       C  
ATOM   1842  N   ALA A1037      65.986  -4.524  48.757  1.00 14.39           N  
ANISOU 1842  N   ALA A1037     2252   1003   2213   -124      3   -160       N  
ATOM   1843  CA  ALA A1037      65.626  -3.787  49.961  1.00 15.81           C  
ANISOU 1843  CA  ALA A1037     2447   1177   2383   -123     31   -163       C  
ATOM   1844  C   ALA A1037      64.635  -2.669  49.656  1.00 27.46           C  
ANISOU 1844  C   ALA A1037     3958   2665   3809   -117     61   -152       C  
ATOM   1845  O   ALA A1037      63.709  -2.418  50.443  1.00 29.35           O  
ANISOU 1845  O   ALA A1037     4178   2906   4068   -114    106   -152       O  
ATOM   1846  CB  ALA A1037      66.880  -3.223  50.625  1.00 15.76           C  
ANISOU 1846  CB  ALA A1037     2448   1150   2389   -126     24   -180       C  
ATOM   1847  N   LEU A1038      64.799  -1.997  48.512  1.00 15.46           N  
ANISOU 1847  N   LEU A1038     2465   1148   2259   -108     10   -144       N  
ATOM   1848  CA  LEU A1038      63.836  -0.971  48.135  1.00 13.35           C  
ANISOU 1848  CA  LEU A1038     2184    879   2007    -84    -72   -135       C  
ATOM   1849  C   LEU A1038      62.451  -1.565  47.933  1.00 18.18           C  
ANISOU 1849  C   LEU A1038     2781   1505   2622    -81    -79   -119       C  
ATOM   1850  O   LEU A1038      61.453  -0.999  48.397  1.00 10.01           O  
ANISOU 1850  O   LEU A1038     1702    459   1640    -67    -95   -119       O  
ATOM   1851  CB  LEU A1038      64.292  -0.259  46.863  1.00 16.32           C  
ANISOU 1851  CB  LEU A1038     2537   1250   2412    -82    -63   -142       C  
ATOM   1852  CG  LEU A1038      63.614   1.079  46.561  1.00 21.29           C  
ANISOU 1852  CG  LEU A1038     3142   1863   3085    -67    -58   -147       C  
ATOM   1853  CD1 LEU A1038      63.836   2.071  47.696  1.00 29.85           C  
ANISOU 1853  CD1 LEU A1038     4228   2921   4194    -59    -60   -162       C  
ATOM   1854  CD2 LEU A1038      64.122   1.632  45.240  1.00 10.29           C  
ANISOU 1854  CD2 LEU A1038     1745    465   1701    -72    -39   -152       C  
ATOM   1855  N   ASP A1039      62.372  -2.721  47.266  1.00 26.79           N  
ANISOU 1855  N   ASP A1039     3883   2612   3685   -100    -22   -113       N  
ATOM   1856  CA  ASP A1039      61.072  -3.349  47.057  1.00  9.58           C  
ANISOU 1856  CA  ASP A1039     1699    444   1498   -102    -18    -98       C  
ATOM   1857  C   ASP A1039      60.474  -3.815  48.375  1.00 13.83           C  
ANISOU 1857  C   ASP A1039     2253    981   2022   -110     29    -96       C  
ATOM   1858  O   ASP A1039      59.269  -3.653  48.610  1.00 16.41           O  
ANISOU 1858  O   ASP A1039     2562   1306   2367    -94    -90    -77       O  
ATOM   1859  CB  ASP A1039      61.204  -4.517  46.081  1.00 36.49           C  
ANISOU 1859  CB  ASP A1039     5072   3862   4929   -116     19    -99       C  
ATOM   1860  CG  ASP A1039      59.864  -5.126  45.707  1.00 61.46           C  
ANISOU 1860  CG  ASP A1039     8226   7034   8091   -121     26    -85       C  
ATOM   1861  OD1 ASP A1039      58.824  -4.460  45.910  1.00 75.01           O  
ANISOU 1861  OD1 ASP A1039     9965   8751   9785   -112     -5    -71       O  
ATOM   1862  OD2 ASP A1039      59.850  -6.277  45.215  1.00 65.70           O  
ANISOU 1862  OD2 ASP A1039     8731   7574   8659   -131     29    -85       O  
ATOM   1863  N   ALA A1040      61.309  -4.334  49.276  1.00 11.71           N  
ANISOU 1863  N   ALA A1040     1917    702   1830   -117     87   -117       N  
ATOM   1864  CA  ALA A1040      60.795  -4.882  50.522  1.00  9.89           C  
ANISOU 1864  CA  ALA A1040     1634    460   1663   -118     84   -118       C  
ATOM   1865  C   ALA A1040      60.396  -3.805  51.516  1.00 15.07           C  
ANISOU 1865  C   ALA A1040     2211   1103   2411    -97     48   -127       C  
ATOM   1866  O   ALA A1040      59.604  -4.083  52.423  1.00 11.90           O  
ANISOU 1866  O   ALA A1040     1822    689   2009    -98     17   -117       O  
ATOM   1867  CB  ALA A1040      61.829  -5.809  51.156  1.00 10.68           C  
ANISOU 1867  CB  ALA A1040     1752    542   1763   -128     36   -124       C  
ATOM   1868  N   GLY A1041      60.876  -2.575  51.341  1.00 32.90           N  
ANISOU 1868  N   GLY A1041     4463   3354   4685    -75    -54   -133       N  
ATOM   1869  CA  GLY A1041      60.401  -1.501  52.195  1.00 33.56           C  
ANISOU 1869  CA  GLY A1041     4614   3408   4730    -67    -66   -136       C  
ATOM   1870  C   GLY A1041      58.947  -1.162  51.941  1.00 28.60           C  
ANISOU 1870  C   GLY A1041     4021   2772   4072    -60    -53   -121       C  
ATOM   1871  O   GLY A1041      58.256  -0.657  52.835  1.00 10.60           O  
ANISOU 1871  O   GLY A1041     1772    467   1788    -55    -24   -125       O  
ATOM   1872  N   SER A1042      58.463  -1.448  50.726  1.00 29.47           N  
ANISOU 1872  N   SER A1042     4130   2903   4166    -60    -65   -105       N  
ATOM   1873  CA  SER A1042      57.098  -1.134  50.299  1.00 10.34           C  
ANISOU 1873  CA  SER A1042     1723    473   1733    -54    -38    -92       C  
ATOM   1874  C   SER A1042      56.723   0.315  50.607  1.00 10.42           C  
ANISOU 1874  C   SER A1042     1759    451   1747    -35      8   -104       C  
ATOM   1875  O   SER A1042      55.580   0.620  50.945  1.00 10.55           O  
ANISOU 1875  O   SER A1042     1786    463   1760    -24     44    -96       O  
ATOM   1876  CB  SER A1042      56.089  -2.099  50.915  1.00 12.60           C  
ANISOU 1876  CB  SER A1042     2002    763   2023    -65    -43    -76       C  
ATOM   1877  OG  SER A1042      54.910  -2.124  50.136  1.00 10.69           O  
ANISOU 1877  OG  SER A1042     1766    525   1772    -63    -31    -58       O  
ATOM   1878  N   GLY A1043      57.691   1.216  50.494  1.00 10.58           N  
ANISOU 1878  N   GLY A1043     1789    462   1770    -29     14   -121       N  
ATOM   1879  CA  GLY A1043      57.447   2.637  50.576  1.00 10.94           C  
ANISOU 1879  CA  GLY A1043     1855    488   1812    -10     60   -130       C  
ATOM   1880  C   GLY A1043      57.751   3.270  51.911  1.00 20.87           C  
ANISOU 1880  C   GLY A1043     3142   1722   3066     -4     80   -147       C  
ATOM   1881  O   GLY A1043      57.563   4.486  52.057  1.00 23.00           O  
ANISOU 1881  O   GLY A1043     3437   1970   3331     14    117   -157       O  
ATOM   1882  N   SER A1044      58.224   2.493  52.888  1.00 11.28           N  
ANISOU 1882  N   SER A1044     1926    508   1851    -17     57   -153       N  
ATOM   1883  CA  SER A1044      58.331   3.021  54.242  1.00 25.43           C  
ANISOU 1883  CA  SER A1044     3753   2277   3632    -13     81   -169       C  
ATOM   1884  C   SER A1044      59.323   4.170  54.324  1.00 42.06           C  
ANISOU 1884  C   SER A1044     5881   4362   5739     -8     88   -190       C  
ATOM   1885  O   SER A1044      59.154   5.076  55.147  1.00 51.78           O  
ANISOU 1885  O   SER A1044     7153   5567   6954      3    121   -203       O  
ATOM   1886  CB  SER A1044      58.740   1.916  55.202  1.00 20.48           C  
ANISOU 1886  CB  SER A1044     3119   1653   3008    -33     52   -170       C  
ATOM   1887  OG  SER A1044      60.135   1.688  55.103  1.00 37.61           O  
ANISOU 1887  OG  SER A1044     5267   3821   5200    -44     17   -182       O  
ATOM   1888  N   GLY A1045      60.348   4.163  53.478  1.00 50.12           N  
ANISOU 1888  N   GLY A1045     6878   5388   6777    -17     58   -193       N  
ATOM   1889  CA  GLY A1045      61.389   5.166  53.566  1.00 51.58           C  
ANISOU 1889  CA  GLY A1045     7082   5551   6967    -17     60   -212       C  
ATOM   1890  C   GLY A1045      62.336   4.842  54.700  1.00 73.50           C  
ANISOU 1890  C   GLY A1045     9863   8315   9749    -30     40   -229       C  
ATOM   1891  O   GLY A1045      62.175   5.337  55.819  1.00 70.57           O  
ANISOU 1891  O   GLY A1045     9532   7922   9358    -27     63   -241       O  
ATOM   1892  N   ASP A1066      63.321   3.996  54.425  1.00 89.10           N  
ANISOU 1892  N   ASP A1066    11799  10301  11754    -44     -1   -230       N  
ATOM   1893  CA  ASP A1066      64.216   3.501  55.455  1.00 95.37           C  
ANISOU 1893  CA  ASP A1066    12585  11088  12562    -59    -14   -243       C  
ATOM   1894  C   ASP A1066      65.651   3.926  55.196  1.00 83.99           C  
ANISOU 1894  C   ASP A1066    11128   9644  11142    -66    -28   -259       C  
ATOM   1895  O   ASP A1066      66.027   4.327  54.091  1.00 83.94           O  
ANISOU 1895  O   ASP A1066    11108   9646  11139    -63    -40   -256       O  
ATOM   1896  CB  ASP A1066      64.157   1.973  55.559  1.00103.15           C  
ANISOU 1896  CB  ASP A1066    13527  12106  13559    -70    -25   -229       C  
ATOM   1897  CG  ASP A1066      63.196   1.504  56.622  1.00107.05           C  
ANISOU 1897  CG  ASP A1066    14054  12587  14033    -73    -13   -223       C  
ATOM   1898  OD1 ASP A1066      62.897   2.295  57.541  1.00111.62           O  
ANISOU 1898  OD1 ASP A1066    14686  13145  14579    -69      6   -233       O  
ATOM   1899  OD2 ASP A1066      62.743   0.345  56.541  1.00110.64           O  
ANISOU 1899  OD2 ASP A1066    14484  13064  14490    -80    -16   -206       O  
ATOM   1900  N   ILE A1067      66.441   3.838  56.265  1.00 57.98           N  
ANISOU 1900  N   ILE A1067     7843   6332   7856    -79    -24   -276       N  
ATOM   1901  CA  ILE A1067      67.882   3.987  56.181  1.00 54.20           C  
ANISOU 1901  CA  ILE A1067     7340   5850   7403    -92    -28   -292       C  
ATOM   1902  C   ILE A1067      68.544   2.826  55.443  1.00 47.67           C  
ANISOU 1902  C   ILE A1067     6451   5060   6599   -104     -6   -284       C  
ATOM   1903  O   ILE A1067      69.662   2.984  54.935  1.00 51.87           O  
ANISOU 1903  O   ILE A1067     6966   5596   7145   -116     23   -296       O  
ATOM   1904  CB  ILE A1067      68.467   4.139  57.600  1.00 63.06           C  
ANISOU 1904  CB  ILE A1067     8507   6938   8516   -107    -21   -312       C  
ATOM   1905  CG1 ILE A1067      68.297   2.838  58.391  1.00 71.15           C  
ANISOU 1905  CG1 ILE A1067     9539   7971   9525   -119    -19   -302       C  
ATOM   1906  CG2 ILE A1067      67.788   5.285  58.326  1.00 55.90           C  
ANISOU 1906  CG2 ILE A1067     7669   5995   7577    -98    -15   -323       C  
ATOM   1907  CD1 ILE A1067      68.851   2.893  59.801  1.00 72.30           C  
ANISOU 1907  CD1 ILE A1067     9740   8088   9645   -135    -33   -316       C  
ATOM   1908  N   LEU A1068      67.887   1.660  55.377  1.00 25.38           N  
ANISOU 1908  N   LEU A1068     3622   2262   3761   -107     14   -266       N  
ATOM   1909  CA  LEU A1068      68.500   0.478  54.773  1.00 18.94           C  
ANISOU 1909  CA  LEU A1068     2829   1467   2901   -127     59   -254       C  
ATOM   1910  C   LEU A1068      68.991   0.725  53.347  1.00 20.37           C  
ANISOU 1910  C   LEU A1068     3036   1667   3036   -134    100   -247       C  
ATOM   1911  O   LEU A1068      70.128   0.379  53.005  1.00 29.74           O  
ANISOU 1911  O   LEU A1068     4269   2845   4185   -144     67   -246       O  
ATOM   1912  CB  LEU A1068      67.513  -0.686  54.797  1.00 17.33           C  
ANISOU 1912  CB  LEU A1068     2628   1279   2678   -125     47   -233       C  
ATOM   1913  CG  LEU A1068      68.076  -2.035  54.332  1.00 29.55           C  
ANISOU 1913  CG  LEU A1068     4205   2832   4192   -135     19   -221       C  
ATOM   1914  CD1 LEU A1068      69.388  -2.350  55.051  1.00 17.53           C  
ANISOU 1914  CD1 LEU A1068     2701   1280   2677   -143    -27   -234       C  
ATOM   1915  CD2 LEU A1068      67.065  -3.170  54.497  1.00 11.24           C  
ANISOU 1915  CD2 LEU A1068     1881    521   1870   -134     -2   -203       C  
ATOM   1916  N   VAL A1069      68.159   1.333  52.497  1.00 11.60           N  
ANISOU 1916  N   VAL A1069     1847    574   1986   -118    116   -247       N  
ATOM   1917  CA  VAL A1069      68.623   1.603  51.138  1.00 11.48           C  
ANISOU 1917  CA  VAL A1069     2066    559   1738   -112    -30   -197       C  
ATOM   1918  C   VAL A1069      69.784   2.587  51.161  1.00 22.00           C  
ANISOU 1918  C   VAL A1069     3402   1865   3090   -111    -72   -212       C  
ATOM   1919  O   VAL A1069      70.722   2.468  50.364  1.00 11.84           O  
ANISOU 1919  O   VAL A1069     2095    576   1826   -127    -31   -224       O  
ATOM   1920  CB  VAL A1069      67.478   2.105  50.236  1.00 11.30           C  
ANISOU 1920  CB  VAL A1069     1933    541   1819    -75   -132   -196       C  
ATOM   1921  CG1 VAL A1069      67.982   2.302  48.814  1.00 11.20           C  
ANISOU 1921  CG1 VAL A1069     1936    532   1789    -86    -92   -195       C  
ATOM   1922  CG2 VAL A1069      66.298   1.139  50.255  1.00 10.99           C  
ANISOU 1922  CG2 VAL A1069     1880    524   1770    -72   -134   -179       C  
ATOM   1923  N   GLY A1070      69.765   3.547  52.089  1.00 29.13           N  
ANISOU 1923  N   GLY A1070     4125   2746   4197    -77   -168   -252       N  
ATOM   1924  CA  GLY A1070      70.868   4.492  52.187  1.00 19.82           C  
ANISOU 1924  CA  GLY A1070     2969   1539   3023    -85   -173   -270       C  
ATOM   1925  C   GLY A1070      72.165   3.828  52.604  1.00 18.59           C  
ANISOU 1925  C   GLY A1070     2984   1384   2696   -166     86   -269       C  
ATOM   1926  O   GLY A1070      73.235   4.148  52.080  1.00 35.52           O  
ANISOU 1926  O   GLY A1070     5152   3512   4832   -168     20   -271       O  
ATOM   1927  N   GLN A1071      72.092   2.890  53.549  1.00 13.11           N  
ANISOU 1927  N   GLN A1071     2193    691   2098   -166    105   -289       N  
ATOM   1928  CA  GLN A1071      73.292   2.163  53.952  1.00 13.46           C  
ANISOU 1928  CA  GLN A1071     2248    715   2149   -174     47   -298       C  
ATOM   1929  C   GLN A1071      73.809   1.283  52.817  1.00 29.27           C  
ANISOU 1929  C   GLN A1071     4242   2728   4150   -170      3   -288       C  
ATOM   1930  O   GLN A1071      75.028   1.165  52.613  1.00 39.84           O  
ANISOU 1930  O   GLN A1071     5571   4049   5518   -177    -28   -302       O  
ATOM   1931  CB  GLN A1071      72.984   1.333  55.193  1.00 12.87           C  
ANISOU 1931  CB  GLN A1071     2155    631   2105   -171     18   -301       C  
ATOM   1932  CG  GLN A1071      72.468   2.153  56.353  1.00 23.68           C  
ANISOU 1932  CG  GLN A1071     3511   1981   3505   -169     30   -317       C  
ATOM   1933  CD  GLN A1071      72.136   1.303  57.555  1.00 43.58           C  
ANISOU 1933  CD  GLN A1071     6050   4486   6022   -169    -14   -313       C  
ATOM   1934  OE1 GLN A1071      72.197   0.077  57.494  1.00 54.08           O  
ANISOU 1934  OE1 GLN A1071     7383   5827   7337   -168    -49   -297       O  
ATOM   1935  NE2 GLN A1071      71.792   1.950  58.662  1.00 56.76           N  
ANISOU 1935  NE2 GLN A1071     7736   6129   7701   -168    -25   -327       N  
ATOM   1936  N   ILE A1072      72.897   0.669  52.057  1.00 22.53           N  
ANISOU 1936  N   ILE A1072     3376   1900   3284   -158      3   -268       N  
ATOM   1937  CA  ILE A1072      73.311  -0.072  50.871  1.00 18.59           C  
ANISOU 1937  CA  ILE A1072     2847   1410   2808   -154    -26   -266       C  
ATOM   1938  C   ILE A1072      73.978   0.867  49.867  1.00 31.54           C  
ANISOU 1938  C   ILE A1072     4494   3043   4445   -157    -26   -273       C  
ATOM   1939  O   ILE A1072      74.958   0.500  49.211  1.00 17.03           O  
ANISOU 1939  O   ILE A1072     2610   1211   2650   -157    -45   -284       O  
ATOM   1940  CB  ILE A1072      72.110  -0.805  50.245  1.00 18.63           C  
ANISOU 1940  CB  ILE A1072     2838   1442   2799   -143    -21   -246       C  
ATOM   1941  CG1 ILE A1072      71.597  -1.908  51.162  1.00 20.30           C  
ANISOU 1941  CG1 ILE A1072     3030   1659   3024   -140    -36   -239       C  
ATOM   1942  CG2 ILE A1072      72.483  -1.427  48.907  1.00 17.31           C  
ANISOU 1942  CG2 ILE A1072     2625   1295   2659   -137    -41   -244       C  
ATOM   1943  CD1 ILE A1072      70.446  -2.664  50.548  1.00 11.15           C  
ANISOU 1943  CD1 ILE A1072     1859    523   1853   -134    -31   -221       C  
ATOM   1944  N   ASP A1073      73.470   2.099  49.746  1.00 19.47           N  
ANISOU 1944  N   ASP A1073     3008   1515   2874   -155    -17   -264       N  
ATOM   1945  CA  ASP A1073      74.102   3.077  48.860  1.00 27.25           C  
ANISOU 1945  CA  ASP A1073     3997   2486   3869   -158    -32   -272       C  
ATOM   1946  C   ASP A1073      75.495   3.455  49.351  1.00 35.80           C  
ANISOU 1946  C   ASP A1073     5086   3541   4975   -176    -33   -295       C  
ATOM   1947  O   ASP A1073      76.398   3.696  48.542  1.00 12.93           O  
ANISOU 1947  O   ASP A1073     2168    632   2111   -185    -37   -310       O  
ATOM   1948  CB  ASP A1073      73.233   4.326  48.726  1.00 33.38           C  
ANISOU 1948  CB  ASP A1073     4800   3258   4626   -143    -60   -261       C  
ATOM   1949  CG  ASP A1073      72.067   4.125  47.788  1.00 42.45           C  
ANISOU 1949  CG  ASP A1073     5918   4427   5783   -127    -61   -246       C  
ATOM   1950  OD1 ASP A1073      72.202   3.305  46.857  1.00 39.08           O  
ANISOU 1950  OD1 ASP A1073     5464   4017   5369   -133    -41   -245       O  
ATOM   1951  OD2 ASP A1073      71.026   4.796  47.970  1.00 44.26           O  
ANISOU 1951  OD2 ASP A1073     6137   4653   6025   -110    -79   -241       O  
ATOM   1952  N   ASP A1074      75.683   3.543  50.669  1.00 13.03           N  
ANISOU 1952  N   ASP A1074     2227    644   2078   -185    -22   -302       N  
ATOM   1953  CA  ASP A1074      77.023   3.773  51.201  1.00 13.46           C  
ANISOU 1953  CA  ASP A1074     2281    670   2164   -204    -28   -327       C  
ATOM   1954  C   ASP A1074      77.963   2.649  50.789  1.00 24.02           C  
ANISOU 1954  C   ASP A1074     3547   2015   3564   -200    -56   -340       C  
ATOM   1955  O   ASP A1074      79.073   2.892  50.288  1.00 19.16           O  
ANISOU 1955  O   ASP A1074     2903   1393   2984   -208    -68   -356       O  
ATOM   1956  CB  ASP A1074      76.983   3.890  52.724  1.00 32.97           C  
ANISOU 1956  CB  ASP A1074     4770   3127   4630   -213     -8   -337       C  
ATOM   1957  CG  ASP A1074      76.191   5.085  53.202  1.00 50.76           C  
ANISOU 1957  CG  ASP A1074     7072   5378   6836   -217     42   -333       C  
ATOM   1958  OD1 ASP A1074      76.006   6.042  52.417  1.00 64.34           O  
ANISOU 1958  OD1 ASP A1074     8851   7094   8502   -208     -6   -314       O  
ATOM   1959  OD2 ASP A1074      75.769   5.072  54.379  1.00 47.94           O  
ANISOU 1959  OD2 ASP A1074     6670   5016   6529   -218     84   -352       O  
ATOM   1960  N   ALA A1075      77.526   1.404  50.985  1.00 13.13           N  
ANISOU 1960  N   ALA A1075     2125    662   2203   -183    -74   -329       N  
ATOM   1961  CA  ALA A1075      78.355   0.276  50.578  1.00 13.14           C  
ANISOU 1961  CA  ALA A1075     2048    681   2263   -170   -113   -335       C  
ATOM   1962  C   ALA A1075      78.608   0.301  49.076  1.00 13.01           C  
ANISOU 1962  C   ALA A1075     1995    680   2268   -167    -98   -339       C  
ATOM   1963  O   ALA A1075      79.726   0.030  48.618  1.00 13.23           O  
ANISOU 1963  O   ALA A1075     1970    709   2349   -165   -113   -357       O  
ATOM   1964  CB  ALA A1075      77.701  -1.042  50.993  1.00 16.83           C  
ANISOU 1964  CB  ALA A1075     2490   1168   2737   -153   -141   -320       C  
ATOM   1965  N   LEU A1076      77.590   0.661  48.295  1.00 16.69           N  
ANISOU 1965  N   LEU A1076     2487   1158   2697   -166    -70   -323       N  
ATOM   1966  CA  LEU A1076      77.750   0.730  46.850  1.00 17.14           C  
ANISOU 1966  CA  LEU A1076     2510   1230   2773   -165    -54   -325       C  
ATOM   1967  C   LEU A1076      78.774   1.785  46.471  1.00 16.94           C  
ANISOU 1967  C   LEU A1076     2489   1184   2764   -181    -42   -345       C  
ATOM   1968  O   LEU A1076      79.601   1.564  45.584  1.00 13.58           O  
ANISOU 1968  O   LEU A1076     2012    766   2383   -182    -35   -361       O  
ATOM   1969  CB  LEU A1076      76.406   1.023  46.187  1.00 16.08           C  
ANISOU 1969  CB  LEU A1076     2407   1108   2595   -160    -34   -304       C  
ATOM   1970  CG  LEU A1076      75.716  -0.186  45.556  1.00 30.63           C  
ANISOU 1970  CG  LEU A1076     4214   2980   4445   -148    -36   -291       C  
ATOM   1971  CD1 LEU A1076      74.358   0.206  44.988  1.00 38.96           C  
ANISOU 1971  CD1 LEU A1076     5301   4045   5457   -145    -21   -270       C  
ATOM   1972  CD2 LEU A1076      76.598  -0.790  44.471  1.00 22.63           C  
ANISOU 1972  CD2 LEU A1076     3138   1978   3483   -146    -33   -306       C  
ATOM   1973  N   LYS A1077      78.754   2.926  47.157  1.00 23.20           N  
ANISOU 1973  N   LYS A1077     3346   1948   3522   -194    -40   -346       N  
ATOM   1974  CA  LYS A1077      79.759   3.948  46.910  1.00 20.19           C  
ANISOU 1974  CA  LYS A1077     2976   1541   3156   -214    -35   -365       C  
ATOM   1975  C   LYS A1077      81.154   3.415  47.205  1.00 19.61           C  
ANISOU 1975  C   LYS A1077     2848   1463   3139   -220    -50   -391       C  
ATOM   1976  O   LYS A1077      82.086   3.629  46.420  1.00 15.82           O  
ANISOU 1976  O   LYS A1077     2330    981   2699   -229    -39   -410       O  
ATOM   1977  CB  LYS A1077      79.447   5.188  47.748  1.00 26.73           C  
ANISOU 1977  CB  LYS A1077     3891   2332   3935   -227    -42   -362       C  
ATOM   1978  CG  LYS A1077      80.392   6.345  47.526  1.00 21.29           C  
ANISOU 1978  CG  LYS A1077     3223   1610   3256   -251    -44   -380       C  
ATOM   1979  CD  LYS A1077      79.982   7.528  48.361  1.00 22.81           C  
ANISOU 1979  CD  LYS A1077     3491   1771   3403   -255    -65   -374       C  
ATOM   1980  CE  LYS A1077      78.672   8.119  47.889  1.00 20.67           C  
ANISOU 1980  CE  LYS A1077     3226   1511   3118   -231    -74   -353       C  
ATOM   1981  NZ  LYS A1077      78.513   9.514  48.398  1.00 28.40           N  
ANISOU 1981  NZ  LYS A1077     4229   2457   4105   -227   -106   -359       N  
ATOM   1982  N   LEU A1078      81.311   2.691  48.317  1.00 35.67           N  
ANISOU 1982  N   LEU A1078     4872   3496   5184   -212    -78   -392       N  
ATOM   1983  CA  LEU A1078      82.601   2.056  48.595  1.00 25.56           C  
ANISOU 1983  CA  LEU A1078     3530   2213   3969   -210   -107   -415       C  
ATOM   1984  C   LEU A1078      83.020   1.135  47.457  1.00 28.17           C  
ANISOU 1984  C   LEU A1078     3778   2568   4356   -193   -105   -424       C  
ATOM   1985  O   LEU A1078      84.180   1.144  47.035  1.00 28.88           O  
ANISOU 1985  O   LEU A1078     3819   2652   4501   -199   -106   -451       O  
ATOM   1986  CB  LEU A1078      82.545   1.270  49.901  1.00 17.69           C  
ANISOU 1986  CB  LEU A1078     2530   1213   2978   -198   -148   -410       C  
ATOM   1987  CG  LEU A1078      82.537   2.092  51.181  1.00 14.67           C  
ANISOU 1987  CG  LEU A1078     2217    800   2558   -218   -151   -413       C  
ATOM   1988  CD1 LEU A1078      82.459   1.173  52.388  1.00 14.71           C  
ANISOU 1988  CD1 LEU A1078     2209    805   2574   -204   -196   -407       C  
ATOM   1989  CD2 LEU A1078      83.783   2.924  51.220  1.00 15.21           C  
ANISOU 1989  CD2 LEU A1078     2289    840   2650   -243   -153   -439       C  
ATOM   1990  N   ALA A1079      82.083   0.342  46.939  1.00 32.17           N  
ANISOU 1990  N   ALA A1079     4271   3101   4851   -176   -100   -405       N  
ATOM   1991  CA  ALA A1079      82.425  -0.578  45.856  1.00 26.94           C  
ANISOU 1991  CA  ALA A1079     3539   2460   4239   -163    -95   -416       C  
ATOM   1992  C   ALA A1079      82.789   0.175  44.580  1.00 26.40           C  
ANISOU 1992  C   ALA A1079     3460   2391   4177   -178    -50   -429       C  
ATOM   1993  O   ALA A1079      83.699  -0.238  43.854  1.00 27.58           O  
ANISOU 1993  O   ALA A1079     3550   2545   4385   -177    -40   -454       O  
ATOM   1994  CB  ALA A1079      81.274  -1.547  45.595  1.00 34.31           C  
ANISOU 1994  CB  ALA A1079     4471   3416   5150   -146   -100   -392       C  
ATOM   1995  N   ASN A1080      82.096   1.285  44.297  1.00 18.49           N  
ANISOU 1995  N   ASN A1080     2520   1384   3121   -193    -21   -415       N  
ATOM   1996  CA  ASN A1080      82.405   2.090  43.118  1.00 14.85           C  
ANISOU 1996  CA  ASN A1080     2058    921   2664   -211     19   -426       C  
ATOM   1997  C   ASN A1080      83.810   2.670  43.188  1.00 26.04           C  
ANISOU 1997  C   ASN A1080     3455   2316   4122   -230     23   -457       C  
ATOM   1998  O   ASN A1080      84.424   2.939  42.150  1.00 39.28           O  
ANISOU 1998  O   ASN A1080     5104   3994   5827   -244     57   -477       O  
ATOM   1999  CB  ASN A1080      81.394   3.230  42.959  1.00 25.87           C  
ANISOU 1999  CB  ASN A1080     3525   2308   3997   -221     34   -403       C  
ATOM   2000  CG  ASN A1080      80.061   2.776  42.383  1.00 38.96           C  
ANISOU 2000  CG  ASN A1080     5192   3990   5623   -205     42   -377       C  
ATOM   2001  OD1 ASN A1080      80.008   1.964  41.460  1.00 29.31           O  
ANISOU 2001  OD1 ASN A1080     3926   2789   4422   -198     56   -380       O  
ATOM   2002  ND2 ASN A1080      78.973   3.313  42.926  1.00 46.65           N  
ANISOU 2002  ND2 ASN A1080     6223   4958   6545   -201     32   -355       N  
ATOM   2003  N   GLU A1081      84.332   2.880  44.394  1.00 19.61           N  
ANISOU 2003  N   GLU A1081     2659   1481   3313   -235     -9   -464       N  
ATOM   2004  CA  GLU A1081      85.677   3.406  44.571  1.00 26.45           C  
ANISOU 2004  CA  GLU A1081     3508   2323   4219   -257    -11   -495       C  
ATOM   2005  C   GLU A1081      86.741   2.319  44.526  1.00 24.87           C  
ANISOU 2005  C   GLU A1081     3218   2132   4100   -241    -28   -523       C  
ATOM   2006  O   GLU A1081      87.915   2.608  44.765  1.00 32.66           O  
ANISOU 2006  O   GLU A1081     4181   3100   5129   -256    -36   -553       O  
ATOM   2007  CB  GLU A1081      85.770   4.171  45.894  1.00 30.09           C  
ANISOU 2007  CB  GLU A1081     4035   2753   4646   -273    -39   -492       C  
ATOM   2008  CG  GLU A1081      84.800   5.343  46.025  1.00 37.44           C  
ANISOU 2008  CG  GLU A1081     5059   3666   5501   -288    -28   -469       C  
ATOM   2009  CD  GLU A1081      84.779   5.915  47.435  1.00 28.42           C  
ANISOU 2009  CD  GLU A1081     3987   2491   4320   -302    -54   -466       C  
ATOM   2010  OE1 GLU A1081      83.688   6.309  47.915  1.00 20.30           O  
ANISOU 2010  OE1 GLU A1081     3026   1455   3233   -297    -56   -443       O  
ATOM   2011  OE2 GLU A1081      85.857   5.954  48.069  1.00 20.20           O  
ANISOU 2011  OE2 GLU A1081     2933   1430   3310   -319    -73   -489       O  
ATOM   2012  N   GLY A1082      86.360   1.081  44.227  1.00 35.03           N  
ANISOU 2012  N   GLY A1082     4457   3444   5410   -212    -38   -517       N  
ATOM   2013  CA  GLY A1082      87.312  -0.009  44.196  1.00 37.18           C  
ANISOU 2013  CA  GLY A1082     4644   3719   5762   -193    -62   -544       C  
ATOM   2014  C   GLY A1082      87.769  -0.504  45.548  1.00 29.44           C  
ANISOU 2014  C   GLY A1082     3652   2725   4810   -178   -124   -547       C  
ATOM   2015  O   GLY A1082      88.706  -1.303  45.610  1.00 38.27           O  
ANISOU 2015  O   GLY A1082     4699   3839   6002   -161   -153   -573       O  
ATOM   2016  N   LYS A1083      87.137  -0.061  46.634  1.00 28.74           N  
ANISOU 2016  N   LYS A1083     3632   2626   4664   -184   -147   -522       N  
ATOM   2017  CA  LYS A1083      87.512  -0.477  47.985  1.00 21.76           C  
ANISOU 2017  CA  LYS A1083     2746   1725   3798   -174   -207   -522       C  
ATOM   2018  C   LYS A1083      86.720  -1.730  48.333  1.00 25.10           C  
ANISOU 2018  C   LYS A1083     3155   2164   4216   -144   -244   -499       C  
ATOM   2019  O   LYS A1083      85.570  -1.648  48.771  1.00 27.61           O  
ANISOU 2019  O   LYS A1083     3531   2490   4470   -145   -241   -469       O  
ATOM   2020  CB  LYS A1083      87.235   0.637  48.986  1.00 19.05           C  
ANISOU 2020  CB  LYS A1083     2488   1358   3392   -201   -208   -511       C  
ATOM   2021  CG  LYS A1083      87.745   2.008  48.592  1.00 16.13           C  
ANISOU 2021  CG  LYS A1083     2156    968   3004   -238   -169   -527       C  
ATOM   2022  CD  LYS A1083      87.307   3.008  49.651  1.00 26.29           C  
ANISOU 2022  CD  LYS A1083     3539   2229   4223   -264   -171   -514       C  
ATOM   2023  CE  LYS A1083      88.133   4.277  49.634  1.00 46.31           C  
ANISOU 2023  CE  LYS A1083     6113   4732   6750   -306   -156   -536       C  
ATOM   2024  NZ  LYS A1083      87.745   5.171  50.763  1.00 50.97           N  
ANISOU 2024  NZ  LYS A1083     6801   5291   7274   -333   -160   -527       N  
ATOM   2025  N   VAL A1084      87.347  -2.898  48.175  1.00 25.01           N  
ANISOU 2025  N   VAL A1084     3069   2156   4276   -118   -282   -514       N  
ATOM   2026  CA  VAL A1084      86.608  -4.154  48.290  1.00 16.60           C  
ANISOU 2026  CA  VAL A1084     1992   1105   3209    -92   -315   -493       C  
ATOM   2027  C   VAL A1084      86.447  -4.567  49.750  1.00 15.67           C  
ANISOU 2027  C   VAL A1084     1902    974   3079    -82   -382   -476       C  
ATOM   2028  O   VAL A1084      85.342  -4.908  50.188  1.00 30.67           O  
ANISOU 2028  O   VAL A1084     3846   2883   4925    -79   -391   -446       O  
ATOM   2029  CB  VAL A1084      87.294  -5.254  47.456  1.00 18.60           C  
ANISOU 2029  CB  VAL A1084     2162   1363   3542    -70   -328   -518       C  
ATOM   2030  CG1 VAL A1084      86.572  -6.571  47.629  1.00 21.96           C  
ANISOU 2030  CG1 VAL A1084     2584   1796   3963    -48   -370   -497       C  
ATOM   2031  CG2 VAL A1084      87.316  -4.865  45.984  1.00 15.38           C  
ANISOU 2031  CG2 VAL A1084     1735    970   3137    -84   -256   -534       C  
ATOM   2032  N   LYS A1085      87.536  -4.536  50.524  1.00 15.90           N  
ANISOU 2032  N   LYS A1085     1906    979   3156    -79   -429   -495       N  
ATOM   2033  CA  LYS A1085      87.465  -4.949  51.925  1.00 24.96           C  
ANISOU 2033  CA  LYS A1085     3080   2110   4293    -70   -499   -478       C  
ATOM   2034  C   LYS A1085      86.490  -4.081  52.715  1.00 32.46           C  
ANISOU 2034  C   LYS A1085     4121   3059   5154    -94   -475   -453       C  
ATOM   2035  O   LYS A1085      85.722  -4.590  53.544  1.00 41.72           O  
ANISOU 2035  O   LYS A1085     5330   4233   6290    -87   -508   -428       O  
ATOM   2036  CB  LYS A1085      88.857  -4.907  52.560  1.00 27.69           C  
ANISOU 2036  CB  LYS A1085     3388   2428   4706    -66   -552   -504       C  
ATOM   2037  CG  LYS A1085      89.919  -5.704  51.810  1.00 33.35           C  
ANISOU 2037  CG  LYS A1085     4008   3142   5521    -41   -573   -537       C  
ATOM   2038  CD  LYS A1085      89.674  -7.197  51.961  1.00 54.92           C  
ANISOU 2038  CD  LYS A1085     6709   5875   8283     -8   -636   -525       C  
ATOM   2039  CE  LYS A1085      90.860  -8.026  51.488  1.00 65.79           C  
ANISOU 2039  CE  LYS A1085     7992   7239   9767     18   -673   -562       C  
ATOM   2040  NZ  LYS A1085      90.547  -9.487  51.495  1.00 62.45           N  
ANISOU 2040  NZ  LYS A1085     7545   6814   9368     46   -730   -551       N  
ATOM   2041  N   GLU A1086      86.514  -2.766  52.483  1.00 22.74           N  
ANISOU 2041  N   GLU A1086     2930   1822   3888   -123   -418   -462       N  
ATOM   2042  CA  GLU A1086      85.614  -1.882  53.215  1.00 29.58           C  
ANISOU 2042  CA  GLU A1086     3884   2683   4674   -146   -390   -444       C  
ATOM   2043  C   GLU A1086      84.161  -2.125  52.829  1.00 28.16           C  
ANISOU 2043  C   GLU A1086     3735   2528   4439   -140   -355   -416       C  
ATOM   2044  O   GLU A1086      83.268  -2.076  53.686  1.00 39.86           O  
ANISOU 2044  O   GLU A1086     5270   4007   5868   -145   -357   -397       O  
ATOM   2045  CB  GLU A1086      86.003  -0.424  52.992  1.00 46.43           C  
ANISOU 2045  CB  GLU A1086     6057   4799   6784   -180   -340   -461       C  
ATOM   2046  CG  GLU A1086      87.478  -0.162  53.200  1.00 53.37           C  
ANISOU 2046  CG  GLU A1086     6901   5653   7722   -190   -369   -492       C  
ATOM   2047  CD  GLU A1086      87.844   1.287  53.000  1.00 50.85           C  
ANISOU 2047  CD  GLU A1086     6632   5314   7375   -231   -321   -508       C  
ATOM   2048  OE1 GLU A1086      87.029   2.158  53.374  1.00 44.45           O  
ANISOU 2048  OE1 GLU A1086     5903   4494   6491   -254   -286   -496       O  
ATOM   2049  OE2 GLU A1086      88.947   1.551  52.472  1.00 56.99           O  
ANISOU 2049  OE2 GLU A1086     7369   6083   8203   -242   -319   -536       O  
ATOM   2050  N   ALA A1087      83.901  -2.389  51.546  1.00 20.73           N  
ANISOU 2050  N   ALA A1087     2760   1609   3509   -132   -321   -416       N  
ATOM   2051  CA  ALA A1087      82.541  -2.724  51.133  1.00 18.58           C  
ANISOU 2051  CA  ALA A1087     2511   1359   3188   -127   -293   -391       C  
ATOM   2052  C   ALA A1087      82.079  -4.009  51.794  1.00 25.32           C  
ANISOU 2052  C   ALA A1087     3353   2219   4047   -107   -347   -373       C  
ATOM   2053  O   ALA A1087      80.927  -4.119  52.229  1.00 47.43           O  
ANISOU 2053  O   ALA A1087     6198   5028   6796   -109   -338   -350       O  
ATOM   2054  CB  ALA A1087      82.463  -2.852  49.613  1.00 13.99           C  
ANISOU 2054  CB  ALA A1087     1893    798   2624   -123   -254   -396       C  
ATOM   2055  N   GLN A1088      82.974  -4.987  51.903  1.00 31.23           N  
ANISOU 2055  N   GLN A1088     4045   2962   4860    -87   -406   -384       N  
ATOM   2056  CA  GLN A1088      82.605  -6.244  52.541  1.00 25.77           C  
ANISOU 2056  CA  GLN A1088     3348   2270   4173    -69   -467   -366       C  
ATOM   2057  C   GLN A1088      82.305  -6.039  54.023  1.00 33.14           C  
ANISOU 2057  C   GLN A1088     4336   3187   5067    -77   -500   -351       C  
ATOM   2058  O   GLN A1088      81.358  -6.632  54.557  1.00 31.61           O  
ANISOU 2058  O   GLN A1088     4175   3000   4836    -74   -518   -327       O  
ATOM   2059  CB  GLN A1088      83.718  -7.273  52.330  1.00 18.00           C  
ANISOU 2059  CB  GLN A1088     2292   1276   3271    -46   -526   -384       C  
ATOM   2060  CG  GLN A1088      83.917  -7.667  50.868  1.00 17.45           C  
ANISOU 2060  CG  GLN A1088     2169   1221   3241    -38   -491   -400       C  
ATOM   2061  CD  GLN A1088      85.123  -8.571  50.646  1.00 30.60           C  
ANISOU 2061  CD  GLN A1088     3760   2871   4996    -16   -542   -427       C  
ATOM   2062  OE1 GLN A1088      86.218  -8.309  51.151  1.00 37.29           O  
ANISOU 2062  OE1 GLN A1088     4578   3698   5890    -12   -575   -447       O  
ATOM   2063  NE2 GLN A1088      84.920  -9.652  49.897  1.00 15.25           N  
ANISOU 2063  NE2 GLN A1088     1784    933   3076     -2   -550   -428       N  
ATOM   2064  N   ALA A1089      83.086  -5.186  54.697  1.00 23.63           N  
ANISOU 2064  N   ALA A1089     3148   1962   3869    -90   -507   -366       N  
ATOM   2065  CA  ALA A1089      82.799  -4.872  56.095  1.00 23.56           C  
ANISOU 2065  CA  ALA A1089     3198   1935   3817   -102   -532   -354       C  
ATOM   2066  C   ALA A1089      81.454  -4.168  56.237  1.00 39.46           C  
ANISOU 2066  C   ALA A1089     5276   3959   5756   -119   -467   -339       C  
ATOM   2067  O   ALA A1089      80.672  -4.465  57.157  1.00 39.88           O  
ANISOU 2067  O   ALA A1089     5371   4010   5770   -122   -485   -321       O  
ATOM   2068  CB  ALA A1089      83.916  -4.018  56.680  1.00 26.90           C  
ANISOU 2068  CB  ALA A1089     3629   2331   4261   -117   -546   -376       C  
ATOM   2069  N   ALA A1090      81.168  -3.229  55.331  1.00 27.60           N  
ANISOU 2069  N   ALA A1090     3786   2467   4236   -132   -394   -348       N  
ATOM   2070  CA  ALA A1090      79.864  -2.577  55.331  1.00 27.87           C  
ANISOU 2070  CA  ALA A1090     3874   2509   4207   -145   -331   -336       C  
ATOM   2071  C   ALA A1090      78.741  -3.591  55.149  1.00 25.13           C  
ANISOU 2071  C   ALA A1090     3521   2185   3842   -131   -337   -311       C  
ATOM   2072  O   ALA A1090      77.691  -3.483  55.789  1.00 28.50           O  
ANISOU 2072  O   ALA A1090     3990   2612   4225   -137   -318   -298       O  
ATOM   2073  CB  ALA A1090      79.809  -1.515  54.233  1.00 27.89           C  
ANISOU 2073  CB  ALA A1090     3887   2515   4197   -158   -262   -346       C  
ATOM   2074  N   ALA A1091      78.950  -4.595  54.294  1.00 16.47           N  
ANISOU 2074  N   ALA A1091     2371   1105   2782   -113   -363   -308       N  
ATOM   2075  CA  ALA A1091      77.923  -5.612  54.083  1.00 13.59           C  
ANISOU 2075  CA  ALA A1091     2003    759   2401   -103   -372   -286       C  
ATOM   2076  C   ALA A1091      77.721  -6.459  55.333  1.00 25.99           C  
ANISOU 2076  C   ALA A1091     3593   2320   3963    -99   -436   -270       C  
ATOM   2077  O   ALA A1091      76.583  -6.815  55.684  1.00 51.10           O  
ANISOU 2077  O   ALA A1091     6804   5508   7103   -102   -429   -251       O  
ATOM   2078  CB  ALA A1091      78.295  -6.488  52.890  1.00 13.32           C  
ANISOU 2078  CB  ALA A1091     1911    739   2411    -88   -385   -290       C  
ATOM   2079  N   GLU A1092      78.818  -6.809  56.004  1.00 27.19           N  
ANISOU 2079  N   GLU A1092     3727   2451   4151    -92   -501   -278       N  
ATOM   2080  CA  GLU A1092      78.700  -7.533  57.262  1.00 40.14           C  
ANISOU 2080  CA  GLU A1092     5396   4078   5779    -90   -569   -261       C  
ATOM   2081  C   GLU A1092      77.861  -6.747  58.256  1.00 47.48           C  
ANISOU 2081  C   GLU A1092     6392   5002   6648   -109   -536   -253       C  
ATOM   2082  O   GLU A1092      76.991  -7.312  58.929  1.00 59.39           O  
ANISOU 2082  O   GLU A1092     7934   6511   8121   -113   -556   -232       O  
ATOM   2083  CB  GLU A1092      80.084  -7.827  57.840  1.00 46.69           C  
ANISOU 2083  CB  GLU A1092     6199   4882   6658    -80   -644   -272       C  
ATOM   2084  CG  GLU A1092      80.046  -8.670  59.113  1.00 63.96           C  
ANISOU 2084  CG  GLU A1092     8418   7051   8832    -78   -728   -250       C  
ATOM   2085  CD  GLU A1092      79.506 -10.070  58.871  1.00 81.41           C  
ANISOU 2085  CD  GLU A1092    10617   9269  11046    -64   -771   -229       C  
ATOM   2086  OE1 GLU A1092      79.760 -10.629  57.783  1.00 89.91           O  
ANISOU 2086  OE1 GLU A1092    11641  10356  12166    -49   -767   -238       O  
ATOM   2087  OE2 GLU A1092      78.826 -10.613  59.769  1.00 85.58           O  
ANISOU 2087  OE2 GLU A1092    11192   9791  11532    -72   -808   -205       O  
ATOM   2088  N   GLN A1093      78.087  -5.435  58.341  1.00 40.97           N  
ANISOU 2088  N   GLN A1093     5588   4167   5811   -124   -484   -271       N  
ATOM   2089  CA  GLN A1093      77.222  -4.613  59.184  1.00 46.32           C  
ANISOU 2089  CA  GLN A1093     6326   4837   6437   -142   -442   -269       C  
ATOM   2090  C   GLN A1093      75.781  -4.627  58.684  1.00 41.94           C  
ANISOU 2090  C   GLN A1093     5783   4304   5850   -143   -383   -257       C  
ATOM   2091  O   GLN A1093      74.837  -4.692  59.480  1.00 54.77           O  
ANISOU 2091  O   GLN A1093     7444   5926   7438   -150   -377   -245       O  
ATOM   2092  CB  GLN A1093      77.758  -3.184  59.253  1.00 58.88           C  
ANISOU 2092  CB  GLN A1093     7936   6408   8027   -159   -394   -295       C  
ATOM   2093  CG  GLN A1093      78.971  -3.036  60.151  1.00 71.16           C  
ANISOU 2093  CG  GLN A1093     9499   7936   9602   -166   -451   -307       C  
ATOM   2094  CD  GLN A1093      78.698  -3.519  61.563  1.00 84.17           C  
ANISOU 2094  CD  GLN A1093    11190   9569  11220   -171   -507   -291       C  
ATOM   2095  OE1 GLN A1093      77.633  -3.253  62.126  1.00 84.16           O  
ANISOU 2095  OE1 GLN A1093    11233   9570  11176   -180   -474   -284       O  
ATOM   2096  NE2 GLN A1093      79.659  -4.233  62.145  1.00 87.50           N  
ANISOU 2096  NE2 GLN A1093    11600   9976  11670   -164   -594   -286       N  
ATOM   2097  N   LEU A1094      75.596  -4.587  57.366  1.00 34.74           N  
ANISOU 2097  N   LEU A1094     4837   3411   4950   -136   -343   -259       N  
ATOM   2098  CA  LEU A1094      74.261  -4.562  56.785  1.00 32.24           C  
ANISOU 2098  CA  LEU A1094     4529   3115   4607   -137   -288   -247       C  
ATOM   2099  C   LEU A1094      73.447  -5.801  57.102  1.00 30.94           C  
ANISOU 2099  C   LEU A1094     4365   2962   4429   -131   -327   -224       C  
ATOM   2100  O   LEU A1094      72.219  -5.745  57.013  1.00 38.32           O  
ANISOU 2100  O   LEU A1094     5316   3908   5338   -135   -287   -213       O  
ATOM   2101  CB  LEU A1094      74.336  -4.408  55.269  1.00 40.37           C  
ANISOU 2101  CB  LEU A1094     5525   4161   5651   -131   -252   -252       C  
ATOM   2102  CG  LEU A1094      74.591  -3.003  54.749  1.00 55.13           C  
ANISOU 2102  CG  LEU A1094     7411   6021   7513   -142   -190   -269       C  
ATOM   2103  CD1 LEU A1094      74.736  -3.030  53.237  1.00 65.72           C  
ANISOU 2103  CD1 LEU A1094     8724   7381   8867   -137   -170   -270       C  
ATOM   2104  CD2 LEU A1094      73.441  -2.117  55.169  1.00 47.56           C  
ANISOU 2104  CD2 LEU A1094     6495   5055   6520   -151   -128   -268       C  
ATOM   2105  N   LYS A1095      74.098  -6.927  57.402  1.00 32.07           N  
ANISOU 2105  N   LYS A1095     4491   3101   4594   -122   -406   -215       N  
ATOM   2106  CA  LYS A1095      73.345  -8.165  57.625  1.00 31.49           C  
ANISOU 2106  CA  LYS A1095     4423   3035   4506   -120   -446   -191       C  
ATOM   2107  C   LYS A1095      72.299  -8.012  58.731  1.00 38.29           C  
ANISOU 2107  C   LYS A1095     5338   3892   5320   -134   -435   -178       C  
ATOM   2108  O   LYS A1095      71.112  -8.315  58.531  1.00 38.14           O  
ANISOU 2108  O   LYS A1095     5328   3886   5278   -138   -408   -164       O  
ATOM   2109  CB  LYS A1095      74.296  -9.316  57.956  1.00 33.98           C  
ANISOU 2109  CB  LYS A1095     4720   3338   4853   -108   -539   -184       C  
ATOM   2110  CG  LYS A1095      73.586 -10.662  58.098  1.00 32.13           C  
ANISOU 2110  CG  LYS A1095     4495   3107   4605   -108   -586   -158       C  
ATOM   2111  CD  LYS A1095      74.560 -11.792  58.423  1.00 39.26           C  
ANISOU 2111  CD  LYS A1095     5383   3992   5544    -96   -682   -152       C  
ATOM   2112  CE  LYS A1095      75.675 -11.884  57.391  1.00 51.96           C  
ANISOU 2112  CE  LYS A1095     6928   5599   7215    -77   -689   -174       C  
ATOM   2113  NZ  LYS A1095      76.657 -12.956  57.720  1.00 56.65           N  
ANISOU 2113  NZ  LYS A1095     7501   6170   7854    -62   -783   -172       N  
ATOM   2114  N   THR A1096      72.720  -7.533  59.906  1.00 50.24           N  
ANISOU 2114  N   THR A1096     6887   5383   6819   -143   -455   -183       N  
ATOM   2115  CA  THR A1096      71.800  -7.426  61.038  1.00 55.57           C  
ANISOU 2115  CA  THR A1096     7615   6050   7449   -158   -449   -171       C  
ATOM   2116  C   THR A1096      70.697  -6.410  60.766  1.00 39.17           C  
ANISOU 2116  C   THR A1096     5546   3981   5356   -162   -359   -181       C  
ATOM   2117  O   THR A1096      69.523  -6.649  61.084  1.00 37.79           O  
ANISOU 2117  O   THR A1096     5392   3812   5154   -169   -341   -168       O  
ATOM   2118  CB  THR A1096      72.576  -7.056  62.299  1.00 59.19           C  
ANISOU 2118  CB  THR A1096     8112   6481   7895   -167   -490   -177       C  
ATOM   2119  OG1 THR A1096      73.349  -5.875  62.051  1.00 59.59           O  
ANISOU 2119  OG1 THR A1096     8151   6522   7968   -167   -452   -204       O  
ATOM   2120  CG2 THR A1096      73.506  -8.196  62.691  1.00 54.88           C  
ANISOU 2120  CG2 THR A1096     7561   5924   7366   -162   -590   -162       C  
ATOM   2121  N   THR A1097      71.066  -5.265  60.196  1.00 31.51           N  
ANISOU 2121  N   THR A1097     4559   3008   4406   -159   -304   -204       N  
ATOM   2122  CA  THR A1097      70.077  -4.264  59.822  1.00 38.70           C  
ANISOU 2122  CA  THR A1097     5469   3922   5313   -160   -223   -214       C  
ATOM   2123  C   THR A1097      69.045  -4.847  58.861  1.00 37.78           C  
ANISOU 2123  C   THR A1097     5327   3830   5197   -154   -199   -199       C  
ATOM   2124  O   THR A1097      67.839  -4.596  58.999  1.00 30.58           O  
ANISOU 2124  O   THR A1097     4422   2921   4276   -155   -161   -194       O  
ATOM   2125  CB  THR A1097      70.795  -3.069  59.199  1.00 36.26           C  
ANISOU 2125  CB  THR A1097     5145   3603   5029   -159   -179   -239       C  
ATOM   2126  OG1 THR A1097      71.701  -2.512  60.159  1.00 28.69           O  
ANISOU 2126  OG1 THR A1097     4214   2619   4069   -167   -203   -254       O  
ATOM   2127  CG2 THR A1097      69.809  -2.007  58.767  1.00 38.76           C  
ANISOU 2127  CG2 THR A1097     5453   3918   5354   -156   -104   -249       C  
ATOM   2128  N   ILE A1098      69.504  -5.646  57.893  1.00 37.50           N  
ANISOU 2128  N   ILE A1098     5260   3811   5177   -147   -225   -191       N  
ATOM   2129  CA  ILE A1098      68.606  -6.276  56.929  1.00 29.19           C  
ANISOU 2129  CA  ILE A1098     4186   2781   4124   -143   -208   -177       C  
ATOM   2130  C   ILE A1098      67.630  -7.200  57.640  1.00 31.04           C  
ANISOU 2130  C   ILE A1098     4442   3019   4334   -150   -238   -156       C  
ATOM   2131  O   ILE A1098      66.422  -7.183  57.370  1.00 32.97           O  
ANISOU 2131  O   ILE A1098     4685   3272   4570   -152   -200   -148       O  
ATOM   2132  CB  ILE A1098      69.415  -7.044  55.873  1.00 27.68           C  
ANISOU 2132  CB  ILE A1098     3960   2603   3956   -134   -243   -176       C  
ATOM   2133  CG1 ILE A1098      70.009  -6.086  54.850  1.00 46.75           C  
ANISOU 2133  CG1 ILE A1098     6357   5020   6387   -130   -198   -193       C  
ATOM   2134  CG2 ILE A1098      68.544  -8.067  55.175  1.00 17.52           C  
ANISOU 2134  CG2 ILE A1098     2658   1334   2664   -132   -253   -157       C  
ATOM   2135  CD1 ILE A1098      71.053  -6.741  54.001  1.00 46.08           C  
ANISOU 2135  CD1 ILE A1098     6235   4942   6333   -121   -237   -197       C  
ATOM   2136  N   ASN A1099      68.146  -8.036  58.545  1.00 21.09           N  
ANISOU 2136  N   ASN A1099     3203   1748   3063   -154   -308   -145       N  
ATOM   2137  CA  ASN A1099      67.270  -8.943  59.285  1.00 29.20           C  
ANISOU 2137  CA  ASN A1099     4260   2774   4059   -167   -341   -122       C  
ATOM   2138  C   ASN A1099      66.202  -8.169  60.054  1.00 42.67           C  
ANISOU 2138  C   ASN A1099     5997   4473   5740   -177   -290   -124       C  
ATOM   2139  O   ASN A1099      65.003  -8.488  59.981  1.00 44.44           O  
ANISOU 2139  O   ASN A1099     6227   4707   5951   -184   -270   -111       O  
ATOM   2140  CB  ASN A1099      68.095  -9.815  60.229  1.00 40.23           C  
ANISOU 2140  CB  ASN A1099     5683   4155   5446   -172   -428   -109       C  
ATOM   2141  CG  ASN A1099      68.752 -10.984  59.513  1.00 61.39           C  
ANISOU 2141  CG  ASN A1099     8332   6840   8153   -162   -489   -100       C  
ATOM   2142  OD1 ASN A1099      68.455 -11.264  58.346  1.00 51.33           O  
ANISOU 2142  OD1 ASN A1099     7022   5582   6897   -154   -467   -100       O  
ATOM   2143  ND2 ASN A1099      69.645 -11.681  60.214  1.00 68.48           N  
ANISOU 2143  ND2 ASN A1099     9243   7720   9056   -161   -570    -91       N  
ATOM   2144  N   ALA A1100      66.622  -7.127  60.779  1.00 38.75           N  
ANISOU 2144  N   ALA A1100     5522   3960   5242   -178   -271   -142       N  
ATOM   2145  CA  ALA A1100      65.680  -6.348  61.575  1.00 39.44           C  
ANISOU 2145  CA  ALA A1100     5640   4037   5309   -184   -228   -147       C  
ATOM   2146  C   ALA A1100      64.605  -5.718  60.697  1.00 43.74           C  
ANISOU 2146  C   ALA A1100     6151   4593   5877   -174   -161   -152       C  
ATOM   2147  O   ALA A1100      63.406  -5.804  60.996  1.00 49.66           O  
ANISOU 2147  O   ALA A1100     6912   5345   6613   -179   -143   -142       O  
ATOM   2148  CB  ALA A1100      66.430  -5.277  62.364  1.00 53.99           C  
ANISOU 2148  CB  ALA A1100     7508   5856   7148   -185   -222   -169       C  
ATOM   2149  N   TYR A1101      65.014  -5.084  59.597  1.00 43.51           N  
ANISOU 2149  N   TYR A1101     6079   4570   5883   -160   -128   -166       N  
ATOM   2150  CA  TYR A1101      64.045  -4.391  58.756  1.00 34.01           C  
ANISOU 2150  CA  TYR A1101     4841   3374   4707   -148    -74   -170       C  
ATOM   2151  C   TYR A1101      63.104  -5.365  58.053  1.00 24.40           C  
ANISOU 2151  C   TYR A1101     3606   2177   3488   -151    -74   -149       C  
ATOM   2152  O   TYR A1101      61.913  -5.070  57.891  1.00 21.20           O  
ANISOU 2152  O   TYR A1101     3187   1773   3093   -146    -48   -143       O  
ATOM   2153  CB  TYR A1101      64.768  -3.482  57.768  1.00 29.91           C  
ANISOU 2153  CB  TYR A1101     4288   2853   4223   -137    -43   -189       C  
ATOM   2154  CG  TYR A1101      65.092  -2.155  58.401  1.00 30.28           C  
ANISOU 2154  CG  TYR A1101     4347   2877   4282   -132    -34   -210       C  
ATOM   2155  CD1 TYR A1101      64.077  -1.334  58.874  1.00 34.12           C  
ANISOU 2155  CD1 TYR A1101     4849   3353   4762   -121    -27   -212       C  
ATOM   2156  CD2 TYR A1101      66.402  -1.731  58.555  1.00 25.47           C  
ANISOU 2156  CD2 TYR A1101     3747   2254   3677   -137    -41   -228       C  
ATOM   2157  CE1 TYR A1101      64.354  -0.120  59.472  1.00 29.93           C  
ANISOU 2157  CE1 TYR A1101     4350   2799   4222   -115    -24   -231       C  
ATOM   2158  CE2 TYR A1101      66.689  -0.510  59.155  1.00 26.04           C  
ANISOU 2158  CE2 TYR A1101     3838   2302   3755   -133    -37   -248       C  
ATOM   2159  CZ  TYR A1101      65.656   0.287  59.610  1.00 31.71           C  
ANISOU 2159  CZ  TYR A1101     4578   3010   4460   -122    -31   -249       C  
ATOM   2160  OH  TYR A1101      65.916   1.499  60.207  1.00 53.55           O  
ANISOU 2160  OH  TYR A1101     7382   5751   7214   -118    -27   -268       O  
ATOM   2161  N   ILE A1102      63.608  -6.528  57.626  1.00 11.36           N  
ANISOU 2161  N   ILE A1102     1954    540   1824   -157   -113   -136       N  
ATOM   2162  CA  ILE A1102      62.723  -7.519  57.019  1.00 11.16           C  
ANISOU 2162  CA  ILE A1102     1918    531   1792   -162   -122   -116       C  
ATOM   2163  C   ILE A1102      61.677  -7.968  58.029  1.00 21.60           C  
ANISOU 2163  C   ILE A1102     3271   1846   3088   -177   -134    -99       C  
ATOM   2164  O   ILE A1102      60.482  -8.077  57.706  1.00 16.71           O  
ANISOU 2164  O   ILE A1102     2640   1234   2475   -180   -108    -89       O  
ATOM   2165  CB  ILE A1102      63.530  -8.714  56.476  1.00 18.31           C  
ANISOU 2165  CB  ILE A1102     2817   1447   2692   -164   -181   -106       C  
ATOM   2166  CG1 ILE A1102      64.383  -8.313  55.265  1.00 11.00           C  
ANISOU 2166  CG1 ILE A1102     1860    530   1790   -151   -163   -120       C  
ATOM   2167  CG2 ILE A1102      62.593  -9.856  56.092  1.00 27.52           C  
ANISOU 2167  CG2 ILE A1102     3983   2626   3847   -174   -203    -83       C  
ATOM   2168  CD1 ILE A1102      63.585  -7.720  54.118  1.00 16.31           C  
ANISOU 2168  CD1 ILE A1102     2510   1214   2472   -146   -102   -123       C  
ATOM   2169  N   GLN A1103      62.105  -8.221  59.274  1.00 35.02           N  
ANISOU 2169  N   GLN A1103     5013   3532   4760   -189   -172    -96       N  
ATOM   2170  CA  GLN A1103      61.150  -8.599  60.312  1.00 31.53           C  
ANISOU 2170  CA  GLN A1103     4612   3083   4286   -208   -180    -81       C  
ATOM   2171  C   GLN A1103      60.102  -7.510  60.504  1.00 32.03           C  
ANISOU 2171  C   GLN A1103     4671   3139   4361   -201   -119    -90       C  
ATOM   2172  O   GLN A1103      58.907  -7.801  60.631  1.00 25.96           O  
ANISOU 2172  O   GLN A1103     3907   2372   3584   -212   -105    -75       O  
ATOM   2173  CB  GLN A1103      61.886  -8.886  61.621  1.00 31.03           C  
ANISOU 2173  CB  GLN A1103     4602   3004   4186   -223   -230    -77       C  
ATOM   2174  CG  GLN A1103      60.977  -9.236  62.792  1.00 47.06           C  
ANISOU 2174  CG  GLN A1103     6685   5024   6173   -250   -236    -61       C  
ATOM   2175  CD  GLN A1103      61.575 -10.300  63.699  1.00 66.38           C  
ANISOU 2175  CD  GLN A1103     9181   7462   8579   -274   -313    -41       C  
ATOM   2176  OE1 GLN A1103      62.794 -10.410  63.824  1.00 68.83           O  
ANISOU 2176  OE1 GLN A1103     9493   7765   8894   -266   -359    -46       O  
ATOM   2177  NE2 GLN A1103      60.715 -11.100  64.325  1.00 74.89           N  
ANISOU 2177  NE2 GLN A1103    10298   8539   9619   -306   -332    -17       N  
ATOM   2178  N   LYS A1104      60.533  -6.244  60.483  1.00 37.49           N  
ANISOU 2178  N   LYS A1104     5351   3820   5072   -182    -90   -114       N  
ATOM   2179  CA  LYS A1104      59.607  -5.123  60.648  1.00 23.54           C  
ANISOU 2179  CA  LYS A1104     3585   2044   3314   -169    -49   -122       C  
ATOM   2180  C   LYS A1104      58.589  -5.070  59.514  1.00 21.22           C  
ANISOU 2180  C   LYS A1104     3245   1765   3055   -157    -27   -112       C  
ATOM   2181  O   LYS A1104      57.401  -4.813  59.743  1.00 25.46           O  
ANISOU 2181  O   LYS A1104     3793   2298   3584   -156     -8   -104       O  
ATOM   2182  CB  LYS A1104      60.388  -3.813  60.723  1.00 29.38           C  
ANISOU 2182  CB  LYS A1104     4327   2770   4066   -152    -36   -148       C  
ATOM   2183  CG  LYS A1104      59.527  -2.585  60.920  1.00 27.55           C  
ANISOU 2183  CG  LYS A1104     4114   2527   3826   -134     -1   -158       C  
ATOM   2184  CD  LYS A1104      60.383  -1.335  60.998  1.00 28.65           C  
ANISOU 2184  CD  LYS A1104     4266   2651   3969   -120      6   -183       C  
ATOM   2185  CE  LYS A1104      59.541  -0.108  61.271  1.00 31.09           C  
ANISOU 2185  CE  LYS A1104     4612   2946   4255   -101     48   -193       C  
ATOM   2186  NZ  LYS A1104      60.357   0.953  61.917  1.00 51.95           N  
ANISOU 2186  NZ  LYS A1104     7294   5564   6881    -97     56   -218       N  
ATOM   2187  N   TYR A1105      59.044  -5.295  58.279  1.00 32.89           N  
ANISOU 2187  N   TYR A1105     4674   3256   4565   -149    -28   -113       N  
ATOM   2188  CA  TYR A1105      58.143  -5.288  57.125  1.00 29.51           C  
ANISOU 2188  CA  TYR A1105     4202   2841   4169   -140    -14   -102       C  
ATOM   2189  C   TYR A1105      57.108  -6.411  57.223  1.00 27.62           C  
ANISOU 2189  C   TYR A1105     3970   2608   3915   -160    -18    -77       C  
ATOM   2190  O   TYR A1105      55.909  -6.202  56.965  1.00 22.96           O  
ANISOU 2190  O   TYR A1105     3366   2018   3339   -156     -8    -64       O  
ATOM   2191  CB  TYR A1105      58.969  -5.436  55.845  1.00 10.69           C  
ANISOU 2191  CB  TYR A1105     1779    476   1805   -134     -7   -108       C  
ATOM   2192  CG  TYR A1105      60.027  -4.370  55.644  1.00 10.74           C  
ANISOU 2192  CG  TYR A1105     1775    483   1825   -119     -3   -129       C  
ATOM   2193  CD1 TYR A1105      59.921  -3.129  56.256  1.00 29.94           C  
ANISOU 2193  CD1 TYR A1105     4226   2893   4256   -106    -11   -142       C  
ATOM   2194  CD2 TYR A1105      61.182  -4.638  54.912  1.00 15.79           C  
ANISOU 2194  CD2 TYR A1105     2405   1134   2460   -122      8   -138       C  
ATOM   2195  CE1 TYR A1105      60.894  -2.154  56.082  1.00 30.63           C  
ANISOU 2195  CE1 TYR A1105     4311   2975   4353    -96    -13   -161       C  
ATOM   2196  CE2 TYR A1105      62.169  -3.681  54.744  1.00 17.17           C  
ANISOU 2196  CE2 TYR A1105     2570   1306   2647   -114     16   -156       C  
ATOM   2197  CZ  TYR A1105      62.020  -2.436  55.334  1.00 32.10           C  
ANISOU 2197  CZ  TYR A1105     4465   3179   4554   -100     -2   -167       C  
ATOM   2198  OH  TYR A1105      62.998  -1.469  55.177  1.00 26.76           O  
ANISOU 2198  OH  TYR A1105     3784   2495   3890    -94     -4   -185       O  
ATOM   2199  N   GLY A1106      57.550  -7.608  57.611  1.00 16.11           N  
ANISOU 2199  N   GLY A1106     2542   1157   2423   -182    -45    -67       N  
ATOM   2200  CA  GLY A1106      56.600  -8.689  57.809  1.00 29.38           C  
ANISOU 2200  CA  GLY A1106     4239   2842   4082   -206    -60    -41       C  
ATOM   2201  C   GLY A1106      55.632  -8.415  58.942  1.00 41.51           C  
ANISOU 2201  C   GLY A1106     5805   4363   5602   -219    -47    -33       C  
ATOM   2202  O   GLY A1106      54.453  -8.784  58.866  1.00 43.13           O  
ANISOU 2202  O   GLY A1106     6005   4569   5812   -233    -36    -12       O  
ATOM   2203  N   GLN A 313      56.098  -7.723  59.987  1.00 25.92           N  
ANISOU 2203  N   GLN A 313     3868   2374   3608   -215    -44    -48       N  
ATOM   2204  CA  GLN A 313      55.201  -7.319  61.062  1.00 29.16           C  
ANISOU 2204  CA  GLN A 313     4318   2769   3993   -226    -22    -44       C  
ATOM   2205  C   GLN A 313      54.147  -6.340  60.558  1.00 29.28           C  
ANISOU 2205  C   GLN A 313     4309   2782   4036   -203     17    -46       C  
ATOM   2206  O   GLN A 313      52.984  -6.410  60.965  1.00 29.21           O  
ANISOU 2206  O   GLN A 313     4316   2767   4016   -215     39    -29       O  
ATOM   2207  CB  GLN A 313      56.001  -6.715  62.217  1.00 38.04           C  
ANISOU 2207  CB  GLN A 313     5494   3877   5082   -226    -24    -65       C  
ATOM   2208  CG  GLN A 313      55.150  -6.289  63.404  1.00 55.48           C  
ANISOU 2208  CG  GLN A 313     7758   6069   7253   -239      9    -65       C  
ATOM   2209  CD  GLN A 313      54.573  -7.464  64.162  1.00 64.79           C  
ANISOU 2209  CD  GLN A 313     8973   7249   8395   -285    -10    -38       C  
ATOM   2210  OE1 GLN A 313      55.131  -8.561  64.147  1.00 68.63           O  
ANISOU 2210  OE1 GLN A 313     9465   7743   8867   -307    -60    -23       O  
ATOM   2211  NE2 GLN A 313      53.443  -7.243  64.826  1.00 66.59           N  
ANISOU 2211  NE2 GLN A 313     9230   7466   8603   -301     30    -30       N  
ATOM   2212  N   SER A 314      54.540  -5.408  59.687  1.00 27.70           N  
ANISOU 2212  N   SER A 314     4076   2585   3863   -170     23    -62       N  
ATOM   2213  CA  SER A 314      53.567  -4.484  59.110  1.00 15.76           C  
ANISOU 2213  CA  SER A 314     2555   1072   2361   -146     51    -61       C  
ATOM   2214  C   SER A 314      52.504  -5.233  58.321  1.00 20.55           C  
ANISOU 2214  C   SER A 314     3125   1689   2992   -158     42    -31       C  
ATOM   2215  O   SER A 314      51.301  -4.947  58.440  1.00 24.43           O  
ANISOU 2215  O   SER A 314     3630   2176   3476   -156     71    -17       O  
ATOM   2216  CB  SER A 314      54.271  -3.468  58.215  1.00 20.02           C  
ANISOU 2216  CB  SER A 314     3074   1617   2917   -116     50    -80       C  
ATOM   2217  OG  SER A 314      55.189  -2.690  58.958  1.00 50.21           O  
ANISOU 2217  OG  SER A 314     6930   5426   6720   -108     60   -105       O  
ATOM   2218  N   ILE A 315      52.930  -6.205  57.512  1.00 28.14           N  
ANISOU 2218  N   ILE A 315     4044   2664   3983   -170     12    -21       N  
ATOM   2219  CA  ILE A 315      51.965  -6.991  56.746  1.00 25.96           C  
ANISOU 2219  CA  ILE A 315     3734   2397   3734   -185      5      9       C  
ATOM   2220  C   ILE A 315      51.020  -7.730  57.686  1.00 29.05           C  
ANISOU 2220  C   ILE A 315     4151   2781   4105   -220     16     35       C  
ATOM   2221  O   ILE A 315      49.807  -7.802  57.445  1.00 35.48           O  
ANISOU 2221  O   ILE A 315     4952   3594   4934   -231     22     65       O  
ATOM   2222  CB  ILE A 315      52.693  -7.962  55.802  1.00 31.22           C  
ANISOU 2222  CB  ILE A 315     4367   3083   4412   -192      2      7       C  
ATOM   2223  CG1 ILE A 315      53.575  -7.192  54.817  1.00 21.97           C  
ANISOU 2223  CG1 ILE A 315     3164   1930   3253   -162     -1    -15       C  
ATOM   2224  CG2 ILE A 315      51.688  -8.844  55.074  1.00 30.25           C  
ANISOU 2224  CG2 ILE A 315     4224   2974   4296   -211     10     34       C  
ATOM   2225  CD1 ILE A 315      54.370  -8.091  53.893  1.00 15.57           C  
ANISOU 2225  CD1 ILE A 315     2350   1136   2430   -171     12    -21       C  
ATOM   2226  N   SER A 316      51.555  -8.275  58.784  1.00 39.63           N  
ANISOU 2226  N   SER A 316     5535   4116   5406   -243     13     30       N  
ATOM   2227  CA  SER A 316      50.708  -8.984  59.740  1.00 24.79           C  
ANISOU 2227  CA  SER A 316     3689   2231   3498   -284     18     57       C  
ATOM   2228  C   SER A 316      49.724  -8.040  60.419  1.00 24.95           C  
ANISOU 2228  C   SER A 316     3732   2237   3512   -280     57     62       C  
ATOM   2229  O   SER A 316      48.579  -8.418  60.689  1.00 39.72           O  
ANISOU 2229  O   SER A 316     5601   4107   5384   -311     72     98       O  
ATOM   2230  CB  SER A 316      51.570  -9.689  60.780  1.00 25.01           C  
ANISOU 2230  CB  SER A 316     3773   2257   3471   -311     -9     50       C  
ATOM   2231  OG  SER A 316      52.341 -10.705  60.168  1.00 44.12           O  
ANISOU 2231  OG  SER A 316     6190   4694   5881   -319    -53     52       O  
ATOM   2232  N   ASN A 317      50.153  -6.813  60.708  1.00 26.00           N  
ANISOU 2232  N   ASN A 317     3888   2359   3630   -242     81     28       N  
ATOM   2233  CA  ASN A 317      49.241  -5.831  61.283  1.00 17.07           C  
ANISOU 2233  CA  ASN A 317     2790   1213   2482   -227    139     23       C  
ATOM   2234  C   ASN A 317      48.105  -5.534  60.320  1.00 29.87           C  
ANISOU 2234  C   ASN A 317     4375   2841   4135   -211    157     46       C  
ATOM   2235  O   ASN A 317      46.941  -5.409  60.731  1.00 29.26           O  
ANISOU 2235  O   ASN A 317     4309   2755   4054   -221    201     70       O  
ATOM   2236  CB  ASN A 317      49.997  -4.555  61.641  1.00 17.76           C  
ANISOU 2236  CB  ASN A 317     2911   1290   2547   -184    169    -22       C  
ATOM   2237  CG  ASN A 317      51.038  -4.777  62.719  1.00 26.16           C  
ANISOU 2237  CG  ASN A 317     4019   2345   3574   -204    151    -40       C  
ATOM   2238  OD1 ASN A 317      51.005  -5.776  63.441  1.00 19.90           O  
ANISOU 2238  OD1 ASN A 317     3249   1552   2759   -248    130    -22       O  
ATOM   2239  ND2 ASN A 317      51.969  -3.840  62.837  1.00 36.57           N  
ANISOU 2239  ND2 ASN A 317     5355   3658   4883   -175    157    -72       N  
ATOM   2240  N   GLU A 318      48.428  -5.409  59.029  1.00 36.15           N  
ANISOU 2240  N   GLU A 318     5129   3649   4958   -189    127     43       N  
ATOM   2241  CA  GLU A 318      47.381  -5.231  58.026  1.00 27.22           C  
ANISOU 2241  CA  GLU A 318     3968   2525   3849   -179    136     69       C  
ATOM   2242  C   GLU A 318      46.410  -6.404  58.044  1.00 25.44           C  
ANISOU 2242  C   GLU A 318     3720   2306   3639   -234    111    125       C  
ATOM   2243  O   GLU A 318      45.188  -6.217  57.972  1.00 32.19           O  
ANISOU 2243  O   GLU A 318     4572   3163   4498   -242    144    160       O  
ATOM   2244  CB  GLU A 318      48.002  -5.081  56.639  1.00 15.57           C  
ANISOU 2244  CB  GLU A 318     2460   1065   2391   -158     97     58       C  
ATOM   2245  CG  GLU A 318      48.800  -3.800  56.453  1.00 29.83           C  
ANISOU 2245  CG  GLU A 318     4279   2869   4186   -112    126     18       C  
ATOM   2246  CD  GLU A 318      49.298  -3.621  55.033  1.00 27.51           C  
ANISOU 2246  CD  GLU A 318     3956   2591   3905    -99     94     14       C  
ATOM   2247  OE1 GLU A 318      48.682  -2.835  54.289  1.00 40.74           O  
ANISOU 2247  OE1 GLU A 318     5624   4269   5587    -71    128     16       O  
ATOM   2248  OE2 GLU A 318      50.295  -4.272  54.657  1.00 32.76           O  
ANISOU 2248  OE2 GLU A 318     4602   3265   4578   -115     40      9       O  
ATOM   2249  N   GLN A 319      46.940  -7.623  58.165  1.00 27.27           N  
ANISOU 2249  N   GLN A 319     3931   2544   3885   -273     66    139       N  
ATOM   2250  CA  GLN A 319      46.079  -8.801  58.229  1.00 24.96           C  
ANISOU 2250  CA  GLN A 319     3607   2262   3615   -328     59    196       C  
ATOM   2251  C   GLN A 319      45.166  -8.758  59.449  1.00 37.09           C  
ANISOU 2251  C   GLN A 319     5175   3797   5122   -366    100    230       C  
ATOM   2252  O   GLN A 319      43.980  -9.108  59.362  1.00 37.11           O  
ANISOU 2252  O   GLN A 319     5145   3818   5137   -408    111    295       O  
ATOM   2253  CB  GLN A 319      46.917 -10.075  58.247  1.00 24.79           C  
ANISOU 2253  CB  GLN A 319     3585   2248   3586   -349     49    182       C  
ATOM   2254  CG  GLN A 319      46.075 -11.332  58.108  1.00 42.82           C  
ANISOU 2254  CG  GLN A 319     5859   4549   5861   -402     59    226       C  
ATOM   2255  CD  GLN A 319      46.903 -12.601  58.127  1.00 56.62           C  
ANISOU 2255  CD  GLN A 319     7657   6312   7546   -431     14    207       C  
ATOM   2256  OE1 GLN A 319      48.130 -12.553  58.174  1.00 57.67           O  
ANISOU 2256  OE1 GLN A 319     7814   6442   7658   -406    -14    169       O  
ATOM   2257  NE2 GLN A 319      46.233 -13.746  58.081  1.00 62.93           N  
ANISOU 2257  NE2 GLN A 319     8468   7132   8310   -487     -9    242       N  
ATOM   2258  N   LYS A 320      45.706  -8.354  60.602  1.00 36.52           N  
ANISOU 2258  N   LYS A 320     5159   3709   5008   -359    126    194       N  
ATOM   2259  CA  LYS A 320      44.892  -8.320  61.815  1.00 41.32           C  
ANISOU 2259  CA  LYS A 320     5799   4318   5583   -400    175    226       C  
ATOM   2260  C   LYS A 320      43.786  -7.279  61.704  1.00 39.89           C  
ANISOU 2260  C   LYS A 320     5617   4136   5404   -379    240    245       C  
ATOM   2261  O   LYS A 320      42.646  -7.525  62.123  1.00 30.52           O  
ANISOU 2261  O   LYS A 320     4464   2953   4180   -441    337    298       O  
ATOM   2262  CB  LYS A 320      45.761  -8.045  63.043  1.00 44.29           C  
ANISOU 2262  CB  LYS A 320     6244   4674   5909   -395    190    177       C  
ATOM   2263  CG  LYS A 320      44.984  -8.141  64.350  1.00 59.18           C  
ANISOU 2263  CG  LYS A 320     8172   6564   7751   -450    243    212       C  
ATOM   2264  CD  LYS A 320      45.819  -7.751  65.561  1.00 71.70           C  
ANISOU 2264  CD  LYS A 320     9839   8123   9279   -445    260    159       C  
ATOM   2265  CE  LYS A 320      45.028  -7.944  66.858  1.00 70.54           C  
ANISOU 2265  CE  LYS A 320     9815   7963   9025   -536    358    182       C  
ATOM   2266  NZ  LYS A 320      45.818  -7.609  68.080  1.00 67.18           N  
ANISOU 2266  NZ  LYS A 320     9485   7509   8532   -541    370    132       N  
ATOM   2267  N   ALA A 321      44.102  -6.113  61.133  1.00 33.92           N  
ANISOU 2267  N   ALA A 321     4871   3359   4659   -300    262    190       N  
ATOM   2268  CA  ALA A 321      43.067  -5.115  60.898  1.00 29.63           C  
ANISOU 2268  CA  ALA A 321     4354   2784   4119   -257    400    191       C  
ATOM   2269  C   ALA A 321      41.996  -5.654  59.957  1.00 29.79           C  
ANISOU 2269  C   ALA A 321     4320   2830   4169   -294    408    263       C  
ATOM   2270  O   ALA A 321      40.796  -5.415  60.164  1.00 27.80           O  
ANISOU 2270  O   ALA A 321     4068   2568   3928   -300    559    314       O  
ATOM   2271  CB  ALA A 321      43.688  -3.839  60.334  1.00 39.63           C  
ANISOU 2271  CB  ALA A 321     5609   4044   5405   -161    389    127       C  
ATOM   2272  N   CYS A 322      42.413  -6.398  58.926  1.00 20.89           N  
ANISOU 2272  N   CYS A 322     3132   1746   3058   -318    251    280       N  
ATOM   2273  CA  CYS A 322      41.458  -7.017  58.008  1.00 23.47           C  
ANISOU 2273  CA  CYS A 322     3415   2107   3395   -368    235    348       C  
ATOM   2274  C   CYS A 322      40.526  -7.978  58.739  1.00 32.71           C  
ANISOU 2274  C   CYS A 322     4571   3315   4543   -470    281    433       C  
ATOM   2275  O   CYS A 322      39.309  -7.968  58.513  1.00 25.91           O  
ANISOU 2275  O   CYS A 322     3675   2489   3681   -505    376    496       O  
ATOM   2276  CB  CYS A 322      42.226  -7.732  56.895  1.00 25.41           C  
ANISOU 2276  CB  CYS A 322     3638   2362   3653   -375    115    335       C  
ATOM   2277  SG  CYS A 322      41.258  -8.646  55.667  1.00 33.77           S  
ANISOU 2277  SG  CYS A 322     4665   3486   4681   -438     69    390       S  
ATOM   2278  N   LYS A 323      41.075  -8.803  59.635  1.00 42.86           N  
ANISOU 2278  N   LYS A 323     5853   4608   5822   -509    229    441       N  
ATOM   2279  CA  LYS A 323      40.236  -9.737  60.391  1.00 38.91           C  
ANISOU 2279  CA  LYS A 323     5329   4159   5295   -600    277    521       C  
ATOM   2280  C   LYS A 323      39.285  -9.011  61.342  1.00 40.55           C  
ANISOU 2280  C   LYS A 323     5592   4389   5427   -635    453    538       C  
ATOM   2281  O   LYS A 323      38.125  -9.414  61.490  1.00 32.48           O  
ANISOU 2281  O   LYS A 323     4512   3459   4371   -709    520    620       O  
ATOM   2282  CB  LYS A 323      41.092 -10.753  61.147  1.00 37.33           C  
ANISOU 2282  CB  LYS A 323     5125   3947   5109   -600    233    498       C  
ATOM   2283  CG  LYS A 323      41.837 -11.730  60.250  1.00 45.70           C  
ANISOU 2283  CG  LYS A 323     6159   4987   6217   -568    185    454       C  
ATOM   2284  CD  LYS A 323      42.902 -12.514  61.016  1.00 57.37           C  
ANISOU 2284  CD  LYS A 323     7721   6450   7628   -588    148    398       C  
ATOM   2285  CE  LYS A 323      43.578 -13.544  60.116  1.00 63.43           C  
ANISOU 2285  CE  LYS A 323     8509   7218   8374   -589     90    360       C  
ATOM   2286  NZ  LYS A 323      44.678 -14.276  60.807  1.00 60.85           N  
ANISOU 2286  NZ  LYS A 323     8254   6885   7979   -608     27    325       N  
ATOM   2287  N   VAL A 324      39.751  -7.954  62.009  1.00 27.86           N  
ANISOU 2287  N   VAL A 324     4068   2713   3804   -568    546    465       N  
ATOM   2288  CA  VAL A 324      38.873  -7.230  62.928  1.00 30.60           C  
ANISOU 2288  CA  VAL A 324     4438   3083   4105   -568    752    484       C  
ATOM   2289  C   VAL A 324      37.720  -6.584  62.163  1.00 35.37           C  
ANISOU 2289  C   VAL A 324     4933   3747   4761   -505    867    533       C  
ATOM   2290  O   VAL A 324      36.548  -6.683  62.557  1.00 36.10           O  
ANISOU 2290  O   VAL A 324     4916   4002   4797   -519    936    579       O  
ATOM   2291  CB  VAL A 324      39.671  -6.191  63.736  1.00 31.18           C  
ANISOU 2291  CB  VAL A 324     4625   3055   4166   -489    825    393       C  
ATOM   2292  CG1 VAL A 324      38.732  -5.246  64.474  1.00 18.55           C  
ANISOU 2292  CG1 VAL A 324     2979   1554   2517   -409    984    376       C  
ATOM   2293  CG2 VAL A 324      40.598  -6.885  64.719  1.00 37.00           C  
ANISOU 2293  CG2 VAL A 324     5438   3785   4836   -553    722    358       C  
ATOM   2294  N   LEU A 325      38.029  -5.923  61.045  1.00 27.20           N  
ANISOU 2294  N   LEU A 325     3890   2624   3821   -414    847    507       N  
ATOM   2295  CA  LEU A 325      36.961  -5.321  60.258  1.00 21.36           C  
ANISOU 2295  CA  LEU A 325     3015   1976   3123   -327    899    539       C  
ATOM   2296  C   LEU A 325      36.033  -6.380  59.677  1.00 25.49           C  
ANISOU 2296  C   LEU A 325     3430   2614   3640   -434    856    643       C  
ATOM   2297  O   LEU A 325      34.827  -6.138  59.538  1.00 47.24           O  
ANISOU 2297  O   LEU A 325     6048   5514   6387   -397    918    688       O  
ATOM   2298  CB  LEU A 325      37.557  -4.453  59.158  1.00 20.08           C  
ANISOU 2298  CB  LEU A 325     2883   1686   3061   -220    875    495       C  
ATOM   2299  CG  LEU A 325      38.360  -3.280  59.728  1.00 34.92           C  
ANISOU 2299  CG  LEU A 325     4861   3460   4946   -108    926    392       C  
ATOM   2300  CD1 LEU A 325      38.814  -2.333  58.638  1.00 32.72           C  
ANISOU 2300  CD1 LEU A 325     4593   3089   4752      1    900    348       C  
ATOM   2301  CD2 LEU A 325      37.536  -2.535  60.768  1.00 30.16           C  
ANISOU 2301  CD2 LEU A 325     4208   2972   4279    -26   1049    365       C  
ATOM   2302  N   GLY A 326      36.558  -7.567  59.370  1.00 25.69           N  
ANISOU 2302  N   GLY A 326     3502   2614   3645   -552    710    658       N  
ATOM   2303  CA  GLY A 326      35.690  -8.648  58.942  1.00 23.56           C  
ANISOU 2303  CA  GLY A 326     3148   2464   3340   -664    646    738       C  
ATOM   2304  C   GLY A 326      34.759  -9.105  60.045  1.00 37.22           C  
ANISOU 2304  C   GLY A 326     4818   4333   4991   -749    736    805       C  
ATOM   2305  O   GLY A 326      33.591  -9.401  59.794  1.00 46.62           O  
ANISOU 2305  O   GLY A 326     5884   5662   6167   -789    770    877       O  
ATOM   2306  N   ILE A 327      35.265  -9.176  61.279  1.00 43.03           N  
ANISOU 2306  N   ILE A 327     5637   5047   5665   -775    764    774       N  
ATOM   2307  CA  ILE A 327      34.413  -9.499  62.425  1.00 39.88           C  
ANISOU 2307  CA  ILE A 327     5192   4791   5170   -850    861    822       C  
ATOM   2308  C   ILE A 327      33.283  -8.487  62.543  1.00 44.21           C  
ANISOU 2308  C   ILE A 327     5602   5485   5712   -731    991    816       C  
ATOM   2309  O   ILE A 327      32.117  -8.850  62.743  1.00 46.75           O  
ANISOU 2309  O   ILE A 327     5799   5980   5985   -783   1037    883       O  
ATOM   2310  CB  ILE A 327      35.241  -9.550  63.721  1.00 42.41           C  
ANISOU 2310  CB  ILE A 327     5641   5057   5418   -872    862    766       C  
ATOM   2311  CG1 ILE A 327      36.140 -10.787  63.755  1.00 47.95           C  
ANISOU 2311  CG1 ILE A 327     6396   5685   6137   -920    674    765       C  
ATOM   2312  CG2 ILE A 327      34.329  -9.496  64.937  1.00 22.04           C  
ANISOU 2312  CG2 ILE A 327     3008   2640   2726   -906    980    785       C  
ATOM   2313  CD1 ILE A 327      36.951 -10.902  65.031  1.00 33.25           C  
ANISOU 2313  CD1 ILE A 327     4648   3777   4207   -941    664    712       C  
ATOM   2314  N   VAL A 328      33.618  -7.200  62.415  1.00 40.38           N  
ANISOU 2314  N   VAL A 328     5136   4931   5276   -567   1048    734       N  
ATOM   2315  CA  VAL A 328      32.616  -6.140  62.534  1.00 27.76           C  
ANISOU 2315  CA  VAL A 328     3414   3454   3679   -431   1169    715       C  
ATOM   2316  C   VAL A 328      31.551  -6.283  61.448  1.00 41.29           C  
ANISOU 2316  C   VAL A 328     4967   5274   5445   -425   1157    795       C  
ATOM   2317  O   VAL A 328      30.340  -6.260  61.724  1.00 39.91           O  
ANISOU 2317  O   VAL A 328     4650   5281   5233   -419   1233    840       O  
ATOM   2318  CB  VAL A 328      33.297  -4.759  62.474  1.00 35.97           C  
ANISOU 2318  CB  VAL A 328     4526   4370   4773   -260   1213    612       C  
ATOM   2319  CG1 VAL A 328      32.267  -3.649  62.285  1.00 30.14           C  
ANISOU 2319  CG1 VAL A 328     3656   3735   4063   -103   1320    599       C  
ATOM   2320  CG2 VAL A 328      34.133  -4.519  63.731  1.00 31.42           C  
ANISOU 2320  CG2 VAL A 328     4087   3725   4127   -262   1246    533       C  
ATOM   2321  N   PHE A 329      31.990  -6.426  60.195  1.00 45.26           N  
ANISOU 2321  N   PHE A 329     5490   5671   6036   -427   1062    813       N  
ATOM   2322  CA  PHE A 329      31.049  -6.560  59.085  1.00 53.45           C  
ANISOU 2322  CA  PHE A 329     6385   6798   7124   -426   1039    890       C  
ATOM   2323  C   PHE A 329      30.179  -7.803  59.245  1.00 47.95           C  
ANISOU 2323  C   PHE A 329     5601   6253   6367   -590   1012    989       C  
ATOM   2324  O   PHE A 329      28.961  -7.750  59.026  1.00 53.21           O  
ANISOU 2324  O   PHE A 329     6104   7083   7028   -579   1057   1049       O  
ATOM   2325  CB  PHE A 329      31.819  -6.560  57.759  1.00 56.20           C  
ANISOU 2325  CB  PHE A 329     6795   6991   7566   -414    936    886       C  
ATOM   2326  CG  PHE A 329      31.395  -7.630  56.785  1.00 62.14           C  
ANISOU 2326  CG  PHE A 329     7488   7784   8337   -542    841    979       C  
ATOM   2327  CD1 PHE A 329      30.210  -7.523  56.073  1.00 49.44           C  
ANISOU 2327  CD1 PHE A 329     5719   6312   6753   -521    855   1048       C  
ATOM   2328  CD2 PHE A 329      32.216  -8.725  56.545  1.00 77.97           C  
ANISOU 2328  CD2 PHE A 329     9619   9691  10314   -664    710    955       C  
ATOM   2329  CE1 PHE A 329      29.835  -8.502  55.166  1.00 53.50           C  
ANISOU 2329  CE1 PHE A 329     6206   6859   7263   -631    744   1096       C  
ATOM   2330  CE2 PHE A 329      31.846  -9.709  55.638  1.00 71.29           C  
ANISOU 2330  CE2 PHE A 329     8764   8876   9446   -745    600    960       C  
ATOM   2331  CZ  PHE A 329      30.654  -9.596  54.949  1.00 64.65           C  
ANISOU 2331  CZ  PHE A 329     7770   8162   8632   -733    616   1034       C  
ATOM   2332  N   PHE A 330      30.783  -8.924  59.646  1.00 31.33           N  
ANISOU 2332  N   PHE A 330     3598   4093   4214   -744    940   1010       N  
ATOM   2333  CA  PHE A 330      30.024 -10.154  59.835  1.00 43.30           C  
ANISOU 2333  CA  PHE A 330     5081   5718   5652   -885    882   1043       C  
ATOM   2334  C   PHE A 330      28.978  -9.990  60.929  1.00 49.77           C  
ANISOU 2334  C   PHE A 330     5790   6729   6392   -892   1001   1073       C  
ATOM   2335  O   PHE A 330      27.839 -10.443  60.778  1.00 57.12           O  
ANISOU 2335  O   PHE A 330     6608   7796   7299   -933    998   1110       O  
ATOM   2336  CB  PHE A 330      30.975 -11.308  60.158  1.00 37.06           C  
ANISOU 2336  CB  PHE A 330     4462   4789   4828   -981    777    991       C  
ATOM   2337  CG  PHE A 330      30.283 -12.611  60.470  1.00 41.30           C  
ANISOU 2337  CG  PHE A 330     4979   5400   5314  -1076    727   1016       C  
ATOM   2338  CD1 PHE A 330      29.895 -13.470  59.449  1.00 40.38           C  
ANISOU 2338  CD1 PHE A 330     4838   5280   5225  -1108    630   1027       C  
ATOM   2339  CD2 PHE A 330      30.039 -12.988  61.788  1.00 42.26           C  
ANISOU 2339  CD2 PHE A 330     5111   5592   5355  -1131    774   1030       C  
ATOM   2340  CE1 PHE A 330      29.266 -14.676  59.732  1.00 35.91           C  
ANISOU 2340  CE1 PHE A 330     4254   4779   4610  -1194    578   1056       C  
ATOM   2341  CE2 PHE A 330      29.411 -14.192  62.080  1.00 38.44           C  
ANISOU 2341  CE2 PHE A 330     4610   5173   4824  -1218    718   1060       C  
ATOM   2342  CZ  PHE A 330      29.027 -15.038  61.051  1.00 39.41           C  
ANISOU 2342  CZ  PHE A 330     4706   5289   4977  -1250    620   1074       C  
ATOM   2343  N   LEU A 331      29.345  -9.354  62.044  1.00 38.74           N  
ANISOU 2343  N   LEU A 331     4428   5340   4950   -845   1109   1048       N  
ATOM   2344  CA  LEU A 331      28.376  -9.158  63.116  1.00 52.64           C  
ANISOU 2344  CA  LEU A 331     6092   7287   6622   -841   1229   1055       C  
ATOM   2345  C   LEU A 331      27.211  -8.301  62.645  1.00 61.77           C  
ANISOU 2345  C   LEU A 331     7062   8588   7821   -712   1317   1070       C  
ATOM   2346  O   LEU A 331      26.044  -8.626  62.899  1.00 63.69           O  
ANISOU 2346  O   LEU A 331     7187   8996   8016   -753   1344   1095       O  
ATOM   2347  CB  LEU A 331      29.049  -8.538  64.340  1.00 50.97           C  
ANISOU 2347  CB  LEU A 331     5996   7021   6351   -779   1303    963       C  
ATOM   2348  CG  LEU A 331      29.753  -9.523  65.276  1.00 40.79           C  
ANISOU 2348  CG  LEU A 331     4846   5680   4973   -935   1251    972       C  
ATOM   2349  CD1 LEU A 331      30.242  -8.796  66.515  1.00 49.30           C  
ANISOU 2349  CD1 LEU A 331     6017   6731   5983   -865   1338    881       C  
ATOM   2350  CD2 LEU A 331      28.828 -10.671  65.654  1.00 27.67           C  
ANISOU 2350  CD2 LEU A 331     3129   4134   3250  -1060   1221   1025       C  
ATOM   2351  N   PHE A 332      27.509  -7.199  61.949  1.00 57.58           N  
ANISOU 2351  N   PHE A 332     6534   7962   7381   -542   1329   1011       N  
ATOM   2352  CA  PHE A 332      26.444  -6.325  61.459  1.00 37.21           C  
ANISOU 2352  CA  PHE A 332     3783   5505   4852   -403   1404   1023       C  
ATOM   2353  C   PHE A 332      25.504  -7.083  60.528  1.00 37.16           C  
ANISOU 2353  C   PHE A 332     3634   5614   4869   -496   1339   1129       C  
ATOM   2354  O   PHE A 332      24.273  -7.032  60.680  1.00 40.98           O  
ANISOU 2354  O   PHE A 332     3974   6270   5326   -481   1382   1146       O  
ATOM   2355  CB  PHE A 332      27.053  -5.117  60.753  1.00 34.30           C  
ANISOU 2355  CB  PHE A 332     3468   4985   4581   -222   1402    949       C  
ATOM   2356  CG  PHE A 332      26.045  -4.124  60.267  1.00 41.50           C  
ANISOU 2356  CG  PHE A 332     4218   5999   5549    -61   1475    955       C  
ATOM   2357  CD1 PHE A 332      25.496  -3.201  61.134  1.00 54.58           C  
ANISOU 2357  CD1 PHE A 332     5815   7748   7175     72   1612    899       C  
ATOM   2358  CD2 PHE A 332      25.663  -4.096  58.938  1.00 50.97           C  
ANISOU 2358  CD2 PHE A 332     5331   7200   6833    -37   1406   1014       C  
ATOM   2359  CE1 PHE A 332      24.573  -2.278  60.690  1.00 59.80           C  
ANISOU 2359  CE1 PHE A 332     6328   8501   7894    231   1678    903       C  
ATOM   2360  CE2 PHE A 332      24.740  -3.175  58.489  1.00 51.25           C  
ANISOU 2360  CE2 PHE A 332     5218   7329   6925    116   1466   1024       C  
ATOM   2361  CZ  PHE A 332      24.194  -2.266  59.365  1.00 53.31           C  
ANISOU 2361  CZ  PHE A 332     5417   7680   7160    254   1602    968       C  
ATOM   2362  N   VAL A 333      26.074  -7.839  59.587  1.00 38.72           N  
ANISOU 2362  N   VAL A 333     3911   5693   5108   -592   1199   1157       N  
ATOM   2363  CA  VAL A 333      25.257  -8.550  58.609  1.00 41.59           C  
ANISOU 2363  CA  VAL A 333     4192   6119   5490   -666   1098   1209       C  
ATOM   2364  C   VAL A 333      24.415  -9.619  59.289  1.00 45.93           C  
ANISOU 2364  C   VAL A 333     4714   6791   5948   -803   1081   1227       C  
ATOM   2365  O   VAL A 333      23.212  -9.738  59.029  1.00 43.54           O  
ANISOU 2365  O   VAL A 333     4271   6632   5642   -806   1087   1267       O  
ATOM   2366  CB  VAL A 333      26.145  -9.149  57.505  1.00 32.12           C  
ANISOU 2366  CB  VAL A 333     3113   4748   4345   -730    954   1210       C  
ATOM   2367  CG1 VAL A 333      25.373 -10.188  56.711  1.00 32.26           C  
ANISOU 2367  CG1 VAL A 333     3087   4820   4351   -833    845   1250       C  
ATOM   2368  CG2 VAL A 333      26.631  -8.046  56.587  1.00 33.91           C  
ANISOU 2368  CG2 VAL A 333     3325   4879   4679   -586    972   1209       C  
ATOM   2369  N   VAL A 334      25.025 -10.403  60.181  1.00 49.65           N  
ANISOU 2369  N   VAL A 334     5317   7198   6349   -910   1059   1201       N  
ATOM   2370  CA  VAL A 334      24.302 -11.496  60.823  1.00 56.26           C  
ANISOU 2370  CA  VAL A 334     6144   8124   7110  -1034   1037   1224       C  
ATOM   2371  C   VAL A 334      23.172 -10.948  61.681  1.00 59.10           C  
ANISOU 2371  C   VAL A 334     6359   8678   7420   -988   1169   1231       C  
ATOM   2372  O   VAL A 334      22.032 -11.422  61.611  1.00 65.76           O  
ANISOU 2372  O   VAL A 334     7093   9652   8243  -1036   1161   1272       O  
ATOM   2373  CB  VAL A 334      25.265 -12.373  61.643  1.00 49.10           C  
ANISOU 2373  CB  VAL A 334     5412   7094   6148  -1131    987   1194       C  
ATOM   2374  CG1 VAL A 334      24.494 -13.240  62.620  1.00 39.90           C  
ANISOU 2374  CG1 VAL A 334     4225   6039   4897  -1229   1001   1220       C  
ATOM   2375  CG2 VAL A 334      26.075 -13.246  60.714  1.00 51.23           C  
ANISOU 2375  CG2 VAL A 334     5803   7197   6465  -1181    838   1183       C  
ATOM   2376  N   MET A 335      23.461  -9.930  62.492  1.00 56.50           N  
ANISOU 2376  N   MET A 335     6029   8370   7070   -887   1294   1185       N  
ATOM   2377  CA  MET A 335      22.436  -9.409  63.382  1.00 63.14           C  
ANISOU 2377  CA  MET A 335     6746   9386   7858   -832   1425   1171       C  
ATOM   2378  C   MET A 335      21.338  -8.655  62.640  1.00 70.43           C  
ANISOU 2378  C   MET A 335     7483  10433   8844   -713   1464   1189       C  
ATOM   2379  O   MET A 335      20.239  -8.508  63.186  1.00 80.65           O  
ANISOU 2379  O   MET A 335     8656  11885  10102   -693   1543   1189       O  
ATOM   2380  CB  MET A 335      23.072  -8.521  64.446  1.00 60.47           C  
ANISOU 2380  CB  MET A 335     6472   9028   7474   -744   1547   1102       C  
ATOM   2381  CG  MET A 335      23.951  -9.284  65.412  1.00 59.48           C  
ANISOU 2381  CG  MET A 335     6517   8815   7267   -868   1520   1087       C  
ATOM   2382  SD  MET A 335      24.587  -8.255  66.743  1.00 63.00           S  
ANISOU 2382  SD  MET A 335     7039   9260   7640   -772   1668   1005       S  
ATOM   2383  CE  MET A 335      25.454  -9.496  67.706  1.00 68.36           C  
ANISOU 2383  CE  MET A 335     7909   9838   8227   -955   1589   1017       C  
ATOM   2384  N   TRP A 336      21.592  -8.172  61.418  1.00 57.36           N  
ANISOU 2384  N   TRP A 336     5803   8707   7284   -629   1410   1206       N  
ATOM   2385  CA  TRP A 336      20.493  -7.589  60.655  1.00 36.29           C  
ANISOU 2385  CA  TRP A 336     2960   6152   4675   -527   1425   1233       C  
ATOM   2386  C   TRP A 336      19.773  -8.592  59.765  1.00 37.01           C  
ANISOU 2386  C   TRP A 336     2994   6289   4779   -647   1306   1307       C  
ATOM   2387  O   TRP A 336      18.670  -8.293  59.297  1.00 36.08           O  
ANISOU 2387  O   TRP A 336     2723   6296   4690   -592   1318   1339       O  
ATOM   2388  CB  TRP A 336      20.981  -6.424  59.792  1.00 37.02           C  
ANISOU 2388  CB  TRP A 336     3042   6154   4869   -352   1437   1215       C  
ATOM   2389  CG  TRP A 336      20.944  -5.101  60.490  1.00 47.94           C  
ANISOU 2389  CG  TRP A 336     4394   7560   6259   -163   1577   1140       C  
ATOM   2390  CD1 TRP A 336      22.009  -4.387  60.956  1.00 56.50           C  
ANISOU 2390  CD1 TRP A 336     5600   8519   7351    -69   1639   1074       C  
ATOM   2391  CD2 TRP A 336      19.779  -4.340  60.815  1.00 48.97           C  
ANISOU 2391  CD2 TRP A 336     4378   7838   6391    -41   1670   1114       C  
ATOM   2392  NE1 TRP A 336      21.578  -3.222  61.542  1.00 53.36           N  
ANISOU 2392  NE1 TRP A 336     5149   8172   6954    107   1760   1000       N  
ATOM   2393  CE2 TRP A 336      20.212  -3.171  61.470  1.00 52.66           C  
ANISOU 2393  CE2 TRP A 336     4894   8251   6863    126   1779   1022       C  
ATOM   2394  CE3 TRP A 336      18.409  -4.531  60.615  1.00 61.07           C  
ANISOU 2394  CE3 TRP A 336     5748   9533   7922    -56   1667   1154       C  
ATOM   2395  CZ2 TRP A 336      19.323  -2.197  61.926  1.00 69.66           C  
ANISOU 2395  CZ2 TRP A 336     6945  10503   9020    277   1880    964       C  
ATOM   2396  CZ3 TRP A 336      17.526  -3.560  61.068  1.00 48.72           C  
ANISOU 2396  CZ3 TRP A 336     4071   8076   6366     94   1774   1104       C  
ATOM   2397  CH2 TRP A 336      17.988  -2.410  61.715  1.00 55.54           C  
ANISOU 2397  CH2 TRP A 336     4991   8876   7234    258   1877   1007       C  
ATOM   2398  N   CYS A 337      20.355  -9.768  59.529  1.00 55.33           N  
ANISOU 2398  N   CYS A 337     5440   8508   7076   -801   1190   1329       N  
ATOM   2399  CA  CYS A 337      19.769 -10.698  58.566  1.00 57.40           C  
ANISOU 2399  CA  CYS A 337     5668   8791   7351   -899   1069   1390       C  
ATOM   2400  C   CYS A 337      18.390 -11.231  58.942  1.00 53.04           C  
ANISOU 2400  C   CYS A 337     4989   8417   6747   -964   1089   1432       C  
ATOM   2401  O   CYS A 337      17.556 -11.367  58.031  1.00 44.98           O  
ANISOU 2401  O   CYS A 337     3863   7469   5759   -967   1034   1484       O  
ATOM   2402  CB  CYS A 337      20.739 -11.858  58.314  1.00 55.48           C  
ANISOU 2402  CB  CYS A 337     5603   8384   7091  -1031    945   1385       C  
ATOM   2403  SG  CYS A 337      21.816 -11.579  56.887  1.00 61.46           S  
ANISOU 2403  SG  CYS A 337     6452   8959   7942   -981    845   1375       S  
ATOM   2404  N   PRO A 338      18.079 -11.572  60.200  1.00 56.16           N  
ANISOU 2404  N   PRO A 338     5388   8888   7062  -1022   1160   1417       N  
ATOM   2405  CA  PRO A 338      16.699 -12.008  60.484  1.00 59.23           C  
ANISOU 2405  CA  PRO A 338     5641   9455   7409  -1077   1181   1462       C  
ATOM   2406  C   PRO A 338      15.657 -10.981  60.080  1.00 58.79           C  
ANISOU 2406  C   PRO A 338     5394   9540   7403   -942   1252   1473       C  
ATOM   2407  O   PRO A 338      14.620 -11.348  59.513  1.00 59.59           O  
ANISOU 2407  O   PRO A 338     5381   9750   7512   -979   1207   1530       O  
ATOM   2408  CB  PRO A 338      16.708 -12.255  62.003  1.00 48.31           C  
ANISOU 2408  CB  PRO A 338     4302   8119   5937  -1130   1270   1432       C  
ATOM   2409  CG  PRO A 338      17.923 -11.559  62.511  1.00 56.16           C  
ANISOU 2409  CG  PRO A 338     5415   8989   6934  -1056   1327   1365       C  
ATOM   2410  CD  PRO A 338      18.923 -11.663  61.404  1.00 53.33           C  
ANISOU 2410  CD  PRO A 338     5158   8461   6643  -1053   1215   1367       C  
ATOM   2411  N   PHE A 339      15.923  -9.695  60.325  1.00 67.64           N  
ANISOU 2411  N   PHE A 339     6482  10656   8561   -778   1355   1418       N  
ATOM   2412  CA  PHE A 339      14.956  -8.657  59.982  1.00 67.68           C  
ANISOU 2412  CA  PHE A 339     6313  10781   8620   -626   1422   1418       C  
ATOM   2413  C   PHE A 339      14.706  -8.611  58.479  1.00 58.79           C  
ANISOU 2413  C   PHE A 339     5129   9636   7574   -600   1315   1475       C  
ATOM   2414  O   PHE A 339      13.553  -8.589  58.031  1.00 61.40           O  
ANISOU 2414  O   PHE A 339     5313  10096   7922   -585   1304   1521       O  
ATOM   2415  CB  PHE A 339      15.437  -7.300  60.500  1.00 41.27           C  
ANISOU 2415  CB  PHE A 339     2977   7401   5303   -443   1542   1336       C  
ATOM   2416  CG  PHE A 339      14.716  -6.127  59.894  1.00 44.84           C  
ANISOU 2416  CG  PHE A 339     3285   7917   5834   -257   1584   1328       C  
ATOM   2417  CD1 PHE A 339      13.428  -5.810  60.284  1.00 44.34           C  
ANISOU 2417  CD1 PHE A 339     3063   8023   5762   -204   1659   1327       C  
ATOM   2418  CD2 PHE A 339      15.335  -5.331  58.938  1.00 41.00           C  
ANISOU 2418  CD2 PHE A 339     2828   7316   5436   -131   1546   1320       C  
ATOM   2419  CE1 PHE A 339      12.764  -4.728  59.725  1.00 47.74           C  
ANISOU 2419  CE1 PHE A 339     3368   8501   6269    -27   1689   1316       C  
ATOM   2420  CE2 PHE A 339      14.676  -4.250  58.379  1.00 41.92           C  
ANISOU 2420  CE2 PHE A 339     2825   7477   5628     46   1575   1312       C  
ATOM   2421  CZ  PHE A 339      13.387  -3.947  58.775  1.00 44.08           C  
ANISOU 2421  CZ  PHE A 339     2942   7915   5891     99   1645   1309       C  
ATOM   2422  N   PHE A 340      15.777  -8.600  57.681  1.00 56.83           N  
ANISOU 2422  N   PHE A 340     4995   9225   7371   -596   1235   1475       N  
ATOM   2423  CA  PHE A 340      15.609  -8.516  56.233  1.00 53.32           C  
ANISOU 2423  CA  PHE A 340     4508   8752   7000   -570   1134   1528       C  
ATOM   2424  C   PHE A 340      15.006  -9.795  55.664  1.00 59.83           C  
ANISOU 2424  C   PHE A 340     5322   9621   7790   -736   1018   1597       C  
ATOM   2425  O   PHE A 340      14.210  -9.742  54.719  1.00 58.33           O  
ANISOU 2425  O   PHE A 340     5026   9501   7636   -719    964   1652       O  
ATOM   2426  CB  PHE A 340      16.944  -8.205  55.566  1.00 36.90           C  
ANISOU 2426  CB  PHE A 340     2562   6483   4976   -530   1082   1507       C  
ATOM   2427  CG  PHE A 340      17.337  -6.762  55.647  1.00 42.39           C  
ANISOU 2427  CG  PHE A 340     3236   7135   5734   -329   1175   1456       C  
ATOM   2428  CD1 PHE A 340      18.135  -6.304  56.688  1.00 49.18           C  
ANISOU 2428  CD1 PHE A 340     4185   7932   6568   -277   1269   1384       C  
ATOM   2429  CD2 PHE A 340      16.910  -5.860  54.684  1.00 47.37           C  
ANISOU 2429  CD2 PHE A 340     3769   7780   6448   -188   1164   1478       C  
ATOM   2430  CE1 PHE A 340      18.508  -4.971  56.768  1.00 45.05           C  
ANISOU 2430  CE1 PHE A 340     3661   7356   6101    -82   1353   1329       C  
ATOM   2431  CE2 PHE A 340      17.277  -4.521  54.753  1.00 51.18           C  
ANISOU 2431  CE2 PHE A 340     4251   8204   6991      9   1244   1424       C  
ATOM   2432  CZ  PHE A 340      18.077  -4.077  55.798  1.00 53.37           C  
ANISOU 2432  CZ  PHE A 340     4624   8412   7242     65   1339   1346       C  
ATOM   2433  N   ILE A 341      15.368 -10.951  56.224  1.00 61.89           N  
ANISOU 2433  N   ILE A 341     5697   9837   7979   -892    976   1594       N  
ATOM   2434  CA  ILE A 341      14.781 -12.211  55.773  1.00 59.37           C  
ANISOU 2434  CA  ILE A 341     5380   9556   7621  -1045    869   1653       C  
ATOM   2435  C   ILE A 341      13.278 -12.204  56.014  1.00 71.30           C  
ANISOU 2435  C   ILE A 341     6710  11272   9106  -1048    915   1697       C  
ATOM   2436  O   ILE A 341      12.486 -12.507  55.113  1.00 78.51           O  
ANISOU 2436  O   ILE A 341     7541  12254  10035  -1080    843   1758       O  
ATOM   2437  CB  ILE A 341      15.463 -13.404  56.466  1.00 49.72           C  
ANISOU 2437  CB  ILE A 341     4321   8243   6327  -1191    823   1633       C  
ATOM   2438  CG1 ILE A 341      16.852 -13.645  55.874  1.00 55.60           C  
ANISOU 2438  CG1 ILE A 341     5243   8778   7104  -1205    738   1599       C  
ATOM   2439  CG2 ILE A 341      14.617 -14.653  56.350  1.00 54.72           C  
ANISOU 2439  CG2 ILE A 341     4932   8954   6903  -1337    745   1689       C  
ATOM   2440  CD1 ILE A 341      17.616 -14.769  56.548  1.00 63.60           C  
ANISOU 2440  CD1 ILE A 341     6424   9684   8055  -1326    689   1571       C  
ATOM   2441  N   THR A 342      12.861 -11.831  57.227  1.00 75.57           N  
ANISOU 2441  N   THR A 342     7188  11915   9608  -1013   1039   1666       N  
ATOM   2442  CA  THR A 342      11.438 -11.783  57.541  1.00 63.51           C  
ANISOU 2442  CA  THR A 342     5486  10586   8058  -1011   1095   1700       C  
ATOM   2443  C   THR A 342      10.715 -10.733  56.707  1.00 61.20           C  
ANISOU 2443  C   THR A 342     5035  10373   7844   -861   1114   1719       C  
ATOM   2444  O   THR A 342       9.565 -10.944  56.309  1.00 67.86           O  
ANISOU 2444  O   THR A 342     5744  11352   8687   -886   1090   1776       O  
ATOM   2445  CB  THR A 342      11.246 -11.511  59.033  1.00 65.91           C  
ANISOU 2445  CB  THR A 342     5768  10971   8306   -991   1233   1651       C  
ATOM   2446  OG1 THR A 342      11.975 -12.487  59.786  1.00 63.14           O  
ANISOU 2446  OG1 THR A 342     5574  10535   7882  -1129   1206   1638       O  
ATOM   2447  CG2 THR A 342       9.778 -11.592  59.410  1.00 80.70           C  
ANISOU 2447  CG2 THR A 342     7465  13049  10149  -1007   1288   1686       C  
ATOM   2448  N   ASN A 343      11.373  -9.612  56.407  1.00 59.18           N  
ANISOU 2448  N   ASN A 343     4797  10031   7658   -705   1151   1675       N  
ATOM   2449  CA  ASN A 343      10.733  -8.569  55.611  1.00 68.79           C  
ANISOU 2449  CA  ASN A 343     5875  11307   8954   -548   1164   1691       C  
ATOM   2450  C   ASN A 343      10.527  -9.023  54.168  1.00 83.93           C  
ANISOU 2450  C   ASN A 343     7781  13201  10907   -605   1024   1767       C  
ATOM   2451  O   ASN A 343       9.439  -8.853  53.600  1.00 91.66           O  
ANISOU 2451  O   ASN A 343     8615  14302  11911   -574   1005   1818       O  
ATOM   2452  CB  ASN A 343      11.569  -7.291  55.670  1.00 63.96           C  
ANISOU 2452  CB  ASN A 343     5308  10590   8404   -367   1232   1622       C  
ATOM   2453  CG  ASN A 343      10.720  -6.046  55.795  1.00 63.00           C  
ANISOU 2453  CG  ASN A 343     5034  10571   8333   -177   1328   1594       C  
ATOM   2454  OD1 ASN A 343       9.594  -6.000  55.308  1.00 66.52           O  
ANISOU 2454  OD1 ASN A 343     5334  11140   8799   -160   1307   1644       O  
ATOM   2455  ND2 ASN A 343      11.256  -5.026  56.454  1.00 63.52           N  
ANISOU 2455  ND2 ASN A 343     5139  10578   8418    -30   1430   1511       N  
ATOM   2456  N   ILE A 344      11.566  -9.598  53.554  1.00 85.36           N  
ANISOU 2456  N   ILE A 344     8117  13225  11092   -686    925   1773       N  
ATOM   2457  CA  ILE A 344      11.435 -10.136  52.202  1.00 83.30           C  
ANISOU 2457  CA  ILE A 344     7867  12931  10853   -754    790   1839       C  
ATOM   2458  C   ILE A 344      10.383 -11.236  52.166  1.00 83.70           C  
ANISOU 2458  C   ILE A 344     7854  13108  10840   -902    735   1901       C  
ATOM   2459  O   ILE A 344       9.583 -11.323  51.225  1.00 92.08           O  
ANISOU 2459  O   ILE A 344     8824  14242  11921   -912    669   1965       O  
ATOM   2460  CB  ILE A 344      12.798 -10.640  51.692  1.00 79.37           C  
ANISOU 2460  CB  ILE A 344     7563  12235  10361   -822    701   1820       C  
ATOM   2461  CG1 ILE A 344      13.787  -9.480  51.555  1.00 74.87           C  
ANISOU 2461  CG1 ILE A 344     7042  11544   9861   -669    748   1770       C  
ATOM   2462  CG2 ILE A 344      12.638 -11.363  50.368  1.00 86.29           C  
ANISOU 2462  CG2 ILE A 344     8466  13078  11242   -912    561   1881       C  
ATOM   2463  CD1 ILE A 344      13.384  -8.450  50.522  1.00 76.70           C  
ANISOU 2463  CD1 ILE A 344     7169  11797  10176   -527    736   1802       C  
ATOM   2464  N   MET A 345      10.355 -12.084  53.197  1.00 76.89           N  
ANISOU 2464  N   MET A 345     7042  12274   9901  -1018    762   1885       N  
ATOM   2465  CA  MET A 345       9.354 -13.142  53.269  1.00 77.99           C  
ANISOU 2465  CA  MET A 345     7123  12533   9975  -1159    716   1943       C  
ATOM   2466  C   MET A 345       7.947 -12.558  53.329  1.00 80.96           C  
ANISOU 2466  C   MET A 345     7285  13108  10366  -1088    780   1980       C  
ATOM   2467  O   MET A 345       7.051 -12.988  52.594  1.00 79.68           O  
ANISOU 2467  O   MET A 345     7038  13038  10199  -1147    710   2049       O  
ATOM   2468  CB  MET A 345       9.636 -14.031  54.482  1.00 79.55           C  
ANISOU 2468  CB  MET A 345     7417  12720  10090  -1279    745   1915       C  
ATOM   2469  CG  MET A 345       8.710 -15.220  54.631  1.00 98.86           C  
ANISOU 2469  CG  MET A 345     9826  15275  12462  -1436    694   1973       C  
ATOM   2470  SD  MET A 345       9.122 -16.213  56.082  1.00125.25           S  
ANISOU 2470  SD  MET A 345    13291  18589  15709  -1567    726   1941       S  
ATOM   2471  CE  MET A 345       8.882 -15.022  57.400  1.00123.48           C  
ANISOU 2471  CE  MET A 345    12962  18468  15489  -1437    912   1884       C  
ATOM   2472  N   ALA A 346       7.738 -11.560  54.193  1.00 77.91           N  
ANISOU 2472  N   ALA A 346     6813  12791  10000   -957    914   1930       N  
ATOM   2473  CA  ALA A 346       6.424 -10.941  54.316  1.00 82.83           C  
ANISOU 2473  CA  ALA A 346     7231  13598  10643   -873    985   1952       C  
ATOM   2474  C   ALA A 346       6.002 -10.263  53.021  1.00 78.92           C  
ANISOU 2474  C   ALA A 346     6641  13117  10227   -770    926   1995       C  
ATOM   2475  O   ALA A 346       4.808 -10.226  52.700  1.00 93.89           O  
ANISOU 2475  O   ALA A 346     8380  15162  12130   -764    920   2047       O  
ATOM   2476  CB  ALA A 346       6.421  -9.939  55.469  1.00 88.17           C  
ANISOU 2476  CB  ALA A 346     7855  14316  11328   -735   1141   1874       C  
ATOM   2477  N   VAL A 347       6.959  -9.723  52.266  1.00 65.66           N  
ANISOU 2477  N   VAL A 347     5055  11286   8606   -691    882   1977       N  
ATOM   2478  CA  VAL A 347       6.607  -9.119  50.986  1.00 64.76           C  
ANISOU 2478  CA  VAL A 347     4866  11175   8565   -603    817   2023       C  
ATOM   2479  C   VAL A 347       6.258 -10.197  49.964  1.00 78.09           C  
ANISOU 2479  C   VAL A 347     6574  12875  10223   -759    678   2106       C  
ATOM   2480  O   VAL A 347       5.398  -9.988  49.098  1.00 80.61           O  
ANISOU 2480  O   VAL A 347     6776  13279  10573   -731    630   2166       O  
ATOM   2481  CB  VAL A 347       7.741  -8.205  50.497  1.00 66.92           C  
ANISOU 2481  CB  VAL A 347     5236  11281   8908   -472    814   1980       C  
ATOM   2482  CG1 VAL A 347       7.442  -7.678  49.100  1.00 71.27           C  
ANISOU 2482  CG1 VAL A 347     5729  11821   9529   -398    732   2035       C  
ATOM   2483  CG2 VAL A 347       7.924  -7.053  51.467  1.00 67.54           C  
ANISOU 2483  CG2 VAL A 347     5282  11362   9017   -301    954   1898       C  
ATOM   2484  N   ILE A 348       6.905 -11.361  50.044  1.00 85.51           N  
ANISOU 2484  N   ILE A 348     7664  13725  11100   -922    610   2108       N  
ATOM   2485  CA  ILE A 348       6.597 -12.450  49.117  1.00 87.32           C  
ANISOU 2485  CA  ILE A 348     7930  13956  11292  -1072    478   2177       C  
ATOM   2486  C   ILE A 348       5.205 -13.006  49.398  1.00 94.18           C  
ANISOU 2486  C   ILE A 348     8655  15018  12111  -1154    485   2234       C  
ATOM   2487  O   ILE A 348       4.311 -12.950  48.546  1.00 93.23           O  
ANISOU 2487  O   ILE A 348     8423  14992  12009  -1153    432   2300       O  
ATOM   2488  CB  ILE A 348       7.671 -13.549  49.196  1.00 92.95           C  
ANISOU 2488  CB  ILE A 348     8851  14513  11952  -1210    406   2152       C  
ATOM   2489  CG1 ILE A 348       8.995 -13.046  48.607  1.00 87.44           C  
ANISOU 2489  CG1 ILE A 348     8289  13624  11310  -1138    376   2109       C  
ATOM   2490  CG2 ILE A 348       7.197 -14.807  48.480  1.00 97.96           C  
ANISOU 2490  CG2 ILE A 348     9520  15169  12529  -1374    284   2216       C  
ATOM   2491  CD1 ILE A 348      10.135 -14.040  48.712  1.00 76.51           C  
ANISOU 2491  CD1 ILE A 348     7113  12075   9883  -1253    311   2070       C  
ATOM   2492  N   CYS A 349       5.001 -13.555  50.599  1.00143.15           N  
ANISOU 2492  N   CYS A 349    12268  22874  19249  -3312  -2542  -1016       N  
ATOM   2493  CA  CYS A 349       3.690 -14.067  51.006  1.00149.24           C  
ANISOU 2493  CA  CYS A 349    12746  23467  20492  -3383  -2573  -1062       C  
ATOM   2494  C   CYS A 349       2.945 -12.951  51.735  1.00144.34           C  
ANISOU 2494  C   CYS A 349    11922  22778  20141  -3156  -2550   -748       C  
ATOM   2495  O   CYS A 349       2.930 -12.860  52.964  1.00150.21           O  
ANISOU 2495  O   CYS A 349    12612  23295  21167  -3057  -2239   -628       O  
ATOM   2496  CB  CYS A 349       3.836 -15.315  51.871  1.00152.73           C  
ANISOU 2496  CB  CYS A 349    13173  23612  21245  -3520  -2243  -1230       C  
ATOM   2497  SG  CYS A 349       5.005 -15.187  53.256  1.00149.02           S  
ANISOU 2497  SG  CYS A 349    12875  22954  20790  -3368  -1776  -1058       S  
ATOM   2498  N   LYS A 350       2.314 -12.079  50.945  1.00138.46           N  
ANISOU 2498  N   LYS A 350    11063  22240  19304  -3070  -2872   -616       N  
ATOM   2499  CA  LYS A 350       1.596 -10.948  51.526  1.00129.84           C  
ANISOU 2499  CA  LYS A 350     9764  21084  18484  -2850  -2844   -339       C  
ATOM   2500  C   LYS A 350       0.372 -11.413  52.309  1.00141.08           C  
ANISOU 2500  C   LYS A 350    10876  22264  20463  -2888  -2746   -389       C  
ATOM   2501  O   LYS A 350       0.069 -10.871  53.378  1.00136.66           O  
ANISOU 2501  O   LYS A 350    10204  21524  20195  -2737  -2488   -247       O  
ATOM   2502  CB  LYS A 350       1.197  -9.964  50.426  1.00121.53           C  
ANISOU 2502  CB  LYS A 350     8643  20314  17220  -2749  -3209   -168       C  
ATOM   2503  CG  LYS A 350       0.721  -8.617  50.942  1.00117.56           C  
ANISOU 2503  CG  LYS A 350     7969  19757  16941  -2496  -3141    145       C  
ATOM   2504  CD  LYS A 350       1.844  -7.883  51.662  1.00109.57           C  
ANISOU 2504  CD  LYS A 350     7169  18659  15801  -2343  -2836    305       C  
ATOM   2505  CE  LYS A 350       1.400  -6.508  52.135  1.00107.46           C  
ANISOU 2505  CE  LYS A 350     6736  18320  15773  -2103  -2747    593       C  
ATOM   2506  NZ  LYS A 350       2.508  -5.783  52.816  1.00 97.33           N  
ANISOU 2506  NZ  LYS A 350     5651  16950  14382  -1969  -2455    715       N  
ATOM   2507  N   GLU A 351      -0.345 -12.413  51.793  1.00153.71           N  
ANISOU 2507  N   GLU A 351    12332  23855  22217  -3096  -2934   -605       N  
ATOM   2508  CA  GLU A 351      -1.488 -12.992  52.484  1.00165.28           C  
ANISOU 2508  CA  GLU A 351    13486  25071  24240  -3162  -2838   -659       C  
ATOM   2509  C   GLU A 351      -1.333 -14.475  52.787  1.00168.24           C  
ANISOU 2509  C   GLU A 351    13904  25250  24770  -3406  -2673   -838       C  
ATOM   2510  O   GLU A 351      -2.187 -15.035  53.484  1.00169.73           O  
ANISOU 2510  O   GLU A 351    13860  25214  25417  -3483  -2543   -778       O  
ATOM   2511  CB  GLU A 351      -2.779 -12.786  51.672  1.00173.82           C  
ANISOU 2511  CB  GLU A 351    14258  26287  25501  -3189  -3218   -701       C  
ATOM   2512  CG  GLU A 351      -3.232 -11.337  51.554  1.00176.64           C  
ANISOU 2512  CG  GLU A 351    14482  26814  25817  -2936  -3319   -478       C  
ATOM   2513  CD  GLU A 351      -2.606 -10.618  50.376  1.00178.92           C  
ANISOU 2513  CD  GLU A 351    14971  27433  25576  -2874  -3628   -341       C  
ATOM   2514  OE1 GLU A 351      -1.820 -11.251  49.640  1.00180.22           O  
ANISOU 2514  OE1 GLU A 351    15387  27732  25358  -3030  -3748   -490       O  
ATOM   2515  OE2 GLU A 351      -2.903  -9.420  50.186  1.00180.14           O  
ANISOU 2515  OE2 GLU A 351    15032  27720  25692  -2670  -3723    -81       O  
ATOM   2516  N   SER A 352      -0.278 -15.125  52.292  1.00165.86           N  
ANISOU 2516  N   SER A 352    13888  25038  24093  -3537  -2650  -1026       N  
ATOM   2517  CA  SER A 352      -0.115 -16.558  52.513  1.00164.66           C  
ANISOU 2517  CA  SER A 352    13774  24705  24083  -3768  -2459  -1242       C  
ATOM   2518  C   SER A 352       0.424 -16.862  53.907  1.00155.32           C  
ANISOU 2518  C   SER A 352    12663  23265  23086  -3689  -1985  -1107       C  
ATOM   2519  O   SER A 352       0.002 -17.839  54.536  1.00159.21           O  
ANISOU 2519  O   SER A 352    13047  23549  23898  -3812  -1764  -1127       O  
ATOM   2520  CB  SER A 352       0.803 -17.151  51.443  1.00167.00           C  
ANISOU 2520  CB  SER A 352    14334  25169  23950  -3930  -2576  -1556       C  
ATOM   2521  OG  SER A 352       0.953 -18.549  51.619  1.00168.71           O  
ANISOU 2521  OG  SER A 352    14575  25172  24355  -4147  -2360  -1813       O  
ATOM   2522  N   CYS A 353       1.346 -16.046  54.407  1.00144.84           N  
ANISOU 2522  N   CYS A 353    11525  21977  21532  -3487  -1816   -954       N  
ATOM   2523  CA  CYS A 353       1.914 -16.266  55.727  1.00135.74           C  
ANISOU 2523  CA  CYS A 353    10455  20622  20499  -3396  -1385   -816       C  
ATOM   2524  C   CYS A 353       1.126 -15.505  56.793  1.00124.74           C  
ANISOU 2524  C   CYS A 353     8867  19117  19411  -3218  -1233   -540       C  
ATOM   2525  O   CYS A 353       0.318 -14.621  56.501  1.00122.66           O  
ANISOU 2525  O   CYS A 353     8426  18919  19260  -3124  -1442   -469       O  
ATOM   2526  CB  CYS A 353       3.388 -15.853  55.761  1.00141.57           C  
ANISOU 2526  CB  CYS A 353    11506  21467  20817  -3293  -1264   -806       C  
ATOM   2527  SG  CYS A 353       4.455 -16.664  54.542  1.00151.44           S  
ANISOU 2527  SG  CYS A 353    13002  22850  21689  -3492  -1386  -1126       S  
ATOM   2528  N   ASN A 354       1.381 -15.862  58.049  1.00121.99           N  
ANISOU 2528  N   ASN A 354     8555  18603  19193  -3164   -845   -395       N  
ATOM   2529  CA  ASN A 354       0.729 -15.221  59.184  1.00126.53           C  
ANISOU 2529  CA  ASN A 354     9008  19111  19958  -3007   -633   -126       C  
ATOM   2530  C   ASN A 354       1.345 -13.845  59.402  1.00127.47           C  
ANISOU 2530  C   ASN A 354     9240  19267  19928  -2768   -587   -152       C  
ATOM   2531  O   ASN A 354       2.558 -13.729  59.606  1.00134.38           O  
ANISOU 2531  O   ASN A 354    10385  20214  20459  -2712   -464   -140       O  
ATOM   2532  CB  ASN A 354       0.878 -16.090  60.432  1.00128.62           C  
ANISOU 2532  CB  ASN A 354     9321  19358  20190  -3055   -215    -25       C  
ATOM   2533  CG  ASN A 354       0.019 -15.613  61.591  1.00132.18           C  
ANISOU 2533  CG  ASN A 354     9660  19918  20646  -2963     58     32       C  
ATOM   2534  OD1 ASN A 354      -0.417 -14.463  61.631  1.00134.37           O  
ANISOU 2534  OD1 ASN A 354     9881  20316  20857  -2834      6      6       O  
ATOM   2535  ND2 ASN A 354      -0.228 -16.504  62.542  1.00134.99           N  
ANISOU 2535  ND2 ASN A 354    10003  20108  21181  -2990    377     57       N  
ATOM   2536  N   GLU A 355       0.508 -12.805  59.375  1.00118.61           N  
ANISOU 2536  N   GLU A 355     7967  18197  18901  -2641   -660   -186       N  
ATOM   2537  CA  GLU A 355       1.020 -11.443  59.478  1.00113.89           C  
ANISOU 2537  CA  GLU A 355     7478  17734  18060  -2458   -657    -75       C  
ATOM   2538  C   GLU A 355       1.248 -11.014  60.924  1.00112.34           C  
ANISOU 2538  C   GLU A 355     7354  17455  17876  -2327   -247     -4       C  
ATOM   2539  O   GLU A 355       2.084 -10.139  61.179  1.00106.99           O  
ANISOU 2539  O   GLU A 355     6862  16826  16964  -2195   -181    109       O  
ATOM   2540  CB  GLU A 355       0.071 -10.471  58.774  1.00105.13           C  
ANISOU 2540  CB  GLU A 355     6160  16764  17023  -2387   -919    -66       C  
ATOM   2541  CG  GLU A 355       0.245 -10.432  57.260  1.00106.69           C  
ANISOU 2541  CG  GLU A 355     6391  17138  17010  -2454  -1360    -70       C  
ATOM   2542  CD  GLU A 355       1.579  -9.826  56.832  1.00117.46           C  
ANISOU 2542  CD  GLU A 355     8057  18646  17927  -2379  -1418     36       C  
ATOM   2543  OE1 GLU A 355       2.173  -9.058  57.620  1.00120.85           O  
ANISOU 2543  OE1 GLU A 355     8606  19030  18283  -2231  -1177    152       O  
ATOM   2544  OE2 GLU A 355       2.037 -10.119  55.707  1.00119.33           O  
ANISOU 2544  OE2 GLU A 355     8411  19060  17870  -2478  -1692    -26       O  
ATOM   2545  N   ASP A 356       0.527 -11.609  61.876  1.00111.35           N  
ANISOU 2545  N   ASP A 356     7140  17314  17855  -2383     33    -75       N  
ATOM   2546  CA  ASP A 356       0.717 -11.246  63.277  1.00112.13           C  
ANISOU 2546  CA  ASP A 356     7327  17414  17863  -2283    405     17       C  
ATOM   2547  C   ASP A 356       2.053 -11.766  63.793  1.00104.74           C  
ANISOU 2547  C   ASP A 356     6645  16317  16835  -2249    588     81       C  
ATOM   2548  O   ASP A 356       2.834 -11.020  64.403  1.00104.17           O  
ANISOU 2548  O   ASP A 356     6727  16260  16594  -2120    727    185       O  
ATOM   2549  CB  ASP A 356      -0.438 -11.794  64.115  1.00117.20           C  
ANISOU 2549  CB  ASP A 356     7780  18135  18615  -2364    598    130       C  
ATOM   2550  CG  ASP A 356      -1.791 -11.456  63.527  1.00126.05           C  
ANISOU 2550  CG  ASP A 356     8636  19272  19986  -2380    392    148       C  
ATOM   2551  OD1 ASP A 356      -1.829 -10.767  62.486  1.00129.71           O  
ANISOU 2551  OD1 ASP A 356     9033  19810  20442  -2348     94     83       O  
ATOM   2552  OD2 ASP A 356      -2.816 -11.885  64.099  1.00132.19           O  
ANISOU 2552  OD2 ASP A 356     9267  19959  21001  -2410    531    219       O  
ATOM   2553  N   VAL A 357       2.331 -13.051  63.554  1.00 99.63           N  
ANISOU 2553  N   VAL A 357     6041  15580  16235  -2376    585     62       N  
ATOM   2554  CA  VAL A 357       3.621 -13.617  63.930  1.00 96.95           C  
ANISOU 2554  CA  VAL A 357     5909  15221  15706  -2371    729    181       C  
ATOM   2555  C   VAL A 357       4.749 -12.890  63.211  1.00 99.42           C  
ANISOU 2555  C   VAL A 357     6453  15712  15609  -2315    520    187       C  
ATOM   2556  O   VAL A 357       5.801 -12.619  63.798  1.00104.97           O  
ANISOU 2556  O   VAL A 357     7377  16485  16023  -2226    670    249       O  
ATOM   2557  CB  VAL A 357       3.647 -15.130  63.643  1.00 94.58           C  
ANISOU 2557  CB  VAL A 357     5591  14796  15549  -2528    739    192       C  
ATOM   2558  CG1 VAL A 357       4.965 -15.741  64.098  1.00 87.49           C  
ANISOU 2558  CG1 VAL A 357     4902  13919  14423  -2524    941    245       C  
ATOM   2559  CG2 VAL A 357       2.476 -15.816  64.326  1.00102.32           C  
ANISOU 2559  CG2 VAL A 357     6412  16030  16434  -2677    891    237       C  
ATOM   2560  N   ILE A 358       4.542 -12.542  61.939  1.00 95.17           N  
ANISOU 2560  N   ILE A 358     5864  15267  15030  -2368    177    107       N  
ATOM   2561  CA  ILE A 358       5.560 -11.799  61.201  1.00 86.74           C  
ANISOU 2561  CA  ILE A 358     5003  14376  13579  -2315     -4     99       C  
ATOM   2562  C   ILE A 358       5.750 -10.411  61.802  1.00 87.11           C  
ANISOU 2562  C   ILE A 358     5102  14465  13533  -2130     95    197       C  
ATOM   2563  O   ILE A 358       6.877  -9.905  61.883  1.00 99.34           O  
ANISOU 2563  O   ILE A 358     6865  16105  14775  -2057    136    222       O  
ATOM   2564  CB  ILE A 358       5.198 -11.738  59.704  1.00 87.07           C  
ANISOU 2564  CB  ILE A 358     4968  14535  13582  -2411   -391      5       C  
ATOM   2565  CG1 ILE A 358       5.554 -13.059  59.016  1.00 83.24           C  
ANISOU 2565  CG1 ILE A 358     4539  14050  13039  -2610   -471   -154       C  
ATOM   2566  CG2 ILE A 358       5.899 -10.580  59.015  1.00 86.70           C  
ANISOU 2566  CG2 ILE A 358     5061  14667  13213  -2306   -566     59       C  
ATOM   2567  CD1 ILE A 358       5.226 -13.091  57.542  1.00 83.69           C  
ANISOU 2567  CD1 ILE A 358     4545  14256  12995  -2729   -854   -289       C  
ATOM   2568  N   GLY A 359       4.659  -9.778  62.241  1.00 79.25           N  
ANISOU 2568  N   GLY A 359     3896  13390  12825  -2061    155    230       N  
ATOM   2569  CA  GLY A 359       4.779  -8.482  62.892  1.00 78.36           C  
ANISOU 2569  CA  GLY A 359     3807  13285  12681  -1902    298    289       C  
ATOM   2570  C   GLY A 359       5.599  -8.548  64.166  1.00 86.17           C  
ANISOU 2570  C   GLY A 359     4984  14263  13494  -1846    621    313       C  
ATOM   2571  O   GLY A 359       6.464  -7.701  64.410  1.00 76.47           O  
ANISOU 2571  O   GLY A 359     3912  13108  12036  -1755    677    324       O  
ATOM   2572  N   ALA A 360       5.333  -9.558  65.001  1.00 86.61           N  
ANISOU 2572  N   ALA A 360     5016  14236  13656  -1901    837    323       N  
ATOM   2573  CA  ALA A 360       6.135  -9.745  66.208  1.00 82.59           C  
ANISOU 2573  CA  ALA A 360     4690  13758  12931  -1850   1122    370       C  
ATOM   2574  C   ALA A 360       7.593 -10.041  65.865  1.00 83.88           C  
ANISOU 2574  C   ALA A 360     5110  14036  12723  -1860   1043    372       C  
ATOM   2575  O   ALA A 360       8.515  -9.525  66.516  1.00 98.20           O  
ANISOU 2575  O   ALA A 360     7100  15941  14269  -1779   1160    385       O  
ATOM   2576  CB  ALA A 360       5.541 -10.864  67.062  1.00 83.37           C  
ANISOU 2576  CB  ALA A 360     4699  13752  13224  -1908   1364    412       C  
ATOM   2577  N   LEU A 361       7.821 -10.872  64.842  1.00 74.38           N  
ANISOU 2577  N   LEU A 361     3920  12831  11510  -1969    849    339       N  
ATOM   2578  CA  LEU A 361       9.183 -11.184  64.427  1.00 76.00           C  
ANISOU 2578  CA  LEU A 361     4347  13129  11401  -1987    787    327       C  
ATOM   2579  C   LEU A 361       9.935  -9.925  64.023  1.00 78.15           C  
ANISOU 2579  C   LEU A 361     4746  13521  11428  -1896    668    303       C  
ATOM   2580  O   LEU A 361      11.089  -9.733  64.418  1.00 80.06           O  
ANISOU 2580  O   LEU A 361     5177  13836  11406  -1841    752    317       O  
ATOM   2581  CB  LEU A 361       9.169 -12.187  63.272  1.00 74.84           C  
ANISOU 2581  CB  LEU A 361     4163  12959  11315  -2141    600    250       C  
ATOM   2582  CG  LEU A 361       8.714 -13.618  63.568  1.00 73.90           C  
ANISOU 2582  CG  LEU A 361     3934  12693  11450  -2258    741    258       C  
ATOM   2583  CD1 LEU A 361       8.811 -14.483  62.316  1.00 74.80           C  
ANISOU 2583  CD1 LEU A 361     4024  12795  11604  -2433    545    117       C  
ATOM   2584  CD2 LEU A 361       9.512 -14.221  64.715  1.00 73.06           C  
ANISOU 2584  CD2 LEU A 361     3956  12558  11244  -2201   1035    387       C  
ATOM   2585  N   LEU A 362       9.291  -9.046  63.250  1.00 70.49           N  
ANISOU 2585  N   LEU A 362     3655  12564  10564  -1874    477    281       N  
ATOM   2586  CA  LEU A 362       9.931  -7.786  62.883  1.00 73.05           C  
ANISOU 2586  CA  LEU A 362     4064  12973  10716  -1779    396    284       C  
ATOM   2587  C   LEU A 362      10.179  -6.914  64.109  1.00 79.05           C  
ANISOU 2587  C   LEU A 362     4869  13717  11447  -1665    640    287       C  
ATOM   2588  O   LEU A 362      11.256  -6.317  64.251  1.00 83.46           O  
ANISOU 2588  O   LEU A 362     5588  14344  11777  -1609    679    264       O  
ATOM   2589  CB  LEU A 362       9.083  -7.041  61.853  1.00 70.79           C  
ANISOU 2589  CB  LEU A 362     3602  12701  10592  -1765    156    309       C  
ATOM   2590  CG  LEU A 362       9.013  -7.680  60.466  1.00 71.64           C  
ANISOU 2590  CG  LEU A 362     3696  12897  10628  -1881   -140    282       C  
ATOM   2591  CD1 LEU A 362       8.214  -6.807  59.517  1.00 76.26           C  
ANISOU 2591  CD1 LEU A 362     4107  13537  11331  -1839   -391    352       C  
ATOM   2592  CD2 LEU A 362      10.410  -7.927  59.916  1.00 79.34           C  
ANISOU 2592  CD2 LEU A 362     4905  13985  11256  -1916   -188    246       C  
ATOM   2593  N   ASN A 363       9.195  -6.835  65.012  1.00 75.61           N  
ANISOU 2593  N   ASN A 363     4287  13196  11245  -1641    817    296       N  
ATOM   2594  CA  ASN A 363       9.343  -6.023  66.216  1.00 83.75           C  
ANISOU 2594  CA  ASN A 363     5350  14229  12241  -1554   1067    264       C  
ATOM   2595  C   ASN A 363      10.488  -6.499  67.100  1.00 78.15           C  
ANISOU 2595  C   ASN A 363     4862  13622  11209  -1552   1217    255       C  
ATOM   2596  O   ASN A 363      11.004  -5.712  67.902  1.00 74.60           O  
ANISOU 2596  O   ASN A 363     4493  13236  10617  -1492   1361    193       O  
ATOM   2597  CB  ASN A 363       8.038  -6.019  67.011  1.00 88.23           C  
ANISOU 2597  CB  ASN A 363     5714  14692  13117  -1544   1252    277       C  
ATOM   2598  CG  ASN A 363       6.898  -5.363  66.255  1.00 89.49           C  
ANISOU 2598  CG  ASN A 363     5623  14750  13630  -1524   1118    289       C  
ATOM   2599  OD1 ASN A 363       7.111  -4.448  65.462  1.00 87.61           O  
ANISOU 2599  OD1 ASN A 363     5363  14529  13397  -1475    961    291       O  
ATOM   2600  ND2 ASN A 363       5.681  -5.836  66.492  1.00 99.49           N  
ANISOU 2600  ND2 ASN A 363     6683  15912  15207  -1560   1183    304       N  
ATOM   2601  N   VAL A 364      10.872  -7.768  66.998  1.00 68.54           N  
ANISOU 2601  N   VAL A 364     3725  12423   9894  -1620   1192    314       N  
ATOM   2602  CA  VAL A 364      12.042  -8.256  67.729  1.00 70.85           C  
ANISOU 2602  CA  VAL A 364     4210  12820   9888  -1608   1302    346       C  
ATOM   2603  C   VAL A 364      13.332  -8.067  66.927  1.00 79.43           C  
ANISOU 2603  C   VAL A 364     5460  13977  10743  -1606   1141    317       C  
ATOM   2604  O   VAL A 364      14.381  -7.697  67.476  1.00 69.33           O  
ANISOU 2604  O   VAL A 364     4323  12802   9219  -1559   1201    295       O  
ATOM   2605  CB  VAL A 364      11.828  -9.732  68.113  1.00 68.05           C  
ANISOU 2605  CB  VAL A 364     3835  12422   9600  -1668   1406    459       C  
ATOM   2606  CG1 VAL A 364      13.067 -10.290  68.792  1.00 68.94           C  
ANISOU 2606  CG1 VAL A 364     4125  12647   9423  -1643   1499    541       C  
ATOM   2607  CG2 VAL A 364      10.628  -9.864  69.016  1.00 70.21           C  
ANISOU 2607  CG2 VAL A 364     3953  12631  10092  -1663   1606    496       C  
ATOM   2608  N   PHE A 365      13.274  -8.306  65.616  1.00 76.65           N  
ANISOU 2608  N   PHE A 365     5080  13584  10459  -1663    934    307       N  
ATOM   2609  CA  PHE A 365      14.488  -8.314  64.812  1.00 73.45           C  
ANISOU 2609  CA  PHE A 365     4825  13241   9841  -1674    810    290       C  
ATOM   2610  C   PHE A 365      15.032  -6.908  64.591  1.00 76.10           C  
ANISOU 2610  C   PHE A 365     5212  13625  10078  -1596    762    231       C  
ATOM   2611  O   PHE A 365      16.249  -6.730  64.438  1.00 70.95           O  
ANISOU 2611  O   PHE A 365     4705  13034   9221  -1577    747    215       O  
ATOM   2612  CB  PHE A 365      14.215  -9.018  63.484  1.00 65.07           C  
ANISOU 2612  CB  PHE A 365     3714  12153   8858  -1779    617    276       C  
ATOM   2613  CG  PHE A 365      13.826 -10.468  63.634  1.00 64.61           C  
ANISOU 2613  CG  PHE A 365     3598  12017   8933  -1877    685    306       C  
ATOM   2614  CD1 PHE A 365      14.069 -11.150  64.817  1.00 64.76           C  
ANISOU 2614  CD1 PHE A 365     3654  12009   8943  -1849    907    396       C  
ATOM   2615  CD2 PHE A 365      13.226 -11.151  62.587  1.00 65.82           C  
ANISOU 2615  CD2 PHE A 365     3649  12132   9228  -2003    530    245       C  
ATOM   2616  CE1 PHE A 365      13.716 -12.481  64.955  1.00 66.03           C  
ANISOU 2616  CE1 PHE A 365     3742  12068   9279  -1932   1001    451       C  
ATOM   2617  CE2 PHE A 365      12.873 -12.483  62.722  1.00 67.11           C  
ANISOU 2617  CE2 PHE A 365     3738  12190   9569  -2109    618    249       C  
ATOM   2618  CZ  PHE A 365      13.119 -13.146  63.906  1.00 67.17           C  
ANISOU 2618  CZ  PHE A 365     3774  12135   9613  -2067    869    367       C  
ATOM   2619  N   VAL A 366      14.160  -5.897  64.596  1.00 77.55           N  
ANISOU 2619  N   VAL A 366     5258  13764  10443  -1549    759    204       N  
ATOM   2620  CA  VAL A 366      14.646  -4.521  64.516  1.00 77.17           C  
ANISOU 2620  CA  VAL A 366     5228  13727  10366  -1472    768    151       C  
ATOM   2621  C   VAL A 366      15.523  -4.203  65.721  1.00 75.43           C  
ANISOU 2621  C   VAL A 366     5130  13565   9966  -1436    952     73       C  
ATOM   2622  O   VAL A 366      16.574  -3.556  65.600  1.00 76.62           O  
ANISOU 2622  O   VAL A 366     5380  13753   9980  -1407    944     18       O  
ATOM   2623  CB  VAL A 366      13.463  -3.544  64.395  1.00 79.98           C  
ANISOU 2623  CB  VAL A 366     5375  13996  11019  -1423    771    156       C  
ATOM   2624  CG1 VAL A 366      13.947  -2.116  64.467  1.00 79.76           C  
ANISOU 2624  CG1 VAL A 366     5339  13943  11025  -1344    842     96       C  
ATOM   2625  CG2 VAL A 366      12.727  -3.773  63.099  1.00 88.60           C  
ANISOU 2625  CG2 VAL A 366     6341  15079  12242  -1458    532    246       C  
ATOM   2626  N   TRP A 367      15.129  -4.680  66.900  1.00 74.40           N  
ANISOU 2626  N   TRP A 367     4986  13462   9821  -1443   1116     69       N  
ATOM   2627  CA  TRP A 367      15.949  -4.445  68.079  1.00 68.95           C  
ANISOU 2627  CA  TRP A 367     4403  12891   8905  -1423   1263     -3       C  
ATOM   2628  C   TRP A 367      17.190  -5.326  68.097  1.00 64.42           C  
ANISOU 2628  C   TRP A 367     3988  12418   8070  -1444   1211     64       C  
ATOM   2629  O   TRP A 367      18.213  -4.927  68.662  1.00 61.21           O  
ANISOU 2629  O   TRP A 367     3674  12126   7456  -1427   1247     -2       O  
ATOM   2630  CB  TRP A 367      15.109  -4.632  69.339  1.00 65.98           C  
ANISOU 2630  CB  TRP A 367     3952  12553   8564  -1423   1464    -11       C  
ATOM   2631  CG  TRP A 367      14.219  -3.459  69.543  1.00 70.10           C  
ANISOU 2631  CG  TRP A 367     4331  12987   9318  -1389   1568   -120       C  
ATOM   2632  CD1 TRP A 367      12.890  -3.376  69.259  1.00 74.25           C  
ANISOU 2632  CD1 TRP A 367     4674  13374  10165  -1381   1588    -76       C  
ATOM   2633  CD2 TRP A 367      14.606  -2.173  70.040  1.00 75.59           C  
ANISOU 2633  CD2 TRP A 367     5029  13706   9984  -1359   1677   -297       C  
ATOM   2634  NE1 TRP A 367      12.418  -2.122  69.564  1.00 74.91           N  
ANISOU 2634  NE1 TRP A 367     4644  13385  10433  -1334   1716   -189       N  
ATOM   2635  CE2 TRP A 367      13.453  -1.364  70.045  1.00 73.64           C  
ANISOU 2635  CE2 TRP A 367     4599  13314  10066  -1324   1782   -339       C  
ATOM   2636  CE3 TRP A 367      15.813  -1.632  70.494  1.00 66.06           C  
ANISOU 2636  CE3 TRP A 367     3944  12624   8531  -1365   1701   -434       C  
ATOM   2637  CZ2 TRP A 367      13.471  -0.041  70.485  1.00 77.94           C  
ANISOU 2637  CZ2 TRP A 367     5087  13813  10713  -1293   1935   -515       C  
ATOM   2638  CZ3 TRP A 367      15.830  -0.317  70.927  1.00 67.25           C  
ANISOU 2638  CZ3 TRP A 367     4040  12742   8770  -1349   1837   -637       C  
ATOM   2639  CH2 TRP A 367      14.668   0.464  70.919  1.00 73.22           C  
ANISOU 2639  CH2 TRP A 367     4622  13330   9867  -1312   1964   -678       C  
ATOM   2640  N   ILE A 368      17.134  -6.507  67.480  1.00 65.08           N  
ANISOU 2640  N   ILE A 368     4086  12458   8185  -1486   1130    186       N  
ATOM   2641  CA  ILE A 368      18.374  -7.254  67.256  1.00 63.21           C  
ANISOU 2641  CA  ILE A 368     3981  12274   7763  -1498   1081    254       C  
ATOM   2642  C   ILE A 368      19.354  -6.421  66.428  1.00 69.30           C  
ANISOU 2642  C   ILE A 368     4830  13047   8452  -1479    971    177       C  
ATOM   2643  O   ILE A 368      20.554  -6.344  66.737  1.00 64.52           O  
ANISOU 2643  O   ILE A 368     4325  12523   7666  -1458    982    169       O  
ATOM   2644  CB  ILE A 368      18.080  -8.613  66.594  1.00 60.20           C  
ANISOU 2644  CB  ILE A 368     3575  11806   7493  -1562   1037    364       C  
ATOM   2645  CG1 ILE A 368      17.121  -9.428  67.457  1.00 65.17           C  
ANISOU 2645  CG1 ILE A 368     4109  12407   8244  -1579   1177    453       C  
ATOM   2646  CG2 ILE A 368      19.368  -9.391  66.378  1.00 59.30           C  
ANISOU 2646  CG2 ILE A 368     3577  11718   7235  -1569   1024    440       C  
ATOM   2647  CD1 ILE A 368      16.950 -10.851  66.982  1.00 69.00           C  
ANISOU 2647  CD1 ILE A 368     4559  12788   8871  -1651   1181    554       C  
ATOM   2648  N   GLY A 369      18.855  -5.774  65.370  1.00 72.56           N  
ANISOU 2648  N   GLY A 369     5181  13381   9009  -1483    865    138       N  
ATOM   2649  CA  GLY A 369      19.712  -4.910  64.566  1.00 59.15           C  
ANISOU 2649  CA  GLY A 369     3538  11680   7257  -1458    786     91       C  
ATOM   2650  C   GLY A 369      20.232  -3.710  65.339  1.00 63.93           C  
ANISOU 2650  C   GLY A 369     4155  12311   7824  -1406    884    -26       C  
ATOM   2651  O   GLY A 369      21.364  -3.263  65.134  1.00 62.58           O  
ANISOU 2651  O   GLY A 369     4063  12161   7555  -1391    871    -67       O  
ATOM   2652  N   TYR A 370      19.416  -3.172  66.244  1.00 78.24           N  
ANISOU 2652  N   TYR A 370     5877  14120   9733  -1389    998   -100       N  
ATOM   2653  CA  TYR A 370      19.897  -2.084  67.096  1.00 84.97           C  
ANISOU 2653  CA  TYR A 370     6729  15012  10546  -1366   1116   -261       C  
ATOM   2654  C   TYR A 370      20.982  -2.571  68.057  1.00 80.99           C  
ANISOU 2654  C   TYR A 370     6333  14681   9759  -1388   1154   -289       C  
ATOM   2655  O   TYR A 370      21.945  -1.848  68.346  1.00 83.75           O  
ANISOU 2655  O   TYR A 370     6716  15087  10017  -1389   1174   -415       O  
ATOM   2656  CB  TYR A 370      18.730  -1.456  67.858  1.00 92.83           C  
ANISOU 2656  CB  TYR A 370     7590  15969  11711  -1353   1259   -349       C  
ATOM   2657  CG  TYR A 370      17.712  -0.767  66.970  1.00 94.00           C  
ANISOU 2657  CG  TYR A 370     7587  15950  12179  -1317   1225   -310       C  
ATOM   2658  CD1 TYR A 370      18.027  -0.407  65.665  1.00 90.93           C  
ANISOU 2658  CD1 TYR A 370     7187  15492  11870  -1295   1085   -232       C  
ATOM   2659  CD2 TYR A 370      16.439  -0.471  67.440  1.00 91.17           C  
ANISOU 2659  CD2 TYR A 370     7076  15522  12043  -1301   1338   -329       C  
ATOM   2660  CE1 TYR A 370      17.099   0.224  64.854  1.00 89.52           C  
ANISOU 2660  CE1 TYR A 370     6839  15206  11969  -1255   1033   -154       C  
ATOM   2661  CE2 TYR A 370      15.507   0.162  66.639  1.00 85.52           C  
ANISOU 2661  CE2 TYR A 370     6185  14663  11645  -1259   1296   -262       C  
ATOM   2662  CZ  TYR A 370      15.843   0.508  65.347  1.00 83.70           C  
ANISOU 2662  CZ  TYR A 370     5935  14392  11473  -1234   1132   -166       C  
ATOM   2663  OH  TYR A 370      14.915   1.135  64.544  1.00 77.53           O  
ANISOU 2663  OH  TYR A 370     4952  13511  10994  -1184   1068    -58       O  
ATOM   2664  N   LEU A 371      20.848  -3.800  68.560  1.00 73.79           N  
ANISOU 2664  N   LEU A 371     5452  13859   8725  -1406   1163   -161       N  
ATOM   2665  CA  LEU A 371      21.922  -4.386  69.355  1.00 71.92           C  
ANISOU 2665  CA  LEU A 371     5293  13808   8226  -1415   1171   -119       C  
ATOM   2666  C   LEU A 371      23.201  -4.512  68.534  1.00 78.11           C  
ANISOU 2666  C   LEU A 371     6164  14563   8953  -1408   1061    -79       C  
ATOM   2667  O   LEU A 371      24.308  -4.336  69.059  1.00 82.59           O  
ANISOU 2667  O   LEU A 371     6764  15269   9348  -1411   1053   -121       O  
ATOM   2668  CB  LEU A 371      21.497  -5.748  69.899  1.00 63.26           C  
ANISOU 2668  CB  LEU A 371     4192  12775   7071  -1421   1216     70       C  
ATOM   2669  CG  LEU A 371      22.439  -6.314  70.962  1.00 64.75           C  
ANISOU 2669  CG  LEU A 371     4417  13203   6984  -1417   1243    159       C  
ATOM   2670  CD1 LEU A 371      22.551  -5.344  72.129  1.00 66.36           C  
ANISOU 2670  CD1 LEU A 371     4584  13631   7000  -1436   1321    -28       C  
ATOM   2671  CD2 LEU A 371      21.969  -7.686  71.434  1.00 70.25           C  
ANISOU 2671  CD2 LEU A 371     5093  13922   7678  -1409   1312    394       C  
ATOM   2672  N   SER A 372      23.069  -4.841  67.248  1.00 76.44           N  
ANISOU 2672  N   SER A 372     5973  14193   8877  -1408    976     -2       N  
ATOM   2673  CA  SER A 372      24.233  -4.784  66.364  1.00 67.30           C  
ANISOU 2673  CA  SER A 372     4891  12993   7687  -1402    901     14       C  
ATOM   2674  C   SER A 372      24.809  -3.378  66.326  1.00 63.47           C  
ANISOU 2674  C   SER A 372     4395  12493   7226  -1386    913   -147       C  
ATOM   2675  O   SER A 372      26.031  -3.193  66.353  1.00 76.73           O  
ANISOU 2675  O   SER A 372     6120  14213   8819  -1383    899   -175       O  
ATOM   2676  CB  SER A 372      23.871  -5.224  64.946  1.00 65.80           C  
ANISOU 2676  CB  SER A 372     4710  12679   7614  -1424    820     90       C  
ATOM   2677  OG  SER A 372      23.480  -4.115  64.150  1.00 54.92           O  
ANISOU 2677  OG  SER A 372     3282  11228   6359  -1411    780     20       O  
ATOM   2678  N   SER A 373      23.936  -2.374  66.232  1.00 65.12           N  
ANISOU 2678  N   SER A 373     4522  12624   7598  -1375    952   -247       N  
ATOM   2679  CA  SER A 373      24.388  -0.986  66.276  1.00 73.20           C  
ANISOU 2679  CA  SER A 373     5505  13597   8711  -1363   1007   -410       C  
ATOM   2680  C   SER A 373      25.177  -0.690  67.545  1.00 79.03           C  
ANISOU 2680  C   SER A 373     6248  14496   9285  -1394   1071   -566       C  
ATOM   2681  O   SER A 373      26.071   0.163  67.538  1.00 85.24           O  
ANISOU 2681  O   SER A 373     7024  15263  10099  -1404   1092   -699       O  
ATOM   2682  CB  SER A 373      23.193  -0.039  66.164  1.00 77.82           C  
ANISOU 2682  CB  SER A 373     5965  14064   9539  -1340   1074   -475       C  
ATOM   2683  OG  SER A 373      23.594   1.308  66.333  1.00 77.46           O  
ANISOU 2683  OG  SER A 373     5859  13942   9629  -1332   1170   -646       O  
ATOM   2684  N   ALA A 374      24.856  -1.374  68.639  1.00 81.19           N  
ANISOU 2684  N   ALA A 374     6518  14948   9383  -1417   1104   -551       N  
ATOM   2685  CA  ALA A 374      25.563  -1.153  69.899  1.00 84.49           C  
ANISOU 2685  CA  ALA A 374     6916  15609   9579  -1463   1146   -694       C  
ATOM   2686  C   ALA A 374      26.837  -1.981  70.048  1.00 79.89           C  
ANISOU 2686  C   ALA A 374     6384  15186   8785  -1468   1052   -571       C  
ATOM   2687  O   ALA A 374      27.726  -1.585  70.809  1.00 78.15           O  
ANISOU 2687  O   ALA A 374     6123  15169   8402  -1512   1047   -704       O  
ATOM   2688  CB  ALA A 374      24.647  -1.455  71.087  1.00 83.60           C  
ANISOU 2688  CB  ALA A 374     6755  15672   9338  -1487   1243   -719       C  
ATOM   2689  N   VAL A 375      26.944  -3.119  69.357  1.00 83.80           N  
ANISOU 2689  N   VAL A 375     6945  15602   9295  -1431    985   -330       N  
ATOM   2690  CA  VAL A 375      27.988  -4.091  69.686  1.00 87.08           C  
ANISOU 2690  CA  VAL A 375     7380  16170   9536  -1423    927   -166       C  
ATOM   2691  C   VAL A 375      29.387  -3.614  69.288  1.00 89.28           C  
ANISOU 2691  C   VAL A 375     7665  16438   9820  -1427    870   -229       C  
ATOM   2692  O   VAL A 375      30.378  -4.031  69.898  1.00 93.08           O  
ANISOU 2692  O   VAL A 375     8107  17120  10137  -1433    826   -159       O  
ATOM   2693  CB  VAL A 375      27.664  -5.455  69.044  1.00 86.39           C  
ANISOU 2693  CB  VAL A 375     7345  15956   9524  -1389    912     86       C  
ATOM   2694  CG1 VAL A 375      27.958  -5.437  67.549  1.00 80.10           C  
ANISOU 2694  CG1 VAL A 375     6613  14917   8904  -1377    869    105       C  
ATOM   2695  CG2 VAL A 375      28.441  -6.569  69.731  1.00 88.15           C  
ANISOU 2695  CG2 VAL A 375     7548  16354   9591  -1369    900    298       C  
ATOM   2696  N   ASN A 376      29.501  -2.752  68.273  1.00 84.37           N  
ANISOU 2696  N   ASN A 376     7070  15593   9394  -1420    874   -335       N  
ATOM   2697  CA  ASN A 376      30.804  -2.492  67.654  1.00 80.69           C  
ANISOU 2697  CA  ASN A 376     6619  15056   8983  -1413    839   -341       C  
ATOM   2698  C   ASN A 376      31.863  -1.961  68.620  1.00 76.12           C  
ANISOU 2698  C   ASN A 376     5953  14691   8278  -1459    818   -487       C  
ATOM   2699  O   ASN A 376      33.014  -2.435  68.556  1.00 74.82           O  
ANISOU 2699  O   ASN A 376     5776  14581   8070  -1448    764   -385       O  
ATOM   2700  CB  ASN A 376      30.622  -1.545  66.462  1.00 91.81           C  
ANISOU 2700  CB  ASN A 376     8050  16212  10623  -1398    873   -417       C  
ATOM   2701  CG  ASN A 376      29.971  -2.226  65.272  1.00105.49           C  
ANISOU 2701  CG  ASN A 376     9852  17795  12435  -1367    856   -247       C  
ATOM   2702  OD1 ASN A 376      30.061  -3.444  65.113  1.00108.59           O  
ANISOU 2702  OD1 ASN A 376    10292  18212  12753  -1361    827    -86       O  
ATOM   2703  ND2 ASN A 376      29.304  -1.441  64.433  1.00111.38           N  
ANISOU 2703  ND2 ASN A 376    10581  18401  13340  -1356    879   -283       N  
ATOM   2704  N   PRO A 377      31.578  -0.989  69.498  1.00 77.79           N  
ANISOU 2704  N   PRO A 377     6084  15032   8438  -1519    863   -737       N  
ATOM   2705  CA  PRO A 377      32.623  -0.546  70.439  1.00 63.58           C  
ANISOU 2705  CA  PRO A 377     4177  13496   6485  -1591    827   -908       C  
ATOM   2706  C   PRO A 377      33.158  -1.665  71.312  1.00 61.79           C  
ANISOU 2706  C   PRO A 377     3900  13612   5967  -1593    740   -717       C  
ATOM   2707  O   PRO A 377      34.347  -1.656  71.659  1.00 62.84           O  
ANISOU 2707  O   PRO A 377     3945  13922   6008  -1622    662   -731       O  
ATOM   2708  CB  PRO A 377      31.910   0.527  71.270  1.00 69.30           C  
ANISOU 2708  CB  PRO A 377     4826  14318   7186  -1668    922  -1226       C  
ATOM   2709  CG  PRO A 377      30.850   1.045  70.365  1.00 77.69           C  
ANISOU 2709  CG  PRO A 377     5950  15033   8536  -1616   1013  -1229       C  
ATOM   2710  CD  PRO A 377      30.371  -0.148  69.599  1.00 72.84           C  
ANISOU 2710  CD  PRO A 377     5440  14308   7929  -1534    960   -906       C  
ATOM   2711  N   LEU A 378      32.316  -2.635  71.674  1.00 61.80           N  
ANISOU 2711  N   LEU A 378     3933  13706   5841  -1557    753   -516       N  
ATOM   2712  CA  LEU A 378      32.796  -3.777  72.443  1.00 63.00           C  
ANISOU 2712  CA  LEU A 378     4023  14164   5752  -1538    688   -259       C  
ATOM   2713  C   LEU A 378      33.845  -4.556  71.661  1.00 62.41           C  
ANISOU 2713  C   LEU A 378     3970  13939   5805  -1471    627    -18       C  
ATOM   2714  O   LEU A 378      34.853  -4.994  72.227  1.00 72.23           O  
ANISOU 2714  O   LEU A 378     5105  15434   6907  -1468    548    114       O  
ATOM   2715  CB  LEU A 378      31.624  -4.680  72.825  1.00 65.78           C  
ANISOU 2715  CB  LEU A 378     4412  14552   6028  -1501    749    -64       C  
ATOM   2716  CG  LEU A 378      31.912  -5.835  73.784  1.00 65.71           C  
ANISOU 2716  CG  LEU A 378     4321  14879   5769  -1471    717    238       C  
ATOM   2717  CD1 LEU A 378      32.444  -5.295  75.099  1.00 67.94           C  
ANISOU 2717  CD1 LEU A 378     4448  15674   5693  -1556    669     96       C  
ATOM   2718  CD2 LEU A 378      30.659  -6.677  74.012  1.00 65.18           C  
ANISOU 2718  CD2 LEU A 378     4305  14746   5714  -1429    810    425       C  
ATOM   2719  N   VAL A 379      33.634  -4.728  70.355  1.00 59.70           N  
ANISOU 2719  N   VAL A 379     3749  13208   5727  -1420    666     41       N  
ATOM   2720  CA  VAL A 379      34.630  -5.396  69.523  1.00 58.82           C  
ANISOU 2720  CA  VAL A 379     3661  12929   5760  -1365    646    226       C  
ATOM   2721  C   VAL A 379      35.913  -4.576  69.456  1.00 60.13           C  
ANISOU 2721  C   VAL A 379     3754  13123   5971  -1394    597     83       C  
ATOM   2722  O   VAL A 379      37.022  -5.126  69.538  1.00 64.87           O  
ANISOU 2722  O   VAL A 379     4278  13793   6575  -1365    549    242       O  
ATOM   2723  CB  VAL A 379      34.059  -5.665  68.120  1.00 63.08           C  
ANISOU 2723  CB  VAL A 379     4337  13103   6527  -1331    711    270       C  
ATOM   2724  CG1 VAL A 379      35.125  -6.277  67.221  1.00 56.13           C  
ANISOU 2724  CG1 VAL A 379     3478  12053   5795  -1289    728    416       C  
ATOM   2725  CG2 VAL A 379      32.834  -6.565  68.208  1.00 62.65           C  
ANISOU 2725  CG2 VAL A 379     4328  13018   6458  -1316    753    404       C  
ATOM   2726  N   TYR A 380      35.788  -3.252  69.291  1.00 61.60           N  
ANISOU 2726  N   TYR A 380     3943  13228   6235  -1449    622   -208       N  
ATOM   2727  CA  TYR A 380      36.982  -2.406  69.280  1.00 60.02           C  
ANISOU 2727  CA  TYR A 380     3654  13033   6115  -1490    591   -372       C  
ATOM   2728  C   TYR A 380      37.775  -2.567  70.571  1.00 66.13           C  
ANISOU 2728  C   TYR A 380     4264  14218   6646  -1540    482   -381       C  
ATOM   2729  O   TYR A 380      39.010  -2.568  70.556  1.00 63.32           O  
ANISOU 2729  O   TYR A 380     3815  13899   6344  -1541    418   -349       O  
ATOM   2730  CB  TYR A 380      36.612  -0.935  69.085  1.00 62.72           C  
ANISOU 2730  CB  TYR A 380     3997  13232   6601  -1548    661   -691       C  
ATOM   2731  CG  TYR A 380      35.945  -0.597  67.773  1.00 58.15           C  
ANISOU 2731  CG  TYR A 380     3541  12288   6265  -1498    755   -666       C  
ATOM   2732  CD1 TYR A 380      35.944  -1.489  66.713  1.00 56.51           C  
ANISOU 2732  CD1 TYR A 380     3436  11902   6133  -1426    769   -422       C  
ATOM   2733  CD2 TYR A 380      35.308   0.624  67.603  1.00 69.19           C  
ANISOU 2733  CD2 TYR A 380     4929  13543   7817  -1527    840   -885       C  
ATOM   2734  CE1 TYR A 380      35.325  -1.173  65.520  1.00 55.20           C  
ANISOU 2734  CE1 TYR A 380     3360  11484   6131  -1395    841   -399       C  
ATOM   2735  CE2 TYR A 380      34.689   0.949  66.417  1.00 70.00           C  
ANISOU 2735  CE2 TYR A 380     5109  13364   8124  -1476    914   -821       C  
ATOM   2736  CZ  TYR A 380      34.701   0.049  65.379  1.00 70.73           C  
ANISOU 2736  CZ  TYR A 380     5301  13344   8230  -1415    903   -578       C  
ATOM   2737  OH  TYR A 380      34.082   0.379  64.198  1.00 83.75           O  
ANISOU 2737  OH  TYR A 380     7005  14790  10028  -1380    963   -514       O  
ATOM   2738  N   THR A 381      37.078  -2.691  71.701  1.00 79.15           N  
ANISOU 2738  N   THR A 381     5857  16202   8013  -1585    461   -419       N  
ATOM   2739  CA  THR A 381      37.766  -2.921  72.968  1.00 82.12           C  
ANISOU 2739  CA  THR A 381     6057  17062   8084  -1637    346   -394       C  
ATOM   2740  C   THR A 381      38.430  -4.293  72.987  1.00 80.00           C  
ANISOU 2740  C   THR A 381     5739  16878   7777  -1542    276     28       C  
ATOM   2741  O   THR A 381      39.591  -4.424  73.391  1.00 76.11           O  
ANISOU 2741  O   THR A 381     5104  16592   7223  -1547    163    104       O  
ATOM   2742  CB  THR A 381      36.786  -2.796  74.136  1.00 83.57           C  
ANISOU 2742  CB  THR A 381     6187  17620   7944  -1708    370   -510       C  
ATOM   2743  OG1 THR A 381      36.140  -1.518  74.093  1.00 79.04           O  
ANISOU 2743  OG1 THR A 381     5647  16920   7465  -1792    467   -910       O  
ATOM   2744  CG2 THR A 381      37.520  -2.935  75.461  1.00 86.67           C  
ANISOU 2744  CG2 THR A 381     6372  18598   7959  -1781    240   -505       C  
ATOM   2745  N   LEU A 382      37.712  -5.321  72.527  1.00 83.20           N  
ANISOU 2745  N   LEU A 382     6252  17099   8259  -1452    350    304       N  
ATOM   2746  CA  LEU A 382      38.206  -6.689  72.643  1.00 82.97           C  
ANISOU 2746  CA  LEU A 382     6160  17136   8227  -1357    324    718       C  
ATOM   2747  C   LEU A 382      39.434  -6.934  71.778  1.00 80.58           C  
ANISOU 2747  C   LEU A 382     5841  16579   8198  -1301    310    827       C  
ATOM   2748  O   LEU A 382      40.321  -7.697  72.179  1.00 74.33           O  
ANISOU 2748  O   LEU A 382     4909  15950   7385  -1244    245   1106       O  
ATOM   2749  CB  LEU A 382      37.106  -7.682  72.266  1.00 80.12           C  
ANISOU 2749  CB  LEU A 382     5924  16563   7955  -1289    437    934       C  
ATOM   2750  CG  LEU A 382      35.901  -7.781  73.196  1.00 85.94           C  
ANISOU 2750  CG  LEU A 382     6660  17546   8447  -1318    474    936       C  
ATOM   2751  CD1 LEU A 382      34.857  -8.723  72.616  1.00 85.40           C  
ANISOU 2751  CD1 LEU A 382     6724  17163   8562  -1254    591   1116       C  
ATOM   2752  CD2 LEU A 382      36.337  -8.238  74.579  1.00 91.75           C  
ANISOU 2752  CD2 LEU A 382     7198  18818   8843  -1319    394   1155       C  
ATOM   2753  N   PHE A 383      39.516  -6.308  70.601  1.00 79.91           N  
ANISOU 2753  N   PHE A 383     5880  16107   8375  -1308    382    636       N  
ATOM   2754  CA  PHE A 383      40.559  -6.657  69.643  1.00 75.09           C  
ANISOU 2754  CA  PHE A 383     5269  15220   8043  -1248    419    757       C  
ATOM   2755  C   PHE A 383      41.543  -5.539  69.326  1.00 85.96           C  
ANISOU 2755  C   PHE A 383     6590  16520   9552  -1299    389    517       C  
ATOM   2756  O   PHE A 383      42.458  -5.759  68.525  1.00 96.69           O  
ANISOU 2756  O   PHE A 383     7935  17650  11154  -1253    439    607       O  
ATOM   2757  CB  PHE A 383      39.932  -7.168  68.341  1.00 71.00           C  
ANISOU 2757  CB  PHE A 383     4933  14302   7744  -1201    566    817       C  
ATOM   2758  CG  PHE A 383      39.215  -8.477  68.494  1.00 74.77           C  
ANISOU 2758  CG  PHE A 383     5443  14769   8196  -1144    620   1084       C  
ATOM   2759  CD1 PHE A 383      39.882  -9.674  68.278  1.00 72.62           C  
ANISOU 2759  CD1 PHE A 383     5114  14393   8086  -1063    679   1381       C  
ATOM   2760  CD2 PHE A 383      37.879  -8.515  68.861  1.00 75.50           C  
ANISOU 2760  CD2 PHE A 383     5609  14928   8149  -1171    635   1038       C  
ATOM   2761  CE1 PHE A 383      39.226 -10.885  68.420  1.00 74.62           C  
ANISOU 2761  CE1 PHE A 383     5386  14594   8373  -1014    758   1623       C  
ATOM   2762  CE2 PHE A 383      37.219  -9.722  69.006  1.00 74.22           C  
ANISOU 2762  CE2 PHE A 383     5465  14727   8008  -1124    702   1281       C  
ATOM   2763  CZ  PHE A 383      37.894 -10.908  68.784  1.00 76.28           C  
ANISOU 2763  CZ  PHE A 383     5672  14870   8443  -1047    767   1571       C  
ATOM   2764  N   ASN A 384      41.396  -4.357  69.918  1.00 86.28           N  
ANISOU 2764  N   ASN A 384     6588  16724   9470  -1396    332    207       N  
ATOM   2765  CA  ASN A 384      42.321  -3.253  69.686  1.00 83.26           C  
ANISOU 2765  CA  ASN A 384     6133  16250   9253  -1456    318    -38       C  
ATOM   2766  C   ASN A 384      42.814  -2.753  71.034  1.00 87.43           C  
ANISOU 2766  C   ASN A 384     6478  17201   9541  -1550    168   -203       C  
ATOM   2767  O   ASN A 384      42.011  -2.323  71.869  1.00 94.61           O  
ANISOU 2767  O   ASN A 384     7382  18364  10200  -1625    146   -389       O  
ATOM   2768  CB  ASN A 384      41.651  -2.122  68.900  1.00 82.08           C  
ANISOU 2768  CB  ASN A 384     6109  15808   9271  -1495    437   -309       C  
ATOM   2769  CG  ASN A 384      42.646  -1.124  68.355  1.00 82.65           C  
ANISOU 2769  CG  ASN A 384     6115  15675   9614  -1532    477   -489       C  
ATOM   2770  OD1 ASN A 384      43.201  -0.314  69.098  1.00 86.09           O  
ANISOU 2770  OD1 ASN A 384     6411  16275  10025  -1623    407   -724       O  
ATOM   2771  ND2 ASN A 384      42.874  -1.171  67.047  1.00 81.06           N  
ANISOU 2771  ND2 ASN A 384     6005  15123   9672  -1471    604   -388       N  
ATOM   2772  N   LYS A 385      44.131  -2.801  71.245  1.00 84.92           N  
ANISOU 2772  N   LYS A 385     5999  16971   9296  -1553     70   -149       N  
ATOM   2773  CA  LYS A 385      44.677  -2.426  72.544  1.00 89.03           C  
ANISOU 2773  CA  LYS A 385     6332  17942   9554  -1649   -100   -291       C  
ATOM   2774  C   LYS A 385      44.676  -0.918  72.755  1.00 90.14           C  
ANISOU 2774  C   LYS A 385     6443  18067   9739  -1790    -81   -772       C  
ATOM   2775  O   LYS A 385      44.512  -0.459  73.891  1.00 99.65           O  
ANISOU 2775  O   LYS A 385     7556  19665  10643  -1902   -169  -1003       O  
ATOM   2776  CB  LYS A 385      46.095  -2.975  72.711  1.00 91.37           C  
ANISOU 2776  CB  LYS A 385     6447  18333   9938  -1603   -226    -65       C  
ATOM   2777  CG  LYS A 385      46.633  -2.829  74.128  1.00 97.95           C  
ANISOU 2777  CG  LYS A 385     7081  19703  10432  -1689   -433   -133       C  
ATOM   2778  CD  LYS A 385      48.042  -3.374  74.263  1.00 99.33           C  
ANISOU 2778  CD  LYS A 385     7061  19953  10728  -1633   -569    119       C  
ATOM   2779  CE  LYS A 385      48.550  -3.206  75.685  1.00105.73           C  
ANISOU 2779  CE  LYS A 385     7679  21330  11164  -1722   -791     52       C  
ATOM   2780  NZ  LYS A 385      49.887  -3.834  75.878  1.00113.48           N  
ANISOU 2780  NZ  LYS A 385     8450  22408  12259  -1653   -943    355       N  
ATOM   2781  N   THR A 386      44.855  -0.137  71.688  1.00 83.34           N  
ANISOU 2781  N   THR A 386     5649  16764   9251  -1792     51   -927       N  
ATOM   2782  CA  THR A 386      44.791   1.315  71.823  1.00 89.30           C  
ANISOU 2782  CA  THR A 386     6369  17440  10120  -1919    109  -1369       C  
ATOM   2783  C   THR A 386      43.398   1.753  72.256  1.00 92.69           C  
ANISOU 2783  C   THR A 386     6894  17967  10359  -1972    187  -1578       C  
ATOM   2784  O   THR A 386      43.242   2.535  73.204  1.00102.16           O  
ANISOU 2784  O   THR A 386     7999  19423  11392  -2105    163  -1929       O  
ATOM   2785  CB  THR A 386      45.173   1.985  70.502  1.00 91.06           C  
ANISOU 2785  CB  THR A 386     6645  17151  10803  -1886    267  -1411       C  
ATOM   2786  OG1 THR A 386      46.457   1.514  70.073  1.00 95.79           O  
ANISOU 2786  OG1 THR A 386     7144  17654  11597  -1834    221  -1205       O  
ATOM   2787  CG2 THR A 386      45.220   3.498  70.667  1.00 88.78           C  
ANISOU 2787  CG2 THR A 386     6286  16749  10697  -2014    345  -1846       C  
ATOM   2788  N   TYR A 387      42.369   1.244  71.572  1.00 84.63           N  
ANISOU 2788  N   TYR A 387     6047  16742   9366  -1876    289  -1378       N  
ATOM   2789  CA  TYR A 387      40.996   1.529  71.972  1.00 84.96           C  
ANISOU 2789  CA  TYR A 387     6166  16865   9248  -1910    365  -1526       C  
ATOM   2790  C   TYR A 387      40.739   1.079  73.403  1.00 91.18           C  
ANISOU 2790  C   TYR A 387     6854  18204   9586  -1978    253  -1553       C  
ATOM   2791  O   TYR A 387      40.076   1.783  74.171  1.00 99.38           O  
ANISOU 2791  O   TYR A 387     7851  19443  10466  -2086    300  -1871       O  
ATOM   2792  CB  TYR A 387      40.014   0.841  71.019  1.00 77.70           C  
ANISOU 2792  CB  TYR A 387     5436  15667   8419  -1787    458  -1251       C  
ATOM   2793  CG  TYR A 387      39.711   1.612  69.752  1.00 68.34           C  
ANISOU 2793  CG  TYR A 387     4357  14011   7598  -1749    607  -1314       C  
ATOM   2794  CD1 TYR A 387      38.837   2.690  69.761  1.00 67.58           C  
ANISOU 2794  CD1 TYR A 387     4278  13785   7615  -1797    722  -1577       C  
ATOM   2795  CD2 TYR A 387      40.293   1.252  68.544  1.00 74.98           C  
ANISOU 2795  CD2 TYR A 387     5265  14555   8669  -1662    647  -1093       C  
ATOM   2796  CE1 TYR A 387      38.557   3.393  68.597  1.00 66.23           C  
ANISOU 2796  CE1 TYR A 387     4178  13207   7778  -1749    857  -1577       C  
ATOM   2797  CE2 TYR A 387      40.020   1.946  67.379  1.00 70.99           C  
ANISOU 2797  CE2 TYR A 387     4840  13680   8453  -1627    786  -1116       C  
ATOM   2798  CZ  TYR A 387      39.152   3.015  67.411  1.00 65.17           C  
ANISOU 2798  CZ  TYR A 387     4109  12830   7822  -1665    882  -1338       C  
ATOM   2799  OH  TYR A 387      38.881   3.703  66.250  1.00 60.80           O  
ANISOU 2799  OH  TYR A 387     3611  11934   7558  -1619   1021  -1309       O  
ATOM   2800  N   ARG A 388      41.260  -0.093  73.778  1.00 92.75           N  
ANISOU 2800  N   ARG A 388     6998  18663   9578  -1915    121  -1213       N  
ATOM   2801  CA  ARG A 388      40.987  -0.640  75.105  1.00 93.88           C  
ANISOU 2801  CA  ARG A 388     7038  19368   9265  -1960     19  -1149       C  
ATOM   2802  C   ARG A 388      41.608   0.221  76.197  1.00 94.03           C  
ANISOU 2802  C   ARG A 388     6884  19784   9060  -2119    -78  -1519       C  
ATOM   2803  O   ARG A 388      40.958   0.527  77.204  1.00 93.87           O  
ANISOU 2803  O   ARG A 388     6807  20153   8704  -2225    -66  -1744       O  
ATOM   2804  CB  ARG A 388      41.488  -2.084  75.186  1.00 89.29           C  
ANISOU 2804  CB  ARG A 388     6415  18933   8577  -1838    -87   -646       C  
ATOM   2805  CG  ARG A 388      41.130  -2.812  76.473  1.00 86.46           C  
ANISOU 2805  CG  ARG A 388     5948  19154   7750  -1853   -174   -462       C  
ATOM   2806  CD  ARG A 388      41.285  -4.316  76.303  1.00 88.43           C  
ANISOU 2806  CD  ARG A 388     6187  19402   8010  -1698   -204     97       C  
ATOM   2807  NE  ARG A 388      42.629  -4.690  75.871  1.00 98.24           N  
ANISOU 2807  NE  ARG A 388     7352  20500   9476  -1627   -296    300       N  
ATOM   2808  CZ  ARG A 388      42.968  -5.907  75.456  1.00100.23           C  
ANISOU 2808  CZ  ARG A 388     7590  20609   9883  -1485   -286    754       C  
ATOM   2809  NH1 ARG A 388      42.058  -6.872  75.416  1.00102.18           N  
ANISOU 2809  NH1 ARG A 388     7904  20827  10091  -1402   -191   1049       N  
ATOM   2810  NH2 ARG A 388      44.214  -6.161  75.075  1.00 95.86           N  
ANISOU 2810  NH2 ARG A 388     6944  19916   9562  -1428   -352    905       N  
ATOM   2811  N   SER A 389      42.867   0.623  76.016  1.00 95.75           N  
ANISOU 2811  N   SER A 389     7008  19912   9462  -2146   -164  -1605       N  
ATOM   2812  CA  SER A 389      43.503   1.504  76.990  1.00104.03           C  
ANISOU 2812  CA  SER A 389     7895  21292  10340  -2308   -252  -1999       C  
ATOM   2813  C   SER A 389      42.794   2.852  77.055  1.00102.13           C  
ANISOU 2813  C   SER A 389     7678  20917  10209  -2445    -86  -2531       C  
ATOM   2814  O   SER A 389      42.577   3.398  78.148  1.00110.96           O  
ANISOU 2814  O   SER A 389     8702  22438  11022  -2594    -94  -2886       O  
ATOM   2815  CB  SER A 389      44.982   1.683  76.647  1.00108.25           C  
ANISOU 2815  CB  SER A 389     8317  21676  11138  -2305   -362  -1976       C  
ATOM   2816  OG  SER A 389      45.669   0.442  76.673  1.00107.29           O  
ANISOU 2816  OG  SER A 389     8140  21691  10935  -2180   -507  -1490       O  
ATOM   2817  N   ALA A 390      42.414   3.401  75.895  1.00 87.85           N  
ANISOU 2817  N   ALA A 390     5990  18546   8842  -2395     83  -2587       N  
ATOM   2818  CA  ALA A 390      41.700   4.673  75.880  1.00 86.04           C  
ANISOU 2818  CA  ALA A 390     5774  18124   8795  -2502    270  -3044       C  
ATOM   2819  C   ALA A 390      40.385   4.577  76.642  1.00 88.94           C  
ANISOU 2819  C   ALA A 390     6168  18784   8840  -2551    349  -3158       C  
ATOM   2820  O   ALA A 390      40.049   5.467  77.428  1.00 87.33           O  
ANISOU 2820  O   ALA A 390     5875  18773   8534  -2709    435  -3621       O  
ATOM   2821  CB  ALA A 390      41.452   5.121  74.440  1.00 86.29           C  
ANISOU 2821  CB  ALA A 390     5936  17508   9341  -2400    435  -2959       C  
ATOM   2822  N   PHE A 391      39.632   3.497  76.430  1.00 86.61           N  
ANISOU 2822  N   PHE A 391     5985  18522   8401  -2424    341  -2755       N  
ATOM   2823  CA  PHE A 391      38.356   3.337  77.118  1.00 91.59           C  
ANISOU 2823  CA  PHE A 391     6631  19415   8753  -2461    431  -2821       C  
ATOM   2824  C   PHE A 391      38.554   3.124  78.613  1.00100.01           C  
ANISOU 2824  C   PHE A 391     7533  21195   9273  -2594    319  -2962       C  
ATOM   2825  O   PHE A 391      37.802   3.674  79.427  1.00113.56           O  
ANISOU 2825  O   PHE A 391     9182  23185  10782  -2729    429  -3318       O  
ATOM   2826  CB  PHE A 391      37.567   2.179  76.509  1.00 86.08           C  
ANISOU 2826  CB  PHE A 391     6086  18554   8066  -2290    450  -2335       C  
ATOM   2827  CG  PHE A 391      37.164   2.403  75.076  1.00 78.38           C  
ANISOU 2827  CG  PHE A 391     5284  16934   7560  -2170    566  -2218       C  
ATOM   2828  CD1 PHE A 391      37.107   3.681  74.545  1.00 73.82           C  
ANISOU 2828  CD1 PHE A 391     4716  15987   7346  -2215    697  -2541       C  
ATOM   2829  CD2 PHE A 391      36.837   1.334  74.264  1.00 71.02           C  
ANISOU 2829  CD2 PHE A 391     4494  15782   6707  -2016    550  -1782       C  
ATOM   2830  CE1 PHE A 391      36.735   3.885  73.231  1.00 70.94           C  
ANISOU 2830  CE1 PHE A 391     4490  15090   7374  -2100    795  -2389       C  
ATOM   2831  CE2 PHE A 391      36.464   1.529  72.951  1.00 68.17           C  
ANISOU 2831  CE2 PHE A 391     4280  14900   6720  -1919    642  -1683       C  
ATOM   2832  CZ  PHE A 391      36.413   2.808  72.432  1.00 68.14           C  
ANISOU 2832  CZ  PHE A 391     4276  14579   7037  -1957    757  -1968       C  
ATOM   2833  N   SER A 392      39.553   2.322  78.996  1.00103.45           N  
ANISOU 2833  N   SER A 392     7896  21942   9468  -2556    111  -2674       N  
ATOM   2834  CA  SER A 392      39.825   2.108  80.415  1.00112.12           C  
ANISOU 2834  CA  SER A 392     8851  23731  10020  -2662    -11  -2750       C  
ATOM   2835  C   SER A 392      40.182   3.416  81.109  1.00113.70           C  
ANISOU 2835  C   SER A 392     8942  24088  10170  -2865     32  -3372       C  
ATOM   2836  O   SER A 392      39.825   3.626  82.275  1.00111.94           O  
ANISOU 2836  O   SER A 392     8638  24365   9528  -2995     57  -3625       O  
ATOM   2837  CB  SER A 392      40.945   1.081  80.596  1.00110.67           C  
ANISOU 2837  CB  SER A 392     8608  23758   9684  -2557   -233  -2288       C  
ATOM   2838  OG  SER A 392      40.541  -0.207  80.162  1.00109.13           O  
ANISOU 2838  OG  SER A 392     8485  23490   9489  -2384   -247  -1727       O  
ATOM   2839  N   ARG A 393      40.884   4.312  80.408  1.00116.00           N  
ANISOU 2839  N   ARG A 393     9228  23941  10905  -2896     64  -3627       N  
ATOM   2840  CA  ARG A 393      41.217   5.602  81.004  1.00118.50           C  
ANISOU 2840  CA  ARG A 393     9430  24340  11255  -3094    136  -4245       C  
ATOM   2841  C   ARG A 393      40.048   6.582  80.963  1.00119.79           C  
ANISOU 2841  C   ARG A 393     9617  24301  11597  -3199    407  -4703       C  
ATOM   2842  O   ARG A 393      39.942   7.447  81.839  1.00130.07           O  
ANISOU 2842  O   ARG A 393    10813  25849  12758  -3386    509  -5233       O  
ATOM   2843  CB  ARG A 393      42.442   6.200  80.311  1.00116.53           C  
ANISOU 2843  CB  ARG A 393     9134  23697  11444  -3093     81  -4338       C  
ATOM   2844  CG  ARG A 393      43.725   5.424  80.577  1.00119.49           C  
ANISOU 2844  CG  ARG A 393     9423  24329  11647  -3035   -183  -3999       C  
ATOM   2845  CD  ARG A 393      44.941   6.103  79.964  1.00121.22           C  
ANISOU 2845  CD  ARG A 393     9562  24183  12314  -3060   -226  -4142       C  
ATOM   2846  NE  ARG A 393      44.958   6.014  78.506  1.00111.07           N  
ANISOU 2846  NE  ARG A 393     8393  22267  11541  -2915   -136  -3877       N  
ATOM   2847  CZ  ARG A 393      44.557   6.985  77.692  1.00110.79           C  
ANISOU 2847  CZ  ARG A 393     8417  21717  11959  -2934     81  -4129       C  
ATOM   2848  NH1 ARG A 393      44.102   8.128  78.188  1.00114.04           N  
ANISOU 2848  NH1 ARG A 393     8773  22135  12421  -3095    241  -4675       N  
ATOM   2849  NH2 ARG A 393      44.611   6.815  76.379  1.00109.26           N  
ANISOU 2849  NH2 ARG A 393     8334  20999  12181  -2789    157  -3827       N  
ATOM   2850  N   TYR A 394      39.165   6.467  79.968  1.00111.53           N  
ANISOU 2850  N   TYR A 394     8704  22789  10883  -3078    543  -4502       N  
ATOM   2851  CA  TYR A 394      38.021   7.372  79.884  1.00117.81           C  
ANISOU 2851  CA  TYR A 394     9515  23333  11915  -3151    814  -4875       C  
ATOM   2852  C   TYR A 394      36.965   7.035  80.931  1.00120.27           C  
ANISOU 2852  C   TYR A 394     9776  24160  11760  -3241    884  -4983       C  
ATOM   2853  O   TYR A 394      36.306   7.936  81.466  1.00121.69           O  
ANISOU 2853  O   TYR A 394     9880  24389  11970  -3398   1097  -5491       O  
ATOM   2854  CB  TYR A 394      37.410   7.329  78.482  1.00118.95           C  
ANISOU 2854  CB  TYR A 394     9836  22795  12563  -2958    933  -4550       C  
ATOM   2855  CG  TYR A 394      38.336   7.800  77.382  1.00117.76           C  
ANISOU 2855  CG  TYR A 394     9723  22121  12900  -2884    917  -4474       C  
ATOM   2856  CD1 TYR A 394      39.411   8.635  77.659  1.00114.17           C  
ANISOU 2856  CD1 TYR A 394     9133  21677  12567  -3015    892  -4840       C  
ATOM   2857  CD2 TYR A 394      38.140   7.399  76.066  1.00117.06           C  
ANISOU 2857  CD2 TYR A 394     9797  21538  13141  -2687    936  -4036       C  
ATOM   2858  CE1 TYR A 394      40.259   9.062  76.655  1.00110.65           C  
ANISOU 2858  CE1 TYR A 394     8703  20754  12583  -2949    898  -4751       C  
ATOM   2859  CE2 TYR A 394      38.985   7.818  75.057  1.00112.16           C  
ANISOU 2859  CE2 TYR A 394     9195  20481  12939  -2627    941  -3955       C  
ATOM   2860  CZ  TYR A 394      40.041   8.650  75.357  1.00109.70           C  
ANISOU 2860  CZ  TYR A 394     8739  20177  12764  -2755    928  -4302       C  
ATOM   2861  OH  TYR A 394      40.882   9.071  74.354  1.00113.79           O  
ANISOU 2861  OH  TYR A 394     9261  20257  13717  -2696    955  -4204       O  
ATOM   2862  N   ILE A 395      36.772   5.743  81.219  1.00119.65           N  
ANISOU 2862  N   ILE A 395     9729  24453  11281  -3143    735  -4506       N  
ATOM   2863  CA  ILE A 395      35.779   5.336  82.212  1.00113.09           C  
ANISOU 2863  CA  ILE A 395     8878  24104   9988  -3201    812  -4532       C  
ATOM   2864  C   ILE A 395      36.095   5.959  83.565  1.00124.40           C  
ANISOU 2864  C   ILE A 395    10188  26103  10975  -3428    799  -5053       C  
ATOM   2865  O   ILE A 395      35.192   6.384  84.298  1.00128.37           O  
ANISOU 2865  O   ILE A 395    10712  26750  11312  -3520   1007  -5369       O  
ATOM   2866  CB  ILE A 395      35.705   3.799  82.297  1.00107.13           C  
ANISOU 2866  CB  ILE A 395     8208  23597   8900  -3024    649  -3864       C  
ATOM   2867  CG1 ILE A 395      35.118   3.217  81.011  1.00105.21           C  
ANISOU 2867  CG1 ILE A 395     8119  22760   9096  -2810    733  -3414       C  
ATOM   2868  CG2 ILE A 395      34.879   3.363  83.494  1.00112.61           C  
ANISOU 2868  CG2 ILE A 395     8944  24803   9040  -3056    725  -3846       C  
ATOM   2869  CD1 ILE A 395      35.148   1.705  80.959  1.00104.01           C  
ANISOU 2869  CD1 ILE A 395     8032  22760   8727  -2641    594  -2773       C  
ATOM   2870  N   GLN A 396      37.377   6.045  83.907  1.00131.34           N  
ANISOU 2870  N   GLN A 396    10997  27135  11773  -3448    637  -5057       N  
ATOM   2871  CA  GLN A 396      37.822   6.623  85.166  1.00134.78           C  
ANISOU 2871  CA  GLN A 396    11306  27991  11911  -3615    646  -5443       C  
ATOM   2872  C   GLN A 396      38.022   8.132  85.082  1.00138.36           C  
ANISOU 2872  C   GLN A 396    11672  28148  12749  -3793    838  -6137       C  
ATOM   2873  O   GLN A 396      38.537   8.729  86.033  1.00153.87           O  
ANISOU 2873  O   GLN A 396    13511  30409  14543  -3949    841  -6507       O  
ATOM   2874  CB  GLN A 396      39.113   5.941  85.625  1.00131.60           C  
ANISOU 2874  CB  GLN A 396    10840  27936  11226  -3559    359  -5099       C  
ATOM   2875  CG  GLN A 396      39.008   4.424  85.683  1.00125.49           C  
ANISOU 2875  CG  GLN A 396    10129  27407  10145  -3370    191  -4381       C  
ATOM   2876  CD  GLN A 396      40.309   3.759  86.079  1.00128.29           C  
ANISOU 2876  CD  GLN A 396    10400  28059  10287  -3308    -81  -4028       C  
ATOM   2877  OE1 GLN A 396      41.382   4.350  85.965  1.00133.99           O  
ANISOU 2877  OE1 GLN A 396    11043  28688  11180  -3372   -177  -4252       O  
ATOM   2878  NE2 GLN A 396      40.219   2.521  86.553  1.00124.81           N  
ANISOU 2878  NE2 GLN A 396     9962  27958   9502  -3179   -201  -3462       N  
ATOM   2879  N   CYS A 397      37.635   8.754  83.964  1.00128.48           N  
ANISOU 2879  N   CYS A 397    10475  26297  12046  -3770    998  -6298       N  
ATOM   2880  CA  CYS A 397      37.720  10.205  83.780  1.00119.64           C  
ANISOU 2880  CA  CYS A 397     9272  24788  11398  -3916   1230  -6925       C  
ATOM   2881  C   CYS A 397      39.160  10.704  83.882  1.00125.94           C  
ANISOU 2881  C   CYS A 397     9974  25567  12308  -3970   1102  -7090       C  
ATOM   2882  O   CYS A 397      39.439  11.720  84.521  1.00134.21           O  
ANISOU 2882  O   CYS A 397    10886  26678  13431  -4152   1239  -7650       O  
ATOM   2883  CB  CYS A 397      36.822  10.942  84.777  1.00116.07           C  
ANISOU 2883  CB  CYS A 397     8726  24552  10824  -4110   1500  -7468       C  
ATOM   2884  SG  CYS A 397      35.073  10.512  84.680  1.00111.68           S  
ANISOU 2884  SG  CYS A 397     8290  23927  10215  -4054   1684  -7329       S  
ATOM   2885  N   GLN A 398      40.084   9.986  83.249  1.00127.50           N  
ANISOU 2885  N   GLN A 398    10228  25666  12551  -3817    847  -6604       N  
ATOM   2886  CA  GLN A 398      41.492  10.377  83.198  1.00137.01           C  
ANISOU 2886  CA  GLN A 398    11337  26802  13917  -3853    704  -6701       C  
ATOM   2887  C   GLN A 398      41.806  10.861  81.785  1.00137.63           C  
ANISOU 2887  C   GLN A 398    11479  26135  14678  -3752    776  -6620       C  
ATOM   2888  O   GLN A 398      42.031  10.055  80.877  1.00135.26           O  
ANISOU 2888  O   GLN A 398    11288  25598  14505  -3566    643  -6075       O  
ATOM   2889  CB  GLN A 398      42.397   9.216  83.598  1.00140.27           C  
ANISOU 2889  CB  GLN A 398    11735  27658  13905  -3761    371  -6201       C  
ATOM   2890  CG  GLN A 398      42.123   8.647  84.977  1.00145.34           C  
ANISOU 2890  CG  GLN A 398    12318  29024  13880  -3828    288  -6160       C  
ATOM   2891  CD  GLN A 398      43.017   7.466  85.298  1.00149.16           C  
ANISOU 2891  CD  GLN A 398    12778  29886  14011  -3712    -32  -5599       C  
ATOM   2892  OE1 GLN A 398      43.471   6.754  84.402  1.00146.49           O  
ANISOU 2892  OE1 GLN A 398    12510  29272  13879  -3541   -164  -5127       O  
ATOM   2893  NE2 GLN A 398      43.283   7.257  86.582  1.00155.53           N  
ANISOU 2893  NE2 GLN A 398    13474  31309  14309  -3803   -147  -5640       N  
ATOM   2894  N   TYR A 399      41.821  12.177  81.605  1.00132.92           N  
ANISOU 2894  N   TYR A 399    10807  25154  14542  -3871   1010  -7144       N  
ATOM   2895  CA  TYR A 399      42.047  12.770  80.292  1.00123.27           C  
ANISOU 2895  CA  TYR A 399     9638  23192  14007  -3774   1127  -7063       C  
ATOM   2896  C   TYR A 399      43.400  13.471  80.232  1.00124.53           C  
ANISOU 2896  C   TYR A 399     9659  23201  14455  -3853   1075  -7294       C  
ATOM   2897  O   TYR A 399      44.112  13.552  81.234  1.00124.32           O  
ANISOU 2897  O   TYR A 399     9491  23639  14104  -3991    949  -7555       O  
ATOM   2898  CB  TYR A 399      40.920  13.744  79.946  1.00118.48           C  
ANISOU 2898  CB  TYR A 399     9058  22128  13830  -3808   1475  -7390       C  
ATOM   2899  CG  TYR A 399      39.539  13.168  80.165  1.00115.66           C  
ANISOU 2899  CG  TYR A 399     8799  21952  13196  -3765   1547  -7247       C  
ATOM   2900  CD1 TYR A 399      39.000  12.256  79.269  1.00109.51           C  
ANISOU 2900  CD1 TYR A 399     8192  20962  12454  -3546   1469  -6631       C  
ATOM   2901  CD2 TYR A 399      38.777  13.528  81.271  1.00117.49           C  
ANISOU 2901  CD2 TYR A 399     8941  22564  13137  -3944   1709  -7729       C  
ATOM   2902  CE1 TYR A 399      37.741  11.722  79.460  1.00110.50           C  
ANISOU 2902  CE1 TYR A 399     8397  21228  12360  -3498   1538  -6479       C  
ATOM   2903  CE2 TYR A 399      37.513  12.997  81.472  1.00115.22           C  
ANISOU 2903  CE2 TYR A 399     8724  22437  12618  -3912   1785  -7594       C  
ATOM   2904  CZ  TYR A 399      37.001  12.093  80.560  1.00114.26           C  
ANISOU 2904  CZ  TYR A 399     8774  22074  12566  -3680   1694  -6951       C  
ATOM   2905  OH  TYR A 399      35.746  11.554  80.741  1.00114.65           O  
ANISOU 2905  OH  TYR A 399     8899  22238  12425  -3622   1780  -6772       O  
TER    2906      TYR A 399                                                      
ATOM   2907  N   GLN B  72       5.739 -16.694  29.329  1.00 97.94           N  
ANISOU 2907  N   GLN B  72     9359  14375  13480  -3575   1903  -1430       N  
ATOM   2908  CA  GLN B  72       6.720 -17.678  29.774  1.00105.77           C  
ANISOU 2908  CA  GLN B  72    10587  15078  14521  -3613   2108  -1456       C  
ATOM   2909  C   GLN B  72       7.739 -17.943  28.659  1.00117.39           C  
ANISOU 2909  C   GLN B  72    12117  16679  15808  -3673   1944  -1701       C  
ATOM   2910  O   GLN B  72       8.945 -18.007  28.907  1.00108.41           O  
ANISOU 2910  O   GLN B  72    11195  15465  14532  -3598   2015  -1650       O  
ATOM   2911  CB  GLN B  72       6.026 -18.968  30.216  1.00102.10           C  
ANISOU 2911  CB  GLN B  72    10091  14276  14427  -3772   2335  -1520       C  
ATOM   2912  CG  GLN B  72       6.966 -20.003  30.814  1.00106.26           C  
ANISOU 2912  CG  GLN B  72    10870  14451  15052  -3786   2584  -1491       C  
ATOM   2913  CD  GLN B  72       6.275 -21.318  31.120  1.00113.77           C  
ANISOU 2913  CD  GLN B  72    11777  15055  16398  -3946   2798  -1559       C  
ATOM   2914  OE1 GLN B  72       5.095 -21.498  30.818  1.00122.40           O  
ANISOU 2914  OE1 GLN B  72    12635  16181  17690  -4068   2750  -1665       O  
ATOM   2915  NE2 GLN B  72       7.007 -22.242  31.732  1.00111.86           N  
ANISOU 2915  NE2 GLN B  72    11755  14467  16281  -3937   3040  -1486       N  
ATOM   2916  N   GLU B  73       7.238 -18.109  27.431  1.00126.33           N  
ANISOU 2916  N   GLU B  73    13050  18020  16928  -3798   1726  -1971       N  
ATOM   2917  CA  GLU B  73       8.114 -18.337  26.284  1.00127.52           C  
ANISOU 2917  CA  GLU B  73    13235  18344  16871  -3846   1558  -2223       C  
ATOM   2918  C   GLU B  73       9.032 -17.142  26.048  1.00126.12           C  
ANISOU 2918  C   GLU B  73    13144  18449  16325  -3667   1406  -2064       C  
ATOM   2919  O   GLU B  73      10.216 -17.307  25.731  1.00129.01           O  
ANISOU 2919  O   GLU B  73    13657  18834  16527  -3648   1397  -2137       O  
ATOM   2920  CB  GLU B  73       7.274 -18.618  25.038  1.00131.17           C  
ANISOU 2920  CB  GLU B  73    13460  19031  17347  -3976   1340  -2521       C  
ATOM   2921  CG  GLU B  73       5.979 -17.812  24.981  1.00131.95           C  
ANISOU 2921  CG  GLU B  73    13326  19332  17477  -3938   1209  -2405       C  
ATOM   2922  CD  GLU B  73       5.393 -17.735  23.584  1.00137.02           C  
ANISOU 2922  CD  GLU B  73    13752  20320  17989  -3999    926  -2654       C  
ATOM   2923  OE1 GLU B  73       6.074 -17.204  22.681  1.00137.99           O  
ANISOU 2923  OE1 GLU B  73    13907  20753  17771  -3919    732  -2699       O  
ATOM   2924  OE2 GLU B  73       4.253 -18.208  23.387  1.00140.15           O  
ANISOU 2924  OE2 GLU B  73    13947  20688  18617  -4119    903  -2796       O  
ATOM   2925  N   LYS B  74       8.492 -15.930  26.191  1.00122.23           N  
ANISOU 2925  N   LYS B  74    12551  18165  15724  -3530   1290  -1844       N  
ATOM   2926  CA  LYS B  74       9.260 -14.699  26.030  1.00114.79           C  
ANISOU 2926  CA  LYS B  74    11675  17462  14479  -3342   1154  -1656       C  
ATOM   2927  C   LYS B  74      10.347 -14.557  27.091  1.00117.39           C  
ANISOU 2927  C   LYS B  74    12254  17585  14766  -3216   1341  -1462       C  
ATOM   2928  O   LYS B  74      11.314 -13.810  26.886  1.00121.13           O  
ANISOU 2928  O   LYS B  74    12818  18207  15001  -3084   1251  -1365       O  
ATOM   2929  CB  LYS B  74       8.297 -13.511  26.050  1.00102.88           C  
ANISOU 2929  CB  LYS B  74     9994  16148  12949  -3225   1022  -1465       C  
ATOM   2930  CG  LYS B  74       7.750 -13.176  27.425  1.00 96.72           C  
ANISOU 2930  CG  LYS B  74     9244  15145  12360  -3134   1216  -1232       C  
ATOM   2931  CD  LYS B  74       6.548 -12.255  27.320  1.00 98.83           C  
ANISOU 2931  CD  LYS B  74     9286  15575  12689  -3068   1095  -1120       C  
ATOM   2932  CE  LYS B  74       5.408 -12.957  26.588  1.00106.29           C  
ANISOU 2932  CE  LYS B  74    10002  16585  13799  -3248   1011  -1338       C  
ATOM   2933  NZ  LYS B  74       4.134 -12.182  26.601  1.00108.43           N  
ANISOU 2933  NZ  LYS B  74    10038  16976  14186  -3193    924  -1230       N  
ATOM   2934  N   ASN B  75      10.202 -15.251  28.222  1.00116.08           N  
ANISOU 2934  N   ASN B  75    12199  17084  14822  -3240   1602  -1391       N  
ATOM   2935  CA  ASN B  75      11.176 -15.146  29.303  1.00110.19           C  
ANISOU 2935  CA  ASN B  75    11711  16142  14016  -3082   1777  -1192       C  
ATOM   2936  C   ASN B  75      12.552 -15.647  28.878  1.00106.81           C  
ANISOU 2936  C   ASN B  75    11505  15632  13446  -3022   1738  -1290       C  
ATOM   2937  O   ASN B  75      13.568 -15.130  29.349  1.00104.96           O  
ANISOU 2937  O   ASN B  75    11472  15362  13045  -2812   1732  -1131       O  
ATOM   2938  CB  ASN B  75      10.687 -15.921  30.528  1.00112.81           C  
ANISOU 2938  CB  ASN B  75    12122  16139  14601  -3114   2072  -1087       C  
ATOM   2939  CG  ASN B  75       9.468 -15.285  31.175  1.00114.06           C  
ANISOU 2939  CG  ASN B  75    12147  16325  14867  -3049   2100   -919       C  
ATOM   2940  OD1 ASN B  75       9.102 -14.152  30.861  1.00113.50           O  
ANISOU 2940  OD1 ASN B  75    11946  16499  14681  -2957   1917   -855       O  
ATOM   2941  ND2 ASN B  75       8.832 -16.016  32.085  1.00112.22           N  
ANISOU 2941  ND2 ASN B  75    11941  15828  14869  -3091   2341   -836       N  
ATOM   2942  N   TRP B  76      12.615 -16.657  28.008  1.00109.82           N  
ANISOU 2942  N   TRP B  76    11842  15979  13905  -3201   1713  -1569       N  
ATOM   2943  CA  TRP B  76      13.918 -17.157  27.574  1.00116.12           C  
ANISOU 2943  CA  TRP B  76    12837  16700  14583  -3140   1688  -1682       C  
ATOM   2944  C   TRP B  76      14.628 -16.136  26.685  1.00112.34           C  
ANISOU 2944  C   TRP B  76    12345  16560  13780  -3020   1450  -1669       C  
ATOM   2945  O   TRP B  76      15.854 -15.960  26.773  1.00111.02           O  
ANISOU 2945  O   TRP B  76    12373  16345  13463  -2858   1440  -1601       O  
ATOM   2946  CB  TRP B  76      13.735 -18.484  26.838  1.00124.69           C  
ANISOU 2946  CB  TRP B  76    13856  17666  15855  -3368   1729  -2020       C  
ATOM   2947  CG  TRP B  76      13.292 -19.611  27.737  1.00132.89           C  
ANISOU 2947  CG  TRP B  76    14948  18295  17251  -3471   2005  -2011       C  
ATOM   2948  CD1 TRP B  76      12.210 -20.422  27.545  1.00139.18           C  
ANISOU 2948  CD1 TRP B  76    15546  18985  18352  -3721   2089  -2207       C  
ATOM   2949  CD2 TRP B  76      13.882 -20.022  28.981  1.00132.30           C  
ANISOU 2949  CD2 TRP B  76    15128  17868  17272  -3324   2236  -1774       C  
ATOM   2950  NE1 TRP B  76      12.101 -21.322  28.575  1.00141.39           N  
ANISOU 2950  NE1 TRP B  76    15944  18845  18933  -3745   2381  -2091       N  
ATOM   2951  CE2 TRP B  76      13.113 -21.098  29.471  1.00134.94           C  
ANISOU 2951  CE2 TRP B  76    15412  17883  17975  -3494   2473  -1813       C  
ATOM   2952  CE3 TRP B  76      14.989 -19.594  29.722  1.00126.71           C  
ANISOU 2952  CE3 TRP B  76    14674  17092  16378  -3061   2263  -1535       C  
ATOM   2953  CZ2 TRP B  76      13.415 -21.750  30.664  1.00130.66           C  
ANISOU 2953  CZ2 TRP B  76    15080  16968  17597  -3396   2743  -1585       C  
ATOM   2954  CZ3 TRP B  76      15.285 -20.243  30.907  1.00124.96           C  
ANISOU 2954  CZ3 TRP B  76    14654  16525  16301  -2961   2505  -1336       C  
ATOM   2955  CH2 TRP B  76      14.501 -21.309  31.366  1.00128.59           C  
ANISOU 2955  CH2 TRP B  76    15073  16680  17106  -3121   2747  -1345       C  
ATOM   2956  N   SER B  77      13.869 -15.435  25.838  1.00105.70           N  
ANISOU 2956  N   SER B  77    11263  16063  12836  -3090   1260  -1715       N  
ATOM   2957  CA  SER B  77      14.437 -14.322  25.085  1.00 92.26           C  
ANISOU 2957  CA  SER B  77     9535  14682  10838  -2957   1056  -1626       C  
ATOM   2958  C   SER B  77      14.899 -13.220  26.028  1.00 86.63           C  
ANISOU 2958  C   SER B  77     8940  13909  10065  -2727   1087  -1307       C  
ATOM   2959  O   SER B  77      15.945 -12.597  25.807  1.00 90.38           O  
ANISOU 2959  O   SER B  77     9524  14461  10357  -2576   1014  -1216       O  
ATOM   2960  CB  SER B  77      13.419 -13.788  24.076  1.00 92.32           C  
ANISOU 2960  CB  SER B  77     9247  15069  10759  -3060    853  -1696       C  
ATOM   2961  OG  SER B  77      12.205 -13.431  24.711  1.00 94.16           O  
ANISOU 2961  OG  SER B  77     9316  15286  11176  -3098    893  -1579       O  
ATOM   2962  N   ALA B  78      14.124 -12.966  27.087  1.00 81.53           N  
ANISOU 2962  N   ALA B  78     8263  13131   9583  -2702   1202  -1151       N  
ATOM   2963  CA  ALA B  78      14.547 -12.001  28.098  1.00 75.59           C  
ANISOU 2963  CA  ALA B  78     7629  12303   8790  -2484   1247   -893       C  
ATOM   2964  C   ALA B  78      15.855 -12.436  28.753  1.00 75.55           C  
ANISOU 2964  C   ALA B  78     7907  12057   8742  -2351   1353   -862       C  
ATOM   2965  O   ALA B  78      16.710 -11.602  29.069  1.00 81.37           O  
ANISOU 2965  O   ALA B  78     8746  12811   9359  -2164   1306   -727       O  
ATOM   2966  CB  ALA B  78      13.450 -11.821  29.147  1.00 66.48           C  
ANISOU 2966  CB  ALA B  78     6395  11047   7818  -2489   1383   -769       C  
ATOM   2967  N   LEU B  79      16.029 -13.742  28.953  1.00 71.47           N  
ANISOU 2967  N   LEU B  79     7506  11304   8345  -2442   1495   -990       N  
ATOM   2968  CA  LEU B  79      17.275 -14.260  29.514  1.00 77.30           C  
ANISOU 2968  CA  LEU B  79     8501  11816   9053  -2310   1588   -964       C  
ATOM   2969  C   LEU B  79      18.449 -13.998  28.577  1.00 80.58           C  
ANISOU 2969  C   LEU B  79     8965  12372   9280  -2246   1440  -1049       C  
ATOM   2970  O   LEU B  79      19.525 -13.559  29.009  1.00 76.81           O  
ANISOU 2970  O   LEU B  79     8635  11845   8704  -2060   1427   -943       O  
ATOM   2971  CB  LEU B  79      17.134 -15.758  29.788  1.00 87.38           C  
ANISOU 2971  CB  LEU B  79     9863  12802  10536  -2433   1774  -1081       C  
ATOM   2972  CG  LEU B  79      18.404 -16.520  30.179  1.00 97.40           C  
ANISOU 2972  CG  LEU B  79    11378  13826  11802  -2313   1866  -1083       C  
ATOM   2973  CD1 LEU B  79      18.998 -15.982  31.478  1.00101.78           C  
ANISOU 2973  CD1 LEU B  79    12111  14284  12278  -2067   1929   -830       C  
ATOM   2974  CD2 LEU B  79      18.121 -18.014  30.283  1.00 95.38           C  
ANISOU 2974  CD2 LEU B  79    11167  13273  11802  -2460   2052  -1209       C  
ATOM   2975  N   LEU B  80      18.260 -14.273  27.284  1.00 81.01           N  
ANISOU 2975  N   LEU B  80     8886  12616   9278  -2398   1331  -1252       N  
ATOM   2976  CA  LEU B  80      19.317 -13.988  26.315  1.00 80.63           C  
ANISOU 2976  CA  LEU B  80     8866  12740   9029  -2340   1206  -1326       C  
ATOM   2977  C   LEU B  80      19.668 -12.504  26.307  1.00 77.02           C  
ANISOU 2977  C   LEU B  80     8369  12478   8418  -2178   1084  -1110       C  
ATOM   2978  O   LEU B  80      20.850 -12.131  26.271  1.00 83.72           O  
ANISOU 2978  O   LEU B  80     9326  13320   9164  -2039   1058  -1056       O  
ATOM   2979  CB  LEU B  80      18.893 -14.441  24.919  1.00 85.74           C  
ANISOU 2979  CB  LEU B  80     9353  13623   9603  -2526   1101  -1581       C  
ATOM   2980  CG  LEU B  80      18.743 -15.945  24.692  1.00 92.32           C  
ANISOU 2980  CG  LEU B  80    10213  14264  10601  -2697   1208  -1867       C  
ATOM   2981  CD1 LEU B  80      18.197 -16.221  23.301  1.00 93.86           C  
ANISOU 2981  CD1 LEU B  80    10211  14756  10696  -2879   1071  -2145       C  
ATOM   2982  CD2 LEU B  80      20.077 -16.644  24.895  1.00 94.65           C  
ANISOU 2982  CD2 LEU B  80    10729  14324  10911  -2597   1309  -1928       C  
ATOM   2983  N   THR B  81      18.652 -11.642  26.358  1.00 69.42           N  
ANISOU 2983  N   THR B  81     7237  11670   7469  -2194   1017   -985       N  
ATOM   2984  CA  THR B  81      18.906 -10.207  26.378  1.00 65.99           C  
ANISOU 2984  CA  THR B  81     6748  11383   6943  -2043    916   -773       C  
ATOM   2985  C   THR B  81      19.630  -9.784  27.651  1.00 66.65           C  
ANISOU 2985  C   THR B  81     6999  11243   7084  -1855   1001   -627       C  
ATOM   2986  O   THR B  81      20.476  -8.885  27.618  1.00 75.65           O  
ANISOU 2986  O   THR B  81     8164  12428   8153  -1715    937   -521       O  
ATOM   2987  CB  THR B  81      17.598  -9.441  26.228  1.00 73.43           C  
ANISOU 2987  CB  THR B  81     7464  12508   7927  -2091    838   -673       C  
ATOM   2988  OG1 THR B  81      16.708  -9.812  27.285  1.00 83.88           O  
ANISOU 2988  OG1 THR B  81     8789  13646   9437  -2130    969   -655       O  
ATOM   2989  CG2 THR B  81      16.956  -9.752  24.885  1.00 73.01           C  
ANISOU 2989  CG2 THR B  81     7226  12737   7776  -2255    712   -820       C  
ATOM   2990  N   ALA B  82      19.315 -10.414  28.783  1.00 59.72           N  
ANISOU 2990  N   ALA B  82     6228  10130   6334  -1846   1148   -620       N  
ATOM   2991  CA  ALA B  82      20.033 -10.098  30.013  1.00 54.25           C  
ANISOU 2991  CA  ALA B  82     5700   9257   5654  -1655   1220   -503       C  
ATOM   2992  C   ALA B  82      21.496 -10.508  29.915  1.00 59.50           C  
ANISOU 2992  C   ALA B  82     6533   9828   6246  -1562   1215   -565       C  
ATOM   2993  O   ALA B  82      22.385  -9.795  30.402  1.00 68.64           O  
ANISOU 2993  O   ALA B  82     7759  10959   7361  -1392   1177   -484       O  
ATOM   2994  CB  ALA B  82      19.361 -10.778  31.204  1.00 57.68           C  
ANISOU 2994  CB  ALA B  82     6217   9489   6208  -1660   1394   -465       C  
ATOM   2995  N   VAL B  83      21.765 -11.657  29.290  1.00 54.69           N  
ANISOU 2995  N   VAL B  83     5976   9163   5642  -1672   1253   -726       N  
ATOM   2996  CA  VAL B  83      23.150 -12.054  29.046  1.00 53.55           C  
ANISOU 2996  CA  VAL B  83     5963   8946   5437  -1587   1246   -801       C  
ATOM   2997  C   VAL B  83      23.859 -11.006  28.195  1.00 56.46           C  
ANISOU 2997  C   VAL B  83     6244   9531   5676  -1530   1107   -770       C  
ATOM   2998  O   VAL B  83      25.008 -10.628  28.468  1.00 62.13           O  
ANISOU 2998  O   VAL B  83     7043  10199   6364  -1381   1086   -728       O  
ATOM   2999  CB  VAL B  83      23.204 -13.444  28.390  1.00 60.10           C  
ANISOU 2999  CB  VAL B  83     6833   9686   6315  -1730   1315  -1011       C  
ATOM   3000  CG1 VAL B  83      24.628 -13.765  27.944  1.00 59.17           C  
ANISOU 3000  CG1 VAL B  83     6816   9535   6131  -1644   1299  -1105       C  
ATOM   3001  CG2 VAL B  83      22.685 -14.502  29.353  1.00 58.60           C  
ANISOU 3001  CG2 VAL B  83     6748   9220   6298  -1763   1484  -1004       C  
ATOM   3002  N   VAL B  84      23.183 -10.520  27.152  1.00 54.02           N  
ANISOU 3002  N   VAL B  84     5760   9471   5296  -1643   1014   -779       N  
ATOM   3003  CA  VAL B  84      23.772  -9.484  26.305  1.00 46.64           C  
ANISOU 3003  CA  VAL B  84     4730   8750   4240  -1587    902   -701       C  
ATOM   3004  C   VAL B  84      24.059  -8.223  27.117  1.00 37.81           C  
ANISOU 3004  C   VAL B  84     3602   7584   3182  -1423    872   -507       C  
ATOM   3005  O   VAL B  84      25.116  -7.596  26.968  1.00 39.62           O  
ANISOU 3005  O   VAL B  84     3843   7825   3386  -1316    837   -454       O  
ATOM   3006  CB  VAL B  84      22.850  -9.191  25.106  1.00 44.81           C  
ANISOU 3006  CB  VAL B  84     4304   8815   3905  -1722    803   -712       C  
ATOM   3007  CG1 VAL B  84      23.444  -8.099  24.231  1.00 50.60           C  
ANISOU 3007  CG1 VAL B  84     4942   9773   4510  -1651    708   -580       C  
ATOM   3008  CG2 VAL B  84      22.626 -10.455  24.294  1.00 41.52           C  
ANISOU 3008  CG2 VAL B  84     3889   8456   3431  -1887    823   -961       C  
ATOM   3009  N   ILE B  85      23.128  -7.840  27.994  1.00 36.47           N  
ANISOU 3009  N   ILE B  85     3397   7352   3109  -1405    895   -416       N  
ATOM   3010  CA  ILE B  85      23.301  -6.641  28.815  1.00 44.69           C  
ANISOU 3010  CA  ILE B  85     4415   8340   4224  -1252    871   -271       C  
ATOM   3011  C   ILE B  85      24.527  -6.782  29.707  1.00 52.96           C  
ANISOU 3011  C   ILE B  85     5630   9203   5290  -1100    908   -303       C  
ATOM   3012  O   ILE B  85      25.350  -5.860  29.825  1.00 39.85           O  
ANISOU 3012  O   ILE B  85     3945   7538   3659   -982    853   -249       O  
ATOM   3013  CB  ILE B  85      22.035  -6.382  29.653  1.00 40.28           C  
ANISOU 3013  CB  ILE B  85     3798   7746   3761  -1260    916   -205       C  
ATOM   3014  CG1 ILE B  85      20.869  -5.983  28.756  1.00 42.41           C  
ANISOU 3014  CG1 ILE B  85     3859   8224   4032  -1382    847   -152       C  
ATOM   3015  CG2 ILE B  85      22.291  -5.313  30.711  1.00 35.00           C  
ANISOU 3015  CG2 ILE B  85     3138   6987   3174  -1088    914   -113       C  
ATOM   3016  CD1 ILE B  85      19.558  -5.927  29.471  1.00 37.32           C  
ANISOU 3016  CD1 ILE B  85     3137   7549   3495  -1416    906   -114       C  
ATOM   3017  N   ILE B  86      24.657  -7.938  30.361  1.00 48.07           N  
ANISOU 3017  N   ILE B  86     5170   8423   4670  -1096   1002   -388       N  
ATOM   3018  CA  ILE B  86      25.770  -8.144  31.279  1.00 47.72           C  
ANISOU 3018  CA  ILE B  86     5282   8219   4629   -933   1026   -409       C  
ATOM   3019  C   ILE B  86      27.089  -8.138  30.521  1.00 53.85           C  
ANISOU 3019  C   ILE B  86     6068   9025   5368   -897    971   -472       C  
ATOM   3020  O   ILE B  86      28.081  -7.558  30.980  1.00 62.43           O  
ANISOU 3020  O   ILE B  86     7176  10066   6479   -752    925   -459       O  
ATOM   3021  CB  ILE B  86      25.577  -9.451  32.065  1.00 52.36           C  
ANISOU 3021  CB  ILE B  86     6036   8630   5229   -932   1151   -448       C  
ATOM   3022  CG1 ILE B  86      24.355  -9.347  32.978  1.00 66.29           C  
ANISOU 3022  CG1 ILE B  86     7790  10363   7034   -941   1231   -362       C  
ATOM   3023  CG2 ILE B  86      26.823  -9.778  32.864  1.00 43.66           C  
ANISOU 3023  CG2 ILE B  86     5092   7391   4107   -750   1158   -464       C  
ATOM   3024  CD1 ILE B  86      24.102 -10.590  33.807  1.00 69.24           C  
ANISOU 3024  CD1 ILE B  86     8321  10554   7432   -936   1383   -353       C  
ATOM   3025  N   LEU B  87      27.119  -8.762  29.342  1.00 47.70           N  
ANISOU 3025  N   LEU B  87     5257   8335   4533  -1029    976   -557       N  
ATOM   3026  CA  LEU B  87      28.332  -8.735  28.534  1.00 46.29           C  
ANISOU 3026  CA  LEU B  87     5070   8211   4307  -1000    943   -617       C  
ATOM   3027  C   LEU B  87      28.706  -7.306  28.164  1.00 46.59           C  
ANISOU 3027  C   LEU B  87     4969   8375   4358   -944    860   -499       C  
ATOM   3028  O   LEU B  87      29.872  -6.910  28.276  1.00 60.13           O  
ANISOU 3028  O   LEU B  87     6690  10044   6113   -835    839   -500       O  
ATOM   3029  CB  LEU B  87      28.145  -9.591  27.281  1.00 58.26           C  
ANISOU 3029  CB  LEU B  87     6559   9842   5735  -1158    966   -747       C  
ATOM   3030  CG  LEU B  87      28.084 -11.104  27.511  1.00 51.11           C  
ANISOU 3030  CG  LEU B  87     5789   8764   4868  -1211   1065   -901       C  
ATOM   3031  CD1 LEU B  87      28.117 -11.846  26.181  1.00 38.28           C  
ANISOU 3031  CD1 LEU B  87     4120   7266   3160  -1355   1077  -1082       C  
ATOM   3032  CD2 LEU B  87      29.210 -11.573  28.443  1.00 39.15           C  
ANISOU 3032  CD2 LEU B  87     4429   7025   3422  -1043   1111   -914       C  
ATOM   3033  N   THR B  88      27.723  -6.517  27.722  1.00 48.86           N  
ANISOU 3033  N   THR B  88     5115   8811   4639  -1016    817   -388       N  
ATOM   3034  CA  THR B  88      27.972  -5.117  27.384  1.00 39.87           C  
ANISOU 3034  CA  THR B  88     3832   7763   3553   -961    754   -241       C  
ATOM   3035  C   THR B  88      28.593  -4.372  28.557  1.00 37.09           C  
ANISOU 3035  C   THR B  88     3506   7240   3347   -803    739   -216       C  
ATOM   3036  O   THR B  88      29.663  -3.755  28.434  1.00 35.82           O  
ANISOU 3036  O   THR B  88     3302   7053   3256   -725    716   -199       O  
ATOM   3037  CB  THR B  88      26.659  -4.442  26.979  1.00 39.48           C  
ANISOU 3037  CB  THR B  88     3634   7862   3504  -1037    712   -111       C  
ATOM   3038  OG1 THR B  88      26.039  -5.185  25.925  1.00 36.41           O  
ANISOU 3038  OG1 THR B  88     3210   7657   2965  -1184    705   -170       O  
ATOM   3039  CG2 THR B  88      26.898  -3.010  26.528  1.00 34.09           C  
ANISOU 3039  CG2 THR B  88     2794   7258   2901   -978    661     71       C  
ATOM   3040  N   ILE B  89      27.927  -4.424  29.710  1.00 32.18           N  
ANISOU 3040  N   ILE B  89     2944   6511   2773   -755    755   -225       N  
ATOM   3041  CA  ILE B  89      28.390  -3.664  30.864  1.00 34.12           C  
ANISOU 3041  CA  ILE B  89     3201   6631   3133   -600    729   -229       C  
ATOM   3042  C   ILE B  89      29.795  -4.103  31.258  1.00 46.10           C  
ANISOU 3042  C   ILE B  89     4822   8046   4647   -492    719   -338       C  
ATOM   3043  O   ILE B  89      30.690  -3.271  31.445  1.00 59.29           O  
ANISOU 3043  O   ILE B  89     6425   9677   6427   -398    666   -350       O  
ATOM   3044  CB  ILE B  89      27.399  -3.804  32.032  1.00 35.59           C  
ANISOU 3044  CB  ILE B  89     3449   6752   3321   -563    769   -233       C  
ATOM   3045  CG1 ILE B  89      26.048  -3.206  31.646  1.00 32.07           C  
ANISOU 3045  CG1 ILE B  89     2860   6406   2917   -655    770   -125       C  
ATOM   3046  CG2 ILE B  89      27.944  -3.112  33.271  1.00 31.40           C  
ANISOU 3046  CG2 ILE B  89     2943   6119   2867   -389    735   -282       C  
ATOM   3047  CD1 ILE B  89      24.978  -3.388  32.697  1.00 38.39           C  
ANISOU 3047  CD1 ILE B  89     3702   7159   3724   -636    835   -126       C  
ATOM   3048  N   ALA B  90      30.018  -5.417  31.361  1.00 31.56           N  
ANISOU 3048  N   ALA B  90     3132   6153   2707   -504    771   -421       N  
ATOM   3049  CA  ALA B  90      31.311  -5.918  31.817  1.00 31.53           C  
ANISOU 3049  CA  ALA B  90     3226   6048   2705   -380    758   -517       C  
ATOM   3050  C   ALA B  90      32.433  -5.535  30.856  1.00 33.76           C  
ANISOU 3050  C   ALA B  90     3410   6383   3036   -387    728   -540       C  
ATOM   3051  O   ALA B  90      33.476  -5.017  31.276  1.00 31.95           O  
ANISOU 3051  O   ALA B  90     3143   6097   2900   -268    674   -583       O  
ATOM   3052  CB  ALA B  90      31.245  -7.433  31.996  1.00 46.58           C  
ANISOU 3052  CB  ALA B  90     5300   7871   4527   -398    837   -578       C  
ATOM   3053  N   GLY B  91      32.241  -5.787  29.559  1.00 46.00           N  
ANISOU 3053  N   GLY B  91     4905   8054   4520   -526    765   -519       N  
ATOM   3054  CA  GLY B  91      33.285  -5.471  28.599  1.00 50.39           C  
ANISOU 3054  CA  GLY B  91     5368   8681   5098   -533    765   -525       C  
ATOM   3055  C   GLY B  91      33.625  -3.993  28.563  1.00 44.19           C  
ANISOU 3055  C   GLY B  91     4418   7910   4460   -488    718   -419       C  
ATOM   3056  O   GLY B  91      34.803  -3.616  28.532  1.00 41.88           O  
ANISOU 3056  O   GLY B  91     4065   7572   4275   -416    707   -452       O  
ATOM   3057  N   ASN B  92      32.605  -3.129  28.580  1.00 39.13           N  
ANISOU 3057  N   ASN B  92     3690   7318   3860   -529    694   -294       N  
ATOM   3058  CA  ASN B  92      32.901  -1.704  28.495  1.00 32.08           C  
ANISOU 3058  CA  ASN B  92     2629   6408   3153   -490    665   -184       C  
ATOM   3059  C   ASN B  92      33.487  -1.168  29.795  1.00 31.73           C  
ANISOU 3059  C   ASN B  92     2583   6191   3280   -349    608   -283       C  
ATOM   3060  O   ASN B  92      34.303  -0.240  29.764  1.00 32.08           O  
ANISOU 3060  O   ASN B  92     2497   6174   3519   -301    588   -272       O  
ATOM   3061  CB  ASN B  92      31.652  -0.946  28.078  1.00 44.05           C  
ANISOU 3061  CB  ASN B  92     4037   8019   4682   -561    658    -13       C  
ATOM   3062  CG  ASN B  92      31.280  -1.223  26.639  1.00 45.68           C  
ANISOU 3062  CG  ASN B  92     4195   8440   4721   -683    691     94       C  
ATOM   3063  OD1 ASN B  92      30.269  -1.863  26.356  1.00 65.97           O  
ANISOU 3063  OD1 ASN B  92     6807  11121   7138   -770    689     88       O  
ATOM   3064  ND2 ASN B  92      32.111  -0.757  25.717  1.00 38.61           N  
ANISOU 3064  ND2 ASN B  92     3201   7618   3849   -690    724    185       N  
ATOM   3065  N   ILE B  93      33.115  -1.747  30.939  1.00 43.99           N  
ANISOU 3065  N   ILE B  93     4274   7674   4767   -279    585   -385       N  
ATOM   3066  CA  ILE B  93      33.792  -1.407  32.187  1.00 45.35           C  
ANISOU 3066  CA  ILE B  93     4462   7727   5041   -125    517   -515       C  
ATOM   3067  C   ILE B  93      35.269  -1.763  32.096  1.00 44.63           C  
ANISOU 3067  C   ILE B  93     4372   7594   4989    -58    493   -621       C  
ATOM   3068  O   ILE B  93      36.142  -0.989  32.513  1.00 40.99           O  
ANISOU 3068  O   ILE B  93     3803   7064   4708     28    430   -702       O  
ATOM   3069  CB  ILE B  93      33.113  -2.119  33.373  1.00 43.94           C  
ANISOU 3069  CB  ILE B  93     4451   7520   4724    -53    516   -577       C  
ATOM   3070  CG1 ILE B  93      31.784  -1.446  33.718  1.00 39.13           C  
ANISOU 3070  CG1 ILE B  93     3794   6932   4142    -85    532   -501       C  
ATOM   3071  CG2 ILE B  93      34.037  -2.164  34.584  1.00 47.36           C  
ANISOU 3071  CG2 ILE B  93     4941   7880   5173    127    438   -729       C  
ATOM   3072  CD1 ILE B  93      31.087  -2.075  34.889  1.00 40.77           C  
ANISOU 3072  CD1 ILE B  93     4153   7123   4214    -13    558   -544       C  
ATOM   3073  N   LEU B  94      35.570  -2.939  31.541  1.00 40.37           N  
ANISOU 3073  N   LEU B  94     3939   7092   4308    -97    545   -641       N  
ATOM   3074  CA  LEU B  94      36.964  -3.337  31.378  1.00 37.65           C  
ANISOU 3074  CA  LEU B  94     3584   6712   4010    -30    535   -741       C  
ATOM   3075  C   LEU B  94      37.714  -2.357  30.486  1.00 37.25           C  
ANISOU 3075  C   LEU B  94     3333   6686   4134    -77    552   -690       C  
ATOM   3076  O   LEU B  94      38.854  -1.982  30.783  1.00 33.13           O  
ANISOU 3076  O   LEU B  94     2718   6096   3773      9    507   -783       O  
ATOM   3077  CB  LEU B  94      37.040  -4.751  30.798  1.00 32.11           C  
ANISOU 3077  CB  LEU B  94     3018   6039   3145    -77    610   -772       C  
ATOM   3078  CG  LEU B  94      36.710  -5.900  31.745  1.00 35.96           C  
ANISOU 3078  CG  LEU B  94     3703   6448   3511      2    611   -828       C  
ATOM   3079  CD1 LEU B  94      36.881  -7.221  31.021  1.00 39.72           C  
ANISOU 3079  CD1 LEU B  94     4280   6919   3895    -58    699   -873       C  
ATOM   3080  CD2 LEU B  94      37.581  -5.846  33.009  1.00 36.14           C  
ANISOU 3080  CD2 LEU B  94     3758   6387   3589    203    514   -922       C  
ATOM   3081  N   VAL B  95      37.089  -1.934  29.386  1.00 46.21           N  
ANISOU 3081  N   VAL B  95     4389   7925   5244   -210    620   -534       N  
ATOM   3082  CA  VAL B  95      37.742  -0.990  28.479  1.00 37.60           C  
ANISOU 3082  CA  VAL B  95     3109   6864   4313   -254    666   -433       C  
ATOM   3083  C   VAL B  95      38.015   0.331  29.190  1.00 43.50           C  
ANISOU 3083  C   VAL B  95     3703   7478   5346   -188    605   -438       C  
ATOM   3084  O   VAL B  95      39.100   0.917  29.055  1.00 44.74           O  
ANISOU 3084  O   VAL B  95     3715   7566   5718   -160    613   -468       O  
ATOM   3085  CB  VAL B  95      36.885  -0.789  27.215  1.00 34.77           C  
ANISOU 3085  CB  VAL B  95     2704   6674   3834   -389    742   -234       C  
ATOM   3086  CG1 VAL B  95      37.420   0.361  26.378  1.00 34.73           C  
ANISOU 3086  CG1 VAL B  95     2496   6691   4009   -419    802    -67       C  
ATOM   3087  CG2 VAL B  95      36.841  -2.070  26.400  1.00 37.89           C  
ANISOU 3087  CG2 VAL B  95     3218   7208   3972   -458    803   -285       C  
ATOM   3088  N   ILE B  96      37.038   0.818  29.958  1.00 46.45           N  
ANISOU 3088  N   ILE B  96     4095   7807   5748   -166    550   -425       N  
ATOM   3089  CA  ILE B  96      37.222   2.063  30.701  1.00 46.71           C  
ANISOU 3089  CA  ILE B  96     3983   7701   6064   -100    491   -474       C  
ATOM   3090  C   ILE B  96      38.390   1.935  31.672  1.00 47.31           C  
ANISOU 3090  C   ILE B  96     4052   7681   6242     27    401   -710       C  
ATOM   3091  O   ILE B  96      39.250   2.822  31.758  1.00 53.31           O  
ANISOU 3091  O   ILE B  96     4631   8336   7286     52    378   -774       O  
ATOM   3092  CB  ILE B  96      35.921   2.451  31.426  1.00 46.64           C  
ANISOU 3092  CB  ILE B  96     4013   7676   6034    -85    456   -453       C  
ATOM   3093  CG1 ILE B  96      34.834   2.813  30.412  1.00 45.92           C  
ANISOU 3093  CG1 ILE B  96     3867   7678   5904   -201    528   -208       C  
ATOM   3094  CG2 ILE B  96      36.161   3.609  32.375  1.00 43.06           C  
ANISOU 3094  CG2 ILE B  96     3426   7071   5864      3    386   -578       C  
ATOM   3095  CD1 ILE B  96      33.449   2.919  31.013  1.00 43.72           C  
ANISOU 3095  CD1 ILE B  96     3640   7412   5560   -196    509   -183       C  
ATOM   3096  N   MET B  97      38.443   0.824  32.411  1.00 46.65           N  
ANISOU 3096  N   MET B  97     4153   7629   5941    111    349   -839       N  
ATOM   3097  CA  MET B  97      39.540   0.628  33.357  1.00 48.25           C  
ANISOU 3097  CA  MET B  97     4354   7776   6204    256    243  -1054       C  
ATOM   3098  C   MET B  97      40.883   0.584  32.646  1.00 55.82           C  
ANISOU 3098  C   MET B  97     5186   8715   7307    244    270  -1087       C  
ATOM   3099  O   MET B  97      41.857   1.193  33.105  1.00 58.24           O  
ANISOU 3099  O   MET B  97     5339   8944   7845    316    192  -1236       O  
ATOM   3100  CB  MET B  97      39.336  -0.655  34.155  1.00 41.88           C  
ANISOU 3100  CB  MET B  97     3778   7016   5120    357    204  -1126       C  
ATOM   3101  CG  MET B  97      38.091  -0.668  34.993  1.00 38.50           C  
ANISOU 3101  CG  MET B  97     3471   6610   4548    385    192  -1103       C  
ATOM   3102  SD  MET B  97      37.980  -2.220  35.877  1.00 48.89           S  
ANISOU 3102  SD  MET B  97     5050   7962   5563    508    179  -1141       S  
ATOM   3103  CE  MET B  97      39.503  -2.185  36.827  1.00 36.90           C  
ANISOU 3103  CE  MET B  97     3478   6425   4118    716     22  -1357       C  
ATOM   3104  N   ALA B  98      40.954  -0.136  31.523  1.00 57.10           N  
ANISOU 3104  N   ALA B  98     5397   8955   7343    153    382   -970       N  
ATOM   3105  CA  ALA B  98      42.223  -0.289  30.822  1.00 56.03           C  
ANISOU 3105  CA  ALA B  98     5150   8819   7321    147    433  -1003       C  
ATOM   3106  C   ALA B  98      42.715   1.042  30.273  1.00 57.46           C  
ANISOU 3106  C   ALA B  98     5077   8936   7818     81    482   -930       C  
ATOM   3107  O   ALA B  98      43.911   1.345  30.350  1.00 56.49           O  
ANISOU 3107  O   ALA B  98     4798   8745   7922    125    464  -1041       O  
ATOM   3108  CB  ALA B  98      42.083  -1.317  29.699  1.00 51.40           C  
ANISOU 3108  CB  ALA B  98     4671   8348   6511     61    557   -908       C  
ATOM   3109  N   VAL B  99      41.811   1.863  29.735  1.00 54.23           N  
ANISOU 3109  N   VAL B  99     4612   8538   7456    -20    548   -737       N  
ATOM   3110  CA  VAL B  99      42.248   3.139  29.181  1.00 49.64           C  
ANISOU 3110  CA  VAL B  99     3787   7870   7204    -81    619   -625       C  
ATOM   3111  C   VAL B  99      42.605   4.114  30.295  1.00 53.07           C  
ANISOU 3111  C   VAL B  99     4077   8125   7962     -5    503   -805       C  
ATOM   3112  O   VAL B  99      43.559   4.890  30.174  1.00 61.56           O  
ANISOU 3112  O   VAL B  99     4933   9082   9375    -15    528   -848       O  
ATOM   3113  CB  VAL B  99      41.179   3.718  28.238  1.00 50.74           C  
ANISOU 3113  CB  VAL B  99     3903   8079   7298   -192    723   -334       C  
ATOM   3114  CG1 VAL B  99      41.616   5.082  27.715  1.00 39.86           C  
ANISOU 3114  CG1 VAL B  99     2269   6580   6295   -242    812   -180       C  
ATOM   3115  CG2 VAL B  99      40.924   2.760  27.085  1.00 51.10           C  
ANISOU 3115  CG2 VAL B  99     4067   8335   7015   -267    825   -199       C  
ATOM   3116  N   SER B 100      41.869   4.082  31.409  1.00 60.00           N  
ANISOU 3116  N   SER B 100     5066   8983   8749     73    382   -932       N  
ATOM   3117  CA  SER B 100      42.133   5.038  32.475  1.00 64.31           C  
ANISOU 3117  CA  SER B 100     5473   9382   9582    148    267  -1139       C  
ATOM   3118  C   SER B 100      43.334   4.662  33.334  1.00 65.90           C  
ANISOU 3118  C   SER B 100     5638   9566   9835    272    132  -1430       C  
ATOM   3119  O   SER B 100      43.898   5.540  33.996  1.00 70.56           O  
ANISOU 3119  O   SER B 100     6043  10035  10733    317     42  -1631       O  
ATOM   3120  CB  SER B 100      40.884   5.204  33.350  1.00 56.10           C  
ANISOU 3120  CB  SER B 100     4551   8350   8413    195    199  -1175       C  
ATOM   3121  OG  SER B 100      40.420   3.957  33.831  1.00 50.79           O  
ANISOU 3121  OG  SER B 100     4132   7814   7351    261    155  -1212       O  
ATOM   3122  N   LEU B 101      43.753   3.397  33.330  1.00 68.93           N  
ANISOU 3122  N   LEU B 101     6177  10063   9948    332    111  -1467       N  
ATOM   3123  CA  LEU B 101      44.857   2.946  34.168  1.00 59.55           C  
ANISOU 3123  CA  LEU B 101     4963   8882   8781    476    -32  -1724       C  
ATOM   3124  C   LEU B 101      46.141   2.708  33.389  1.00 67.36           C  
ANISOU 3124  C   LEU B 101     5808   9858   9926    449     33  -1731       C  
ATOM   3125  O   LEU B 101      47.203   3.193  33.790  1.00 73.73           O  
ANISOU 3125  O   LEU B 101     6409  10593  11011    503    -54  -1928       O  
ATOM   3126  CB  LEU B 101      44.464   1.662  34.913  1.00 57.17           C  
ANISOU 3126  CB  LEU B 101     4935   8699   8087    602   -110  -1768       C  
ATOM   3127  CG  LEU B 101      43.341   1.768  35.945  1.00 52.93           C  
ANISOU 3127  CG  LEU B 101     4544   8196   7371    669   -185  -1805       C  
ATOM   3128  CD1 LEU B 101      43.002   0.391  36.490  1.00 61.91           C  
ANISOU 3128  CD1 LEU B 101     5951   9439   8135    778   -212  -1784       C  
ATOM   3129  CD2 LEU B 101      43.733   2.704  37.075  1.00 49.59           C  
ANISOU 3129  CD2 LEU B 101     3972   7728   7143    777   -348  -2070       C  
ATOM   3130  N   GLU B 102      46.077   1.963  32.286  1.00 77.73           N  
ANISOU 3130  N   GLU B 102     7212  11249  11071    368    184  -1540       N  
ATOM   3131  CA  GLU B 102      47.284   1.596  31.553  1.00 78.32           C  
ANISOU 3131  CA  GLU B 102     7168  11334  11255    357    263  -1556       C  
ATOM   3132  C   GLU B 102      47.869   2.819  30.859  1.00 82.06           C  
ANISOU 3132  C   GLU B 102     7353  11703  12122    247    371  -1487       C  
ATOM   3133  O   GLU B 102      47.193   3.473  30.056  1.00 83.51           O  
ANISOU 3133  O   GLU B 102     7503  11877  12350    120    507  -1255       O  
ATOM   3134  CB  GLU B 102      46.976   0.499  30.537  1.00 81.71           C  
ANISOU 3134  CB  GLU B 102     7773  11885  11387    298    408  -1394       C  
ATOM   3135  CG  GLU B 102      46.475  -0.794  31.165  1.00 94.36           C  
ANISOU 3135  CG  GLU B 102     9648  13552  12652    399    330  -1454       C  
ATOM   3136  CD  GLU B 102      47.507  -1.461  32.064  1.00 97.54           C  
ANISOU 3136  CD  GLU B 102    10050  13934  13076    581    191  -1670       C  
ATOM   3137  OE1 GLU B 102      48.723  -1.298  31.819  1.00 97.92           O  
ANISOU 3137  OE1 GLU B 102     9904  13954  13349    608    197  -1766       O  
ATOM   3138  OE2 GLU B 102      47.097  -2.150  33.022  1.00 93.53           O  
ANISOU 3138  OE2 GLU B 102     9729  13446  12362    704     78  -1731       O  
ATOM   3139  N   LYS B 103      49.136   3.115  31.156  1.00 83.33           N  
ANISOU 3139  N   LYS B 103     7299  11784  12577    298    314  -1673       N  
ATOM   3140  CA  LYS B 103      49.791   4.289  30.594  1.00 80.20           C  
ANISOU 3140  CA  LYS B 103     6740  11213  12520    186    408  -1558       C  
ATOM   3141  C   LYS B 103      50.193   4.106  29.136  1.00 64.13           C  
ANISOU 3141  C   LYS B 103     4644   9243  10481     81    644  -1322       C  
ATOM   3142  O   LYS B 103      50.470   5.101  28.458  1.00 64.76           O  
ANISOU 3142  O   LYS B 103     4603   9215  10789    -23    768  -1140       O  
ATOM   3143  CB  LYS B 103      51.015   4.658  31.433  1.00 90.24           C  
ANISOU 3143  CB  LYS B 103     7908  12347  14032    257    254  -1808       C  
ATOM   3144  CG  LYS B 103      50.678   4.997  32.877  1.00 97.17           C  
ANISOU 3144  CG  LYS B 103     8833  13176  14912    360     23  -2058       C  
ATOM   3145  CD  LYS B 103      49.582   6.053  32.952  1.00100.68           C  
ANISOU 3145  CD  LYS B 103     9280  13521  15453    280     57  -1953       C  
ATOM   3146  CE  LYS B 103      49.201   6.357  34.392  1.00100.18           C  
ANISOU 3146  CE  LYS B 103     9265  13434  15363    389   -157  -2225       C  
ATOM   3147  NZ  LYS B 103      50.371   6.858  35.173  1.00 99.20           N  
ANISOU 3147  NZ  LYS B 103     9026  13193  15472    438   -304  -2511       N  
ATOM   3148  N   LYS B 104      50.240   2.865  28.644  1.00 50.37           N  
ANISOU 3148  N   LYS B 104     2984   7682   8471    112    716  -1329       N  
ATOM   3149  CA  LYS B 104      50.517   2.638  27.229  1.00 54.66           C  
ANISOU 3149  CA  LYS B 104     3490   8329   8950     15    954  -1119       C  
ATOM   3150  C   LYS B 104      49.381   3.140  26.341  1.00 65.21           C  
ANISOU 3150  C   LYS B 104     4857   9747  10173   -112   1105   -825       C  
ATOM   3151  O   LYS B 104      49.622   3.522  25.190  1.00 66.02           O  
ANISOU 3151  O   LYS B 104     4885   9894  10304   -203   1298   -585       O  
ATOM   3152  CB  LYS B 104      50.776   1.153  26.981  1.00 61.23           C  
ANISOU 3152  CB  LYS B 104     4462   9320   9484     84    981  -1221       C  
ATOM   3153  CG  LYS B 104      51.645   0.869  25.762  1.00 67.90           C  
ANISOU 3153  CG  LYS B 104     5197  10252  10350     30   1202  -1136       C  
ATOM   3154  CD  LYS B 104      52.287  -0.509  25.852  1.00 57.33           C  
ANISOU 3154  CD  LYS B 104     3957   8985   8842    143   1178  -1326       C  
ATOM   3155  CE  LYS B 104      53.237  -0.752  24.694  1.00 54.58           C  
ANISOU 3155  CE  LYS B 104     3496   8710   8532    102   1397  -1265       C  
ATOM   3156  NZ  LYS B 104      53.905  -2.077  24.801  1.00 53.25           N  
ANISOU 3156  NZ  LYS B 104     3386   8594   8252    223   1385  -1477       N  
ATOM   3157  N   LEU B 105      48.150   3.130  26.842  1.00 68.99           N  
ANISOU 3157  N   LEU B 105     5514  10240  10458   -105    999   -793       N  
ATOM   3158  CA  LEU B 105      46.961   3.498  26.068  1.00 62.14           C  
ANISOU 3158  CA  LEU B 105     4726   9461   9423   -205   1099   -506       C  
ATOM   3159  C   LEU B 105      46.507   4.921  26.372  1.00 68.44           C  
ANISOU 3159  C   LEU B 105     5369  10091  10545   -245   1084   -399       C  
ATOM   3160  O   LEU B 105      45.323   5.167  26.589  1.00 85.38           O  
ANISOU 3160  O   LEU B 105     7621  12246  12574   -258   1031   -304       O  
ATOM   3161  CB  LEU B 105      45.831   2.511  26.338  1.00 60.21           C  
ANISOU 3161  CB  LEU B 105     4769   9342   8766   -180   1009   -531       C  
ATOM   3162  CG  LEU B 105      46.050   1.026  26.064  1.00 52.75           C  
ANISOU 3162  CG  LEU B 105     4006   8538   7498   -144   1025   -638       C  
ATOM   3163  CD1 LEU B 105      44.894   0.224  26.628  1.00 47.24           C  
ANISOU 3163  CD1 LEU B 105     3562   7890   6497   -118    919   -683       C  
ATOM   3164  CD2 LEU B 105      46.175   0.793  24.570  1.00 48.94           C  
ANISOU 3164  CD2 LEU B 105     3500   8234   6859   -239   1228   -457       C  
ATOM   3165  N   GLN B 106      47.424   5.884  26.391  1.00 71.72           N  
ANISOU 3165  N   GLN B 106     5602  10325  11324   -258   1107   -391       N  
ATOM   3166  CA  GLN B 106      47.076   7.258  26.729  1.00 81.35           C  
ANISOU 3166  CA  GLN B 106     6752  11337  12821   -286   1066   -310       C  
ATOM   3167  C   GLN B 106      47.053   8.176  25.511  1.00 86.79           C  
ANISOU 3167  C   GLN B 106     7364  12006  13604   -387   1254     29       C  
ATOM   3168  O   GLN B 106      47.199   9.393  25.655  1.00 92.08           O  
ANISOU 3168  O   GLN B 106     7944  12448  14595   -411   1257     79       O  
ATOM   3169  CB  GLN B 106      48.031   7.804  27.792  1.00 89.82           C  
ANISOU 3169  CB  GLN B 106     7740  12182  14207   -227    919   -591       C  
ATOM   3170  CG  GLN B 106      48.034   7.001  29.086  1.00 90.94           C  
ANISOU 3170  CG  GLN B 106     7972  12355  14227   -105    707   -932       C  
ATOM   3171  CD  GLN B 106      46.749   7.146  29.881  1.00 85.94           C  
ANISOU 3171  CD  GLN B 106     7435  11724  13492    -68    598   -985       C  
ATOM   3172  OE1 GLN B 106      45.961   8.061  29.650  1.00 93.76           O  
ANISOU 3172  OE1 GLN B 106     8399  12628  14596   -128    654   -807       O  
ATOM   3173  NE2 GLN B 106      46.530   6.234  30.822  1.00 78.73           N  
ANISOU 3173  NE2 GLN B 106     6636  10920  12358     43    446  -1225       N  
ATOM   3174  N   ASN B 107      46.862   7.622  24.316  1.00 80.22           N  
ANISOU 3174  N   ASN B 107     6579  11403  12497   -440   1414    247       N  
ATOM   3175  CA  ASN B 107      46.766   8.441  23.119  1.00 77.20           C  
ANISOU 3175  CA  ASN B 107     6164  11026  12145   -518   1585    571       C  
ATOM   3176  C   ASN B 107      45.332   8.934  22.932  1.00 71.45           C  
ANISOU 3176  C   ASN B 107     5519  10313  11318   -534   1572    791       C  
ATOM   3177  O   ASN B 107      44.420   8.566  23.674  1.00 79.04           O  
ANISOU 3177  O   ASN B 107     6558  11307  12165   -499   1446    689       O  
ATOM   3178  CB  ASN B 107      47.247   7.659  21.899  1.00 75.32           C  
ANISOU 3178  CB  ASN B 107     5959  11030  11630   -556   1757    681       C  
ATOM   3179  CG  ASN B 107      46.528   6.338  21.735  1.00 73.72           C  
ANISOU 3179  CG  ASN B 107     5914  11087  11010   -541   1744    630       C  
ATOM   3180  OD1 ASN B 107      45.327   6.299  21.473  1.00 75.71           O  
ANISOU 3180  OD1 ASN B 107     6292  11438  11037   -553   1719    787       O  
ATOM   3181  ND2 ASN B 107      47.263   5.244  21.891  1.00 75.12           N  
ANISOU 3181  ND2 ASN B 107     6090  11368  11084   -503   1753    417       N  
ATOM   3182  N   ALA B 108      45.132   9.782  21.920  1.00 68.77           N  
ANISOU 3182  N   ALA B 108     5158   9946  11025   -575   1704   1114       N  
ATOM   3183  CA  ALA B 108      43.817  10.380  21.697  1.00 68.84           C  
ANISOU 3183  CA  ALA B 108     5226   9950  10979   -569   1685   1358       C  
ATOM   3184  C   ALA B 108      42.803   9.346  21.223  1.00 75.41           C  
ANISOU 3184  C   ALA B 108     6227  11092  11334   -569   1661   1430       C  
ATOM   3185  O   ALA B 108      41.633   9.382  21.630  1.00 69.38           O  
ANISOU 3185  O   ALA B 108     5528  10349  10484   -549   1559   1460       O  
ATOM   3186  CB  ALA B 108      43.924  11.524  20.692  1.00 64.74           C  
ANISOU 3186  CB  ALA B 108     4632   9329  10636   -585   1834   1717       C  
ATOM   3187  N   THR B 109      43.230   8.429  20.348  1.00 75.13           N  
ANISOU 3187  N   THR B 109     6265  11296  10986   -591   1753   1449       N  
ATOM   3188  CA  THR B 109      42.325   7.400  19.850  1.00 71.04           C  
ANISOU 3188  CA  THR B 109     5922  11074   9997   -593   1716   1486       C  
ATOM   3189  C   THR B 109      41.785   6.549  20.992  1.00 72.46           C  
ANISOU 3189  C   THR B 109     6178  11277  10077   -571   1563   1218       C  
ATOM   3190  O   THR B 109      40.595   6.215  21.017  1.00 73.77           O  
ANISOU 3190  O   THR B 109     6459  11576   9994   -572   1475   1266       O  
ATOM   3191  CB  THR B 109      43.036   6.525  18.818  1.00 73.84           C  
ANISOU 3191  CB  THR B 109     6340  11654  10061   -612   1837   1479       C  
ATOM   3192  OG1 THR B 109      43.452   7.335  17.713  1.00 79.96           O  
ANISOU 3192  OG1 THR B 109     7049  12439  10894   -623   1987   1760       O  
ATOM   3193  CG2 THR B 109      42.105   5.432  18.309  1.00 70.81           C  
ANISOU 3193  CG2 THR B 109     6147  11574   9185   -616   1774   1465       C  
ATOM   3194  N   ASN B 110      42.641   6.203  21.956  1.00 72.07           N  
ANISOU 3194  N   ASN B 110     6056  11109  10219   -543   1521    939       N  
ATOM   3195  CA  ASN B 110      42.172   5.424  23.096  1.00 64.82           C  
ANISOU 3195  CA  ASN B 110     5207  10225   9197   -500   1372    701       C  
ATOM   3196  C   ASN B 110      41.230   6.233  23.977  1.00 62.42           C  
ANISOU 3196  C   ASN B 110     4884   9751   9081   -475   1256    710       C  
ATOM   3197  O   ASN B 110      40.313   5.665  24.576  1.00 60.77           O  
ANISOU 3197  O   ASN B 110     4844   9591   8655   -452   1132    595       O  
ATOM   3198  CB  ASN B 110      43.358   4.918  23.916  1.00 65.57           C  
ANISOU 3198  CB  ASN B 110     5290  10188   9436   -440   1310    375       C  
ATOM   3199  CG  ASN B 110      44.126   3.816  23.213  1.00 65.98           C  
ANISOU 3199  CG  ASN B 110     5410  10415   9242   -445   1398    299       C  
ATOM   3200  OD1 ASN B 110      45.355   3.858  23.129  1.00 58.44           O  
ANISOU 3200  OD1 ASN B 110     4322   9394   8489   -429   1469    215       O  
ATOM   3201  ND2 ASN B 110      43.405   2.820  22.703  1.00 65.43           N  
ANISOU 3201  ND2 ASN B 110     5534  10567   8758   -470   1396    309       N  
ATOM   3202  N   TYR B 111      41.419   7.555  24.052  1.00 65.82           N  
ANISOU 3202  N   TYR B 111     5165   9948   9897   -477   1286    811       N  
ATOM   3203  CA  TYR B 111      40.458   8.391  24.768  1.00 78.98           C  
ANISOU 3203  CA  TYR B 111     6809  11458  11742   -450   1196    831       C  
ATOM   3204  C   TYR B 111      39.099   8.384  24.080  1.00 78.26           C  
ANISOU 3204  C   TYR B 111     6824  11534  11379   -474   1201   1090       C  
ATOM   3205  O   TYR B 111      38.057   8.289  24.743  1.00 81.11           O  
ANISOU 3205  O   TYR B 111     7231  11912  11673   -450   1105   1043       O  
ATOM   3206  CB  TYR B 111      40.984   9.821  24.895  1.00 88.90           C  
ANISOU 3206  CB  TYR B 111     7923  12415  13438   -446   1224    872       C  
ATOM   3207  CG  TYR B 111      42.134   9.981  25.864  1.00 94.26           C  
ANISOU 3207  CG  TYR B 111     8510  12899  14406   -410   1153    558       C  
ATOM   3208  CD1 TYR B 111      42.081   9.422  27.136  1.00 92.81           C  
ANISOU 3208  CD1 TYR B 111     8361  12697  14206   -341    999    233       C  
ATOM   3209  CD2 TYR B 111      43.272  10.693  25.508  1.00103.36           C  
ANISOU 3209  CD2 TYR B 111     9548  13886  15839   -436   1232    586       C  
ATOM   3210  CE1 TYR B 111      43.132   9.568  28.026  1.00 99.57           C  
ANISOU 3210  CE1 TYR B 111     9156  13390  15285   -290    902    -67       C  
ATOM   3211  CE2 TYR B 111      44.330  10.841  26.388  1.00105.06           C  
ANISOU 3211  CE2 TYR B 111     9685  13927  16306   -401   1147    290       C  
ATOM   3212  CZ  TYR B 111      44.255  10.278  27.645  1.00102.12           C  
ANISOU 3212  CZ  TYR B 111     9363  13554  15884   -324    972    -39       C  
ATOM   3213  OH  TYR B 111      45.308  10.431  28.518  1.00 96.87           O  
ANISOU 3213  OH  TYR B 111     8634  12732  15441   -278    866   -342       O  
ATOM   3214  N   PHE B 112      39.087   8.483  22.751  1.00 71.02           N  
ANISOU 3214  N   PHE B 112     5937  10753  10294   -511   1307   1359       N  
ATOM   3215  CA  PHE B 112      37.824   8.401  22.026  1.00 73.45           C  
ANISOU 3215  CA  PHE B 112     6338  11259  10311   -519   1286   1593       C  
ATOM   3216  C   PHE B 112      37.183   7.028  22.186  1.00 74.96           C  
ANISOU 3216  C   PHE B 112     6688  11702  10091   -540   1203   1434       C  
ATOM   3217  O   PHE B 112      35.956   6.912  22.287  1.00 86.89           O  
ANISOU 3217  O   PHE B 112     8260  13309  11445   -542   1122   1488       O  
ATOM   3218  CB  PHE B 112      38.042   8.736  20.556  1.00 77.61           C  
ANISOU 3218  CB  PHE B 112     6856  11919  10713   -533   1404   1902       C  
ATOM   3219  CG  PHE B 112      38.004  10.208  20.261  1.00 86.09           C  
ANISOU 3219  CG  PHE B 112     7796  12784  12130   -502   1467   2181       C  
ATOM   3220  CD1 PHE B 112      36.804  10.840  19.980  1.00 83.89           C  
ANISOU 3220  CD1 PHE B 112     7501  12538  11835   -464   1424   2440       C  
ATOM   3221  CD2 PHE B 112      39.167  10.960  20.261  1.00 92.62           C  
ANISOU 3221  CD2 PHE B 112     8502  13377  13312   -506   1571   2189       C  
ATOM   3222  CE1 PHE B 112      36.763  12.193  19.707  1.00 87.05           C  
ANISOU 3222  CE1 PHE B 112     7771  12728  12575   -419   1490   2720       C  
ATOM   3223  CE2 PHE B 112      39.133  12.315  19.988  1.00 95.70           C  
ANISOU 3223  CE2 PHE B 112     8771  13549  14043   -474   1639   2456       C  
ATOM   3224  CZ  PHE B 112      37.927  12.932  19.711  1.00 93.36           C  
ANISOU 3224  CZ  PHE B 112     8463  13274  13735   -425   1603   2731       C  
ATOM   3225  N   LEU B 113      37.996   5.973  22.220  1.00 72.46           N  
ANISOU 3225  N   LEU B 113     6436  11484   9610   -557   1224   1230       N  
ATOM   3226  CA  LEU B 113      37.451   4.640  22.448  1.00 64.50           C  
ANISOU 3226  CA  LEU B 113     5589  10677   8241   -579   1152   1046       C  
ATOM   3227  C   LEU B 113      36.889   4.497  23.856  1.00 56.09           C  
ANISOU 3227  C   LEU B 113     4587   9463   7263   -537   1021    834       C  
ATOM   3228  O   LEU B 113      35.907   3.779  24.057  1.00 57.03           O  
ANISOU 3228  O   LEU B 113     4846   9688   7137   -555    949    767       O  
ATOM   3229  CB  LEU B 113      38.512   3.575  22.183  1.00 64.00           C  
ANISOU 3229  CB  LEU B 113     5587  10713   8016   -590   1210    861       C  
ATOM   3230  CG  LEU B 113      38.962   3.471  20.727  1.00 55.49           C  
ANISOU 3230  CG  LEU B 113     4532   9791   6761   -619   1322   1014       C  
ATOM   3231  CD1 LEU B 113      39.864   2.264  20.547  1.00 50.07           C  
ANISOU 3231  CD1 LEU B 113     3923   9203   5898   -624   1373    785       C  
ATOM   3232  CD2 LEU B 113      37.762   3.407  19.794  1.00 43.36           C  
ANISOU 3232  CD2 LEU B 113     3080   8473   4922   -652   1283   1197       C  
ATOM   3233  N   MET B 114      37.489   5.168  24.842  1.00 56.51           N  
ANISOU 3233  N   MET B 114     4554   9256   7660   -475    985    705       N  
ATOM   3234  CA  MET B 114      36.918   5.150  26.186  1.00 63.25           C  
ANISOU 3234  CA  MET B 114     5485   9970   8579   -414    858    504       C  
ATOM   3235  C   MET B 114      35.604   5.918  26.229  1.00 63.57           C  
ANISOU 3235  C   MET B 114     5474  10001   8679   -421    836    679       C  
ATOM   3236  O   MET B 114      34.672   5.530  26.944  1.00 62.36           O  
ANISOU 3236  O   MET B 114     5433   9862   8399   -402    758    576       O  
ATOM   3237  CB  MET B 114      37.905   5.737  27.198  1.00 63.43           C  
ANISOU 3237  CB  MET B 114     5406   9747   8946   -339    812    296       C  
ATOM   3238  CG  MET B 114      37.354   5.814  28.623  1.00 62.45           C  
ANISOU 3238  CG  MET B 114     5352   9505   8873   -258    685     78       C  
ATOM   3239  SD  MET B 114      38.543   6.424  29.834  1.00 60.56           S  
ANISOU 3239  SD  MET B 114     4990   9030   8990   -160    598   -225       S  
ATOM   3240  CE  MET B 114      38.824   8.073  29.196  1.00 70.77           C  
ANISOU 3240  CE  MET B 114     5987  10132  10771   -214    702    -20       C  
ATOM   3241  N   SER B 115      35.511   7.010  25.468  1.00 58.02           N  
ANISOU 3241  N   SER B 115     4592   9270   8181   -443    917    960       N  
ATOM   3242  CA  SER B 115      34.233   7.702  25.331  1.00 62.41           C  
ANISOU 3242  CA  SER B 115     5088   9843   8784   -442    902   1168       C  
ATOM   3243  C   SER B 115      33.180   6.784  24.718  1.00 64.88           C  
ANISOU 3243  C   SER B 115     5532  10441   8677   -494    870   1245       C  
ATOM   3244  O   SER B 115      32.031   6.732  25.182  1.00 62.32           O  
ANISOU 3244  O   SER B 115     5246  10138   8294   -485    802   1226       O  
ATOM   3245  CB  SER B 115      34.418   8.963  24.486  1.00 60.61           C  
ANISOU 3245  CB  SER B 115     4739   9483   8808   -434    982   1447       C  
ATOM   3246  OG  SER B 115      33.199   9.664  24.325  1.00 63.95           O  
ANISOU 3246  OG  SER B 115     5129   9892   9278   -409    952   1646       O  
ATOM   3247  N   LEU B 116      33.569   6.042  23.679  1.00 65.00           N  
ANISOU 3247  N   LEU B 116     5630  10660   8408   -545    913   1295       N  
ATOM   3248  CA  LEU B 116      32.682   5.054  23.072  1.00 58.69           C  
ANISOU 3248  CA  LEU B 116     4958  10130   7212   -603    870   1300       C  
ATOM   3249  C   LEU B 116      32.260   3.996  24.084  1.00 67.12           C  
ANISOU 3249  C   LEU B 116     6167  11195   8142   -616    801   1018       C  
ATOM   3250  O   LEU B 116      31.105   3.557  24.096  1.00 63.23           O  
ANISOU 3250  O   LEU B 116     5728  10821   7475   -654    747   1016       O  
ATOM   3251  CB  LEU B 116      33.385   4.411  21.880  1.00 59.57           C  
ANISOU 3251  CB  LEU B 116     5131  10433   7068   -644    932   1331       C  
ATOM   3252  CG  LEU B 116      32.611   3.409  21.033  1.00 68.42           C  
ANISOU 3252  CG  LEU B 116     6364  11849   7785   -707    885   1312       C  
ATOM   3253  CD1 LEU B 116      31.641   4.146  20.149  1.00 73.49           C  
ANISOU 3253  CD1 LEU B 116     6922  12643   8358   -697    846   1604       C  
ATOM   3254  CD2 LEU B 116      33.566   2.571  20.199  1.00 73.78           C  
ANISOU 3254  CD2 LEU B 116     7119  12665   8248   -736    951   1214       C  
ATOM   3255  N   ALA B 117      33.191   3.574  24.943  1.00 68.79           N  
ANISOU 3255  N   ALA B 117     6459  11240   8437   -573    793    775       N  
ATOM   3256  CA  ALA B 117      32.883   2.575  25.961  1.00 67.22           C  
ANISOU 3256  CA  ALA B 117     6435  10988   8116   -555    729    522       C  
ATOM   3257  C   ALA B 117      31.914   3.122  27.000  1.00 64.93           C  
ANISOU 3257  C   ALA B 117     6132  10577   7962   -507    670    501       C  
ATOM   3258  O   ALA B 117      31.027   2.402  27.470  1.00 68.01           O  
ANISOU 3258  O   ALA B 117     6637  11012   8194   -526    639    416       O  
ATOM   3259  CB  ALA B 117      34.169   2.101  26.634  1.00 71.63           C  
ANISOU 3259  CB  ALA B 117     7065  11411   8742   -491    725    299       C  
ATOM   3260  N   ILE B 118      32.073   4.390  27.379  1.00 56.42           N  
ANISOU 3260  N   ILE B 118     4905   9334   7197   -447    667    567       N  
ATOM   3261  CA  ILE B 118      31.123   5.004  28.303  1.00 48.43           C  
ANISOU 3261  CA  ILE B 118     3860   8213   6329   -396    625    541       C  
ATOM   3262  C   ILE B 118      29.743   5.067  27.668  1.00 51.29           C  
ANISOU 3262  C   ILE B 118     4181   8734   6573   -454    625    740       C  
ATOM   3263  O   ILE B 118      28.725   4.806  28.325  1.00 45.56           O  
ANISOU 3263  O   ILE B 118     3509   8017   5785   -448    596    673       O  
ATOM   3264  CB  ILE B 118      31.608   6.402  28.734  1.00 43.69           C  
ANISOU 3264  CB  ILE B 118     3083   7388   6129   -325    630    556       C  
ATOM   3265  CG1 ILE B 118      32.830   6.292  29.647  1.00 48.17           C  
ANISOU 3265  CG1 ILE B 118     3685   7804   6812   -255    595    287       C  
ATOM   3266  CG2 ILE B 118      30.485   7.167  29.421  1.00 36.43           C  
ANISOU 3266  CG2 ILE B 118     2095   6378   5371   -277    607    570       C  
ATOM   3267  CD1 ILE B 118      33.320   7.621  30.182  1.00 36.95           C  
ANISOU 3267  CD1 ILE B 118     2081   6147   5813   -193    589    229       C  
ATOM   3268  N   ALA B 119      29.688   5.412  26.378  1.00 55.81           N  
ANISOU 3268  N   ALA B 119     4648   9451   7107   -506    660    993       N  
ATOM   3269  CA  ALA B 119      28.411   5.425  25.675  1.00 44.09           C  
ANISOU 3269  CA  ALA B 119     3109   8162   5480   -554    638   1184       C  
ATOM   3270  C   ALA B 119      27.781   4.038  25.661  1.00 48.88           C  
ANISOU 3270  C   ALA B 119     3872   8943   5758   -632    604   1033       C  
ATOM   3271  O   ALA B 119      26.579   3.891  25.913  1.00 50.06           O  
ANISOU 3271  O   ALA B 119     4012   9150   5858   -654    568   1037       O  
ATOM   3272  CB  ALA B 119      28.600   5.945  24.253  1.00 39.25           C  
ANISOU 3272  CB  ALA B 119     2413   7675   4824   -569    663   1464       C  
ATOM   3273  N   ASP B 120      28.587   3.006  25.399  1.00 49.52           N  
ANISOU 3273  N   ASP B 120     4084   9087   5642   -676    625    888       N  
ATOM   3274  CA  ASP B 120      28.067   1.641  25.376  1.00 51.10           C  
ANISOU 3274  CA  ASP B 120     4429   9413   5575   -757    609    727       C  
ATOM   3275  C   ASP B 120      27.580   1.200  26.750  1.00 48.83           C  
ANISOU 3275  C   ASP B 120     4252   8964   5338   -724    598    546       C  
ATOM   3276  O   ASP B 120      26.552   0.522  26.865  1.00 40.71           O  
ANISOU 3276  O   ASP B 120     3268   8012   4189   -789    588    498       O  
ATOM   3277  CB  ASP B 120      29.139   0.683  24.867  1.00 49.78           C  
ANISOU 3277  CB  ASP B 120     4371   9304   5237   -793    648    598       C  
ATOM   3278  CG  ASP B 120      29.149   0.571  23.363  1.00 67.64           C  
ANISOU 3278  CG  ASP B 120     6567  11842   7293   -866    664    729       C  
ATOM   3279  OD1 ASP B 120      28.052   0.596  22.768  1.00 66.37           O  
ANISOU 3279  OD1 ASP B 120     6347  11862   7008   -919    611    830       O  
ATOM   3280  OD2 ASP B 120      30.249   0.448  22.778  1.00 88.35           O  
ANISOU 3280  OD2 ASP B 120     9198  14503   9869   -860    720    722       O  
ATOM   3281  N   MET B 121      28.298   1.578  27.806  1.00 55.78           N  
ANISOU 3281  N   MET B 121     5167   9631   6394   -622    602    441       N  
ATOM   3282  CA  MET B 121      27.875   1.209  29.151  1.00 54.59           C  
ANISOU 3282  CA  MET B 121     5125   9357   6259   -568    599    283       C  
ATOM   3283  C   MET B 121      26.574   1.912  29.529  1.00 53.81           C  
ANISOU 3283  C   MET B 121     4924   9256   6265   -558    591    371       C  
ATOM   3284  O   MET B 121      25.680   1.298  30.124  1.00 44.44           O  
ANISOU 3284  O   MET B 121     3811   8082   4992   -580    611    304       O  
ATOM   3285  CB  MET B 121      28.991   1.529  30.145  1.00 49.56           C  
ANISOU 3285  CB  MET B 121     4530   8537   5764   -446    586    139       C  
ATOM   3286  CG  MET B 121      28.739   1.054  31.565  1.00 59.04           C  
ANISOU 3286  CG  MET B 121     5866   9645   6923   -364    584    -27       C  
ATOM   3287  SD  MET B 121      30.099   1.490  32.675  1.00 66.64           S  
ANISOU 3287  SD  MET B 121     6850  10444   8025   -205    532   -216       S  
ATOM   3288  CE  MET B 121      30.068   3.283  32.577  1.00 66.27           C  
ANISOU 3288  CE  MET B 121     6563  10298   8320   -171    509   -139       C  
ATOM   3289  N   LEU B 122      26.438   3.192  29.168  1.00 55.39           N  
ANISOU 3289  N   LEU B 122     4944   9431   6670   -524    576    534       N  
ATOM   3290  CA  LEU B 122      25.178   3.891  29.406  1.00 49.35           C  
ANISOU 3290  CA  LEU B 122     4058   8668   6026   -508    571    632       C  
ATOM   3291  C   LEU B 122      24.048   3.266  28.600  1.00 53.02           C  
ANISOU 3291  C   LEU B 122     4496   9350   6301   -618    557    732       C  
ATOM   3292  O   LEU B 122      22.904   3.202  29.063  1.00 52.66           O  
ANISOU 3292  O   LEU B 122     4418   9322   6269   -628    563    722       O  
ATOM   3293  CB  LEU B 122      25.324   5.373  29.062  1.00 45.03           C  
ANISOU 3293  CB  LEU B 122     3312   8030   5767   -445    565    810       C  
ATOM   3294  CG  LEU B 122      26.232   6.191  29.983  1.00 52.29           C  
ANISOU 3294  CG  LEU B 122     4206   8706   6953   -337    574    679       C  
ATOM   3295  CD1 LEU B 122      26.350   7.627  29.497  1.00 59.63           C  
ANISOU 3295  CD1 LEU B 122     4922   9523   8214   -294    588    877       C  
ATOM   3296  CD2 LEU B 122      25.706   6.148  31.409  1.00 43.30           C  
ANISOU 3296  CD2 LEU B 122     3133   7467   5851   -261    577    470       C  
ATOM   3297  N   LEU B 123      24.354   2.791  27.392  1.00 58.00           N  
ANISOU 3297  N   LEU B 123     5127  10159   6752   -702    538    810       N  
ATOM   3298  CA  LEU B 123      23.351   2.101  26.589  1.00 49.76           C  
ANISOU 3298  CA  LEU B 123     4053   9349   5506   -814    505    854       C  
ATOM   3299  C   LEU B 123      22.916   0.803  27.258  1.00 45.90           C  
ANISOU 3299  C   LEU B 123     3716   8837   4886   -884    537    638       C  
ATOM   3300  O   LEU B 123      21.726   0.469  27.274  1.00 44.94           O  
ANISOU 3300  O   LEU B 123     3542   8803   4730   -951    528    635       O  
ATOM   3301  CB  LEU B 123      23.912   1.836  25.192  1.00 48.16           C  
ANISOU 3301  CB  LEU B 123     3830   9358   5110   -878    483    941       C  
ATOM   3302  CG  LEU B 123      22.944   1.393  24.100  1.00 48.92           C  
ANISOU 3302  CG  LEU B 123     3863   9730   4994   -971    411   1003       C  
ATOM   3303  CD1 LEU B 123      21.890   2.455  23.877  1.00 45.57           C  
ANISOU 3303  CD1 LEU B 123     3270   9347   4699   -914    346   1225       C  
ATOM   3304  CD2 LEU B 123      23.710   1.122  22.814  1.00 59.23           C  
ANISOU 3304  CD2 LEU B 123     5177  11246   6082  -1010    401   1053       C  
ATOM   3305  N   GLY B 124      23.867   0.068  27.833  1.00 49.51           N  
ANISOU 3305  N   GLY B 124     4351   9167   5293   -864    581    469       N  
ATOM   3306  CA  GLY B 124      23.531  -1.169  28.511  1.00 50.07           C  
ANISOU 3306  CA  GLY B 124     4575   9184   5266   -915    632    298       C  
ATOM   3307  C   GLY B 124      22.848  -0.973  29.846  1.00 48.82           C  
ANISOU 3307  C   GLY B 124     4440   8887   5221   -847    680    259       C  
ATOM   3308  O   GLY B 124      22.178  -1.891  30.326  1.00 58.12           O  
ANISOU 3308  O   GLY B 124     5699  10047   6337   -905    739    178       O  
ATOM   3309  N   PHE B 125      23.000   0.203  30.454  1.00 47.00           N  
ANISOU 3309  N   PHE B 125     4135   8556   5165   -725    667    310       N  
ATOM   3310  CA  PHE B 125      22.357   0.489  31.733  1.00 39.09           C  
ANISOU 3310  CA  PHE B 125     3146   7447   4258   -644    718    256       C  
ATOM   3311  C   PHE B 125      20.974   1.112  31.583  1.00 53.98           C  
ANISOU 3311  C   PHE B 125     4853   9408   6251   -672    719    369       C  
ATOM   3312  O   PHE B 125      20.068   0.802  32.365  1.00 53.25           O  
ANISOU 3312  O   PHE B 125     4776   9296   6162   -675    789    322       O  
ATOM   3313  CB  PHE B 125      23.225   1.434  32.566  1.00 41.64           C  
ANISOU 3313  CB  PHE B 125     3473   7619   4730   -490    703    196       C  
ATOM   3314  CG  PHE B 125      24.140   0.738  33.531  1.00 59.55           C  
ANISOU 3314  CG  PHE B 125     5937   9792   6898   -410    725     30       C  
ATOM   3315  CD1 PHE B 125      23.647   0.220  34.718  1.00 57.48           C  
ANISOU 3315  CD1 PHE B 125     5791   9492   6558   -354    796    -58       C  
ATOM   3316  CD2 PHE B 125      25.499   0.630  33.269  1.00 68.12           C  
ANISOU 3316  CD2 PHE B 125     7080  10835   7968   -377    680    -24       C  
ATOM   3317  CE1 PHE B 125      24.488  -0.410  35.616  1.00 62.39           C  
ANISOU 3317  CE1 PHE B 125     6591  10047   7066   -257    809   -182       C  
ATOM   3318  CE2 PHE B 125      26.346   0.000  34.164  1.00 66.45           C  
ANISOU 3318  CE2 PHE B 125     7033  10549   7667   -284    684   -169       C  
ATOM   3319  CZ  PHE B 125      25.840  -0.520  35.341  1.00 63.06           C  
ANISOU 3319  CZ  PHE B 125     6726  10093   7139   -218    742   -240       C  
ATOM   3320  N   LEU B 126      20.786   1.992  30.598  1.00 63.62           N  
ANISOU 3320  N   LEU B 126     5892  10717   7564   -684    650    535       N  
ATOM   3321  CA  LEU B 126      19.583   2.809  30.541  1.00 66.97           C  
ANISOU 3321  CA  LEU B 126     6120  11186   8139   -668    640    658       C  
ATOM   3322  C   LEU B 126      18.597   2.414  29.454  1.00 67.54           C  
ANISOU 3322  C   LEU B 126     6080  11472   8110   -789    584    765       C  
ATOM   3323  O   LEU B 126      17.410   2.719  29.591  1.00 84.06           O  
ANISOU 3323  O   LEU B 126     8065  13573  10299   -781    578    811       O  
ATOM   3324  CB  LEU B 126      19.959   4.286  30.344  1.00 61.79           C  
ANISOU 3324  CB  LEU B 126     5314  10442   7722   -558    603    795       C  
ATOM   3325  CG  LEU B 126      20.970   4.866  31.337  1.00 52.15           C  
ANISOU 3325  CG  LEU B 126     4166   9001   6648   -434    633    664       C  
ATOM   3326  CD1 LEU B 126      21.148   6.356  31.109  1.00 52.93           C  
ANISOU 3326  CD1 LEU B 126     4077   8984   7049   -343    611    799       C  
ATOM   3327  CD2 LEU B 126      20.548   4.591  32.767  1.00 53.26           C  
ANISOU 3327  CD2 LEU B 126     4401   9050   6784   -372    704    474       C  
ATOM   3328  N   VAL B 127      19.037   1.754  28.389  1.00 56.84           N  
ANISOU 3328  N   VAL B 127     4775  10257   6566   -881    528    775       N  
ATOM   3329  CA  VAL B 127      18.189   1.463  27.240  1.00 52.52           C  
ANISOU 3329  CA  VAL B 127     4137   9918   5900   -973    437    851       C  
ATOM   3330  C   VAL B 127      17.889  -0.027  27.123  1.00 57.18           C  
ANISOU 3330  C   VAL B 127     4814  10604   6307  -1128    462    670       C  
ATOM   3331  O   VAL B 127      16.731  -0.428  27.010  1.00 62.03           O  
ANISOU 3331  O   VAL B 127     5348  11299   6920  -1206    442    638       O  
ATOM   3332  CB  VAL B 127      18.818   2.003  25.939  1.00 43.69           C  
ANISOU 3332  CB  VAL B 127     2957   8946   4696   -954    352   1022       C  
ATOM   3333  CG1 VAL B 127      17.967   1.618  24.746  1.00 47.62           C  
ANISOU 3333  CG1 VAL B 127     3346   9736   5012  -1048    250   1080       C  
ATOM   3334  CG2 VAL B 127      18.983   3.509  26.026  1.00 52.33           C  
ANISOU 3334  CG2 VAL B 127     3944   9911   6027   -809    343   1223       C  
ATOM   3335  N   MET B 128      18.925  -0.861  27.148  1.00 56.60           N  
ANISOU 3335  N   MET B 128     4893  10507   6107  -1174    513    542       N  
ATOM   3336  CA  MET B 128      18.724  -2.287  26.909  1.00 50.85           C  
ANISOU 3336  CA  MET B 128     4247   9840   5232  -1324    543    363       C  
ATOM   3337  C   MET B 128      17.838  -2.963  27.954  1.00 47.48           C  
ANISOU 3337  C   MET B 128     3861   9283   4895  -1373    643    259       C  
ATOM   3338  O   MET B 128      16.948  -3.735  27.553  1.00 48.91           O  
ANISOU 3338  O   MET B 128     3971   9570   5043  -1516    638    177       O  
ATOM   3339  CB  MET B 128      20.093  -2.975  26.805  1.00 53.65           C  
ANISOU 3339  CB  MET B 128     4797  10113   5475  -1318    578    247       C  
ATOM   3340  CG  MET B 128      20.933  -2.472  25.634  1.00 67.30           C  
ANISOU 3340  CG  MET B 128     6477  12003   7092  -1296    503    342       C  
ATOM   3341  SD  MET B 128      22.611  -3.130  25.587  1.00 69.23           S  
ANISOU 3341  SD  MET B 128     6923  12135   7246  -1264    557    211       S  
ATOM   3342  CE  MET B 128      22.276  -4.889  25.558  1.00 66.76           C  
ANISOU 3342  CE  MET B 128     6734  11806   6825  -1415    611    -43       C  
ATOM   3343  N   PRO B 129      17.989  -2.724  29.264  1.00 54.35           N  
ANISOU 3343  N   PRO B 129     4830   9944   5876  -1264    740    252       N  
ATOM   3344  CA  PRO B 129      17.052  -3.354  30.211  1.00 48.58           C  
ANISOU 3344  CA  PRO B 129     4125   9119   5215  -1309    859    186       C  
ATOM   3345  C   PRO B 129      15.622  -2.872  30.046  1.00 48.30           C  
ANISOU 3345  C   PRO B 129     3874   9183   5294  -1348    829    259       C  
ATOM   3346  O   PRO B 129      14.689  -3.664  30.227  1.00 40.78           O  
ANISOU 3346  O   PRO B 129     2894   8220   4380  -1458    893    188       O  
ATOM   3347  CB  PRO B 129      17.634  -2.982  31.584  1.00 39.73           C  
ANISOU 3347  CB  PRO B 129     3149   7800   4147  -1144    949    180       C  
ATOM   3348  CG  PRO B 129      18.455  -1.776  31.337  1.00 47.92           C  
ANISOU 3348  CG  PRO B 129     4140   8841   5227  -1019    855    260       C  
ATOM   3349  CD  PRO B 129      19.040  -1.968  29.972  1.00 52.08           C  
ANISOU 3349  CD  PRO B 129     4639   9504   5644  -1099    754    281       C  
ATOM   3350  N   VAL B 130      15.419  -1.602  29.693  1.00 46.21           N  
ANISOU 3350  N   VAL B 130     3470   8972   5115  -1246    727    400       N  
ATOM   3351  CA  VAL B 130      14.069  -1.122  29.406  1.00 48.56           C  
ANISOU 3351  CA  VAL B 130     3577   9345   5528  -1255    671    475       C  
ATOM   3352  C   VAL B 130      13.495  -1.847  28.193  1.00 53.80           C  
ANISOU 3352  C   VAL B 130     4150  10212   6079  -1409    565    431       C  
ATOM   3353  O   VAL B 130      12.297  -2.149  28.139  1.00 51.27           O  
ANISOU 3353  O   VAL B 130     3708   9941   5832  -1484    561    396       O  
ATOM   3354  CB  VAL B 130      14.084   0.404  29.204  1.00 49.91           C  
ANISOU 3354  CB  VAL B 130     3625   9514   5826  -1103    589    651       C  
ATOM   3355  CG1 VAL B 130      12.688   0.914  28.889  1.00 57.12           C  
ANISOU 3355  CG1 VAL B 130     4336  10503   6866  -1097    528    737       C  
ATOM   3356  CG2 VAL B 130      14.658   1.098  30.432  1.00 40.43           C  
ANISOU 3356  CG2 VAL B 130     2488   8124   4750   -963    693    642       C  
ATOM   3357  N   SER B 131      14.344  -2.157  27.210  1.00 56.76           N  
ANISOU 3357  N   SER B 131     4570  10724   6272  -1459    484    411       N  
ATOM   3358  CA  SER B 131      13.890  -2.931  26.059  1.00 55.34           C  
ANISOU 3358  CA  SER B 131     4301  10775   5949  -1613    387    320       C  
ATOM   3359  C   SER B 131      13.500  -4.347  26.466  1.00 56.92           C  
ANISOU 3359  C   SER B 131     4562  10896   6168  -1780    494    101       C  
ATOM   3360  O   SER B 131      12.484  -4.878  25.997  1.00 53.34           O  
ANISOU 3360  O   SER B 131     3978  10556   5735  -1903    446      9       O  
ATOM   3361  CB  SER B 131      14.976  -2.957  24.984  1.00 50.84           C  
ANISOU 3361  CB  SER B 131     3770  10383   5164  -1624    305    333       C  
ATOM   3362  OG  SER B 131      14.515  -3.605  23.812  1.00 51.44           O  
ANISOU 3362  OG  SER B 131     3736  10738   5072  -1762    197    231       O  
ATOM   3363  N   MET B 132      14.283  -4.968  27.353  1.00 55.52           N  
ANISOU 3363  N   MET B 132     4576  10514   6004  -1780    645     21       N  
ATOM   3364  CA  MET B 132      13.913  -6.288  27.862  1.00 57.46           C  
ANISOU 3364  CA  MET B 132     4888  10633   6310  -1926    784   -149       C  
ATOM   3365  C   MET B 132      12.591  -6.241  28.621  1.00 55.03           C  
ANISOU 3365  C   MET B 132     4482  10232   6196  -1937    862   -120       C  
ATOM   3366  O   MET B 132      11.753  -7.144  28.490  1.00 49.56           O  
ANISOU 3366  O   MET B 132     3715   9531   5585  -2094    903   -244       O  
ATOM   3367  CB  MET B 132      15.020  -6.837  28.761  1.00 59.44           C  
ANISOU 3367  CB  MET B 132     5390  10655   6538  -1869    932   -189       C  
ATOM   3368  CG  MET B 132      14.725  -8.224  29.310  1.00 64.21           C  
ANISOU 3368  CG  MET B 132     6100  11074   7225  -1993   1094   -327       C  
ATOM   3369  SD  MET B 132      16.014  -8.824  30.412  1.00 68.54           S  
ANISOU 3369  SD  MET B 132     6973  11331   7740  -1861   1243   -327       S  
ATOM   3370  CE  MET B 132      15.742  -7.771  31.836  1.00 76.94           C  
ANISOU 3370  CE  MET B 132     8054  12314   8865  -1669   1326   -155       C  
ATOM   3371  N   LEU B 133      12.397  -5.198  29.433  1.00 53.26           N  
ANISOU 3371  N   LEU B 133     4244   9926   6065  -1774    894     28       N  
ATOM   3372  CA  LEU B 133      11.140  -5.036  30.158  1.00 50.45           C  
ANISOU 3372  CA  LEU B 133     3778   9497   5894  -1766    979     62       C  
ATOM   3373  C   LEU B 133       9.970  -4.880  29.195  1.00 65.35           C  
ANISOU 3373  C   LEU B 133     5426  11563   7841  -1847    836     55       C  
ATOM   3374  O   LEU B 133       8.899  -5.461  29.404  1.00 69.78           O  
ANISOU 3374  O   LEU B 133     5884  12087   8540  -1950    904    -14       O  
ATOM   3375  CB  LEU B 133      11.230  -3.834  31.099  1.00 44.57           C  
ANISOU 3375  CB  LEU B 133     3044   8663   5226  -1568   1027    194       C  
ATOM   3376  CG  LEU B 133       9.953  -3.496  31.875  1.00 53.09           C  
ANISOU 3376  CG  LEU B 133     3995   9680   6497  -1535   1128    233       C  
ATOM   3377  CD1 LEU B 133       9.627  -4.585  32.886  1.00 48.70           C  
ANISOU 3377  CD1 LEU B 133     3544   8972   5988  -1610   1352    163       C  
ATOM   3378  CD2 LEU B 133      10.056  -2.137  32.558  1.00 53.06           C  
ANISOU 3378  CD2 LEU B 133     3958   9629   6572  -1339   1140    337       C  
ATOM   3379  N   THR B 134      10.158  -4.095  28.132  1.00 65.53           N  
ANISOU 3379  N   THR B 134     5354  11784   7762  -1793    643    137       N  
ATOM   3380  CA  THR B 134       9.137  -3.984  27.097  1.00 57.02           C  
ANISOU 3380  CA  THR B 134     4055  10922   6687  -1857    484    133       C  
ATOM   3381  C   THR B 134       8.846  -5.343  26.475  1.00 61.83           C  
ANISOU 3381  C   THR B 134     4637  11616   7241  -2070    469    -89       C  
ATOM   3382  O   THR B 134       7.690  -5.663  26.176  1.00 73.52           O  
ANISOU 3382  O   THR B 134     5942  13169   8824  -2163    425   -165       O  
ATOM   3383  CB  THR B 134       9.585  -2.981  26.036  1.00 62.15           C  
ANISOU 3383  CB  THR B 134     4641  11785   7189  -1751    297    286       C  
ATOM   3384  OG1 THR B 134       9.722  -1.689  26.638  1.00 67.34           O  
ANISOU 3384  OG1 THR B 134     5294  12324   7968  -1561    322    479       O  
ATOM   3385  CG2 THR B 134       8.573  -2.897  24.911  1.00 64.62           C  
ANISOU 3385  CG2 THR B 134     4732  12363   7457  -1802    122    290       C  
ATOM   3386  N   ILE B 135       9.886  -6.158  26.283  1.00 64.40           N  
ANISOU 3386  N   ILE B 135     5124  11919   7426  -2151    508   -212       N  
ATOM   3387  CA  ILE B 135       9.687  -7.516  25.780  1.00 64.50           C  
ANISOU 3387  CA  ILE B 135     5121  11963   7424  -2361    520   -460       C  
ATOM   3388  C   ILE B 135       8.805  -8.316  26.731  1.00 60.03           C  
ANISOU 3388  C   ILE B 135     4537  11161   7109  -2463    703   -542       C  
ATOM   3389  O   ILE B 135       7.909  -9.050  26.298  1.00 58.84           O  
ANISOU 3389  O   ILE B 135     4245  11053   7059  -2617    676   -703       O  
ATOM   3390  CB  ILE B 135      11.041  -8.214  25.551  1.00 60.33           C  
ANISOU 3390  CB  ILE B 135     4780  11407   6736  -2414    565   -576       C  
ATOM   3391  CG1 ILE B 135      11.746  -7.627  24.332  1.00 57.64           C  
ANISOU 3391  CG1 ILE B 135     4408  11357   6137  -2359    378   -533       C  
ATOM   3392  CG2 ILE B 135      10.857  -9.713  25.384  1.00 56.34           C  
ANISOU 3392  CG2 ILE B 135     4288  10818   6302  -2632    647   -851       C  
ATOM   3393  CD1 ILE B 135      12.976  -8.384  23.944  1.00 56.54           C  
ANISOU 3393  CD1 ILE B 135     4411  11228   5844  -2430    415   -685       C  
ATOM   3394  N   LEU B 136       9.042  -8.187  28.041  1.00 61.26           N  
ANISOU 3394  N   LEU B 136     4832  11073   7370  -2371    896   -431       N  
ATOM   3395  CA  LEU B 136       8.259  -8.958  29.006  1.00 63.68           C  
ANISOU 3395  CA  LEU B 136     5137  11156   7902  -2454   1104   -469       C  
ATOM   3396  C   LEU B 136       6.780  -8.589  28.967  1.00 61.34           C  
ANISOU 3396  C   LEU B 136     4596  10920   7789  -2470   1064   -439       C  
ATOM   3397  O   LEU B 136       5.922  -9.446  29.202  1.00 71.20           O  
ANISOU 3397  O   LEU B 136     5761  12061   9233  -2610   1172   -536       O  
ATOM   3398  CB  LEU B 136       8.806  -8.760  30.421  1.00 63.00           C  
ANISOU 3398  CB  LEU B 136     5250  10848   7839  -2316   1313   -331       C  
ATOM   3399  CG  LEU B 136      10.124  -9.455  30.762  1.00 66.01           C  
ANISOU 3399  CG  LEU B 136     5884  11094   8100  -2315   1422   -370       C  
ATOM   3400  CD1 LEU B 136      10.515  -9.162  32.199  1.00 68.15           C  
ANISOU 3400  CD1 LEU B 136     6333  11187   8372  -2150   1609   -225       C  
ATOM   3401  CD2 LEU B 136      10.010 -10.954  30.533  1.00 62.36           C  
ANISOU 3401  CD2 LEU B 136     5448  10509   7736  -2527   1528   -550       C  
ATOM   3402  N   TYR B 137       6.459  -7.332  28.666  1.00 56.69           N  
ANISOU 3402  N   TYR B 137     3884  10488   7167  -2329    916   -302       N  
ATOM   3403  CA  TYR B 137       5.075  -6.876  28.623  1.00 60.96           C  
ANISOU 3403  CA  TYR B 137     4181  11090   7891  -2321    873   -262       C  
ATOM   3404  C   TYR B 137       4.475  -6.952  27.225  1.00 66.50           C  
ANISOU 3404  C   TYR B 137     4675  12057   8534  -2412    634   -364       C  
ATOM   3405  O   TYR B 137       3.587  -6.156  26.894  1.00 64.83           O  
ANISOU 3405  O   TYR B 137     4260  11976   8396  -2341    515   -279       O  
ATOM   3406  CB  TYR B 137       4.975  -5.450  29.167  1.00 64.99           C  
ANISOU 3406  CB  TYR B 137     4660  11592   8441  -2106    868    -57       C  
ATOM   3407  CG  TYR B 137       4.983  -5.359  30.677  1.00 68.86           C  
ANISOU 3407  CG  TYR B 137     5266  11844   9053  -2020   1120     16       C  
ATOM   3408  CD1 TYR B 137       6.164  -5.505  31.394  1.00 62.13           C  
ANISOU 3408  CD1 TYR B 137     4668  10863   8076  -1955   1239     39       C  
ATOM   3409  CD2 TYR B 137       3.809  -5.124  31.385  1.00 72.53           C  
ANISOU 3409  CD2 TYR B 137     5580  12233   9745  -1996   1241     59       C  
ATOM   3410  CE1 TYR B 137       6.177  -5.419  32.776  1.00 66.11           C  
ANISOU 3410  CE1 TYR B 137     5283  11189   8645  -1861   1464    103       C  
ATOM   3411  CE2 TYR B 137       3.811  -5.038  32.768  1.00 71.56           C  
ANISOU 3411  CE2 TYR B 137     5565  11927   9696  -1908   1483    125       C  
ATOM   3412  CZ  TYR B 137       4.999  -5.186  33.458  1.00 72.30           C  
ANISOU 3412  CZ  TYR B 137     5923  11918   9631  -1837   1590    146       C  
ATOM   3413  OH  TYR B 137       5.017  -5.099  34.832  1.00 72.94           O  
ANISOU 3413  OH  TYR B 137     6117  11857   9739  -1733   1824    207       O  
ATOM   3414  N   GLY B 138       4.937  -7.884  26.394  1.00 66.10           N  
ANISOU 3414  N   GLY B 138     4669  12098   8350  -2559    561   -554       N  
ATOM   3415  CA  GLY B 138       4.381  -8.037  25.059  1.00 75.80           C  
ANISOU 3415  CA  GLY B 138     5708  13606   9488  -2643    334   -685       C  
ATOM   3416  C   GLY B 138       4.528  -6.818  24.178  1.00 80.71           C  
ANISOU 3416  C   GLY B 138     6252  14509   9904  -2484    113   -517       C  
ATOM   3417  O   GLY B 138       3.660  -6.558  23.337  1.00 84.41           O  
ANISOU 3417  O   GLY B 138     6509  15205  10357  -2488    -64   -533       O  
ATOM   3418  N   TYR B 139       5.604  -6.051  24.358  1.00 81.91           N  
ANISOU 3418  N   TYR B 139     6566  14646   9910  -2337    125   -342       N  
ATOM   3419  CA  TYR B 139       5.888  -4.843  23.583  1.00 85.10           C  
ANISOU 3419  CA  TYR B 139     6918  15276  10138  -2173    -50   -135       C  
ATOM   3420  C   TYR B 139       4.830  -3.763  23.768  1.00 78.50           C  
ANISOU 3420  C   TYR B 139     5889  14459   9477  -2042   -103     49       C  
ATOM   3421  O   TYR B 139       4.671  -2.894  22.904  1.00 86.80           O  
ANISOU 3421  O   TYR B 139     6826  15738  10416  -1933   -276    204       O  
ATOM   3422  CB  TYR B 139       6.082  -5.152  22.091  1.00 87.54           C  
ANISOU 3422  CB  TYR B 139     7167  15926  10167  -2237   -250   -235       C  
ATOM   3423  CG  TYR B 139       7.282  -6.025  21.815  1.00 89.33           C  
ANISOU 3423  CG  TYR B 139     7584  16155  10203  -2335   -203   -402       C  
ATOM   3424  CD1 TYR B 139       8.570  -5.546  22.028  1.00 92.72           C  
ANISOU 3424  CD1 TYR B 139     8193  16525  10512  -2231   -148   -263       C  
ATOM   3425  CD2 TYR B 139       7.135  -7.324  21.345  1.00 89.46           C  
ANISOU 3425  CD2 TYR B 139     7589  16215  10187  -2530   -208   -713       C  
ATOM   3426  CE1 TYR B 139       9.677  -6.332  21.784  1.00 92.62           C  
ANISOU 3426  CE1 TYR B 139     8340  16511  10341  -2316   -100   -418       C  
ATOM   3427  CE2 TYR B 139       8.239  -8.121  21.096  1.00 95.27           C  
ANISOU 3427  CE2 TYR B 139     8492  16935  10771  -2614   -155   -881       C  
ATOM   3428  CZ  TYR B 139       9.509  -7.618  21.319  1.00 96.07           C  
ANISOU 3428  CZ  TYR B 139     8766  16992  10744  -2506   -102   -728       C  
ATOM   3429  OH  TYR B 139      10.617  -8.398  21.076  1.00 94.32           O  
ANISOU 3429  OH  TYR B 139     8697  16754  10386  -2585    -46   -898       O  
ATOM   3430  N   ARG B 140       4.106  -3.792  24.884  1.00 69.54           N  
ANISOU 3430  N   ARG B 140     4715  13089   8619  -2042     55     45       N  
ATOM   3431  CA  ARG B 140       3.217  -2.704  25.268  1.00 66.79           C  
ANISOU 3431  CA  ARG B 140     4202  12706   8469  -1899     48    214       C  
ATOM   3432  C   ARG B 140       3.876  -1.896  26.375  1.00 66.74           C  
ANISOU 3432  C   ARG B 140     4346  12465   8546  -1744    203    360       C  
ATOM   3433  O   ARG B 140       4.317  -2.461  27.381  1.00 67.36           O  
ANISOU 3433  O   ARG B 140     4591  12328   8674  -1784    398    285       O  
ATOM   3434  CB  ARG B 140       1.858  -3.228  25.731  1.00 63.59           C  
ANISOU 3434  CB  ARG B 140     3611  12219   8330  -1999    124     99       C  
ATOM   3435  CG  ARG B 140       0.909  -2.127  26.159  1.00 74.69           C  
ANISOU 3435  CG  ARG B 140     4833  13584   9964  -1852    132    251       C  
ATOM   3436  CD  ARG B 140      -0.344  -2.681  26.809  1.00 69.28           C  
ANISOU 3436  CD  ARG B 140     3978  12779   9568  -1951    260    142       C  
ATOM   3437  NE  ARG B 140      -1.530  -2.144  26.154  1.00 69.62           N  
ANISOU 3437  NE  ARG B 140     3726  12994   9733  -1912     94    177       N  
ATOM   3438  CZ  ARG B 140      -2.114  -2.710  25.106  1.00 72.32           C  
ANISOU 3438  CZ  ARG B 140     3901  13557  10019  -2028    -93     55       C  
ATOM   3439  NH1 ARG B 140      -1.621  -3.832  24.601  1.00 72.36           N  
ANISOU 3439  NH1 ARG B 140     4008  13626   9858  -2197   -126   -128       N  
ATOM   3440  NH2 ARG B 140      -3.189  -2.158  24.563  1.00 85.29           N  
ANISOU 3440  NH2 ARG B 140     5271  15359  11775  -1971   -249    100       N  
ATOM   3441  N   TRP B 141       3.921  -0.584  26.195  1.00 73.72           N  
ANISOU 3441  N   TRP B 141     5167  13390   9453  -1563    121    564       N  
ATOM   3442  CA  TRP B 141       4.659   0.304  27.085  1.00 68.18           C  
ANISOU 3442  CA  TRP B 141     4597  12485   8822  -1406    237    686       C  
ATOM   3443  C   TRP B 141       4.040   0.337  28.475  1.00 71.36           C  
ANISOU 3443  C   TRP B 141     4987  12655   9470  -1379    448    632       C  
ATOM   3444  O   TRP B 141       2.937   0.880  28.634  1.00 70.82           O  
ANISOU 3444  O   TRP B 141     4720  12585   9604  -1326    448    671       O  
ATOM   3445  CB  TRP B 141       4.704   1.709  26.492  1.00 64.42           C  
ANISOU 3445  CB  TRP B 141     4018  12092   8366  -1228    103    915       C  
ATOM   3446  CG  TRP B 141       5.660   2.619  27.187  1.00 61.73           C  
ANISOU 3446  CG  TRP B 141     3812  11557   8087  -1078    193   1021       C  
ATOM   3447  CD1 TRP B 141       5.352   3.739  27.903  1.00 55.03           C  
ANISOU 3447  CD1 TRP B 141     2889  10544   7474   -923    262   1111       C  
ATOM   3448  CD2 TRP B 141       7.088   2.489  27.236  1.00 73.34           C  
ANISOU 3448  CD2 TRP B 141     5497  12970   9400  -1072    223   1021       C  
ATOM   3449  NE1 TRP B 141       6.498   4.316  28.395  1.00 71.50           N  
ANISOU 3449  NE1 TRP B 141     5127  12473   9565   -825    329   1156       N  
ATOM   3450  CE2 TRP B 141       7.578   3.570  27.999  1.00 74.05           C  
ANISOU 3450  CE2 TRP B 141     5627  12858   9649   -912    304   1110       C  
ATOM   3451  CE3 TRP B 141       7.999   1.565  26.709  1.00 59.17           C  
ANISOU 3451  CE3 TRP B 141     3852  11272   7358  -1186    192    936       C  
ATOM   3452  CZ2 TRP B 141       8.940   3.752  28.248  1.00 55.36           C  
ANISOU 3452  CZ2 TRP B 141     3438  10388   7211   -865    346   1121       C  
ATOM   3453  CZ3 TRP B 141       9.346   1.746  26.958  1.00 51.04           C  
ANISOU 3453  CZ3 TRP B 141     3004  10140   6251  -1133    241    959       C  
ATOM   3454  CH2 TRP B 141       9.804   2.831  27.722  1.00 52.68           C  
ANISOU 3454  CH2 TRP B 141     3240  10147   6627   -975    313   1053       C  
ATOM   3455  N   PRO B 142       4.690  -0.227  29.495  1.00 73.25           N  
ANISOU 3455  N   PRO B 142     5426  12714   9692  -1408    635    548       N  
ATOM   3456  CA  PRO B 142       4.108  -0.213  30.843  1.00 81.23           C  
ANISOU 3456  CA  PRO B 142     6431  13537  10896  -1373    857    510       C  
ATOM   3457  C   PRO B 142       4.410   1.075  31.595  1.00 81.67           C  
ANISOU 3457  C   PRO B 142     6500  13479  11052  -1175    918    604       C  
ATOM   3458  O   PRO B 142       3.604   1.531  32.415  1.00 86.00           O  
ANISOU 3458  O   PRO B 142     6940  13939  11795  -1107   1045    597       O  
ATOM   3459  CB  PRO B 142       4.765  -1.426  31.510  1.00 81.74           C  
ANISOU 3459  CB  PRO B 142     6716  13489  10852  -1482   1022    397       C  
ATOM   3460  CG  PRO B 142       6.120  -1.503  30.856  1.00 76.95           C  
ANISOU 3460  CG  PRO B 142     6278  12944  10014  -1479    905    407       C  
ATOM   3461  CD  PRO B 142       5.976  -0.948  29.453  1.00 69.22           C  
ANISOU 3461  CD  PRO B 142     5152  12179   8970  -1469    660    484       C  
ATOM   3462  N   LEU B 143       5.573   1.668  31.308  1.00 74.04           N  
ANISOU 3462  N   LEU B 143     5652  12511   9967  -1084    833    677       N  
ATOM   3463  CA  LEU B 143       6.059   2.843  32.013  1.00 62.22           C  
ANISOU 3463  CA  LEU B 143     4180  10888   8574   -906    889    736       C  
ATOM   3464  C   LEU B 143       5.203   4.062  31.678  1.00 59.22           C  
ANISOU 3464  C   LEU B 143     3570  10525   8407   -788    805    847       C  
ATOM   3465  O   LEU B 143       4.361   4.015  30.778  1.00 60.43           O  
ANISOU 3465  O   LEU B 143     3558  10817   8584   -835    677    902       O  
ATOM   3466  CB  LEU B 143       7.525   3.085  31.652  1.00 70.90           C  
ANISOU 3466  CB  LEU B 143     5441  11979   9518   -861    811    785       C  
ATOM   3467  CG  LEU B 143       8.482   1.906  31.861  1.00 75.62           C  
ANISOU 3467  CG  LEU B 143     6266  12569   9897   -967    873    678       C  
ATOM   3468  CD1 LEU B 143       9.902   2.290  31.481  1.00 64.97           C  
ANISOU 3468  CD1 LEU B 143     5043  11212   8432   -907    793    728       C  
ATOM   3469  CD2 LEU B 143       8.431   1.405  33.296  1.00 76.64           C  
ANISOU 3469  CD2 LEU B 143     6506  12571  10043   -959   1096    566       C  
ATOM   3470  N   PRO B 144       5.382   5.170  32.403  1.00 55.87           N  
ANISOU 3470  N   PRO B 144     3119   9964   8146   -629    876    869       N  
ATOM   3471  CA  PRO B 144       4.651   6.396  32.059  1.00 69.48           C  
ANISOU 3471  CA  PRO B 144     4630  11680  10090   -502    797    980       C  
ATOM   3472  C   PRO B 144       4.925   6.845  30.630  1.00 65.52           C  
ANISOU 3472  C   PRO B 144     4075  11304   9518   -481    578   1175       C  
ATOM   3473  O   PRO B 144       5.979   6.563  30.056  1.00 70.44           O  
ANISOU 3473  O   PRO B 144     4841  11975   9950   -519    505   1225       O  
ATOM   3474  CB  PRO B 144       5.173   7.419  33.073  1.00 75.51           C  
ANISOU 3474  CB  PRO B 144     5421  12258  11011   -344    912    938       C  
ATOM   3475  CG  PRO B 144       5.606   6.609  34.242  1.00 62.06           C  
ANISOU 3475  CG  PRO B 144     3885  10499   9196   -390   1099    771       C  
ATOM   3476  CD  PRO B 144       6.050   5.274  33.716  1.00 53.62           C  
ANISOU 3476  CD  PRO B 144     2971   9533   7869   -557   1056    761       C  
ATOM   3477  N   SER B 145       3.950   7.554  30.054  1.00 78.20           N  
ANISOU 3477  N   SER B 145     4646  12666  12399    -25   1618   1411       N  
ATOM   3478  CA  SER B 145       4.074   7.987  28.666  1.00 83.81           C  
ANISOU 3478  CA  SER B 145     5035  13681  13128    148   1333   1862       C  
ATOM   3479  C   SER B 145       5.205   8.992  28.489  1.00103.92           C  
ANISOU 3479  C   SER B 145     7680  16030  15774    266   1320   2083       C  
ATOM   3480  O   SER B 145       5.793   9.079  27.403  1.00104.50           O  
ANISOU 3480  O   SER B 145     7668  16372  15665    344   1058   2391       O  
ATOM   3481  CB  SER B 145       2.755   8.584  28.181  1.00 83.15           C  
ANISOU 3481  CB  SER B 145     4421  13679  13492    316   1349   2138       C  
ATOM   3482  OG  SER B 145       1.735   7.603  28.158  1.00 87.00           O  
ANISOU 3482  OG  SER B 145     4773  14434  13848    185   1312   1956       O  
ATOM   3483  N   LYS B 146       5.522   9.759  29.536  1.00114.25           N  
ANISOU 3483  N   LYS B 146     9171  16879  17358    250   1618   1913       N  
ATOM   3484  CA  LYS B 146       6.613  10.720  29.447  1.00117.61           C  
ANISOU 3484  CA  LYS B 146     9702  17097  17886    320   1644   2072       C  
ATOM   3485  C   LYS B 146       7.971  10.042  29.346  1.00107.40           C  
ANISOU 3485  C   LYS B 146     8761  15975  16073    189   1437   1980       C  
ATOM   3486  O   LYS B 146       8.932  10.674  28.895  1.00114.42           O  
ANISOU 3486  O   LYS B 146     9681  16827  16966    256   1361   2183       O  
ATOM   3487  CB  LYS B 146       6.601  11.649  30.663  1.00124.01           C  
ANISOU 3487  CB  LYS B 146    10645  17383  19089    263   2054   1840       C  
ATOM   3488  CG  LYS B 146       5.374  12.540  30.776  1.00128.83           C  
ANISOU 3488  CG  LYS B 146    10892  17721  20337    426   2344   1962       C  
ATOM   3489  CD  LYS B 146       5.251  13.471  29.585  1.00129.21           C  
ANISOU 3489  CD  LYS B 146    10535  17826  20732    720   2234   2514       C  
ATOM   3490  CE  LYS B 146       4.041  14.377  29.720  1.00130.79           C  
ANISOU 3490  CE  LYS B 146    10336  17723  21634    917   2551   2686       C  
ATOM   3491  NZ  LYS B 146       3.867  15.237  28.520  1.00134.36           N  
ANISOU 3491  NZ  LYS B 146    10536  18225  22288   1199   2361   3228       N  
ATOM   3492  N   LEU B 147       8.073   8.775  29.754  1.00 91.08           N  
ANISOU 3492  N   LEU B 147     6944  14073  13589     13   1367   1695       N  
ATOM   3493  CA  LEU B 147       9.346   8.069  29.714  1.00 78.39           C  
ANISOU 3493  CA  LEU B 147     5647  12604  11534    -92   1203   1626       C  
ATOM   3494  C   LEU B 147       9.637   7.401  28.375  1.00 79.54           C  
ANISOU 3494  C   LEU B 147     5692  13156  11375    -41    910   1854       C  
ATOM   3495  O   LEU B 147      10.790   7.039  28.128  1.00 80.53           O  
ANISOU 3495  O   LEU B 147     6012  13371  11216    -80    787   1880       O  
ATOM   3496  CB  LEU B 147       9.404   7.018  30.826  1.00 71.38           C  
ANISOU 3496  CB  LEU B 147     5092  11667  10360   -295   1302   1248       C  
ATOM   3497  CG  LEU B 147       9.439   7.575  32.251  1.00 69.67           C  
ANISOU 3497  CG  LEU B 147     5080  11088  10305   -426   1581    980       C  
ATOM   3498  CD1 LEU B 147       9.588   6.454  33.267  1.00 74.75           C  
ANISOU 3498  CD1 LEU B 147     6062  11746  10593   -628   1636    672       C  
ATOM   3499  CD2 LEU B 147      10.554   8.589  32.405  1.00 68.06           C  
ANISOU 3499  CD2 LEU B 147     4958  10710  10189   -429   1599   1065       C  
ATOM   3500  N   CYS B 148       8.636   7.222  27.510  1.00 80.04           N  
ANISOU 3500  N   CYS B 148     5447  13482  11483     22    804   2015       N  
ATOM   3501  CA  CYS B 148       8.902   6.652  26.190  1.00 80.25           C  
ANISOU 3501  CA  CYS B 148     5380  13924  11187     19    542   2218       C  
ATOM   3502  C   CYS B 148       9.737   7.598  25.335  1.00 85.25           C  
ANISOU 3502  C   CYS B 148     5917  14582  11891    159    417   2582       C  
ATOM   3503  O   CYS B 148      10.697   7.176  24.673  1.00 93.43           O  
ANISOU 3503  O   CYS B 148     7088  15801  12610    115    276   2647       O  
ATOM   3504  CB  CYS B 148       7.590   6.313  25.485  1.00 83.50           C  
ANISOU 3504  CB  CYS B 148     5455  14663  11609     11    444   2308       C  
ATOM   3505  SG  CYS B 148       7.781   5.999  23.719  1.00 81.78           S  
ANISOU 3505  SG  CYS B 148     5039  14996  11036    -12    123   2632       S  
ATOM   3506  N   ALA B 149       9.373   8.883  25.320  1.00 88.82           N  
ANISOU 3506  N   ALA B 149     6131  14832  12784    331    500   2829       N  
ATOM   3507  CA  ALA B 149      10.160   9.862  24.579  1.00 87.78           C  
ANISOU 3507  CA  ALA B 149     5920  14668  12764    469    427   3184       C  
ATOM   3508  C   ALA B 149      11.578   9.950  25.124  1.00 75.57           C  
ANISOU 3508  C   ALA B 149     4717  12898  11100    393    494   3023       C  
ATOM   3509  O   ALA B 149      12.540  10.032  24.355  1.00 70.44           O  
ANISOU 3509  O   ALA B 149     4117  12378  10269    410    361   3205       O  
ATOM   3510  CB  ALA B 149       9.478  11.230  24.625  1.00 93.80           C  
ANISOU 3510  CB  ALA B 149     6379  15166  14095    674    583   3464       C  
ATOM   3511  N   VAL B 150      11.724   9.916  26.450  1.00 70.97           N  
ANISOU 3511  N   VAL B 150     4363  12006  10598    289    697   2681       N  
ATOM   3512  CA  VAL B 150      13.047   9.966  27.068  1.00 74.37           C  
ANISOU 3512  CA  VAL B 150     5092  12272  10894    184    739   2524       C  
ATOM   3513  C   VAL B 150      13.851   8.718  26.722  1.00 72.35           C  
ANISOU 3513  C   VAL B 150     5031  12298  10160     87    553   2445       C  
ATOM   3514  O   VAL B 150      15.068   8.785  26.516  1.00 64.44           O  
ANISOU 3514  O   VAL B 150     4151  11307   9026     69    484   2508       O  
ATOM   3515  CB  VAL B 150      12.909  10.152  28.591  1.00 67.94           C  
ANISOU 3515  CB  VAL B 150     4469  11127  10218     49    988   2174       C  
ATOM   3516  CG1 VAL B 150      14.271  10.107  29.268  1.00 66.35           C  
ANISOU 3516  CG1 VAL B 150     4555  10840   9816    -99    987   2016       C  
ATOM   3517  CG2 VAL B 150      12.206  11.463  28.895  1.00 73.92           C  
ANISOU 3517  CG2 VAL B 150     5039  11545  11502    139   1244   2241       C  
ATOM   3518  N   TRP B 151      13.189   7.562  26.658  1.00 64.79           N  
ANISOU 3518  N   TRP B 151     4098  11550   8969     18    502   2302       N  
ATOM   3519  CA  TRP B 151      13.877   6.325  26.304  1.00 62.88           C  
ANISOU 3519  CA  TRP B 151     4036  11533   8321    -72    392   2222       C  
ATOM   3520  C   TRP B 151      14.393   6.383  24.872  1.00 63.28           C  
ANISOU 3520  C   TRP B 151     3968  11847   8229    -14    224   2504       C  
ATOM   3521  O   TRP B 151      15.564   6.072  24.605  1.00 69.47           O  
ANISOU 3521  O   TRP B 151     4898  12670   8829    -39    177   2531       O  
ATOM   3522  CB  TRP B 151      12.932   5.141  26.509  1.00 64.45           C  
ANISOU 3522  CB  TRP B 151     4273  11868   8346   -175    430   1996       C  
ATOM   3523  CG  TRP B 151      13.513   3.795  26.186  1.00 69.59           C  
ANISOU 3523  CG  TRP B 151     5114  12700   8628   -274    393   1888       C  
ATOM   3524  CD1 TRP B 151      14.504   3.144  26.864  1.00 66.99           C  
ANISOU 3524  CD1 TRP B 151     5055  12258   8141   -326    446   1764       C  
ATOM   3525  CD2 TRP B 151      13.102   2.914  25.133  1.00 74.59           C  
ANISOU 3525  CD2 TRP B 151     5672  13649   9020   -349    329   1892       C  
ATOM   3526  NE1 TRP B 151      14.752   1.924  26.283  1.00 66.71           N  
ANISOU 3526  NE1 TRP B 151     5115  12399   7834   -394    452   1705       N  
ATOM   3527  CE2 TRP B 151      13.902   1.757  25.220  1.00 77.52           C  
ANISOU 3527  CE2 TRP B 151     6293  14028   9133   -433    395   1749       C  
ATOM   3528  CE3 TRP B 151      12.143   2.995  24.117  1.00 70.65           C  
ANISOU 3528  CE3 TRP B 151     4905  13445   8494   -369    228   2011       C  
ATOM   3529  CZ2 TRP B 151      13.772   0.692  24.331  1.00 80.24           C  
ANISOU 3529  CZ2 TRP B 151     6658  14621   9211   -555    414   1675       C  
ATOM   3530  CZ3 TRP B 151      12.014   1.936  23.238  1.00 69.41           C  
ANISOU 3530  CZ3 TRP B 151     4764  13594   8015   -521    202   1931       C  
ATOM   3531  CH2 TRP B 151      12.824   0.801  23.350  1.00 77.50           C  
ANISOU 3531  CH2 TRP B 151     6069  14575   8801   -621    319   1742       C  
ATOM   3532  N   ILE B 152      13.530   6.786  23.935  1.00 65.37           N  
ANISOU 3532  N   ILE B 152     3952  12310   8575     57    134   2733       N  
ATOM   3533  CA  ILE B 152      13.961   6.933  22.546  1.00 69.78           C  
ANISOU 3533  CA  ILE B 152     4394  13149   8971     88    -26   3027       C  
ATOM   3534  C   ILE B 152      15.079   7.965  22.440  1.00 75.20           C  
ANISOU 3534  C   ILE B 152     5115  13638   9818    188    -12   3228       C  
ATOM   3535  O   ILE B 152      16.051   7.777  21.696  1.00 79.03           O  
ANISOU 3535  O   ILE B 152     5679  14253  10096    162    -83   3331       O  
ATOM   3536  CB  ILE B 152      12.768   7.304  21.646  1.00 70.49           C  
ANISOU 3536  CB  ILE B 152     4139  13515   9128    144   -146   3292       C  
ATOM   3537  CG1 ILE B 152      11.727   6.185  21.640  1.00 75.89           C  
ANISOU 3537  CG1 ILE B 152     4779  14453   9603     -4   -168   3067       C  
ATOM   3538  CG2 ILE B 152      13.242   7.586  20.233  1.00 78.79           C  
ANISOU 3538  CG2 ILE B 152     5079  14868   9990    161   -314   3634       C  
ATOM   3539  CD1 ILE B 152      10.547   6.450  20.717  1.00 72.85           C  
ANISOU 3539  CD1 ILE B 152     4036  14412   9232     14   -326   3326       C  
ATOM   3540  N   TYR B 153      14.969   9.058  23.199  1.00 69.49           N  
ANISOU 3540  N   TYR B 153     4342  12580   9480    281    116   3258       N  
ATOM   3541  CA  TYR B 153      15.986  10.103  23.169  1.00 67.42           C  
ANISOU 3541  CA  TYR B 153     4111  12100   9406    348    170   3416       C  
ATOM   3542  C   TYR B 153      17.327   9.582  23.665  1.00 67.07           C  
ANISOU 3542  C   TYR B 153     4337  11991   9155    234    179   3211       C  
ATOM   3543  O   TYR B 153      18.362   9.842  23.051  1.00 69.07           O  
ANISOU 3543  O   TYR B 153     4618  12283   9344    248    132   3364       O  
ATOM   3544  CB  TYR B 153      15.532  11.301  24.003  1.00 68.93           C  
ANISOU 3544  CB  TYR B 153     4216  11908  10064    425    374   3415       C  
ATOM   3545  CG  TYR B 153      16.660  12.206  24.456  1.00 68.87           C  
ANISOU 3545  CG  TYR B 153     4331  11602  10235    401    504   3397       C  
ATOM   3546  CD1 TYR B 153      17.288  13.070  23.568  1.00 70.22           C  
ANISOU 3546  CD1 TYR B 153     4403  11752  10526    500    489   3719       C  
ATOM   3547  CD2 TYR B 153      17.093  12.198  25.779  1.00 67.81           C  
ANISOU 3547  CD2 TYR B 153     4408  11227  10129    251    647   3055       C  
ATOM   3548  CE1 TYR B 153      18.313  13.901  23.983  1.00 75.37           C  
ANISOU 3548  CE1 TYR B 153     5157  12130  11349    450    629   3676       C  
ATOM   3549  CE2 TYR B 153      18.119  13.022  26.203  1.00 68.16           C  
ANISOU 3549  CE2 TYR B 153     4548  11040  10310    179    761   3011       C  
ATOM   3550  CZ  TYR B 153      18.726  13.870  25.302  1.00 77.53           C  
ANISOU 3550  CZ  TYR B 153     5627  12190  11642    278    760   3310       C  
ATOM   3551  OH  TYR B 153      19.749  14.692  25.721  1.00 76.46           O  
ANISOU 3551  OH  TYR B 153     5578  11823  11650    179    894   3242       O  
ATOM   3552  N   LEU B 154      17.331   8.855  24.786  1.00 63.35           N  
ANISOU 3552  N   LEU B 154     4054  11428   8587    123    243   2889       N  
ATOM   3553  CA  LEU B 154      18.588   8.339  25.318  1.00 74.70           C  
ANISOU 3553  CA  LEU B 154     5709  12831   9840     28    234   2745       C  
ATOM   3554  C   LEU B 154      19.214   7.321  24.375  1.00 78.57           C  
ANISOU 3554  C   LEU B 154     6248  13586  10017     16    126   2813       C  
ATOM   3555  O   LEU B 154      20.434   7.334  24.158  1.00 86.06           O  
ANISOU 3555  O   LEU B 154     7259  14537  10904      9    100   2881       O  
ATOM   3556  CB  LEU B 154      18.374   7.727  26.700  1.00 68.45           C  
ANISOU 3556  CB  LEU B 154     5100  11923   8985    -88    316   2435       C  
ATOM   3557  CG  LEU B 154      18.122   8.716  27.840  1.00 73.43           C  
ANISOU 3557  CG  LEU B 154     5755  12260   9883   -149    471   2295       C  
ATOM   3558  CD1 LEU B 154      18.111   7.993  29.176  1.00 78.60           C  
ANISOU 3558  CD1 LEU B 154     6628  12860  10377   -303    530   2002       C  
ATOM   3559  CD2 LEU B 154      19.166   9.820  27.842  1.00 65.77           C  
ANISOU 3559  CD2 LEU B 154     4769  11142   9077   -164    502   2394       C  
ATOM   3560  N   ASP B 155      18.396   6.438  23.796  1.00 70.68           N  
ANISOU 3560  N   ASP B 155     5214  12809   8832     -5     89   2782       N  
ATOM   3561  CA  ASP B 155      18.923   5.476  22.833  1.00 74.42           C  
ANISOU 3561  CA  ASP B 155     5742  13520   9014    -53     45   2813       C  
ATOM   3562  C   ASP B 155      19.560   6.191  21.645  1.00 81.60           C  
ANISOU 3562  C   ASP B 155     6542  14538   9924     -1    -24   3098       C  
ATOM   3563  O   ASP B 155      20.715   5.914  21.281  1.00 89.79           O  
ANISOU 3563  O   ASP B 155     7667  15593  10857    -20     -9   3132       O  
ATOM   3564  CB  ASP B 155      17.807   4.536  22.378  1.00 74.87           C  
ANISOU 3564  CB  ASP B 155     5762  13809   8876   -134     41   2705       C  
ATOM   3565  CG  ASP B 155      18.334   3.275  21.721  1.00 72.92           C  
ANISOU 3565  CG  ASP B 155     5646  13736   8324   -241     91   2610       C  
ATOM   3566  OD1 ASP B 155      19.559   3.177  21.498  1.00 76.08           O  
ANISOU 3566  OD1 ASP B 155     6136  14087   8686   -223    119   2671       O  
ATOM   3567  OD2 ASP B 155      17.517   2.372  21.440  1.00 74.81           O  
ANISOU 3567  OD2 ASP B 155     5893  14148   8384   -355    131   2458       O  
ATOM   3568  N   VAL B 156      18.822   7.126  21.033  1.00 63.18           N  
ANISOU 3568  N   VAL B 156     4004  12273   7728     73    -87   3329       N  
ATOM   3569  CA  VAL B 156      19.342   7.847  19.875  1.00 72.36           C  
ANISOU 3569  CA  VAL B 156     5061  13550   8881    123   -149   3642       C  
ATOM   3570  C   VAL B 156      20.583   8.644  20.250  1.00 73.72           C  
ANISOU 3570  C   VAL B 156     5302  13459   9249    172    -83   3696       C  
ATOM   3571  O   VAL B 156      21.545   8.712  19.480  1.00 64.43           O  
ANISOU 3571  O   VAL B 156     4153  12354   7972    160    -89   3828       O  
ATOM   3572  CB  VAL B 156      18.251   8.748  19.266  1.00 78.26           C  
ANISOU 3572  CB  VAL B 156     5550  14405   9782    220   -227   3936       C  
ATOM   3573  CG1 VAL B 156      18.858   9.709  18.254  1.00 69.02           C  
ANISOU 3573  CG1 VAL B 156     4283  13278   8664    297   -265   4304       C  
ATOM   3574  CG2 VAL B 156      17.172   7.899  18.607  1.00 80.75           C  
ANISOU 3574  CG2 VAL B 156     5762  15096   9822    124   -333   3916       C  
ATOM   3575  N   LEU B 157      20.594   9.239  21.446  1.00 73.41           N  
ANISOU 3575  N   LEU B 157     5294  13120   9477    197      0   3571       N  
ATOM   3576  CA  LEU B 157      21.729  10.048  21.876  1.00 73.10           C  
ANISOU 3576  CA  LEU B 157     5305  12848   9622    196     70   3589       C  
ATOM   3577  C   LEU B 157      22.986   9.203  22.015  1.00 80.95           C  
ANISOU 3577  C   LEU B 157     6447  13899  10412    114     54   3464       C  
ATOM   3578  O   LEU B 157      24.053   9.572  21.511  1.00 88.03           O  
ANISOU 3578  O   LEU B 157     7334  14785  11327    116     63   3591       O  
ATOM   3579  CB  LEU B 157      21.408  10.743  23.200  1.00 64.11           C  
ANISOU 3579  CB  LEU B 157     4189  11408   8760    172    186   3416       C  
ATOM   3580  CG  LEU B 157      22.577  11.460  23.881  1.00 63.85           C  
ANISOU 3580  CG  LEU B 157     4228  11157   8874     92    268   3341       C  
ATOM   3581  CD1 LEU B 157      23.042  12.635  23.039  1.00 67.56           C  
ANISOU 3581  CD1 LEU B 157     4582  11528   9559    167    327   3616       C  
ATOM   3582  CD2 LEU B 157      22.217  11.920  25.284  1.00 67.38           C  
ANISOU 3582  CD2 LEU B 157     4742  11354   9503     -8    398   3088       C  
ATOM   3583  N   PHE B 158      22.881   8.058  22.694  1.00 71.09           N  
ANISOU 3583  N   PHE B 158     5321  12699   8990     52     47   3235       N  
ATOM   3584  CA  PHE B 158      24.059   7.215  22.879  1.00 70.36           C  
ANISOU 3584  CA  PHE B 158     5337  12643   8752      6     49   3161       C  
ATOM   3585  C   PHE B 158      24.558   6.658  21.552  1.00 69.96           C  
ANISOU 3585  C   PHE B 158     5274  12782   8524     15     55   3291       C  
ATOM   3586  O   PHE B 158      25.769   6.654  21.290  1.00 70.34           O  
ANISOU 3586  O   PHE B 158     5327  12816   8582     13     81   3360       O  
ATOM   3587  CB  PHE B 158      23.748   6.087  23.859  1.00 75.72           C  
ANISOU 3587  CB  PHE B 158     6148  13319   9302    -43     66   2937       C  
ATOM   3588  CG  PHE B 158      23.426   6.567  25.244  1.00 87.97           C  
ANISOU 3588  CG  PHE B 158     7747  14698  10981    -97     79   2785       C  
ATOM   3589  CD1 PHE B 158      23.886   7.798  25.689  1.00 87.80           C  
ANISOU 3589  CD1 PHE B 158     7676  14520  11165   -132     92   2813       C  
ATOM   3590  CD2 PHE B 158      22.653   5.797  26.097  1.00 87.97           C  
ANISOU 3590  CD2 PHE B 158     7853  14684  10887   -143    110   2594       C  
ATOM   3591  CE1 PHE B 158      23.589   8.247  26.960  1.00 86.44           C  
ANISOU 3591  CE1 PHE B 158     7566  14193  11084   -234    141   2634       C  
ATOM   3592  CE2 PHE B 158      22.350   6.242  27.368  1.00 89.66           C  
ANISOU 3592  CE2 PHE B 158     8131  14748  11187   -227    145   2437       C  
ATOM   3593  CZ  PHE B 158      22.819   7.469  27.800  1.00 89.54           C  
ANISOU 3593  CZ  PHE B 158     8072  14590  11359   -283    163   2447       C  
ATOM   3594  N   SER B 159      23.642   6.211  20.687  1.00 72.48           N  
ANISOU 3594  N   SER B 159     5567  13297   8677      0     44   3318       N  
ATOM   3595  CA  SER B 159      24.068   5.664  19.402  1.00 68.35           C  
ANISOU 3595  CA  SER B 159     5054  12976   7939    -49     79   3404       C  
ATOM   3596  C   SER B 159      24.674   6.743  18.506  1.00 75.03           C  
ANISOU 3596  C   SER B 159     5805  13839   8864    -12     58   3668       C  
ATOM   3597  O   SER B 159      25.660   6.492  17.798  1.00 87.39           O  
ANISOU 3597  O   SER B 159     7405  15457  10342    -48    129   3724       O  
ATOM   3598  CB  SER B 159      22.887   4.983  18.719  1.00 77.31           C  
ANISOU 3598  CB  SER B 159     6174  14361   8838   -131     63   3349       C  
ATOM   3599  OG  SER B 159      22.407   3.899  19.495  1.00 83.05           O  
ANISOU 3599  OG  SER B 159     7008  15053   9493   -179    126   3090       O  
ATOM   3600  N   THR B 160      24.101   7.950  18.523  1.00 70.41           N  
ANISOU 3600  N   THR B 160     5097  13185   8470     61     -5   3840       N  
ATOM   3601  CA  THR B 160      24.637   9.048  17.729  1.00 70.31           C  
ANISOU 3601  CA  THR B 160     4998  13149   8567    108      1   4120       C  
ATOM   3602  C   THR B 160      26.008   9.469  18.238  1.00 68.49           C  
ANISOU 3602  C   THR B 160     4809  12696   8518    110     78   4086       C  
ATOM   3603  O   THR B 160      26.916   9.746  17.443  1.00 77.18           O  
ANISOU 3603  O   THR B 160     5901  13824   9598     95    128   4230       O  
ATOM   3604  CB  THR B 160      23.660  10.225  17.751  1.00 73.69           C  
ANISOU 3604  CB  THR B 160     5273  13499   9226    211    -40   4327       C  
ATOM   3605  OG1 THR B 160      22.363   9.775  17.339  1.00 79.96           O  
ANISOU 3605  OG1 THR B 160     5985  14539   9855    202   -135   4364       O  
ATOM   3606  CG2 THR B 160      24.116  11.329  16.818  1.00 71.99           C  
ANISOU 3606  CG2 THR B 160     4970  13266   9119    270    -15   4668       C  
ATOM   3607  N   ALA B 161      26.177   9.522  19.562  1.00 66.44           N  
ANISOU 3607  N   ALA B 161     4587  12237   8419    103     88   3892       N  
ATOM   3608  CA  ALA B 161      27.494   9.784  20.125  1.00 66.24           C  
ANISOU 3608  CA  ALA B 161     4579  12066   8522     63    131   3837       C  
ATOM   3609  C   ALA B 161      28.495   8.734  19.666  1.00 64.59           C  
ANISOU 3609  C   ALA B 161     4419  11984   8140     33    162   3809       C  
ATOM   3610  O   ALA B 161      29.625   9.068  19.295  1.00 62.91           O  
ANISOU 3610  O   ALA B 161     4164  11736   8003     17    215   3899       O  
ATOM   3611  CB  ALA B 161      27.416   9.827  21.652  1.00 62.01           C  
ANISOU 3611  CB  ALA B 161     4087  11377   8099     12    115   3617       C  
ATOM   3612  N   LYS B 162      28.089   7.462  19.658  1.00 61.37           N  
ANISOU 3612  N   LYS B 162     4091  11701   7526     21    166   3683       N  
ATOM   3613  CA  LYS B 162      28.980   6.404  19.189  1.00 65.80           C  
ANISOU 3613  CA  LYS B 162     4697  12338   7964      0    261   3654       C  
ATOM   3614  C   LYS B 162      29.408   6.635  17.745  1.00 72.18           C  
ANISOU 3614  C   LYS B 162     5482  13258   8685    -29    344   3816       C  
ATOM   3615  O   LYS B 162      30.606   6.614  17.426  1.00 81.72           O  
ANISOU 3615  O   LYS B 162     6663  14425   9964    -35    437   3871       O  
ATOM   3616  CB  LYS B 162      28.300   5.043  19.324  1.00 71.19           C  
ANISOU 3616  CB  LYS B 162     5484  13107   8457    -22    308   3486       C  
ATOM   3617  CG  LYS B 162      28.135   4.538  20.747  1.00 68.55           C  
ANISOU 3617  CG  LYS B 162     5200  12666   8179      0    266   3335       C  
ATOM   3618  CD  LYS B 162      27.616   3.111  20.722  1.00 70.22           C  
ANISOU 3618  CD  LYS B 162     5525  12936   8220    -23    373   3186       C  
ATOM   3619  CE  LYS B 162      28.571   2.207  19.945  1.00 61.22           C  
ANISOU 3619  CE  LYS B 162     4410  11815   7036    -28    560   3208       C  
ATOM   3620  NZ  LYS B 162      28.064   0.812  19.808  1.00 62.50           N  
ANISOU 3620  NZ  LYS B 162     4695  11999   7052    -74    736   3043       N  
ATOM   3621  N   ILE B 163      28.436   6.827  16.851  1.00 66.66           N  
ANISOU 3621  N   ILE B 163     4784  12724   7820    -60    313   3904       N  
ATOM   3622  CA  ILE B 163      28.753   6.913  15.427  1.00 66.82           C  
ANISOU 3622  CA  ILE B 163     4808  12908   7671   -129    391   4056       C  
ATOM   3623  C   ILE B 163      29.597   8.151  15.134  1.00 67.36           C  
ANISOU 3623  C   ILE B 163     4798  12858   7938    -88    407   4269       C  
ATOM   3624  O   ILE B 163      30.534   8.103  14.323  1.00 67.21           O  
ANISOU 3624  O   ILE B 163     4794  12869   7873   -140    532   4340       O  
ATOM   3625  CB  ILE B 163      27.465   6.874  14.583  1.00 81.07           C  
ANISOU 3625  CB  ILE B 163     6604  14982   9216   -197    311   4134       C  
ATOM   3626  CG1 ILE B 163      27.803   6.806  13.095  1.00 83.19           C  
ANISOU 3626  CG1 ILE B 163     6905  15480   9224   -324    397   4270       C  
ATOM   3627  CG2 ILE B 163      26.575   8.067  14.870  1.00 77.90           C  
ANISOU 3627  CG2 ILE B 163     6080  14537   8984    -94    158   4323       C  
ATOM   3628  CD1 ILE B 163      28.367   5.484  12.668  1.00 86.05           C  
ANISOU 3628  CD1 ILE B 163     7397  15909   9388   -462    603   4047       C  
ATOM   3629  N   TRP B 164      29.311   9.272  15.806  1.00 70.25           N  
ANISOU 3629  N   TRP B 164     5085  13059   8548     -9    321   4354       N  
ATOM   3630  CA  TRP B 164      30.112  10.466  15.572  1.00 72.33           C  
ANISOU 3630  CA  TRP B 164     5281  13172   9028     12    378   4535       C  
ATOM   3631  C   TRP B 164      31.478  10.374  16.238  1.00 68.91           C  
ANISOU 3631  C   TRP B 164     4830  12584   8769    -14    448   4411       C  
ATOM   3632  O   TRP B 164      32.430  10.993  15.759  1.00 70.49           O  
ANISOU 3632  O   TRP B 164     4986  12714   9082    -38    543   4527       O  
ATOM   3633  CB  TRP B 164      29.376  11.715  16.056  1.00 81.41           C  
ANISOU 3633  CB  TRP B 164     6353  14156  10424     89    329   4654       C  
ATOM   3634  CG  TRP B 164      28.307  12.177  15.112  1.00 92.81           C  
ANISOU 3634  CG  TRP B 164     7743  15751  11771    142    276   4925       C  
ATOM   3635  CD1 TRP B 164      26.964  12.192  15.341  1.00 88.82           C  
ANISOU 3635  CD1 TRP B 164     7182  15311  11257    202    175   4954       C  
ATOM   3636  CD2 TRP B 164      28.490  12.666  13.775  1.00 96.20           C  
ANISOU 3636  CD2 TRP B 164     8149  16319  12086    134    312   5235       C  
ATOM   3637  NE1 TRP B 164      26.299  12.675  14.240  1.00 91.16           N  
ANISOU 3637  NE1 TRP B 164     7390  15795  11451    242    123   5289       N  
ATOM   3638  CE2 TRP B 164      27.212  12.971  13.263  1.00 94.75           C  
ANISOU 3638  CE2 TRP B 164     7876  16306  11818    196    201   5472       C  
ATOM   3639  CE3 TRP B 164      29.610  12.882  12.964  1.00 88.56           C  
ANISOU 3639  CE3 TRP B 164     7216  15356  11077     74    431   5347       C  
ATOM   3640  CZ2 TRP B 164      27.023  13.480  11.978  1.00 91.14           C  
ANISOU 3640  CZ2 TRP B 164     7367  16054  11208    196    181   5847       C  
ATOM   3641  CZ3 TRP B 164      29.419  13.387  11.688  1.00 85.99           C  
ANISOU 3641  CZ3 TRP B 164     6871  15206  10597     65    440   5687       C  
ATOM   3642  CH2 TRP B 164      28.136  13.680  11.209  1.00 84.69           C  
ANISOU 3642  CH2 TRP B 164     6620  15238  10321    124    303   5947       C  
ATOM   3643  N   HIS B 165      31.611   9.586  17.307  1.00 66.63           N  
ANISOU 3643  N   HIS B 165     4561  12261   8496    -17    403   4197       N  
ATOM   3644  CA  HIS B 165      32.935   9.311  17.851  1.00 68.88           C  
ANISOU 3644  CA  HIS B 165     4790  12473   8908    -43    445   4123       C  
ATOM   3645  C   HIS B 165      33.773   8.513  16.864  1.00 73.88           C  
ANISOU 3645  C   HIS B 165     5433  13198   9441    -57    591   4165       C  
ATOM   3646  O   HIS B 165      34.960   8.801  16.670  1.00 66.66           O  
ANISOU 3646  O   HIS B 165     4431  12225   8673    -79    678   4224       O  
ATOM   3647  CB  HIS B 165      32.814   8.562  19.178  1.00 67.92           C  
ANISOU 3647  CB  HIS B 165     4684  12335   8788    -36    352   3940       C  
ATOM   3648  CG  HIS B 165      32.686   9.459  20.369  1.00 76.23           C  
ANISOU 3648  CG  HIS B 165     5698  13263  10004    -85    257   3863       C  
ATOM   3649  ND1 HIS B 165      33.584  10.468  20.639  1.00 83.34           N  
ANISOU 3649  ND1 HIS B 165     6499  14061  11106   -161    277   3892       N  
ATOM   3650  CD2 HIS B 165      31.770   9.494  21.366  1.00 80.77           C  
ANISOU 3650  CD2 HIS B 165     6329  13794  10565   -101    175   3728       C  
ATOM   3651  CE1 HIS B 165      33.224  11.091  21.746  1.00 84.57           C  
ANISOU 3651  CE1 HIS B 165     6660  14120  11353   -241    219   3764       C  
ATOM   3652  NE2 HIS B 165      32.128  10.517  22.209  1.00 83.11           N  
ANISOU 3652  NE2 HIS B 165     6572  13965  11042   -200    160   3667       N  
ATOM   3653  N   LEU B 166      33.169   7.507  16.228  1.00 72.63           N  
ANISOU 3653  N   LEU B 166     5376  13178   9042    -67    650   4114       N  
ATOM   3654  CA  LEU B 166      33.894   6.742  15.217  1.00 66.55           C  
ANISOU 3654  CA  LEU B 166     4639  12475   8171   -115    854   4119       C  
ATOM   3655  C   LEU B 166      34.305   7.636  14.051  1.00 74.39           C  
ANISOU 3655  C   LEU B 166     5618  13504   9141   -173    940   4302       C  
ATOM   3656  O   LEU B 166      35.452   7.579  13.578  1.00 77.20           O  
ANISOU 3656  O   LEU B 166     5931  13810   9591   -202   1107   4337       O  
ATOM   3657  CB  LEU B 166      33.035   5.576  14.729  1.00 66.42           C  
ANISOU 3657  CB  LEU B 166     4756  12606   7876   -171    930   3992       C  
ATOM   3658  CG  LEU B 166      32.634   4.521  15.766  1.00 65.02           C  
ANISOU 3658  CG  LEU B 166     4618  12378   7708   -120    906   3812       C  
ATOM   3659  CD1 LEU B 166      31.791   3.424  15.127  1.00 67.18           C  
ANISOU 3659  CD1 LEU B 166     5030  12791   7704   -218   1033   3665       C  
ATOM   3660  CD2 LEU B 166      33.849   3.924  16.461  1.00 65.04           C  
ANISOU 3660  CD2 LEU B 166     4539  12234   7940    -40   1000   3795       C  
ATOM   3661  N   CYS B 167      33.380   8.480  13.586  1.00 73.47           N  
ANISOU 3661  N   CYS B 167     5526  13470   8921   -184    837   4444       N  
ATOM   3662  CA  CYS B 167      33.697   9.403  12.500  1.00 80.48           C  
ANISOU 3662  CA  CYS B 167     6406  14392   9780   -230    911   4672       C  
ATOM   3663  C   CYS B 167      34.818  10.360  12.890  1.00 71.51           C  
ANISOU 3663  C   CYS B 167     5163  13036   8972   -200    964   4741       C  
ATOM   3664  O   CYS B 167      35.708  10.648  12.079  1.00 73.36           O  
ANISOU 3664  O   CYS B 167     5389  13256   9230   -258   1124   4842       O  
ATOM   3665  CB  CYS B 167      32.444  10.180  12.098  1.00 87.07           C  
ANISOU 3665  CB  CYS B 167     7243  15343  10498   -208    769   4871       C  
ATOM   3666  SG  CYS B 167      32.716  11.388  10.793  1.00 94.37           S  
ANISOU 3666  SG  CYS B 167     8156  16316  11386   -242    847   5233       S  
ATOM   3667  N   ALA B 168      34.793  10.859  14.130  1.00 70.74           N  
ANISOU 3667  N   ALA B 168     4986  12774   9118   -143    848   4667       N  
ATOM   3668  CA  ALA B 168      35.832  11.772  14.589  1.00 73.02           C  
ANISOU 3668  CA  ALA B 168     5164  12875   9706   -165    897   4688       C  
ATOM   3669  C   ALA B 168      37.180  11.075  14.678  1.00 80.95           C  
ANISOU 3669  C   ALA B 168     6086  13875  10797   -200   1002   4595       C  
ATOM   3670  O   ALA B 168      38.208  11.666  14.337  1.00 83.25           O  
ANISOU 3670  O   ALA B 168     6293  14084  11252   -251   1124   4667       O  
ATOM   3671  CB  ALA B 168      35.450  12.365  15.943  1.00 71.49           C  
ANISOU 3671  CB  ALA B 168     4919  12539   9704   -153    766   4579       C  
ATOM   3672  N   ILE B 169      37.197   9.823  15.139  1.00 84.27           N  
ANISOU 3672  N   ILE B 169     6513  14369  11137   -166    975   4453       N  
ATOM   3673  CA  ILE B 169      38.440   9.055  15.163  1.00 78.93           C  
ANISOU 3673  CA  ILE B 169     5730  13682  10578   -164   1101   4412       C  
ATOM   3674  C   ILE B 169      39.016   8.949  13.760  1.00 81.26           C  
ANISOU 3674  C   ILE B 169     6065  14003  10807   -218   1349   4498       C  
ATOM   3675  O   ILE B 169      40.207   9.207  13.534  1.00 87.72           O  
ANISOU 3675  O   ILE B 169     6756  14751  11823   -248   1485   4544       O  
ATOM   3676  CB  ILE B 169      38.200   7.660  15.767  1.00 79.35           C  
ANISOU 3676  CB  ILE B 169     5806  13785  10556    -94   1076   4288       C  
ATOM   3677  CG1 ILE B 169      37.886   7.763  17.257  1.00 76.95           C  
ANISOU 3677  CG1 ILE B 169     5445  13462  10328    -64    843   4212       C  
ATOM   3678  CG2 ILE B 169      39.408   6.771  15.539  1.00 75.94           C  
ANISOU 3678  CG2 ILE B 169     5261  13326  10269    -63   1275   4295       C  
ATOM   3679  CD1 ILE B 169      37.539   6.437  17.897  1.00 74.02           C  
ANISOU 3679  CD1 ILE B 169     5117  13130   9877     12    818   4121       C  
ATOM   3680  N   SER B 170      38.177   8.553  12.799  1.00 77.33           N  
ANISOU 3680  N   SER B 170     5739  13628  10014   -256   1419   4511       N  
ATOM   3681  CA  SER B 170      38.642   8.410  11.422  1.00 77.44           C  
ANISOU 3681  CA  SER B 170     5827  13703   9894   -356   1671   4572       C  
ATOM   3682  C   SER B 170      39.214   9.725  10.895  1.00 77.44           C  
ANISOU 3682  C   SER B 170     5778  13631  10014   -402   1722   4755       C  
ATOM   3683  O   SER B 170      40.351   9.774  10.399  1.00 82.58           O  
ANISOU 3683  O   SER B 170     6363  14212  10800   -453   1937   4778       O  
ATOM   3684  CB  SER B 170      37.497   7.916  10.537  1.00 76.31           C  
ANISOU 3684  CB  SER B 170     5876  13767   9352   -442   1686   4559       C  
ATOM   3685  OG  SER B 170      37.976   7.453   9.287  1.00 79.46           O  
ANISOU 3685  OG  SER B 170     6371  14249   9570   -584   1969   4548       O  
ATOM   3686  N   LEU B 171      38.433  10.805  11.001  1.00 77.12           N  
ANISOU 3686  N   LEU B 171     5762  13584   9957   -380   1556   4894       N  
ATOM   3687  CA  LEU B 171      38.866  12.099  10.485  1.00 83.73           C  
ANISOU 3687  CA  LEU B 171     6572  14321  10922   -416   1635   5094       C  
ATOM   3688  C   LEU B 171      40.147  12.568  11.163  1.00 97.93           C  
ANISOU 3688  C   LEU B 171     8193  15926  13090   -427   1703   5030       C  
ATOM   3689  O   LEU B 171      41.054  13.091  10.502  1.00105.06           O  
ANISOU 3689  O   LEU B 171     9060  16756  14102   -498   1897   5120       O  
ATOM   3690  CB  LEU B 171      37.752  13.130  10.670  1.00 86.82           C  
ANISOU 3690  CB  LEU B 171     6991  14685  11311   -356   1468   5259       C  
ATOM   3691  CG  LEU B 171      38.032  14.567  10.223  1.00 85.40           C  
ANISOU 3691  CG  LEU B 171     6788  14351  11307   -368   1567   5502       C  
ATOM   3692  CD1 LEU B 171      38.385  14.617   8.743  1.00 89.67           C  
ANISOU 3692  CD1 LEU B 171     7426  15016  11627   -459   1755   5699       C  
ATOM   3693  CD2 LEU B 171      36.836  15.459  10.519  1.00 82.01           C  
ANISOU 3693  CD2 LEU B 171     6365  13860  10935   -272   1429   5670       C  
ATOM   3694  N   ASP B 172      40.241  12.387  12.482  1.00101.86           N  
ANISOU 3694  N   ASP B 172     8573  16364  13766   -381   1544   4876       N  
ATOM   3695  CA  ASP B 172      41.413  12.845  13.215  1.00107.01           C  
ANISOU 3695  CA  ASP B 172     9026  16895  14737   -430   1564   4812       C  
ATOM   3696  C   ASP B 172      42.657  12.087  12.782  1.00102.78           C  
ANISOU 3696  C   ASP B 172     8374  16385  14294   -451   1753   4784       C  
ATOM   3697  O   ASP B 172      43.706  12.690  12.540  1.00109.30           O  
ANISOU 3697  O   ASP B 172     9103  17103  15322   -520   1880   4800       O  
ATOM   3698  CB  ASP B 172      41.186  12.691  14.719  1.00109.82           C  
ANISOU 3698  CB  ASP B 172     9289  17250  15186   -408   1333   4659       C  
ATOM   3699  CG  ASP B 172      42.339  13.240  15.540  1.00114.35           C  
ANISOU 3699  CG  ASP B 172     9639  17762  16045   -511   1315   4589       C  
ATOM   3700  OD1 ASP B 172      42.396  14.472  15.732  1.00118.08           O  
ANISOU 3700  OD1 ASP B 172    10094  18104  16668   -610   1342   4593       O  
ATOM   3701  OD2 ASP B 172      43.188  12.442  15.992  1.00112.40           O  
ANISOU 3701  OD2 ASP B 172     9225  17599  15884   -499   1285   4535       O  
ATOM   3702  N   ARG B 173      42.561  10.758  12.676  1.00 92.39           N  
ANISOU 3702  N   ARG B 173     7098  15157  12848   -386   1788   4706       N  
ATOM   3703  CA  ARG B 173      43.729   9.984  12.273  1.00 87.41           C  
ANISOU 3703  CA  ARG B 173     6410  14461  12340   -373   1983   4633       C  
ATOM   3704  C   ARG B 173      44.169  10.346  10.861  1.00 90.58           C  
ANISOU 3704  C   ARG B 173     6927  14814  12674   -466   2254   4692       C  
ATOM   3705  O   ARG B 173      45.373  10.463  10.589  1.00 94.78           O  
ANISOU 3705  O   ARG B 173     7356  15232  13422   -497   2418   4663       O  
ATOM   3706  CB  ARG B 173      43.441   8.486  12.384  1.00 85.50           C  
ANISOU 3706  CB  ARG B 173     6224  14270  11994   -284   2027   4532       C  
ATOM   3707  CG  ARG B 173      43.308   7.994  13.818  1.00 86.82           C  
ANISOU 3707  CG  ARG B 173     6260  14462  12266   -183   1787   4484       C  
ATOM   3708  CD  ARG B 173      43.055   6.495  13.886  1.00 92.56           C  
ANISOU 3708  CD  ARG B 173     7048  15196  12926    -86   1885   4408       C  
ATOM   3709  NE  ARG B 173      44.135   5.721  13.280  1.00108.23           N  
ANISOU 3709  NE  ARG B 173     8987  17052  15085    -52   2173   4375       N  
ATOM   3710  CZ  ARG B 173      45.208   5.288  13.938  1.00114.72           C  
ANISOU 3710  CZ  ARG B 173     9595  17785  16207     50   2164   4404       C  
ATOM   3711  NH1 ARG B 173      46.143   4.590  13.305  1.00115.24           N  
ANISOU 3711  NH1 ARG B 173     9618  17708  16461     88   2465   4378       N  
ATOM   3712  NH2 ARG B 173      45.347   5.550  15.232  1.00113.03           N  
ANISOU 3712  NH2 ARG B 173     9216  17633  16097     99   1857   4460       N  
ATOM   3713  N   TYR B 174      43.211  10.558   9.952  1.00 87.97           N  
ANISOU 3713  N   TYR B 174     6808  14585  12031   -522   2295   4783       N  
ATOM   3714  CA  TYR B 174      43.582  10.939   8.590  1.00 93.39           C  
ANISOU 3714  CA  TYR B 174     7636  15253  12595   -634   2535   4853       C  
ATOM   3715  C   TYR B 174      44.278  12.295   8.558  1.00 96.02           C  
ANISOU 3715  C   TYR B 174     7876  15443  13163   -678   2570   4972       C  
ATOM   3716  O   TYR B 174      45.364  12.435   7.979  1.00 93.53           O  
ANISOU 3716  O   TYR B 174     7534  15017  12985   -745   2794   4938       O  
ATOM   3717  CB  TYR B 174      42.359  10.956   7.682  1.00 92.61           C  
ANISOU 3717  CB  TYR B 174     7773  15342  12074   -699   2508   4957       C  
ATOM   3718  CG  TYR B 174      42.687  11.405   6.278  1.00101.98           C  
ANISOU 3718  CG  TYR B 174     9126  16542  13079   -836   2723   5048       C  
ATOM   3719  CD1 TYR B 174      43.413  10.591   5.420  1.00104.17           C  
ANISOU 3719  CD1 TYR B 174     9505  16799  13278   -948   3017   4882       C  
ATOM   3720  CD2 TYR B 174      42.280  12.651   5.814  1.00108.29           C  
ANISOU 3720  CD2 TYR B 174     9986  17356  13804   -858   2658   5304       C  
ATOM   3721  CE1 TYR B 174      43.721  11.002   4.135  1.00112.99           C  
ANISOU 3721  CE1 TYR B 174    10792  17937  14201  -1105   3226   4948       C  
ATOM   3722  CE2 TYR B 174      42.580  13.069   4.531  1.00113.09           C  
ANISOU 3722  CE2 TYR B 174    10758  17987  14226   -986   2845   5407       C  
ATOM   3723  CZ  TYR B 174      43.300  12.241   3.696  1.00117.49           C  
ANISOU 3723  CZ  TYR B 174    11427  18551  14664  -1123   3122   5218       C  
ATOM   3724  OH  TYR B 174      43.601  12.656   2.418  1.00124.40           O  
ANISOU 3724  OH  TYR B 174    12484  19457  15326  -1281   3321   5305       O  
ATOM   3725  N   VAL B 175      43.647  13.317   9.145  1.00 95.06           N  
ANISOU 3725  N   VAL B 175     7713  15301  13105   -655   2389   5100       N  
ATOM   3726  CA  VAL B 175      44.244  14.651   9.161  1.00 95.26           C  
ANISOU 3726  CA  VAL B 175     7664  15152  13379   -714   2461   5195       C  
ATOM   3727  C   VAL B 175      45.597  14.630   9.863  1.00 87.63           C  
ANISOU 3727  C   VAL B 175     6472  14067  12757   -749   2501   5024       C  
ATOM   3728  O   VAL B 175      46.501  15.397   9.511  1.00 88.10           O  
ANISOU 3728  O   VAL B 175     6481  13987  13006   -837   2668   5038       O  
ATOM   3729  CB  VAL B 175      43.275  15.660   9.813  1.00 97.86           C  
ANISOU 3729  CB  VAL B 175     7980  15436  13767   -682   2297   5328       C  
ATOM   3730  CG1 VAL B 175      43.925  17.035   9.947  1.00 92.51           C  
ANISOU 3730  CG1 VAL B 175     7225  14527  13398   -762   2418   5383       C  
ATOM   3731  CG2 VAL B 175      41.984  15.758   9.007  1.00 91.27           C  
ANISOU 3731  CG2 VAL B 175     7339  14733  12607   -637   2252   5551       C  
ATOM   3732  N   ALA B 176      45.766  13.751  10.853  1.00 85.94           N  
ANISOU 3732  N   ALA B 176     6116  13917  12622   -683   2343   4872       N  
ATOM   3733  CA  ALA B 176      47.040  13.662  11.555  1.00 86.54           C  
ANISOU 3733  CA  ALA B 176     5951  13932  12997   -711   2331   4740       C  
ATOM   3734  C   ALA B 176      48.129  13.087  10.657  1.00 97.96           C  
ANISOU 3734  C   ALA B 176     7377  15321  14523   -722   2597   4698       C  
ATOM   3735  O   ALA B 176      49.217  13.664  10.543  1.00106.86           O  
ANISOU 3735  O   ALA B 176     8370  16346  15885   -808   2718   4667       O  
ATOM   3736  CB  ALA B 176      46.882  12.823  12.823  1.00 83.99           C  
ANISOU 3736  CB  ALA B 176     5498  13715  12701   -625   2075   4638       C  
ATOM   3737  N   ILE B 177      47.861  11.947  10.010  1.00100.65           N  
ANISOU 3737  N   ILE B 177     7849  15713  14680   -656   2719   4673       N  
ATOM   3738  CA  ILE B 177      48.910  11.337   9.197  1.00106.77           C  
ANISOU 3738  CA  ILE B 177     8604  16402  15562   -677   3018   4598       C  
ATOM   3739  C   ILE B 177      49.180  12.114   7.912  1.00118.25           C  
ANISOU 3739  C   ILE B 177    10217  17783  16928   -816   3283   4658       C  
ATOM   3740  O   ILE B 177      50.283  12.013   7.359  1.00118.85           O  
ANISOU 3740  O   ILE B 177    10229  17752  17176   -873   3535   4589       O  
ATOM   3741  CB  ILE B 177      48.586   9.869   8.856  1.00107.44           C  
ANISOU 3741  CB  ILE B 177     8800  16523  15498   -602   3143   4510       C  
ATOM   3742  CG1 ILE B 177      47.453   9.785   7.834  1.00114.88           C  
ANISOU 3742  CG1 ILE B 177    10059  17570  16020   -685   3232   4541       C  
ATOM   3743  CG2 ILE B 177      48.242   9.087  10.117  1.00104.80           C  
ANISOU 3743  CG2 ILE B 177     8335  16249  15235   -454   2889   4482       C  
ATOM   3744  CD1 ILE B 177      47.314   8.419   7.202  1.00119.96           C  
ANISOU 3744  CD1 ILE B 177    10850  18221  16507   -700   3472   4392       C  
ATOM   3745  N   GLN B 178      48.215  12.895   7.416  1.00119.00           N  
ANISOU 3745  N   GLN B 178    10515  17933  16765   -870   3237   4802       N  
ATOM   3746  CA  GLN B 178      48.504  13.725   6.250  1.00121.74           C  
ANISOU 3746  CA  GLN B 178    11015  18211  17030   -999   3471   4901       C  
ATOM   3747  C   GLN B 178      49.339  14.942   6.621  1.00124.54           C  
ANISOU 3747  C   GLN B 178    11203  18404  17711  -1058   3495   4932       C  
ATOM   3748  O   GLN B 178      50.275  15.299   5.897  1.00129.10           O  
ANISOU 3748  O   GLN B 178    11786  18870  18398  -1160   3753   4911       O  
ATOM   3749  CB  GLN B 178      47.209  14.149   5.560  1.00124.63           C  
ANISOU 3749  CB  GLN B 178    11642  18703  17009  -1023   3400   5093       C  
ATOM   3750  CG  GLN B 178      46.551  13.033   4.761  1.00124.72           C  
ANISOU 3750  CG  GLN B 178    11869  18891  16628  -1062   3470   5031       C  
ATOM   3751  CD  GLN B 178      47.481  12.429   3.724  1.00118.82           C  
ANISOU 3751  CD  GLN B 178    11216  18089  15842  -1196   3833   4882       C  
ATOM   3752  OE1 GLN B 178      48.204  11.472   4.004  1.00117.30           O  
ANISOU 3752  OE1 GLN B 178    10904  17818  15846  -1165   3966   4681       O  
ATOM   3753  NE2 GLN B 178      47.462  12.985   2.518  1.00116.42           N  
ANISOU 3753  NE2 GLN B 178    11127  17817  15290  -1348   4006   4989       N  
ATOM   3754  N   ASN B 179      49.006  15.602   7.733  1.00126.95           N  
ANISOU 3754  N   ASN B 179    11372  18692  18170  -1023   3255   4958       N  
ATOM   3755  CA  ASN B 179      49.700  16.801   8.196  1.00130.62           C  
ANISOU 3755  CA  ASN B 179    11688  19003  18940  -1121   3283   4945       C  
ATOM   3756  C   ASN B 179      50.324  16.474   9.549  1.00130.75           C  
ANISOU 3756  C   ASN B 179    11407  19061  19211  -1114   3082   4766       C  
ATOM   3757  O   ASN B 179      49.748  16.790  10.602  1.00133.60           O  
ANISOU 3757  O   ASN B 179    11698  19462  19602  -1109   2846   4744       O  
ATOM   3758  CB  ASN B 179      48.741  17.988   8.289  1.00127.75           C  
ANISOU 3758  CB  ASN B 179    11445  18563  18532  -1134   3221   5119       C  
ATOM   3759  CG  ASN B 179      49.433  19.276   8.697  1.00126.42           C  
ANISOU 3759  CG  ASN B 179    11156  18191  18688  -1270   3322   5079       C  
ATOM   3760  OD1 ASN B 179      50.662  19.351   8.741  1.00126.58           O  
ANISOU 3760  OD1 ASN B 179    11014  18153  18928  -1374   3445   4933       O  
ATOM   3761  ND2 ASN B 179      48.642  20.300   9.000  1.00125.42           N  
ANISOU 3761  ND2 ASN B 179    11100  17943  18609  -1277   3292   5198       N  
ATOM   3762  N   PRO B 180      51.512  15.848   9.563  1.00133.08           N  
ANISOU 3762  N   PRO B 180    11518  19358  19689  -1122   3169   4641       N  
ATOM   3763  CA  PRO B 180      52.127  15.356  10.801  1.00131.36           C  
ANISOU 3763  CA  PRO B 180    11008  19233  19670  -1095   2945   4514       C  
ATOM   3764  C   PRO B 180      52.401  16.470  11.809  1.00129.41           C  
ANISOU 3764  C   PRO B 180    10586  18978  19605  -1253   2797   4437       C  
ATOM   3765  O   PRO B 180      52.265  16.239  13.010  1.00125.67           O  
ANISOU 3765  O   PRO B 180     9963  18636  19149  -1251   2517   4365       O  
ATOM   3766  CB  PRO B 180      53.433  14.723  10.313  1.00137.63           C  
ANISOU 3766  CB  PRO B 180    11647  19987  20659  -1086   3151   4446       C  
ATOM   3767  CG  PRO B 180      53.146  14.326   8.906  1.00138.38           C  
ANISOU 3767  CG  PRO B 180    12011  20011  20557  -1060   3446   4503       C  
ATOM   3768  CD  PRO B 180      52.267  15.419   8.372  1.00135.86           C  
ANISOU 3768  CD  PRO B 180    11937  19643  20040  -1143   3485   4628       C  
ATOM   3769  N   SER B 188      47.731  17.777  23.742  1.00110.90           N  
ANISOU 3769  N   SER B 188     7768  17877  16491  -2361    533   3384       N  
ATOM   3770  CA  SER B 188      47.084  16.778  22.901  1.00107.84           C  
ANISOU 3770  CA  SER B 188     7547  17406  16022  -1964    545   3605       C  
ATOM   3771  C   SER B 188      45.978  16.055  23.662  1.00111.03           C  
ANISOU 3771  C   SER B 188     8077  17923  16186  -1872    345   3605       C  
ATOM   3772  O   SER B 188      44.968  15.659  23.077  1.00101.25           O  
ANISOU 3772  O   SER B 188     7045  16553  14873  -1635    413   3707       O  
ATOM   3773  CB  SER B 188      48.108  15.769  22.378  1.00110.10           C  
ANISOU 3773  CB  SER B 188     7716  17778  16338  -1752    494   3746       C  
ATOM   3774  OG  SER B 188      47.474  14.729  21.654  1.00105.94           O  
ANISOU 3774  OG  SER B 188     7359  17183  15711  -1422    527   3914       O  
ATOM   3775  N   ARG B 189      46.174  15.888  24.973  1.00119.36           N  
ANISOU 3775  N   ARG B 189     9027  19231  17093  -2075     97   3476       N  
ATOM   3776  CA  ARG B 189      45.151  15.245  25.793  1.00124.65           C  
ANISOU 3776  CA  ARG B 189     9819  20017  17525  -2026    -83   3460       C  
ATOM   3777  C   ARG B 189      43.972  16.178  26.038  1.00133.19           C  
ANISOU 3777  C   ARG B 189    11195  20837  18573  -2141     61   3239       C  
ATOM   3778  O   ARG B 189      42.809  15.767  25.921  1.00137.15           O  
ANISOU 3778  O   ARG B 189    11932  21215  18963  -1936     71   3262       O  
ATOM   3779  CB  ARG B 189      45.753  14.804  27.126  1.00126.65           C  
ANISOU 3779  CB  ARG B 189     9929  20609  17582  -2211   -390   3391       C  
ATOM   3780  CG  ARG B 189      44.716  14.624  28.222  1.00128.80           C  
ANISOU 3780  CG  ARG B 189    10325  21011  17604  -2337   -538   3282       C  
ATOM   3781  CD  ARG B 189      45.349  14.364  29.576  1.00135.02           C  
ANISOU 3781  CD  ARG B 189    10982  22165  18156  -2590   -837   3211       C  
ATOM   3782  NE  ARG B 189      44.382  14.563  30.652  1.00140.62           N  
ANISOU 3782  NE  ARG B 189    11841  22968  18620  -2835   -914   3015       N  
ATOM   3783  CZ  ARG B 189      44.556  14.160  31.906  1.00145.09           C  
ANISOU 3783  CZ  ARG B 189    12354  23886  18888  -3044  -1188   2981       C  
ATOM   3784  NH1 ARG B 189      43.615  14.390  32.812  1.00146.47           N  
ANISOU 3784  NH1 ARG B 189    12748  24073  18830  -3265  -1199   2753       N  
ATOM   3785  NH2 ARG B 189      45.669  13.531  32.257  1.00145.27           N  
ANISOU 3785  NH2 ARG B 189    12204  24163  18829  -2990  -1418   3153       N  
ATOM   3786  N   THR B 190      44.252  17.442  26.368  1.00132.03           N  
ANISOU 3786  N   THR B 190    11031  20586  18549  -2472    205   3016       N  
ATOM   3787  CA  THR B 190      43.172  18.384  26.636  1.00124.58           C  
ANISOU 3787  CA  THR B 190    10351  19343  17642  -2583    404   2803       C  
ATOM   3788  C   THR B 190      42.368  18.658  25.373  1.00116.97           C  
ANISOU 3788  C   THR B 190     9581  18022  16841  -2271    646   2971       C  
ATOM   3789  O   THR B 190      41.136  18.743  25.422  1.00127.15           O  
ANISOU 3789  O   THR B 190    11089  19127  18097  -2150    712   2945       O  
ATOM   3790  CB  THR B 190      43.731  19.680  27.222  1.00123.93           C  
ANISOU 3790  CB  THR B 190    10202  19193  17692  -3030    570   2514       C  
ATOM   3791  OG1 THR B 190      44.371  19.399  28.473  1.00125.97           O  
ANISOU 3791  OG1 THR B 190    10284  19855  17725  -3364    305   2353       O  
ATOM   3792  CG2 THR B 190      42.615  20.686  27.454  1.00121.02           C  
ANISOU 3792  CG2 THR B 190    10104  18444  17436  -3128    855   2300       C  
ATOM   3793  N   LYS B 191      43.046  18.796  24.231  1.00103.20           N  
ANISOU 3793  N   LYS B 191     7746  16199  15267  -2147    778   3160       N  
ATOM   3794  CA  LYS B 191      42.331  19.011  22.978  1.00 97.55           C  
ANISOU 3794  CA  LYS B 191     7202  15212  14651  -1867    979   3365       C  
ATOM   3795  C   LYS B 191      41.460  17.809  22.636  1.00103.25           C  
ANISOU 3795  C   LYS B 191     8042  16036  15153  -1551    822   3526       C  
ATOM   3796  O   LYS B 191      40.351  17.964  22.111  1.00106.53           O  
ANISOU 3796  O   LYS B 191     8641  16275  15560  -1374    912   3618       O  
ATOM   3797  CB  LYS B 191      43.321  19.308  21.852  1.00 98.27           C  
ANISOU 3797  CB  LYS B 191     7177  15242  14920  -1832   1148   3532       C  
ATOM   3798  CG  LYS B 191      42.687  19.938  20.619  1.00 95.80           C  
ANISOU 3798  CG  LYS B 191     7038  14631  14730  -1643   1404   3736       C  
ATOM   3799  CD  LYS B 191      43.569  21.039  20.034  1.00 93.62           C  
ANISOU 3799  CD  LYS B 191     6687  14155  14727  -1797   1687   3759       C  
ATOM   3800  CE  LYS B 191      44.904  20.501  19.546  1.00 88.19           C  
ANISOU 3800  CE  LYS B 191     5787  13665  14055  -1820   1656   3831       C  
ATOM   3801  NZ  LYS B 191      45.727  21.575  18.923  1.00 90.98           N  
ANISOU 3801  NZ  LYS B 191     6080  13811  14679  -1973   1957   3852       N  
ATOM   3802  N   ALA B 192      41.938  16.599  22.942  1.00102.78           N  
ANISOU 3802  N   ALA B 192     7863  16263  14927  -1484    597   3571       N  
ATOM   3803  CA  ALA B 192      41.127  15.406  22.718  1.00 92.23           C  
ANISOU 3803  CA  ALA B 192     6645  15012  13387  -1222    479   3682       C  
ATOM   3804  C   ALA B 192      39.892  15.405  23.609  1.00 82.04           C  
ANISOU 3804  C   ALA B 192     5527  13681  11963  -1244    396   3533       C  
ATOM   3805  O   ALA B 192      38.790  15.078  23.151  1.00 85.53           O  
ANISOU 3805  O   ALA B 192     6136  14041  12320  -1049    421   3602       O  
ATOM   3806  CB  ALA B 192      41.959  14.147  22.957  1.00 93.36           C  
ANISOU 3806  CB  ALA B 192     6609  15425  13439  -1151    306   3768       C  
ATOM   3807  N   PHE B 193      40.059  15.760  24.886  1.00 83.22           N  
ANISOU 3807  N   PHE B 193     5633  13909  12079  -1504    303   3319       N  
ATOM   3808  CA  PHE B 193      38.905  15.847  25.777  1.00 93.31           C  
ANISOU 3808  CA  PHE B 193     7085  15124  13244  -1563    271   3144       C  
ATOM   3809  C   PHE B 193      37.907  16.888  25.281  1.00 92.81           C  
ANISOU 3809  C   PHE B 193     7182  14716  13364  -1514    521   3123       C  
ATOM   3810  O   PHE B 193      36.689  16.678  25.349  1.00 86.52           O  
ANISOU 3810  O   PHE B 193     6537  13828  12508  -1380    530   3116       O  
ATOM   3811  CB  PHE B 193      39.360  16.174  27.201  1.00104.37           C  
ANISOU 3811  CB  PHE B 193     8417  16681  14557  -1920    164   2896       C  
ATOM   3812  CG  PHE B 193      40.040  15.028  27.907  1.00114.17           C  
ANISOU 3812  CG  PHE B 193     9509  18298  15574  -1940   -130   2964       C  
ATOM   3813  CD1 PHE B 193      40.053  13.756  27.355  1.00115.96           C  
ANISOU 3813  CD1 PHE B 193     9707  18633  15721  -1628   -237   3203       C  
ATOM   3814  CD2 PHE B 193      40.659  15.226  29.132  1.00118.51           C  
ANISOU 3814  CD2 PHE B 193     9941  19096  15990  -2286   -283   2799       C  
ATOM   3815  CE1 PHE B 193      40.677  12.704  28.010  1.00115.88           C  
ANISOU 3815  CE1 PHE B 193     9542  18931  15556  -1614   -474   3314       C  
ATOM   3816  CE2 PHE B 193      41.283  14.180  29.791  1.00116.47           C  
ANISOU 3816  CE2 PHE B 193     9516  19206  15530  -2286   -571   2930       C  
ATOM   3817  CZ  PHE B 193      41.292  12.918  29.230  1.00115.03           C  
ANISOU 3817  CZ  PHE B 193     9296  19087  15323  -1927   -658   3207       C  
ATOM   3818  N   LEU B 194      38.409  18.015  24.773  1.00 94.07           N  
ANISOU 3818  N   LEU B 194     7293  14675  13773  -1615    739   3133       N  
ATOM   3819  CA  LEU B 194      37.528  19.038  24.216  1.00 95.29           C  
ANISOU 3819  CA  LEU B 194     7571  14479  14157  -1533   1005   3189       C  
ATOM   3820  C   LEU B 194      36.772  18.514  23.001  1.00 89.38           C  
ANISOU 3820  C   LEU B 194     6891  13716  13352  -1184    990   3488       C  
ATOM   3821  O   LEU B 194      35.572  18.768  22.853  1.00 89.35           O  
ANISOU 3821  O   LEU B 194     6993  13551  13403  -1048   1066   3549       O  
ATOM   3822  CB  LEU B 194      38.331  20.289  23.857  1.00 97.42           C  
ANISOU 3822  CB  LEU B 194     7769  14530  14715  -1704   1266   3174       C  
ATOM   3823  CG  LEU B 194      39.009  21.020  25.019  1.00 98.70           C  
ANISOU 3823  CG  LEU B 194     7870  14682  14951  -2120   1341   2834       C  
ATOM   3824  CD1 LEU B 194      39.777  22.239  24.525  1.00 99.36           C  
ANISOU 3824  CD1 LEU B 194     7889  14519  15344  -2282   1644   2825       C  
ATOM   3825  CD2 LEU B 194      37.992  21.411  26.085  1.00 94.96           C  
ANISOU 3825  CD2 LEU B 194     7542  14055  14483  -2266   1432   2574       C  
ATOM   3826  N   LYS B 195      37.463  17.794  22.112  1.00 80.36           N  
ANISOU 3826  N   LYS B 195     5677  12751  12104  -1057    907   3675       N  
ATOM   3827  CA  LYS B 195      36.794  17.213  20.952  1.00 74.76           C  
ANISOU 3827  CA  LYS B 195     5041  12088  11275   -789    890   3926       C  
ATOM   3828  C   LYS B 195      35.708  16.231  21.377  1.00 82.76           C  
ANISOU 3828  C   LYS B 195     6149  13228  12068   -670    721   3872       C  
ATOM   3829  O   LYS B 195      34.627  16.190  20.779  1.00 88.50           O  
ANISOU 3829  O   LYS B 195     6958  13917  12750   -507    739   4008       O  
ATOM   3830  CB  LYS B 195      37.817  16.523  20.051  1.00 74.57           C  
ANISOU 3830  CB  LYS B 195     4935  12235  11164   -729    869   4068       C  
ATOM   3831  CG  LYS B 195      38.797  17.475  19.382  1.00 77.48           C  
ANISOU 3831  CG  LYS B 195     5221  12469  11748   -820   1068   4161       C  
ATOM   3832  CD  LYS B 195      39.913  16.718  18.680  1.00 76.82           C  
ANISOU 3832  CD  LYS B 195     5034  12556  11599   -792   1063   4251       C  
ATOM   3833  CE  LYS B 195      40.950  17.671  18.112  1.00 82.83           C  
ANISOU 3833  CE  LYS B 195     5703  13183  12587   -910   1274   4315       C  
ATOM   3834  NZ  LYS B 195      42.145  16.950  17.593  1.00 81.63           N  
ANISOU 3834  NZ  LYS B 195     5411  13186  12420   -909   1291   4365       N  
ATOM   3835  N   ILE B 196      35.974  15.438  22.415  1.00 80.96           N  
ANISOU 3835  N   ILE B 196     5898  13166  11697   -759    554   3691       N  
ATOM   3836  CA  ILE B 196      34.971  14.490  22.892  1.00 69.79           C  
ANISOU 3836  CA  ILE B 196     4584  11854  10080   -664    418   3625       C  
ATOM   3837  C   ILE B 196      33.763  15.226  23.458  1.00 75.52           C  
ANISOU 3837  C   ILE B 196     5406  12384  10903   -692    497   3516       C  
ATOM   3838  O   ILE B 196      32.610  14.854  23.194  1.00 82.01           O  
ANISOU 3838  O   ILE B 196     6307  13204  11649   -542    476   3570       O  
ATOM   3839  CB  ILE B 196      35.594  13.533  23.925  1.00 69.36           C  
ANISOU 3839  CB  ILE B 196     4477  12010   9865   -754    237   3497       C  
ATOM   3840  CG1 ILE B 196      36.634  12.636  23.246  1.00 69.18           C  
ANISOU 3840  CG1 ILE B 196     4341  12153   9790   -659    196   3650       C  
ATOM   3841  CG2 ILE B 196      34.513  12.702  24.605  1.00 67.74           C  
ANISOU 3841  CG2 ILE B 196     4398  11867   9474   -694    133   3400       C  
ATOM   3842  CD1 ILE B 196      37.372  11.709  24.190  1.00 72.04           C  
ANISOU 3842  CD1 ILE B 196     4599  12724  10049   -712     27   3611       C  
ATOM   3843  N   ILE B 197      34.003  16.283  24.238  1.00 80.85           N  
ANISOU 3843  N   ILE B 197     6067  12889  11764   -902    614   3346       N  
ATOM   3844  CA  ILE B 197      32.895  17.065  24.784  1.00 81.63           C  
ANISOU 3844  CA  ILE B 197     6252  12743  12019   -940    763   3226       C  
ATOM   3845  C   ILE B 197      32.099  17.712  23.656  1.00 81.56           C  
ANISOU 3845  C   ILE B 197     6243  12537  12208   -722    921   3488       C  
ATOM   3846  O   ILE B 197      30.868  17.806  23.718  1.00 76.24           O  
ANISOU 3846  O   ILE B 197     5615  11757  11597   -606    968   3514       O  
ATOM   3847  CB  ILE B 197      33.418  18.110  25.789  1.00 85.91           C  
ANISOU 3847  CB  ILE B 197     6787  13124  12732  -1258    920   2961       C  
ATOM   3848  CG1 ILE B 197      34.053  17.417  26.998  1.00 85.31           C  
ANISOU 3848  CG1 ILE B 197     6701  13316  12397  -1494    717   2728       C  
ATOM   3849  CG2 ILE B 197      32.295  19.032  26.245  1.00 86.99           C  
ANISOU 3849  CG2 ILE B 197     7013  12932  13109  -1294   1169   2838       C  
ATOM   3850  CD1 ILE B 197      34.668  18.375  28.005  1.00 82.45           C  
ANISOU 3850  CD1 ILE B 197     6323  12881  12125  -1883    844   2436       C  
ATOM   3851  N   ALA B 198      32.787  18.150  22.600  1.00 85.54           N  
ANISOU 3851  N   ALA B 198     6682  13008  12810   -662   1000   3710       N  
ATOM   3852  CA  ALA B 198      32.097  18.729  21.453  1.00 86.00           C  
ANISOU 3852  CA  ALA B 198     6729  12934  13015   -453   1121   4028       C  
ATOM   3853  C   ALA B 198      31.242  17.687  20.742  1.00 86.01           C  
ANISOU 3853  C   ALA B 198     6751  13179  12751   -245    935   4201       C  
ATOM   3854  O   ALA B 198      30.137  17.993  20.277  1.00101.17           O  
ANISOU 3854  O   ALA B 198     8656  15035  14750    -87    973   4394       O  
ATOM   3855  CB  ALA B 198      33.107  19.349  20.487  1.00 81.47           C  
ANISOU 3855  CB  ALA B 198     6097  12300  12557   -462   1247   4228       C  
ATOM   3856  N   VAL B 199      31.736  16.451  20.647  1.00 75.68           N  
ANISOU 3856  N   VAL B 199     5460  12153  11141   -251    750   4139       N  
ATOM   3857  CA  VAL B 199      30.942  15.390  20.033  1.00 77.45           C  
ANISOU 3857  CA  VAL B 199     5720  12608  11097   -107    608   4239       C  
ATOM   3858  C   VAL B 199      29.701  15.101  20.871  1.00 78.75           C  
ANISOU 3858  C   VAL B 199     5928  12751  11242    -79    550   4091       C  
ATOM   3859  O   VAL B 199      28.598  14.937  20.333  1.00 74.32           O  
ANISOU 3859  O   VAL B 199     5356  12261  10623     49    513   4232       O  
ATOM   3860  CB  VAL B 199      31.797  14.125  19.831  1.00 81.22           C  
ANISOU 3860  CB  VAL B 199     6215  13330  11315   -134    496   4174       C  
ATOM   3861  CG1 VAL B 199      30.931  12.972  19.347  1.00 86.28           C  
ANISOU 3861  CG1 VAL B 199     6916  14187  11679    -37    392   4201       C  
ATOM   3862  CG2 VAL B 199      32.917  14.393  18.841  1.00 81.23           C  
ANISOU 3862  CG2 VAL B 199     6166  13352  11345   -149    585   4339       C  
ATOM   3863  N   TRP B 200      29.852  15.053  22.198  1.00 75.53           N  
ANISOU 3863  N   TRP B 200     5562  12266  10872   -219    543   3809       N  
ATOM   3864  CA  TRP B 200      28.684  14.878  23.061  1.00 75.22           C  
ANISOU 3864  CA  TRP B 200     5576  12169  10836   -217    533   3648       C  
ATOM   3865  C   TRP B 200      27.695  16.026  22.890  1.00 81.03           C  
ANISOU 3865  C   TRP B 200     6260  12648  11881   -133    709   3767       C  
ATOM   3866  O   TRP B 200      26.477  15.807  22.849  1.00 88.76           O  
ANISOU 3866  O   TRP B 200     7222  13641  12860    -20    688   3809       O  
ATOM   3867  CB  TRP B 200      29.104  14.762  24.528  1.00 67.70           C  
ANISOU 3867  CB  TRP B 200     4689  11183   9853   -427    519   3331       C  
ATOM   3868  CG  TRP B 200      29.519  13.381  24.952  1.00 67.79           C  
ANISOU 3868  CG  TRP B 200     4749  11451   9557   -453    329   3234       C  
ATOM   3869  CD1 TRP B 200      30.786  12.950  25.213  1.00 71.23           C  
ANISOU 3869  CD1 TRP B 200     5147  12028   9889   -549    236   3206       C  
ATOM   3870  CD2 TRP B 200      28.661  12.253  25.169  1.00 64.22           C  
ANISOU 3870  CD2 TRP B 200     4374  11130   8897   -375    231   3174       C  
ATOM   3871  NE1 TRP B 200      30.772  11.626  25.577  1.00 68.25           N  
ANISOU 3871  NE1 TRP B 200     4818  11842   9271   -511     98   3164       N  
ATOM   3872  CE2 TRP B 200      29.480  11.174  25.556  1.00 63.30           C  
ANISOU 3872  CE2 TRP B 200     4279  11203   8570   -415    104   3128       C  
ATOM   3873  CE3 TRP B 200      27.282  12.051  25.070  1.00 63.71           C  
ANISOU 3873  CE3 TRP B 200     4344  11039   8824   -276    253   3167       C  
ATOM   3874  CZ2 TRP B 200      28.967   9.913  25.845  1.00 61.89           C  
ANISOU 3874  CZ2 TRP B 200     4184  11153   8179   -358     27   3069       C  
ATOM   3875  CZ3 TRP B 200      26.774  10.800  25.357  1.00 62.18           C  
ANISOU 3875  CZ3 TRP B 200     4230  10997   8397   -246    161   3076       C  
ATOM   3876  CH2 TRP B 200      27.615   9.746  25.741  1.00 65.81           C  
ANISOU 3876  CH2 TRP B 200     4738  11611   8655   -287     63   3025       C  
ATOM   3877  N   THR B 201      28.201  17.258  22.777  1.00 86.85           N  
ANISOU 3877  N   THR B 201     6952  13136  12910   -182    903   3837       N  
ATOM   3878  CA  THR B 201      27.327  18.418  22.627  1.00 88.43           C  
ANISOU 3878  CA  THR B 201     7088  13033  13479    -82   1128   3986       C  
ATOM   3879  C   THR B 201      26.554  18.366  21.313  1.00 84.55           C  
ANISOU 3879  C   THR B 201     6493  12666  12965    169   1056   4393       C  
ATOM   3880  O   THR B 201      25.344  18.618  21.282  1.00 85.37           O  
ANISOU 3880  O   THR B 201     6519  12689  13229    308   1103   4517       O  
ATOM   3881  CB  THR B 201      28.143  19.709  22.723  1.00 81.68           C  
ANISOU 3881  CB  THR B 201     6218  11867  12950   -203   1391   3977       C  
ATOM   3882  OG1 THR B 201      28.698  19.830  24.039  1.00 76.93           O  
ANISOU 3882  OG1 THR B 201     5699  11175  12355   -487   1463   3572       O  
ATOM   3883  CG2 THR B 201      27.266  20.918  22.444  1.00 80.99           C  
ANISOU 3883  CG2 THR B 201     6050  11421  13302    -59   1673   4197       C  
ATOM   3884  N   ILE B 202      27.236  18.040  20.212  1.00 81.69           N  
ANISOU 3884  N   ILE B 202     6117  12523  12398    215    945   4613       N  
ATOM   3885  CA  ILE B 202      26.536  17.973  18.933  1.00 84.85           C  
ANISOU 3885  CA  ILE B 202     6425  13110  12704    403    857   5004       C  
ATOM   3886  C   ILE B 202      25.571  16.791  18.908  1.00 80.66           C  
ANISOU 3886  C   ILE B 202     5894  12883  11871    448    643   4940       C  
ATOM   3887  O   ILE B 202      24.517  16.861  18.268  1.00 81.74           O  
ANISOU 3887  O   ILE B 202     5915  13140  12004    586    581   5204       O  
ATOM   3888  CB  ILE B 202      27.526  17.929  17.752  1.00 91.74           C  
ANISOU 3888  CB  ILE B 202     7309  14147  13403    396    826   5228       C  
ATOM   3889  CG1 ILE B 202      28.359  16.646  17.778  1.00 99.53           C  
ANISOU 3889  CG1 ILE B 202     8392  15402  14021    274    674   4996       C  
ATOM   3890  CG2 ILE B 202      28.416  19.168  17.756  1.00 85.98           C  
ANISOU 3890  CG2 ILE B 202     6569  13093  13005    347   1068   5300       C  
ATOM   3891  CD1 ILE B 202      29.301  16.502  16.602  1.00102.84           C  
ANISOU 3891  CD1 ILE B 202     8827  15982  14266    253    678   5184       C  
ATOM   3892  N   SER B 203      25.884  15.704  19.621  1.00 77.99           N  
ANISOU 3892  N   SER B 203     5668  12676  11288    327    535   4606       N  
ATOM   3893  CA  SER B 203      24.931  14.601  19.720  1.00 75.25           C  
ANISOU 3893  CA  SER B 203     5335  12564  10692    349    382   4504       C  
ATOM   3894  C   SER B 203      23.675  15.028  20.468  1.00 79.52           C  
ANISOU 3894  C   SER B 203     5809  12930  11476    411    452   4447       C  
ATOM   3895  O   SER B 203      22.556  14.698  20.055  1.00 77.48           O  
ANISOU 3895  O   SER B 203     5454  12840  11147    503    363   4571       O  
ATOM   3896  CB  SER B 203      25.579  13.402  20.411  1.00 73.89           C  
ANISOU 3896  CB  SER B 203     5302  12509  10262    222    300   4183       C  
ATOM   3897  OG  SER B 203      26.715  12.956  19.696  1.00 87.72           O  
ANISOU 3897  OG  SER B 203     7091  14407  11832    180    268   4242       O  
ATOM   3898  N   VAL B 204      23.843  15.760  21.572  1.00 84.69           N  
ANISOU 3898  N   VAL B 204     6504  13256  12418    337    627   4246       N  
ATOM   3899  CA  VAL B 204      22.690  16.273  22.309  1.00 84.36           C  
ANISOU 3899  CA  VAL B 204     6401  12986  12665    383    766   4174       C  
ATOM   3900  C   VAL B 204      21.876  17.219  21.434  1.00 93.18           C  
ANISOU 3900  C   VAL B 204     7313  14009  14084    593    852   4587       C  
ATOM   3901  O   VAL B 204      20.638  17.194  21.447  1.00 96.37           O  
ANISOU 3901  O   VAL B 204     7585  14429  14603    710    849   4678       O  
ATOM   3902  CB  VAL B 204      23.152  16.951  23.613  1.00 80.74           C  
ANISOU 3902  CB  VAL B 204     6047  12189  12441    207    986   3854       C  
ATOM   3903  CG1 VAL B 204      21.990  17.655  24.291  1.00 87.27           C  
ANISOU 3903  CG1 VAL B 204     6809  12712  13638    250   1216   3789       C  
ATOM   3904  CG2 VAL B 204      23.768  15.923  24.554  1.00 73.45           C  
ANISOU 3904  CG2 VAL B 204     5296  11423  11191     10    857   3496       C  
ATOM   3905  N   GLY B 205      22.557  18.065  20.657  1.00 98.88           N  
ANISOU 3905  N   GLY B 205     7987  14636  14948    649    935   4869       N  
ATOM   3906  CA  GLY B 205      21.851  18.974  19.765  1.00104.93           C  
ANISOU 3906  CA  GLY B 205     8547  15325  15997    868   1013   5339       C  
ATOM   3907  C   GLY B 205      21.093  18.255  18.664  1.00112.36           C  
ANISOU 3907  C   GLY B 205     9353  16713  16625    985    736   5647       C  
ATOM   3908  O   GLY B 205      20.015  18.691  18.253  1.00117.98           O  
ANISOU 3908  O   GLY B 205     9846  17444  17538   1165    736   5979       O  
ATOM   3909  N   ILE B 206      21.648  17.148  18.168  1.00110.76           N  
ANISOU 3909  N   ILE B 206     9265  16884  15934    869    515   5543       N  
ATOM   3910  CA  ILE B 206      20.953  16.348  17.164  1.00111.33           C  
ANISOU 3910  CA  ILE B 206     9238  17418  15642    900    267   5750       C  
ATOM   3911  C   ILE B 206      19.755  15.639  17.784  1.00106.84           C  
ANISOU 3911  C   ILE B 206     8606  16956  15031    898    185   5551       C  
ATOM   3912  O   ILE B 206      18.708  15.480  17.145  1.00117.03           O  
ANISOU 3912  O   ILE B 206     9701  18523  16242    977     43   5801       O  
ATOM   3913  CB  ILE B 206      21.927  15.348  16.511  1.00113.22           C  
ANISOU 3913  CB  ILE B 206     9643  17971  15404    743    133   5636       C  
ATOM   3914  CG1 ILE B 206      22.973  16.079  15.671  1.00113.65           C  
ANISOU 3914  CG1 ILE B 206     9722  17971  15490    753    212   5903       C  
ATOM   3915  CG2 ILE B 206      21.181  14.337  15.651  1.00114.78           C  
ANISOU 3915  CG2 ILE B 206     9782  18653  15176    692    -88   5715       C  
ATOM   3916  CD1 ILE B 206      24.012  15.158  15.067  1.00112.24           C  
ANISOU 3916  CD1 ILE B 206     9702  18043  14902    597    143   5773       C  
ATOM   3917  N   SER B 207      19.883  15.216  19.042  1.00 99.49           N  
ANISOU 3917  N   SER B 207     7828  15827  14146    794    270   5110       N  
ATOM   3918  CA  SER B 207      18.852  14.381  19.648  1.00 96.47           C  
ANISOU 3918  CA  SER B 207     7429  15557  13670    760    204   4874       C  
ATOM   3919  C   SER B 207      17.700  15.185  20.245  1.00 98.11           C  
ANISOU 3919  C   SER B 207     7452  15499  14325    892    356   4945       C  
ATOM   3920  O   SER B 207      16.581  14.671  20.310  1.00 95.24           O  
ANISOU 3920  O   SER B 207     6965  15304  13919    917    275   4920       O  
ATOM   3921  CB  SER B 207      19.477  13.485  20.719  1.00 89.07           C  
ANISOU 3921  CB  SER B 207     6743  14552  12547    586    226   4402       C  
ATOM   3922  OG  SER B 207      20.422  12.589  20.155  1.00 75.35           O  
ANISOU 3922  OG  SER B 207     5142  13064  10423    485    105   4346       O  
ATOM   3923  N   MET B 208      17.941  16.430  20.660  1.00101.17           N  
ANISOU 3923  N   MET B 208     7811  15467  15163    967    605   5025       N  
ATOM   3924  CA  MET B 208      16.916  17.232  21.336  1.00109.42           C  
ANISOU 3924  CA  MET B 208     8696  16174  16703   1083    837   5050       C  
ATOM   3925  C   MET B 208      15.571  17.329  20.610  1.00107.38           C  
ANISOU 3925  C   MET B 208     8105  16119  16575   1285    733   5442       C  
ATOM   3926  O   MET B 208      14.530  17.339  21.298  1.00107.99           O  
ANISOU 3926  O   MET B 208     8067  16059  16905   1330    847   5324       O  
ATOM   3927  CB  MET B 208      17.485  18.637  21.592  1.00119.96           C  
ANISOU 3927  CB  MET B 208    10038  17030  18510   1132   1158   5148       C  
ATOM   3928  CG  MET B 208      16.543  19.602  22.307  1.00130.42           C  
ANISOU 3928  CG  MET B 208    11213  17909  20432   1245   1500   5161       C  
ATOM   3929  SD  MET B 208      17.238  21.268  22.450  1.00139.02           S  
ANISOU 3929  SD  MET B 208    12314  18413  22096   1286   1937   5293       S  
ATOM   3930  CE  MET B 208      16.016  22.071  23.487  1.00138.97           C  
ANISOU 3930  CE  MET B 208    12168  17884  22748   1366   2381   5171       C  
ATOM   3931  N   PRO B 209      15.502  17.427  19.274  1.00102.34           N  
ANISOU 3931  N   PRO B 209     7326  15795  15765   1389    529   5895       N  
ATOM   3932  CA  PRO B 209      14.181  17.427  18.623  1.00 95.85           C  
ANISOU 3932  CA  PRO B 209     6358  15150  14911   1483    395   6157       C  
ATOM   3933  C   PRO B 209      13.336  16.206  18.950  1.00 98.65           C  
ANISOU 3933  C   PRO B 209     6743  15786  14954   1353    228   5830       C  
ATOM   3934  O   PRO B 209      12.103  16.310  18.965  1.00 96.94           O  
ANISOU 3934  O   PRO B 209     6363  15573  14897   1431    222   5921       O  
ATOM   3935  CB  PRO B 209      14.524  17.497  17.126  1.00 90.19           C  
ANISOU 3935  CB  PRO B 209     5645  14779  13843   1478    187   6563       C  
ATOM   3936  CG  PRO B 209      15.980  17.169  17.032  1.00 89.72           C  
ANISOU 3936  CG  PRO B 209     5772  14784  13534   1357    165   6415       C  
ATOM   3937  CD  PRO B 209      16.570  17.691  18.295  1.00 98.29           C  
ANISOU 3937  CD  PRO B 209     6872  15414  15060   1384    448   6161       C  
ATOM   3938  N   ILE B 210      13.954  15.054  19.224  1.00101.14           N  
ANISOU 3938  N   ILE B 210     7249  16322  14858   1159    116   5460       N  
ATOM   3939  CA  ILE B 210      13.174  13.855  19.538  1.00100.75           C  
ANISOU 3939  CA  ILE B 210     7231  16522  14528   1027     -4   5147       C  
ATOM   3940  C   ILE B 210      12.379  14.017  20.830  1.00 95.04           C  
ANISOU 3940  C   ILE B 210     6422  15483  14204   1070    210   4900       C  
ATOM   3941  O   ILE B 210      11.151  13.832  20.797  1.00100.39           O  
ANISOU 3941  O   ILE B 210     6959  16247  14940   1101    168   4916       O  
ATOM   3942  CB  ILE B 210      14.082  12.614  19.539  1.00104.28           C  
ANISOU 3942  CB  ILE B 210     7904  17230  14490    821   -118   4838       C  
ATOM   3943  CG1 ILE B 210      14.584  12.320  18.125  1.00117.79           C  
ANISOU 3943  CG1 ILE B 210     9667  19309  15777    750   -312   5070       C  
ATOM   3944  CG2 ILE B 210      13.342  11.414  20.105  1.00100.50           C  
ANISOU 3944  CG2 ILE B 210     7463  16918  13806    685   -159   4479       C  
ATOM   3945  CD1 ILE B 210      15.490  11.117  18.039  1.00120.85           C  
ANISOU 3945  CD1 ILE B 210    10257  19928  15734    559   -377   4791       C  
ATOM   3946  N   PRO B 211      12.982  14.366  21.978  1.00 90.35           N  
ANISOU 3946  N   PRO B 211     5918  14527  13885   1042    462   4652       N  
ATOM   3947  CA  PRO B 211      12.139  14.657  23.148  1.00 88.46           C  
ANISOU 3947  CA  PRO B 211     5640  13938  14032   1055    721   4412       C  
ATOM   3948  C   PRO B 211      11.227  15.850  22.940  1.00 97.59           C  
ANISOU 3948  C   PRO B 211     6489  14842  15749   1291    892   4772       C  
ATOM   3949  O   PRO B 211      10.088  15.821  23.419  1.00103.68           O  
ANISOU 3949  O   PRO B 211     7135  15510  16749   1331    996   4679       O  
ATOM   3950  CB  PRO B 211      13.156  14.894  24.275  1.00 80.14           C  
ANISOU 3950  CB  PRO B 211     4926  12503  13019    898    944   4026       C  
ATOM   3951  CG  PRO B 211      14.415  15.223  23.594  1.00 80.74           C  
ANISOU 3951  CG  PRO B 211     5102  12626  12948    896    856   4204       C  
ATOM   3952  CD  PRO B 211      14.408  14.418  22.336  1.00 85.00           C  
ANISOU 3952  CD  PRO B 211     5553  13675  13068    919    526   4445       C  
ATOM   3953  N   VAL B 212      11.678  16.895  22.233  1.00 98.23           N  
ANISOU 3953  N   VAL B 212     6507  14777  16040   1439    936   5159       N  
ATOM   3954  CA  VAL B 212      10.812  18.058  22.015  1.00103.61           C  
ANISOU 3954  CA  VAL B 212     6971  15151  17247   1666   1121   5515       C  
ATOM   3955  C   VAL B 212       9.495  17.633  21.365  1.00107.00           C  
ANISOU 3955  C   VAL B 212     7234  15894  17529   1724    885   5701       C  
ATOM   3956  O   VAL B 212       8.403  17.871  21.901  1.00100.91           O  
ANISOU 3956  O   VAL B 212     6305  14919  17117   1805   1047   5659       O  
ATOM   3957  CB  VAL B 212      11.538  19.124  21.175  1.00101.60           C  
ANISOU 3957  CB  VAL B 212     6682  14757  17163   1805   1173   5960       C  
ATOM   3958  CG1 VAL B 212      10.546  20.145  20.646  1.00102.84           C  
ANISOU 3958  CG1 VAL B 212     6604  14719  17752   2041   1283   6437       C  
ATOM   3959  CG2 VAL B 212      12.608  19.812  22.008  1.00 98.51           C  
ANISOU 3959  CG2 VAL B 212     6385  13931  17111   1756   1528   5759       C  
ATOM   3960  N   PHE B 213       9.582  16.948  20.225  1.00112.39           N  
ANISOU 3960  N   PHE B 213     7946  17089  17667   1648    520   5873       N  
ATOM   3961  CA  PHE B 213       8.400  16.565  19.463  1.00119.60           C  
ANISOU 3961  CA  PHE B 213     8681  18367  18393   1656    286   6072       C  
ATOM   3962  C   PHE B 213       7.763  15.270  19.950  1.00116.71           C  
ANISOU 3962  C   PHE B 213     8350  18263  17733   1480    166   5642       C  
ATOM   3963  O   PHE B 213       6.715  14.882  19.421  1.00116.62           O  
ANISOU 3963  O   PHE B 213     8169  18560  17580   1458    -11   5748       O  
ATOM   3964  CB  PHE B 213       8.752  16.449  17.976  1.00125.78           C  
ANISOU 3964  CB  PHE B 213     9472  19599  18718   1604     -1   6440       C  
ATOM   3965  CG  PHE B 213       9.044  17.770  17.316  1.00128.82           C  
ANISOU 3965  CG  PHE B 213     9751  19781  19412   1792    109   6968       C  
ATOM   3966  CD1 PHE B 213       8.075  18.411  16.560  1.00135.91           C  
ANISOU 3966  CD1 PHE B 213    10385  20778  20477   1926     61   7448       C  
ATOM   3967  CD2 PHE B 213      10.286  18.371  17.449  1.00122.91           C  
ANISOU 3967  CD2 PHE B 213     9147  18751  18800   1829    274   6999       C  
ATOM   3968  CE1 PHE B 213       8.338  19.626  15.951  1.00136.94           C  
ANISOU 3968  CE1 PHE B 213    10409  20715  20907   2096    193   7961       C  
ATOM   3969  CE2 PHE B 213      10.554  19.586  16.844  1.00127.61           C  
ANISOU 3969  CE2 PHE B 213     9642  19140  19705   1997    411   7487       C  
ATOM   3970  CZ  PHE B 213       9.578  20.214  16.094  1.00133.03           C  
ANISOU 3970  CZ  PHE B 213    10076  19913  20557   2132    379   7975       C  
ATOM   3971  N   GLY B 214       8.358  14.590  20.931  1.00110.09           N  
ANISOU 3971  N   GLY B 214     7709  17324  16796   1340    267   5176       N  
ATOM   3972  CA  GLY B 214       7.698  13.449  21.531  1.00 99.17           C  
ANISOU 3972  CA  GLY B 214     6347  16113  15220   1184    228   4777       C  
ATOM   3973  C   GLY B 214       6.862  13.893  22.711  1.00 97.93           C  
ANISOU 3973  C   GLY B 214     6064  15552  15594   1265    537   4597       C  
ATOM   3974  O   GLY B 214       5.788  13.341  22.969  1.00105.37           O  
ANISOU 3974  O   GLY B 214     6884  16608  16545   1220    521   4441       O  
ATOM   3975  N   LEU B 215       7.351  14.896  23.446  1.00 95.74           N  
ANISOU 3975  N   LEU B 215     5815  14787  15773   1363    858   4594       N  
ATOM   3976  CA  LEU B 215       6.549  15.485  24.508  1.00 96.98           C  
ANISOU 3976  CA  LEU B 215     5858  14499  16490   1434   1226   4440       C  
ATOM   3977  C   LEU B 215       5.441  16.361  23.941  1.00105.88           C  
ANISOU 3977  C   LEU B 215     6700  15514  18015   1664   1253   4850       C  
ATOM   3978  O   LEU B 215       4.356  16.441  24.531  1.00 98.80           O  
ANISOU 3978  O   LEU B 215     5653  14440  17448   1706   1435   4736       O  
ATOM   3979  CB  LEU B 215       7.440  16.287  25.456  1.00 90.60           C  
ANISOU 3979  CB  LEU B 215     5187  13197  16041   1413   1612   4271       C  
ATOM   3980  CG  LEU B 215       8.524  15.479  26.172  1.00 85.98           C  
ANISOU 3980  CG  LEU B 215     4934  12682  15052   1151   1604   3840       C  
ATOM   3981  CD1 LEU B 215       9.303  16.354  27.139  1.00 86.02           C  
ANISOU 3981  CD1 LEU B 215     5202  12161  15320   1052   1969   3586       C  
ATOM   3982  CD2 LEU B 215       7.916  14.286  26.891  1.00 83.91           C  
ANISOU 3982  CD2 LEU B 215     4802  12575  14506    964   1568   3420       C  
ATOM   3983  N   GLN B 216       5.685  17.016  22.800  1.00120.06           N  
ANISOU 3983  N   GLN B 216     8413  17418  19787   1805   1089   5345       N  
ATOM   3984  CA  GLN B 216       4.625  17.802  22.172  1.00130.72           C  
ANISOU 3984  CA  GLN B 216     9472  18721  21475   2014   1089   5805       C  
ATOM   3985  C   GLN B 216       3.564  16.901  21.547  1.00129.43           C  
ANISOU 3985  C   GLN B 216     9138  19080  20961   1944    753   5845       C  
ATOM   3986  O   GLN B 216       2.363  17.087  21.776  1.00126.11           O  
ANISOU 3986  O   GLN B 216     8476  18576  20863   2036    841   5903       O  
ATOM   3987  CB  GLN B 216       5.217  18.746  21.124  1.00134.02           C  
ANISOU 3987  CB  GLN B 216     9853  19125  21943   2159   1031   6347       C  
ATOM   3988  CG  GLN B 216       6.023  19.886  21.712  1.00133.84           C  
ANISOU 3988  CG  GLN B 216     9919  18504  22429   2264   1438   6375       C  
ATOM   3989  CD  GLN B 216       5.218  20.706  22.697  1.00138.89           C  
ANISOU 3989  CD  GLN B 216    10431  18558  23784   2390   1895   6295       C  
ATOM   3990  OE1 GLN B 216       4.102  21.135  22.400  1.00147.40           O  
ANISOU 3990  OE1 GLN B 216    11254  19590  25162   2547   1924   6609       O  
ATOM   3991  NE2 GLN B 216       5.776  20.918  23.883  1.00133.90           N  
ANISOU 3991  NE2 GLN B 216     9975  17480  23422   2296   2276   5859       N  
ATOM   3992  N   ASP B 217       3.987  15.920  20.755  1.00110.40           N  
ANISOU 3992  N   ASP B 217     8515  19218  14213    574   1837   5193       N  
ATOM   3993  CA  ASP B 217       3.083  15.021  20.048  1.00103.19           C  
ANISOU 3993  CA  ASP B 217     7582  18419  13209    548   1759   5273       C  
ATOM   3994  C   ASP B 217       3.347  13.601  20.526  1.00107.71           C  
ANISOU 3994  C   ASP B 217     8204  19039  13682    510   1723   5164       C  
ATOM   3995  O   ASP B 217       4.481  13.117  20.445  1.00122.05           O  
ANISOU 3995  O   ASP B 217    10066  20871  15437    488   1723   5083       O  
ATOM   3996  CB  ASP B 217       3.282  15.134  18.534  1.00100.56           C  
ANISOU 3996  CB  ASP B 217     7217  18181  12810    533   1718   5386       C  
ATOM   3997  CG  ASP B 217       2.170  14.476  17.741  1.00 93.35           C  
ANISOU 3997  CG  ASP B 217     6258  17393  11819    509   1645   5480       C  
ATOM   3998  OD1 ASP B 217       1.610  13.462  18.207  1.00 88.06           O  
ANISOU 3998  OD1 ASP B 217     5601  16755  11104    483   1613   5422       O  
ATOM   3999  OD2 ASP B 217       1.859  14.978  16.641  1.00 94.96           O  
ANISOU 3999  OD2 ASP B 217     6406  17668  12004    516   1621   5613       O  
ATOM   4000  N   ASP B 218       2.302  12.935  21.017  1.00105.81           N  
ANISOU 4000  N   ASP B 218     7953  18818  13434    505   1697   5165       N  
ATOM   4001  CA  ASP B 218       2.432  11.566  21.498  1.00102.53           C  
ANISOU 4001  CA  ASP B 218     7576  18437  12944    473   1669   5076       C  
ATOM   4002  C   ASP B 218       2.384  10.533  20.379  1.00 96.71           C  
ANISOU 4002  C   ASP B 218     6827  17816  12104    420   1607   5100       C  
ATOM   4003  O   ASP B 218       2.729   9.370  20.618  1.00 90.46           O  
ANISOU 4003  O   ASP B 218     6065  17047  11257    388   1592   5020       O  
ATOM   4004  CB  ASP B 218       1.336  11.263  22.524  1.00110.06           C  
ANISOU 4004  CB  ASP B 218     8520  19359  13941    488   1673   5066       C  
ATOM   4005  CG  ASP B 218       1.347  12.232  23.690  1.00116.84           C  
ANISOU 4005  CG  ASP B 218     9381  20114  14897    534   1738   5021       C  
ATOM   4006  OD1 ASP B 218       2.389  12.886  23.906  1.00120.82           O  
ANISOU 4006  OD1 ASP B 218     9908  20570  15428    547   1783   4963       O  
ATOM   4007  OD2 ASP B 218       0.319  12.336  24.394  1.00118.34           O  
ANISOU 4007  OD2 ASP B 218     9548  20276  15139    553   1746   5036       O  
ATOM   4008  N   SER B 219       1.960  10.920  19.174  1.00 99.15           N  
ANISOU 4008  N   SER B 219     7084  18202  12386    410   1573   5206       N  
ATOM   4009  CA  SER B 219       1.848   9.972  18.073  1.00100.22           C  
ANISOU 4009  CA  SER B 219     7193  18468  12418    353   1514   5217       C  
ATOM   4010  C   SER B 219       3.190   9.670  17.422  1.00111.52           C  
ANISOU 4010  C   SER B 219     8657  19939  13778    321   1510   5160       C  
ATOM   4011  O   SER B 219       3.318   8.641  16.749  1.00120.04           O  
ANISOU 4011  O   SER B 219     9725  21113  14772    265   1472   5119       O  
ATOM   4012  CB  SER B 219       0.876  10.497  17.016  1.00 87.96           C  
ANISOU 4012  CB  SER B 219     5565  17009  10848    354   1475   5354       C  
ATOM   4013  OG  SER B 219       1.361  11.692  16.433  1.00 88.41           O  
ANISOU 4013  OG  SER B 219     5606  17055  10930    387   1495   5440       O  
ATOM   4014  N   LYS B 220       4.183  10.544  17.600  1.00107.12           N  
ANISOU 4014  N   LYS B 220     8133  19311  13257    353   1553   5148       N  
ATOM   4015  CA  LYS B 220       5.498  10.363  16.999  1.00 95.30           C  
ANISOU 4015  CA  LYS B 220     6667  17845  11697    327   1553   5097       C  
ATOM   4016  C   LYS B 220       6.381   9.393  17.773  1.00 95.42           C  
ANISOU 4016  C   LYS B 220     6747  17819  11690    307   1570   4958       C  
ATOM   4017  O   LYS B 220       7.400   8.947  17.235  1.00102.41           O  
ANISOU 4017  O   LYS B 220     7656  18743  12512    274   1562   4903       O  
ATOM   4018  CB  LYS B 220       6.201  11.719  16.878  1.00 89.25           C  
ANISOU 4018  CB  LYS B 220     5906  17014  10990    369   1599   5141       C  
ATOM   4019  CG  LYS B 220       5.508  12.671  15.918  1.00 99.63           C  
ANISOU 4019  CG  LYS B 220     7153  18378  12324    390   1584   5296       C  
ATOM   4020  CD  LYS B 220       6.131  14.056  15.929  1.00104.91           C  
ANISOU 4020  CD  LYS B 220     7822  18955  13087    437   1645   5344       C  
ATOM   4021  CE  LYS B 220       5.334  15.015  15.051  1.00109.05           C  
ANISOU 4021  CE  LYS B 220     8270  19518  13647    468   1637   5520       C  
ATOM   4022  NZ  LYS B 220       5.922  16.383  15.035  1.00110.70           N  
ANISOU 4022  NZ  LYS B 220     8470  19621  13970    516   1706   5573       N  
ATOM   4023  N   VAL B 221       6.021   9.055  19.009  1.00 93.21           N  
ANISOU 4023  N   VAL B 221     6490  17466  11459    328   1592   4906       N  
ATOM   4024  CA  VAL B 221       6.769   8.083  19.799  1.00 88.62           C  
ANISOU 4024  CA  VAL B 221     5961  16852  10858    317   1608   4792       C  
ATOM   4025  C   VAL B 221       5.942   6.866  20.184  1.00 87.77           C  
ANISOU 4025  C   VAL B 221     5841  16763  10744    294   1587   4772       C  
ATOM   4026  O   VAL B 221       6.498   5.919  20.760  1.00 83.51           O  
ANISOU 4026  O   VAL B 221     5336  16201  10191    284   1600   4693       O  
ATOM   4027  CB  VAL B 221       7.372   8.726  21.069  1.00 83.53           C  
ANISOU 4027  CB  VAL B 221     5359  16107  10272    367   1665   4732       C  
ATOM   4028  CG1 VAL B 221       8.285   9.879  20.704  1.00 83.59           C  
ANISOU 4028  CG1 VAL B 221     5376  16084  10300    385   1696   4735       C  
ATOM   4029  CG2 VAL B 221       6.269   9.189  22.004  1.00 83.73           C  
ANISOU 4029  CG2 VAL B 221     5362  16080  10372    406   1683   4763       C  
ATOM   4030  N   PHE B 222       4.641   6.852  19.898  1.00 84.55           N  
ANISOU 4030  N   PHE B 222     5381  16393  10350    287   1559   4844       N  
ATOM   4031  CA  PHE B 222       3.769   5.733  20.226  1.00 84.62           C  
ANISOU 4031  CA  PHE B 222     5371  16416  10365    264   1543   4827       C  
ATOM   4032  C   PHE B 222       3.107   5.183  18.971  1.00 85.30           C  
ANISOU 4032  C   PHE B 222     5395  16615  10399    205   1495   4859       C  
ATOM   4033  O   PHE B 222       2.729   5.939  18.069  1.00 85.88           O  
ANISOU 4033  O   PHE B 222     5427  16756  10448    203   1468   4939       O  
ATOM   4034  CB  PHE B 222       2.683   6.141  21.228  1.00 84.71           C  
ANISOU 4034  CB  PHE B 222     5370  16369  10446    308   1558   4867       C  
ATOM   4035  CG  PHE B 222       3.172   6.265  22.638  1.00 84.12           C  
ANISOU 4035  CG  PHE B 222     5346  16204  10413    353   1604   4809       C  
ATOM   4036  CD1 PHE B 222       3.527   5.137  23.362  1.00 83.72           C  
ANISOU 4036  CD1 PHE B 222     5324  16133  10354    347   1617   4741       C  
ATOM   4037  CD2 PHE B 222       3.266   7.505  23.246  1.00 84.09           C  
ANISOU 4037  CD2 PHE B 222     5350  16141  10459    402   1638   4820       C  
ATOM   4038  CE1 PHE B 222       3.978   5.245  24.663  1.00 83.30           C  
ANISOU 4038  CE1 PHE B 222     5309  16019  10322    391   1656   4692       C  
ATOM   4039  CE2 PHE B 222       3.715   7.621  24.547  1.00 86.56           C  
ANISOU 4039  CE2 PHE B 222     5699  16393  10798    439   1681   4752       C  
ATOM   4040  CZ  PHE B 222       4.071   6.488  25.257  1.00 83.27           C  
ANISOU 4040  CZ  PHE B 222     5312  15974  10353    435   1686   4691       C  
ATOM   4041  N   LYS B 223       2.943   3.859  18.938  1.00 85.31           N  
ANISOU 4041  N   LYS B 223     5385  16640  10391    158   1487   4797       N  
ATOM   4042  CA  LYS B 223       2.212   3.175  17.868  1.00 86.05           C  
ANISOU 4042  CA  LYS B 223     5408  16845  10442     94   1447   4799       C  
ATOM   4043  C   LYS B 223       1.379   2.076  18.526  1.00 94.12           C  
ANISOU 4043  C   LYS B 223     6412  17832  11519     77   1459   4761       C  
ATOM   4044  O   LYS B 223       1.860   0.957  18.727  1.00100.31           O  
ANISOU 4044  O   LYS B 223     7206  18588  12319     45   1481   4678       O  
ATOM   4045  CB  LYS B 223       3.153   2.606  16.814  1.00 86.17           C  
ANISOU 4045  CB  LYS B 223     5415  16941  10386     33   1435   4733       C  
ATOM   4046  CG  LYS B 223       2.439   1.844  15.707  1.00 88.64           C  
ANISOU 4046  CG  LYS B 223     5644  17383  10650    -43   1397   4709       C  
ATOM   4047  CD  LYS B 223       3.417   1.181  14.745  1.00 93.27           C  
ANISOU 4047  CD  LYS B 223     6219  18048  11171   -109   1391   4620       C  
ATOM   4048  CE  LYS B 223       4.221   2.206  13.960  1.00 97.51           C  
ANISOU 4048  CE  LYS B 223     6770  18647  11632    -95   1372   4670       C  
ATOM   4049  NZ  LYS B 223       5.176   1.550  13.020  1.00105.11           N  
ANISOU 4049  NZ  LYS B 223     7719  19692  12525   -163   1366   4577       N  
ATOM   4050  N   GLU B 224       0.131   2.413  18.865  1.00101.96           N  
ANISOU 4050  N   GLU B 224     7373  18819  12549    100   1448   4827       N  
ATOM   4051  CA  GLU B 224      -0.831   1.459  19.418  1.00 86.64           C  
ANISOU 4051  CA  GLU B 224     5404  16851  10664     84   1457   4805       C  
ATOM   4052  C   GLU B 224      -0.319   0.838  20.716  1.00 85.98           C  
ANISOU 4052  C   GLU B 224     5377  16650  10640    116   1505   4755       C  
ATOM   4053  O   GLU B 224      -0.261  -0.384  20.869  1.00 86.04           O  
ANISOU 4053  O   GLU B 224     5374  16637  10681     81   1526   4693       O  
ATOM   4054  CB  GLU B 224      -1.180   0.385  18.388  1.00 87.33           C  
ANISOU 4054  CB  GLU B 224     5422  17035  10725      0   1435   4745       C  
ATOM   4055  CG  GLU B 224      -1.615   0.965  17.056  1.00 99.27           C  
ANISOU 4055  CG  GLU B 224     6870  18691  12156    -33   1383   4792       C  
ATOM   4056  CD  GLU B 224      -1.772  -0.091  15.990  1.00107.52           C  
ANISOU 4056  CD  GLU B 224     7841  19851  13160   -124   1364   4706       C  
ATOM   4057  OE1 GLU B 224      -1.904  -1.281  16.347  1.00106.26           O  
ANISOU 4057  OE1 GLU B 224     7667  19644  13063   -162   1395   4620       O  
ATOM   4058  OE2 GLU B 224      -1.757   0.269  14.793  1.00112.46           O  
ANISOU 4058  OE2 GLU B 224     8418  20618  13695   -159   1322   4723       O  
ATOM   4059  N   GLY B 225       0.046   1.698  21.665  1.00 85.43           N  
ANISOU 4059  N   GLY B 225     5363  16510  10589    183   1527   4783       N  
ATOM   4060  CA  GLY B 225       0.554   1.261  22.947  1.00 86.46           C  
ANISOU 4060  CA  GLY B 225     5543  16550  10757    222   1570   4746       C  
ATOM   4061  C   GLY B 225       2.028   0.921  22.982  1.00 98.21           C  
ANISOU 4061  C   GLY B 225     7079  18019  12217    219   1592   4681       C  
ATOM   4062  O   GLY B 225       2.628   0.957  24.062  1.00 99.24           O  
ANISOU 4062  O   GLY B 225     7256  18089  12361    266   1624   4661       O  
ATOM   4063  N   SER B 226       2.634   0.584  21.845  1.00 99.94           N  
ANISOU 4063  N   SER B 226     7284  18297  12392    165   1576   4644       N  
ATOM   4064  CA  SER B 226       4.061   0.301  21.805  1.00 93.38           C  
ANISOU 4064  CA  SER B 226     6497  17449  11533    160   1596   4582       C  
ATOM   4065  C   SER B 226       4.851   1.599  21.676  1.00102.84           C  
ANISOU 4065  C   SER B 226     7734  18651  12687    194   1592   4598       C  
ATOM   4066  O   SER B 226       4.355   2.604  21.159  1.00110.33           O  
ANISOU 4066  O   SER B 226     8661  19637  13622    202   1568   4657       O  
ATOM   4067  CB  SER B 226       4.395  -0.635  20.643  1.00 84.47           C  
ANISOU 4067  CB  SER B 226     5332  16381  10381     83   1586   4523       C  
ATOM   4068  OG  SER B 226       3.921  -0.115  19.414  1.00 86.34           O  
ANISOU 4068  OG  SER B 226     5522  16720  10565     43   1541   4551       O  
ATOM   4069  N   CYS B 227       6.093   1.569  22.153  1.00101.71           N  
ANISOU 4069  N   CYS B 227     7645  18470  12532    216   1620   4547       N  
ATOM   4070  CA  CYS B 227       6.969   2.737  22.152  1.00 95.12           C  
ANISOU 4070  CA  CYS B 227     6848  17626  11668    248   1627   4545       C  
ATOM   4071  C   CYS B 227       8.036   2.551  21.080  1.00102.13           C  
ANISOU 4071  C   CYS B 227     7745  18560  12500    204   1617   4503       C  
ATOM   4072  O   CYS B 227       8.937   1.718  21.230  1.00103.69           O  
ANISOU 4072  O   CYS B 227     7968  18741  12688    190   1635   4439       O  
ATOM   4073  CB  CYS B 227       7.595   2.947  23.531  1.00 98.76           C  
ANISOU 4073  CB  CYS B 227     7357  18020  12147    307   1666   4510       C  
ATOM   4074  SG  CYS B 227       8.845   4.266  23.632  1.00 97.98           S  
ANISOU 4074  SG  CYS B 227     7300  17902  12024    340   1689   4476       S  
ATOM   4075  N   LEU B 228       7.930   3.326  20.004  1.00105.52           N  
ANISOU 4075  N   LEU B 228     8149  19051  12894    184   1589   4545       N  
ATOM   4076  CA  LEU B 228       8.906   3.313  18.922  1.00 95.05           C  
ANISOU 4076  CA  LEU B 228     6828  17782  11507    144   1576   4514       C  
ATOM   4077  C   LEU B 228       8.665   4.532  18.044  1.00101.89           C  
ANISOU 4077  C   LEU B 228     7667  18700  12347    150   1553   4592       C  
ATOM   4078  O   LEU B 228       7.571   5.105  18.033  1.00104.89           O  
ANISOU 4078  O   LEU B 228     8009  19090  12753    169   1538   4671       O  
ATOM   4079  CB  LEU B 228       8.829   2.017  18.101  1.00 85.57           C  
ANISOU 4079  CB  LEU B 228     5588  16646  10279     71   1558   4463       C  
ATOM   4080  CG  LEU B 228       7.464   1.555  17.581  1.00 86.82           C  
ANISOU 4080  CG  LEU B 228     5675  16869  10443     31   1528   4496       C  
ATOM   4081  CD1 LEU B 228       7.159   2.136  16.202  1.00 84.91           C  
ANISOU 4081  CD1 LEU B 228     5381  16751  10131     -5   1483   4543       C  
ATOM   4082  CD2 LEU B 228       7.390   0.034  17.563  1.00 88.24           C  
ANISOU 4082  CD2 LEU B 228     5829  17047  10652    -23   1542   4416       C  
ATOM   4083  N   LEU B 229       9.705   4.920  17.308  1.00104.94           N  
ANISOU 4083  N   LEU B 229     8070  19118  12686    136   1552   4576       N  
ATOM   4084  CA  LEU B 229       9.617   6.066  16.411  1.00103.75           C  
ANISOU 4084  CA  LEU B 229     7891  19018  12512    144   1535   4661       C  
ATOM   4085  C   LEU B 229       8.610   5.809  15.298  1.00106.45           C  
ANISOU 4085  C   LEU B 229     8159  19483  12804    100   1485   4722       C  
ATOM   4086  O   LEU B 229       8.755   4.860  14.521  1.00 99.73           O  
ANISOU 4086  O   LEU B 229     7282  18721  11892     36   1460   4668       O  
ATOM   4087  CB  LEU B 229      10.996   6.378  15.832  1.00 95.85           C  
ANISOU 4087  CB  LEU B 229     6922  18030  11465    133   1546   4624       C  
ATOM   4088  CG  LEU B 229      11.942   7.063  16.821  1.00 89.82           C  
ANISOU 4088  CG  LEU B 229     6220  17155  10753    185   1597   4582       C  
ATOM   4089  CD1 LEU B 229      13.369   7.016  16.329  1.00 91.79           C  
ANISOU 4089  CD1 LEU B 229     6506  17417  10953    165   1608   4520       C  
ATOM   4090  CD2 LEU B 229      11.515   8.504  17.064  1.00 87.64           C  
ANISOU 4090  CD2 LEU B 229     5929  16827  10544    240   1620   4665       C  
ATOM   4091  N   ALA B 230       7.580   6.657  15.231  1.00110.35           N  
ANISOU 4091  N   ALA B 230     8612  19988  13329    133   1472   4828       N  
ATOM   4092  CA  ALA B 230       6.532   6.539  14.229  1.00108.51           C  
ANISOU 4092  CA  ALA B 230     8301  19882  13045     99   1423   4899       C  
ATOM   4093  C   ALA B 230       6.548   7.647  13.186  1.00102.71           C  
ANISOU 4093  C   ALA B 230     7527  19227  12272    115   1404   5014       C  
ATOM   4094  O   ALA B 230       6.027   7.441  12.085  1.00106.58           O  
ANISOU 4094  O   ALA B 230     7948  19864  12681     75   1357   5058       O  
ATOM   4095  CB  ALA B 230       5.151   6.512  14.903  1.00 99.51           C  
ANISOU 4095  CB  ALA B 230     7133  18710  11967    122   1419   4946       C  
ATOM   4096  N   ASP B 231       7.133   8.803  13.496  1.00 93.83           N  
ANISOU 4096  N   ASP B 231     6434  18013  11203    171   1442   5062       N  
ATOM   4097  CA  ASP B 231       7.143   9.919  12.559  1.00 99.82           C  
ANISOU 4097  CA  ASP B 231     7150  18829  11947    195   1433   5188       C  
ATOM   4098  C   ASP B 231       8.081   9.618  11.394  1.00115.00           C  
ANISOU 4098  C   ASP B 231     9065  20870  13761    147   1408   5163       C  
ATOM   4099  O   ASP B 231       9.234   9.224  11.597  1.00120.43           O  
ANISOU 4099  O   ASP B 231     9810  21514  14434    128   1429   5058       O  
ATOM   4100  CB  ASP B 231       7.567  11.201  13.276  1.00 91.05           C  
ANISOU 4100  CB  ASP B 231     6074  17572  10950    265   1495   5229       C  
ATOM   4101  CG  ASP B 231       7.328  12.447  12.441  1.00 90.10           C  
ANISOU 4101  CG  ASP B 231     5898  17484  10852    303   1498   5387       C  
ATOM   4102  OD1 ASP B 231       6.155  12.859  12.312  1.00 94.22           O  
ANISOU 4102  OD1 ASP B 231     6362  18033  11405    328   1483   5498       O  
ATOM   4103  OD2 ASP B 231       8.309  13.021  11.923  1.00 88.87           O  
ANISOU 4103  OD2 ASP B 231     5753  17325  10688    311   1519   5405       O  
ATOM   4104  N   ASP B 232       7.583   9.807  10.169  1.00123.74           N  
ANISOU 4104  N   ASP B 232    10096  22134  14784    128   1361   5261       N  
ATOM   4105  CA  ASP B 232       8.370   9.477   8.983  1.00133.79           C  
ANISOU 4105  CA  ASP B 232    11350  23549  15938     77   1331   5236       C  
ATOM   4106  C   ASP B 232       9.549  10.431   8.810  1.00130.24           C  
ANISOU 4106  C   ASP B 232    10937  23035  15512    113   1368   5272       C  
ATOM   4107  O   ASP B 232      10.680   9.997   8.550  1.00131.54           O  
ANISOU 4107  O   ASP B 232    11141  23214  15626     77   1374   5176       O  
ATOM   4108  CB  ASP B 232       7.475   9.497   7.744  1.00141.15           C  
ANISOU 4108  CB  ASP B 232    12180  24686  16765     51   1270   5339       C  
ATOM   4109  CG  ASP B 232       6.261   8.597   7.886  1.00145.40           C  
ANISOU 4109  CG  ASP B 232    12672  25289  17283     13   1236   5300       C  
ATOM   4110  OD1 ASP B 232       6.047   8.050   8.989  1.00147.02           O  
ANISOU 4110  OD1 ASP B 232    12925  25365  17570     15   1262   5214       O  
ATOM   4111  OD2 ASP B 232       5.521   8.439   6.893  1.00148.12           O  
ANISOU 4111  OD2 ASP B 232    12929  25819  17529    -19   1184   5355       O  
ATOM   4112  N   ASN B 233       9.299  11.739   8.939  1.00124.03           N  
ANISOU 4112  N   ASN B 233    10136  22176  14813    184   1399   5407       N  
ATOM   4113  CA  ASN B 233      10.382  12.713   8.839  1.00109.99           C  
ANISOU 4113  CA  ASN B 233     8389  20319  13084    222   1446   5440       C  
ATOM   4114  C   ASN B 233      11.430  12.476   9.919  1.00103.51           C  
ANISOU 4114  C   ASN B 233     7660  19342  12326    223   1499   5289       C  
ATOM   4115  O   ASN B 233      12.632  12.629   9.670  1.00 94.46           O  
ANISOU 4115  O   ASN B 233     6552  18178  11162    215   1521   5242       O  
ATOM   4116  CB  ASN B 233       9.829  14.137   8.929  1.00108.24           C  
ANISOU 4116  CB  ASN B 233     8128  20018  12979    299   1484   5604       C  
ATOM   4117  CG  ASN B 233       8.950  14.503   7.744  1.00108.83           C  
ANISOU 4117  CG  ASN B 233     8105  20260  12985    308   1435   5778       C  
ATOM   4118  OD1 ASN B 233       9.147  14.009   6.635  1.00105.67           O  
ANISOU 4118  OD1 ASN B 233     7666  20041  12442    262   1381   5789       O  
ATOM   4119  ND2 ASN B 233       7.978  15.380   7.975  1.00112.02           N  
ANISOU 4119  ND2 ASN B 233     8463  20610  13489    368   1454   5915       N  
ATOM   4120  N   PHE B 234      10.991  12.098  11.123  1.00106.25           N  
ANISOU 4120  N   PHE B 234     8043  19586  12743    234   1519   5214       N  
ATOM   4121  CA  PHE B 234      11.930  11.735  12.179  1.00103.31           C  
ANISOU 4121  CA  PHE B 234     7750  19091  12410    234   1562   5069       C  
ATOM   4122  C   PHE B 234      12.845  10.605  11.731  1.00 97.69           C  
ANISOU 4122  C   PHE B 234     7070  18455  11593    170   1535   4954       C  
ATOM   4123  O   PHE B 234      14.072  10.705  11.844  1.00106.31           O  
ANISOU 4123  O   PHE B 234     8212  19497  12684    169   1566   4882       O  
ATOM   4124  CB  PHE B 234      11.174  11.330  13.445  1.00107.37           C  
ANISOU 4124  CB  PHE B 234     8284  19521  12992    250   1575   5016       C  
ATOM   4125  CG  PHE B 234      11.150  12.389  14.507  1.00106.41           C  
ANISOU 4125  CG  PHE B 234     8181  19250  13001    313   1640   5025       C  
ATOM   4126  CD1 PHE B 234      11.592  13.673  14.237  1.00107.67           C  
ANISOU 4126  CD1 PHE B 234     8326  19352  13230    351   1685   5093       C  
ATOM   4127  CD2 PHE B 234      10.698  12.095  15.784  1.00102.25           C  
ANISOU 4127  CD2 PHE B 234     7678  18641  12532    331   1661   4958       C  
ATOM   4128  CE1 PHE B 234      11.572  14.647  15.216  1.00108.48           C  
ANISOU 4128  CE1 PHE B 234     8437  19316  13467    401   1753   5081       C  
ATOM   4129  CE2 PHE B 234      10.679  13.063  16.768  1.00101.41           C  
ANISOU 4129  CE2 PHE B 234     7579  18409  12541    382   1723   4948       C  
ATOM   4130  CZ  PHE B 234      11.117  14.341  16.483  1.00104.14           C  
ANISOU 4130  CZ  PHE B 234     7909  18696  12965    414   1772   5002       C  
ATOM   4131  N   VAL B 235      12.262   9.524  11.207  1.00 86.22           N  
ANISOU 4131  N   VAL B 235     5582  17122  10056    114   1483   4929       N  
ATOM   4132  CA  VAL B 235      13.056   8.365  10.808  1.00 87.00           C  
ANISOU 4132  CA  VAL B 235     5701  17285  10069     48   1465   4807       C  
ATOM   4133  C   VAL B 235      14.040   8.737   9.707  1.00 98.72           C  
ANISOU 4133  C   VAL B 235     7180  18851  11478     28   1456   4823       C  
ATOM   4134  O   VAL B 235      15.219   8.369   9.760  1.00 96.99           O  
ANISOU 4134  O   VAL B 235     7012  18602  11238      6   1476   4724       O  
ATOM   4135  CB  VAL B 235      12.134   7.207  10.379  1.00 86.32           C  
ANISOU 4135  CB  VAL B 235     5560  17315   9921    -12   1417   4775       C  
ATOM   4136  CG1 VAL B 235      12.951   6.067   9.789  1.00 86.19           C  
ANISOU 4136  CG1 VAL B 235     5550  17375   9825    -87   1404   4649       C  
ATOM   4137  CG2 VAL B 235      11.321   6.719  11.562  1.00 85.88           C  
ANISOU 4137  CG2 VAL B 235     5520  17163   9946      7   1432   4744       C  
ATOM   4138  N   LEU B 236      13.580   9.485   8.700  1.00106.57           N  
ANISOU 4138  N   LEU B 236     8109  19950  12430     37   1429   4955       N  
ATOM   4139  CA  LEU B 236      14.454   9.828   7.579  1.00102.36           C  
ANISOU 4139  CA  LEU B 236     7562  19513  11816     18   1418   4983       C  
ATOM   4140  C   LEU B 236      15.595  10.740   8.020  1.00 91.33           C  
ANISOU 4140  C   LEU B 236     6228  17979  10496     65   1477   4979       C  
ATOM   4141  O   LEU B 236      16.767  10.477   7.714  1.00 94.18           O  
ANISOU 4141  O   LEU B 236     6625  18348  10809     36   1486   4898       O  
ATOM   4142  CB  LEU B 236      13.640  10.477   6.460  1.00109.34           C  
ANISOU 4142  CB  LEU B 236     8355  20548  12640     28   1376   5145       C  
ATOM   4143  CG  LEU B 236      12.576   9.579   5.824  1.00110.50           C  
ANISOU 4143  CG  LEU B 236     8426  20870  12687    -28   1313   5139       C  
ATOM   4144  CD1 LEU B 236      11.884  10.288   4.670  1.00110.69           C  
ANISOU 4144  CD1 LEU B 236     8356  21065  12637    -13   1271   5308       C  
ATOM   4145  CD2 LEU B 236      13.188   8.264   5.363  1.00111.13           C  
ANISOU 4145  CD2 LEU B 236     8511  21047  12666   -118   1289   4975       C  
ATOM   4146  N   ILE B 237      15.272  11.827   8.728  1.00 87.17           N  
ANISOU 4146  N   ILE B 237     5707  17322  10092    136   1523   5060       N  
ATOM   4147  CA  ILE B 237      16.305  12.757   9.174  1.00 92.08           C  
ANISOU 4147  CA  ILE B 237     6377  17808  10801    178   1589   5047       C  
ATOM   4148  C   ILE B 237      17.279  12.061  10.114  1.00102.13           C  
ANISOU 4148  C   ILE B 237     7730  18988  12085    160   1618   4875       C  
ATOM   4149  O   ILE B 237      18.489  12.308  10.066  1.00 95.55           O  
ANISOU 4149  O   ILE B 237     6940  18113  11254    159   1650   4817       O  
ATOM   4150  CB  ILE B 237      15.667  13.996   9.828  1.00 87.12           C  
ANISOU 4150  CB  ILE B 237     5729  17054  10319    250   1640   5147       C  
ATOM   4151  CG1 ILE B 237      14.846  14.775   8.800  1.00 89.32           C  
ANISOU 4151  CG1 ILE B 237     5923  17424  10591    276   1616   5338       C  
ATOM   4152  CG2 ILE B 237      16.734  14.895  10.434  1.00 86.72           C  
ANISOU 4152  CG2 ILE B 237     5724  16852  10375    287   1719   5101       C  
ATOM   4153  CD1 ILE B 237      14.149  15.992   9.367  1.00 88.92           C  
ANISOU 4153  CD1 ILE B 237     5842  17246  10696    347   1671   5447       C  
ATOM   4154  N   GLY B 238      16.779  11.169  10.972  1.00104.98           N  
ANISOU 4154  N   GLY B 238     8112  19321  12454    147   1608   4794       N  
ATOM   4155  CA  GLY B 238      17.671  10.448  11.862  1.00109.59           C  
ANISOU 4155  CA  GLY B 238     8765  19830  13044    135   1633   4645       C  
ATOM   4156  C   GLY B 238      18.590   9.497  11.122  1.00106.58           C  
ANISOU 4156  C   GLY B 238     8402  19535  12559     73   1607   4559       C  
ATOM   4157  O   GLY B 238      19.788   9.438  11.405  1.00117.59           O  
ANISOU 4157  O   GLY B 238     9851  20875  13954     72   1638   4471       O  
ATOM   4158  N   SER B 239      18.049   8.750  10.156  1.00 93.12           N  
ANISOU 4158  N   SER B 239     6648  17971  10764     19   1552   4576       N  
ATOM   4159  CA  SER B 239      18.876   7.823   9.392  1.00 90.78           C  
ANISOU 4159  CA  SER B 239     6357  17764  10372    -48   1530   4484       C  
ATOM   4160  C   SER B 239      19.923   8.555   8.566  1.00 96.84           C  
ANISOU 4160  C   SER B 239     7134  18564  11098    -48   1540   4509       C  
ATOM   4161  O   SER B 239      21.015   8.022   8.335  1.00 96.38           O  
ANISOU 4161  O   SER B 239     7110  18516  10993    -84   1546   4410       O  
ATOM   4162  CB  SER B 239      18.002   6.950   8.494  1.00 85.29           C  
ANISOU 4162  CB  SER B 239     5591  17225   9591   -111   1474   4488       C  
ATOM   4163  OG  SER B 239      17.046   6.238   9.259  1.00 87.26           O  
ANISOU 4163  OG  SER B 239     5831  17437   9888   -113   1470   4461       O  
ATOM   4164  N   PHE B 240      19.623   9.773   8.113  1.00 91.88           N  
ANISOU 4164  N   PHE B 240     6471  17946  10492     -6   1544   4645       N  
ATOM   4165  CA  PHE B 240      20.634  10.493   7.347  1.00 90.98           C  
ANISOU 4165  CA  PHE B 240     6363  17854  10350     -2   1560   4677       C  
ATOM   4166  C   PHE B 240      21.662  11.166   8.251  1.00 96.79           C  
ANISOU 4166  C   PHE B 240     7168  18424  11183     42   1628   4623       C  
ATOM   4167  O   PHE B 240      22.870  10.990   8.062  1.00109.89           O  
ANISOU 4167  O   PHE B 240     8869  20076  12809     20   1644   4540       O  
ATOM   4168  CB  PHE B 240      19.975  11.515   6.421  1.00 90.52           C  
ANISOU 4168  CB  PHE B 240     6232  17878  10282     27   1542   4854       C  
ATOM   4169  CG  PHE B 240      19.728  10.997   5.033  1.00 96.74           C  
ANISOU 4169  CG  PHE B 240     6954  18882  10923    -30   1477   4889       C  
ATOM   4170  CD1 PHE B 240      20.747  10.996   4.092  1.00 91.39           C  
ANISOU 4170  CD1 PHE B 240     6276  18290  10158    -63   1469   4869       C  
ATOM   4171  CD2 PHE B 240      18.485  10.509   4.666  1.00103.01           C  
ANISOU 4171  CD2 PHE B 240     7679  19800  11661    -54   1424   4934       C  
ATOM   4172  CE1 PHE B 240      20.529  10.520   2.813  1.00 92.28           C  
ANISOU 4172  CE1 PHE B 240     6318  18619  10125   -119   1408   4889       C  
ATOM   4173  CE2 PHE B 240      18.260  10.033   3.386  1.00101.26           C  
ANISOU 4173  CE2 PHE B 240     7385  19796  11295   -112   1365   4951       C  
ATOM   4174  CZ  PHE B 240      19.284  10.038   2.459  1.00 99.23           C  
ANISOU 4174  CZ  PHE B 240     7125  19632  10946   -145   1356   4927       C  
ATOM   4175  N   VAL B 241      21.209  11.924   9.251  1.00 91.97           N  
ANISOU 4175  N   VAL B 241     6566  17684  10693    101   1672   4657       N  
ATOM   4176  CA  VAL B 241      22.131  12.712  10.062  1.00 94.82           C  
ANISOU 4176  CA  VAL B 241     6976  17900  11151    142   1743   4604       C  
ATOM   4177  C   VAL B 241      22.949  11.817  10.988  1.00101.66           C  
ANISOU 4177  C   VAL B 241     7910  18711  12004    124   1758   4439       C  
ATOM   4178  O   VAL B 241      24.140  12.064  11.218  1.00114.39           O  
ANISOU 4178  O   VAL B 241     9567  20265  13631    128   1798   4361       O  
ATOM   4179  CB  VAL B 241      21.354  13.790  10.840  1.00 93.24           C  
ANISOU 4179  CB  VAL B 241     6752  17587  11087    205   1790   4678       C  
ATOM   4180  CG1 VAL B 241      22.248  14.479  11.860  1.00 84.82           C  
ANISOU 4180  CG1 VAL B 241     5730  16374  10125    239   1869   4587       C  
ATOM   4181  CG2 VAL B 241      20.764  14.807   9.872  1.00 92.79           C  
ANISOU 4181  CG2 VAL B 241     6627  17571  11058    231   1789   4854       C  
ATOM   4182  N   SER B 242      22.343  10.753  11.512  1.00 88.54           N  
ANISOU 4182  N   SER B 242     6254  17070  10316    105   1727   4388       N  
ATOM   4183  CA  SER B 242      22.981   9.936  12.533  1.00 91.20           C  
ANISOU 4183  CA  SER B 242     6648  17347  10657    101   1745   4253       C  
ATOM   4184  C   SER B 242      23.511   8.605  12.015  1.00 98.75           C  
ANISOU 4184  C   SER B 242     7619  18383  11518     40   1710   4171       C  
ATOM   4185  O   SER B 242      24.253   7.935  12.739  1.00105.01           O  
ANISOU 4185  O   SER B 242     8459  19129  12313     38   1729   4065       O  
ATOM   4186  CB  SER B 242      21.999   9.676  13.683  1.00 92.16           C  
ANISOU 4186  CB  SER B 242     6766  17414  10837    131   1749   4250       C  
ATOM   4187  OG  SER B 242      21.625  10.886  14.317  1.00 96.30           O  
ANISOU 4187  OG  SER B 242     7277  17851  11460    186   1793   4298       O  
ATOM   4188  N   PHE B 243      23.151   8.195  10.800  1.00102.38           N  
ANISOU 4188  N   PHE B 243     8034  18967  11899    -10   1662   4213       N  
ATOM   4189  CA  PHE B 243      23.629   6.911  10.295  1.00100.82           C  
ANISOU 4189  CA  PHE B 243     7840  18844  11624    -76   1637   4119       C  
ATOM   4190  C   PHE B 243      24.326   7.030   8.943  1.00101.30           C  
ANISOU 4190  C   PHE B 243     7883  19012  11596   -122   1616   4123       C  
ATOM   4191  O   PHE B 243      25.481   6.617   8.802  1.00101.14           O  
ANISOU 4191  O   PHE B 243     7900  18985  11543   -148   1630   4030       O  
ATOM   4192  CB  PHE B 243      22.464   5.923  10.207  1.00 82.27           C  
ANISOU 4192  CB  PHE B 243     5442  16558   9257   -112   1600   4121       C  
ATOM   4193  CG  PHE B 243      22.881   4.512   9.913  1.00 82.16           C  
ANISOU 4193  CG  PHE B 243     5426  16592   9199   -178   1590   4007       C  
ATOM   4194  CD1 PHE B 243      23.513   3.746  10.877  1.00 81.43           C  
ANISOU 4194  CD1 PHE B 243     5383  16406   9153   -169   1623   3913       C  
ATOM   4195  CD2 PHE B 243      22.613   3.942   8.682  1.00 82.90           C  
ANISOU 4195  CD2 PHE B 243     5459  16828   9210   -250   1551   3993       C  
ATOM   4196  CE1 PHE B 243      23.884   2.441  10.612  1.00 81.44           C  
ANISOU 4196  CE1 PHE B 243     5373  16436   9134   -228   1624   3813       C  
ATOM   4197  CE2 PHE B 243      22.980   2.639   8.410  1.00 82.91           C  
ANISOU 4197  CE2 PHE B 243     5447  16866   9188   -316   1551   3875       C  
ATOM   4198  CZ  PHE B 243      23.617   1.888   9.376  1.00 82.17           C  
ANISOU 4198  CZ  PHE B 243     5404  16659   9159   -304   1591   3788       C  
ATOM   4199  N   PHE B 244      23.645   7.602   7.947  1.00106.27           N  
ANISOU 4199  N   PHE B 244     8451  19744  12180   -129   1583   4233       N  
ATOM   4200  CA  PHE B 244      24.161   7.556   6.582  1.00105.24           C  
ANISOU 4200  CA  PHE B 244     8289  19752  11945   -180   1554   4239       C  
ATOM   4201  C   PHE B 244      25.367   8.472   6.405  1.00101.72           C  
ANISOU 4201  C   PHE B 244     7885  19253  11511   -153   1590   4249       C  
ATOM   4202  O   PHE B 244      26.418   8.042   5.909  1.00105.29           O  
ANISOU 4202  O   PHE B 244     8359  19743  11902   -194   1591   4164       O  
ATOM   4203  CB  PHE B 244      23.056   7.929   5.595  1.00106.51           C  
ANISOU 4203  CB  PHE B 244     8365  20055  12048   -189   1506   4367       C  
ATOM   4204  CG  PHE B 244      21.935   6.932   5.534  1.00105.32           C  
ANISOU 4204  CG  PHE B 244     8163  19988  11867   -232   1467   4340       C  
ATOM   4205  CD1 PHE B 244      22.190   5.576   5.665  1.00100.69           C  
ANISOU 4205  CD1 PHE B 244     7585  19415  11258   -294   1464   4194       C  
ATOM   4206  CD2 PHE B 244      20.629   7.350   5.336  1.00102.53           C  
ANISOU 4206  CD2 PHE B 244     7746  19695  11515   -211   1437   4461       C  
ATOM   4207  CE1 PHE B 244      21.163   4.655   5.606  1.00 98.00           C  
ANISOU 4207  CE1 PHE B 244     7190  19142  10905   -337   1436   4162       C  
ATOM   4208  CE2 PHE B 244      19.597   6.434   5.277  1.00102.09           C  
ANISOU 4208  CE2 PHE B 244     7640  19717  11434   -253   1404   4428       C  
ATOM   4209  CZ  PHE B 244      19.865   5.084   5.412  1.00101.78           C  
ANISOU 4209  CZ  PHE B 244     7608  19686  11379   -318   1405   4275       C  
ATOM   4210  N   ILE B 245      25.230   9.743   6.793  1.00 96.64           N  
ANISOU 4210  N   ILE B 245     7247  18519  10954    -85   1626   4347       N  
ATOM   4211  CA  ILE B 245      26.320  10.702   6.596  1.00 94.55           C  
ANISOU 4211  CA  ILE B 245     7011  18197  10718    -59   1669   4362       C  
ATOM   4212  C   ILE B 245      27.587  10.298   7.342  1.00 99.30           C  
ANISOU 4212  C   ILE B 245     7689  18702  11340    -65   1708   4214       C  
ATOM   4213  O   ILE B 245      28.664  10.284   6.719  1.00105.93           O  
ANISOU 4213  O   ILE B 245     8548  19573  12127    -91   1714   4169       O  
ATOM   4214  CB  ILE B 245      25.845  12.123   6.952  1.00 88.95           C  
ANISOU 4214  CB  ILE B 245     6281  17392  10124     13   1712   4488       C  
ATOM   4215  CG1 ILE B 245      24.724  12.560   6.005  1.00 87.77           C  
ANISOU 4215  CG1 ILE B 245     6049  17358   9942     21   1671   4654       C  
ATOM   4216  CG2 ILE B 245      27.010  13.101   6.913  1.00 86.18           C  
ANISOU 4216  CG2 ILE B 245     5960  16954   9830     41   1772   4485       C  
ATOM   4217  CD1 ILE B 245      24.184  13.943   6.294  1.00 88.27           C  
ANISOU 4217  CD1 ILE B 245     6082  17323  10133     93   1718   4791       C  
ATOM   4218  N   PRO B 246      27.553   9.985   8.643  1.00 97.55           N  
ANISOU 4218  N   PRO B 246     7507  18369  11186    -39   1736   4137       N  
ATOM   4219  CA  PRO B 246      28.791   9.536   9.298  1.00 98.87           C  
ANISOU 4219  CA  PRO B 246     7740  18467  11358    -44   1768   4000       C  
ATOM   4220  C   PRO B 246      29.345   8.258   8.698  1.00105.16           C  
ANISOU 4220  C   PRO B 246     8546  19351  12059   -111   1734   3908       C  
ATOM   4221  O   PRO B 246      30.569   8.093   8.646  1.00105.14           O  
ANISOU 4221  O   PRO B 246     8585  19328  12033   -125   1755   3822       O  
ATOM   4222  CB  PRO B 246      28.368   9.340  10.762  1.00 97.20           C  
ANISOU 4222  CB  PRO B 246     7552  18155  11224     -3   1792   3955       C  
ATOM   4223  CG  PRO B 246      27.113  10.123  10.918  1.00 96.06           C  
ANISOU 4223  CG  PRO B 246     7363  17994  11142     35   1791   4072       C  
ATOM   4224  CD  PRO B 246      26.428  10.034   9.597  1.00 98.39           C  
ANISOU 4224  CD  PRO B 246     7600  18417  11365     -1   1739   4171       C  
ATOM   4225  N   LEU B 247      28.480   7.355   8.229  1.00107.31           N  
ANISOU 4225  N   LEU B 247     8775  19719  12280   -155   1687   3917       N  
ATOM   4226  CA  LEU B 247      28.949   6.134   7.578  1.00104.33           C  
ANISOU 4226  CA  LEU B 247     8391  19428  11823   -227   1663   3820       C  
ATOM   4227  C   LEU B 247      29.761   6.454   6.328  1.00102.72           C  
ANISOU 4227  C   LEU B 247     8176  19317  11534   -265   1651   3822       C  
ATOM   4228  O   LEU B 247      30.871   5.934   6.140  1.00101.12           O  
ANISOU 4228  O   LEU B 247     8007  19117  11299   -298   1663   3720       O  
ATOM   4229  CB  LEU B 247      27.757   5.240   7.236  1.00102.07           C  
ANISOU 4229  CB  LEU B 247     8043  19232  11506   -270   1621   3830       C  
ATOM   4230  CG  LEU B 247      27.914   4.172   6.153  1.00103.29           C  
ANISOU 4230  CG  LEU B 247     8154  19522  11571   -359   1590   3750       C  
ATOM   4231  CD1 LEU B 247      28.959   3.141   6.543  1.00108.09           C  
ANISOU 4231  CD1 LEU B 247     8804  20071  12194   -388   1619   3609       C  
ATOM   4232  CD2 LEU B 247      26.573   3.504   5.894  1.00102.23           C  
ANISOU 4232  CD2 LEU B 247     7947  19472  11423   -395   1554   3768       C  
ATOM   4233  N   THR B 248      29.218   7.308   5.456  1.00101.87           N  
ANISOU 4233  N   THR B 248     8019  19295  11393   -258   1627   3944       N  
ATOM   4234  CA  THR B 248      29.943   7.675   4.243  1.00 96.32           C  
ANISOU 4234  CA  THR B 248     7299  18693  10604   -289   1614   3964       C  
ATOM   4235  C   THR B 248      31.243   8.391   4.576  1.00 89.22           C  
ANISOU 4235  C   THR B 248     6464  17685   9751   -255   1666   3933       C  
ATOM   4236  O   THR B 248      32.283   8.121   3.959  1.00 84.23           O  
ANISOU 4236  O   THR B 248     5850  17098   9056   -295   1667   3863       O  
ATOM   4237  CB  THR B 248      29.073   8.549   3.342  1.00 96.87           C  
ANISOU 4237  CB  THR B 248     7298  18870  10639   -273   1583   4125       C  
ATOM   4238  OG1 THR B 248      28.810   9.797   3.996  1.00 97.29           O  
ANISOU 4238  OG1 THR B 248     7363  18798  10802   -193   1624   4234       O  
ATOM   4239  CG2 THR B 248      27.758   7.848   3.033  1.00 94.38           C  
ANISOU 4239  CG2 THR B 248     6913  18672  10274   -308   1532   4149       C  
ATOM   4240  N   ILE B 249      31.205   9.316   5.541  1.00 82.30           N  
ANISOU 4240  N   ILE B 249     5617  16667   8984   -185   1713   3976       N  
ATOM   4241  CA  ILE B 249      32.423  10.034   5.911  1.00 81.83           C  
ANISOU 4241  CA  ILE B 249     5612  16503   8978   -155   1769   3934       C  
ATOM   4242  C   ILE B 249      33.476   9.062   6.426  1.00 91.09           C  
ANISOU 4242  C   ILE B 249     6843  17638  10129   -183   1781   3774       C  
ATOM   4243  O   ILE B 249      34.661   9.174   6.087  1.00 91.42           O  
ANISOU 4243  O   ILE B 249     6917  17674  10145   -198   1801   3715       O  
ATOM   4244  CB  ILE B 249      32.119  11.138   6.940  1.00 81.68           C  
ANISOU 4244  CB  ILE B 249     5603  16343   9090    -81   1823   3986       C  
ATOM   4245  CG1 ILE B 249      31.162  12.172   6.347  1.00 82.67           C  
ANISOU 4245  CG1 ILE B 249     5664  16497   9249    -50   1819   4156       C  
ATOM   4246  CG2 ILE B 249      33.402  11.822   7.370  1.00 81.25           C  
ANISOU 4246  CG2 ILE B 249     5596  16183   9093    -57   1887   3918       C  
ATOM   4247  CD1 ILE B 249      30.868  13.332   7.275  1.00 82.68           C  
ANISOU 4247  CD1 ILE B 249     5664  16354   9396     18   1883   4204       C  
ATOM   4248  N   MET B 250      33.062   8.080   7.232  1.00 94.34           N  
ANISOU 4248  N   MET B 250     7266  18023  10556   -189   1771   3707       N  
ATOM   4249  CA  MET B 250      34.015   7.111   7.760  1.00 98.91           C  
ANISOU 4249  CA  MET B 250     7893  18564  11124   -208   1786   3570       C  
ATOM   4250  C   MET B 250      34.615   6.266   6.648  1.00 96.62           C  
ANISOU 4250  C   MET B 250     7591  18381  10738   -283   1758   3506       C  
ATOM   4251  O   MET B 250      35.824   6.024   6.636  1.00103.02           O  
ANISOU 4251  O   MET B 250     8443  19168  11532   -297   1779   3415       O  
ATOM   4252  CB  MET B 250      33.349   6.198   8.785  1.00 99.10           C  
ANISOU 4252  CB  MET B 250     7920  18545  11190   -197   1782   3533       C  
ATOM   4253  CG  MET B 250      33.130   6.806  10.145  1.00 95.68           C  
ANISOU 4253  CG  MET B 250     7513  17997  10846   -125   1818   3546       C  
ATOM   4254  SD  MET B 250      32.465   5.558  11.256  1.00 93.27           S  
ANISOU 4254  SD  MET B 250     7208  17658  10574   -116   1811   3503       S  
ATOM   4255  CE  MET B 250      31.017   5.040  10.344  1.00 95.98           C  
ANISOU 4255  CE  MET B 250     7481  18104  10884   -163   1758   3580       C  
ATOM   4256  N   VAL B 251      33.786   5.803   5.709  1.00 91.51           N  
ANISOU 4256  N   VAL B 251     6883  17860  10027   -333   1711   3543       N  
ATOM   4257  CA  VAL B 251      34.302   5.001   4.601  1.00 91.03           C  
ANISOU 4257  CA  VAL B 251     6798  17919   9872   -412   1687   3468       C  
ATOM   4258  C   VAL B 251      35.325   5.797   3.797  1.00 96.86           C  
ANISOU 4258  C   VAL B 251     7552  18690  10559   -416   1695   3482       C  
ATOM   4259  O   VAL B 251      36.434   5.318   3.510  1.00 90.65           O  
ANISOU 4259  O   VAL B 251     6794  17912   9737   -453   1707   3379       O  
ATOM   4260  CB  VAL B 251      33.146   4.503   3.716  1.00 86.75           C  
ANISOU 4260  CB  VAL B 251     6172  17524   9263   -465   1636   3504       C  
ATOM   4261  CG1 VAL B 251      33.687   3.854   2.450  1.00 82.60           C  
ANISOU 4261  CG1 VAL B 251     5609  17145   8630   -550   1611   3424       C  
ATOM   4262  CG2 VAL B 251      32.281   3.524   4.489  1.00 91.38           C  
ANISOU 4262  CG2 VAL B 251     6743  18071   9907   -471   1635   3465       C  
ATOM   4263  N   ILE B 252      34.965   7.027   3.418  1.00 94.62           N  
ANISOU 4263  N   ILE B 252     7248  18423  10280   -378   1693   3614       N  
ATOM   4264  CA  ILE B 252      35.860   7.849   2.606  1.00 87.45           C  
ANISOU 4264  CA  ILE B 252     6347  17548   9334   -378   1705   3647       C  
ATOM   4265  C   ILE B 252      37.171   8.094   3.343  1.00 83.93           C  
ANISOU 4265  C   ILE B 252     5977  16967   8946   -350   1760   3560       C  
ATOM   4266  O   ILE B 252      38.262   7.907   2.788  1.00 94.25           O  
ANISOU 4266  O   ILE B 252     7306  18304  10200   -385   1766   3489       O  
ATOM   4267  CB  ILE B 252      35.172   9.172   2.220  1.00 87.08           C  
ANISOU 4267  CB  ILE B 252     6259  17516   9314   -328   1705   3822       C  
ATOM   4268  CG1 ILE B 252      33.925   8.902   1.374  1.00 94.76           C  
ANISOU 4268  CG1 ILE B 252     7148  18650  10207   -358   1645   3909       C  
ATOM   4269  CG2 ILE B 252      36.136  10.081   1.476  1.00 84.44           C  
ANISOU 4269  CG2 ILE B 252     5931  17193   8961   -319   1729   3867       C  
ATOM   4270  CD1 ILE B 252      33.217  10.157   0.900  1.00 88.92           C  
ANISOU 4270  CD1 ILE B 252     6355  17941   9489   -306   1642   4098       C  
ATOM   4271  N   THR B 253      37.082   8.505   4.610  1.00 80.63           N  
ANISOU 4271  N   THR B 253     5596  16407   8634   -290   1800   3558       N  
ATOM   4272  CA  THR B 253      38.284   8.814   5.374  1.00 83.48           C  
ANISOU 4272  CA  THR B 253     6019  16649   9048   -260   1854   3472       C  
ATOM   4273  C   THR B 253      39.145   7.573   5.580  1.00 89.58           C  
ANISOU 4273  C   THR B 253     6829  17426   9780   -301   1850   3327       C  
ATOM   4274  O   THR B 253      40.377   7.642   5.498  1.00 89.88           O  
ANISOU 4274  O   THR B 253     6907  17438   9806   -309   1876   3251       O  
ATOM   4275  CB  THR B 253      37.892   9.437   6.716  1.00 79.49           C  
ANISOU 4275  CB  THR B 253     5531  16014   8656   -192   1895   3488       C  
ATOM   4276  OG1 THR B 253      37.045  10.570   6.490  1.00 80.15           O  
ANISOU 4276  OG1 THR B 253     5573  16089   8793   -156   1904   3626       O  
ATOM   4277  CG2 THR B 253      39.108   9.892   7.463  1.00 78.89           C  
ANISOU 4277  CG2 THR B 253     5508  15835   8633   -162   1952   3398       C  
ATOM   4278  N   TYR B 254      38.511   6.418   5.799  1.00 84.07           N  
ANISOU 4278  N   TYR B 254     6114  16761   9067   -329   1821   3288       N  
ATOM   4279  CA  TYR B 254      39.249   5.176   6.000  1.00 90.96           C  
ANISOU 4279  CA  TYR B 254     7011  17630   9920   -366   1825   3160       C  
ATOM   4280  C   TYR B 254      40.018   4.782   4.745  1.00105.37           C  
ANISOU 4280  C   TYR B 254     8824  19557  11656   -436   1808   3103       C  
ATOM   4281  O   TYR B 254      41.190   4.388   4.818  1.00104.63           O  
ANISOU 4281  O   TYR B 254     8769  19432  11553   -451   1831   3003       O  
ATOM   4282  CB  TYR B 254      38.283   4.069   6.413  1.00 78.78           C  
ANISOU 4282  CB  TYR B 254     5437  16099   8398   -382   1805   3145       C  
ATOM   4283  CG  TYR B 254      38.941   2.754   6.750  1.00 78.41           C  
ANISOU 4283  CG  TYR B 254     5405  16027   8361   -411   1820   3026       C  
ATOM   4284  CD1 TYR B 254      39.471   2.529   8.013  1.00 77.71           C  
ANISOU 4284  CD1 TYR B 254     5363  15829   8336   -359   1855   2982       C  
ATOM   4285  CD2 TYR B 254      39.021   1.731   5.812  1.00 78.87           C  
ANISOU 4285  CD2 TYR B 254     5422  16175   8369   -491   1803   2957       C  
ATOM   4286  CE1 TYR B 254      40.067   1.327   8.335  1.00 78.72           C  
ANISOU 4286  CE1 TYR B 254     5498  15930   8484   -378   1874   2891       C  
ATOM   4287  CE2 TYR B 254      39.617   0.522   6.125  1.00 82.12           C  
ANISOU 4287  CE2 TYR B 254     5840  16551   8813   -517   1827   2850       C  
ATOM   4288  CZ  TYR B 254      40.140   0.326   7.389  1.00 85.87           C  
ANISOU 4288  CZ  TYR B 254     6362  16909   9357   -457   1863   2827       C  
ATOM   4289  OH  TYR B 254      40.736  -0.873   7.713  1.00 89.38           O  
ANISOU 4289  OH  TYR B 254     6805  17313   9842   -475   1892   2739       O  
ATOM   4290  N   PHE B 255      39.367   4.864   3.580  1.00108.09           N  
ANISOU 4290  N   PHE B 255     9110  20032  11928   -481   1768   3162       N  
ATOM   4291  CA  PHE B 255      40.064   4.505   2.346  1.00108.98           C  
ANISOU 4291  CA  PHE B 255     9203  20261  11944   -551   1749   3103       C  
ATOM   4292  C   PHE B 255      41.179   5.494   2.023  1.00 96.45           C  
ANISOU 4292  C   PHE B 255     7656  18647  10343   -530   1775   3118       C  
ATOM   4293  O   PHE B 255      42.266   5.088   1.588  1.00 92.94           O  
ANISOU 4293  O   PHE B 255     7234  18225   9855   -570   1784   3021       O  
ATOM   4294  CB  PHE B 255      39.075   4.388   1.190  1.00117.11           C  
ANISOU 4294  CB  PHE B 255    10151  21460  12887   -602   1697   3163       C  
ATOM   4295  CG  PHE B 255      38.366   3.067   1.145  1.00126.57           C  
ANISOU 4295  CG  PHE B 255    11299  22716  14076   -661   1677   3084       C  
ATOM   4296  CD1 PHE B 255      38.873   2.026   0.382  1.00130.53           C  
ANISOU 4296  CD1 PHE B 255    11769  23309  14517   -745   1669   2953       C  
ATOM   4297  CD2 PHE B 255      37.210   2.854   1.879  1.00126.53           C  
ANISOU 4297  CD2 PHE B 255    11274  22668  14133   -633   1671   3132       C  
ATOM   4298  CE1 PHE B 255      38.232   0.802   0.341  1.00135.39           C  
ANISOU 4298  CE1 PHE B 255    12329  23967  15145   -803   1662   2868       C  
ATOM   4299  CE2 PHE B 255      36.563   1.633   1.841  1.00128.52           C  
ANISOU 4299  CE2 PHE B 255    11476  22964  14392   -687   1660   3056       C  
ATOM   4300  CZ  PHE B 255      37.075   0.605   1.071  1.00133.63           C  
ANISOU 4300  CZ  PHE B 255    12087  23697  14990   -774   1658   2922       C  
ATOM   4301  N   LEU B 256      40.945   6.791   2.240  1.00 88.93           N  
ANISOU 4301  N   LEU B 256     6710  17640   9438   -468   1793   3235       N  
ATOM   4302  CA  LEU B 256      42.026   7.753   2.048  1.00 81.53           C  
ANISOU 4302  CA  LEU B 256     5810  16655   8513   -444   1830   3244       C  
ATOM   4303  C   LEU B 256      43.194   7.454   2.983  1.00 86.47           C  
ANISOU 4303  C   LEU B 256     6505  17163   9189   -428   1874   3117       C  
ATOM   4304  O   LEU B 256      44.363   7.587   2.594  1.00 81.92           O  
ANISOU 4304  O   LEU B 256     5958  16583   8583   -445   1893   3057       O  
ATOM   4305  CB  LEU B 256      41.513   9.175   2.264  1.00 80.67           C  
ANISOU 4305  CB  LEU B 256     5688  16484   8480   -377   1856   3385       C  
ATOM   4306  CG  LEU B 256      40.474   9.699   1.273  1.00 82.75           C  
ANISOU 4306  CG  LEU B 256     5878  16864   8698   -381   1818   3537       C  
ATOM   4307  CD1 LEU B 256      40.142  11.150   1.579  1.00 86.82           C  
ANISOU 4307  CD1 LEU B 256     6383  17287   9318   -308   1862   3672       C  
ATOM   4308  CD2 LEU B 256      40.965   9.543  -0.157  1.00 94.49           C  
ANISOU 4308  CD2 LEU B 256     7333  18505  10063   -438   1785   3542       C  
ATOM   4309  N   THR B 257      42.897   7.003   4.207  1.00 80.46           N  
ANISOU 4309  N   THR B 257     5766  16311   8494   -395   1888   3075       N  
ATOM   4310  CA  THR B 257      43.955   6.698   5.165  1.00 85.51           C  
ANISOU 4310  CA  THR B 257     6463  16853   9174   -372   1926   2963       C  
ATOM   4311  C   THR B 257      44.750   5.461   4.753  1.00 91.74           C  
ANISOU 4311  C   THR B 257     7263  17690   9905   -432   1914   2845       C  
ATOM   4312  O   THR B 257      45.985   5.454   4.846  1.00 90.24           O  
ANISOU 4312  O   THR B 257     7115  17462   9710   -433   1941   2762       O  
ATOM   4313  CB  THR B 257      43.356   6.518   6.560  1.00 82.72           C  
ANISOU 4313  CB  THR B 257     6120  16412   8898   -318   1940   2961       C  
ATOM   4314  OG1 THR B 257      42.787   7.759   6.997  1.00 81.12           O  
ANISOU 4314  OG1 THR B 257     5907  16152   8761   -263   1963   3050       O  
ATOM   4315  CG2 THR B 257      44.421   6.076   7.555  1.00 81.83           C  
ANISOU 4315  CG2 THR B 257     6056  16221   8812   -294   1973   2847       C  
ATOM   4316  N   ILE B 258      44.068   4.404   4.300  1.00 90.97           N  
ANISOU 4316  N   ILE B 258     7122  17671   9770   -483   1879   2829       N  
ATOM   4317  CA  ILE B 258      44.801   3.218   3.861  1.00 89.06           C  
ANISOU 4317  CA  ILE B 258     6879  17471   9489   -546   1877   2710       C  
ATOM   4318  C   ILE B 258      45.645   3.544   2.635  1.00 96.83           C  
ANISOU 4318  C   ILE B 258     7862  18539  10390   -595   1869   2683       C  
ATOM   4319  O   ILE B 258      46.773   3.053   2.493  1.00 94.35           O  
ANISOU 4319  O   ILE B 258     7575  18214  10059   -622   1887   2579       O  
ATOM   4320  CB  ILE B 258      43.851   2.029   3.602  1.00 78.50           C  
ANISOU 4320  CB  ILE B 258     5482  16199   8144   -597   1850   2687       C  
ATOM   4321  CG1 ILE B 258      43.028   2.227   2.330  1.00 81.71           C  
ANISOU 4321  CG1 ILE B 258     5823  16754   8468   -652   1805   2744       C  
ATOM   4322  CG2 ILE B 258      42.952   1.793   4.799  1.00 79.88           C  
ANISOU 4322  CG2 ILE B 258     5656  16292   8402   -544   1858   2731       C  
ATOM   4323  CD1 ILE B 258      42.140   1.053   1.984  1.00 90.73           C  
ANISOU 4323  CD1 ILE B 258     6897  17974   9603   -714   1783   2698       C  
ATOM   4324  N   LYS B 259      45.134   4.409   1.750  1.00 99.82           N  
ANISOU 4324  N   LYS B 259     8207  19002  10717   -602   1844   2784       N  
ATOM   4325  CA  LYS B 259      45.913   4.813   0.583  1.00 98.38           C  
ANISOU 4325  CA  LYS B 259     8019  18906  10453   -642   1837   2776       C  
ATOM   4326  C   LYS B 259      47.160   5.585   0.998  1.00 93.29           C  
ANISOU 4326  C   LYS B 259     7440  18157   9848   -600   1883   2750       C  
ATOM   4327  O   LYS B 259      48.259   5.338   0.481  1.00 90.00           O  
ANISOU 4327  O   LYS B 259     7045  17765   9387   -637   1892   2665       O  
ATOM   4328  CB  LYS B 259      45.041   5.647  -0.356  1.00 98.99           C  
ANISOU 4328  CB  LYS B 259     8041  19095  10476   -644   1803   2915       C  
ATOM   4329  CG  LYS B 259      45.683   5.979  -1.693  1.00101.38           C  
ANISOU 4329  CG  LYS B 259     8321  19520  10677   -689   1786   2922       C  
ATOM   4330  CD  LYS B 259      44.733   6.781  -2.570  1.00 99.82           C  
ANISOU 4330  CD  LYS B 259     8057  19444  10426   -681   1751   3079       C  
ATOM   4331  CE  LYS B 259      44.346   8.099  -1.914  1.00100.04           C  
ANISOU 4331  CE  LYS B 259     8102  19354  10555   -593   1784   3222       C  
ATOM   4332  NZ  LYS B 259      43.400   8.893  -2.751  1.00101.64           N  
ANISOU 4332  NZ  LYS B 259     8234  19668  10717   -577   1753   3393       N  
ATOM   4333  N   SER B 260      47.011   6.516   1.945  1.00 86.40           N  
ANISOU 4333  N   SER B 260     6596  17170   9063   -525   1916   2814       N  
ATOM   4334  CA  SER B 260      48.162   7.280   2.412  1.00 84.33           C  
ANISOU 4334  CA  SER B 260     6388  16808   8848   -487   1967   2776       C  
ATOM   4335  C   SER B 260      49.191   6.376   3.080  1.00 83.14           C  
ANISOU 4335  C   SER B 260     6283  16601   8706   -495   1986   2632       C  
ATOM   4336  O   SER B 260      50.398   6.543   2.873  1.00 90.49           O  
ANISOU 4336  O   SER B 260     7249  17513   9622   -504   2011   2563       O  
ATOM   4337  CB  SER B 260      47.709   8.376   3.375  1.00 84.34           C  
ANISOU 4337  CB  SER B 260     6395  16700   8950   -412   2005   2852       C  
ATOM   4338  OG  SER B 260      46.837   9.288   2.731  1.00 85.81           O  
ANISOU 4338  OG  SER B 260     6535  16928   9141   -399   1995   2996       O  
ATOM   4339  N   LEU B 261      48.735   5.402   3.871  1.00 84.12           N  
ANISOU 4339  N   LEU B 261     6405  16699   8858   -488   1977   2591       N  
ATOM   4340  CA  LEU B 261      49.677   4.505   4.538  1.00 87.66           C  
ANISOU 4340  CA  LEU B 261     6889  17094   9323   -488   1998   2471       C  
ATOM   4341  C   LEU B 261      50.401   3.608   3.539  1.00 85.26           C  
ANISOU 4341  C   LEU B 261     6577  16867   8952   -563   1985   2381       C  
ATOM   4342  O   LEU B 261      51.606   3.357   3.682  1.00 84.39           O  
ANISOU 4342  O   LEU B 261     6504  16721   8840   -567   2010   2289       O  
ATOM   4343  CB  LEU B 261      48.953   3.663   5.587  1.00 94.88           C  
ANISOU 4343  CB  LEU B 261     7793  17965  10291   -460   1995   2468       C  
ATOM   4344  CG  LEU B 261      48.396   4.408   6.802  1.00 97.50           C  
ANISOU 4344  CG  LEU B 261     8137  18216  10692   -382   2013   2527       C  
ATOM   4345  CD1 LEU B 261      47.717   3.433   7.745  1.00105.56           C  
ANISOU 4345  CD1 LEU B 261     9144  19208  11756   -359   2007   2524       C  
ATOM   4346  CD2 LEU B 261      49.489   5.182   7.524  1.00 90.63           C  
ANISOU 4346  CD2 LEU B 261     7312  17270   9852   -335   2055   2474       C  
ATOM   4347  N   GLN B 262      49.689   3.118   2.520  1.00 88.91           N  
ANISOU 4347  N   GLN B 262     6985  17439   9356   -626   1948   2400       N  
ATOM   4348  CA  GLN B 262      50.342   2.331   1.478  1.00 95.87           C  
ANISOU 4348  CA  GLN B 262     7848  18408  10170   -706   1938   2304       C  
ATOM   4349  C   GLN B 262      51.392   3.155   0.744  1.00 92.20           C  
ANISOU 4349  C   GLN B 262     7413  17969   9652   -717   1947   2294       C  
ATOM   4350  O   GLN B 262      52.507   2.677   0.493  1.00 78.59           O  
ANISOU 4350  O   GLN B 262     5711  16243   7908   -749   1963   2188       O  
ATOM   4351  CB  GLN B 262      49.301   1.793   0.495  1.00102.15           C  
ANISOU 4351  CB  GLN B 262     8567  19337  10906   -774   1895   2322       C  
ATOM   4352  CG  GLN B 262      48.397   0.712   1.066  1.00110.58           C  
ANISOU 4352  CG  GLN B 262     9597  20386  12031   -783   1893   2300       C  
ATOM   4353  CD  GLN B 262      47.329   0.270   0.083  1.00121.30           C  
ANISOU 4353  CD  GLN B 262    10873  21886  13330   -852   1852   2310       C  
ATOM   4354  OE1 GLN B 262      47.150   0.882  -0.971  1.00128.72           O  
ANISOU 4354  OE1 GLN B 262    11784  22947  14179   -883   1820   2357       O  
ATOM   4355  NE2 GLN B 262      46.608  -0.792   0.427  1.00119.24           N  
ANISOU 4355  NE2 GLN B 262    10569  21615  13123   -876   1856   2269       N  
ATOM   4356  N   LYS B 263      51.055   4.398   0.388  1.00 97.07           N  
ANISOU 4356  N   LYS B 263     8025  18604  10253   -688   1941   2408       N  
ATOM   4357  CA  LYS B 263      52.026   5.254  -0.284  1.00 89.24           C  
ANISOU 4357  CA  LYS B 263     7056  17626   9225   -693   1957   2414       C  
ATOM   4358  C   LYS B 263      53.234   5.522   0.604  1.00 87.55           C  
ANISOU 4358  C   LYS B 263     6909  17285   9072   -650   2007   2339       C  
ATOM   4359  O   LYS B 263      54.376   5.517   0.129  1.00102.26           O  
ANISOU 4359  O   LYS B 263     8798  19157  10901   -676   2021   2266       O  
ATOM   4360  CB  LYS B 263      51.367   6.567  -0.703  1.00 88.92           C  
ANISOU 4360  CB  LYS B 263     6990  17609   9185   -659   1953   2568       C  
ATOM   4361  CG  LYS B 263      52.324   7.578  -1.316  1.00 85.03           C  
ANISOU 4361  CG  LYS B 263     6517  17112   8679   -652   1981   2595       C  
ATOM   4362  CD  LYS B 263      51.601   8.871  -1.650  1.00 88.78           C  
ANISOU 4362  CD  LYS B 263     6957  17595   9180   -610   1988   2764       C  
ATOM   4363  CE  LYS B 263      52.562   9.942  -2.130  1.00 82.04           C  
ANISOU 4363  CE  LYS B 263     6120  16711   8341   -594   2031   2799       C  
ATOM   4364  NZ  LYS B 263      51.849  11.224  -2.389  1.00 81.32           N  
ANISOU 4364  NZ  LYS B 263     5987  16609   8303   -546   2050   2975       N  
ATOM   4365  N   GLU B 264      53.002   5.747   1.898  1.00 76.86           N  
ANISOU 4365  N   GLU B 264     5580  15821   7804   -584   2032   2350       N  
ATOM   4366  CA  GLU B 264      54.107   5.994   2.818  1.00 76.38           C  
ANISOU 4366  CA  GLU B 264     5573  15654   7796   -541   2078   2272       C  
ATOM   4367  C   GLU B 264      55.037   4.788   2.893  1.00 85.00           C  
ANISOU 4367  C   GLU B 264     6685  16748   8863   -575   2079   2141       C  
ATOM   4368  O   GLU B 264      56.266   4.927   2.813  1.00 80.44           O  
ANISOU 4368  O   GLU B 264     6143  16144   8275   -579   2104   2064       O  
ATOM   4369  CB  GLU B 264      53.559   6.356   4.199  1.00 77.33           C  
ANISOU 4369  CB  GLU B 264     5702  15681   8001   -469   2099   2303       C  
ATOM   4370  CG  GLU B 264      54.561   7.046   5.107  1.00 81.65           C  
ANISOU 4370  CG  GLU B 264     6289  16132   8602   -418   2150   2240       C  
ATOM   4371  CD  GLU B 264      53.895   7.791   6.248  1.00 92.09           C  
ANISOU 4371  CD  GLU B 264     7604  17381  10004   -352   2175   2285       C  
ATOM   4372  OE1 GLU B 264      52.728   8.205   6.091  1.00 95.35           O  
ANISOU 4372  OE1 GLU B 264     7983  17809  10438   -344   2161   2391       O  
ATOM   4373  OE2 GLU B 264      54.541   7.970   7.302  1.00 99.13           O  
ANISOU 4373  OE2 GLU B 264     8520  18208  10937   -310   2209   2211       O  
ATOM   4374  N   ALA B 265      54.463   3.587   3.037  1.00 83.61           N  
ANISOU 4374  N   ALA B 265     6482  16599   8688   -599   2057   2116       N  
ATOM   4375  CA  ALA B 265      55.285   2.382   3.114  1.00 79.80           C  
ANISOU 4375  CA  ALA B 265     6008  16110   8204   -630   2066   1999       C  
ATOM   4376  C   ALA B 265      56.044   2.142   1.814  1.00 91.09           C  
ANISOU 4376  C   ALA B 265     7430  17621   9559   -705   2058   1931       C  
ATOM   4377  O   ALA B 265      57.215   1.743   1.835  1.00 90.54           O  
ANISOU 4377  O   ALA B 265     7390  17525   9488   -717   2080   1833       O  
ATOM   4378  CB  ALA B 265      54.419   1.172   3.458  1.00 77.81           C  
ANISOU 4378  CB  ALA B 265     5714  15865   7987   -643   2054   1995       C  
ATOM   4379  N   ALA B1001      55.400   2.394   0.670  1.00 92.29           N  
ANISOU 4379  N   ALA B1001     7541  17881   9644   -756   2025   1982       N  
ATOM   4380  CA  ALA B1001      56.073   2.213  -0.613  1.00 81.74           C  
ANISOU 4380  CA  ALA B1001     6190  16642   8224   -830   2013   1919       C  
ATOM   4381  C   ALA B1001      57.247   3.173  -0.761  1.00 84.14           C  
ANISOU 4381  C   ALA B1001     6546  16909   8514   -808   2038   1910       C  
ATOM   4382  O   ALA B1001      58.338   2.778  -1.189  1.00 87.01           O  
ANISOU 4382  O   ALA B1001     6928  17285   8848   -847   2050   1808       O  
ATOM   4383  CB  ALA B1001      55.079   2.394  -1.758  1.00 79.74           C  
ANISOU 4383  CB  ALA B1001     5874  16531   7893   -881   1968   1991       C  
ATOM   4384  N   ASP B1002      57.036   4.449  -0.424  1.00 76.86           N  
ANISOU 4384  N   ASP B1002     5643  15937   7623   -749   2052   2012       N  
ATOM   4385  CA  ASP B1002      58.120   5.421  -0.518  1.00 76.69           C  
ANISOU 4385  CA  ASP B1002     5663  15868   7608   -727   2087   2003       C  
ATOM   4386  C   ASP B1002      59.265   5.067   0.423  1.00 82.70           C  
ANISOU 4386  C   ASP B1002     6477  16529   8417   -699   2124   1888       C  
ATOM   4387  O   ASP B1002      60.440   5.209   0.063  1.00 84.76           O  
ANISOU 4387  O   ASP B1002     6767  16783   8655   -717   2144   1816       O  
ATOM   4388  CB  ASP B1002      57.594   6.823  -0.217  1.00 76.84           C  
ANISOU 4388  CB  ASP B1002     5680  15835   7680   -667   2109   2130       C  
ATOM   4389  CG  ASP B1002      56.533   7.269  -1.200  1.00 90.28           C  
ANISOU 4389  CG  ASP B1002     7327  17641   9335   -687   2074   2261       C  
ATOM   4390  OD1 ASP B1002      56.225   6.499  -2.135  1.00 90.22           O  
ANISOU 4390  OD1 ASP B1002     7282  17759   9241   -752   2030   2243       O  
ATOM   4391  OD2 ASP B1002      56.003   8.387  -1.036  1.00 98.63           O  
ANISOU 4391  OD2 ASP B1002     8372  18659  10445   -639   2094   2378       O  
ATOM   4392  N   LEU B1003      58.943   4.603   1.635  1.00 81.17           N  
ANISOU 4392  N   LEU B1003     6291  16263   8285   -653   2132   1872       N  
ATOM   4393  CA  LEU B1003      59.993   4.195   2.563  1.00 77.44           C  
ANISOU 4393  CA  LEU B1003     5860  15713   7852   -621   2163   1771       C  
ATOM   4394  C   LEU B1003      60.786   3.015   2.016  1.00 78.24           C  
ANISOU 4394  C   LEU B1003     5960  15852   7915   -680   2157   1662       C  
ATOM   4395  O   LEU B1003      62.020   2.995   2.105  1.00 93.95           O  
ANISOU 4395  O   LEU B1003     7986  17809   9902   -678   2181   1577       O  
ATOM   4396  CB  LEU B1003      59.397   3.853   3.925  1.00 74.37           C  
ANISOU 4396  CB  LEU B1003     5468  15261   7528   -560   2167   1789       C  
ATOM   4397  CG  LEU B1003      60.426   3.442   4.979  1.00 73.81           C  
ANISOU 4397  CG  LEU B1003     5431  15123   7492   -517   2196   1698       C  
ATOM   4398  CD1 LEU B1003      61.338   4.610   5.303  1.00 73.58           C  
ANISOU 4398  CD1 LEU B1003     5438  15044   7476   -482   2231   1666       C  
ATOM   4399  CD2 LEU B1003      59.733   2.939   6.234  1.00 84.18           C  
ANISOU 4399  CD2 LEU B1003     6731  16397   8858   -461   2194   1728       C  
ATOM   4400  N   GLU B1004      60.095   2.014   1.463  1.00 75.18           N  
ANISOU 4400  N   GLU B1004     5527  15533   7505   -734   2129   1656       N  
ATOM   4401  CA  GLU B1004      60.792   0.878   0.867  1.00 75.35           C  
ANISOU 4401  CA  GLU B1004     5534  15591   7503   -798   2132   1543       C  
ATOM   4402  C   GLU B1004      61.694   1.319  -0.278  1.00 80.19           C  
ANISOU 4402  C   GLU B1004     6162  16264   8042   -850   2130   1496       C  
ATOM   4403  O   GLU B1004      62.831   0.844  -0.404  1.00 92.31           O  
ANISOU 4403  O   GLU B1004     7718  17783   9573   -872   2150   1391       O  
ATOM   4404  CB  GLU B1004      59.782  -0.157   0.376  1.00 75.91           C  
ANISOU 4404  CB  GLU B1004     5540  15733   7571   -856   2109   1539       C  
ATOM   4405  CG  GLU B1004      60.402  -1.338  -0.349  1.00 76.27           C  
ANISOU 4405  CG  GLU B1004     5554  15822   7604   -934   2118   1411       C  
ATOM   4406  CD  GLU B1004      61.097  -2.305   0.587  1.00 84.46           C  
ANISOU 4406  CD  GLU B1004     6601  16763   8728   -904   2159   1339       C  
ATOM   4407  OE1 GLU B1004      60.902  -2.195   1.816  1.00 86.82           O  
ANISOU 4407  OE1 GLU B1004     6922  16976   9089   -824   2172   1396       O  
ATOM   4408  OE2 GLU B1004      61.837  -3.179   0.092  1.00 85.92           O  
ANISOU 4408  OE2 GLU B1004     6766  16960   8920   -960   2178   1227       O  
ATOM   4409  N   ASP B1005      61.208   2.234  -1.120  1.00 79.62           N  
ANISOU 4409  N   ASP B1005     6076  16265   7913   -867   2107   1579       N  
ATOM   4410  CA  ASP B1005      62.025   2.724  -2.224  1.00 83.91           C  
ANISOU 4410  CA  ASP B1005     6628  16872   8384   -912   2106   1551       C  
ATOM   4411  C   ASP B1005      63.271   3.436  -1.713  1.00 83.18           C  
ANISOU 4411  C   ASP B1005     6597  16684   8323   -866   2146   1515       C  
ATOM   4412  O   ASP B1005      64.377   3.215  -2.224  1.00 86.01           O  
ANISOU 4412  O   ASP B1005     6976  17056   8648   -903   2157   1422       O  
ATOM   4413  CB  ASP B1005      61.202   3.655  -3.115  1.00 94.66           C  
ANISOU 4413  CB  ASP B1005     7955  18325   9687   -923   2078   1676       C  
ATOM   4414  CG  ASP B1005      60.715   2.973  -4.380  1.00103.54           C  
ANISOU 4414  CG  ASP B1005     9015  19608  10717  -1010   2034   1652       C  
ATOM   4415  OD1 ASP B1005      61.475   2.159  -4.949  1.00104.82           O  
ANISOU 4415  OD1 ASP B1005     9171  19817  10840  -1073   2035   1526       O  
ATOM   4416  OD2 ASP B1005      59.574   3.253  -4.808  1.00105.14           O  
ANISOU 4416  OD2 ASP B1005     9170  19895  10885  -1016   2001   1753       O  
ATOM   4417  N   ASN B1006      63.111   4.294  -0.704  1.00 75.78           N  
ANISOU 4417  N   ASN B1006     5686  15653   7453   -790   2171   1577       N  
ATOM   4418  CA  ASN B1006      64.258   5.016  -0.165  1.00 83.54           C  
ANISOU 4418  CA  ASN B1006     6719  16549   8473   -748   2214   1531       C  
ATOM   4419  C   ASN B1006      65.263   4.065   0.477  1.00 86.06           C  
ANISOU 4419  C   ASN B1006     7067  16820   8811   -743   2229   1403       C  
ATOM   4420  O   ASN B1006      66.480   4.253   0.346  1.00 92.39           O  
ANISOU 4420  O   ASN B1006     7903  17597   9604   -749   2253   1325       O  
ATOM   4421  CB  ASN B1006      63.785   6.073   0.833  1.00 86.24           C  
ANISOU 4421  CB  ASN B1006     7069  16808   8890   -673   2242   1607       C  
ATOM   4422  CG  ASN B1006      62.993   7.188   0.167  1.00 90.50           C  
ANISOU 4422  CG  ASN B1006     7580  17379   9427   -671   2242   1739       C  
ATOM   4423  OD1 ASN B1006      63.238   7.533  -0.990  1.00 84.59           O  
ANISOU 4423  OD1 ASN B1006     6819  16697   8623   -713   2235   1768       O  
ATOM   4424  ND2 ASN B1006      62.040   7.757   0.897  1.00 99.20           N  
ANISOU 4424  ND2 ASN B1006     8664  18435  10591   -620   2250   1824       N  
ATOM   4425  N   TRP B1007      64.776   3.034   1.171  1.00 78.63           N  
ANISOU 4425  N   TRP B1007     6109  15865   7903   -731   2219   1387       N  
ATOM   4426  CA  TRP B1007      65.679   2.057   1.773  1.00 80.18           C  
ANISOU 4426  CA  TRP B1007     6321  16017   8126   -722   2236   1283       C  
ATOM   4427  C   TRP B1007      66.448   1.284   0.708  1.00 84.52           C  
ANISOU 4427  C   TRP B1007     6863  16622   8628   -799   2233   1188       C  
ATOM   4428  O   TRP B1007      67.662   1.062   0.841  1.00 81.63           O  
ANISOU 4428  O   TRP B1007     6527  16222   8267   -797   2255   1097       O  
ATOM   4429  CB  TRP B1007      64.883   1.114   2.675  1.00 77.79           C  
ANISOU 4429  CB  TRP B1007     5989  15690   7877   -691   2231   1308       C  
ATOM   4430  CG  TRP B1007      65.651  -0.064   3.187  1.00 78.12           C  
ANISOU 4430  CG  TRP B1007     6029  15696   7957   -684   2251   1224       C  
ATOM   4431  CD1 TRP B1007      66.539  -0.077   4.223  1.00 73.13           C  
ANISOU 4431  CD1 TRP B1007     5427  15001   7358   -622   2276   1184       C  
ATOM   4432  CD2 TRP B1007      65.570  -1.412   2.711  1.00 80.58           C  
ANISOU 4432  CD2 TRP B1007     6297  16034   8286   -740   2253   1172       C  
ATOM   4433  NE1 TRP B1007      67.029  -1.347   4.410  1.00 76.89           N  
ANISOU 4433  NE1 TRP B1007     5881  15461   7871   -630   2293   1126       N  
ATOM   4434  CE2 TRP B1007      66.449  -2.186   3.495  1.00 78.02           C  
ANISOU 4434  CE2 TRP B1007     5979  15651   8015   -703   2284   1114       C  
ATOM   4435  CE3 TRP B1007      64.846  -2.039   1.691  1.00 81.39           C  
ANISOU 4435  CE3 TRP B1007     6347  16208   8368   -819   2236   1162       C  
ATOM   4436  CZ2 TRP B1007      66.624  -3.554   3.291  1.00 81.99           C  
ANISOU 4436  CZ2 TRP B1007     6436  16149   8568   -741   2306   1055       C  
ATOM   4437  CZ3 TRP B1007      65.020  -3.398   1.491  1.00 81.04           C  
ANISOU 4437  CZ3 TRP B1007     6257  16164   8372   -864   2257   1084       C  
ATOM   4438  CH2 TRP B1007      65.902  -4.140   2.287  1.00 80.46           C  
ANISOU 4438  CH2 TRP B1007     6189  16015   8368   -824   2296   1035       C  
ATOM   4439  N   GLU B1008      65.758   0.867  -0.357  1.00 85.55           N  
ANISOU 4439  N   GLU B1008     6950  16845   8712   -870   2205   1200       N  
ATOM   4440  CA  GLU B1008      66.437   0.202  -1.463  1.00 88.75           C  
ANISOU 4440  CA  GLU B1008     7339  17318   9066   -952   2201   1098       C  
ATOM   4441  C   GLU B1008      67.505   1.102  -2.072  1.00 82.34           C  
ANISOU 4441  C   GLU B1008     6569  16516   8202   -963   2210   1072       C  
ATOM   4442  O   GLU B1008      68.611   0.643  -2.377  1.00 78.31           O  
ANISOU 4442  O   GLU B1008     6074  16000   7680   -994   2226    964       O  
ATOM   4443  CB  GLU B1008      65.420  -0.226  -2.520  1.00 90.37           C  
ANISOU 4443  CB  GLU B1008     7479  17641   9217  -1027   2166   1116       C  
ATOM   4444  CG  GLU B1008      64.598  -1.434  -2.112  1.00101.75           C  
ANISOU 4444  CG  GLU B1008     8868  19074  10717  -1041   2167   1097       C  
ATOM   4445  CD  GLU B1008      63.404  -1.659  -3.015  1.00112.04           C  
ANISOU 4445  CD  GLU B1008    10104  20496  11971  -1105   2131   1127       C  
ATOM   4446  OE1 GLU B1008      63.345  -1.025  -4.090  1.00117.37           O  
ANISOU 4446  OE1 GLU B1008    10768  21277  12551  -1148   2102   1149       O  
ATOM   4447  OE2 GLU B1008      62.522  -2.466  -2.649  1.00113.03           O  
ANISOU 4447  OE2 GLU B1008    10182  20613  12151  -1111   2132   1132       O  
ATOM   4448  N   THR B1009      67.188   2.386  -2.260  1.00 78.12           N  
ANISOU 4448  N   THR B1009     6047  15989   7646   -936   2206   1172       N  
ATOM   4449  CA  THR B1009      68.165   3.322  -2.810  1.00 75.27           C  
ANISOU 4449  CA  THR B1009     5721  15627   7252   -941   2223   1160       C  
ATOM   4450  C   THR B1009      69.384   3.439  -1.904  1.00 81.66           C  
ANISOU 4450  C   THR B1009     6583  16331   8114   -893   2263   1079       C  
ATOM   4451  O   THR B1009      70.530   3.420  -2.374  1.00 74.54           O  
ANISOU 4451  O   THR B1009     5707  15431   7186   -921   2277    995       O  
ATOM   4452  CB  THR B1009      67.520   4.694  -3.016  1.00 75.58           C  
ANISOU 4452  CB  THR B1009     5753  15673   7289   -909   2225   1297       C  
ATOM   4453  OG1 THR B1009      66.559   4.619  -4.076  1.00 83.34           O  
ANISOU 4453  OG1 THR B1009     6683  16779   8203   -959   2184   1370       O  
ATOM   4454  CG2 THR B1009      68.570   5.735  -3.366  1.00 75.60           C  
ANISOU 4454  CG2 THR B1009     5790  15645   7289   -900   2260   1291       C  
ATOM   4455  N   LEU B1010      69.150   3.566  -0.596  1.00 82.86           N  
ANISOU 4455  N   LEU B1010     6749  16398   8336   -820   2280   1102       N  
ATOM   4456  CA  LEU B1010      70.255   3.681   0.352  1.00 86.77           C  
ANISOU 4456  CA  LEU B1010     7285  16807   8875   -770   2314   1024       C  
ATOM   4457  C   LEU B1010      71.163   2.460   0.286  1.00 81.09           C  
ANISOU 4457  C   LEU B1010     6572  16090   8149   -800   2315    908       C  
ATOM   4458  O   LEU B1010      72.391   2.590   0.238  1.00 84.70           O  
ANISOU 4458  O   LEU B1010     7062  16521   8600   -802   2336    826       O  
ATOM   4459  CB  LEU B1010      69.712   3.870   1.769  1.00 92.55           C  
ANISOU 4459  CB  LEU B1010     8018  17474   9673   -692   2324   1066       C  
ATOM   4460  CG  LEU B1010      69.171   5.256   2.118  1.00 91.33           C  
ANISOU 4460  CG  LEU B1010     7863  17284   9553   -648   2343   1150       C  
ATOM   4461  CD1 LEU B1010      68.453   5.223   3.453  1.00 84.25           C  
ANISOU 4461  CD1 LEU B1010     6956  16344   8712   -581   2344   1185       C  
ATOM   4462  CD2 LEU B1010      70.301   6.266   2.144  1.00 94.18           C  
ANISOU 4462  CD2 LEU B1010     8256  17597   9930   -634   2386   1096       C  
ATOM   4463  N   ASN B1011      70.574   1.261   0.261  1.00 77.19           N  
ANISOU 4463  N   ASN B1011     6039  15625   7664   -826   2298    900       N  
ATOM   4464  CA  ASN B1011      71.391   0.050   0.222  1.00 73.50           C  
ANISOU 4464  CA  ASN B1011     5565  15150   7212   -854   2311    793       C  
ATOM   4465  C   ASN B1011      72.146  -0.075  -1.097  1.00 84.99           C  
ANISOU 4465  C   ASN B1011     7021  16665   8605   -936   2307    711       C  
ATOM   4466  O   ASN B1011      73.329  -0.445  -1.110  1.00 84.36           O  
ANISOU 4466  O   ASN B1011     6964  16558   8532   -944   2328    614       O  
ATOM   4467  CB  ASN B1011      70.523  -1.180   0.460  1.00 73.74           C  
ANISOU 4467  CB  ASN B1011     5541  15189   7288   -866   2306    805       C  
ATOM   4468  CG  ASN B1011      70.502  -1.594   1.908  1.00 73.35           C  
ANISOU 4468  CG  ASN B1011     5492  15063   7314   -783   2324    831       C  
ATOM   4469  OD1 ASN B1011      70.992  -0.870   2.775  1.00 72.91           O  
ANISOU 4469  OD1 ASN B1011     5475  14960   7266   -715   2334    844       O  
ATOM   4470  ND2 ASN B1011      69.938  -2.764   2.184  1.00 73.59           N  
ANISOU 4470  ND2 ASN B1011     5473  15086   7403   -788   2333    838       N  
ATOM   4471  N   ASP B1012      71.471   0.201  -2.216  1.00 87.15           N  
ANISOU 4471  N   ASP B1012     7268  17029   8816   -997   2280    748       N  
ATOM   4472  CA  ASP B1012      72.130   0.154  -3.516  1.00 74.88           C  
ANISOU 4472  CA  ASP B1012     5711  15552   7190  -1075   2272    676       C  
ATOM   4473  C   ASP B1012      73.340   1.076  -3.545  1.00 74.56           C  
ANISOU 4473  C   ASP B1012     5727  15469   7134  -1052   2293    649       C  
ATOM   4474  O   ASP B1012      74.433   0.677  -3.967  1.00 77.34           O  
ANISOU 4474  O   ASP B1012     6094  15822   7469  -1088   2306    542       O  
ATOM   4475  CB  ASP B1012      71.140   0.531  -4.618  1.00 75.61           C  
ANISOU 4475  CB  ASP B1012     5762  15762   7206  -1129   2235    747       C  
ATOM   4476  CG  ASP B1012      70.121  -0.556  -4.884  1.00 76.12           C  
ANISOU 4476  CG  ASP B1012     5758  15890   7273  -1179   2215    731       C  
ATOM   4477  OD1 ASP B1012      70.198  -1.614  -4.227  1.00 80.37           O  
ANISOU 4477  OD1 ASP B1012     6281  16370   7886  -1173   2236    667       O  
ATOM   4478  OD2 ASP B1012      69.241  -0.351  -5.747  1.00 76.79           O  
ANISOU 4478  OD2 ASP B1012     5799  16085   7292  -1224   2181    784       O  
ATOM   4479  N   ASN B1013      73.167   2.318  -3.092  1.00 74.33           N  
ANISOU 4479  N   ASN B1013     5725  15397   7119   -994   2304    739       N  
ATOM   4480  CA  ASN B1013      74.277   3.257  -3.174  1.00 74.14           C  
ANISOU 4480  CA  ASN B1013     5746  15331   7091   -976   2332    711       C  
ATOM   4481  C   ASN B1013      75.353   2.953  -2.139  1.00 85.88           C  
ANISOU 4481  C   ASN B1013     7272  16727   8633   -929   2361    618       C  
ATOM   4482  O   ASN B1013      76.532   3.233  -2.384  1.00 90.32           O  
ANISOU 4482  O   ASN B1013     7867  17268   9184   -938   2381    544       O  
ATOM   4483  CB  ASN B1013      73.768   4.687  -3.033  1.00 74.23           C  
ANISOU 4483  CB  ASN B1013     5763  15319   7121   -932   2347    829       C  
ATOM   4484  CG  ASN B1013      73.028   5.156  -4.265  1.00 76.85           C  
ANISOU 4484  CG  ASN B1013     6060  15752   7389   -980   2323    924       C  
ATOM   4485  OD1 ASN B1013      73.643   5.514  -5.267  1.00 84.66           O  
ANISOU 4485  OD1 ASN B1013     7052  16791   8325  -1021   2326    911       O  
ATOM   4486  ND2 ASN B1013      71.703   5.151  -4.203  1.00 87.62           N  
ANISOU 4486  ND2 ASN B1013     7385  17152   8753   -971   2297   1024       N  
ATOM   4487  N   LEU B1014      74.988   2.353  -1.002  1.00 78.33           N  
ANISOU 4487  N   LEU B1014     6307  15723   7732   -878   2362    623       N  
ATOM   4488  CA  LEU B1014      76.003   1.861  -0.075  1.00 76.61           C  
ANISOU 4488  CA  LEU B1014     6112  15440   7555   -835   2384    538       C  
ATOM   4489  C   LEU B1014      76.876   0.806  -0.741  1.00 82.99           C  
ANISOU 4489  C   LEU B1014     6916  16272   8346   -892   2386    430       C  
ATOM   4490  O   LEU B1014      78.110   0.837  -0.636  1.00 77.78           O  
ANISOU 4490  O   LEU B1014     6288  15578   7688   -885   2405    346       O  
ATOM   4491  CB  LEU B1014      75.342   1.293   1.181  1.00 76.05           C  
ANISOU 4491  CB  LEU B1014     6021  15333   7542   -771   2383    580       C  
ATOM   4492  CG  LEU B1014      75.153   2.250   2.357  1.00 79.76           C  
ANISOU 4492  CG  LEU B1014     6507  15751   8048   -690   2395    627       C  
ATOM   4493  CD1 LEU B1014      74.631   1.502   3.573  1.00 85.83           C  
ANISOU 4493  CD1 LEU B1014     7251  16497   8863   -630   2391    660       C  
ATOM   4494  CD2 LEU B1014      76.451   2.961   2.683  1.00 86.78           C  
ANISOU 4494  CD2 LEU B1014     7436  16597   8940   -663   2423    549       C  
ATOM   4495  N   LYS B1015      76.245  -0.137  -1.444  1.00 80.04           N  
ANISOU 4495  N   LYS B1015     6497  15955   7958   -954   2369    423       N  
ATOM   4496  CA  LYS B1015      77.011  -1.159  -2.146  1.00 74.89           C  
ANISOU 4496  CA  LYS B1015     5830  15327   7299  -1019   2377    309       C  
ATOM   4497  C   LYS B1015      77.890  -0.537  -3.223  1.00 73.71           C  
ANISOU 4497  C   LYS B1015     5710  15218   7080  -1071   2375    252       C  
ATOM   4498  O   LYS B1015      79.041  -0.948  -3.409  1.00 73.65           O  
ANISOU 4498  O   LYS B1015     5718  15189   7075  -1091   2392    148       O  
ATOM   4499  CB  LYS B1015      76.070  -2.200  -2.750  1.00 79.41           C  
ANISOU 4499  CB  LYS B1015     6336  15960   7877  -1084   2364    301       C  
ATOM   4500  CG  LYS B1015      76.719  -3.554  -2.965  1.00 85.28           C  
ANISOU 4500  CG  LYS B1015     7045  16691   8668  -1129   2390    181       C  
ATOM   4501  CD  LYS B1015      77.186  -4.141  -1.641  1.00 85.89           C  
ANISOU 4501  CD  LYS B1015     7125  16671   8838  -1048   2424    183       C  
ATOM   4502  CE  LYS B1015      77.934  -5.450  -1.842  1.00 90.77           C  
ANISOU 4502  CE  LYS B1015     7703  17263   9522  -1087   2461     70       C  
ATOM   4503  NZ  LYS B1015      78.436  -6.006  -0.553  1.00 85.63           N  
ANISOU 4503  NZ  LYS B1015     7049  16527   8961  -1000   2495     91       N  
ATOM   4504  N   VAL B1016      77.357   0.447  -3.954  1.00 77.44           N  
ANISOU 4504  N   VAL B1016     6184  15747   7492  -1093   2355    325       N  
ATOM   4505  CA  VAL B1016      78.148   1.150  -4.963  1.00 74.25           C  
ANISOU 4505  CA  VAL B1016     5804  15384   7024  -1135   2356    294       C  
ATOM   4506  C   VAL B1016      79.370   1.803  -4.328  1.00 80.36           C  
ANISOU 4506  C   VAL B1016     6635  16069   7830  -1083   2389    252       C  
ATOM   4507  O   VAL B1016      80.478   1.748  -4.878  1.00 90.98           O  
ANISOU 4507  O   VAL B1016     8002  17417   9149  -1117   2399    163       O  
ATOM   4508  CB  VAL B1016      77.276   2.180  -5.707  1.00 74.73           C  
ANISOU 4508  CB  VAL B1016     5849  15516   7030  -1150   2336    414       C  
ATOM   4509  CG1 VAL B1016      78.133   3.073  -6.596  1.00 75.00           C  
ANISOU 4509  CG1 VAL B1016     5908  15578   7011  -1175   2347    407       C  
ATOM   4510  CG2 VAL B1016      76.219   1.471  -6.534  1.00 78.26           C  
ANISOU 4510  CG2 VAL B1016     6235  16077   7425  -1216   2299    432       C  
ATOM   4511  N   ILE B1017      79.192   2.427  -3.162  1.00 76.85           N  
ANISOU 4511  N   ILE B1017     6209  15548   7441  -1002   2406    307       N  
ATOM   4512  CA  ILE B1017      80.323   3.028  -2.459  1.00 91.18           C  
ANISOU 4512  CA  ILE B1017     8069  17284   9290   -951   2438    253       C  
ATOM   4513  C   ILE B1017      81.350   1.967  -2.090  1.00 96.91           C  
ANISOU 4513  C   ILE B1017     8805  17981  10036   -950   2445    138       C  
ATOM   4514  O   ILE B1017      82.562   2.182  -2.223  1.00 99.06           O  
ANISOU 4514  O   ILE B1017     9110  18227  10303   -954   2463     56       O  
ATOM   4515  CB  ILE B1017      79.840   3.793  -1.212  1.00100.53           C  
ANISOU 4515  CB  ILE B1017     9259  18406  10533   -868   2454    320       C  
ATOM   4516  CG1 ILE B1017      78.985   4.997  -1.610  1.00102.89           C  
ANISOU 4516  CG1 ILE B1017     9547  18720  10828   -867   2461    431       C  
ATOM   4517  CG2 ILE B1017      81.024   4.234  -0.362  1.00 97.60           C  
ANISOU 4517  CG2 ILE B1017     8922  17963  10197   -817   2486    241       C  
ATOM   4518  CD1 ILE B1017      78.380   5.735  -0.433  1.00 92.70           C  
ANISOU 4518  CD1 ILE B1017     8251  17371   9601   -794   2480    491       C  
ATOM   4519  N   GLU B1018      80.882   0.803  -1.628  1.00 96.90           N  
ANISOU 4519  N   GLU B1018     8770  17981  10066   -943   2436    134       N  
ATOM   4520  CA  GLU B1018      81.794  -0.265  -1.222  1.00 96.57           C  
ANISOU 4520  CA  GLU B1018     8726  17907  10061   -934   2451     42       C  
ATOM   4521  C   GLU B1018      82.762  -0.659  -2.334  1.00 88.48           C  
ANISOU 4521  C   GLU B1018     7708  16910   8999  -1010   2455    -65       C  
ATOM   4522  O   GLU B1018      83.907  -1.032  -2.055  1.00 82.89           O  
ANISOU 4522  O   GLU B1018     7018  16163   8314   -995   2474   -149       O  
ATOM   4523  CB  GLU B1018      80.992  -1.484  -0.761  1.00103.83           C  
ANISOU 4523  CB  GLU B1018     9593  18827  11031   -926   2449     70       C  
ATOM   4524  CG  GLU B1018      81.843  -2.681  -0.366  1.00112.63           C  
ANISOU 4524  CG  GLU B1018    10688  19905  12202   -915   2475     -8       C  
ATOM   4525  CD  GLU B1018      81.012  -3.903  -0.033  1.00123.04           C  
ANISOU 4525  CD  GLU B1018    11941  21219  13589   -914   2486     26       C  
ATOM   4526  OE1 GLU B1018      79.794  -3.751   0.201  1.00126.39           O  
ANISOU 4526  OE1 GLU B1018    12345  21661  14018   -901   2470    116       O  
ATOM   4527  OE2 GLU B1018      81.577  -5.018  -0.008  1.00125.79           O  
ANISOU 4527  OE2 GLU B1018    12256  21542  13997   -926   2516    -38       O  
ATOM   4528  N   LYS B1019      82.335  -0.574  -3.588  1.00101.44           N  
ANISOU 4528  N   LYS B1019     7911  18809  11822    112   2765  -2133       N  
ATOM   4529  CA  LYS B1019      83.149  -0.973  -4.735  1.00101.50           C  
ANISOU 4529  CA  LYS B1019     8017  18701  11849    175   3138  -2352       C  
ATOM   4530  C   LYS B1019      83.267   0.205  -5.701  1.00109.95           C  
ANISOU 4530  C   LYS B1019     9312  20003  12462    244   3304  -2313       C  
ATOM   4531  O   LYS B1019      82.747   0.163  -6.819  1.00114.58           O  
ANISOU 4531  O   LYS B1019    10163  20784  12590    256   3374  -2528       O  
ATOM   4532  CB  LYS B1019      82.547  -2.209  -5.411  1.00 95.86           C  
ANISOU 4532  CB  LYS B1019     7406  17905  11112    132   3166  -2742       C  
ATOM   4533  CG  LYS B1019      82.499  -3.433  -4.509  1.00 95.28           C  
ANISOU 4533  CG  LYS B1019     7045  17533  11625     83   3070  -2724       C  
ATOM   4534  CD  LYS B1019      81.676  -4.552  -5.124  1.00 98.02           C  
ANISOU 4534  CD  LYS B1019     7464  17774  12004     15   3038  -3140       C  
ATOM   4535  CE  LYS B1019      81.516  -5.713  -4.154  1.00100.19           C  
ANISOU 4535  CE  LYS B1019     7392  17726  12950    -24   2943  -3030       C  
ATOM   4536  NZ  LYS B1019      80.704  -6.826  -4.726  1.00107.97           N  
ANISOU 4536  NZ  LYS B1019     8388  18532  14104   -105   2911  -3464       N  
ATOM   4537  N   ALA B1020      83.951   1.259  -5.263  1.00113.62           N  
ANISOU 4537  N   ALA B1020     9650  20456  13064    284   3353  -2023       N  
ATOM   4538  CA  ALA B1020      84.115   2.471  -6.051  1.00116.35           C  
ANISOU 4538  CA  ALA B1020    10125  20970  13113    362   3533  -1880       C  
ATOM   4539  C   ALA B1020      85.593   2.714  -6.331  1.00110.41           C  
ANISOU 4539  C   ALA B1020     9263  19960  12728    456   3910  -1742       C  
ATOM   4540  O   ALA B1020      86.461   2.347  -5.533  1.00106.02           O  
ANISOU 4540  O   ALA B1020     8443  19131  12709    437   3913  -1664       O  
ATOM   4541  CB  ALA B1020      83.510   3.685  -5.336  1.00114.32           C  
ANISOU 4541  CB  ALA B1020     9800  20835  12800    324   3267  -1643       C  
ATOM   4542  N   ASP B1021      85.871   3.337  -7.477  1.00111.00           N  
ANISOU 4542  N   ASP B1021     9535  20105  12534    562   4215  -1657       N  
ATOM   4543  CA  ASP B1021      87.243   3.611  -7.890  1.00109.98           C  
ANISOU 4543  CA  ASP B1021     9322  19688  12777    674   4634  -1481       C  
ATOM   4544  C   ASP B1021      87.724   4.984  -7.432  1.00105.84           C  
ANISOU 4544  C   ASP B1021     8605  19022  12586    690   4601  -1119       C  
ATOM   4545  O   ASP B1021      88.770   5.095  -6.786  1.00107.40           O  
ANISOU 4545  O   ASP B1021     8503  18912  13390    685   4659   -989       O  
ATOM   4546  CB  ASP B1021      87.365   3.504  -9.414  1.00112.44           C  
ANISOU 4546  CB  ASP B1021     9954  20140  12628    797   5055  -1564       C  
ATOM   4547  CG  ASP B1021      87.615   2.087  -9.881  1.00114.66           C  
ANISOU 4547  CG  ASP B1021    10333  20338  12892    807   5296  -1963       C  
ATOM   4548  OD1 ASP B1021      86.956   1.658 -10.852  1.00118.42           O  
ANISOU 4548  OD1 ASP B1021    11136  21106  12753    812   5358  -2261       O  
ATOM   4549  OD2 ASP B1021      88.444   1.391  -9.257  1.00114.69           O  
ANISOU 4549  OD2 ASP B1021    10066  19986  13525    799   5403  -1992       O  
ATOM   4550  N   ASN B1022      86.972   6.029  -7.752  1.00103.14           N  
ANISOU 4550  N   ASN B1022     8383  18895  11912    703   4505   -958       N  
ATOM   4551  CA  ASN B1022      87.398   7.411  -7.583  1.00101.80           C  
ANISOU 4551  CA  ASN B1022     8028  18566  12085    735   4573   -638       C  
ATOM   4552  C   ASN B1022      86.428   8.144  -6.662  1.00104.57           C  
ANISOU 4552  C   ASN B1022     8297  19019  12416    627   4157   -619       C  
ATOM   4553  O   ASN B1022      85.427   7.589  -6.202  1.00114.69           O  
ANISOU 4553  O   ASN B1022     9678  20503  13396    540   3837   -811       O  
ATOM   4554  CB  ASN B1022      87.502   8.117  -8.937  1.00102.05           C  
ANISOU 4554  CB  ASN B1022     8228  18704  11843    879   4959   -386       C  
ATOM   4555  CG  ASN B1022      86.272   7.912  -9.797  1.00105.96           C  
ANISOU 4555  CG  ASN B1022     9053  19667  11541    900   4856   -449       C  
ATOM   4556  OD1 ASN B1022      85.596   6.889  -9.701  1.00107.03           O  
ANISOU 4556  OD1 ASN B1022     9335  20000  11332    826   4637   -777       O  
ATOM   4557  ND2 ASN B1022      85.975   8.889 -10.646  1.00108.17           N  
ANISOU 4557  ND2 ASN B1022     9407  20137  11558    995   5003   -115       N  
ATOM   4558  N   ALA B1023      86.739   9.414  -6.397  1.00106.77           N  
ANISOU 4558  N   ALA B1023     8368  19119  13081    635   4202   -396       N  
ATOM   4559  CA  ALA B1023      85.905  10.217  -5.511  1.00103.80           C  
ANISOU 4559  CA  ALA B1023     7893  18775  12770    538   3885   -411       C  
ATOM   4560  C   ALA B1023      84.595  10.636  -6.164  1.00100.43           C  
ANISOU 4560  C   ALA B1023     7650  18645  11864    575   3834   -290       C  
ATOM   4561  O   ALA B1023      83.627  10.914  -5.450  1.00106.37           O  
ANISOU 4561  O   ALA B1023     8381  19475  12561    491   3554   -368       O  
ATOM   4562  CB  ALA B1023      86.671  11.455  -5.044  1.00104.42           C  
ANISOU 4562  CB  ALA B1023     7643  18533  13500    523   3977   -271       C  
ATOM   4563  N   ALA B1024      84.540  10.689  -7.498  1.00 96.84           N  
ANISOU 4563  N   ALA B1024     7359  18382  11054    702   4102    -83       N  
ATOM   4564  CA  ALA B1024      83.318  11.122  -8.168  1.00 99.57           C  
ANISOU 4564  CA  ALA B1024     7815  19083  10932    743   4025    108       C  
ATOM   4565  C   ALA B1024      82.185  10.119  -7.972  1.00112.64           C  
ANISOU 4565  C   ALA B1024     9637  21066  12095    653   3692   -176       C  
ATOM   4566  O   ALA B1024      81.043  10.510  -7.696  1.00 93.92           O  
ANISOU 4566  O   ALA B1024     7210  18859   9614    607   3465   -110       O  
ATOM   4567  CB  ALA B1024      83.589  11.345  -9.656  1.00101.40           C  
ANISOU 4567  CB  ALA B1024     8194  19529  10802    902   4372    416       C  
ATOM   4568  N   GLN B1025      82.478   8.823  -8.119  1.00110.15           N  
ANISOU 4568  N   GLN B1025     9485  20812  11556    628   3689   -486       N  
ATOM   4569  CA  GLN B1025      81.463   7.801  -7.881  1.00114.53           C  
ANISOU 4569  CA  GLN B1025    10137  21616  11763    531   3391   -786       C  
ATOM   4570  C   GLN B1025      80.955   7.859  -6.447  1.00115.26           C  
ANISOU 4570  C   GLN B1025    10062  21539  12194    414   3082   -875       C  
ATOM   4571  O   GLN B1025      79.744   7.759  -6.200  1.00120.70           O  
ANISOU 4571  O   GLN B1025    10790  22360  12711    350   2805   -905       O  
ATOM   4572  CB  GLN B1025      82.030   6.415  -8.194  1.00117.51           C  
ANISOU 4572  CB  GLN B1025    10653  21971  12025    522   3501  -1128       C  
ATOM   4573  CG  GLN B1025      82.401   6.210  -9.654  1.00127.94           C  
ANISOU 4573  CG  GLN B1025    12221  23497  12893    631   3815  -1137       C  
ATOM   4574  CD  GLN B1025      83.155   4.914  -9.893  1.00131.97           C  
ANISOU 4574  CD  GLN B1025    12833  23855  13454    630   4020  -1506       C  
ATOM   4575  OE1 GLN B1025      83.682   4.306  -8.961  1.00128.54           O  
ANISOU 4575  OE1 GLN B1025    12214  23104  13522    574   3986  -1639       O  
ATOM   4576  NE2 GLN B1025      83.210   4.485 -11.149  1.00137.07           N  
ANISOU 4576  NE2 GLN B1025    13765  24731  13584    693   4244  -1667       N  
ATOM   4577  N   VAL B1026      81.872   8.007  -5.488  1.00107.40           N  
ANISOU 4577  N   VAL B1026     8924  20193  11690    379   3093   -902       N  
ATOM   4578  CA  VAL B1026      81.486   8.102  -4.085  1.00 89.63           C  
ANISOU 4578  CA  VAL B1026     6552  17824   9678    273   2818   -994       C  
ATOM   4579  C   VAL B1026      80.598   9.317  -3.859  1.00 85.39           C  
ANISOU 4579  C   VAL B1026     5952  17307   9186    265   2748   -838       C  
ATOM   4580  O   VAL B1026      79.586   9.240  -3.152  1.00 83.86           O  
ANISOU 4580  O   VAL B1026     5752  17182   8928    199   2534   -910       O  
ATOM   4581  CB  VAL B1026      82.739   8.143  -3.193  1.00 85.47           C  
ANISOU 4581  CB  VAL B1026     5854  17014   9605    236   2837  -1039       C  
ATOM   4582  CG1 VAL B1026      82.348   8.226  -1.725  1.00 83.57           C  
ANISOU 4582  CG1 VAL B1026     5515  16758   9480    125   2551  -1155       C  
ATOM   4583  CG2 VAL B1026      83.611   6.928  -3.459  1.00 86.33           C  
ANISOU 4583  CG2 VAL B1026     5966  17066   9768    258   2950  -1140       C  
ATOM   4584  N   LYS B1027      80.951  10.453  -4.466  1.00 87.20           N  
ANISOU 4584  N   LYS B1027     6100  17446   9587    342   2969   -593       N  
ATOM   4585  CA  LYS B1027      80.150  11.660  -4.288  1.00 88.83           C  
ANISOU 4585  CA  LYS B1027     6181  17608   9961    344   2960   -417       C  
ATOM   4586  C   LYS B1027      78.758  11.493  -4.884  1.00 91.82           C  
ANISOU 4586  C   LYS B1027     6624  18331   9934    363   2842   -289       C  
ATOM   4587  O   LYS B1027      77.767  11.928  -4.288  1.00 90.68           O  
ANISOU 4587  O   LYS B1027     6393  18159   9904    317   2714   -271       O  
ATOM   4588  CB  LYS B1027      80.858  12.862  -4.912  1.00 89.99           C  
ANISOU 4588  CB  LYS B1027     6168  17562  10461    436   3263   -120       C  
ATOM   4589  CG  LYS B1027      80.024  14.132  -4.896  1.00 91.04           C  
ANISOU 4589  CG  LYS B1027     6122  17609  10859    457   3312    121       C  
ATOM   4590  CD  LYS B1027      80.816  15.339  -5.358  1.00 93.88           C  
ANISOU 4590  CD  LYS B1027     6259  17680  11733    539   3629    414       C  
ATOM   4591  CE  LYS B1027      79.973  16.601  -5.296  1.00 95.37           C  
ANISOU 4591  CE  LYS B1027     6223  17703  12309    556   3700    656       C  
ATOM   4592  NZ  LYS B1027      80.775  17.822  -5.575  1.00106.89           N  
ANISOU 4592  NZ  LYS B1027     7412  18771  14430    611   4005    890       N  
ATOM   4593  N   ASP B1028      78.660  10.851  -6.049  1.00 94.40           N  
ANISOU 4593  N   ASP B1028     7114  18961   9795    422   2873   -217       N  
ATOM   4594  CA  ASP B1028      77.357  10.641  -6.675  1.00107.85           C  
ANISOU 4594  CA  ASP B1028     8932  20930  11115    413   2649   -102       C  
ATOM   4595  C   ASP B1028      76.482   9.721  -5.826  1.00104.33           C  
ANISOU 4595  C   ASP B1028     8531  20472  10637    298   2338   -382       C  
ATOM   4596  O   ASP B1028      75.297  10.008  -5.585  1.00 99.85           O  
ANISOU 4596  O   ASP B1028     7891  19930  10118    264   2155   -267       O  
ATOM   4597  CB  ASP B1028      77.551  10.074  -8.083  1.00120.03           C  
ANISOU 4597  CB  ASP B1028    10707  22790  12108    478   2707    -58       C  
ATOM   4598  CG  ASP B1028      76.241   9.828  -8.802  1.00134.32           C  
ANISOU 4598  CG  ASP B1028    12630  24924  13482    447   2400     40       C  
ATOM   4599  OD1 ASP B1028      75.448  10.783  -8.944  1.00141.59           O  
ANISOU 4599  OD1 ASP B1028    13398  25896  14505    476   2327    420       O  
ATOM   4600  OD2 ASP B1028      76.009   8.680  -9.235  1.00139.29           O  
ANISOU 4600  OD2 ASP B1028    13469  25735  13718    388   2225   -265       O  
ATOM   4601  N   ALA B1029      77.055   8.607  -5.361  1.00100.29           N  
ANISOU 4601  N   ALA B1029     8100  19894  10111    247   2304   -704       N  
ATOM   4602  CA  ALA B1029      76.305   7.684  -4.517  1.00 89.65           C  
ANISOU 4602  CA  ALA B1029     6755  18511   8796    154   2053   -911       C  
ATOM   4603  C   ALA B1029      75.877   8.351  -3.216  1.00 94.25           C  
ANISOU 4603  C   ALA B1029     7170  18939   9703    117   2019   -872       C  
ATOM   4604  O   ALA B1029      74.755   8.136  -2.739  1.00 90.71           O  
ANISOU 4604  O   ALA B1029     6687  18503   9277     75   1849   -864       O  
ATOM   4605  CB  ALA B1029      77.140   6.437  -4.235  1.00 84.19           C  
ANISOU 4605  CB  ALA B1029     6117  17738   8134    124   2075  -1185       C  
ATOM   4606  N   LEU B1030      76.750   9.177  -2.635  1.00 91.18           N  
ANISOU 4606  N   LEU B1030     6664  18396   9585    130   2193   -869       N  
ATOM   4607  CA  LEU B1030      76.399   9.873  -1.404  1.00 83.85           C  
ANISOU 4607  CA  LEU B1030     5660  17268   8932     84   2157   -910       C  
ATOM   4608  C   LEU B1030      75.322  10.917  -1.641  1.00 84.86           C  
ANISOU 4608  C   LEU B1030     5672  17388   9183    114   2211   -698       C  
ATOM   4609  O   LEU B1030      74.483  11.140  -0.766  1.00 98.13           O  
ANISOU 4609  O   LEU B1030     7311  18977  10998     79   2167   -743       O  
ATOM   4610  CB  LEU B1030      77.636  10.522  -0.791  1.00 84.86           C  
ANISOU 4610  CB  LEU B1030     5736  17155   9353     65   2261  -1007       C  
ATOM   4611  CG  LEU B1030      78.565   9.586  -0.019  1.00 85.27           C  
ANISOU 4611  CG  LEU B1030     5809  17201   9389     11   2159  -1200       C  
ATOM   4612  CD1 LEU B1030      79.813  10.328   0.427  1.00 83.57           C  
ANISOU 4612  CD1 LEU B1030     5453  16811   9490    -17   2243  -1277       C  
ATOM   4613  CD2 LEU B1030      77.840   8.976   1.169  1.00 86.06           C  
ANISOU 4613  CD2 LEU B1030     5930  17396   9374    -50   1983  -1316       C  
ATOM   4614  N   THR B1031      75.322  11.562  -2.807  1.00 84.31           N  
ANISOU 4614  N   THR B1031     5538  17410   9088    189   2329   -426       N  
ATOM   4615  CA  THR B1031      74.252  12.502  -3.128  1.00 85.84           C  
ANISOU 4615  CA  THR B1031     5589  17572   9452    226   2353   -125       C  
ATOM   4616  C   THR B1031      72.908  11.788  -3.213  1.00 88.66           C  
ANISOU 4616  C   THR B1031     5997  18071   9617    191   2094    -75       C  
ATOM   4617  O   THR B1031      71.899  12.259  -2.668  1.00 85.87           O  
ANISOU 4617  O   THR B1031     5499  17600   9529    180   2091     17       O  
ATOM   4618  CB  THR B1031      74.564  13.223  -4.439  1.00 88.56           C  
ANISOU 4618  CB  THR B1031     5885  18000   9763    326   2493    254       C  
ATOM   4619  OG1 THR B1031      75.846  13.856  -4.343  1.00 97.44           O  
ANISOU 4619  OG1 THR B1031     6917  18940  11166    362   2757    224       O  
ATOM   4620  CG2 THR B1031      73.509  14.275  -4.724  1.00 90.66           C  
ANISOU 4620  CG2 THR B1031     5931  18202  10312    372   2526    650       C  
ATOM   4621  N   LYS B1032      72.873  10.648  -3.909  1.00 89.18           N  
ANISOU 4621  N   LYS B1032     6245  18360   9280    171   1892   -151       N  
ATOM   4622  CA  LYS B1032      71.637   9.872  -3.978  1.00 86.13           C  
ANISOU 4622  CA  LYS B1032     5872  18072   8781    117   1609   -147       C  
ATOM   4623  C   LYS B1032      71.192   9.400  -2.594  1.00 83.98           C  
ANISOU 4623  C   LYS B1032     5540  17633   8735     63   1590   -343       C  
ATOM   4624  O   LYS B1032      69.997   9.447  -2.267  1.00 87.60           O  
ANISOU 4624  O   LYS B1032     5875  18035   9375     46   1498   -219       O  
ATOM   4625  CB  LYS B1032      71.802   8.697  -4.943  1.00 87.32           C  
ANISOU 4625  CB  LYS B1032     6225  18455   8498     85   1410   -302       C  
ATOM   4626  CG  LYS B1032      71.881   9.135  -6.409  1.00 90.71           C  
ANISOU 4626  CG  LYS B1032     6734  19157   8575    140   1385    -59       C  
ATOM   4627  CD  LYS B1032      72.020   7.960  -7.366  1.00 92.78           C  
ANISOU 4627  CD  LYS B1032     7230  19673   8349     95   1205   -315       C  
ATOM   4628  CE  LYS B1032      73.472   7.597  -7.598  1.00 92.56           C  
ANISOU 4628  CE  LYS B1032     7368  19633   8166    142   1485   -542       C  
ATOM   4629  NZ  LYS B1032      73.601   6.424  -8.505  1.00 95.16           N  
ANISOU 4629  NZ  LYS B1032     7929  20170   8057     96   1370   -870       N  
ATOM   4630  N   MET B1033      72.137   8.931  -1.771  1.00 85.03           N  
ANISOU 4630  N   MET B1033     5741  17700   8865     42   1684   -605       N  
ATOM   4631  CA  MET B1033      71.798   8.511  -0.412  1.00 85.62           C  
ANISOU 4631  CA  MET B1033     5769  17685   9078      6   1689   -739       C  
ATOM   4632  C   MET B1033      71.246   9.670   0.404  1.00 88.49           C  
ANISOU 4632  C   MET B1033     5996  17909   9719     24   1870   -674       C  
ATOM   4633  O   MET B1033      70.297   9.497   1.177  1.00100.09           O  
ANISOU 4633  O   MET B1033     7399  19324  11306     17   1878   -653       O  
ATOM   4634  CB  MET B1033      73.020   7.916   0.284  1.00 85.20           C  
ANISOU 4634  CB  MET B1033     5784  17632   8955    -16   1734   -962       C  
ATOM   4635  CG  MET B1033      73.363   6.510  -0.154  1.00 89.23           C  
ANISOU 4635  CG  MET B1033     6380  18203   9320    -37   1595  -1060       C  
ATOM   4636  SD  MET B1033      74.826   5.858   0.670  1.00 85.03           S  
ANISOU 4636  SD  MET B1033     5849  17641   8819    -52   1652  -1217       S  
ATOM   4637  CE  MET B1033      74.315   5.933   2.384  1.00 78.66           C  
ANISOU 4637  CE  MET B1033     5005  16799   8084    -74   1627  -1191       C  
ATOM   4638  N   ARG B1034      71.841  10.855   0.261  1.00 81.84           N  
ANISOU 4638  N   ARG B1034     5124  16931   9040     50   2041   -648       N  
ATOM   4639  CA  ARG B1034      71.357  12.018   0.990  1.00 82.88           C  
ANISOU 4639  CA  ARG B1034     5163  16802   9524     59   2234   -642       C  
ATOM   4640  C   ARG B1034      69.939  12.364   0.565  1.00 84.28           C  
ANISOU 4640  C   ARG B1034     5141  16972   9909     96   2244   -343       C  
ATOM   4641  O   ARG B1034      69.091  12.671   1.406  1.00 84.94           O  
ANISOU 4641  O   ARG B1034     5161  16877  10237     98   2368   -363       O  
ATOM   4642  CB  ARG B1034      72.288  13.208   0.768  1.00 83.95           C  
ANISOU 4642  CB  ARG B1034     5239  16748   9911     75   2419   -659       C  
ATOM   4643  CG  ARG B1034      72.103  14.327   1.780  1.00 85.39           C  
ANISOU 4643  CG  ARG B1034     5321  16639  10485     57   2653   -831       C  
ATOM   4644  CD  ARG B1034      72.645  15.646   1.258  1.00 87.36           C  
ANISOU 4644  CD  ARG B1034     5377  16645  11171     89   2868   -727       C  
ATOM   4645  NE  ARG B1034      72.572  16.700   2.266  1.00 89.33           N  
ANISOU 4645  NE  ARG B1034     5498  16602  11842     53   3115   -998       N  
ATOM   4646  CZ  ARG B1034      71.563  17.556   2.380  1.00 91.42           C  
ANISOU 4646  CZ  ARG B1034     5566  16624  12546     92   3342   -877       C  
ATOM   4647  NH1 ARG B1034      70.537  17.489   1.543  1.00 92.05           N  
ANISOU 4647  NH1 ARG B1034     5528  16739  12709    161   3309   -438       N  
ATOM   4648  NH2 ARG B1034      71.580  18.481   3.329  1.00 93.75           N  
ANISOU 4648  NH2 ARG B1034     5761  16649  13213     54   3595  -1208       N  
ATOM   4649  N   ALA B1035      69.667  12.324  -0.742  1.00 90.30           N  
ANISOU 4649  N   ALA B1035     5838  17893  10579    126   2100    -44       N  
ATOM   4650  CA  ALA B1035      68.312  12.584  -1.219  1.00 87.19           C  
ANISOU 4650  CA  ALA B1035     5263  17467  10397    149   2006    304       C  
ATOM   4651  C   ALA B1035      67.318  11.584  -0.636  1.00 86.60           C  
ANISOU 4651  C   ALA B1035     5187  17402  10315    108   1851    244       C  
ATOM   4652  O   ALA B1035      66.228  11.968  -0.193  1.00 87.83           O  
ANISOU 4652  O   ALA B1035     5145  17386  10840    127   1945    407       O  
ATOM   4653  CB  ALA B1035      68.275  12.552  -2.747  1.00 89.04           C  
ANISOU 4653  CB  ALA B1035     5510  17929  10394    172   1779    622       C  
ATOM   4654  N   ALA B1036      67.678  10.298  -0.620  1.00 85.12           N  
ANISOU 4654  N   ALA B1036     5180  17371   9792     59   1651     33       N  
ATOM   4655  CA  ALA B1036      66.771   9.283  -0.085  1.00 91.54           C  
ANISOU 4655  CA  ALA B1036     5947  18157  10677     26   1520     12       C  
ATOM   4656  C   ALA B1036      66.517   9.495   1.407  1.00 95.27           C  
ANISOU 4656  C   ALA B1036     6367  18476  11356     52   1812    -93       C  
ATOM   4657  O   ALA B1036      65.364   9.475   1.869  1.00 97.07           O  
ANISOU 4657  O   ALA B1036     6429  18573  11881     72   1878     64       O  
ATOM   4658  CB  ALA B1036      67.335   7.886  -0.344  1.00 89.69           C  
ANISOU 4658  CB  ALA B1036     5879  18064  10134    -27   1300   -203       C  
ATOM   4659  N   ALA B1037      67.588   9.702   2.178  1.00 85.38           N  
ANISOU 4659  N   ALA B1037     5254  17246   9938     52   1991   -358       N  
ATOM   4660  CA  ALA B1037      67.439   9.909   3.614  1.00 83.83           C  
ANISOU 4660  CA  ALA B1037     5149  16886   9816     67   2220   -501       C  
ATOM   4661  C   ALA B1037      66.639  11.172   3.902  1.00 85.55           C  
ANISOU 4661  C   ALA B1037     5230  16847  10428    108   2498   -419       C  
ATOM   4662  O   ALA B1037      65.859  11.220   4.860  1.00 92.67           O  
ANISOU 4662  O   ALA B1037     6103  17624  11482    140   2711   -427       O  
ATOM   4663  CB  ALA B1037      68.812   9.975   4.282  1.00 82.67           C  
ANISOU 4663  CB  ALA B1037     5213  16792   9404     36   2255   -798       C  
ATOM   4664  N   LEU B1038      66.827  12.209   3.084  1.00 86.31           N  
ANISOU 4664  N   LEU B1038     5215  16848  10732    120   2545   -316       N  
ATOM   4665  CA  LEU B1038      66.029  13.420   3.208  1.00 89.42           C  
ANISOU 4665  CA  LEU B1038     5398  16943  11634    165   2827   -181       C  
ATOM   4666  C   LEU B1038      64.558  13.128   2.935  1.00 91.01           C  
ANISOU 4666  C   LEU B1038     5355  17089  12133    198   2775    175       C  
ATOM   4667  O   LEU B1038      63.674  13.676   3.603  1.00 92.14           O  
ANISOU 4667  O   LEU B1038     5364  16955  12690    239   3070    221       O  
ATOM   4668  CB  LEU B1038      66.567  14.488   2.252  1.00 89.63           C  
ANISOU 4668  CB  LEU B1038     5297  16885  11873    181   2864    -38       C  
ATOM   4669  CG  LEU B1038      66.206  15.945   2.543  1.00 95.26           C  
ANISOU 4669  CG  LEU B1038     5791  17204  13201    219   3241     -7       C  
ATOM   4670  CD1 LEU B1038      66.712  16.335   3.923  1.00 97.47           C  
ANISOU 4670  CD1 LEU B1038     6222  17335  13478    190   3530   -505       C  
ATOM   4671  CD2 LEU B1038      66.774  16.877   1.482  1.00 93.61           C  
ANISOU 4671  CD2 LEU B1038     5419  16915  13234    247   3257    236       C  
ATOM   4672  N   ASP B1039      64.280  12.264   1.951  1.00 97.69           N  
ANISOU 4672  N   ASP B1039     6113  18198  12806    175   2408    414       N  
ATOM   4673  CA  ASP B1039      62.898  11.894   1.654  1.00 91.58           C  
ANISOU 4673  CA  ASP B1039     5094  17350  12351    183   2262    757       C  
ATOM   4674  C   ASP B1039      62.261  11.172   2.831  1.00 91.23           C  
ANISOU 4674  C   ASP B1039     5059  17204  12401    200   2427    658       C  
ATOM   4675  O   ASP B1039      61.065  11.337   3.098  1.00 93.40           O  
ANISOU 4675  O   ASP B1039     5110  17230  13146    238   2553    898       O  
ATOM   4676  CB  ASP B1039      62.836  11.014   0.406  1.00 93.78           C  
ANISOU 4676  CB  ASP B1039     5409  17859  12365    121   1754    908       C  
ATOM   4677  CG  ASP B1039      62.460  11.789  -0.839  1.00103.12           C  
ANISOU 4677  CG  ASP B1039     6406  19076  13698    130   1562   1304       C  
ATOM   4678  OD1 ASP B1039      62.364  13.031  -0.760  1.00106.48           O  
ANISOU 4678  OD1 ASP B1039     6654  19309  14494    194   1849   1491       O  
ATOM   4679  OD2 ASP B1039      62.255  11.155  -1.897  1.00106.75           O  
ANISOU 4679  OD2 ASP B1039     6884  19762  13912     71   1126   1431       O  
ATOM   4680  N   ALA B1040      63.041  10.355   3.540  1.00 98.03           N  
ANISOU 4680  N   ALA B1040     6186  18210  12851    178   2430    354       N  
ATOM   4681  CA  ALA B1040      62.490   9.637   4.684  1.00 95.21           C  
ANISOU 4681  CA  ALA B1040     5862  17771  12543    212   2602    328       C  
ATOM   4682  C   ALA B1040      62.318  10.526   5.911  1.00 96.08           C  
ANISOU 4682  C   ALA B1040     6062  17665  12781    272   3081    171       C  
ATOM   4683  O   ALA B1040      61.622  10.129   6.850  1.00 92.96           O  
ANISOU 4683  O   ALA B1040     5651  17184  12487    324   3313    223       O  
ATOM   4684  CB  ALA B1040      63.372   8.437   5.038  1.00 98.46           C  
ANISOU 4684  CB  ALA B1040     6485  18422  12505    178   2439    140       C  
ATOM   4685  N   GLY B1041      62.931  11.705   5.930  1.00101.56           N  
ANISOU 4685  N   GLY B1041     6829  18269  13490    266   3258    -31       N  
ATOM   4686  CA  GLY B1041      62.752  12.646   7.021  1.00106.70           C  
ANISOU 4686  CA  GLY B1041     7526  18712  14302    310   3732   -253       C  
ATOM   4687  C   GLY B1041      64.009  13.432   7.348  1.00110.22           C  
ANISOU 4687  C   GLY B1041     8173  19213  14492    267   3811   -656       C  
ATOM   4688  O   GLY B1041      64.104  14.625   7.055  1.00110.05           O  
ANISOU 4688  O   GLY B1041     8024  18957  14832    271   3994   -712       O  
ATOM   4689  N   GLY B1065      65.616  12.744  12.863  1.00104.98           N  
ANISOU 4689  N   GLY B1065     8491  19552  11843    235   4461  -1996       N  
ATOM   4690  CA  GLY B1065      65.964  11.735  11.881  1.00107.67           C  
ANISOU 4690  CA  GLY B1065     8747  19973  12189    216   4027  -1646       C  
ATOM   4691  C   GLY B1065      66.967  12.232  10.857  1.00117.30           C  
ANISOU 4691  C   GLY B1065     9905  21130  13533    126   3750  -1775       C  
ATOM   4692  O   GLY B1065      67.053  11.714   9.741  1.00109.15           O  
ANISOU 4692  O   GLY B1065     8776  20038  12657    123   3467  -1491       O  
ATOM   4693  N   ASP B1066      67.738  13.248  11.239  1.00126.90           N  
ANISOU 4693  N   ASP B1066    11167  22362  14686     51   3850  -2229       N  
ATOM   4694  CA  ASP B1066      68.686  13.870  10.326  1.00131.32           C  
ANISOU 4694  CA  ASP B1066    11628  22807  15461    -22   3670  -2342       C  
ATOM   4695  C   ASP B1066      70.125  13.717  10.805  1.00139.40           C  
ANISOU 4695  C   ASP B1066    12735  24190  16041   -133   3449  -2700       C  
ATOM   4696  O   ASP B1066      71.033  14.323  10.219  1.00143.19           O  
ANISOU 4696  O   ASP B1066    13110  24574  16723   -200   3352  -2856       O  
ATOM   4697  CB  ASP B1066      68.322  15.345  10.100  1.00130.65           C  
ANISOU 4697  CB  ASP B1066    11383  22306  15953    -17   3995  -2510       C  
ATOM   4698  CG  ASP B1066      68.869  16.272  11.175  1.00132.70           C  
ANISOU 4698  CG  ASP B1066    11701  22610  16109   -107   4226  -3151       C  
ATOM   4699  OD1 ASP B1066      69.260  17.406  10.824  1.00131.47           O  
ANISOU 4699  OD1 ASP B1066    11381  22152  16419   -156   4350  -3382       O  
ATOM   4700  OD2 ASP B1066      68.912  15.877  12.360  1.00134.56           O  
ANISOU 4700  OD2 ASP B1066    12133  23187  15808   -132   4283  -3428       O  
ATOM   4701  N   ILE B1067      70.365  12.911  11.844  1.00134.53           N  
ANISOU 4701  N   ILE B1067    12264  23998  14854   -148   3372  -2783       N  
ATOM   4702  CA  ILE B1067      71.744  12.563  12.167  1.00122.16           C  
ANISOU 4702  CA  ILE B1067    10702  22836  12877   -248   3094  -3002       C  
ATOM   4703  C   ILE B1067      72.317  11.713  11.046  1.00104.25           C  
ANISOU 4703  C   ILE B1067     8352  20526  10733   -233   2775  -2627       C  
ATOM   4704  O   ILE B1067      73.528  11.736  10.787  1.00110.20           O  
ANISOU 4704  O   ILE B1067     9067  21336  11468   -310   2541  -2739       O  
ATOM   4705  CB  ILE B1067      71.818  11.853  13.533  1.00126.13           C  
ANISOU 4705  CB  ILE B1067    11361  23857  12706   -252   3072  -3074       C  
ATOM   4706  CG1 ILE B1067      71.149  10.478  13.476  1.00126.52           C  
ANISOU 4706  CG1 ILE B1067    11438  23972  12661   -135   2993  -2498       C  
ATOM   4707  CG2 ILE B1067      71.160  12.704  14.608  1.00129.05           C  
ANISOU 4707  CG2 ILE B1067    11879  24234  12920   -256   3428  -3467       C  
ATOM   4708  CD1 ILE B1067      72.134   9.327  13.411  1.00122.50           C  
ANISOU 4708  CD1 ILE B1067    10873  23784  11888   -158   2634  -2257       C  
ATOM   4709  N   LEU B1068      71.458  10.951  10.366  1.00 95.32           N  
ANISOU 4709  N   LEU B1068     7232  19209   9778   -139   2734  -2183       N  
ATOM   4710  CA  LEU B1068      71.873  10.260   9.155  1.00 87.06           C  
ANISOU 4710  CA  LEU B1068     6134  18059   8886   -128   2480  -1904       C  
ATOM   4711  C   LEU B1068      72.356  11.264   8.122  1.00 90.48           C  
ANISOU 4711  C   LEU B1068     6492  18216   9670   -155   2490  -1987       C  
ATOM   4712  O   LEU B1068      73.386  11.056   7.473  1.00100.48           O  
ANISOU 4712  O   LEU B1068     7729  19504  10946   -185   2316  -1971       O  
ATOM   4713  CB  LEU B1068      70.718   9.423   8.605  1.00 85.64           C  
ANISOU 4713  CB  LEU B1068     5940  17735   8866    -45   2460  -1519       C  
ATOM   4714  CG  LEU B1068      71.012   8.523   7.406  1.00 84.04           C  
ANISOU 4714  CG  LEU B1068     5699  17483   8750    -41   2210  -1296       C  
ATOM   4715  CD1 LEU B1068      72.263   7.694   7.634  1.00 82.49           C  
ANISOU 4715  CD1 LEU B1068     5513  17517   8314    -80   2022  -1340       C  
ATOM   4716  CD2 LEU B1068      69.818   7.621   7.137  1.00 84.07           C  
ANISOU 4716  CD2 LEU B1068     5627  17422   8894     15   2189  -1006       C  
ATOM   4717  N   VAL B1069      71.614  12.364   7.960  1.00 87.56           N  
ANISOU 4717  N   VAL B1069     6061  17566   9642   -131   2732  -2032       N  
ATOM   4718  CA  VAL B1069      72.013  13.411   7.025  1.00 90.31           C  
ANISOU 4718  CA  VAL B1069     6285  17638  10389   -138   2794  -2036       C  
ATOM   4719  C   VAL B1069      73.332  14.038   7.457  1.00 99.05           C  
ANISOU 4719  C   VAL B1069     7327  18817  11491   -235   2786  -2429       C  
ATOM   4720  O   VAL B1069      74.172  14.380   6.620  1.00101.96           O  
ANISOU 4720  O   VAL B1069     7603  19054  12082   -245   2722  -2367       O  
ATOM   4721  CB  VAL B1069      70.899  14.466   6.900  1.00 89.89           C  
ANISOU 4721  CB  VAL B1069     6107  17257  10790    -86   3095  -1967       C  
ATOM   4722  CG1 VAL B1069      71.283  15.542   5.893  1.00 89.93           C  
ANISOU 4722  CG1 VAL B1069     5929  16974  11267    -74   3178  -1863       C  
ATOM   4723  CG2 VAL B1069      69.589  13.807   6.505  1.00 99.03           C  
ANISOU 4723  CG2 VAL B1069     7251  18381  11996     -5   3076  -1578       C  
ATOM   4724  N   GLY B1070      73.549  14.178   8.765  1.00 96.43           N  
ANISOU 4724  N   GLY B1070     7017  18729  10892   -311   2854  -2846       N  
ATOM   4725  CA  GLY B1070      74.812  14.732   9.229  1.00100.13           C  
ANISOU 4725  CA  GLY B1070     7443  19231  11369   -431   2748  -3245       C  
ATOM   4726  C   GLY B1070      75.993  13.823   8.936  1.00105.39           C  
ANISOU 4726  C   GLY B1070     8129  20082  11832   -462   2404  -3093       C  
ATOM   4727  O   GLY B1070      77.053  14.283   8.494  1.00112.70           O  
ANISOU 4727  O   GLY B1070     8930  20852  13039   -516   2318  -3174       O  
ATOM   4728  N   GLN B1071      75.823  12.519   9.156  1.00100.68           N  
ANISOU 4728  N   GLN B1071     7647  19774  10832   -420   2236  -2841       N  
ATOM   4729  CA  GLN B1071      76.900  11.583   8.848  1.00 99.60           C  
ANISOU 4729  CA  GLN B1071     7491  19761  10592   -437   1954  -2663       C  
ATOM   4730  C   GLN B1071      77.148  11.503   7.346  1.00 95.83           C  
ANISOU 4730  C   GLN B1071     6931  19039  10442   -371   1985  -2394       C  
ATOM   4731  O   GLN B1071      78.302  11.413   6.901  1.00108.99           O  
ANISOU 4731  O   GLN B1071     8516  20643  12254   -397   1872  -2372       O  
ATOM   4732  CB  GLN B1071      76.580  10.203   9.419  1.00 97.22           C  
ANISOU 4732  CB  GLN B1071     7280  19767   9890   -396   1817  -2419       C  
ATOM   4733  CG  GLN B1071      76.358  10.173  10.919  1.00107.25           C  
ANISOU 4733  CG  GLN B1071     8653  21376  10723   -440   1797  -2605       C  
ATOM   4734  CD  GLN B1071      76.018   8.783  11.427  1.00109.12           C  
ANISOU 4734  CD  GLN B1071     8928  21896  10635   -372   1701  -2244       C  
ATOM   4735  OE1 GLN B1071      75.854   7.846  10.643  1.00111.17           O  
ANISOU 4735  OE1 GLN B1071     9127  22042  11069   -302   1661  -1906       O  
ATOM   4736  NE2 GLN B1071      75.914   8.642  12.745  1.00103.67           N  
ANISOU 4736  NE2 GLN B1071     8330  21581   9478   -394   1676  -2319       N  
ATOM   4737  N   ILE B1072      76.079  11.543   6.548  1.00 84.64           N  
ANISOU 4737  N   ILE B1072     5552  17465   9140   -282   2125  -2167       N  
ATOM   4738  CA  ILE B1072      76.235  11.588   5.097  1.00 85.56           C  
ANISOU 4738  CA  ILE B1072     5685  17340   9484   -218   2129  -1902       C  
ATOM   4739  C   ILE B1072      76.955  12.862   4.674  1.00 93.50           C  
ANISOU 4739  C   ILE B1072     6538  18111  10875   -237   2272  -2000       C  
ATOM   4740  O   ILE B1072      77.761  12.851   3.739  1.00 91.70           O  
ANISOU 4740  O   ILE B1072     6275  17778  10788   -204   2271  -1847       O  
ATOM   4741  CB  ILE B1072      74.865  11.450   4.405  1.00 85.47           C  
ANISOU 4741  CB  ILE B1072     5747  17226   9501   -140   2180  -1635       C  
ATOM   4742  CG1 ILE B1072      74.289  10.052   4.631  1.00 86.04           C  
ANISOU 4742  CG1 ILE B1072     5911  17480   9301   -123   2029  -1513       C  
ATOM   4743  CG2 ILE B1072      74.979  11.729   2.919  1.00 81.64           C  
ANISOU 4743  CG2 ILE B1072     5234  16613   9172    -80   2212  -1391       C  
ATOM   4744  CD1 ILE B1072      72.954   9.824   3.948  1.00 90.27           C  
ANISOU 4744  CD1 ILE B1072     6439  17959   9902    -68   2036  -1277       C  
ATOM   4745  N   ASP B1073      76.685  13.979   5.355  1.00 95.53           N  
ANISOU 4745  N   ASP B1073     6681  18262  11354   -284   2438  -2262       N  
ATOM   4746  CA  ASP B1073      77.376  15.225   5.035  1.00 97.43           C  
ANISOU 4746  CA  ASP B1073     6709  18219  12089   -311   2594  -2376       C  
ATOM   4747  C   ASP B1073      78.861  15.129   5.362  1.00100.56           C  
ANISOU 4747  C   ASP B1073     6997  18676  12535   -404   2439  -2592       C  
ATOM   4748  O   ASP B1073      79.703  15.637   4.612  1.00 91.65           O  
ANISOU 4748  O   ASP B1073     5700  17326  11797   -386   2517  -2483       O  
ATOM   4749  CB  ASP B1073      76.735  16.388   5.794  1.00 96.52           C  
ANISOU 4749  CB  ASP B1073     6475  17931  12267   -359   2825  -2696       C  
ATOM   4750  CG  ASP B1073      75.411  16.821   5.190  1.00100.74           C  
ANISOU 4750  CG  ASP B1073     7028  18223  13027   -249   3021  -2363       C  
ATOM   4751  OD1 ASP B1073      75.234  16.668   3.963  1.00100.84           O  
ANISOU 4751  OD1 ASP B1073     7043  18156  13116   -150   3005  -1902       O  
ATOM   4752  OD2 ASP B1073      74.545  17.312   5.946  1.00106.00           O  
ANISOU 4752  OD2 ASP B1073     7678  18808  13788   -264   3204  -2569       O  
ATOM   4753  N   ASP B1074      79.198  14.475   6.475  1.00107.62           N  
ANISOU 4753  N   ASP B1074     7995  19834  13060   -495   2202  -2831       N  
ATOM   4754  CA  ASP B1074      80.603  14.233   6.798  1.00111.31           C  
ANISOU 4754  CA  ASP B1074     8369  20349  13573   -586   1966  -2952       C  
ATOM   4755  C   ASP B1074      81.276  13.398   5.713  1.00103.34           C  
ANISOU 4755  C   ASP B1074     7334  19314  12616   -498   1937  -2571       C  
ATOM   4756  O   ASP B1074      82.383  13.720   5.254  1.00 97.89           O  
ANISOU 4756  O   ASP B1074     6464  18429  12302   -513   1948  -2536       O  
ATOM   4757  CB  ASP B1074      80.718  13.544   8.159  1.00112.11           C  
ANISOU 4757  CB  ASP B1074     8590  20824  13185   -682   1685  -3164       C  
ATOM   4758  CG  ASP B1074      80.211  14.409   9.297  1.00113.88           C  
ANISOU 4758  CG  ASP B1074     8863  21110  13295   -780   1735  -3633       C  
ATOM   4759  OD1 ASP B1074      80.157  15.645   9.130  1.00114.67           O  
ANISOU 4759  OD1 ASP B1074     8831  20886  13852   -817   1939  -3888       O  
ATOM   4760  OD2 ASP B1074      79.865  13.851  10.359  1.00116.37           O  
ANISOU 4760  OD2 ASP B1074     9341  21795  13080   -816   1602  -3743       O  
ATOM   4761  N   ALA B1075      80.621  12.309   5.299  1.00 94.39           N  
ANISOU 4761  N   ALA B1075     6364  18354  11145   -409   1923  -2305       N  
ATOM   4762  CA  ALA B1075      81.168  11.470   4.236  1.00 84.74           C  
ANISOU 4762  CA  ALA B1075     5147  17105   9946   -326   1943  -2017       C  
ATOM   4763  C   ALA B1075      81.307  12.245   2.929  1.00 86.45           C  
ANISOU 4763  C   ALA B1075     5346  17021  10480   -236   2180  -1817       C  
ATOM   4764  O   ALA B1075      82.278  12.058   2.187  1.00 85.28           O  
ANISOU 4764  O   ALA B1075     5137  16752  10513   -192   2253  -1671       O  
ATOM   4765  CB  ALA B1075      80.291  10.235   4.037  1.00 82.67           C  
ANISOU 4765  CB  ALA B1075     5089  17001   9321   -263   1876  -1835       C  
ATOM   4766  N   LEU B1076      80.338  13.109   2.624  1.00 92.95           N  
ANISOU 4766  N   LEU B1076     6207  17719  11393   -196   2328  -1756       N  
ATOM   4767  CA  LEU B1076      80.403  13.910   1.406  1.00 89.24           C  
ANISOU 4767  CA  LEU B1076     5677  17009  11219    -98   2561  -1479       C  
ATOM   4768  C   LEU B1076      81.568  14.891   1.452  1.00 94.41           C  
ANISOU 4768  C   LEU B1076     6052  17408  12412   -131   2691  -1556       C  
ATOM   4769  O   LEU B1076      82.258  15.090   0.447  1.00 89.28           O  
ANISOU 4769  O   LEU B1076     5329  16608  11985    -43   2869  -1287       O  
ATOM   4770  CB  LEU B1076      79.079  14.649   1.199  1.00 89.95           C  
ANISOU 4770  CB  LEU B1076     5780  17027  11372    -54   2677  -1356       C  
ATOM   4771  CG  LEU B1076      78.107  14.047   0.180  1.00 87.97           C  
ANISOU 4771  CG  LEU B1076     5694  16938  10793     39   2655  -1040       C  
ATOM   4772  CD1 LEU B1076      76.803  14.829   0.137  1.00 86.00           C  
ANISOU 4772  CD1 LEU B1076     5365  16611  10701     68   2749   -899       C  
ATOM   4773  CD2 LEU B1076      78.741  13.996  -1.201  1.00 92.85           C  
ANISOU 4773  CD2 LEU B1076     6312  17581  11385    138   2786   -742       C  
ATOM   4774  N   LYS B1077      81.798  15.514   2.611  1.00100.21           N  
ANISOU 4774  N   LYS B1077     6604  18102  13370   -264   2619  -1946       N  
ATOM   4775  CA  LYS B1077      82.954  16.392   2.761  1.00 96.09           C  
ANISOU 4775  CA  LYS B1077     5763  17312  13436   -333   2684  -2098       C  
ATOM   4776  C   LYS B1077      84.253  15.624   2.571  1.00 97.94           C  
ANISOU 4776  C   LYS B1077     5920  17592  13702   -340   2573  -2018       C  
ATOM   4777  O   LYS B1077      85.177  16.102   1.901  1.00 96.04           O  
ANISOU 4777  O   LYS B1077     5483  17060  13947   -292   2741  -1828       O  
ATOM   4778  CB  LYS B1077      82.934  17.065   4.133  1.00 95.22           C  
ANISOU 4778  CB  LYS B1077     5546  17162  13473   -506   2543  -2632       C  
ATOM   4779  CG  LYS B1077      84.092  18.020   4.354  1.00 99.67           C  
ANISOU 4779  CG  LYS B1077     5773  17377  14720   -610   2546  -2855       C  
ATOM   4780  CD  LYS B1077      84.029  18.682   5.718  1.00104.76           C  
ANISOU 4780  CD  LYS B1077     6365  17995  15443   -803   2373  -3476       C  
ATOM   4781  CE  LYS B1077      85.300  19.474   5.994  1.00111.79           C  
ANISOU 4781  CE  LYS B1077     6897  18554  17023   -942   2275  -3754       C  
ATOM   4782  NZ  LYS B1077      85.314  20.059   7.363  1.00118.90           N  
ANISOU 4782  NZ  LYS B1077     7771  19483  17921  -1162   2046  -4459       N  
ATOM   4783  N   LEU B1078      84.343  14.430   3.163  1.00105.48           N  
ANISOU 4783  N   LEU B1078     7035  18840  14201   -387   2302  -2098       N  
ATOM   4784  CA  LEU B1078      85.518  13.588   2.962  1.00 93.65           C  
ANISOU 4784  CA  LEU B1078     5456  17347  12780   -380   2213  -1965       C  
ATOM   4785  C   LEU B1078      85.728  13.266   1.486  1.00 90.78           C  
ANISOU 4785  C   LEU B1078     5172  16858  12463   -207   2517  -1570       C  
ATOM   4786  O   LEU B1078      86.854  13.336   0.981  1.00105.30           O  
ANISOU 4786  O   LEU B1078     6826  18482  14701   -167   2655  -1419       O  
ATOM   4787  CB  LEU B1078      85.377  12.302   3.774  1.00 90.03           C  
ANISOU 4787  CB  LEU B1078     5154  17210  11842   -431   1909  -2024       C  
ATOM   4788  CG  LEU B1078      85.516  12.476   5.285  1.00 92.84           C  
ANISOU 4788  CG  LEU B1078     5457  17730  12086   -601   1560  -2361       C  
ATOM   4789  CD1 LEU B1078      85.331  11.148   5.996  1.00 95.01           C  
ANISOU 4789  CD1 LEU B1078     5866  18349  11885   -616   1303  -2280       C  
ATOM   4790  CD2 LEU B1078      86.860  13.094   5.631  1.00 95.36           C  
ANISOU 4790  CD2 LEU B1078     5460  17843  12930   -718   1413  -2505       C  
ATOM   4791  N   ALA B1079      84.653  12.916   0.778  1.00 88.65           N  
ANISOU 4791  N   ALA B1079     5202  16696  11784   -103   2614  -1396       N  
ATOM   4792  CA  ALA B1079      84.774  12.560  -0.633  1.00 88.64           C  
ANISOU 4792  CA  ALA B1079     5345  16646  11691     48   2869  -1076       C  
ATOM   4793  C   ALA B1079      85.154  13.762  -1.489  1.00104.34           C  
ANISOU 4793  C   ALA B1079     7163  18372  14111    140   3194   -826       C  
ATOM   4794  O   ALA B1079      85.905  13.623  -2.461  1.00102.11           O  
ANISOU 4794  O   ALA B1079     6861  17993  13942    250   3457   -585       O  
ATOM   4795  CB  ALA B1079      83.471  11.939  -1.132  1.00 87.72           C  
ANISOU 4795  CB  ALA B1079     5538  16764  11029    101   2823  -1007       C  
ATOM   4796  N   ASN B1080      84.637  14.948  -1.154  1.00108.48           N  
ANISOU 4796  N   ASN B1080     7541  18760  14918    106   3226   -862       N  
ATOM   4797  CA  ASN B1080      84.949  16.144  -1.933  1.00117.28           C  
ANISOU 4797  CA  ASN B1080     8423  19586  16550    200   3560   -563       C  
ATOM   4798  C   ASN B1080      86.435  16.476  -1.888  1.00115.14           C  
ANISOU 4798  C   ASN B1080     7833  19029  16886    192   3681   -531       C  
ATOM   4799  O   ASN B1080      86.962  17.094  -2.821  1.00119.25           O  
ANISOU 4799  O   ASN B1080     8180  19336  17793    322   4034   -161       O  
ATOM   4800  CB  ASN B1080      84.130  17.332  -1.428  1.00124.47           C  
ANISOU 4800  CB  ASN B1080     9177  20340  17775    152   3575   -644       C  
ATOM   4801  CG  ASN B1080      82.683  17.282  -1.883  1.00124.30           C  
ANISOU 4801  CG  ASN B1080     9372  20514  17341    216   3582   -470       C  
ATOM   4802  OD1 ASN B1080      82.388  16.925  -3.024  1.00122.60           O  
ANISOU 4802  OD1 ASN B1080     9324  20471  16788    335   3692   -131       O  
ATOM   4803  ND2 ASN B1080      81.772  17.647  -0.990  1.00125.12           N  
ANISOU 4803  ND2 ASN B1080     9470  20610  17462    130   3456   -717       N  
ATOM   4804  N   GLU B1081      87.121  16.081  -0.819  1.00108.50           N  
ANISOU 4804  N   GLU B1081     6879  18186  16158     40   3391   -883       N  
ATOM   4805  CA  GLU B1081      88.552  16.299  -0.675  1.00102.84           C  
ANISOU 4805  CA  GLU B1081     5842  17191  16043      3   3410   -868       C  
ATOM   4806  C   GLU B1081      89.381  15.199  -1.329  1.00106.28           C  
ANISOU 4806  C   GLU B1081     6336  17688  16357    102   3537   -645       C  
ATOM   4807  O   GLU B1081      90.607  15.192  -1.180  1.00112.50           O  
ANISOU 4807  O   GLU B1081     6864  18258  17623     73   3521   -603       O  
ATOM   4808  CB  GLU B1081      88.912  16.420   0.807  1.00100.46           C  
ANISOU 4808  CB  GLU B1081     5342  16876  15951   -234   2999  -1375       C  
ATOM   4809  CG  GLU B1081      88.183  17.552   1.520  1.00101.65           C  
ANISOU 4809  CG  GLU B1081     5415  16918  16289   -347   2925  -1704       C  
ATOM   4810  CD  GLU B1081      88.374  17.521   3.024  1.00102.87           C  
ANISOU 4810  CD  GLU B1081     5433  17227  16428   -591   2503  -2300       C  
ATOM   4811  OE1 GLU B1081      89.479  17.162   3.482  1.00104.56           O  
ANISOU 4811  OE1 GLU B1081     5461  17405  16864   -692   2250  -2387       O  
ATOM   4812  OE2 GLU B1081      87.415  17.854   3.750  1.00102.64           O  
ANISOU 4812  OE2 GLU B1081     5555  17328  16116   -671   2398  -2625       O  
ATOM   4813  N   GLY B1082      88.743  14.277  -2.047  1.00105.16           N  
ANISOU 4813  N   GLY B1082     6547  17801  15608    208   3646   -529       N  
ATOM   4814  CA  GLY B1082      89.442  13.181  -2.684  1.00104.17           C  
ANISOU 4814  CA  GLY B1082     6519  17699  15363    297   3811   -399       C  
ATOM   4815  C   GLY B1082      89.879  12.069  -1.760  1.00102.48           C  
ANISOU 4815  C   GLY B1082     6260  17594  15082    182   3485   -624       C  
ATOM   4816  O   GLY B1082      90.641  11.196  -2.188  1.00116.27           O  
ANISOU 4816  O   GLY B1082     7989  19273  16916    251   3646   -513       O  
ATOM   4817  N   LYS B1083      89.421  12.069  -0.510  1.00 95.52           N  
ANISOU 4817  N   LYS B1083     5342  16885  14067     16   3065   -923       N  
ATOM   4818  CA  LYS B1083      89.798  11.051   0.470  1.00 94.45           C  
ANISOU 4818  CA  LYS B1083     5116  16911  13859    -98   2725  -1078       C  
ATOM   4819  C   LYS B1083      88.793   9.906   0.390  1.00 97.06           C  
ANISOU 4819  C   LYS B1083     5802  17527  13548    -59   2652  -1103       C  
ATOM   4820  O   LYS B1083      87.695   9.986   0.946  1.00 99.86           O  
ANISOU 4820  O   LYS B1083     6329  18113  13501   -116   2454  -1258       O  
ATOM   4821  CB  LYS B1083      89.864  11.661   1.865  1.00 95.96           C  
ANISOU 4821  CB  LYS B1083     5105  17169  14188   -295   2308  -1373       C  
ATOM   4822  CG  LYS B1083      90.660  12.958   1.910  1.00 98.60           C  
ANISOU 4822  CG  LYS B1083     5092  17161  15211   -355   2367  -1426       C  
ATOM   4823  CD  LYS B1083      90.641  13.596   3.288  1.00100.37           C  
ANISOU 4823  CD  LYS B1083     5191  17444  15501   -572   1928  -1821       C  
ATOM   4824  CE  LYS B1083      91.783  14.592   3.442  1.00106.41           C  
ANISOU 4824  CE  LYS B1083     5513  17819  17099   -670   1892  -1903       C  
ATOM   4825  NZ  LYS B1083      91.854  15.164   4.816  1.00110.19           N  
ANISOU 4825  NZ  LYS B1083     5871  18383  17612   -912   1413  -2380       N  
ATOM   4826  N   VAL B1084      89.176   8.830  -0.299  1.00 92.52           N  
ANISOU 4826  N   VAL B1084     6247  14995  13911   -302   4159   2077       N  
ATOM   4827  CA  VAL B1084      88.242   7.748  -0.603  1.00 92.00           C  
ANISOU 4827  CA  VAL B1084     6236  15090  13630   -322   4160   1969       C  
ATOM   4828  C   VAL B1084      88.102   6.787   0.575  1.00107.19           C  
ANISOU 4828  C   VAL B1084     8144  16914  15671   -276   4019   1819       C  
ATOM   4829  O   VAL B1084      86.989   6.377   0.927  1.00104.51           O  
ANISOU 4829  O   VAL B1084     7868  16646  15197   -248   3923   1813       O  
ATOM   4830  CB  VAL B1084      88.682   7.015  -1.884  1.00 93.76           C  
ANISOU 4830  CB  VAL B1084     6449  15453  13723   -413   4354   1850       C  
ATOM   4831  CG1 VAL B1084      87.758   5.843  -2.170  1.00 93.21           C  
ANISOU 4831  CG1 VAL B1084     6441  15531  13445   -433   4354   1730       C  
ATOM   4832  CG2 VAL B1084      88.703   7.978  -3.060  1.00 95.54           C  
ANISOU 4832  CG2 VAL B1084     6708  15783  13810   -461   4488   2006       C  
ATOM   4833  N   LYS B1085      89.227   6.396   1.186  1.00105.59           N  
ANISOU 4833  N   LYS B1085     7859  16547  15713   -268   4002   1696       N  
ATOM   4834  CA  LYS B1085      89.193   5.418   2.273  1.00117.06           C  
ANISOU 4834  CA  LYS B1085     9297  17899  17281   -227   3873   1543       C  
ATOM   4835  C   LYS B1085      88.321   5.904   3.425  1.00131.49           C  
ANISOU 4835  C   LYS B1085    11179  19633  19146   -150   3683   1644       C  
ATOM   4836  O   LYS B1085      87.523   5.139   3.990  1.00134.54           O  
ANISOU 4836  O   LYS B1085    11606  20048  19464   -127   3587   1564       O  
ATOM   4837  CB  LYS B1085      90.614   5.161   2.778  1.00120.46           C  
ANISOU 4837  CB  LYS B1085     9638  18144  17988   -219   3868   1435       C  
ATOM   4838  CG  LYS B1085      91.642   4.812   1.708  1.00125.80           C  
ANISOU 4838  CG  LYS B1085    10248  18889  18660   -291   4051   1347       C  
ATOM   4839  CD  LYS B1085      91.457   3.420   1.130  1.00126.30           C  
ANISOU 4839  CD  LYS B1085    10309  19109  18569   -341   4129   1161       C  
ATOM   4840  CE  LYS B1085      92.680   3.023   0.306  1.00123.54           C  
ANISOU 4840  CE  LYS B1085     9881  18788  18271   -399   4285   1062       C  
ATOM   4841  NZ  LYS B1085      92.497   1.734  -0.417  1.00123.79           N  
ANISOU 4841  NZ  LYS B1085     9913  18997  18124   -455   4379    895       N  
ATOM   4842  N   GLU B1086      88.458   7.182   3.779  1.00133.74           N  
ANISOU 4842  N   GLU B1086    11468  19809  19539   -111   3631   1821       N  
ATOM   4843  CA  GLU B1086      87.692   7.745   4.883  1.00134.57           C  
ANISOU 4843  CA  GLU B1086    11624  19815  19692    -38   3453   1926       C  
ATOM   4844  C   GLU B1086      86.206   7.778   4.553  1.00120.42           C  
ANISOU 4844  C   GLU B1086     9914  18214  17625    -33   3425   2009       C  
ATOM   4845  O   GLU B1086      85.364   7.491   5.413  1.00122.30           O  
ANISOU 4845  O   GLU B1086    10198  18428  17841     11   3287   1994       O  
ATOM   4846  CB  GLU B1086      88.220   9.145   5.193  1.00144.85           C  
ANISOU 4846  CB  GLU B1086    12910  20966  21159     -4   3423   2102       C  
ATOM   4847  CG  GLU B1086      89.742   9.194   5.296  1.00148.80           C  
ANISOU 4847  CG  GLU B1086    13329  21297  21912    -17   3474   2034       C  
ATOM   4848  CD  GLU B1086      90.280  10.583   5.576  1.00151.85           C  
ANISOU 4848  CD  GLU B1086    13703  21532  22462     14   3449   2207       C  
ATOM   4849  OE1 GLU B1086      89.626  11.342   6.321  1.00155.21           O  
ANISOU 4849  OE1 GLU B1086    14179  21886  22909     71   3320   2340       O  
ATOM   4850  OE2 GLU B1086      91.360  10.918   5.046  1.00152.16           O  
ANISOU 4850  OE2 GLU B1086    13681  21525  22607    -20   3560   2210       O  
ATOM   4851  N   ALA B1087      85.869   8.104   3.302  1.00108.87           N  
ANISOU 4851  N   ALA B1087     8477  16941  15949    -80   3554   2093       N  
ATOM   4852  CA  ALA B1087      84.475   8.082   2.876  1.00 98.90           C  
ANISOU 4852  CA  ALA B1087     7296  15873  14408    -78   3530   2168       C  
ATOM   4853  C   ALA B1087      83.896   6.674   2.947  1.00 99.46           C  
ANISOU 4853  C   ALA B1087     7394  16036  14359    -95   3512   1986       C  
ATOM   4854  O   ALA B1087      82.740   6.489   3.347  1.00108.92           O  
ANISOU 4854  O   ALA B1087     8655  17304  15426    -63   3405   2009       O  
ATOM   4855  CB  ALA B1087      84.355   8.646   1.461  1.00 87.13           C  
ANISOU 4855  CB  ALA B1087     5831  14558  12718   -129   3677   2282       C  
ATOM   4856  N   GLN B1088      84.684   5.665   2.568  1.00 87.57           N  
ANISOU 4856  N   GLN B1088     5840  14532  12898   -146   3614   1803       N  
ATOM   4857  CA  GLN B1088      84.195   4.290   2.626  1.00 95.07           C  
ANISOU 4857  CA  GLN B1088     6815  15563  13743   -164   3603   1624       C  
ATOM   4858  C   GLN B1088      83.972   3.840   4.067  1.00101.99           C  
ANISOU 4858  C   GLN B1088     7690  16294  14767   -105   3430   1545       C  
ATOM   4859  O   GLN B1088      82.986   3.147   4.368  1.00109.63           O  
ANISOU 4859  O   GLN B1088     8714  17339  15603    -93   3357   1487       O  
ATOM   4860  CB  GLN B1088      85.171   3.367   1.899  1.00101.03           C  
ANISOU 4860  CB  GLN B1088     7514  16342  14531   -230   3755   1449       C  
ATOM   4861  CG  GLN B1088      85.258   3.659   0.405  1.00110.16           C  
ANISOU 4861  CG  GLN B1088     8691  17658  15506   -297   3933   1511       C  
ATOM   4862  CD  GLN B1088      86.353   2.876  -0.297  1.00118.70           C  
ANISOU 4862  CD  GLN B1088     9710  18745  16647   -365   4093   1345       C  
ATOM   4863  OE1 GLN B1088      87.487   2.802   0.181  1.00120.08           O  
ANISOU 4863  OE1 GLN B1088     9795  18777  17054   -361   4093   1265       O  
ATOM   4864  NE2 GLN B1088      86.019   2.295  -1.445  1.00118.53           N  
ANISOU 4864  NE2 GLN B1088     9740  18888  16410   -426   4223   1297       N  
ATOM   4865  N   ALA B1089      84.868   4.233   4.975  1.00 93.94           N  
ANISOU 4865  N   ALA B1089     6615  15059  14021    -67   3361   1545       N  
ATOM   4866  CA  ALA B1089      84.647   3.939   6.388  1.00 95.96           C  
ANISOU 4866  CA  ALA B1089     6882  15156  14422     -8   3186   1491       C  
ATOM   4867  C   ALA B1089      83.389   4.636   6.900  1.00 96.32           C  
ANISOU 4867  C   ALA B1089     7005  15233  14361     41   3062   1641       C  
ATOM   4868  O   ALA B1089      82.595   4.048   7.652  1.00 95.09           O  
ANISOU 4868  O   ALA B1089     6893  15073  14163     68   2949   1578       O  
ATOM   4869  CB  ALA B1089      85.868   4.355   7.206  1.00 97.54           C  
ANISOU 4869  CB  ALA B1089     7022  15106  14932     24   3131   1483       C  
ATOM   4870  N   ALA B1090      83.193   5.895   6.498  1.00 92.98           N  
ANISOU 4870  N   ALA B1090     6598  14842  13890     52   3081   1842       N  
ATOM   4871  CA  ALA B1090      81.978   6.614   6.861  1.00 84.61           C  
ANISOU 4871  CA  ALA B1090     5607  13832  12710     98   2972   1995       C  
ATOM   4872  C   ALA B1090      80.737   5.899   6.344  1.00 84.98           C  
ANISOU 4872  C   ALA B1090     5718  14102  12471     77   2978   1956       C  
ATOM   4873  O   ALA B1090      79.707   5.873   7.020  1.00 91.25           O  
ANISOU 4873  O   ALA B1090     6565  14912  13193    115   2853   1982       O  
ATOM   4874  CB  ALA B1090      82.035   8.044   6.327  1.00 83.52           C  
ANISOU 4874  CB  ALA B1090     5470  13713  12551    107   3013   2214       C  
ATOM   4875  N   ALA B1091      80.814   5.317   5.145  1.00 87.95           N  
ANISOU 4875  N   ALA B1091     6093  14647  12678     15   3120   1891       N  
ATOM   4876  CA  ALA B1091      79.669   4.587   4.603  1.00 98.29           C  
ANISOU 4876  CA  ALA B1091     7471  16164  13710     -8   3125   1847       C  
ATOM   4877  C   ALA B1091      79.380   3.325   5.410  1.00 98.10           C  
ANISOU 4877  C   ALA B1091     7459  16102  13711     -1   3045   1658       C  
ATOM   4878  O   ALA B1091      78.211   3.004   5.691  1.00107.09           O  
ANISOU 4878  O   ALA B1091     8664  17334  14691     16   2955   1654       O  
ATOM   4879  CB  ALA B1091      79.918   4.238   3.135  1.00 98.74           C  
ANISOU 4879  CB  ALA B1091     7532  16388  13596    -78   3298   1815       C  
ATOM   4880  N   GLU B1092      80.431   2.594   5.788  1.00 84.49           N  
ANISOU 4880  N   GLU B1092     5673  14244  12186    -15   3074   1499       N  
ATOM   4881  CA  GLU B1092      80.228   1.434   6.649  1.00 89.22           C  
ANISOU 4881  CA  GLU B1092     6281  14786  12834     -4   2990   1323       C  
ATOM   4882  C   GLU B1092      79.549   1.838   7.954  1.00 90.39           C  
ANISOU 4882  C   GLU B1092     6464  14821  13058     61   2810   1384       C  
ATOM   4883  O   GLU B1092      78.662   1.130   8.449  1.00 82.20           O  
ANISOU 4883  O   GLU B1092     5478  13832  11922     71   2726   1307       O  
ATOM   4884  CB  GLU B1092      81.553   0.726   6.926  1.00 98.69           C  
ANISOU 4884  CB  GLU B1092     7398  15837  14263    -20   3036   1158       C  
ATOM   4885  CG  GLU B1092      81.385  -0.559   7.728  1.00105.36           C  
ANISOU 4885  CG  GLU B1092     8249  16632  15150    -13   2959    967       C  
ATOM   4886  CD  GLU B1092      80.616  -1.628   6.965  1.00109.83           C  
ANISOU 4886  CD  GLU B1092     8870  17397  15462    -57   3025    866       C  
ATOM   4887  OE1 GLU B1092      80.779  -1.715   5.729  1.00111.57           O  
ANISOU 4887  OE1 GLU B1092     9094  17751  15546   -107   3170    872       O  
ATOM   4888  OE2 GLU B1092      79.836  -2.370   7.600  1.00108.92           O  
ANISOU 4888  OE2 GLU B1092     8806  17300  15280    -41   2928    783       O  
ATOM   4889  N   GLN B1093      79.959   2.972   8.530  1.00 98.58           N  
ANISOU 4889  N   GLN B1093     7480  15702  14274    103   2750   1518       N  
ATOM   4890  CA  GLN B1093      79.261   3.492   9.706  1.00105.39           C  
ANISOU 4890  CA  GLN B1093     8387  16456  15199    164   2584   1597       C  
ATOM   4891  C   GLN B1093      77.814   3.854   9.386  1.00101.02           C  
ANISOU 4891  C   GLN B1093     7907  16090  14385    173   2546   1711       C  
ATOM   4892  O   GLN B1093      76.915   3.638  10.208  1.00104.24           O  
ANISOU 4892  O   GLN B1093     8366  16487  14755    204   2425   1693       O  
ATOM   4893  CB  GLN B1093      80.003   4.702  10.271  1.00112.16           C  
ANISOU 4893  CB  GLN B1093     9217  17112  16288    205   2536   1730       C  
ATOM   4894  CG  GLN B1093      81.270   4.338  11.016  1.00116.42           C  
ANISOU 4894  CG  GLN B1093     9702  17418  17113    214   2509   1611       C  
ATOM   4895  CD  GLN B1093      81.013   3.344  12.133  1.00118.94           C  
ANISOU 4895  CD  GLN B1093    10049  17632  17510    235   2387   1457       C  
ATOM   4896  OE1 GLN B1093      80.030   3.458  12.868  1.00116.45           O  
ANISOU 4896  OE1 GLN B1093     9797  17308  17142    269   2269   1496       O  
ATOM   4897  NE2 GLN B1093      81.893   2.357  12.261  1.00122.60           N  
ANISOU 4897  NE2 GLN B1093    10467  18017  18098    215   2414   1280       N  
ATOM   4898  N   LEU B1094      77.576   4.416   8.197  1.00 91.81           N  
ANISOU 4898  N   LEU B1094     6748  15094  13040    147   2647   1828       N  
ATOM   4899  CA  LEU B1094      76.230   4.809   7.795  1.00 85.60           C  
ANISOU 4899  CA  LEU B1094     6029  14493  12002    156   2610   1943       C  
ATOM   4900  C   LEU B1094      75.296   3.611   7.730  1.00 87.77           C  
ANISOU 4900  C   LEU B1094     6357  14911  12078    133   2585   1803       C  
ATOM   4901  O   LEU B1094      74.078   3.760   7.887  1.00 89.30           O  
ANISOU 4901  O   LEU B1094     6610  15210  12110    154   2502   1860       O  
ATOM   4902  CB  LEU B1094      76.282   5.491   6.428  1.00 76.06           C  
ANISOU 4902  CB  LEU B1094     4818  13441  10640    125   2734   2074       C  
ATOM   4903  CG  LEU B1094      76.756   6.936   6.346  1.00 76.74           C  
ANISOU 4903  CG  LEU B1094     4875  13444  10838    153   2746   2270       C  
ATOM   4904  CD1 LEU B1094      76.839   7.371   4.893  1.00 78.59           C  
ANISOU 4904  CD1 LEU B1094     5111  13849  10900    109   2884   2366       C  
ATOM   4905  CD2 LEU B1094      75.804   7.817   7.106  1.00 75.64           C  
ANISOU 4905  CD2 LEU B1094     4775  13276  10688    215   2606   2416       C  
ATOM   4906  N   LYS B1095      75.854   2.427   7.479  1.00 90.71           N  
ANISOU 4906  N   LYS B1095     6710  15293  12462     90   2657   1619       N  
ATOM   4907  CA  LYS B1095      75.033   1.223   7.356  1.00 96.26           C  
ANISOU 4907  CA  LYS B1095     7469  16132  12974     63   2641   1476       C  
ATOM   4908  C   LYS B1095      74.189   0.989   8.610  1.00 89.48           C  
ANISOU 4908  C   LYS B1095     6652  15208  12140    105   2482   1438       C  
ATOM   4909  O   LYS B1095      72.980   0.736   8.522  1.00 86.24           O  
ANISOU 4909  O   LYS B1095     6308  14942  11517    103   2428   1439       O  
ATOM   4910  CB  LYS B1095      75.927   0.016   7.069  1.00105.20           C  
ANISOU 4910  CB  LYS B1095     8566  17238  14167     18   2735   1280       C  
ATOM   4911  CG  LYS B1095      75.186  -1.287   6.814  1.00105.02           C  
ANISOU 4911  CG  LYS B1095     8607  17355  13942    -16   2734   1126       C  
ATOM   4912  CD  LYS B1095      76.171  -2.410   6.523  1.00104.60           C  
ANISOU 4912  CD  LYS B1095     8514  17260  13971    -57   2833    943       C  
ATOM   4913  CE  LYS B1095      77.087  -2.040   5.362  1.00101.80           C  
ANISOU 4913  CE  LYS B1095     8112  16937  13629    -95   2995    990       C  
ATOM   4914  NZ  LYS B1095      78.095  -3.096   5.071  1.00 97.67           N  
ANISOU 4914  NZ  LYS B1095     7543  16363  13204   -133   3099    815       N  
ATOM   4915  N   THR B1096      74.819   1.053   9.789  1.00 95.17           N  
ANISOU 4915  N   THR B1096     7335  15705  13120    140   2405   1400       N  
ATOM   4916  CA  THR B1096      74.113   0.773  11.039  1.00 93.04           C  
ANISOU 4916  CA  THR B1096     7106  15351  12893    176   2257   1352       C  
ATOM   4917  C   THR B1096      73.020   1.799  11.307  1.00 88.35           C  
ANISOU 4917  C   THR B1096     6561  14803  12205    216   2167   1522       C  
ATOM   4918  O   THR B1096      71.901   1.443  11.709  1.00 86.92           O  
ANISOU 4918  O   THR B1096     6440  14698  11887    223   2084   1489       O  
ATOM   4919  CB  THR B1096      75.107   0.754  12.202  1.00 91.63           C  
ANISOU 4919  CB  THR B1096     6881  14905  13028    208   2191   1294       C  
ATOM   4920  OG1 THR B1096      76.173  -0.156  11.906  1.00101.88           O  
ANISOU 4920  OG1 THR B1096     8123  16162  14425    173   2279   1140       O  
ATOM   4921  CG2 THR B1096      74.421   0.332  13.492  1.00 81.82           C  
ANISOU 4921  CG2 THR B1096     5688  13571  11831    239   2044   1225       C  
ATOM   4922  N   THR B1097      73.335   3.082  11.107  1.00 84.71           N  
ANISOU 4922  N   THR B1097     6075  14291  11820    243   2181   1703       N  
ATOM   4923  CA  THR B1097      72.338   4.133  11.269  1.00 78.46           C  
ANISOU 4923  CA  THR B1097     5324  13548  10941    283   2103   1878       C  
ATOM   4924  C   THR B1097      71.154   3.907  10.342  1.00 74.08           C  
ANISOU 4924  C   THR B1097     4817  13255  10073    257   2130   1899       C  
ATOM   4925  O   THR B1097      69.993   4.055  10.753  1.00 72.58           O  
ANISOU 4925  O   THR B1097     4677  13128   9774    281   2035   1937       O  
ATOM   4926  CB  THR B1097      72.970   5.498  10.990  1.00 78.77           C  
ANISOU 4926  CB  THR B1097     5325  13511  11095    308   2137   2066       C  
ATOM   4927  OG1 THR B1097      74.034   5.739  11.918  1.00 79.88           O  
ANISOU 4927  OG1 THR B1097     5428  13392  11530    334   2097   2046       O  
ATOM   4928  CG2 THR B1097      71.930   6.605  11.108  1.00 72.05           C  
ANISOU 4928  CG2 THR B1097     4512  12715  10149    351   2060   2252       C  
ATOM   4929  N   ILE B1098      71.431   3.534   9.089  1.00 76.59           N  
ANISOU 4929  N   ILE B1098     5125  13727  10250    208   2256   1872       N  
ATOM   4930  CA  ILE B1098      70.364   3.291   8.124  1.00 79.18           C  
ANISOU 4930  CA  ILE B1098     5504  14302  10279    180   2281   1889       C  
ATOM   4931  C   ILE B1098      69.479   2.148   8.597  1.00 69.97           C  
ANISOU 4931  C   ILE B1098     4393  13199   8995    167   2210   1730       C  
ATOM   4932  O   ILE B1098      68.248   2.245   8.572  1.00 71.12           O  
ANISOU 4932  O   ILE B1098     4588  13472   8962    177   2142   1771       O  
ATOM   4933  CB  ILE B1098      70.953   3.013   6.727  1.00 76.70           C  
ANISOU 4933  CB  ILE B1098     5175  14114   9854    125   2433   1872       C  
ATOM   4934  CG1 ILE B1098      71.376   4.322   6.056  1.00 82.42           C  
ANISOU 4934  CG1 ILE B1098     5866  14846  10604    136   2494   2070       C  
ATOM   4935  CG2 ILE B1098      69.954   2.262   5.855  1.00 75.12           C  
ANISOU 4935  CG2 ILE B1098     5038  14145   9357     85   2451   1812       C  
ATOM   4936  CD1 ILE B1098      72.242   4.132   4.825  1.00 85.72           C  
ANISOU 4936  CD1 ILE B1098     6259  15332  10976     81   2654   2050       C  
ATOM   4937  N   ASN B1099      70.093   1.050   9.042  1.00 69.45           N  
ANISOU 4937  N   ASN B1099     4316  13041   9029    144   2223   1544       N  
ATOM   4938  CA  ASN B1099      69.306  -0.086   9.512  1.00 72.34           C  
ANISOU 4938  CA  ASN B1099     4739  13461   9288    128   2157   1383       C  
ATOM   4939  C   ASN B1099      68.394   0.314  10.666  1.00 71.53           C  
ANISOU 4939  C   ASN B1099     4668  13291   9218    174   2014   1426       C  
ATOM   4940  O   ASN B1099      67.185   0.042  10.643  1.00 67.47           O  
ANISOU 4940  O   ASN B1099     4213  12912   8512    169   1958   1409       O  
ATOM   4941  CB  ASN B1099      70.231  -1.230   9.929  1.00 84.93           C  
ANISOU 4941  CB  ASN B1099     6309  14938  11021    103   2186   1186       C  
ATOM   4942  CG  ASN B1099      70.745  -2.028   8.746  1.00 89.50           C  
ANISOU 4942  CG  ASN B1099     6885  15632  11490     46   2320   1092       C  
ATOM   4943  OD1 ASN B1099      70.276  -1.862   7.618  1.00 93.53           O  
ANISOU 4943  OD1 ASN B1099     7425  16323  11791     20   2382   1158       O  
ATOM   4944  ND2 ASN B1099      71.718  -2.900   8.998  1.00 86.93           N  
ANISOU 4944  ND2 ASN B1099     6522  15197  11309     27   2362    938       N  
ATOM   4945  N   ALA B1100      68.953   0.997  11.671  1.00 79.30           N  
ANISOU 4945  N   ALA B1100     5617  14064  10449    220   1954   1487       N  
ATOM   4946  CA  ALA B1100      68.167   1.374  12.846  1.00 85.42           C  
ANISOU 4946  CA  ALA B1100     6427  14749  11280    265   1818   1523       C  
ATOM   4947  C   ALA B1100      67.001   2.284  12.469  1.00 90.44           C  
ANISOU 4947  C   ALA B1100     7094  15525  11743    288   1781   1685       C  
ATOM   4948  O   ALA B1100      65.854   2.056  12.882  1.00 82.18           O  
ANISOU 4948  O   ALA B1100     6099  14549  10578    294   1701   1656       O  
ATOM   4949  CB  ALA B1100      69.068   2.059  13.874  1.00 83.69           C  
ANISOU 4949  CB  ALA B1100     6169  14265  11362    310   1764   1579       C  
ATOM   4950  N   TYR B1101      67.285   3.317  11.666  1.00 98.13           N  
ANISOU 4950  N   TYR B1101     8036  16546  12704    299   1841   1856       N  
ATOM   4951  CA  TYR B1101      66.291   4.326  11.300  1.00102.12           C  
ANISOU 4951  CA  TYR B1101     8558  17172  13071    328   1805   2031       C  
ATOM   4952  C   TYR B1101      65.193   3.730  10.433  1.00 97.91           C  
ANISOU 4952  C   TYR B1101     8067  16890  12244    293   1821   1988       C  
ATOM   4953  O   TYR B1101      64.001   4.011  10.640  1.00102.85           O  
ANISOU 4953  O   TYR B1101     8726  17602  12751    315   1741   2040       O  
ATOM   4954  CB  TYR B1101      67.039   5.459  10.581  1.00115.90           C  
ANISOU 4954  CB  TYR B1101    10255  18903  14880    341   1879   2207       C  
ATOM   4955  CG  TYR B1101      66.292   6.588   9.917  1.00125.72           C  
ANISOU 4955  CG  TYR B1101    11501  20282  15986    367   1872   2409       C  
ATOM   4956  CD1 TYR B1101      66.365   7.877  10.414  1.00131.46           C  
ANISOU 4956  CD1 TYR B1101    12210  20888  16850    422   1819   2583       C  
ATOM   4957  CD2 TYR B1101      65.608   6.388   8.709  1.00129.54           C  
ANISOU 4957  CD2 TYR B1101    12002  21010  16206    335   1925   2431       C  
ATOM   4958  CE1 TYR B1101      65.748   8.917   9.796  1.00137.90           C  
ANISOU 4958  CE1 TYR B1101    13022  21824  17550    447   1815   2770       C  
ATOM   4959  CE2 TYR B1101      64.982   7.430   8.076  1.00133.87           C  
ANISOU 4959  CE2 TYR B1101    12547  21682  16636    359   1917   2619       C  
ATOM   4960  CZ  TYR B1101      65.040   8.691   8.632  1.00138.17           C  
ANISOU 4960  CZ  TYR B1101    13070  22106  17323    416   1862   2788       C  
ATOM   4961  OH  TYR B1101      64.409   9.757   8.032  1.00139.46           O  
ANISOU 4961  OH  TYR B1101    13226  22389  17374    445   1851   2981       O  
ATOM   4962  N   ILE B1102      65.571   2.871   9.485  1.00 88.35           N  
ANISOU 4962  N   ILE B1102     6858  15793  10918    239   1919   1885       N  
ATOM   4963  CA  ILE B1102      64.583   2.220   8.636  1.00 79.97           C  
ANISOU 4963  CA  ILE B1102     5845  14961   9580    202   1931   1832       C  
ATOM   4964  C   ILE B1102      63.689   1.315   9.466  1.00 73.03           C  
ANISOU 4964  C   ILE B1102     5018  14087   8643    196   1839   1684       C  
ATOM   4965  O   ILE B1102      62.464   1.299   9.289  1.00 68.12           O  
ANISOU 4965  O   ILE B1102     4435  13612   7837    197   1783   1703       O  
ATOM   4966  CB  ILE B1102      65.278   1.446   7.501  1.00 76.91           C  
ANISOU 4966  CB  ILE B1102     5455  14666   9101    143   2057   1742       C  
ATOM   4967  CG1 ILE B1102      65.931   2.421   6.515  1.00 73.94           C  
ANISOU 4967  CG1 ILE B1102     5037  14325   8731    143   2152   1905       C  
ATOM   4968  CG2 ILE B1102      64.293   0.526   6.798  1.00 73.74           C  
ANISOU 4968  CG2 ILE B1102     5115  14471   8431    101   2055   1645       C  
ATOM   4969  CD1 ILE B1102      64.979   3.431   5.919  1.00 71.88           C  
ANISOU 4969  CD1 ILE B1102     4787  14216   8309    168   2119   2091       C  
ATOM   4970  N   GLN B1103      64.282   0.544  10.382  1.00 83.64           N  
ANISOU 4970  N   GLN B1103     6363  15273  10145    189   1820   1533       N  
ATOM   4971  CA  GLN B1103      63.466  -0.322  11.223  1.00 91.67           C  
ANISOU 4971  CA  GLN B1103     7433  16286  11113    181   1733   1389       C  
ATOM   4972  C   GLN B1103      62.482   0.482  12.058  1.00 92.26           C  
ANISOU 4972  C   GLN B1103     7523  16325  11205    230   1621   1489       C  
ATOM   4973  O   GLN B1103      61.305   0.124  12.149  1.00 87.61           O  
ANISOU 4973  O   GLN B1103     6983  15851  10456    221   1563   1443       O  
ATOM   4974  CB  GLN B1103      64.347  -1.175  12.131  1.00 95.08           C  
ANISOU 4974  CB  GLN B1103     7856  16536  11733    171   1726   1224       C  
ATOM   4975  CG  GLN B1103      63.550  -2.065  13.079  1.00 97.57           C  
ANISOU 4975  CG  GLN B1103     8231  16834  12007    160   1635   1070       C  
ATOM   4976  CD  GLN B1103      63.672  -1.645  14.534  1.00 98.50           C  
ANISOU 4976  CD  GLN B1103     8341  16738  12346    206   1536   1084       C  
ATOM   4977  OE1 GLN B1103      64.769  -1.615  15.093  1.00 99.06           O  
ANISOU 4977  OE1 GLN B1103     8371  16626  12642    220   1541   1061       O  
ATOM   4978  NE2 GLN B1103      62.540  -1.325  15.155  1.00 90.34           N  
ANISOU 4978  NE2 GLN B1103     7348  15722  11254    228   1444   1119       N  
ATOM   4979  N   LYS B1104      62.931   1.596  12.638  1.00 92.06           N  
ANISOU 4979  N   LYS B1104     7460  16145  11375    281   1589   1630       N  
ATOM   4980  CA  LYS B1104      62.034   2.376  13.483  1.00 94.22           C  
ANISOU 4980  CA  LYS B1104     7752  16366  11682    329   1482   1724       C  
ATOM   4981  C   LYS B1104      60.865   2.933  12.682  1.00110.81           C  
ANISOU 4981  C   LYS B1104     9864  18676  13561    337   1471   1842       C  
ATOM   4982  O   LYS B1104      59.709   2.891  13.131  1.00100.16           O  
ANISOU 4982  O   LYS B1104     8550  17381  12124    348   1391   1827       O  
ATOM   4983  CB  LYS B1104      62.812   3.500  14.172  1.00 96.36           C  
ANISOU 4983  CB  LYS B1104     7986  16422  12204    382   1454   1860       C  
ATOM   4984  CG  LYS B1104      61.996   4.331  15.152  1.00102.98           C  
ANISOU 4984  CG  LYS B1104     8849  17170  13109    434   1341   1955       C  
ATOM   4985  CD  LYS B1104      62.858   5.365  15.866  1.00102.52           C  
ANISOU 4985  CD  LYS B1104     8765  16877  13311    483   1310   2075       C  
ATOM   4986  CE  LYS B1104      62.056   6.098  16.933  1.00103.92           C  
ANISOU 4986  CE  LYS B1104     8979  16943  13562    533   1194   2149       C  
ATOM   4987  NZ  LYS B1104      62.926   6.620  18.024  1.00106.82           N  
ANISOU 4987  NZ  LYS B1104     9349  17027  14209    570   1139   2181       N  
ATOM   4988  N   TYR B1105      61.149   3.466  11.492  1.00127.78           N  
ANISOU 4988  N   TYR B1105    11981  20947  15623    331   1550   1961       N  
ATOM   4989  CA  TYR B1105      60.085   4.089  10.697  1.00133.84           C  
ANISOU 4989  CA  TYR B1105    12751  21913  16189    343   1535   2091       C  
ATOM   4990  C   TYR B1105      59.126   3.063  10.119  1.00129.60           C  
ANISOU 4990  C   TYR B1105    12258  21577  15405    297   1532   1967       C  
ATOM   4991  O   TYR B1105      57.905   3.272  10.123  1.00133.09           O  
ANISOU 4991  O   TYR B1105    12717  22135  15715    312   1464   2006       O  
ATOM   4992  CB  TYR B1105      60.646   4.997   9.592  1.00144.48           C  
ANISOU 4992  CB  TYR B1105    14054  23331  17509    349   1616   2262       C  
ATOM   4993  CG  TYR B1105      61.349   6.170  10.177  1.00154.71           C  
ANISOU 4993  CG  TYR B1105    15312  24441  19030    400   1600   2409       C  
ATOM   4994  CD1 TYR B1105      61.685   6.152  11.518  1.00155.15           C  
ANISOU 4994  CD1 TYR B1105    15374  24272  19303    427   1534   2354       C  
ATOM   4995  CD2 TYR B1105      61.644   7.300   9.440  1.00160.14           C  
ANISOU 4995  CD2 TYR B1105    15962  25170  19715    422   1644   2602       C  
ATOM   4996  CE1 TYR B1105      62.287   7.165  12.113  1.00155.06           C  
ANISOU 4996  CE1 TYR B1105    15338  24080  19499    472   1509   2477       C  
ATOM   4997  CE2 TYR B1105      62.271   8.353  10.025  1.00159.71           C  
ANISOU 4997  CE2 TYR B1105    15878  24936  19870    468   1624   2731       C  
ATOM   4998  CZ  TYR B1105      62.576   8.275  11.360  1.00155.84           C  
ANISOU 4998  CZ  TYR B1105    15399  24222  19592    493   1554   2666       C  
ATOM   4999  OH  TYR B1105      63.201   9.400  11.854  1.00151.59           O  
ANISOU 4999  OH  TYR B1105    14835  23506  19254    539   1533   2808       O  
ATOM   5000  N   GLY B1106      59.651   1.952   9.598  1.00108.12           N  
ANISOU 5000  N   GLY B1106     9557  18902  12622    242   1604   1817       N  
ATOM   5001  CA  GLY B1106      58.772   0.906   9.125  1.00 85.10           C  
ANISOU 5001  CA  GLY B1106     6692  16157   9484    197   1594   1686       C  
ATOM   5002  C   GLY B1106      57.962   0.338  10.260  1.00 90.97           C  
ANISOU 5002  C   GLY B1106     7477  16845  10243    201   1499   1565       C  
ATOM   5003  O   GLY B1106      56.829  -0.098  10.057  1.00 92.84           O  
ANISOU 5003  O   GLY B1106     7751  17227  10298    183   1454   1513       O  
ATOM   5004  N   GLN B 313      58.526   0.344  11.473  1.00 92.70           N  
ANISOU 5004  N   GLN B 313     7692  16850  10681    222   1464   1517       N  
ATOM   5005  CA  GLN B 313      57.771  -0.081  12.641  1.00 89.02           C  
ANISOU 5005  CA  GLN B 313     7267  16312  10246    228   1370   1414       C  
ATOM   5006  C   GLN B 313      56.605   0.861  12.898  1.00 75.03           C  
ANISOU 5006  C   GLN B 313     5492  14591   8424    272   1290   1546       C  
ATOM   5007  O   GLN B 313      55.491   0.416  13.197  1.00 70.90           O  
ANISOU 5007  O   GLN B 313     5009  14145   7785    260   1231   1469       O  
ATOM   5008  CB  GLN B 313      58.695  -0.134  13.860  1.00 98.55           C  
ANISOU 5008  CB  GLN B 313     8465  17269  11711    246   1347   1358       C  
ATOM   5009  CG  GLN B 313      58.059  -0.695  15.122  1.00104.91           C  
ANISOU 5009  CG  GLN B 313     9319  17982  12560    245   1257   1229       C  
ATOM   5010  CD  GLN B 313      57.863  -2.195  15.036  1.00108.91           C  
ANISOU 5010  CD  GLN B 313     9878  18563  12940    183   1273   1010       C  
ATOM   5011  OE1 GLN B 313      58.588  -2.883  14.316  1.00112.90           O  
ANISOU 5011  OE1 GLN B 313    10379  19114  13405    146   1351    934       O  
ATOM   5012  NE2 GLN B 313      56.883  -2.711  15.769  1.00102.20           N  
ANISOU 5012  NE2 GLN B 313     9081  17722  12026    170   1201    905       N  
ATOM   5013  N   SER B 314      56.844   2.169  12.768  1.00 67.52           N  
ANISOU 5013  N   SER B 314     4495  13599   7562    322   1290   1744       N  
ATOM   5014  CA  SER B 314      55.757   3.135  12.913  1.00 66.45           C  
ANISOU 5014  CA  SER B 314     4350  13521   7379    367   1217   1883       C  
ATOM   5015  C   SER B 314      54.674   2.908  11.866  1.00 68.49           C  
ANISOU 5015  C   SER B 314     4615  14037   7371    344   1220   1893       C  
ATOM   5016  O   SER B 314      53.474   2.938  12.177  1.00 69.95           O  
ANISOU 5016  O   SER B 314     4817  14293   7469    355   1148   1883       O  
ATOM   5017  CB  SER B 314      56.304   4.557  12.807  1.00 62.94           C  
ANISOU 5017  CB  SER B 314     3854  12995   7065    422   1226   2098       C  
ATOM   5018  OG  SER B 314      55.281   5.462  12.425  1.00 63.63           O  
ANISOU 5018  OG  SER B 314     3923  13210   7043    458   1182   2250       O  
ATOM   5019  N   ILE B 315      55.083   2.681  10.617  1.00 84.24           N  
ANISOU 5019  N   ILE B 315     6596  16172   9240    312   1302   1909       N  
ATOM   5020  CA  ILE B 315      54.119   2.450   9.544  1.00 95.16           C  
ANISOU 5020  CA  ILE B 315     7987  17801  10369    288   1302   1920       C  
ATOM   5021  C   ILE B 315      53.304   1.191   9.815  1.00 91.84           C  
ANISOU 5021  C   ILE B 315     7623  17447   9825    244   1263   1722       C  
ATOM   5022  O   ILE B 315      52.084   1.169   9.610  1.00 89.82           O  
ANISOU 5022  O   ILE B 315     7374  17336   9415    245   1207   1727       O  
ATOM   5023  CB  ILE B 315      54.838   2.379   8.184  1.00104.94           C  
ANISOU 5023  CB  ILE B 315     9211  19154  11509    257   1402   1963       C  
ATOM   5024  CG1 ILE B 315      55.563   3.695   7.905  1.00106.22           C  
ANISOU 5024  CG1 ILE B 315     9317  19256  11784    300   1439   2169       C  
ATOM   5025  CG2 ILE B 315      53.848   2.069   7.073  1.00110.41           C  
ANISOU 5025  CG2 ILE B 315     9917  20095  11937    229   1395   1965       C  
ATOM   5026  CD1 ILE B 315      54.687   4.906   8.096  1.00108.03           C  
ANISOU 5026  CD1 ILE B 315     9513  19524  12009    360   1364   2349       C  
ATOM   5027  N   SER B 316      53.958   0.130  10.292  1.00 89.67           N  
ANISOU 5027  N   SER B 316     7387  17065   9618    205   1290   1544       N  
ATOM   5028  CA  SER B 316      53.238  -1.106  10.586  1.00 87.53           C  
ANISOU 5028  CA  SER B 316     7177  16845   9235    160   1255   1349       C  
ATOM   5029  C   SER B 316      52.277  -0.924  11.755  1.00 88.66           C  
ANISOU 5029  C   SER B 316     7336  16920   9429    186   1159   1326       C  
ATOM   5030  O   SER B 316      51.176  -1.490  11.754  1.00 90.18           O  
ANISOU 5030  O   SER B 316     7563  17225   9475    162   1112   1239       O  
ATOM   5031  CB  SER B 316      54.228  -2.235  10.871  1.00 86.83           C  
ANISOU 5031  CB  SER B 316     7123  16645   9222    116   1305   1171       C  
ATOM   5032  OG  SER B 316      53.557  -3.474  11.032  1.00 85.71           O  
ANISOU 5032  OG  SER B 316     7046  16565   8956     67   1276    983       O  
ATOM   5033  N   ASN B 317      52.672  -0.143  12.764  1.00 81.38           N  
ANISOU 5033  N   ASN B 317     6393  15809   8719    233   1128   1400       N  
ATOM   5034  CA  ASN B 317      51.763   0.123  13.874  1.00 70.56           C  
ANISOU 5034  CA  ASN B 317     5041  14364   7406    260   1039   1388       C  
ATOM   5035  C   ASN B 317      50.528   0.876  13.398  1.00 63.06           C  
ANISOU 5035  C   ASN B 317     4064  13576   6321    289    993   1513       C  
ATOM   5036  O   ASN B 317      49.399   0.542  13.782  1.00 67.44           O  
ANISOU 5036  O   ASN B 317     4645  14188   6792    279    934   1439       O  
ATOM   5037  CB  ASN B 317      52.476   0.913  14.973  1.00 68.76           C  
ANISOU 5037  CB  ASN B 317     4796  13896   7436    308   1012   1461       C  
ATOM   5038  CG  ASN B 317      53.619   0.138  15.604  1.00 71.15           C  
ANISOU 5038  CG  ASN B 317     5121  14028   7887    283   1042   1326       C  
ATOM   5039  OD1 ASN B 317      54.496   0.718  16.244  1.00 72.76           O  
ANISOU 5039  OD1 ASN B 317     5302  14043   8301    317   1037   1389       O  
ATOM   5040  ND2 ASN B 317      53.624  -1.176  15.410  1.00 68.48           N  
ANISOU 5040  ND2 ASN B 317     4825  13754   7441    223   1070   1139       N  
ATOM   5041  N   GLU B 318      50.722   1.895  12.557  1.00 63.79           N  
ANISOU 5041  N   GLU B 318     4101  13745   6393    324   1018   1703       N  
ATOM   5042  CA  GLU B 318      49.573   2.604  12.002  1.00 73.51           C  
ANISOU 5042  CA  GLU B 318     5296  15146   7487    352    974   1827       C  
ATOM   5043  C   GLU B 318      48.688   1.672  11.185  1.00 76.78           C  
ANISOU 5043  C   GLU B 318     5733  15781   7660    302    973   1721       C  
ATOM   5044  O   GLU B 318      47.457   1.739  11.275  1.00 74.89           O  
ANISOU 5044  O   GLU B 318     5489  15643   7322    310    909   1718       O  
ATOM   5045  CB  GLU B 318      50.028   3.795  11.157  1.00 73.93           C  
ANISOU 5045  CB  GLU B 318     5289  15252   7550    393   1009   2046       C  
ATOM   5046  CG  GLU B 318      50.625   4.935  11.967  1.00 80.80           C  
ANISOU 5046  CG  GLU B 318     6133  15916   8650    453    989   2182       C  
ATOM   5047  CD  GLU B 318      49.634   5.532  12.955  1.00 85.77           C  
ANISOU 5047  CD  GLU B 318     6767  16474   9350    498    893   2219       C  
ATOM   5048  OE1 GLU B 318      48.409   5.438  12.716  1.00 88.41           O  
ANISOU 5048  OE1 GLU B 318     7096  16961   9535    497    847   2208       O  
ATOM   5049  OE2 GLU B 318      50.082   6.094  13.978  1.00 88.93           O  
ANISOU 5049  OE2 GLU B 318     7175  16656   9957    535    863   2257       O  
ATOM   5050  N   GLN B 319      49.299   0.790  10.391  1.00 76.31           N  
ANISOU 5050  N   GLN B 319     5697  15790   7505    249   1040   1629       N  
ATOM   5051  CA  GLN B 319      48.527  -0.155   9.591  1.00 77.10           C  
ANISOU 5051  CA  GLN B 319     5826  16088   7381    198   1035   1520       C  
ATOM   5052  C   GLN B 319      47.686  -1.069  10.476  1.00 84.09           C  
ANISOU 5052  C   GLN B 319     6765  16943   8242    169    976   1340       C  
ATOM   5053  O   GLN B 319      46.505  -1.303  10.197  1.00 97.34           O  
ANISOU 5053  O   GLN B 319     8445  18772   9768    157    927   1310       O  
ATOM   5054  CB  GLN B 319      49.478  -0.968   8.712  1.00 84.84           C  
ANISOU 5054  CB  GLN B 319     6832  17103   8298    147   1120   1442       C  
ATOM   5055  CG  GLN B 319      48.824  -1.852   7.668  1.00 90.79           C  
ANISOU 5055  CG  GLN B 319     7615  18061   8819     94   1120   1355       C  
ATOM   5056  CD  GLN B 319      49.846  -2.609   6.829  1.00 95.56           C  
ANISOU 5056  CD  GLN B 319     8249  18677   9384     46   1208   1282       C  
ATOM   5057  OE1 GLN B 319      51.055  -2.414   6.974  1.00 95.91           O  
ANISOU 5057  OE1 GLN B 319     8283  18588   9572     53   1274   1305       O  
ATOM   5058  NE2 GLN B 319      49.362  -3.470   5.940  1.00 97.13           N  
ANISOU 5058  NE2 GLN B 319     8480  19031   9393     -4   1208   1192       N  
ATOM   5059  N   LYS B 320      48.271  -1.577  11.563  1.00 81.57           N  
ANISOU 5059  N   LYS B 320     6487  16429   8075    158    980   1219       N  
ATOM   5060  CA  LYS B 320      47.538  -2.480  12.446  1.00 75.99           C  
ANISOU 5060  CA  LYS B 320     5839  15683   7350    125    929   1040       C  
ATOM   5061  C   LYS B 320      46.410  -1.757  13.180  1.00 76.39           C  
ANISOU 5061  C   LYS B 320     5871  15724   7431    166    851   1102       C  
ATOM   5062  O   LYS B 320      45.306  -2.302  13.330  1.00 73.22           O  
ANISOU 5062  O   LYS B 320     5496  15409   6916    140    805   1003       O  
ATOM   5063  CB  LYS B 320      48.507  -3.130  13.434  1.00 85.48           C  
ANISOU 5063  CB  LYS B 320     7086  16676   8716    106    952    908       C  
ATOM   5064  CG  LYS B 320      47.895  -4.211  14.314  1.00 96.44           C  
ANISOU 5064  CG  LYS B 320     8546  18019  10078     62    911    704       C  
ATOM   5065  CD  LYS B 320      48.910  -4.710  15.336  1.00101.31           C  
ANISOU 5065  CD  LYS B 320     9197  18422  10873     50    928    592       C  
ATOM   5066  CE  LYS B 320      48.353  -5.846  16.180  1.00101.67           C  
ANISOU 5066  CE  LYS B 320     9321  18426  10884      0    892    382       C  
ATOM   5067  NZ  LYS B 320      49.362  -6.349  17.157  1.00 96.53           N  
ANISOU 5067  NZ  LYS B 320     8700  17574  10403    -12    904    271       N  
ATOM   5068  N   ALA B 321      46.667  -0.531  13.649  1.00 78.53           N  
ANISOU 5068  N   ALA B 321     6096  15882   7859    229    835   1262       N  
ATOM   5069  CA  ALA B 321      45.605   0.248  14.282  1.00 67.50           C  
ANISOU 5069  CA  ALA B 321     4679  14471   6497    272    761   1334       C  
ATOM   5070  C   ALA B 321      44.478   0.529  13.296  1.00 69.52           C  
ANISOU 5070  C   ALA B 321     4892  14966   6558    278    734   1410       C  
ATOM   5071  O   ALA B 321      43.294   0.471  13.654  1.00 81.61           O  
ANISOU 5071  O   ALA B 321     6425  16550   8032    279    676   1368       O  
ATOM   5072  CB  ALA B 321      46.169   1.553  14.844  1.00 61.87           C  
ANISOU 5072  CB  ALA B 321     3928  13592   5988    340    748   1506       C  
ATOM   5073  N   CYS B 322      44.834   0.834  12.048  1.00 65.57           N  
ANISOU 5073  N   CYS B 322     4349  14610   5954    282    777   1522       N  
ATOM   5074  CA  CYS B 322      43.837   1.015  11.004  1.00 63.59           C  
ANISOU 5074  CA  CYS B 322     4054  14602   5505    283    752   1589       C  
ATOM   5075  C   CYS B 322      43.014  -0.252  10.818  1.00 74.95           C  
ANISOU 5075  C   CYS B 322     5538  16162   6777    220    732   1401       C  
ATOM   5076  O   CYS B 322      41.791  -0.188  10.658  1.00 77.52           O  
ANISOU 5076  O   CYS B 322     5838  16624   6992    224    676   1403       O  
ATOM   5077  CB  CYS B 322      44.530   1.416   9.703  1.00 78.92           C  
ANISOU 5077  CB  CYS B 322     5956  16662   7366    286    810   1722       C  
ATOM   5078  SG  CYS B 322      43.449   1.629   8.282  1.00 87.04           S  
ANISOU 5078  SG  CYS B 322     6929  17998   8142    284    783   1815       S  
ATOM   5079  N   LYS B 323      43.669  -1.415  10.858  1.00 74.67           N  
ANISOU 5079  N   LYS B 323     5568  16073   6728    162    774   1235       N  
ATOM   5080  CA  LYS B 323      42.951  -2.678  10.699  1.00 76.60           C  
ANISOU 5080  CA  LYS B 323     5865  16417   6824     99    752   1048       C  
ATOM   5081  C   LYS B 323      41.951  -2.885  11.829  1.00 74.35           C  
ANISOU 5081  C   LYS B 323     5605  16068   6578     97    689    949       C  
ATOM   5082  O   LYS B 323      40.798  -3.274  11.594  1.00 71.72           O  
ANISOU 5082  O   LYS B 323     5268  15874   6107     74    643    887       O  
ATOM   5083  CB  LYS B 323      43.947  -3.837  10.677  1.00 81.16           C  
ANISOU 5083  CB  LYS B 323     6512  16912   7413     42    808    891       C  
ATOM   5084  CG  LYS B 323      44.911  -3.837   9.501  1.00 93.98           C  
ANISOU 5084  CG  LYS B 323     8121  18603   8984     31    877    956       C  
ATOM   5085  CD  LYS B 323      46.081  -4.779   9.775  1.00 99.65           C  
ANISOU 5085  CD  LYS B 323     8900  19181   9782    -10    937    816       C  
ATOM   5086  CE  LYS B 323      47.056  -4.840   8.608  1.00 96.81           C  
ANISOU 5086  CE  LYS B 323     8529  18879   9376    -25   1013    867       C  
ATOM   5087  NZ  LYS B 323      48.241  -5.692   8.926  1.00 91.77           N  
ANISOU 5087  NZ  LYS B 323     7940  18095   8836    -59   1074    736       N  
ATOM   5088  N   VAL B 324      42.364  -2.593  13.062  1.00 73.43           N  
ANISOU 5088  N   VAL B 324     5510  15737   6653    120    686    935       N  
ATOM   5089  CA  VAL B 324      41.474  -2.799  14.203  1.00 71.27           C  
ANISOU 5089  CA  VAL B 324     5269  15382   6429    114    633    833       C  
ATOM   5090  C   VAL B 324      40.279  -1.853  14.131  1.00 60.84           C  
ANISOU 5090  C   VAL B 324     3883  14158   5074    161    575    954       C  
ATOM   5091  O   VAL B 324      39.121  -2.267  14.292  1.00 59.88           O  
ANISOU 5091  O   VAL B 324     3771  14119   4861    138    531    864       O  
ATOM   5092  CB  VAL B 324      42.244  -2.628  15.524  1.00 63.23           C  
ANISOU 5092  CB  VAL B 324     4287  14106   5633    131    639    803       C  
ATOM   5093  CG1 VAL B 324      41.274  -2.576  16.699  1.00 57.16           C  
ANISOU 5093  CG1 VAL B 324     3543  13247   4927    134    583    733       C  
ATOM   5094  CG2 VAL B 324      43.260  -3.748  15.699  1.00 64.90           C  
ANISOU 5094  CG2 VAL B 324     4564  14226   5867     77    688    648       C  
ATOM   5095  N   LEU B 325      40.538  -0.569  13.878  1.00 60.57           N  
ANISOU 5095  N   LEU B 325     3783  14115   5115    227    572   1160       N  
ATOM   5096  CA  LEU B 325      39.439   0.387  13.813  1.00 63.16           C  
ANISOU 5096  CA  LEU B 325     4048  14526   5423    277    514   1283       C  
ATOM   5097  C   LEU B 325      38.523   0.111  12.629  1.00 69.40           C  
ANISOU 5097  C   LEU B 325     4794  15586   5988    257    496   1290       C  
ATOM   5098  O   LEU B 325      37.315   0.366  12.710  1.00 74.24           O  
ANISOU 5098  O   LEU B 325     5373  16285   6549    272    440   1299       O  
ATOM   5099  CB  LEU B 325      39.990   1.810  13.773  1.00 72.58           C  
ANISOU 5099  CB  LEU B 325     5186  15642   6749    352    513   1503       C  
ATOM   5100  CG  LEU B 325      40.776   2.156  15.045  1.00 79.59           C  
ANISOU 5100  CG  LEU B 325     6116  16253   7873    376    515   1499       C  
ATOM   5101  CD1 LEU B 325      41.169   3.621  15.088  1.00 85.87           C  
ANISOU 5101  CD1 LEU B 325     6861  16960   8805    452    501   1718       C  
ATOM   5102  CD2 LEU B 325      39.992   1.778  16.293  1.00 74.71           C  
ANISOU 5102  CD2 LEU B 325     5549  15514   7324    361    470   1361       C  
ATOM   5103  N   GLY B 326      39.062  -0.430  11.535  1.00 71.17           N  
ANISOU 5103  N   GLY B 326     5019  15941   6080    222    540   1280       N  
ATOM   5104  CA  GLY B 326      38.204  -0.842  10.439  1.00 71.85           C  
ANISOU 5104  CA  GLY B 326     5073  16277   5949    194    517   1264       C  
ATOM   5105  C   GLY B 326      37.305  -1.999  10.824  1.00 67.04           C  
ANISOU 5105  C   GLY B 326     4513  15702   5256    135    484   1057       C  
ATOM   5106  O   GLY B 326      36.126  -2.026  10.461  1.00 68.63           O  
ANISOU 5106  O   GLY B 326     4674  16067   5337    132    433   1051       O  
ATOM   5107  N   ILE B 327      37.846  -2.964  11.570  1.00 62.61           N  
ANISOU 5107  N   ILE B 327     4040  14987   4760     88    509    885       N  
ATOM   5108  CA  ILE B 327      37.021  -4.058  12.081  1.00 69.31           C  
ANISOU 5108  CA  ILE B 327     4944  15841   5548     30    477    683       C  
ATOM   5109  C   ILE B 327      35.876  -3.504  12.923  1.00 79.34           C  
ANISOU 5109  C   ILE B 327     6188  17085   6873     60    424    694       C  
ATOM   5110  O   ILE B 327      34.715  -3.917  12.789  1.00 81.26           O  
ANISOU 5110  O   ILE B 327     6419  17453   7004     35    380    617       O  
ATOM   5111  CB  ILE B 327      37.886  -5.044  12.887  1.00 64.10           C  
ANISOU 5111  CB  ILE B 327     4384  14994   4979    -18    514    514       C  
ATOM   5112  CG1 ILE B 327      38.814  -5.827  11.960  1.00 72.60           C  
ANISOU 5112  CG1 ILE B 327     5491  16116   5976    -60    560    467       C  
ATOM   5113  CG2 ILE B 327      37.014  -5.989  13.699  1.00 59.76           C  
ANISOU 5113  CG2 ILE B 327     3896  14407   4405    -70    477    319       C  
ATOM   5114  CD1 ILE B 327      39.685  -6.833  12.680  1.00 66.60           C  
ANISOU 5114  CD1 ILE B 327     4824  15181   5299   -106    595    301       C  
ATOM   5115  N   VAL B 328      36.193  -2.549  13.800  1.00 79.80           N  
ANISOU 5115  N   VAL B 328     6236  16971   7114    116    424    791       N  
ATOM   5116  CA  VAL B 328      35.177  -1.964  14.676  1.00 60.37           C  
ANISOU 5116  CA  VAL B 328     3757  14447   4734    147    374    802       C  
ATOM   5117  C   VAL B 328      34.095  -1.268  13.857  1.00 61.65           C  
ANISOU 5117  C   VAL B 328     3827  14811   4785    184    328    923       C  
ATOM   5118  O   VAL B 328      32.892  -1.462  14.088  1.00 61.67           O  
ANISOU 5118  O   VAL B 328     3820  14878   4736    171    285    851       O  
ATOM   5119  CB  VAL B 328      35.829  -1.000  15.680  1.00 59.54           C  
ANISOU 5119  CB  VAL B 328     3659  14107   4856    203    377    900       C  
ATOM   5120  CG1 VAL B 328      34.770  -0.166  16.380  1.00 60.19           C  
ANISOU 5120  CG1 VAL B 328     3712  14135   5022    248    321    953       C  
ATOM   5121  CG2 VAL B 328      36.652  -1.780  16.686  1.00 58.17           C  
ANISOU 5121  CG2 VAL B 328     3576  13733   4793    162    411    751       C  
ATOM   5122  N   PHE B 329      34.509  -0.430  12.899  1.00 66.73           N  
ANISOU 5122  N   PHE B 329     4402  15558   5396    230    335   1110       N  
ATOM   5123  CA  PHE B 329      33.542   0.288  12.071  1.00 73.98           C  
ANISOU 5123  CA  PHE B 329     5227  16673   6208    268    289   1239       C  
ATOM   5124  C   PHE B 329      32.655  -0.680  11.301  1.00 64.78           C  
ANISOU 5124  C   PHE B 329     4049  15733   4830    211    269   1123       C  
ATOM   5125  O   PHE B 329      31.435  -0.488  11.219  1.00 65.27           O  
ANISOU 5125  O   PHE B 329     4063  15905   4832    223    217   1125       O  
ATOM   5126  CB  PHE B 329      34.258   1.215  11.084  1.00 77.82           C  
ANISOU 5126  CB  PHE B 329     5648  17244   6675    316    309   1451       C  
ATOM   5127  CG  PHE B 329      35.158   2.235  11.725  1.00 75.44           C  
ANISOU 5127  CG  PHE B 329     5352  16732   6579    374    325   1582       C  
ATOM   5128  CD1 PHE B 329      34.979   2.627  13.039  1.00 82.51           C  
ANISOU 5128  CD1 PHE B 329     6286  17405   7660    400    298   1555       C  
ATOM   5129  CD2 PHE B 329      36.183   2.813  10.997  1.00 77.12           C  
ANISOU 5129  CD2 PHE B 329     5535  16969   6799    399    366   1733       C  
ATOM   5130  CE1 PHE B 329      35.814   3.570  13.615  1.00 83.27           C  
ANISOU 5130  CE1 PHE B 329     6390  17305   7945    453    307   1678       C  
ATOM   5131  CE2 PHE B 329      37.017   3.755  11.567  1.00 84.43           C  
ANISOU 5131  CE2 PHE B 329     6464  17700   7914    451    379   1855       C  
ATOM   5132  CZ  PHE B 329      36.833   4.133  12.878  1.00 79.99           C  
ANISOU 5132  CZ  PHE B 329     5940  16916   7536    479    346   1828       C  
ATOM   5133  N   PHE B 330      33.256  -1.729  10.732  1.00 64.86           N  
ANISOU 5133  N   PHE B 330     4105  15804   4734    150    306   1018       N  
ATOM   5134  CA  PHE B 330      32.490  -2.697   9.956  1.00 70.26           C  
ANISOU 5134  CA  PHE B 330     4782  16690   5224     93    279    904       C  
ATOM   5135  C   PHE B 330      31.466  -3.411  10.822  1.00 68.19           C  
ANISOU 5135  C   PHE B 330     4558  16387   4965     54    244    726       C  
ATOM   5136  O   PHE B 330      30.311  -3.577  10.415  1.00 82.17           O  
ANISOU 5136  O   PHE B 330     6278  18327   6615     42    196    696       O  
ATOM   5137  CB  PHE B 330      33.429  -3.710   9.302  1.00 65.66           C  
ANISOU 5137  CB  PHE B 330     4258  16118   4572     33    321    814       C  
ATOM   5138  CG  PHE B 330      32.718  -4.808   8.555  1.00 66.28           C  
ANISOU 5138  CG  PHE B 330     4336  16361   4486    -32    285    680       C  
ATOM   5139  CD1 PHE B 330      32.313  -4.621   7.241  1.00 67.83           C  
ANISOU 5139  CD1 PHE B 330     4454  16784   4534    -29    260    770       C  
ATOM   5140  CD2 PHE B 330      32.459  -6.029   9.164  1.00 65.33           C  
ANISOU 5140  CD2 PHE B 330     4290  16158   4374    -99    273    464       C  
ATOM   5141  CE1 PHE B 330      31.663  -5.630   6.547  1.00 68.78           C  
ANISOU 5141  CE1 PHE B 330     4565  17034   4535    -90    225    647       C  
ATOM   5142  CE2 PHE B 330      31.807  -7.042   8.479  1.00 66.04           C  
ANISOU 5142  CE2 PHE B 330     4370  16377   4345   -160    237    342       C  
ATOM   5143  CZ  PHE B 330      31.411  -6.842   7.168  1.00 68.76           C  
ANISOU 5143  CZ  PHE B 330     4631  16936   4559   -156    214    433       C  
ATOM   5144  N   LEU B 331      31.867  -3.842  12.019  1.00 63.26           N  
ANISOU 5144  N   LEU B 331     4021  15540   4476     31    267    604       N  
ATOM   5145  CA  LEU B 331      30.919  -4.525  12.893  1.00 62.46           C  
ANISOU 5145  CA  LEU B 331     3963  15388   4381    -10    239    430       C  
ATOM   5146  C   LEU B 331      29.770  -3.602  13.275  1.00 62.73           C  
ANISOU 5146  C   LEU B 331     3934  15441   4459     40    198    507       C  
ATOM   5147  O   LEU B 331      28.592  -3.981  13.177  1.00 66.19           O  
ANISOU 5147  O   LEU B 331     4350  15996   4803     15    161    425       O  
ATOM   5148  CB  LEU B 331      31.634  -5.048  14.136  1.00 60.88           C  
ANISOU 5148  CB  LEU B 331     3867  14938   4328    -39    274    302       C  
ATOM   5149  CG  LEU B 331      32.337  -6.389  13.938  1.00 65.16           C  
ANISOU 5149  CG  LEU B 331     4490  15456   4811   -114    298    142       C  
ATOM   5150  CD1 LEU B 331      32.892  -6.898  15.253  1.00 59.46           C  
ANISOU 5150  CD1 LEU B 331     3868  14495   4229   -143    326     10       C  
ATOM   5151  CD2 LEU B 331      31.382  -7.406  13.321  1.00 65.38           C  
ANISOU 5151  CD2 LEU B 331     4511  15652   4680   -177    254     10       C  
ATOM   5152  N   PHE B 332      30.092  -2.367  13.672  1.00 62.62           N  
ANISOU 5152  N   PHE B 332     3890  15307   4597    114    199    669       N  
ATOM   5153  CA  PHE B 332      29.049  -1.430  14.079  1.00 64.90           C  
ANISOU 5153  CA  PHE B 332     4127  15572   4959    166    152    745       C  
ATOM   5154  C   PHE B 332      28.058  -1.180  12.949  1.00 69.61           C  
ANISOU 5154  C   PHE B 332     4632  16422   5394    181    111    819       C  
ATOM   5155  O   PHE B 332      26.840  -1.213  13.161  1.00 64.63           O  
ANISOU 5155  O   PHE B 332     3981  15835   4742    177     74    761       O  
ATOM   5156  CB  PHE B 332      29.671  -0.113  14.549  1.00 70.52           C  
ANISOU 5156  CB  PHE B 332     4823  16113   5859    245    151    922       C  
ATOM   5157  CG  PHE B 332      28.661   0.897  15.024  1.00 70.33           C  
ANISOU 5157  CG  PHE B 332     4759  16031   5934    302    100   1001       C  
ATOM   5158  CD1 PHE B 332      28.130   0.820  16.299  1.00 71.09           C  
ANISOU 5158  CD1 PHE B 332     4904  15947   6159    292     91    893       C  
ATOM   5159  CD2 PHE B 332      28.240   1.922  14.192  1.00 69.60           C  
ANISOU 5159  CD2 PHE B 332     4580  16058   5806    363     60   1182       C  
ATOM   5160  CE1 PHE B 332      27.198   1.746  16.735  1.00 70.00           C  
ANISOU 5160  CE1 PHE B 332     4731  15747   6118    344     46    961       C  
ATOM   5161  CE2 PHE B 332      27.310   2.848  14.624  1.00 64.39           C  
ANISOU 5161  CE2 PHE B 332     3890  15330   5246    416     11   1250       C  
ATOM   5162  CZ  PHE B 332      26.791   2.761  15.896  1.00 67.38           C  
ANISOU 5162  CZ  PHE B 332     4318  15526   5758    407      5   1138       C  
ATOM   5163  N   VAL B 333      28.561  -0.920  11.739  1.00 69.04           N  
ANISOU 5163  N   VAL B 333     4503  16519   5210    198    117    948       N  
ATOM   5164  CA  VAL B 333      27.675  -0.595  10.623  1.00 73.61           C  
ANISOU 5164  CA  VAL B 333     4989  17343   5636    216     76   1037       C  
ATOM   5165  C   VAL B 333      26.851  -1.810  10.208  1.00 79.96           C  
ANISOU 5165  C   VAL B 333     5799  18323   6260    143     64    864       C  
ATOM   5166  O   VAL B 333      25.637  -1.709   9.990  1.00 84.77           O  
ANISOU 5166  O   VAL B 333     6360  19044   6806    148     25    853       O  
ATOM   5167  CB  VAL B 333      28.482  -0.034   9.440  1.00 72.42           C  
ANISOU 5167  CB  VAL B 333     4777  17332   5405    247     90   1218       C  
ATOM   5168  CG1 VAL B 333      27.627  -0.021   8.181  1.00 70.50           C  
ANISOU 5168  CG1 VAL B 333     4447  17377   4963    245     53   1276       C  
ATOM   5169  CG2 VAL B 333      28.989   1.364   9.763  1.00 73.58           C  
ANISOU 5169  CG2 VAL B 333     4901  17330   5724    329     85   1413       C  
ATOM   5170  N   VAL B 334      27.494  -2.975  10.088  1.00 73.91           N  
ANISOU 5170  N   VAL B 334     5094  17568   5420     74     92    726       N  
ATOM   5171  CA  VAL B 334      26.801  -4.163   9.596  1.00 71.89           C  
ANISOU 5171  CA  VAL B 334     4840  17476   4998      1     62    565       C  
ATOM   5172  C   VAL B 334      25.703  -4.590  10.561  1.00 82.05           C  
ANISOU 5172  C   VAL B 334     6164  18691   6321    -27     46    410       C  
ATOM   5173  O   VAL B 334      24.573  -4.877  10.148  1.00 70.27           O  
ANISOU 5173  O   VAL B 334     4629  17364   4706    -47     16    359       O  
ATOM   5174  CB  VAL B 334      27.805  -5.302   9.349  1.00 72.98           C  
ANISOU 5174  CB  VAL B 334     5042  17564   5123    -66     82    444       C  
ATOM   5175  CG1 VAL B 334      27.081  -6.635   9.224  1.00 71.26           C  
ANISOU 5175  CG1 VAL B 334     4828  17411   4837   -149     42    239       C  
ATOM   5176  CG2 VAL B 334      28.605  -5.015   8.103  1.00 83.29           C  
ANISOU 5176  CG2 VAL B 334     6301  18985   6361    -50     98    579       C  
ATOM   5177  N   MET B 335      26.011  -4.640  11.861  1.00 83.63           N  
ANISOU 5177  N   MET B 335     6443  18642   6690    -31     73    332       N  
ATOM   5178  CA  MET B 335      25.019  -5.157  12.798  1.00 92.97           C  
ANISOU 5178  CA  MET B 335     7667  19748   7908    -68     62    168       C  
ATOM   5179  C   MET B 335      23.820  -4.229  12.973  1.00 99.39           C  
ANISOU 5179  C   MET B 335     8414  20579   8772    -14     35    246       C  
ATOM   5180  O   MET B 335      22.756  -4.691  13.399  1.00107.94           O  
ANISOU 5180  O   MET B 335     9506  21668   9836    -48     23    116       O  
ATOM   5181  CB  MET B 335      25.668  -5.443  14.150  1.00 92.43           C  
ANISOU 5181  CB  MET B 335     7700  19410   8008    -88     95     66       C  
ATOM   5182  CG  MET B 335      26.666  -6.586  14.118  1.00 91.06           C  
ANISOU 5182  CG  MET B 335     7606  19185   7806   -154    115    -59       C  
ATOM   5183  SD  MET B 335      27.306  -7.016  15.748  1.00 83.53           S  
ANISOU 5183  SD  MET B 335     6777  17923   7036   -185    156   -197       S  
ATOM   5184  CE  MET B 335      28.346  -8.416  15.329  1.00 89.58           C  
ANISOU 5184  CE  MET B 335     7618  18671   7748   -263    168   -332       C  
ATOM   5185  N   TRP B 336      23.955  -2.943  12.650  1.00 91.33           N  
ANISOU 5185  N   TRP B 336     7327  19551   7823     67     19    450       N  
ATOM   5186  CA  TRP B 336      22.821  -2.027  12.674  1.00 87.58           C  
ANISOU 5186  CA  TRP B 336     6784  19087   7404    122    -25    533       C  
ATOM   5187  C   TRP B 336      22.099  -1.936  11.337  1.00 91.35           C  
ANISOU 5187  C   TRP B 336     7174  19824   7711    130    -55    604       C  
ATOM   5188  O   TRP B 336      20.979  -1.416  11.291  1.00 90.59           O  
ANISOU 5188  O   TRP B 336     7025  19752   7643    161    -97    634       O  
ATOM   5189  CB  TRP B 336      23.278  -0.625  13.088  1.00 76.12           C  
ANISOU 5189  CB  TRP B 336     5314  17470   6139    208    -40    718       C  
ATOM   5190  CG  TRP B 336      23.289  -0.400  14.568  1.00 78.47           C  
ANISOU 5190  CG  TRP B 336     5674  17504   6638    216    -31    654       C  
ATOM   5191  CD1 TRP B 336      24.386  -0.353  15.380  1.00 73.64           C  
ANISOU 5191  CD1 TRP B 336     5129  16697   6155    217      4    652       C  
ATOM   5192  CD2 TRP B 336      22.156  -0.166  15.412  1.00 80.83           C  
ANISOU 5192  CD2 TRP B 336     5969  17704   7037    224    -57    587       C  
ATOM   5193  NE1 TRP B 336      24.005  -0.117  16.677  1.00 69.17           N  
ANISOU 5193  NE1 TRP B 336     4603  15922   5755    224      2    587       N  
ATOM   5194  CE2 TRP B 336      22.641   0.002  16.724  1.00 72.73           C  
ANISOU 5194  CE2 TRP B 336     5012  16430   6193    227    -34    546       C  
ATOM   5195  CE3 TRP B 336      20.778  -0.089  15.187  1.00 85.41           C  
ANISOU 5195  CE3 TRP B 336     6494  18382   7577    227    -96    555       C  
ATOM   5196  CZ2 TRP B 336      21.798   0.243  17.808  1.00 65.54           C  
ANISOU 5196  CZ2 TRP B 336     4114  15373   5415    232    -45    475       C  
ATOM   5197  CZ3 TRP B 336      19.943   0.150  16.265  1.00 70.78           C  
ANISOU 5197  CZ3 TRP B 336     4653  16378   5864    233   -108    482       C  
ATOM   5198  CH2 TRP B 336      20.456   0.313  17.559  1.00 67.23           C  
ANISOU 5198  CH2 TRP B 336     4271  15688   5586    235    -81    443       C  
ATOM   5199  N   CYS B 337      22.709  -2.424  10.257  1.00 97.56           N  
ANISOU 5199  N   CYS B 337     7942  20798   8328    101    -35    630       N  
ATOM   5200  CA  CYS B 337      22.120  -2.240   8.933  1.00 96.54           C  
ANISOU 5200  CA  CYS B 337     7725  20913   8043    112    -56    719       C  
ATOM   5201  C   CYS B 337      20.777  -2.937   8.744  1.00 95.37           C  
ANISOU 5201  C   CYS B 337     7554  20881   7802     68    -67    582       C  
ATOM   5202  O   CYS B 337      19.900  -2.338   8.097  1.00 98.19           O  
ANISOU 5202  O   CYS B 337     7836  21334   8139    105   -110    671       O  
ATOM   5203  CB  CYS B 337      23.113  -2.689   7.857  1.00 93.68           C  
ANISOU 5203  CB  CYS B 337     7350  20728   7516     83    -21    764       C  
ATOM   5204  SG  CYS B 337      24.117  -1.340   7.222  1.00 95.63           S  
ANISOU 5204  SG  CYS B 337     7543  20977   7816    163    -30   1031       S  
ATOM   5205  N   PRO B 338      20.545  -4.166   9.227  1.00 86.43           N  
ANISOU 5205  N   PRO B 338     6483  19743   6614     -9    -33    373       N  
ATOM   5206  CA  PRO B 338      19.193  -4.732   9.082  1.00 82.72           C  
ANISOU 5206  CA  PRO B 338     5981  19368   6079    -46    -37    251       C  
ATOM   5207  C   PRO B 338      18.119  -3.858   9.701  1.00 84.20           C  
ANISOU 5207  C   PRO B 338     6139  19440   6415      9    -97    287       C  
ATOM   5208  O   PRO B 338      17.048  -3.682   9.106  1.00 87.28           O  
ANISOU 5208  O   PRO B 338     6459  19941   6761     21   -133    305       O  
ATOM   5209  CB  PRO B 338      19.308  -6.091   9.786  1.00 73.05           C  
ANISOU 5209  CB  PRO B 338     4852  18063   4843   -132      2     24       C  
ATOM   5210  CG  PRO B 338      20.735  -6.456   9.643  1.00 69.42           C  
ANISOU 5210  CG  PRO B 338     4454  17502   4421   -152      5     35       C  
ATOM   5211  CD  PRO B 338      21.489  -5.163   9.766  1.00 76.75           C  
ANISOU 5211  CD  PRO B 338     5356  18443   5364    -71     -2    236       C  
ATOM   5212  N   PHE B 339      18.392  -3.279  10.872  1.00 86.24           N  
ANISOU 5212  N   PHE B 339     6442  19469   6857     43   -108    301       N  
ATOM   5213  CA  PHE B 339      17.406  -2.434  11.539  1.00 85.41           C  
ANISOU 5213  CA  PHE B 339     6304  19240   6908     93   -155    330       C  
ATOM   5214  C   PHE B 339      17.077  -1.199  10.708  1.00 89.81           C  
ANISOU 5214  C   PHE B 339     6771  19867   7485    174   -214    536       C  
ATOM   5215  O   PHE B 339      15.904  -0.875  10.498  1.00 97.31           O  
ANISOU 5215  O   PHE B 339     7662  20864   8447    196   -263    540       O  
ATOM   5216  CB  PHE B 339      17.915  -2.031  12.921  1.00 83.84           C  
ANISOU 5216  CB  PHE B 339     6170  18779   6908    113   -141    317       C  
ATOM   5217  CG  PHE B 339      17.157  -0.893  13.533  1.00 85.36           C  
ANISOU 5217  CG  PHE B 339     6322  18835   7278    181   -186    397       C  
ATOM   5218  CD1 PHE B 339      15.902  -1.093  14.075  1.00 81.00           C  
ANISOU 5218  CD1 PHE B 339     5753  18253   6771    163   -203    278       C  
ATOM   5219  CD2 PHE B 339      17.701   0.382  13.564  1.00 89.33           C  
ANISOU 5219  CD2 PHE B 339     6801  19238   7904    262   -210    589       C  
ATOM   5220  CE1 PHE B 339      15.204  -0.044  14.638  1.00 89.06           C  
ANISOU 5220  CE1 PHE B 339     6731  19148   7958    225   -244    348       C  
ATOM   5221  CE2 PHE B 339      17.006   1.435  14.126  1.00 87.39           C  
ANISOU 5221  CE2 PHE B 339     6517  18864   7821    324   -252    660       C  
ATOM   5222  CZ  PHE B 339      15.757   1.222  14.665  1.00 86.96           C  
ANISOU 5222  CZ  PHE B 339     6444  18783   7814    306   -270    539       C  
ATOM   5223  N   PHE B 340      18.103  -0.492  10.228  1.00 85.55           N  
ANISOU 5223  N   PHE B 340     6223  19332   6952    220   -214    707       N  
ATOM   5224  CA  PHE B 340      17.854   0.723   9.458  1.00 83.50           C  
ANISOU 5224  CA  PHE B 340     5887  19126   6714    297   -272    908       C  
ATOM   5225  C   PHE B 340      17.215   0.408   8.111  1.00 95.35           C  
ANISOU 5225  C   PHE B 340     7323  20871   8034    279   -298    925       C  
ATOM   5226  O   PHE B 340      16.358   1.162   7.635  1.00101.59           O  
ANISOU 5226  O   PHE B 340     8049  21705   8846    327   -364   1017       O  
ATOM   5227  CB  PHE B 340      19.151   1.504   9.266  1.00 82.85           C  
ANISOU 5227  CB  PHE B 340     5814  18990   6676    344   -259   1083       C  
ATOM   5228  CG  PHE B 340      19.540   2.329  10.454  1.00 76.27           C  
ANISOU 5228  CG  PHE B 340     5018  17901   6060    393   -258   1133       C  
ATOM   5229  CD1 PHE B 340      20.383   1.818  11.426  1.00 77.13           C  
ANISOU 5229  CD1 PHE B 340     5206  17856   6243    360   -205   1038       C  
ATOM   5230  CD2 PHE B 340      19.058   3.619  10.601  1.00 75.31           C  
ANISOU 5230  CD2 PHE B 340     4855  17687   6072    472   -313   1272       C  
ATOM   5231  CE1 PHE B 340      20.742   2.580  12.524  1.00 81.27           C  
ANISOU 5231  CE1 PHE B 340     5767  18140   6973    403   -202   1084       C  
ATOM   5232  CE2 PHE B 340      19.413   4.388  11.693  1.00 75.86           C  
ANISOU 5232  CE2 PHE B 340     4959  17520   6343    516   -309   1318       C  
ATOM   5233  CZ  PHE B 340      20.255   3.868  12.657  1.00 77.91           C  
ANISOU 5233  CZ  PHE B 340     5298  17630   6676    481   -253   1225       C  
ATOM   5234  N   ILE B 341      17.610  -0.703   7.486  1.00 90.65           N  
ANISOU 5234  N   ILE B 341     6744  20431   7268    209   -248    834       N  
ATOM   5235  CA  ILE B 341      16.988  -1.105   6.227  1.00 90.73           C  
ANISOU 5235  CA  ILE B 341     6695  20663   7114    183   -265    834       C  
ATOM   5236  C   ILE B 341      15.506  -1.389   6.440  1.00 88.40           C  
ANISOU 5236  C   ILE B 341     6373  20382   6834    168   -304    717       C  
ATOM   5237  O   ILE B 341      14.651  -0.902   5.692  1.00 93.41           O  
ANISOU 5237  O   ILE B 341     6941  21108   7443    200   -369    791       O  
ATOM   5238  CB  ILE B 341      17.718  -2.319   5.624  1.00 88.74           C  
ANISOU 5238  CB  ILE B 341     6465  20554   6700    104   -188    740       C  
ATOM   5239  CG1 ILE B 341      19.069  -1.894   5.044  1.00 86.80           C  
ANISOU 5239  CG1 ILE B 341     6216  20344   6418    125   -161    890       C  
ATOM   5240  CG2 ILE B 341      16.862  -2.980   4.550  1.00 79.24           C  
ANISOU 5240  CG2 ILE B 341     5206  19542   5358     61   -195    682       C  
ATOM   5241  CD1 ILE B 341      18.964  -0.830   3.975  1.00 88.77           C  
ANISOU 5241  CD1 ILE B 341     6401  20686   6641    186   -221   1097       C  
ATOM   5242  N   THR B 342      15.180  -2.168   7.478  1.00 89.98           N  
ANISOU 5242  N   THR B 342     6625  20484   7081    120   -269    533       N  
ATOM   5243  CA  THR B 342      13.784  -2.495   7.755  1.00 98.32           C  
ANISOU 5243  CA  THR B 342     7654  21547   8157    101   -299    409       C  
ATOM   5244  C   THR B 342      12.983  -1.253   8.129  1.00102.32           C  
ANISOU 5244  C   THR B 342     8110  21944   8824    181   -378    511       C  
ATOM   5245  O   THR B 342      11.810  -1.129   7.758  1.00105.63           O  
ANISOU 5245  O   THR B 342     8467  22431   9236    192   -433    497       O  
ATOM   5246  CB  THR B 342      13.704  -3.541   8.867  1.00 90.55           C  
ANISOU 5246  CB  THR B 342     6744  20462   7197     32   -240    195       C  
ATOM   5247  OG1 THR B 342      14.500  -4.678   8.509  1.00 84.32           O  
ANISOU 5247  OG1 THR B 342     6001  19768   6267    -41   -164    103       O  
ATOM   5248  CG2 THR B 342      12.264  -3.989   9.083  1.00 91.55           C  
ANISOU 5248  CG2 THR B 342     6841  20615   7330      3   -262     58       C  
ATOM   5249  N   ASN B 343      13.603  -0.309   8.840  1.00100.01           N  
ANISOU 5249  N   ASN B 343     7839  21478   8683    239   -384    617       N  
ATOM   5250  CA  ASN B 343      12.898   0.907   9.233  1.00104.29           C  
ANISOU 5250  CA  ASN B 343     8331  21902   9391    316   -452    716       C  
ATOM   5251  C   ASN B 343      12.607   1.794   8.025  1.00110.71           C  
ANISOU 5251  C   ASN B 343     9069  22839  10157    375   -524    896       C  
ATOM   5252  O   ASN B 343      11.481   2.285   7.858  1.00108.32           O  
ANISOU 5252  O   ASN B 343     8702  22550   9904    410   -593    914       O  
ATOM   5253  CB  ASN B 343      13.715   1.664  10.279  1.00103.04           C  
ANISOU 5253  CB  ASN B 343     8220  21522   9409    359   -432    786       C  
ATOM   5254  CG  ASN B 343      12.855   2.254  11.373  1.00101.48           C  
ANISOU 5254  CG  ASN B 343     8008  21145   9403    393   -460    748       C  
ATOM   5255  OD1 ASN B 343      11.700   2.610  11.144  1.00105.03           O  
ANISOU 5255  OD1 ASN B 343     8390  21635   9882    418   -518    751       O  
ATOM   5256  ND2 ASN B 343      13.415   2.363  12.572  1.00 96.80           N  
ANISOU 5256  ND2 ASN B 343     7479  20352   8950    393   -419    711       N  
ATOM   5257  N   ILE B 344      13.614   2.016   7.174  1.00112.40           N  
ANISOU 5257  N   ILE B 344     9288  23142  10278    387   -512   1029       N  
ATOM   5258  CA  ILE B 344      13.400   2.784   5.949  1.00118.85           C  
ANISOU 5258  CA  ILE B 344    10041  24084  11030    435   -579   1196       C  
ATOM   5259  C   ILE B 344      12.353   2.103   5.076  1.00120.54           C  
ANISOU 5259  C   ILE B 344    10210  24481  11110    396   -614   1114       C  
ATOM   5260  O   ILE B 344      11.499   2.765   4.473  1.00121.73           O  
ANISOU 5260  O   ILE B 344    10299  24682  11273    440   -698   1195       O  
ATOM   5261  CB  ILE B 344      14.733   2.978   5.199  1.00117.49           C  
ANISOU 5261  CB  ILE B 344     9890  23984  10767    441   -545   1334       C  
ATOM   5262  CG1 ILE B 344      15.699   3.829   6.027  1.00117.20           C  
ANISOU 5262  CG1 ILE B 344     9890  23756  10883    491   -522   1438       C  
ATOM   5263  CG2 ILE B 344      14.502   3.619   3.838  1.00115.22           C  
ANISOU 5263  CG2 ILE B 344     9547  23845  10388    477   -611   1492       C  
ATOM   5264  CD1 ILE B 344      15.222   5.246   6.265  1.00118.71           C  
ANISOU 5264  CD1 ILE B 344    10045  23823  11235    579   -594   1582       C  
ATOM   5265  N   MET B 345      12.390   0.769   5.013  1.00115.97           N  
ANISOU 5265  N   MET B 345     9660  23993  10408    312   -553    948       N  
ATOM   5266  CA  MET B 345      11.403   0.024   4.241  1.00112.94           C  
ANISOU 5266  CA  MET B 345     9237  23771   9903    268   -578    855       C  
ATOM   5267  C   MET B 345       9.996   0.253   4.784  1.00115.09           C  
ANISOU 5267  C   MET B 345     9465  23980  10285    289   -639    781       C  
ATOM   5268  O   MET B 345       9.064   0.548   4.027  1.00113.64           O  
ANISOU 5268  O   MET B 345     9218  23889  10072    312   -717    822       O  
ATOM   5269  CB  MET B 345      11.766  -1.463   4.258  1.00108.06           C  
ANISOU 5269  CB  MET B 345     8668  23231   9159    173   -487    678       C  
ATOM   5270  CG  MET B 345      10.862  -2.361   3.432  1.00114.17           C  
ANISOU 5270  CG  MET B 345     9406  24170   9802    118   -498    574       C  
ATOM   5271  SD  MET B 345      11.386  -4.087   3.509  1.00114.10           S  
ANISOU 5271  SD  MET B 345     9454  24227   9672      6   -379    369       S  
ATOM   5272  CE  MET B 345      10.070  -4.883   2.591  1.00112.68           C  
ANISOU 5272  CE  MET B 345     9219  24209   9385    -41   -413    268       C  
ATOM   5273  N   ALA B 346       9.829   0.142   6.105  1.00117.29           N  
ANISOU 5273  N   ALA B 346     9776  24093  10696    282   -608    673       N  
ATOM   5274  CA  ALA B 346       8.516   0.346   6.709  1.00117.58           C  
ANISOU 5274  CA  ALA B 346     9767  24058  10850    299   -658    594       C  
ATOM   5275  C   ALA B 346       8.014   1.768   6.502  1.00123.44           C  
ANISOU 5275  C   ALA B 346    10442  24745  11716    392   -753    762       C  
ATOM   5276  O   ALA B 346       6.804   1.985   6.372  1.00129.54           O  
ANISOU 5276  O   ALA B 346    11148  25540  12533    412   -821    735       O  
ATOM   5277  CB  ALA B 346       8.568   0.019   8.201  1.00107.24           C  
ANISOU 5277  CB  ALA B 346     8513  22566   9668    272   -599    457       C  
ATOM   5278  N   VAL B 347       8.920   2.747   6.476  1.00120.98           N  
ANISOU 5278  N   VAL B 347    10145  24358  11464    451   -759    933       N  
ATOM   5279  CA  VAL B 347       8.493   4.125   6.249  1.00121.21           C  
ANISOU 5279  CA  VAL B 347    10116  24331  11608    541   -848   1098       C  
ATOM   5280  C   VAL B 347       8.110   4.342   4.787  1.00123.00           C  
ANISOU 5280  C   VAL B 347    10289  24741  11705    558   -923   1200       C  
ATOM   5281  O   VAL B 347       7.171   5.088   4.484  1.00129.51           O  
ANISOU 5281  O   VAL B 347    11047  25564  12596    610  -1016   1262       O  
ATOM   5282  CB  VAL B 347       9.588   5.106   6.707  1.00123.77           C  
ANISOU 5282  CB  VAL B 347    10478  24507  12040    597   -827   1248       C  
ATOM   5283  CG1 VAL B 347       9.215   6.536   6.348  1.00120.82           C  
ANISOU 5283  CG1 VAL B 347    10049  24086  11769    688   -918   1428       C  
ATOM   5284  CG2 VAL B 347       9.805   4.983   8.204  1.00127.95           C  
ANISOU 5284  CG2 VAL B 347    11058  24836  12722    585   -767   1146       C  
ATOM   5285  N   ILE B 348       8.809   3.682   3.859  1.00119.01           N  
ANISOU 5285  N   ILE B 348     9811  24391  11015    512   -888   1215       N  
ATOM   5286  CA  ILE B 348       8.507   3.857   2.437  1.00119.88           C  
ANISOU 5286  CA  ILE B 348     9881  24674  10996    522   -958   1313       C  
ATOM   5287  C   ILE B 348       7.165   3.219   2.087  1.00126.44           C  
ANISOU 5287  C   ILE B 348    10660  25604  11777    490  -1009   1187       C  
ATOM   5288  O   ILE B 348       6.220   3.904   1.678  1.00119.00           O  
ANISOU 5288  O   ILE B 348     9655  24675  10884    539  -1111   1249       O  
ATOM   5289  CB  ILE B 348       9.644   3.294   1.565  1.00112.02           C  
ANISOU 5289  CB  ILE B 348     8930  23811   9822    476   -898   1356       C  
ATOM   5290  CG1 ILE B 348      10.897   4.165   1.686  1.00101.72           C  
ANISOU 5290  CG1 ILE B 348     7660  22421   8569    523   -870   1521       C  
ATOM   5291  CG2 ILE B 348       9.204   3.205   0.107  1.00118.66           C  
ANISOU 5291  CG2 ILE B 348     9737  24837  10512    468   -964   1415       C  
ATOM   5292  CD1 ILE B 348      12.083   3.643   0.902  1.00 87.10           C  
ANISOU 5292  CD1 ILE B 348     5847  20688   6558    478   -804   1562       C  
ATOM   5293  N   CYS B 349       7.061   1.897   2.240  1.00130.03           N  
ANISOU 5293  N   CYS B 349    11141  26127  12138    407   -942   1007       N  
ATOM   5294  CA  CYS B 349       5.807   1.188   1.977  1.00138.90           C  
ANISOU 5294  CA  CYS B 349    12220  27340  13217    369   -980    872       C  
ATOM   5295  C   CYS B 349       5.020   1.092   3.281  1.00142.16           C  
ANISOU 5295  C   CYS B 349    12618  27610  13785    368   -969    735       C  
ATOM   5296  O   CYS B 349       5.053   0.092   4.001  1.00143.85           O  
ANISOU 5296  O   CYS B 349    12873  27798  13984    302   -888    565       O  
ATOM   5297  CB  CYS B 349       6.069  -0.185   1.367  1.00141.02           C  
ANISOU 5297  CB  CYS B 349    12523  27760  13298    278   -913    754       C  
ATOM   5298  SG  CYS B 349       7.308  -1.189   2.220  1.00141.21           S  
ANISOU 5298  SG  CYS B 349    12639  27726  13287    208   -765    634       S  
ATOM   5299  N   LYS B 350       4.298   2.172   3.587  1.00144.15           N  
ANISOU 5299  N   LYS B 350    12811  27763  14195    442  -1051    810       N  
ATOM   5300  CA  LYS B 350       3.511   2.205   4.815  1.00146.73           C  
ANISOU 5300  CA  LYS B 350    13116  27945  14688    446  -1044    690       C  
ATOM   5301  C   LYS B 350       2.351   1.219   4.754  1.00148.32           C  
ANISOU 5301  C   LYS B 350    13280  28233  14841    387  -1053    511       C  
ATOM   5302  O   LYS B 350       2.030   0.566   5.754  1.00143.00           O  
ANISOU 5302  O   LYS B 350    12627  27482  14225    342   -993    346       O  
ATOM   5303  CB  LYS B 350       3.002   3.622   5.079  1.00148.93           C  
ANISOU 5303  CB  LYS B 350    13334  28102  15152    540  -1131    817       C  
ATOM   5304  CG  LYS B 350       2.416   3.823   6.471  1.00146.36           C  
ANISOU 5304  CG  LYS B 350    12993  27595  15023    551  -1111    716       C  
ATOM   5305  CD  LYS B 350       3.471   3.640   7.551  1.00142.70           C  
ANISOU 5305  CD  LYS B 350    12617  26991  14613    529  -1007    680       C  
ATOM   5306  CE  LYS B 350       2.894   3.897   8.933  1.00144.26           C  
ANISOU 5306  CE  LYS B 350    12802  27000  15011    540   -988    587       C  
ATOM   5307  NZ  LYS B 350       3.922   3.744  10.001  1.00144.44           N  
ANISOU 5307  NZ  LYS B 350    12916  26875  15092    518   -894    554       N  
ATOM   5308  N   GLU B 351       1.711   1.095   3.589  1.00154.47           N  
ANISOU 5308  N   GLU B 351    14008  29169  15515    386  -1128    539       N  
ATOM   5309  CA  GLU B 351       0.625   0.144   3.402  1.00158.61           C  
ANISOU 5309  CA  GLU B 351    14494  29786  15982    330  -1140    377       C  
ATOM   5310  C   GLU B 351       0.906  -0.909   2.341  1.00151.98           C  
ANISOU 5310  C   GLU B 351    13686  29133  14926    262  -1111    336       C  
ATOM   5311  O   GLU B 351       0.112  -1.848   2.207  1.00153.95           O  
ANISOU 5311  O   GLU B 351    13917  29461  15115    204  -1105    189       O  
ATOM   5312  CB  GLU B 351      -0.679   0.874   3.035  1.00164.29           C  
ANISOU 5312  CB  GLU B 351    15110  30515  16796    387  -1268    419       C  
ATOM   5313  CG  GLU B 351      -1.250   1.757   4.137  1.00163.59           C  
ANISOU 5313  CG  GLU B 351    14975  30244  16937    445  -1295    418       C  
ATOM   5314  CD  GLU B 351      -0.689   3.167   4.110  1.00162.12           C  
ANISOU 5314  CD  GLU B 351    14784  29961  16855    536  -1344    620       C  
ATOM   5315  OE1 GLU B 351       0.143   3.463   3.228  1.00162.60           O  
ANISOU 5315  OE1 GLU B 351    14877  30098  16804    553  -1358    762       O  
ATOM   5316  OE2 GLU B 351      -1.085   3.981   4.971  1.00160.11           O  
ANISOU 5316  OE2 GLU B 351    14491  29550  16794    588  -1365    637       O  
ATOM   5317  N   SER B 352       1.998  -0.789   1.584  1.00146.24           N  
ANISOU 5317  N   SER B 352    13005  28474  14085    264  -1091    459       N  
ATOM   5318  CA  SER B 352       2.279  -1.772   0.545  1.00141.38           C  
ANISOU 5318  CA  SER B 352    12417  28029  13272    198  -1061    422       C  
ATOM   5319  C   SER B 352       2.903  -3.039   1.124  1.00137.66           C  
ANISOU 5319  C   SER B 352    12019  27556  12731    112   -927    260       C  
ATOM   5320  O   SER B 352       2.573  -4.148   0.688  1.00135.25           O  
ANISOU 5320  O   SER B 352    11720  27358  12311     42   -894    137       O  
ATOM   5321  CB  SER B 352       3.188  -1.163  -0.525  1.00142.70           C  
ANISOU 5321  CB  SER B 352    12603  28271  13347    231  -1089    613       C  
ATOM   5322  OG  SER B 352       3.450  -2.089  -1.565  1.00140.74           O  
ANISOU 5322  OG  SER B 352    12380  28180  12915    166  -1060    580       O  
ATOM   5323  N   CYS B 353       3.799  -2.899   2.099  1.00133.02           N  
ANISOU 5323  N   CYS B 353    11487  26840  12216    116   -851    257       N  
ATOM   5324  CA  CYS B 353       4.446  -4.049   2.711  1.00125.80           C  
ANISOU 5324  CA  CYS B 353    10646  25907  11247     37   -729    105       C  
ATOM   5325  C   CYS B 353       3.690  -4.494   3.963  1.00120.21           C  
ANISOU 5325  C   CYS B 353     9944  25086  10644      9   -697    -71       C  
ATOM   5326  O   CYS B 353       2.852  -3.774   4.510  1.00121.31           O  
ANISOU 5326  O   CYS B 353    10033  25134  10924     57   -761    -61       O  
ATOM   5327  CB  CYS B 353       5.899  -3.728   3.061  1.00127.68           C  
ANISOU 5327  CB  CYS B 353    10948  26067  11497     51   -665    192       C  
ATOM   5328  SG  CYS B 353       6.908  -3.111   1.692  1.00134.37           S  
ANISOU 5328  SG  CYS B 353    11792  27028  12236     86   -693    408       S  
ATOM   5329  N   ASN B 354       4.007  -5.705   4.420  1.00116.88           N  
ANISOU 5329  N   ASN B 354     9585  24665  10159    -73   -594   -236       N  
ATOM   5330  CA  ASN B 354       3.405  -6.262   5.627  1.00116.13           C  
ANISOU 5330  CA  ASN B 354     9514  24463  10146   -113   -550   -417       C  
ATOM   5331  C   ASN B 354       4.052  -5.632   6.859  1.00122.59           C  
ANISOU 5331  C   ASN B 354    10383  25089  11108    -81   -523   -392       C  
ATOM   5332  O   ASN B 354       5.274  -5.704   7.028  1.00127.68           O  
ANISOU 5332  O   ASN B 354    11094  25693  11724    -89   -464   -352       O  
ATOM   5333  CB  ASN B 354       3.568  -7.782   5.638  1.00111.44           C  
ANISOU 5333  CB  ASN B 354     8975  23934   9434   -213   -447   -597       C  
ATOM   5334  CG  ASN B 354       2.752  -8.456   6.727  1.00115.21           C  
ANISOU 5334  CG  ASN B 354     9473  24327   9976   -263   -406   -795       C  
ATOM   5335  OD1 ASN B 354       2.336  -7.824   7.698  1.00122.75           O  
ANISOU 5335  OD1 ASN B 354    10421  25144  11076   -229   -435   -807       O  
ATOM   5336  ND2 ASN B 354       2.528  -9.755   6.572  1.00111.96           N  
ANISOU 5336  ND2 ASN B 354     9083  23990   9466   -346   -333   -952       N  
ATOM   5337  N   GLU B 355       3.236  -5.022   7.720  1.00118.89           N  
ANISOU 5337  N   GLU B 355     9879  24494  10801    -45   -565   -416       N  
ATOM   5338  CA  GLU B 355       3.750  -4.306   8.883  1.00116.55           C  
ANISOU 5338  CA  GLU B 355     9621  24000  10663     -7   -549   -380       C  
ATOM   5339  C   GLU B 355       4.002  -5.196  10.096  1.00115.85           C  
ANISOU 5339  C   GLU B 355     9621  23796  10600    -78   -456   -563       C  
ATOM   5340  O   GLU B 355       4.839  -4.851  10.936  1.00121.91           O  
ANISOU 5340  O   GLU B 355    10451  24415  11456    -63   -422   -535       O  
ATOM   5341  CB  GLU B 355       2.790  -3.176   9.275  1.00116.28           C  
ANISOU 5341  CB  GLU B 355     9503  23867  10811     66   -632   -316       C  
ATOM   5342  CG  GLU B 355       2.938  -1.910   8.437  1.00121.47           C  
ANISOU 5342  CG  GLU B 355    10098  24556  11501    158   -721    -93       C  
ATOM   5343  CD  GLU B 355       4.255  -1.188   8.688  1.00126.43           C  
ANISOU 5343  CD  GLU B 355    10780  25084  12174    201   -696     50       C  
ATOM   5344  OE1 GLU B 355       4.850  -1.384   9.770  1.00128.64           O  
ANISOU 5344  OE1 GLU B 355    11131  25221  12526    179   -628    -17       O  
ATOM   5345  OE2 GLU B 355       4.696  -0.422   7.805  1.00127.14           O  
ANISOU 5345  OE2 GLU B 355    10843  25235  12229    256   -746    228       O  
ATOM   5346  N   ASP B 356       3.307  -6.331  10.214  1.00112.98           N  
ANISOU 5346  N   ASP B 356     9270  23492  10164   -155   -415   -749       N  
ATOM   5347  CA  ASP B 356       3.493  -7.198  11.377  1.00118.70           C  
ANISOU 5347  CA  ASP B 356    10085  24104  10910   -226   -329   -930       C  
ATOM   5348  C   ASP B 356       4.848  -7.900  11.335  1.00125.85           C  
ANISOU 5348  C   ASP B 356    11090  25021  11707   -271   -248   -948       C  
ATOM   5349  O   ASP B 356       5.592  -7.918  12.331  1.00130.18           O  
ANISOU 5349  O   ASP B 356    11721  25418  12324   -284   -205   -984       O  
ATOM   5350  CB  ASP B 356       2.356  -8.218  11.447  1.00121.32           C  
ANISOU 5350  CB  ASP B 356    10401  24504  11190   -296   -304  -1121       C  
ATOM   5351  CG  ASP B 356       0.984  -7.572  11.329  1.00128.27           C  
ANISOU 5351  CG  ASP B 356    11171  25397  12170   -253   -388  -1103       C  
ATOM   5352  OD1 ASP B 356       0.917  -6.329  11.228  1.00130.85           O  
ANISOU 5352  OD1 ASP B 356    11434  25671  12611   -167   -463   -944       O  
ATOM   5353  OD2 ASP B 356      -0.027  -8.307  11.337  1.00129.64           O  
ANISOU 5353  OD2 ASP B 356    11318  25628  12312   -303   -378  -1248       O  
ATOM   5354  N   VAL B 357       5.174  -8.502  10.190  1.00120.81           N  
ANISOU 5354  N   VAL B 357    10440  24556  10907   -298   -226   -927       N  
ATOM   5355  CA  VAL B 357       6.484  -9.119  10.022  1.00117.70           C  
ANISOU 5355  CA  VAL B 357    10120  24181  10420   -336   -147   -930       C  
ATOM   5356  C   VAL B 357       7.581  -8.078  10.201  1.00104.80           C  
ANISOU 5356  C   VAL B 357     8509  22451   8857   -269   -174   -761       C  
ATOM   5357  O   VAL B 357       8.631  -8.360  10.786  1.00 96.63           O  
ANISOU 5357  O   VAL B 357     7558  21326   7830   -292   -117   -789       O  
ATOM   5358  CB  VAL B 357       6.571  -9.816   8.652  1.00121.58           C  
ANISOU 5358  CB  VAL B 357    10566  24872  10758   -369   -120   -916       C  
ATOM   5359  CG1 VAL B 357       7.907 -10.534   8.496  1.00118.98           C  
ANISOU 5359  CG1 VAL B 357    10286  24551  10370   -413    -24   -931       C  
ATOM   5360  CG2 VAL B 357       5.408 -10.785   8.481  1.00122.06           C  
ANISOU 5360  CG2 VAL B 357    10592  25014  10772   -430    -98  -1075       C  
ATOM   5361  N   ILE B 358       7.346  -6.855   9.715  1.00104.27           N  
ANISOU 5361  N   ILE B 358     8369  22397   8854   -185   -262   -583       N  
ATOM   5362  CA  ILE B 358       8.320  -5.779   9.879  1.00105.64           C  
ANISOU 5362  CA  ILE B 358     8555  22472   9112   -116   -286   -410       C  
ATOM   5363  C   ILE B 358       8.491  -5.429  11.353  1.00111.21           C  
ANISOU 5363  C   ILE B 358     9316  22950   9988   -105   -272   -457       C  
ATOM   5364  O   ILE B 358       9.605  -5.148  11.815  1.00121.93           O  
ANISOU 5364  O   ILE B 358    10734  24199  11396    -90   -246   -399       O  
ATOM   5365  CB  ILE B 358       7.902  -4.552   9.044  1.00104.22           C  
ANISOU 5365  CB  ILE B 358     8279  22349   8970    -29   -381   -216       C  
ATOM   5366  CG1 ILE B 358       8.249  -4.765   7.568  1.00106.93           C  
ANISOU 5366  CG1 ILE B 358     8590  22893   9145    -35   -388   -127       C  
ATOM   5367  CG2 ILE B 358       8.556  -3.286   9.570  1.00100.50           C  
ANISOU 5367  CG2 ILE B 358     7813  21721   8650     50   -410    -58       C  
ATOM   5368  CD1 ILE B 358       7.859  -3.606   6.668  1.00106.91           C  
ANISOU 5368  CD1 ILE B 358     8503  22954   9164     45   -486     62       C  
ATOM   5369  N   GLY B 359       7.397  -5.444  12.116  1.00 99.14           N  
ANISOU 5369  N   GLY B 359     7767  21341   8559   -114   -287   -564       N  
ATOM   5370  CA  GLY B 359       7.506  -5.198  13.545  1.00 87.10           C  
ANISOU 5370  CA  GLY B 359     6296  19598   7200   -114   -264   -625       C  
ATOM   5371  C   GLY B 359       8.356  -6.243  14.240  1.00 74.57           C  
ANISOU 5371  C   GLY B 359     4828  17944   5561   -191   -183   -767       C  
ATOM   5372  O   GLY B 359       9.227  -5.918  15.054  1.00 78.34           O  
ANISOU 5372  O   GLY B 359     5369  18259   6138   -178   -163   -738       O  
ATOM   5373  N   ALA B 360       8.125  -7.518  13.913  1.00 72.37           N  
ANISOU 5373  N   ALA B 360     4581  17787   5130   -273   -135   -921       N  
ATOM   5374  CA  ALA B 360       8.951  -8.580  14.489  1.00 77.42           C  
ANISOU 5374  CA  ALA B 360     5335  18373   5707   -350    -59  -1061       C  
ATOM   5375  C   ALA B 360      10.416  -8.430  14.079  1.00 90.89           C  
ANISOU 5375  C   ALA B 360     7083  20087   7364   -330    -43   -946       C  
ATOM   5376  O   ALA B 360      11.333  -8.594  14.903  1.00 93.51           O  
ANISOU 5376  O   ALA B 360     7507  20276   7748   -350    -15   -983       O  
ATOM   5377  CB  ALA B 360       8.411  -9.948  14.070  1.00 70.49           C  
ANISOU 5377  CB  ALA B 360     4470  17638   4675   -436      2  -1234       C  
ATOM   5378  N   LEU B 361      10.653  -8.105  12.806  1.00 88.56           N  
ANISOU 5378  N   LEU B 361     6720  19956   6975   -293    -63   -805       N  
ATOM   5379  CA  LEU B 361      12.012  -7.913  12.320  1.00 77.50           C  
ANISOU 5379  CA  LEU B 361     5344  18577   5526   -273    -46   -686       C  
ATOM   5380  C   LEU B 361      12.712  -6.790  13.071  1.00 75.47           C  
ANISOU 5380  C   LEU B 361     5109  18130   5435   -206    -82   -558       C  
ATOM   5381  O   LEU B 361      13.888  -6.915  13.426  1.00 82.37           O  
ANISOU 5381  O   LEU B 361     6055  18919   6323   -215    -54   -547       O  
ATOM   5382  CB  LEU B 361      11.997  -7.635  10.817  1.00 80.54           C  
ANISOU 5382  CB  LEU B 361     5638  19166   5798   -242    -66   -548       C  
ATOM   5383  CG  LEU B 361      11.583  -8.813   9.931  1.00 79.91           C  
ANISOU 5383  CG  LEU B 361     5520  19270   5570   -312     -6   -657       C  
ATOM   5384  CD1 LEU B 361      11.657  -8.429   8.463  1.00 88.44           C  
ANISOU 5384  CD1 LEU B 361     6510  20527   6565   -279    -37   -505       C  
ATOM   5385  CD2 LEU B 361      12.425 -10.049  10.216  1.00 71.59           C  
ANISOU 5385  CD2 LEU B 361     4564  18051   4584   -391     40   -785       C  
ATOM   5386  N   LEU B 362      12.011  -5.680  13.311  1.00 70.78           N  
ANISOU 5386  N   LEU B 362     4450  17463   4980   -136   -141   -458       N  
ATOM   5387  CA  LEU B 362      12.598  -4.591  14.087  1.00 72.81           C  
ANISOU 5387  CA  LEU B 362     4721  17524   5418    -71   -161   -339       C  
ATOM   5388  C   LEU B 362      12.891  -5.032  15.515  1.00 71.92           C  
ANISOU 5388  C   LEU B 362     4704  17207   5414   -115   -117   -479       C  
ATOM   5389  O   LEU B 362      13.952  -4.714  16.070  1.00 85.94           O  
ANISOU 5389  O   LEU B 362     6535  18841   7276    -97   -100   -425       O  
ATOM   5390  CB  LEU B 362      11.670  -3.376  14.086  1.00 72.85           C  
ANISOU 5390  CB  LEU B 362     4634  17490   5553      8   -227   -222       C  
ATOM   5391  CG  LEU B 362      11.480  -2.616  12.774  1.00 72.49           C  
ANISOU 5391  CG  LEU B 362     4497  17604   5443     70   -286    -44       C  
ATOM   5392  CD1 LEU B 362      10.602  -1.405  13.006  1.00 73.12           C  
ANISOU 5392  CD1 LEU B 362     4500  17602   5681    147   -352     56       C  
ATOM   5393  CD2 LEU B 362      12.817  -2.200  12.190  1.00 79.12           C  
ANISOU 5393  CD2 LEU B 362     5355  18468   6241    102   -276    113       C  
ATOM   5394  N   ASN B 363      11.958  -5.768  16.127  1.00 71.23           N  
ANISOU 5394  N   ASN B 363     4637  17099   5327   -175    -99   -661       N  
ATOM   5395  CA  ASN B 363      12.159  -6.225  17.498  1.00 68.41           C  
ANISOU 5395  CA  ASN B 363     4374  16548   5070   -224    -58   -805       C  
ATOM   5396  C   ASN B 363      13.371  -7.142  17.617  1.00 72.02           C  
ANISOU 5396  C   ASN B 363     4936  16987   5442   -283    -14   -880       C  
ATOM   5397  O   ASN B 363      13.960  -7.251  18.698  1.00 78.51           O  
ANISOU 5397  O   ASN B 363     5841  17620   6370   -305     11   -941       O  
ATOM   5398  CB  ASN B 363      10.902  -6.937  18.003  1.00 67.98           C  
ANISOU 5398  CB  ASN B 363     4321  16501   5007   -286    -44   -993       C  
ATOM   5399  CG  ASN B 363       9.696  -6.015  18.072  1.00 70.24           C  
ANISOU 5399  CG  ASN B 363     4505  16773   5409   -229    -89   -934       C  
ATOM   5400  OD1 ASN B 363       9.829  -4.811  18.291  1.00 68.67           O  
ANISOU 5400  OD1 ASN B 363     4263  16473   5356   -149   -122   -783       O  
ATOM   5401  ND2 ASN B 363       8.507  -6.582  17.895  1.00 72.56           N  
ANISOU 5401  ND2 ASN B 363     4760  17165   5644   -270    -92  -1055       N  
ATOM   5402  N   VAL B 364      13.755  -7.810  16.532  1.00 72.02           N  
ANISOU 5402  N   VAL B 364     4935  17175   5256   -311     -5   -881       N  
ATOM   5403  CA  VAL B 364      14.973  -8.627  16.563  1.00 81.30           C  
ANISOU 5403  CA  VAL B 364     6204  18334   6352   -362     24   -941       C  
ATOM   5404  C   VAL B 364      16.218  -7.808  16.209  1.00 79.69           C  
ANISOU 5404  C   VAL B 364     5989  18093   6196   -298     13   -753       C  
ATOM   5405  O   VAL B 364      17.285  -7.971  16.817  1.00 72.21           O  
ANISOU 5405  O   VAL B 364     5121  17003   5314   -312     26   -771       O  
ATOM   5406  CB  VAL B 364      14.812  -9.842  15.628  1.00 69.30           C  
ANISOU 5406  CB  VAL B 364     4694  16903   4734   -429     39  -1030       C  
ATOM   5407  CG1 VAL B 364      16.095 -10.650  15.583  1.00 66.20           C  
ANISOU 5407  CG1 VAL B 364     4392  16359   4401   -474     37  -1061       C  
ATOM   5408  CG2 VAL B 364      13.658 -10.710  16.088  1.00 65.10           C  
ANISOU 5408  CG2 VAL B 364     4184  16316   4235   -496     54  -1210       C  
ATOM   5409  N   PHE B 365      16.105  -6.908  15.231  1.00 83.48           N  
ANISOU 5409  N   PHE B 365     6373  18692   6653   -227    -15   -571       N  
ATOM   5410  CA  PHE B 365      17.277  -6.196  14.740  1.00 92.61           C  
ANISOU 5410  CA  PHE B 365     7516  19842   7828   -171    -21   -393       C  
ATOM   5411  C   PHE B 365      17.764  -5.165  15.747  1.00 94.03           C  
ANISOU 5411  C   PHE B 365     7714  19784   8227   -111    -28   -298       C  
ATOM   5412  O   PHE B 365      18.960  -4.843  15.778  1.00102.23           O  
ANISOU 5412  O   PHE B 365     8783  20747   9313    -86    -16   -206       O  
ATOM   5413  CB  PHE B 365      16.961  -5.541  13.394  1.00 99.18           C  
ANISOU 5413  CB  PHE B 365     8242  20872   8569   -118    -52   -229       C  
ATOM   5414  CG  PHE B 365      16.608  -6.524  12.306  1.00 96.25           C  
ANISOU 5414  CG  PHE B 365     7846  20741   7984   -175    -27   -306       C  
ATOM   5415  CD1 PHE B 365      16.915  -7.870  12.436  1.00 97.18           C  
ANISOU 5415  CD1 PHE B 365     8042  20839   8042   -262     13   -481       C  
ATOM   5416  CD2 PHE B 365      15.969  -6.101  11.154  1.00 93.52           C  
ANISOU 5416  CD2 PHE B 365     7399  20575   7560   -142    -53   -199       C  
ATOM   5417  CE1 PHE B 365      16.590  -8.773  11.441  1.00 93.27           C  
ANISOU 5417  CE1 PHE B 365     7519  20421   7497   -312     29   -540       C  
ATOM   5418  CE2 PHE B 365      15.645  -7.001  10.155  1.00 96.18           C  
ANISOU 5418  CE2 PHE B 365     7698  21119   7729   -195    -11   -267       C  
ATOM   5419  CZ  PHE B 365      15.955  -8.338  10.300  1.00 94.21           C  
ANISOU 5419  CZ  PHE B 365     7522  20763   7510   -279     23   -436       C  
ATOM   5420  N   VAL B 366      16.866  -4.649  16.588  1.00 83.12           N  
ANISOU 5420  N   VAL B 366     6316  18281   6986    -89    -44   -320       N  
ATOM   5421  CA  VAL B 366      17.304  -3.764  17.663  1.00 82.58           C  
ANISOU 5421  CA  VAL B 366     6273  17977   7127    -40    -42   -251       C  
ATOM   5422  C   VAL B 366      18.250  -4.502  18.607  1.00 93.84           C  
ANISOU 5422  C   VAL B 366     7812  19245   8599    -96      6   -372       C  
ATOM   5423  O   VAL B 366      19.266  -3.951  19.057  1.00 98.30           O  
ANISOU 5423  O   VAL B 366     8408  19661   9280    -60     19   -282       O  
ATOM   5424  CB  VAL B 366      16.083  -3.184  18.397  1.00 72.71           C  
ANISOU 5424  CB  VAL B 366     4983  16635   6010    -16    -64   -276       C  
ATOM   5425  CG1 VAL B 366      16.513  -2.420  19.620  1.00 72.07           C  
ANISOU 5425  CG1 VAL B 366     4939  16305   6140     21    -52   -233       C  
ATOM   5426  CG2 VAL B 366      15.324  -2.264  17.468  1.00 78.74           C  
ANISOU 5426  CG2 VAL B 366     5634  17526   6757     54   -121   -126       C  
ATOM   5427  N   TRP B 367      17.958  -5.771  18.896  1.00 86.23           N  
ANISOU 5427  N   TRP B 367     6911  18309   7543   -186     31   -576       N  
ATOM   5428  CA  TRP B 367      18.860  -6.534  19.753  1.00 86.36           C  
ANISOU 5428  CA  TRP B 367     7039  18174   7597   -244     68   -697       C  
ATOM   5429  C   TRP B 367      20.124  -6.949  19.012  1.00 79.46           C  
ANISOU 5429  C   TRP B 367     6195  17366   6629   -254     75   -654       C  
ATOM   5430  O   TRP B 367      21.186  -7.096  19.630  1.00 77.90           O  
ANISOU 5430  O   TRP B 367     6071  17012   6515   -265    101   -671       O  
ATOM   5431  CB  TRP B 367      18.136  -7.746  20.328  1.00 87.64           C  
ANISOU 5431  CB  TRP B 367     7266  18333   7699   -340     82   -931       C  
ATOM   5432  CG  TRP B 367      17.201  -7.341  21.408  1.00 88.46           C  
ANISOU 5432  CG  TRP B 367     7367  18300   7943   -336     91   -987       C  
ATOM   5433  CD1 TRP B 367      15.846  -7.222  21.319  1.00 87.81           C  
ANISOU 5433  CD1 TRP B 367     7220  18296   7846   -336     76  -1026       C  
ATOM   5434  CD2 TRP B 367      17.556  -6.942  22.734  1.00 86.59           C  
ANISOU 5434  CD2 TRP B 367     7187  17821   7891   -329    118  -1004       C  
ATOM   5435  NE1 TRP B 367      15.331  -6.796  22.517  1.00 86.76           N  
ANISOU 5435  NE1 TRP B 367     7102  17983   7878   -332     91  -1071       N  
ATOM   5436  CE2 TRP B 367      16.361  -6.617  23.404  1.00 92.78           C  
ANISOU 5436  CE2 TRP B 367     7940  18551   8762   -329    119  -1059       C  
ATOM   5437  CE3 TRP B 367      18.767  -6.841  23.425  1.00 88.47           C  
ANISOU 5437  CE3 TRP B 367     7499  17883   8231   -325    145   -983       C  
ATOM   5438  CZ2 TRP B 367      16.340  -6.197  24.735  1.00 98.86           C  
ANISOU 5438  CZ2 TRP B 367     8751  19101   9709   -327    146  -1092       C  
ATOM   5439  CZ3 TRP B 367      18.747  -6.421  24.745  1.00 95.42           C  
ANISOU 5439  CZ3 TRP B 367     8422  18547   9287   -322    170  -1014       C  
ATOM   5440  CH2 TRP B 367      17.542  -6.103  25.386  1.00100.88           C  
ANISOU 5440  CH2 TRP B 367     9082  19194  10055   -324    171  -1068       C  
ATOM   5441  N   ILE B 368      20.042  -7.123  17.693  1.00 75.84           N  
ANISOU 5441  N   ILE B 368     5678  17135   6004   -251     54   -597       N  
ATOM   5442  CA  ILE B 368      21.273  -7.273  16.918  1.00 66.22           C  
ANISOU 5442  CA  ILE B 368     4469  15977   4716   -246     57   -520       C  
ATOM   5443  C   ILE B 368      22.172  -6.055  17.126  1.00 63.70           C  
ANISOU 5443  C   ILE B 368     4131  15524   4548   -163     69   -330       C  
ATOM   5444  O   ILE B 368      23.382  -6.180  17.367  1.00 65.78           O  
ANISOU 5444  O   ILE B 368     4450  15677   4866   -166     94   -317       O  
ATOM   5445  CB  ILE B 368      20.950  -7.495  15.427  1.00 69.54           C  
ANISOU 5445  CB  ILE B 368     4813  16674   4933   -249     30   -469       C  
ATOM   5446  CG1 ILE B 368      20.028  -8.707  15.238  1.00 63.14           C  
ANISOU 5446  CG1 ILE B 368     4018  15938   4032   -331     15   -654       C  
ATOM   5447  CG2 ILE B 368      22.232  -7.680  14.624  1.00 69.11           C  
ANISOU 5447  CG2 ILE B 368     4763  16678   4819   -249     24   -396       C  
ATOM   5448  CD1 ILE B 368      20.617 -10.027  15.706  1.00 62.02           C  
ANISOU 5448  CD1 ILE B 368     3963  15614   3988   -419     15   -825       C  
ATOM   5449  N   GLY B 369      21.586  -4.856  17.070  1.00 64.71           N  
ANISOU 5449  N   GLY B 369     4181  15647   4759    -87     45   -184       N  
ATOM   5450  CA  GLY B 369      22.352  -3.643  17.313  1.00 67.08           C  
ANISOU 5450  CA  GLY B 369     4463  15812   5214     -8     44     -2       C  
ATOM   5451  C   GLY B 369      22.887  -3.529  18.731  1.00 69.04           C  
ANISOU 5451  C   GLY B 369     4789  15794   5649    -11     71    -55       C  
ATOM   5452  O   GLY B 369      23.977  -2.992  18.952  1.00 69.40           O  
ANISOU 5452  O   GLY B 369     4853  15717   5796     27     86     48       O  
ATOM   5453  N   TYR B 370      22.134  -4.014  19.713  1.00 69.23           N  
ANISOU 5453  N   TYR B 370     4857  15724   5722    -56     79   -214       N  
ATOM   5454  CA  TYR B 370      22.653  -4.002  21.079  1.00 75.63           C  
ANISOU 5454  CA  TYR B 370     5748  16290   6699    -69    109   -278       C  
ATOM   5455  C   TYR B 370      23.832  -4.961  21.228  1.00 77.78           C  
ANISOU 5455  C   TYR B 370     6110  16507   6934   -125    147   -373       C  
ATOM   5456  O   TYR B 370      24.811  -4.664  21.932  1.00 83.26           O  
ANISOU 5456  O   TYR B 370     6853  17022   7762   -107    170   -338       O  
ATOM   5457  CB  TYR B 370      21.533  -4.339  22.063  1.00 79.31           C  
ANISOU 5457  CB  TYR B 370     6240  16681   7214   -112    113   -433       C  
ATOM   5458  CG  TYR B 370      20.426  -3.305  22.092  1.00 74.84           C  
ANISOU 5458  CG  TYR B 370     5588  16125   6724    -51     78   -339       C  
ATOM   5459  CD1 TYR B 370      20.629  -2.025  21.582  1.00 74.19           C  
ANISOU 5459  CD1 TYR B 370     5430  16050   6708     42     44   -123       C  
ATOM   5460  CD2 TYR B 370      19.182  -3.605  22.626  1.00 74.58           C  
ANISOU 5460  CD2 TYR B 370     5549  16089   6698    -87     77   -469       C  
ATOM   5461  CE1 TYR B 370      19.625  -1.078  21.603  1.00 76.53           C  
ANISOU 5461  CE1 TYR B 370     5651  16348   7080     99      6    -40       C  
ATOM   5462  CE2 TYR B 370      18.169  -2.663  22.657  1.00 78.06           C  
ANISOU 5462  CE2 TYR B 370     5908  16532   7218    -31     43   -388       C  
ATOM   5463  CZ  TYR B 370      18.396  -1.399  22.145  1.00 78.34           C  
ANISOU 5463  CZ  TYR B 370     5871  16571   7322     63      6   -174       C  
ATOM   5464  OH  TYR B 370      17.387  -0.459  22.167  1.00 71.34           O  
ANISOU 5464  OH  TYR B 370     4906  15681   6519    120    -32    -95       O  
ATOM   5465  N   LEU B 371      23.773  -6.109  20.552  1.00 76.57           N  
ANISOU 5465  N   LEU B 371     5981  16504   6607   -192    150   -492       N  
ATOM   5466  CA  LEU B 371      24.938  -6.987  20.527  1.00 73.86           C  
ANISOU 5466  CA  LEU B 371     5718  16115   6230   -240    176   -568       C  
ATOM   5467  C   LEU B 371      26.129  -6.283  19.885  1.00 73.16           C  
ANISOU 5467  C   LEU B 371     5597  16029   6173   -179    186   -387       C  
ATOM   5468  O   LEU B 371      27.273  -6.445  20.331  1.00 68.64           O  
ANISOU 5468  O   LEU B 371     5087  15313   5681   -185    217   -397       O  
ATOM   5469  CB  LEU B 371      24.609  -8.282  19.787  1.00 73.70           C  
ANISOU 5469  CB  LEU B 371     5716  16260   6025   -320    156   -712       C  
ATOM   5470  CG  LEU B 371      25.652  -9.385  19.958  1.00 70.48           C  
ANISOU 5470  CG  LEU B 371     5403  15759   5616   -385    170   -833       C  
ATOM   5471  CD1 LEU B 371      25.813  -9.712  21.438  1.00 63.02           C  
ANISOU 5471  CD1 LEU B 371     4561  14580   4805   -423    200   -963       C  
ATOM   5472  CD2 LEU B 371      25.281 -10.625  19.158  1.00 71.58           C  
ANISOU 5472  CD2 LEU B 371     5529  16036   5632   -463    126   -958       C  
ATOM   5473  N   SER B 372      25.874  -5.482  18.845  1.00 71.66           N  
ANISOU 5473  N   SER B 372     5308  15996   5922   -120    160   -221       N  
ATOM   5474  CA  SER B 372      26.932  -4.640  18.287  1.00 64.89           C  
ANISOU 5474  CA  SER B 372     4413  15130   5110    -56    169    -32       C  
ATOM   5475  C   SER B 372      27.501  -3.701  19.341  1.00 57.79           C  
ANISOU 5475  C   SER B 372     3533  13994   4429     -2    179     55       C  
ATOM   5476  O   SER B 372      28.718  -3.502  19.419  1.00 68.68           O  
ANISOU 5476  O   SER B 372     4938  15273   5884     17    205    119       O  
ATOM   5477  CB  SER B 372      26.404  -3.825  17.113  1.00 72.56           C  
ANISOU 5477  CB  SER B 372     5275  16300   5994      0    134    135       C  
ATOM   5478  OG  SER B 372      25.907  -2.580  17.570  1.00 75.39           O  
ANISOU 5478  OG  SER B 372     5586  16568   6492     72    107    263       O  
ATOM   5479  N   SER B 373      26.629  -3.090  20.140  1.00 68.40           N  
ANISOU 5479  N   SER B 373     4862  15245   5881     24    157     60       N  
ATOM   5480  CA  SER B 373      27.091  -2.274  21.261  1.00 81.76           C  
ANISOU 5480  CA  SER B 373     6581  16701   7785     68    162    122       C  
ATOM   5481  C   SER B 373      28.003  -3.069  22.189  1.00 74.00           C  
ANISOU 5481  C   SER B 373     5698  15549   6868     14    203    -13       C  
ATOM   5482  O   SER B 373      28.876  -2.496  22.852  1.00 73.06           O  
ANISOU 5482  O   SER B 373     5602  15253   6906     50    213     58       O  
ATOM   5483  CB  SER B 373      25.897  -1.718  22.041  1.00 90.29           C  
ANISOU 5483  CB  SER B 373     7639  17710   8957     87    135    106       C  
ATOM   5484  OG  SER B 373      26.322  -1.033  23.207  1.00 82.74           O  
ANISOU 5484  OG  SER B 373     6716  16521   8202    121    140    146       O  
ATOM   5485  N   ALA B 374      27.801  -4.382  22.264  1.00 70.43           N  
ANISOU 5485  N   ALA B 374     5309  15147   6304    -71    223   -209       N  
ATOM   5486  CA  ALA B 374      28.626  -5.224  23.127  1.00 53.67           C  
ANISOU 5486  CA  ALA B 374     3289  12869   4234   -127    261   -352       C  
ATOM   5487  C   ALA B 374      29.930  -5.714  22.492  1.00 54.76           C  
ANISOU 5487  C   ALA B 374     3455  13029   4324   -139    287   -337       C  
ATOM   5488  O   ALA B 374      30.858  -6.063  23.229  1.00 57.22           O  
ANISOU 5488  O   ALA B 374     3837  13178   4725   -161    316   -402       O  
ATOM   5489  CB  ALA B 374      27.830  -6.445  23.591  1.00 68.84           C  
ANISOU 5489  CB  ALA B 374     5280  14810   6066   -218    269   -580       C  
ATOM   5490  N   VAL B 375      30.028  -5.773  21.159  1.00 61.67           N  
ANISOU 5490  N   VAL B 375     4277  14097   5060   -129    280   -262       N  
ATOM   5491  CA  VAL B 375      31.119  -6.548  20.545  1.00 63.14           C  
ANISOU 5491  CA  VAL B 375     4503  14314   5174   -162    308   -299       C  
ATOM   5492  C   VAL B 375      32.506  -5.926  20.740  1.00 68.31           C  
ANISOU 5492  C   VAL B 375     5160  14827   5968   -114    337   -182       C  
ATOM   5493  O   VAL B 375      33.511  -6.647  20.703  1.00 73.82           O  
ANISOU 5493  O   VAL B 375     5916  15471   6661   -149    369   -253       O  
ATOM   5494  CB  VAL B 375      30.875  -6.781  19.040  1.00 56.05           C  
ANISOU 5494  CB  VAL B 375     3544  13661   4090   -166    292   -250       C  
ATOM   5495  CG1 VAL B 375      29.610  -7.584  18.805  1.00 56.42           C  
ANISOU 5495  CG1 VAL B 375     3592  13848   3997   -224    257   -386       C  
ATOM   5496  CG2 VAL B 375      30.874  -5.463  18.274  1.00 57.11           C  
ANISOU 5496  CG2 VAL B 375     3573  13887   4238    -82    278    -20       C  
ATOM   5497  N   ASN B 376      32.606  -4.606  20.910  1.00 60.82           N  
ANISOU 5497  N   ASN B 376     4149  13813   5147    -36    323     -2       N  
ATOM   5498  CA  ASN B 376      33.910  -3.947  20.780  1.00 54.45           C  
ANISOU 5498  CA  ASN B 376     3326  12913   4451     13    344    138       C  
ATOM   5499  C   ASN B 376      34.990  -4.464  21.728  1.00 53.22           C  
ANISOU 5499  C   ASN B 376     3250  12555   4416    -15    376     39       C  
ATOM   5500  O   ASN B 376      36.130  -4.665  21.268  1.00 58.94           O  
ANISOU 5500  O   ASN B 376     3981  13268   5144    -16    409     68       O  
ATOM   5501  CB  ASN B 376      33.743  -2.431  20.931  1.00 56.26           C  
ANISOU 5501  CB  ASN B 376     3485  13083   4810    101    313    340       C  
ATOM   5502  CG  ASN B 376      33.122  -1.791  19.713  1.00 63.94           C  
ANISOU 5502  CG  ASN B 376     4367  14262   5665    141    288    483       C  
ATOM   5503  OD1 ASN B 376      33.224  -2.315  18.604  1.00 63.13           O  
ANISOU 5503  OD1 ASN B 376     4245  14342   5402    115    303    476       O  
ATOM   5504  ND2 ASN B 376      32.474  -0.650  19.909  1.00 78.87           N  
ANISOU 5504  ND2 ASN B 376     6206  16126   7637    204    249    614       N  
ATOM   5505  N   PRO B 377      34.739  -4.675  23.028  1.00 52.11           N  
ANISOU 5505  N   PRO B 377     3167  12252   4379    -39    370    -74       N  
ATOM   5506  CA  PRO B 377      35.817  -5.191  23.888  1.00 51.00           C  
ANISOU 5506  CA  PRO B 377     3099  11930   4349    -68    397   -169       C  
ATOM   5507  C   PRO B 377      36.384  -6.524  23.432  1.00 54.72           C  
ANISOU 5507  C   PRO B 377     3633  12459   4699   -137    433   -319       C  
ATOM   5508  O   PRO B 377      37.589  -6.758  23.589  1.00 51.92           O  
ANISOU 5508  O   PRO B 377     3305  12002   4419   -139    460   -332       O  
ATOM   5509  CB  PRO B 377      35.142  -5.305  25.261  1.00 49.99           C  
ANISOU 5509  CB  PRO B 377     3046  11638   4311    -94    376   -286       C  
ATOM   5510  CG  PRO B 377      34.072  -4.295  25.218  1.00 50.55           C  
ANISOU 5510  CG  PRO B 377     3028  11779   4400    -44    345   -169       C  
ATOM   5511  CD  PRO B 377      33.548  -4.321  23.820  1.00 55.73           C  
ANISOU 5511  CD  PRO B 377     3624  12670   4882    -36    339   -105       C  
ATOM   5512  N   LEU B 378      35.560  -7.404  22.861  1.00 51.36           N  
ANISOU 5512  N   LEU B 378     3231  12189   4094   -192    429   -433       N  
ATOM   5513  CA  LEU B 378      36.086  -8.665  22.351  1.00 51.37           C  
ANISOU 5513  CA  LEU B 378     3297  12241   3979   -255    452   -569       C  
ATOM   5514  C   LEU B 378      37.094  -8.425  21.236  1.00 58.17           C  
ANISOU 5514  C   LEU B 378     4110  13176   4814   -223    476   -444       C  
ATOM   5515  O   LEU B 378      38.139  -9.085  21.178  1.00 65.42           O  
ANISOU 5515  O   LEU B 378     5077  14033   5749   -249    507   -511       O  
ATOM   5516  CB  LEU B 378      34.940  -9.549  21.865  1.00 51.81           C  
ANISOU 5516  CB  LEU B 378     3377  12449   3859   -316    424   -692       C  
ATOM   5517  CG  LEU B 378      35.304 -10.974  21.450  1.00 54.97           C  
ANISOU 5517  CG  LEU B 378     3856  12873   4156   -391    426   -853       C  
ATOM   5518  CD1 LEU B 378      35.929 -11.729  22.614  1.00 51.99           C  
ANISOU 5518  CD1 LEU B 378     3592  12294   3870   -438    445  -1013       C  
ATOM   5519  CD2 LEU B 378      34.071 -11.700  20.931  1.00 52.28           C  
ANISOU 5519  CD2 LEU B 378     3513  12674   3677   -445    379   -947       C  
ATOM   5520  N   VAL B 379      36.806  -7.467  20.352  1.00 71.30           N  
ANISOU 5520  N   VAL B 379     5679  14970   6443   -166    463   -264       N  
ATOM   5521  CA  VAL B 379      37.747  -7.128  19.289  1.00 62.67           C  
ANISOU 5521  CA  VAL B 379     4538  13947   5328   -134    491   -134       C  
ATOM   5522  C   VAL B 379      39.027  -6.551  19.875  1.00 59.70           C  
ANISOU 5522  C   VAL B 379     4159  13384   5141    -93    520    -56       C  
ATOM   5523  O   VAL B 379      40.135  -6.902  19.451  1.00 57.63           O  
ANISOU 5523  O   VAL B 379     3909  13099   4888   -102    559    -60       O  
ATOM   5524  CB  VAL B 379      37.095  -6.156  18.290  1.00 55.68           C  
ANISOU 5524  CB  VAL B 379     3553  13237   4365    -81    468     46       C  
ATOM   5525  CG1 VAL B 379      38.098  -5.724  17.240  1.00 56.27           C  
ANISOU 5525  CG1 VAL B 379     3580  13375   4426    -49    502    187       C  
ATOM   5526  CG2 VAL B 379      35.876  -6.803  17.647  1.00 56.03           C  
ANISOU 5526  CG2 VAL B 379     3592  13476   4222   -124    434    -38       C  
ATOM   5527  N   TYR B 380      38.897  -5.661  20.864  1.00 62.17           N  
ANISOU 5527  N   TYR B 380     4455  13552   5616    -49    497     15       N  
ATOM   5528  CA  TYR B 380      40.090  -5.120  21.509  1.00 52.27           C  
ANISOU 5528  CA  TYR B 380     3197  12105   4557    -11    511     84       C  
ATOM   5529  C   TYR B 380      40.941  -6.237  22.098  1.00 63.18           C  
ANISOU 5529  C   TYR B 380     4659  13371   5975    -68    540    -94       C  
ATOM   5530  O   TYR B 380      42.174  -6.187  22.040  1.00 68.86           O  
ANISOU 5530  O   TYR B 380     5376  13997   6789    -53    567    -58       O  
ATOM   5531  CB  TYR B 380      39.708  -4.115  22.595  1.00 51.64           C  
ANISOU 5531  CB  TYR B 380     3101  11875   4644     38    469    162       C  
ATOM   5532  CG  TYR B 380      38.987  -2.887  22.088  1.00 52.51           C  
ANISOU 5532  CG  TYR B 380     3133  12071   4748    103    438    351       C  
ATOM   5533  CD1 TYR B 380      38.955  -2.583  20.734  1.00 56.84           C  
ANISOU 5533  CD1 TYR B 380     3620  12806   5171    124    450    469       C  
ATOM   5534  CD2 TYR B 380      38.336  -2.032  22.966  1.00 54.40           C  
ANISOU 5534  CD2 TYR B 380     3362  12202   5106    144    394    411       C  
ATOM   5535  CE1 TYR B 380      38.293  -1.465  20.268  1.00 57.88           C  
ANISOU 5535  CE1 TYR B 380     3680  13019   5294    184    418    639       C  
ATOM   5536  CE2 TYR B 380      37.674  -0.911  22.510  1.00 60.90           C  
ANISOU 5536  CE2 TYR B 380     4116  13096   5926    205    363    581       C  
ATOM   5537  CZ  TYR B 380      37.656  -0.632  21.160  1.00 65.45           C  
ANISOU 5537  CZ  TYR B 380     4630  13862   6375    225    373    694       C  
ATOM   5538  OH  TYR B 380      36.998   0.484  20.700  1.00 72.97           O  
ANISOU 5538  OH  TYR B 380     5513  14888   7322    286    338    862       O  
ATOM   5539  N   THR B 381      40.295  -7.260  22.661  1.00 65.92           N  
ANISOU 5539  N   THR B 381     5082  13715   6250   -134    533   -289       N  
ATOM   5540  CA  THR B 381      41.039  -8.389  23.212  1.00 60.39           C  
ANISOU 5540  CA  THR B 381     4491  12882   5574   -191    547   -469       C  
ATOM   5541  C   THR B 381      41.739  -9.184  22.117  1.00 59.15           C  
ANISOU 5541  C   THR B 381     4322  12856   5297   -221    595   -509       C  
ATOM   5542  O   THR B 381      42.911  -9.549  22.262  1.00 57.04           O  
ANISOU 5542  O   THR B 381     4075  12487   5110   -228    624   -551       O  
ATOM   5543  CB  THR B 381      40.109  -9.304  24.011  1.00 58.15           C  
ANISOU 5543  CB  THR B 381     4306  12563   5225   -259    525   -667       C  
ATOM   5544  OG1 THR B 381      39.462  -8.552  25.044  1.00 58.06           O  
ANISOU 5544  OG1 THR B 381     4330  12397   5334   -232    476   -630       O  
ATOM   5545  CG2 THR B 381      40.896 -10.443  24.636  1.00 55.43           C  
ANISOU 5545  CG2 THR B 381     4090  12057   4915   -316    529   -851       C  
ATOM   5546  N   LEU B 382      41.039  -9.453  21.012  1.00 58.59           N  
ANISOU 5546  N   LEU B 382     4236  12980   5046   -238    589   -496       N  
ATOM   5547  CA  LEU B 382      41.581 -10.344  19.988  1.00 60.40           C  
ANISOU 5547  CA  LEU B 382     4487  13304   5156   -275    616   -555       C  
ATOM   5548  C   LEU B 382      42.783  -9.744  19.262  1.00 63.60           C  
ANISOU 5548  C   LEU B 382     4831  13709   5627   -229    660   -410       C  
ATOM   5549  O   LEU B 382      43.701 -10.480  18.882  1.00 60.10           O  
ANISOU 5549  O   LEU B 382     4417  13247   5170   -258    696   -480       O  
ATOM   5550  CB  LEU B 382      40.489 -10.711  18.982  1.00 59.26           C  
ANISOU 5550  CB  LEU B 382     4332  13366   4818   -303    586   -567       C  
ATOM   5551  CG  LEU B 382      39.348 -11.572  19.532  1.00 62.22           C  
ANISOU 5551  CG  LEU B 382     4776  13749   5117   -364    541   -738       C  
ATOM   5552  CD1 LEU B 382      38.267 -11.787  18.485  1.00 55.02           C  
ANISOU 5552  CD1 LEU B 382     3824  13041   4040   -383    502   -725       C  
ATOM   5553  CD2 LEU B 382      39.873 -12.905  20.051  1.00 65.25           C  
ANISOU 5553  CD2 LEU B 382     5267  14014   5509   -433    547   -940       C  
ATOM   5554  N   PHE B 383      42.809  -8.428  19.061  1.00 65.03           N  
ANISOU 5554  N   PHE B 383     4927  13902   5881   -160    658   -210       N  
ATOM   5555  CA  PHE B 383      43.803  -7.821  18.186  1.00 65.08           C  
ANISOU 5555  CA  PHE B 383     4870  13935   5921   -121    700    -61       C  
ATOM   5556  C   PHE B 383      44.759  -6.856  18.880  1.00 66.52           C  
ANISOU 5556  C   PHE B 383     5011  13937   6325    -63    710     57       C  
ATOM   5557  O   PHE B 383      45.647  -6.312  18.213  1.00 73.64           O  
ANISOU 5557  O   PHE B 383     5862  14844   7273    -31    748    183       O  
ATOM   5558  CB  PHE B 383      43.101  -7.085  17.036  1.00 64.00           C  
ANISOU 5558  CB  PHE B 383     4663  13995   5660    -89    688     95       C  
ATOM   5559  CG  PHE B 383      42.323  -7.990  16.125  1.00 68.15           C  
ANISOU 5559  CG  PHE B 383     5213  14709   5972   -142    675      1       C  
ATOM   5560  CD1 PHE B 383      42.913  -8.542  15.004  1.00 70.57           C  
ANISOU 5560  CD1 PHE B 383     5521  15112   6179   -169    712    -11       C  
ATOM   5561  CD2 PHE B 383      40.998  -8.292  16.397  1.00 68.28           C  
ANISOU 5561  CD2 PHE B 383     5248  14797   5897   -167    623    -78       C  
ATOM   5562  CE1 PHE B 383      42.198  -9.375  14.168  1.00 64.54           C  
ANISOU 5562  CE1 PHE B 383     4778  14509   5235   -218    689    -95       C  
ATOM   5563  CE2 PHE B 383      40.277  -9.125  15.564  1.00 59.17           C  
ANISOU 5563  CE2 PHE B 383     4109  13808   4564   -216    600   -163       C  
ATOM   5564  CZ  PHE B 383      40.878  -9.668  14.449  1.00 58.26           C  
ANISOU 5564  CZ  PHE B 383     3996  13783   4359   -241    629   -170       C  
ATOM   5565  N   ASN B 384      44.616  -6.622  20.182  1.00 67.23           N  
ANISOU 5565  N   ASN B 384     5124  13864   6558    -52    675     21       N  
ATOM   5566  CA  ASN B 384      45.489  -5.701  20.902  1.00 66.96           C  
ANISOU 5566  CA  ASN B 384     5062  13634   6747      3    665    132       C  
ATOM   5567  C   ASN B 384      46.058  -6.406  22.123  1.00 75.40           C  
ANISOU 5567  C   ASN B 384     6257  14442   7949    -28    634    -28       C  
ATOM   5568  O   ASN B 384      45.300  -6.866  22.982  1.00 76.20           O  
ANISOU 5568  O   ASN B 384     6444  14471   8039    -61    591   -154       O  
ATOM   5569  CB  ASN B 384      44.732  -4.434  21.311  1.00 66.13           C  
ANISOU 5569  CB  ASN B 384     4922  13488   6717     63    613    285       C  
ATOM   5570  CG  ASN B 384      45.657  -3.319  21.747  1.00 69.13           C  
ANISOU 5570  CG  ASN B 384     5290  13665   7313    128    596    441       C  
ATOM   5571  OD1 ASN B 384      46.230  -3.363  22.835  1.00 68.24           O  
ANISOU 5571  OD1 ASN B 384     5263  13296   7368    129    561    386       O  
ATOM   5572  ND2 ASN B 384      45.802  -2.305  20.902  1.00 75.14           N  
ANISOU 5572  ND2 ASN B 384     5948  14535   8068    180    617    638       N  
ATOM   5573  N   LYS B 385      47.390  -6.487  22.202  1.00 76.26           N  
ANISOU 5573  N   LYS B 385     6381  14408   8188    -19    653    -26       N  
ATOM   5574  CA  LYS B 385      48.015  -7.214  23.302  1.00 77.07           C  
ANISOU 5574  CA  LYS B 385     6605  14262   8415    -50    619   -182       C  
ATOM   5575  C   LYS B 385      47.980  -6.434  24.608  1.00 67.27           C  
ANISOU 5575  C   LYS B 385     5434  12756   7370    -13    545   -135       C  
ATOM   5576  O   LYS B 385      47.872  -7.040  25.678  1.00 66.42           O  
ANISOU 5576  O   LYS B 385     5448  12471   7316    -48    498   -281       O  
ATOM   5577  CB  LYS B 385      49.461  -7.573  22.959  1.00 77.52           C  
ANISOU 5577  CB  LYS B 385     6651  14248   8555    -52    661   -200       C  
ATOM   5578  CG  LYS B 385      50.098  -8.531  23.958  1.00 76.70           C  
ANISOU 5578  CG  LYS B 385     6674  13916   8553    -91    624   -386       C  
ATOM   5579  CD  LYS B 385      51.532  -8.859  23.582  1.00 94.02           C  
ANISOU 5579  CD  LYS B 385     8843  16042  10838    -89    665   -402       C  
ATOM   5580  CE  LYS B 385      52.161  -9.815  24.586  1.00100.39           C  
ANISOU 5580  CE  LYS B 385     9778  16614  11750   -126    619   -588       C  
ATOM   5581  NZ  LYS B 385      53.529 -10.242  24.172  1.00102.33           N  
ANISOU 5581  NZ  LYS B 385     9994  16807  12078   -128    661   -622       N  
ATOM   5582  N   THR B 386      48.081  -5.105  24.550  1.00 63.32           N  
ANISOU 5582  N   THR B 386     4863  12220   6974     55    533     66       N  
ATOM   5583  CA  THR B 386      47.983  -4.307  25.768  1.00 56.39           C  
ANISOU 5583  CA  THR B 386     4051  11098   6276     91    463    119       C  
ATOM   5584  C   THR B 386      46.592  -4.422  26.380  1.00 52.68           C  
ANISOU 5584  C   THR B 386     3635  10652   5727     69    425     48       C  
ATOM   5585  O   THR B 386      46.450  -4.655  27.586  1.00 69.62           O  
ANISOU 5585  O   THR B 386     5902  12587   7965     48    374    -52       O  
ATOM   5586  CB  THR B 386      48.326  -2.848  25.473  1.00 50.33           C  
ANISOU 5586  CB  THR B 386     3190  10312   5621    169    463    355       C  
ATOM   5587  OG1 THR B 386      47.265  -2.257  24.717  1.00 66.25           O  
ANISOU 5587  OG1 THR B 386     5113  12559   7500    192    478    466       O  
ATOM   5588  CG2 THR B 386      49.619  -2.758  24.672  1.00 49.47           C  
ANISOU 5588  CG2 THR B 386     3011  10224   5562    186    517    428       C  
ATOM   5589  N   TYR B 387      45.550  -4.253  25.557  1.00 48.49           N  
ANISOU 5589  N   TYR B 387     3018  10376   5028     70    450     99       N  
ATOM   5590  CA  TYR B 387      44.184  -4.460  26.029  1.00 49.26           C  
ANISOU 5590  CA  TYR B 387     3156  10524   5038     43    422     17       C  
ATOM   5591  C   TYR B 387      43.989  -5.872  26.564  1.00 51.81           C  
ANISOU 5591  C   TYR B 387     3596  10804   5287    -38    419   -223       C  
ATOM   5592  O   TYR B 387      43.331  -6.070  27.591  1.00 55.23           O  
ANISOU 5592  O   TYR B 387     4126  11109   5751    -65    380   -321       O  
ATOM   5593  CB  TYR B 387      43.178  -4.188  24.906  1.00 50.83           C  
ANISOU 5593  CB  TYR B 387     3234  11024   5055     53    449     98       C  
ATOM   5594  CG  TYR B 387      42.742  -2.745  24.755  1.00 54.13           C  
ANISOU 5594  CG  TYR B 387     3564  11468   5536    129    427    309       C  
ATOM   5595  CD1 TYR B 387      41.804  -2.188  25.620  1.00 49.27           C  
ANISOU 5595  CD1 TYR B 387     2979  10762   4981    147    379    323       C  
ATOM   5596  CD2 TYR B 387      43.243  -1.949  23.733  1.00 56.67           C  
ANISOU 5596  CD2 TYR B 387     3773  11907   5850    180    455    492       C  
ATOM   5597  CE1 TYR B 387      41.392  -0.870  25.481  1.00 50.54           C  
ANISOU 5597  CE1 TYR B 387     3059  10946   5200    217    356    514       C  
ATOM   5598  CE2 TYR B 387      42.834  -0.632  23.583  1.00 63.68           C  
ANISOU 5598  CE2 TYR B 387     4585  12819   6791    249    431    686       C  
ATOM   5599  CZ  TYR B 387      41.908  -0.098  24.458  1.00 58.18           C  
ANISOU 5599  CZ  TYR B 387     3917  12030   6158    269    380    696       C  
ATOM   5600  OH  TYR B 387      41.505   1.211  24.308  1.00 55.54           O  
ANISOU 5600  OH  TYR B 387     3505  11717   5880    340    354    887       O  
ATOM   5601  N   ARG B 388      44.550  -6.870  25.877  1.00 51.24           N  
ANISOU 5601  N   ARG B 388     3519  10836   5115    -81    463   -321       N  
ATOM   5602  CA  ARG B 388      44.348  -8.255  26.290  1.00 50.12           C  
ANISOU 5602  CA  ARG B 388     3485  10672   4886   -160    462   -551       C  
ATOM   5603  C   ARG B 388      44.997  -8.517  27.644  1.00 50.03           C  
ANISOU 5603  C   ARG B 388     3619  10341   5048   -175    411   -649       C  
ATOM   5604  O   ARG B 388      44.383  -9.122  28.531  1.00 50.28           O  
ANISOU 5604  O   ARG B 388     3766  10276   5061   -224    380   -797       O  
ATOM   5605  CB  ARG B 388      44.900  -9.208  25.227  1.00 47.72           C  
ANISOU 5605  CB  ARG B 388     3141  10542   4447   -197    522   -624       C  
ATOM   5606  CG  ARG B 388      44.575 -10.675  25.484  1.00 47.23           C  
ANISOU 5606  CG  ARG B 388     3179  10501   4263   -281    526   -859       C  
ATOM   5607  CD  ARG B 388      44.804 -11.544  24.252  1.00 50.78           C  
ANISOU 5607  CD  ARG B 388     3569  11185   4537   -317    591   -918       C  
ATOM   5608  NE  ARG B 388      46.179 -11.462  23.768  1.00 58.18           N  
ANISOU 5608  NE  ARG B 388     4467  12076   5562   -291    624   -859       N  
ATOM   5609  CZ  ARG B 388      46.551 -10.817  22.667  1.00 65.07           C  
ANISOU 5609  CZ  ARG B 388     5215  13103   6405   -249    673   -701       C  
ATOM   5610  NH1 ARG B 388      47.831 -10.798  22.311  1.00 60.90           N  
ANISOU 5610  NH1 ARG B 388     4658  12513   5968   -231    708   -664       N  
ATOM   5611  NH2 ARG B 388      45.644 -10.199  21.920  1.00 67.52           N  
ANISOU 5611  NH2 ARG B 388     5430  13628   6596   -228    688   -584       N  
ATOM   5612  N   SER B 389      46.235  -8.053  27.824  1.00 45.82           N  
ANISOU 5612  N   SER B 389     3086   9637   4686   -134    400   -568       N  
ATOM   5613  CA  SER B 389      46.909  -8.207  29.106  1.00 44.78           C  
ANISOU 5613  CA  SER B 389     3090   9190   4732   -141    342   -646       C  
ATOM   5614  C   SER B 389      46.172  -7.458  30.207  1.00 53.26           C  
ANISOU 5614  C   SER B 389     4233  10102   5902   -123    287   -607       C  
ATOM   5615  O   SER B 389      46.008  -7.978  31.320  1.00 65.66           O  
ANISOU 5615  O   SER B 389     5949  11480   7519   -164    242   -745       O  
ATOM   5616  CB  SER B 389      48.352  -7.718  28.997  1.00 44.93           C  
ANISOU 5616  CB  SER B 389     3076   9073   4924    -94    341   -545       C  
ATOM   5617  OG  SER B 389      49.021  -7.826  30.241  1.00 50.92           O  
ANISOU 5617  OG  SER B 389     3966   9518   5862    -99    276   -614       O  
ATOM   5618  N   ALA B 390      45.710  -6.237  29.913  1.00 44.60           N  
ANISOU 5618  N   ALA B 390     3036   9079   4831    -62    289   -421       N  
ATOM   5619  CA  ALA B 390      44.967  -5.469  30.906  1.00 46.60           C  
ANISOU 5619  CA  ALA B 390     3344   9189   5172    -41    242   -377       C  
ATOM   5620  C   ALA B 390      43.701  -6.197  31.335  1.00 56.33           C  
ANISOU 5620  C   ALA B 390     4648  10481   6273   -104    240   -534       C  
ATOM   5621  O   ALA B 390      43.395  -6.273  32.530  1.00 64.96           O  
ANISOU 5621  O   ALA B 390     5872  11368   7444   -128    198   -617       O  
ATOM   5622  CB  ALA B 390      44.627  -4.085  30.352  1.00 47.11           C  
ANISOU 5622  CB  ALA B 390     3274   9360   5265     35    250   -152       C  
ATOM   5623  N   PHE B 391      42.957  -6.751  30.375  1.00 46.96           N  
ANISOU 5623  N   PHE B 391     3383   9572   4886   -135    286   -580       N  
ATOM   5624  CA  PHE B 391      41.728  -7.453  30.719  1.00 44.47           C  
ANISOU 5624  CA  PHE B 391     3127   9328   4442   -197    288   -730       C  
ATOM   5625  C   PHE B 391      42.026  -8.734  31.487  1.00 49.87           C  
ANISOU 5625  C   PHE B 391     3971   9863   5114   -274    274   -952       C  
ATOM   5626  O   PHE B 391      41.346  -9.048  32.471  1.00 61.36           O  
ANISOU 5626  O   PHE B 391     5543  11196   6575   -318    250  -1068       O  
ATOM   5627  CB  PHE B 391      40.920  -7.757  29.456  1.00 46.62           C  
ANISOU 5627  CB  PHE B 391     3274   9936   4503   -211    336   -725       C  
ATOM   5628  CG  PHE B 391      40.443  -6.529  28.723  1.00 56.65           C  
ANISOU 5628  CG  PHE B 391     4395  11362   5768   -139    343   -517       C  
ATOM   5629  CD1 PHE B 391      40.347  -5.306  29.369  1.00 59.88           C  
ANISOU 5629  CD1 PHE B 391     4798  11620   6334    -78    307   -377       C  
ATOM   5630  CD2 PHE B 391      40.088  -6.601  27.384  1.00 51.22           C  
ANISOU 5630  CD2 PHE B 391     3577  10968   4914   -134    383   -461       C  
ATOM   5631  CE1 PHE B 391      39.910  -4.179  28.691  1.00 59.04           C  
ANISOU 5631  CE1 PHE B 391     4556  11653   6222    -11    309   -186       C  
ATOM   5632  CE2 PHE B 391      39.650  -5.478  26.703  1.00 47.91           C  
ANISOU 5632  CE2 PHE B 391     3027  10688   4487    -69    383   -270       C  
ATOM   5633  CZ  PHE B 391      39.560  -4.267  27.358  1.00 51.50           C  
ANISOU 5633  CZ  PHE B 391     3476  10991   5102     -6    345   -133       C  
ATOM   5634  N   SER B 392      43.050  -9.478  31.063  1.00 56.52           N  
ANISOU 5634  N   SER B 392     4825  10707   5943   -293    289  -1013       N  
ATOM   5635  CA  SER B 392      43.409 -10.707  31.762  1.00 67.80           C  
ANISOU 5635  CA  SER B 392     6407  11989   7365   -364    270  -1222       C  
ATOM   5636  C   SER B 392      43.804 -10.426  33.203  1.00 68.90           C  
ANISOU 5636  C   SER B 392     6696  11790   7692   -361    205  -1250       C  
ATOM   5637  O   SER B 392      43.516 -11.229  34.098  1.00 76.10           O  
ANISOU 5637  O   SER B 392     7760  12567   8589   -425    180  -1421       O  
ATOM   5638  CB  SER B 392      44.543 -11.417  31.025  1.00 76.46           C  
ANISOU 5638  CB  SER B 392     7476  13136   8438   -372    296  -1263       C  
ATOM   5639  OG  SER B 392      44.106 -11.871  29.756  1.00 91.66           O  
ANISOU 5639  OG  SER B 392     9290  15370  10168   -390    357  -1271       O  
ATOM   5640  N   ARG B 393      44.457  -9.288  33.450  1.00 72.62           N  
ANISOU 5640  N   ARG B 393     7132  12118   8340   -289    177  -1082       N  
ATOM   5641  CA  ARG B 393      44.829  -8.939  34.818  1.00 63.36           C  
ANISOU 5641  CA  ARG B 393     6103  10620   7351   -284    112  -1096       C  
ATOM   5642  C   ARG B 393      43.659  -8.369  35.612  1.00 55.08           C  
ANISOU 5642  C   ARG B 393     5104   9513   6311   -287     96  -1082       C  
ATOM   5643  O   ARG B 393      43.611  -8.536  36.835  1.00 51.27           O  
ANISOU 5643  O   ARG B 393     4782   8786   5913   -319     50  -1174       O  
ATOM   5644  CB  ARG B 393      46.001  -7.955  34.809  1.00 52.69           C  
ANISOU 5644  CB  ARG B 393     4700   9129   6191   -208     86   -925       C  
ATOM   5645  CG  ARG B 393      47.304  -8.576  34.321  1.00 58.33           C  
ANISOU 5645  CG  ARG B 393     5399   9825   6939   -210     92   -964       C  
ATOM   5646  CD  ARG B 393      48.480  -7.616  34.415  1.00 59.74           C  
ANISOU 5646  CD  ARG B 393     5535   9841   7323   -140     64   -806       C  
ATOM   5647  NE  ARG B 393      48.400  -6.549  33.421  1.00 61.29           N  
ANISOU 5647  NE  ARG B 393     5555  10225   7508    -74    109   -600       N  
ATOM   5648  CZ  ARG B 393      47.944  -5.326  33.669  1.00 70.08           C  
ANISOU 5648  CZ  ARG B 393     6627  11305   8695    -20     94   -441       C  
ATOM   5649  NH1 ARG B 393      47.910  -4.427  32.697  1.00 65.54           N  
ANISOU 5649  NH1 ARG B 393     5895  10909   8100     37    134   -260       N  
ATOM   5650  NH2 ARG B 393      47.525  -4.999  34.887  1.00 78.58           N  
ANISOU 5650  NH2 ARG B 393     7824  12167   9864    -25     39   -465       N  
ATOM   5651  N   TYR B 394      42.710  -7.703  34.951  1.00 45.98           N  
ANISOU 5651  N   TYR B 394     3819   8576   5075   -256    132   -974       N  
ATOM   5652  CA  TYR B 394      41.571  -7.152  35.678  1.00 55.49           C  
ANISOU 5652  CA  TYR B 394     5060   9731   6293   -258    121   -963       C  
ATOM   5653  C   TYR B 394      40.591  -8.245  36.091  1.00 54.92           C  
ANISOU 5653  C   TYR B 394     5089   9697   6081   -348    136  -1172       C  
ATOM   5654  O   TYR B 394      40.017  -8.191  37.187  1.00 39.71           O  
ANISOU 5654  O   TYR B 394     3284   7599   4203   -378    114  -1242       O  
ATOM   5655  CB  TYR B 394      40.860  -6.100  34.826  1.00 58.26           C  
ANISOU 5655  CB  TYR B 394     5234  10299   6602   -195    149   -783       C  
ATOM   5656  CG  TYR B 394      41.689  -4.880  34.499  1.00 55.92           C  
ANISOU 5656  CG  TYR B 394     4843   9957   6448   -106    135   -565       C  
ATOM   5657  CD1 TYR B 394      42.776  -4.517  35.284  1.00 58.72           C  
ANISOU 5657  CD1 TYR B 394     5284  10035   6991    -80     89   -526       C  
ATOM   5658  CD2 TYR B 394      41.379  -4.086  33.403  1.00 62.73           C  
ANISOU 5658  CD2 TYR B 394     5531  11049   7254    -48    164   -397       C  
ATOM   5659  CE1 TYR B 394      43.532  -3.396  34.983  1.00 71.18           C  
ANISOU 5659  CE1 TYR B 394     6775  11571   8701     -1     78   -327       C  
ATOM   5660  CE2 TYR B 394      42.125  -2.968  33.095  1.00 72.00           C  
ANISOU 5660  CE2 TYR B 394     6621  12182   8553     31    153   -197       C  
ATOM   5661  CZ  TYR B 394      43.201  -2.624  33.885  1.00 76.71           C  
ANISOU 5661  CZ  TYR B 394     7302  12505   9338     54    112   -163       C  
ATOM   5662  OH  TYR B 394      43.945  -1.506  33.571  1.00 76.29           O  
ANISOU 5662  OH  TYR B 394     7164  12411   9411    130    104     36       O  
ATOM   5663  N   ILE B 395      40.383  -9.240  35.226  1.00 62.30           N  
ANISOU 5663  N   ILE B 395     5977  10854   6839   -394    176  -1274       N  
ATOM   5664  CA  ILE B 395      39.450 -10.319  35.541  1.00 57.96           C  
ANISOU 5664  CA  ILE B 395     5518  10358   6148   -482    194  -1475       C  
ATOM   5665  C   ILE B 395      39.890 -11.053  36.800  1.00 65.93           C  
ANISOU 5665  C   ILE B 395     6739  11079   7230   -542    153  -1638       C  
ATOM   5666  O   ILE B 395      39.064 -11.429  37.641  1.00 83.39           O  
ANISOU 5666  O   ILE B 395     9068  13205   9410   -601    150  -1764       O  
ATOM   5667  CB  ILE B 395      39.318 -11.276  34.342  1.00 59.69           C  
ANISOU 5667  CB  ILE B 395     5651  10859   6171   -518    241  -1550       C  
ATOM   5668  CG1 ILE B 395      38.618 -10.580  33.173  1.00 57.90           C  
ANISOU 5668  CG1 ILE B 395     5228  10921   5849   -469    278  -1404       C  
ATOM   5669  CG2 ILE B 395      38.565 -12.533  34.738  1.00 68.08           C  
ANISOU 5669  CG2 ILE B 395     6828  11943   7096   -616    255  -1776       C  
ATOM   5670  CD1 ILE B 395      38.593 -11.404  31.900  1.00 52.27           C  
ANISOU 5670  CD1 ILE B 395     4424  10487   4950   -497    322  -1452       C  
ATOM   5671  N   GLN B 396      41.195 -11.256  36.958  1.00 56.98           N  
ANISOU 5671  N   GLN B 396     5663   9787   6201   -528    119  -1639       N  
ATOM   5672  CA  GLN B 396      41.737 -11.944  38.120  1.00 45.13           C  
ANISOU 5672  CA  GLN B 396     4368   8003   4779   -580     69  -1788       C  
ATOM   5673  C   GLN B 396      42.048 -11.006  39.279  1.00 47.84           C  
ANISOU 5673  C   GLN B 396     4807   8049   5321   -544     13  -1706       C  
ATOM   5674  O   GLN B 396      42.582 -11.462  40.295  1.00 54.58           O  
ANISOU 5674  O   GLN B 396     5838   8640   6260   -581    -39  -1813       O  
ATOM   5675  CB  GLN B 396      43.004 -12.707  37.719  1.00 43.96           C  
ANISOU 5675  CB  GLN B 396     4233   7825   4644   -586     55  -1843       C  
ATOM   5676  CG  GLN B 396      42.812 -13.622  36.514  1.00 54.83           C  
ANISOU 5676  CG  GLN B 396     5513   9493   5826   -618    112  -1916       C  
ATOM   5677  CD  GLN B 396      44.097 -14.309  36.094  1.00 66.32           C  
ANISOU 5677  CD  GLN B 396     6974  10918   7308   -618    103  -1963       C  
ATOM   5678  OE1 GLN B 396      45.191 -13.860  36.439  1.00 69.66           O  
ANISOU 5678  OE1 GLN B 396     7419  11147   7903   -574     60  -1891       O  
ATOM   5679  NE2 GLN B 396      43.972 -15.401  35.343  1.00 67.21           N  
ANISOU 5679  NE2 GLN B 396     7063  11221   7251   -669    144  -2085       N  
ATOM   5680  N   CYS B 397      41.718  -9.718  39.155  1.00 50.22           N  
ANISOU 5680  N   CYS B 397     5001   8382   5698   -474     19  -1522       N  
ATOM   5681  CA  CYS B 397      41.945  -8.730  40.213  1.00 41.92           C  
ANISOU 5681  CA  CYS B 397     4032   7063   4835   -435    -31  -1430       C  
ATOM   5682  C   CYS B 397      43.423  -8.646  40.589  1.00 39.14           C  
ANISOU 5682  C   CYS B 397     3746   6478   4648   -406    -90  -1397       C  
ATOM   5683  O   CYS B 397      43.784  -8.586  41.764  1.00 36.36           O  
ANISOU 5683  O   CYS B 397     3558   5835   4421   -422   -148  -1442       O  
ATOM   5684  CB  CYS B 397      41.083  -9.016  41.443  1.00 36.79           C  
ANISOU 5684  CB  CYS B 397     3556   6242   4179   -501    -43  -1565       C  
ATOM   5685  SG  CYS B 397      39.317  -8.989  41.114  1.00 80.44           S  
ANISOU 5685  SG  CYS B 397     9003  12018   9543   -532     25  -1599       S  
ATOM   5686  N   GLN B 398      44.283  -8.655  39.580  1.00 63.00           N  
ANISOU 5686  N   GLN B 398     6641   9628   7670   -366    -76  -1321       N  
ATOM   5687  CA  GLN B 398      45.725  -8.493  39.751  1.00 67.72           C  
ANISOU 5687  CA  GLN B 398     7263  10037   8430   -329   -125  -1270       C  
ATOM   5688  C   GLN B 398      46.073  -7.114  39.207  1.00 67.19           C  
ANISOU 5688  C   GLN B 398     7039  10021   8470   -235   -117  -1033       C  
ATOM   5689  O   GLN B 398      46.189  -6.928  37.992  1.00 81.82           O  
ANISOU 5689  O   GLN B 398     8722  12114  10251   -200    -66   -939       O  
ATOM   5690  CB  GLN B 398      46.493  -9.599  39.037  1.00 74.39           C  
ANISOU 5690  CB  GLN B 398     8087  10977   9199   -359   -110  -1376       C  
ATOM   5691  CG  GLN B 398      46.109 -10.993  39.501  1.00 82.34           C  
ANISOU 5691  CG  GLN B 398     9246  11953  10087   -453   -116  -1612       C  
ATOM   5692  CD  GLN B 398      46.838 -12.082  38.749  1.00 81.77           C  
ANISOU 5692  CD  GLN B 398     9147  11985   9937   -480    -98  -1716       C  
ATOM   5693  OE1 GLN B 398      47.238 -11.899  37.601  1.00 86.40           O  
ANISOU 5693  OE1 GLN B 398     9569  12771  10489   -440    -53  -1621       O  
ATOM   5694  NE2 GLN B 398      47.016 -13.226  39.396  1.00 84.22           N  
ANISOU 5694  NE2 GLN B 398     9623  12159  10218   -551   -133  -1912       N  
ATOM   5695  N   TYR B 399      46.248  -6.151  40.107  1.00 53.90           N  
ANISOU 5695  N   TYR B 399     5418   8108   6955   -196   -166   -935       N  
ATOM   5696  CA  TYR B 399      46.456  -4.770  39.709  1.00 38.05           C  
ANISOU 5696  CA  TYR B 399     3275   6133   5051   -109   -161   -708       C  
ATOM   5697  C   TYR B 399      47.881  -4.284  39.918  1.00 60.05           C  
ANISOU 5697  C   TYR B 399     6067   8717   8032    -60   -211   -615       C  
ATOM   5698  O   TYR B 399      48.190  -3.149  39.540  1.00 74.68           O  
ANISOU 5698  O   TYR B 399     7804  10592   9977     13   -206   -422       O  
ATOM   5699  CB  TYR B 399      45.495  -3.859  40.480  1.00 37.80           C  
ANISOU 5699  CB  TYR B 399     3283   6015   5066    -92   -173   -641       C  
ATOM   5700  CG  TYR B 399      44.072  -4.369  40.511  1.00 46.28           C  
ANISOU 5700  CG  TYR B 399     4376   7237   5970   -148   -131   -754       C  
ATOM   5701  CD1 TYR B 399      43.248  -4.274  39.396  1.00 46.84           C  
ANISOU 5701  CD1 TYR B 399     4283   7626   5890   -134    -68   -703       C  
ATOM   5702  CD2 TYR B 399      43.551  -4.945  41.662  1.00 49.51           C  
ANISOU 5702  CD2 TYR B 399     4972   7468   6374   -216   -155   -915       C  
ATOM   5703  CE1 TYR B 399      41.942  -4.742  39.429  1.00 45.55           C  
ANISOU 5703  CE1 TYR B 399     4132   7596   5579   -186    -32   -810       C  
ATOM   5704  CE2 TYR B 399      42.251  -5.414  41.706  1.00 37.11           C  
ANISOU 5704  CE2 TYR B 399     3417   6029   4653   -270   -112  -1023       C  
ATOM   5705  CZ  TYR B 399      41.452  -5.310  40.590  1.00 39.36           C  
ANISOU 5705  CZ  TYR B 399     3530   6630   4797   -254    -52   -971       C  
ATOM   5706  OH  TYR B 399      40.162  -5.783  40.644  1.00 41.28           O  
ANISOU 5706  OH  TYR B 399     3785   7000   4899   -309    -12  -1083       O  
ATOM   5707  N   LYS B 400      48.749  -5.097  40.510  1.00 42.44           N  
ANISOU 5707  N   LYS B 400     3968   6289   5870    -98   -261   -745       N  
ATOM   5708  CA  LYS B 400      50.160  -4.770  40.620  1.00 42.99           C  
ANISOU 5708  CA  LYS B 400     4033   6179   6121    -55   -308   -673       C  
ATOM   5709  C   LYS B 400      50.915  -5.342  39.425  1.00 63.85           C  
ANISOU 5709  C   LYS B 400     6547   9009   8704    -50   -262   -682       C  
ATOM   5710  O   LYS B 400      50.407  -6.190  38.687  1.00 82.21           O  
ANISOU 5710  O   LYS B 400     8827  11564  10847    -91   -206   -778       O  
ATOM   5711  CB  LYS B 400      50.743  -5.319  41.923  1.00 37.90           C  
ANISOU 5711  CB  LYS B 400     3601   5203   5595    -96   -396   -807       C  
ATOM   5712  CG  LYS B 400      49.809  -5.217  43.116  1.00 40.97           C  
ANISOU 5712  CG  LYS B 400     4155   5429   5981   -134   -429   -872       C  
ATOM   5713  CD  LYS B 400      50.366  -5.953  44.329  1.00 35.03           C  
ANISOU 5713  CD  LYS B 400     3626   4366   5316   -186   -514  -1029       C  
ATOM   5714  CE  LYS B 400      49.310  -6.061  45.424  1.00 51.00           C  
ANISOU 5714  CE  LYS B 400     5821   6261   7294   -241   -530  -1125       C  
ATOM   5715  NZ  LYS B 400      49.787  -6.822  46.613  1.00 52.81           N  
ANISOU 5715  NZ  LYS B 400     6286   6188   7592   -299   -615  -1285       N  
ATOM   5716  N   GLU B 401      52.143  -4.868  39.241  1.00 65.07           N  
ANISOU 5716  N   GLU B 401     6643   9063   9016      0   -284   -581       N  
ATOM   5717  CA  GLU B 401      52.975  -5.331  38.132  1.00 77.66           C  
ANISOU 5717  CA  GLU B 401     8115  10814  10577      8   -237   -580       C  
ATOM   5718  C   GLU B 401      54.440  -5.449  38.542  1.00 85.15           C  
ANISOU 5718  C   GLU B 401     9110  11522  11722     24   -297   -596       C  
ATOM   5719  O   GLU B 401      55.167  -6.314  38.047  1.00 84.58           O  
ANISOU 5719  O   GLU B 401     9014  11494  11630      3   -281   -690       O  
ATOM   5720  CB  GLU B 401      52.839  -4.392  36.929  1.00 89.62           C  
ANISOU 5720  CB  GLU B 401     9425  12577  12048     68   -164   -385       C  
ATOM   5721  CG  GLU B 401      51.535  -4.553  36.154  1.00102.67           C  
ANISOU 5721  CG  GLU B 401    11001  14533  13477     47    -94   -391       C  
ATOM   5722  CD  GLU B 401      51.414  -3.585  34.992  1.00110.84           C  
ANISOU 5722  CD  GLU B 401    11844  15798  14471    107    -31   -192       C  
ATOM   5723  OE1 GLU B 401      50.950  -2.444  35.209  1.00113.21           O  
ANISOU 5723  OE1 GLU B 401    12111  16075  14829    155    -43    -43       O  
ATOM   5724  OE2 GLU B 401      51.789  -3.966  33.862  1.00112.03           O  
ANISOU 5724  OE2 GLU B 401    11884  16151  14532    105     31   -186       O  
TER    5725      GLU B 401                                                      
HETATM 5726  C1  ZOT A3001      14.011  -1.942  54.562  1.00 42.00           C  
HETATM 5727  C10 ZOT A3001      18.413  -1.198  57.550  1.00 42.84           C  
HETATM 5728  C11 ZOT A3001      18.874  -0.783  56.307  1.00 48.79           C  
HETATM 5729  C12 ZOT A3001      16.464  -0.729  55.027  1.00 56.28           C  
HETATM 5730  C13 ZOT A3001      16.009  -0.908  53.724  1.00 49.26           C  
HETATM 5731  C14 ZOT A3001      14.787  -1.526  53.490  1.00 41.66           C  
HETATM 5732  C15 ZOT A3001      20.203  -0.997  55.951  1.00 49.33           C  
HETATM 5733  C16 ZOT A3001      21.060  -1.668  56.817  1.00 57.09           C  
HETATM 5734  C17 ZOT A3001      20.591  -2.112  58.050  1.00 55.01           C  
HETATM 5735  C18 ZOT A3001      19.268  -1.878  58.411  1.00 41.00           C  
HETATM 5736  C2  ZOT A3001      14.447  -1.737  55.858  1.00 42.18           C  
HETATM 5737  C3  ZOT A3001      15.665  -1.120  56.095  1.00 54.45           C  
HETATM 5738  C4  ZOT A3001      15.904  -1.053  57.463  1.00 61.64           C  
HETATM 5739  C5  ZOT A3001      14.860  -0.042  59.240  1.00 59.08           C  
HETATM 5740  C6  ZOT A3001      13.602   0.825  59.203  1.00 57.47           C  
HETATM 5741  C7  ZOT A3001      11.854   1.846  60.484  1.00 58.75           C  
HETATM 5742  C8  ZOT A3001      12.796  -0.278  61.163  1.00 56.47           C  
HETATM 5743  C9  ZOT A3001      17.141  -1.105  58.105  1.00 55.64           C  
HETATM 5744  N1  ZOT A3001      13.079   1.034  60.557  1.00 58.81           N  
HETATM 5745  O1  ZOT A3001      14.765  -1.024  58.210  1.00 63.32           O  
HETATM 5746  S1  ZOT A3001      18.023   0.093  55.046  1.00 52.69           S  
HETATM 5747 CL1  ZOT A3001      12.507  -2.699  54.307  1.00 61.40          CL  
HETATM 5748  C1  CLR A3002      22.505  14.737  56.182  1.00 87.12           C  
HETATM 5749  C2  CLR A3002      21.109  15.301  55.924  1.00 89.47           C  
HETATM 5750  C3  CLR A3002      20.073  14.667  56.847  1.00 87.61           C  
HETATM 5751  C4  CLR A3002      20.451  14.952  58.296  1.00 84.00           C  
HETATM 5752  C5  CLR A3002      21.864  14.474  58.535  1.00 86.46           C  
HETATM 5753  C6  CLR A3002      22.089  13.637  59.561  1.00 86.34           C  
HETATM 5754  C7  CLR A3002      23.456  13.093  59.895  1.00 77.77           C  
HETATM 5755  C8  CLR A3002      24.538  13.998  59.337  1.00 68.76           C  
HETATM 5756  C9  CLR A3002      24.284  14.240  57.855  1.00 70.30           C  
HETATM 5757  C10 CLR A3002      22.962  14.970  57.619  1.00 80.50           C  
HETATM 5758  C11 CLR A3002      25.456  14.962  57.172  1.00 69.93           C  
HETATM 5759  C12 CLR A3002      26.823  14.330  57.453  1.00 71.29           C  
HETATM 5760  C13 CLR A3002      27.032  14.161  58.953  1.00 78.09           C  
HETATM 5761  C14 CLR A3002      25.891  13.326  59.493  1.00 73.64           C  
HETATM 5762  C15 CLR A3002      26.323  12.938  60.898  1.00 74.54           C  
HETATM 5763  C16 CLR A3002      27.834  12.755  60.754  1.00 80.98           C  
HETATM 5764  C17 CLR A3002      28.242  13.348  59.401  1.00 79.48           C  
HETATM 5765  C18 CLR A3002      27.065  15.517  59.653  1.00 77.33           C  
HETATM 5766  C19 CLR A3002      23.146  16.464  57.874  1.00 71.53           C  
HETATM 5767  C20 CLR A3002      29.565  14.104  59.509  1.00 69.66           C  
HETATM 5768  C21 CLR A3002      30.232  14.288  58.147  1.00 76.28           C  
HETATM 5769  C22 CLR A3002      30.492  13.380  60.485  1.00 56.95           C  
HETATM 5770  C23 CLR A3002      31.964  13.720  60.276  1.00 54.49           C  
HETATM 5771  C24 CLR A3002      32.844  12.694  60.981  1.00 66.88           C  
HETATM 5772  C25 CLR A3002      34.324  12.955  60.717  1.00 81.36           C  
HETATM 5773  C26 CLR A3002      34.905  13.958  61.707  1.00 78.44           C  
HETATM 5774  C27 CLR A3002      35.118  11.654  60.727  1.00 83.37           C  
HETATM 5775  O1  CLR A3002      18.779  15.217  56.574  1.00 87.39           O  
HETATM 5776  OH2 1PE A3003      50.107 -15.550  53.585  1.00 74.26           O  
HETATM 5777  C12 1PE A3003      51.531 -15.629  53.688  1.00 75.50           C  
HETATM 5778  C22 1PE A3003      52.095 -16.456  52.529  1.00 73.76           C  
HETATM 5779  OH3 1PE A3003      53.522 -16.516  52.641  1.00 72.85           O  
HETATM 5780  C13 1PE A3003      55.413 -17.080  54.004  1.00 67.14           C  
HETATM 5781  C23 1PE A3003      53.901 -17.206  53.833  1.00 68.96           C  
HETATM 5782  OH4 1PE A3003      55.753 -15.696  54.111  1.00 68.94           O  
HETATM 5783  C14 1PE A3003      55.926 -13.774  55.569  1.00 51.05           C  
HETATM 5784  C24 1PE A3003      55.465 -15.229  55.433  1.00 64.59           C  
HETATM 5785  OH5 1PE A3003      55.659 -13.293  56.892  1.00 32.97           O  
HETATM 5786  C15 1PE A3003      53.286 -12.768  56.827  1.00 38.58           C  
HETATM 5787  C25 1PE A3003      54.716 -12.215  56.832  1.00 39.90           C  
HETATM 5788  OH6 1PE A3003      52.353 -11.687  56.757  1.00 38.56           O  
HETATM 5789  C16 1PE A3003      50.530 -13.246  56.194  1.00 44.50           C  
HETATM 5790  C26 1PE A3003      51.044 -12.132  57.128  1.00 39.54           C  
HETATM 5791  OH7 1PE A3003      50.431 -12.797  54.837  1.00 35.52           O  
HETATM 5792 ZN    ZN A3004      50.982  -3.598  52.994  1.00 27.46          ZN  
HETATM 5793  C1  ZOT B3001      16.246   6.560  14.042  1.00 98.95           C  
HETATM 5794  C10 ZOT B3001      20.904   4.531  15.921  1.00 72.74           C  
HETATM 5795  C11 ZOT B3001      21.248   5.871  15.769  1.00 76.32           C  
HETATM 5796  C12 ZOT B3001      18.732   6.829  15.266  1.00 92.11           C  
HETATM 5797  C13 ZOT B3001      18.160   7.906  14.596  1.00 93.31           C  
HETATM 5798  C14 ZOT B3001      16.925   7.770  13.973  1.00 95.45           C  
HETATM 5799  C15 ZOT B3001      22.565   6.228  15.485  1.00 67.47           C  
HETATM 5800  C16 ZOT B3001      23.526   5.240  15.302  1.00 66.69           C  
HETATM 5801  C17 ZOT B3001      23.178   3.897  15.423  1.00 64.23           C  
HETATM 5802  C18 ZOT B3001      21.868   3.545  15.728  1.00 67.27           C  
HETATM 5803  C2  ZOT B3001      16.799   5.495  14.737  1.00 92.76           C  
HETATM 5804  C3  ZOT B3001      18.033   5.631  15.361  1.00 93.43           C  
HETATM 5805  C4  ZOT B3001      18.387   4.431  15.961  1.00 95.21           C  
HETATM 5806  C5  ZOT B3001      17.365   3.146  17.604  1.00100.08           C  
HETATM 5807  C6  ZOT B3001      16.026   3.432  18.294  1.00 92.97           C  
HETATM 5808  C7  ZOT B3001      14.593   2.977  20.164  1.00 69.91           C  
HETATM 5809  C8  ZOT B3001      15.621   1.165  18.954  1.00 71.90           C  
HETATM 5810  C9  ZOT B3001      19.671   3.946  16.190  1.00 84.57           C  
HETATM 5811  N1  ZOT B3001      15.798   2.540  19.441  1.00 77.31           N  
HETATM 5812  O1  ZOT B3001      17.313   3.646  16.261  1.00103.08           O  
HETATM 5813  S1  ZOT B3001      20.273   7.300  15.964  1.00 85.93           S  
HETATM 5814 CL1  ZOT B3001      14.718   6.376  13.277  1.00114.15          CL  
HETATM 5815  C1  PLM B3002      38.075 -10.074  40.453  1.00 34.93           C  
HETATM 5816  O2  PLM B3002      39.185 -10.684  40.409  1.00 38.84           O  
HETATM 5817  C2  PLM B3002      36.826 -11.020  40.510  1.00 29.07           C  
HETATM 5818  C3  PLM B3002      35.492 -10.353  40.844  1.00 35.39           C  
HETATM 5819  C4  PLM B3002      34.259 -11.220  40.519  1.00 42.98           C  
HETATM 5820  C5  PLM B3002      32.957 -10.415  40.400  1.00 44.72           C  
HETATM 5821  C6  PLM B3002      31.673 -11.264  40.482  1.00 48.85           C  
HETATM 5822  C7  PLM B3002      30.398 -10.426  40.690  1.00 46.23           C  
HETATM 5823  C8  PLM B3002      29.084 -11.205  40.537  1.00 38.93           C  
HETATM 5824  C9  PLM B3002      27.838 -10.306  40.597  1.00 34.43           C  
HETATM 5825  C1  CLR B3003      35.694  -6.761  36.333  1.00 56.12           C  
HETATM 5826  C2  CLR B3003      37.134  -6.980  36.792  1.00 58.89           C  
HETATM 5827  C3  CLR B3003      37.640  -5.811  37.630  1.00 38.77           C  
HETATM 5828  C4  CLR B3003      36.772  -5.705  38.873  1.00 42.24           C  
HETATM 5829  C5  CLR B3003      35.330  -5.578  38.436  1.00 52.50           C  
HETATM 5830  C6  CLR B3003      34.618  -4.530  38.880  1.00 61.50           C  
HETATM 5831  C7  CLR B3003      33.175  -4.294  38.515  1.00 57.38           C  
HETATM 5832  C8  CLR B3003      32.528  -5.608  38.121  1.00 50.95           C  
HETATM 5833  C9  CLR B3003      33.356  -6.275  37.031  1.00 44.22           C  
HETATM 5834  C10 CLR B3003      34.754  -6.636  37.524  1.00 45.20           C  
HETATM 5835  C11 CLR B3003      32.653  -7.498  36.421  1.00 46.89           C  
HETATM 5836  C12 CLR B3003      31.189  -7.263  36.037  1.00 47.65           C  
HETATM 5837  C13 CLR B3003      30.432  -6.648  37.207  1.00 60.04           C  
HETATM 5838  C14 CLR B3003      31.134  -5.358  37.571  1.00 60.32           C  
HETATM 5839  C15 CLR B3003      30.152  -4.599  38.452  1.00 52.17           C  
HETATM 5840  C16 CLR B3003      28.792  -4.981  37.866  1.00 59.29           C  
HETATM 5841  C17 CLR B3003      29.004  -6.185  36.942  1.00 56.73           C  
HETATM 5842  C18 CLR B3003      30.430  -7.600  38.403  1.00 56.93           C  
HETATM 5843  C19 CLR B3003      34.709  -7.955  38.286  1.00 38.32           C  
HETATM 5844  C20 CLR B3003      27.947  -7.257  37.183  1.00 49.74           C  
HETATM 5845  C21 CLR B3003      27.827  -8.219  36.006  1.00 61.59           C  
HETATM 5846  C22 CLR B3003      26.592  -6.637  37.509  1.00 51.11           C  
HETATM 5847  C23 CLR B3003      25.785  -6.327  36.251  1.00 59.46           C  
HETATM 5848  C24 CLR B3003      24.541  -5.512  36.599  1.00 62.49           C  
HETATM 5849  C25 CLR B3003      23.461  -5.654  35.533  1.00 57.81           C  
HETATM 5850  C26 CLR B3003      22.947  -7.089  35.483  1.00 58.68           C  
HETATM 5851  C27 CLR B3003      22.323  -4.659  35.751  1.00 44.19           C  
HETATM 5852  O1  CLR B3003      39.008  -6.022  38.001  1.00 34.64           O  
HETATM 5853  CA  A6L B3004      44.320  -0.560  40.449  1.00 25.40           C  
HETATM 5854  C   A6L B3004      45.433   0.334  40.911  1.00 52.71           C  
HETATM 5855  O   A6L B3004      45.364   1.172  41.804  1.00 55.16           O  
HETATM 5856  C3  A6L B3004      43.253  -0.784  41.524  1.00 13.15           C  
HETATM 5857  C4  A6L B3004      42.012  -1.541  41.021  1.00  3.21           C  
HETATM 5858  C5  A6L B3004      40.810  -1.384  41.964  1.00  1.41           C  
HETATM 5859  C6  A6L B3004      39.651  -2.332  41.634  1.00  6.09           C  
HETATM 5860  C7  A6L B3004      38.484  -2.232  42.635  1.00 17.95           C  
HETATM 5861  C8  A6L B3004      37.484  -3.408  42.581  1.00 30.29           C  
HETATM 5862  C9  A6L B3004      37.804  -4.568  43.468  1.00 38.32           C  
HETATM 5863  C10 A6L B3004      36.954  -5.295  44.208  1.00 49.17           C  
HETATM 5864  C11 A6L B3004      35.478  -5.132  44.347  1.00 50.64           C  
HETATM 5865  C12 A6L B3004      34.634  -6.116  43.502  1.00 55.60           C  
HETATM 5866  C13 A6L B3004      33.160  -6.130  43.952  1.00 53.26           C  
HETATM 5867  C14 A6L B3004      32.166  -5.721  42.851  1.00 41.41           C  
HETATM 5868  C15 A6L B3004      30.864  -6.507  42.964  1.00 44.79           C  
HETATM 5869  C16 A6L B3004      29.697  -5.827  42.244  1.00 51.41           C  
HETATM 5870  C17 A6L B3004      28.709  -6.855  41.673  1.00 49.62           C  
HETATM 5871  C18 A6L B3004      27.267  -6.558  42.063  1.00 45.33           C  
HETATM 5872  OXT A6L B3004      46.611   0.153  40.242  1.00 65.70           O  
CONECT  624 1257                                                                
CONECT  905 5792                                                                
CONECT  915 5792                                                                
CONECT 1257  624                                                                
CONECT 1556 5792                                                                
CONECT 2248 5792                                                                
CONECT 2497 2527                                                                
CONECT 2527 2497                                                                
CONECT 3505 4074                                                                
CONECT 4074 3505                                                                
CONECT 5298 5328                                                                
CONECT 5328 5298                                                                
CONECT 5685 5815                                                                
CONECT 5726 5731 5736 5747                                                      
CONECT 5727 5728 5735 5743                                                      
CONECT 5728 5727 5732 5746                                                      
CONECT 5729 5730 5737 5746                                                      
CONECT 5730 5729 5731                                                           
CONECT 5731 5726 5730                                                           
CONECT 5732 5728 5733                                                           
CONECT 5733 5732 5734                                                           
CONECT 5734 5733 5735                                                           
CONECT 5735 5727 5734                                                           
CONECT 5736 5726 5737                                                           
CONECT 5737 5729 5736 5738                                                      
CONECT 5738 5737 5743 5745                                                      
CONECT 5739 5740 5745                                                           
CONECT 5740 5739 5744                                                           
CONECT 5741 5744                                                                
CONECT 5742 5744                                                                
CONECT 5743 5727 5738                                                           
CONECT 5744 5740 5741 5742                                                      
CONECT 5745 5738 5739                                                           
CONECT 5746 5728 5729                                                           
CONECT 5747 5726                                                                
CONECT 5748 5749 5757                                                           
CONECT 5749 5748 5750                                                           
CONECT 5750 5749 5751 5775                                                      
CONECT 5751 5750 5752                                                           
CONECT 5752 5751 5753 5757                                                      
CONECT 5753 5752 5754                                                           
CONECT 5754 5753 5755                                                           
CONECT 5755 5754 5756 5761                                                      
CONECT 5756 5755 5757 5758                                                      
CONECT 5757 5748 5752 5756 5766                                                 
CONECT 5758 5756 5759                                                           
CONECT 5759 5758 5760                                                           
CONECT 5760 5759 5761 5764 5765                                                 
CONECT 5761 5755 5760 5762                                                      
CONECT 5762 5761 5763                                                           
CONECT 5763 5762 5764                                                           
CONECT 5764 5760 5763 5767                                                      
CONECT 5765 5760                                                                
CONECT 5766 5757                                                                
CONECT 5767 5764 5768 5769                                                      
CONECT 5768 5767                                                                
CONECT 5769 5767 5770                                                           
CONECT 5770 5769 5771                                                           
CONECT 5771 5770 5772                                                           
CONECT 5772 5771 5773 5774                                                      
CONECT 5773 5772                                                                
CONECT 5774 5772                                                                
CONECT 5775 5750                                                                
CONECT 5776 5777                                                                
CONECT 5777 5776 5778                                                           
CONECT 5778 5777 5779                                                           
CONECT 5779 5778 5781                                                           
CONECT 5780 5781 5782                                                           
CONECT 5781 5779 5780                                                           
CONECT 5782 5780 5784                                                           
CONECT 5783 5784 5785                                                           
CONECT 5784 5782 5783                                                           
CONECT 5785 5783 5787                                                           
CONECT 5786 5787 5788                                                           
CONECT 5787 5785 5786                                                           
CONECT 5788 5786 5790                                                           
CONECT 5789 5790 5791                                                           
CONECT 5790 5788 5789                                                           
CONECT 5791 5789                                                                
CONECT 5792  905  915 1556 2248                                                 
CONECT 5793 5798 5803 5814                                                      
CONECT 5794 5795 5802 5810                                                      
CONECT 5795 5794 5799 5813                                                      
CONECT 5796 5797 5804 5813                                                      
CONECT 5797 5796 5798                                                           
CONECT 5798 5793 5797                                                           
CONECT 5799 5795 5800                                                           
CONECT 5800 5799 5801                                                           
CONECT 5801 5800 5802                                                           
CONECT 5802 5794 5801                                                           
CONECT 5803 5793 5804                                                           
CONECT 5804 5796 5803 5805                                                      
CONECT 5805 5804 5810 5812                                                      
CONECT 5806 5807 5812                                                           
CONECT 5807 5806 5811                                                           
CONECT 5808 5811                                                                
CONECT 5809 5811                                                                
CONECT 5810 5794 5805                                                           
CONECT 5811 5807 5808 5809                                                      
CONECT 5812 5805 5806                                                           
CONECT 5813 5795 5796                                                           
CONECT 5814 5793                                                                
CONECT 5815 5685 5816 5817                                                      
CONECT 5816 5815                                                                
CONECT 5817 5815 5818                                                           
CONECT 5818 5817 5819                                                           
CONECT 5819 5818 5820                                                           
CONECT 5820 5819 5821                                                           
CONECT 5821 5820 5822                                                           
CONECT 5822 5821 5823                                                           
CONECT 5823 5822 5824                                                           
CONECT 5824 5823                                                                
CONECT 5825 5826 5834                                                           
CONECT 5826 5825 5827                                                           
CONECT 5827 5826 5828 5852                                                      
CONECT 5828 5827 5829                                                           
CONECT 5829 5828 5830 5834                                                      
CONECT 5830 5829 5831                                                           
CONECT 5831 5830 5832                                                           
CONECT 5832 5831 5833 5838                                                      
CONECT 5833 5832 5834 5835                                                      
CONECT 5834 5825 5829 5833 5843                                                 
CONECT 5835 5833 5836                                                           
CONECT 5836 5835 5837                                                           
CONECT 5837 5836 5838 5841 5842                                                 
CONECT 5838 5832 5837 5839                                                      
CONECT 5839 5838 5840                                                           
CONECT 5840 5839 5841                                                           
CONECT 5841 5837 5840 5844                                                      
CONECT 5842 5837                                                                
CONECT 5843 5834                                                                
CONECT 5844 5841 5845 5846                                                      
CONECT 5845 5844                                                                
CONECT 5846 5844 5847                                                           
CONECT 5847 5846 5848                                                           
CONECT 5848 5847 5849                                                           
CONECT 5849 5848 5850 5851                                                      
CONECT 5850 5849                                                                
CONECT 5851 5849                                                                
CONECT 5852 5827                                                                
CONECT 5853 5854 5856                                                           
CONECT 5854 5853 5855 5872                                                      
CONECT 5855 5854                                                                
CONECT 5856 5853 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 5864                                                           
CONECT 5864 5863 5865                                                           
CONECT 5865 5864 5866                                                           
CONECT 5866 5865 5867                                                           
CONECT 5867 5866 5868                                                           
CONECT 5868 5867 5869                                                           
CONECT 5869 5868 5870                                                           
CONECT 5870 5869 5871                                                           
CONECT 5871 5870                                                                
CONECT 5872 5854                                                                
MASTER      441    0    8   28    4    0   15    6 5870    2  160   58          
END