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HEADER    LIGASE                                  27-AUG-12   4GS5              
TITLE     THE CRYSTAL STRUCTURE OF ACYL-COA SYNTHETASE (AMP-FORMING)/AMP-ACID   
TITLE    2 LIGASE II-LIKE PROTEIN FROM DYADOBACTER FERMENTANS DSM 18053         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ACYL-COA SYNTHETASE (AMP-FORMING)/AMP-ACID LIGASE II-LIKE  
COMPND   3 PROTEIN;                                                             
COMPND   4 CHAIN: A;                                                            
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: DYADOBACTER FERMENTANS;                         
SOURCE   3 ORGANISM_TAXID: 471854;                                              
SOURCE   4 STRAIN: DSM 18053;                                                   
SOURCE   5 GENE: DFER_1215;                                                     
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)MAGIC;                            
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PMCSG7                                    
KEYWDS    STRUCTURAL GENOMICS, PSI-BIOLOGY, PROTEIN STRUCTURE INITIATIVE, MCSG, 
KEYWDS   2 MIDWEST CENTER FOR STRUCTURAL GENOMICS, LIGASE                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.TAN,J.HOLOWICKI,S.CLANCY,A.JOACHIMIAK,MIDWEST CENTER FOR STRUCTURAL 
AUTHOR   2 GENOMICS (MCSG)                                                      
REVDAT   1   12-SEP-12 4GS5    0                                                
JRNL        AUTH   K.TAN,J.HOLOWICKI,S.CLANCY,A.JOACHIMIAK                      
JRNL        TITL   THE CRYSTAL STRUCTURE OF ACYL-COA SYNTHETASE                 
JRNL        TITL 2 (AMP-FORMING)/AMP-ACID LIGASE II-LIKE PROTEIN FROM           
JRNL        TITL 3 DYADOBACTER FERMENTANS DSM 18053                             
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.02 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.7.1_743)                    
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.02                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 32.98                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 27373                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.198                           
REMARK   3   R VALUE            (WORKING SET) : 0.196                           
REMARK   3   FREE R VALUE                     : 0.255                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.020                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1373                            
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 32.9854 -  4.3444    0.98     2796   121  0.1741 0.1937        
REMARK   3     2  4.3444 -  3.4495    1.00     2659   139  0.1675 0.2401        
REMARK   3     3  3.4495 -  3.0138    1.00     2614   147  0.2110 0.2645        
REMARK   3     4  3.0138 -  2.7384    1.00     2586   151  0.2209 0.2841        
REMARK   3     5  2.7384 -  2.5422    1.00     2573   143  0.2224 0.3008        
REMARK   3     6  2.5422 -  2.3923    1.00     2555   144  0.2256 0.3082        
REMARK   3     7  2.3923 -  2.2726    1.00     2549   147  0.2138 0.2880        
REMARK   3     8  2.2726 -  2.1737    1.00     2551   132  0.2093 0.2607        
REMARK   3     9  2.1737 -  2.0900    1.00     2556   129  0.2141 0.2909        
REMARK   3    10  2.0900 -  2.0179    1.00     2561   120  0.2276 0.2840        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.10                                          
REMARK   3   SHRINKAGE RADIUS   : 0.83                                          
REMARK   3   K_SOL              : 0.32                                          
REMARK   3   B_SOL              : 33.61                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.530            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.760           
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) : 3.38290                                              
REMARK   3    B22 (A**2) : 3.38290                                              
REMARK   3    B33 (A**2) : -6.76580                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.00000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.007           2790                                  
REMARK   3   ANGLE     :  1.015           3768                                  
REMARK   3   CHIRALITY :  0.069            427                                  
REMARK   3   PLANARITY :  0.004            483                                  
REMARK   3   DIHEDRAL  : 15.012           1009                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 9                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: chain 'A' and (resseq 1:18)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  14.8177  31.2517 -18.7229              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4837 T22:   1.5166                                     
REMARK   3      T33:  -0.1963 T12:   0.4504                                     
REMARK   3      T13:  -0.0231 T23:   0.3434                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2642 L22:   1.4320                                     
REMARK   3      L33:   6.0224 L12:   0.3414                                     
REMARK   3      L13:  -0.1696 L23:   0.2047                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1081 S12:   0.7475 S13:   0.1378                       
REMARK   3      S21:  -0.4679 S22:  -0.2569 S23:   0.0528                       
REMARK   3      S31:  -0.0510 S32:  -0.0933 S33:   0.0602                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: chain 'A' and (resseq 19:69)                           
REMARK   3    ORIGIN FOR THE GROUP (A):  18.8647  16.8786 -10.7174              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2416 T22:   0.7170                                     
REMARK   3      T33:   0.1502 T12:  -0.0221                                     
REMARK   3      T13:  -0.0423 T23:  -0.1183                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9787 L22:   0.5133                                     
REMARK   3      L33:   0.0651 L12:  -0.8238                                     
REMARK   3      L13:  -0.3180 L23:   0.1188                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2393 S12:   1.2861 S13:   0.1043                       
REMARK   3      S21:  -0.4569 S22:  -0.3546 S23:   0.0511                       
REMARK   3      S31:  -0.0686 S32:  -0.6552 S33:   0.0973                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: chain 'A' and (resseq 70:127)                          
REMARK   3    ORIGIN FOR THE GROUP (A):  17.4686  29.9914  -5.1629              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1880 T22:   0.5016                                     
REMARK   3      T33:   0.2094 T12:   0.1254                                     
REMARK   3      T13:   0.0178 T23:   0.1135                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.9715 L22:   1.3393                                     
REMARK   3      L33:   2.8656 L12:   0.4941                                     
REMARK   3      L13:  -0.5504 L23:   0.2851                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2504 S12:   1.1286 S13:   0.6037                       
REMARK   3      S21:  -0.2995 S22:  -0.1709 S23:  -0.0903                       
REMARK   3      S31:   0.0272 S32:   0.0799 S33:  -0.0559                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: chain 'A' and (resseq 128:177)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  24.9032  33.6444   7.3907              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1040 T22:   0.3016                                     
REMARK   3      T33:   0.3021 T12:   0.0101                                     
REMARK   3      T13:   0.0245 T23:   0.0011                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9284 L22:   6.2648                                     
REMARK   3      L33:   2.6808 L12:  -0.1727                                     
REMARK   3      L13:  -0.9358 L23:  -0.2408                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1296 S12:   0.1475 S13:   0.5890                       
REMARK   3      S21:   0.1768 S22:  -0.0185 S23:  -0.3872                       
REMARK   3      S31:  -0.2426 S32:   0.1471 S33:  -0.0941                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: chain 'A' and (resseq 178:198)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  19.7315  19.9063   9.9259              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2180 T22:   0.2752                                     
REMARK   3      T33:   0.1559 T12:  -0.0199                                     
REMARK   3      T13:   0.0221 T23:  -0.0263                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1915 L22:   4.3506                                     
REMARK   3      L33:   4.5756 L12:  -1.3139                                     
REMARK   3      L13:  -1.5416 L23:   4.4283                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1362 S12:   0.2867 S13:  -0.1645                       
REMARK   3      S21:   0.1530 S22:   0.0332 S23:   0.0946                       
REMARK   3      S31:   0.3491 S32:  -0.2450 S33:   0.1018                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: chain 'A' and (resseq 199:230)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  18.6748   6.8938   8.9969              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3910 T22:   0.2329                                     
REMARK   3      T33:   0.2858 T12:  -0.1113                                     
REMARK   3      T13:   0.0787 T23:  -0.0745                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.8416 L22:   2.8147                                     
REMARK   3      L33:   4.0349 L12:  -0.2244                                     
REMARK   3      L13:   1.2835 L23:  -0.4811                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0232 S12:   0.2828 S13:  -0.5757                       
REMARK   3      S21:  -0.2077 S22:  -0.0346 S23:   0.1041                       
REMARK   3      S31:   1.0239 S32:  -0.4769 S33:  -0.0332                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: chain 'A' and (resseq 231:254)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  26.7051   9.9334  19.5539              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2842 T22:   0.1517                                     
REMARK   3      T33:   0.2038 T12:  -0.0055                                     
REMARK   3      T13:   0.0317 T23:  -0.0112                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.4267 L22:   1.9904                                     
REMARK   3      L33:   6.5288 L12:  -0.9801                                     
REMARK   3      L13:   4.8190 L23:  -2.5735                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0581 S12:  -0.0196 S13:  -0.0767                       
REMARK   3      S21:   0.1187 S22:  -0.2120 S23:  -0.1386                       
REMARK   3      S31:   0.6851 S32:   0.1716 S33:   0.1433                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: chain 'A' and (resseq 255:314)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  47.8326   7.2679  29.0315              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3333 T22:   0.1905                                     
REMARK   3      T33:   0.2734 T12:   0.1049                                     
REMARK   3      T13:   0.0139 T23:   0.1134                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.1184 L22:   3.0007                                     
REMARK   3      L33:   3.2003 L12:   0.9652                                     
REMARK   3      L13:  -0.7268 L23:   0.5874                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1167 S12:  -0.0685 S13:   0.1819                       
REMARK   3      S21:   0.2106 S22:  -0.1477 S23:  -0.3273                       
REMARK   3      S31:   0.2580 S32:   0.5940 S33:   0.0371                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: chain 'A' and (resseq 315:350)                         
REMARK   3    ORIGIN FOR THE GROUP (A):  47.1655   1.4085  23.7686              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4839 T22:   0.3483                                     
REMARK   3      T33:   0.3949 T12:   0.1633                                     
REMARK   3      T13:   0.0962 T23:   0.0750                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8280 L22:   1.6073                                     
REMARK   3      L33:   4.3519 L12:  -1.8107                                     
REMARK   3      L13:  -2.1750 L23:  -0.3833                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4189 S12:   0.2794 S13:  -0.3098                       
REMARK   3      S21:  -0.0229 S22:  -0.2474 S23:   0.0497                       
REMARK   3      S31:   0.9503 S32:   0.5685 S33:   0.5213                       
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 4GS5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-AUG-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB074568.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 23-JUL-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97937                            
REMARK 200  MONOCHROMATOR                  : SI 111 CRYSTAL                     
REMARK 200  OPTICS                         : MIRROR                             
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 27429                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.018                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 33.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 7.100                              
REMARK 200  R MERGE                    (I) : 0.08500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 31.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.02                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.05                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.60200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 3.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SHELXD/MLPHARE/DM/RESOLVE/HKL3000                     
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.89                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M AMMONIUM IODINE,  20% (W/V)         
REMARK 280  PEG3350, PH 7.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 289K    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y,X,Z+3/4                                              
REMARK 290       4555   Y,-X,Z+1/4                                              
REMARK 290       5555   -X,Y,-Z                                                 
REMARK 290       6555   X,-Y,-Z+1/2                                             
REMARK 290       7555   Y,X,-Z+1/4                                              
REMARK 290       8555   -Y,-X,-Z+3/4                                            
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       88.12850            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      132.19275            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       44.06425            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       88.12850            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       44.06425            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000      132.19275            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
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 300 REMARK: EXPERIMENTALLY UNKNOWN. THE MOLECULE IS PREDICTED TO BE A    
REMARK 300 MONOMER.                                                             
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     SER A    -2                                                      
REMARK 465     ASN A    -1                                                      
REMARK 465     ALA A     0                                                      
REMARK 465     ASP A   351                                                      
REMARK 465     SER A   352                                                      
REMARK 465     SER A   353                                                      
REMARK 465     ASN A   354                                                      
REMARK 465     GLY A   355                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A  14    CG   CD   CE   NZ                                   
REMARK 470     LYS A 330    CG   CD   CE   NZ                                   
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   I    IOD A   412     O    HOH A   650              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PRO A  16      150.65    -48.55                                   
REMARK 500    SER A 138        2.67    -66.85                                   
REMARK 500    VAL A 182      -66.68     67.39                                   
REMARK 500    SER A 183     -138.48   -136.91                                   
REMARK 500    ASN A 238       41.78    -84.86                                   
REMARK 500    ASN A 299      141.28     72.01                                   
REMARK 500    LEU A 349      -16.42    -49.73                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 408                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 410                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 411                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 412                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 413                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 414                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 415                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 416                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 417                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 418                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 419                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 420                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 421                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 422                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 423                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 424                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: MCSG-APC103395   RELATED DB: TARGETTRACK                 
DBREF  4GS5 A    1   355  UNP    C6W5A4   C6W5A4_DYAFD     1    355             
SEQADV 4GS5 SER A   -2  UNP  C6W5A4              EXPRESSION TAG                 
SEQADV 4GS5 ASN A   -1  UNP  C6W5A4              EXPRESSION TAG                 
SEQADV 4GS5 ALA A    0  UNP  C6W5A4              EXPRESSION TAG                 
SEQRES   1 A  358  SER ASN ALA MSE ILE TRP THR THR GLY LYS THR LEU CYS          
SEQRES   2 A  358  LYS THR GLN LYS ARG PRO ARG ASN PRO TYR PHE ALA GLN          
SEQRES   3 A  358  ALA TYR ASP PHE MSE GLU LYS TRP LEU GLY GLY ALA ARG          
SEQRES   4 A  358  GLU PHE VAL LEU HIS THR SER GLY SER THR GLY MSE PRO          
SEQRES   5 A  358  LYS PRO ILE THR VAL THR ARG ALA GLN LEU ALA ALA SER          
SEQRES   6 A  358  ALA ALA MSE THR GLY LYS ALA LEU SER LEU GLY PRO GLY          
SEQRES   7 A  358  THR ARG ALA LEU VAL CYS LEU ASN VAL GLY TYR ILE ALA          
SEQRES   8 A  358  GLY LEU MSE MSE LEU VAL ARG GLY MSE GLU LEU ASP TRP          
SEQRES   9 A  358  GLU LEU THR VAL THR GLU PRO THR ALA ASN PRO LEU ALA          
SEQRES  10 A  358  GLY LEU ASP HIS ALA ASP PHE ASP PHE VAL ALA MSE VAL          
SEQRES  11 A  358  PRO MSE GLN LEU GLN SER ILE LEU GLU ASN SER ALA THR          
SEQRES  12 A  358  SER GLY GLN VAL ASP ARG LEU GLY LYS VAL LEU LEU GLY          
SEQRES  13 A  358  GLY ALA PRO VAL ASN HIS ALA LEU ALA MSE GLN ILE SER          
SEQRES  14 A  358  ASP LEU ALA MSE PRO VAL TYR GLN SER TYR GLY MSE THR          
SEQRES  15 A  358  GLU THR VAL SER HIS VAL ALA LEU LYS ALA LEU ASN GLY          
SEQRES  16 A  358  PRO GLU ALA SER GLU LEU TYR VAL PHE LEU PRO GLY ILE          
SEQRES  17 A  358  GLN TYR GLY VAL ASP GLU ARG GLY CYS LEU HIS ILE SER          
SEQRES  18 A  358  GLY ALA VAL THR ASN GLY GLN THR VAL GLN THR ASN ASP          
SEQRES  19 A  358  LEU VAL GLU ILE HIS GLY ASN ALA PHE GLN TRP ILE GLY          
SEQRES  20 A  358  ARG ALA ASP ASN VAL ILE ASN SER GLY GLY VAL LYS ILE          
SEQRES  21 A  358  VAL LEU ASP GLN ILE ASP GLN ARG ILE ALA ALA VAL PHE          
SEQRES  22 A  358  HIS HIS LEU ASN ILE GLY ASN ALA PHE PHE CYS TRP TRP          
SEQRES  23 A  358  GLU PRO ASP ALA LYS LEU GLY GLN LYS LEU VAL LEU VAL          
SEQRES  24 A  358  ILE GLU ASN ALA MSE PRO GLU ALA LEU THR GLU ARG LEU          
SEQRES  25 A  358  THR ALA GLU ILE ARG SER ARG VAL SER THR TYR GLU ASN          
SEQRES  26 A  358  PRO LYS HIS ILE TYR PHE ALA LYS ALA PHE ALA LYS THR          
SEQRES  27 A  358  GLN THR ASP LYS ILE ASP LYS ARG ALA THR PHE GLN LYS          
SEQRES  28 A  358  LEU SER ASP SER SER ASN GLY                                  
MODRES 4GS5 MSE A    1  MET  SELENOMETHIONINE                                   
MODRES 4GS5 MSE A   28  MET  SELENOMETHIONINE                                   
MODRES 4GS5 MSE A   48  MET  SELENOMETHIONINE                                   
MODRES 4GS5 MSE A   65  MET  SELENOMETHIONINE                                   
MODRES 4GS5 MSE A   91  MET  SELENOMETHIONINE                                   
MODRES 4GS5 MSE A   92  MET  SELENOMETHIONINE                                   
MODRES 4GS5 MSE A   97  MET  SELENOMETHIONINE                                   
MODRES 4GS5 MSE A  126  MET  SELENOMETHIONINE                                   
MODRES 4GS5 MSE A  129  MET  SELENOMETHIONINE                                   
MODRES 4GS5 MSE A  163  MET  SELENOMETHIONINE                                   
MODRES 4GS5 MSE A  170  MET  SELENOMETHIONINE                                   
MODRES 4GS5 MSE A  178  MET  SELENOMETHIONINE                                   
MODRES 4GS5 MSE A  301  MET  SELENOMETHIONINE                                   
HET    MSE  A   1       8                                                       
HET    MSE  A  28       8                                                       
HET    MSE  A  48       8                                                       
HET    MSE  A  65       8                                                       
HET    MSE  A  91       8                                                       
HET    MSE  A  92       8                                                       
HET    MSE  A  97       8                                                       
HET    MSE  A 126       8                                                       
HET    MSE  A 129       8                                                       
HET    MSE  A 163       8                                                       
HET    MSE  A 170       8                                                       
HET    MSE  A 178       8                                                       
HET    MSE  A 301       8                                                       
HET    IOD  A 401       1                                                       
HET    IOD  A 402       1                                                       
HET    IOD  A 403       1                                                       
HET    IOD  A 404       1                                                       
HET    IOD  A 405       1                                                       
HET    IOD  A 406       1                                                       
HET    IOD  A 407       1                                                       
HET    IOD  A 408       1                                                       
HET    IOD  A 409       1                                                       
HET    IOD  A 410       1                                                       
HET    IOD  A 411       1                                                       
HET    IOD  A 412       1                                                       
HET    EDO  A 413       4                                                       
HET    EDO  A 414       4                                                       
HET    EDO  A 415       4                                                       
HET    EDO  A 416       4                                                       
HET    EDO  A 417       4                                                       
HET    EDO  A 418       4                                                       
HET    EDO  A 419       4                                                       
HET    EDO  A 420       4                                                       
HET    EDO  A 421       4                                                       
HET    EDO  A 422       4                                                       
HET    EDO  A 423       4                                                       
HET    EDO  A 424       4                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     IOD IODIDE ION                                                       
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   1  MSE    13(C5 H11 N O2 SE)                                           
FORMUL   2  IOD    12(I 1-)                                                     
FORMUL  14  EDO    12(C2 H6 O2)                                                 
FORMUL  26  HOH   *155(H2 O)                                                    
HELIX    1   1 THR A    8  THR A   12  5                                   5    
HELIX    2   2 ASN A   18  GLY A   34  1                                  17    
HELIX    3   3 ARG A   56  LEU A   70  1                                  15    
HELIX    4   4 TYR A   86  ASP A  100  1                                  15    
HELIX    5   5 VAL A  127  ASN A  137  1                                  11    
HELIX    6   6 THR A  140  GLY A  148  5                                   9    
HELIX    7   7 ASN A  158  ASP A  167  1                                  10    
HELIX    8   8 THR A  179  VAL A  182  5                                   4    
HELIX    9   9 GLY A  219  ASN A  223  5                                   5    
HELIX   10  10 LEU A  259  LEU A  273  1                                  15    
HELIX   11  11 PRO A  302  VAL A  317  1                                  16    
HELIX   12  12 SER A  318  ASN A  322  5                                   5    
HELIX   13  13 ASP A  341  LEU A  349  1                                   9    
SHEET    1   A12 ILE A   2  THR A   5  0                                        
SHEET    2   A12 GLU A 102  THR A 106 -1  O  LEU A 103   N  THR A   5           
SHEET    3   A12 ARG A  77  VAL A  80  1  N  VAL A  80   O  THR A 104           
SHEET    4   A12 PHE A 123  MSE A 126  1  O  PHE A 123   N  LEU A  79           
SHEET    5   A12 VAL A 150  LEU A 152  1  O  LEU A 151   N  MSE A 126           
SHEET    6   A12 VAL A 172  GLY A 177  1  O  TYR A 173   N  LEU A 152           
SHEET    7   A12 HIS A 184  ALA A 189 -1  O  LYS A 188   N  GLN A 174           
SHEET    8   A12 TYR A 199  PHE A 201 -1  O  VAL A 200   N  LEU A 187           
SHEET    9   A12 ALA A 239  ARG A 245 -1  O  PHE A 240   N  TYR A 199           
SHEET   10   A12 VAL A 227  ILE A 235 -1  N  LEU A 232   O  ILE A 243           
SHEET   11   A12 CYS A 214  SER A 218 -1  N  ILE A 217   O  VAL A 227           
SHEET   12   A12 GLN A 206  VAL A 209 -1  N  GLN A 206   O  SER A 218           
SHEET    1   B 2 GLU A  37  SER A  43  0                                        
SHEET    2   B 2 PRO A  49  THR A  55 -1  O  VAL A  54   N  PHE A  38           
SHEET    1   C 2 VAL A 249  SER A 252  0                                        
SHEET    2   C 2 VAL A 255  VAL A 258 -1  O  ILE A 257   N  ILE A 250           
SHEET    1   D 3 PHE A 279  ASP A 286  0                                        
SHEET    2   D 3 GLY A 290  GLU A 298 -1  O  LYS A 292   N  GLU A 284           
SHEET    3   D 3 ILE A 326  ALA A 329  1  O  TYR A 327   N  LEU A 295           
LINK         C   MSE A   1                 N   ILE A   2     1555   1555  1.33  
LINK         C   PHE A  27                 N   MSE A  28     1555   1555  1.33  
LINK         C   MSE A  28                 N   GLU A  29     1555   1555  1.33  
LINK         C   GLY A  47                 N   MSE A  48     1555   1555  1.33  
LINK         C   MSE A  48                 N   PRO A  49     1555   1555  1.35  
LINK         C   ALA A  64                 N   MSE A  65     1555   1555  1.33  
LINK         C   MSE A  65                 N   THR A  66     1555   1555  1.33  
LINK         C   LEU A  90                 N   MSE A  91     1555   1555  1.33  
LINK         C   MSE A  91                 N   MSE A  92     1555   1555  1.33  
LINK         C   MSE A  92                 N   LEU A  93     1555   1555  1.34  
LINK         C   GLY A  96                 N   MSE A  97     1555   1555  1.33  
LINK         C   MSE A  97                 N   GLU A  98     1555   1555  1.33  
LINK         C   ALA A 125                 N   MSE A 126     1555   1555  1.33  
LINK         C   MSE A 126                 N   VAL A 127     1555   1555  1.33  
LINK         C   PRO A 128                 N   MSE A 129     1555   1555  1.33  
LINK         C   MSE A 129                 N   GLN A 130     1555   1555  1.32  
LINK         C   ALA A 162                 N   MSE A 163     1555   1555  1.33  
LINK         C   MSE A 163                 N   GLN A 164     1555   1555  1.33  
LINK         C   ALA A 169                 N   MSE A 170     1555   1555  1.33  
LINK         C   MSE A 170                 N   PRO A 171     1555   1555  1.34  
LINK         C   GLY A 177                 N   MSE A 178     1555   1555  1.33  
LINK         C   MSE A 178                 N   THR A 179     1555   1555  1.33  
LINK         C   ALA A 300                 N   MSE A 301     1555   1555  1.33  
LINK         C   MSE A 301                 N   PRO A 302     1555   1555  1.34  
SITE     1 AC1  2 SER A  45  ARG A 245                                          
SITE     1 AC2  2 GLN A 132  EDO A 422                                          
SITE     1 AC3  1 EDO A 414                                                     
SITE     1 AC4  3 THR A 337  LYS A 339  HOH A 645                               
SITE     1 AC5  2 HIS A  41  IOD A 408                                          
SITE     1 AC6  3 ARG A 245  ASN A 248  IOD A 407                               
SITE     1 AC7  1 ALA A 300                                                     
SITE     1 AC8  2 ASN A 111  ASN A 137                                          
SITE     1 AC9  2 LEU A   9  HOH A 650                                          
SITE     1 BC1  3 LEU A  82  ASN A  83  ALA A  88                               
SITE     1 BC2  5 LEU A 151  GLY A 153  SER A 175  SER A 183                    
SITE     2 BC2  5 IOD A 404                                                     
SITE     1 BC3  3 ARG A  36  ALA A 278  PHE A 279                               
SITE     1 BC4  4 SER A  45  GLU A 180  THR A 229  HOH A 561                    
SITE     1 BC5  5 ALA A 329  LYS A 330  LYS A 348  LEU A 349                    
SITE     2 BC5  5 HOH A 649                                                     
SITE     1 BC6  1 HOH A 506                                                     
SITE     1 BC7  4 GLY A  67  SER A  71  LEU A  72  HOH A 559                    
SITE     1 BC8  3 LYS A  30  PHE A  38  VAL A  39                               
SITE     1 BC9  2 TYR A  20  GLN A  23                                          
SITE     1 CC1  5 VAL A 127  PRO A 128  MSE A 129  IOD A 403                    
SITE     2 CC1  5 HOH A 527                                                     
SITE     1 CC2  5 ALA A  64  MSE A  65  LYS A  68  PRO A 203                    
SITE     2 CC2  5 HOH A 603                                                     
SITE     1 CC3  9 LEU A 168  MSE A 170  PRO A 171  ASN A 191                    
SITE     2 CC3  9 GLY A 192  GLU A 321  HOH A 508  HOH A 554                    
SITE     3 CC3  9 HOH A 643                                                     
CRYST1   67.148   67.148  176.257  90.00  90.00  90.00 P 43 2 2      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      0.014892  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014892  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005674        0.00000                         
HETATM    1  N   MSE A   1      23.537  38.983 -15.595  1.00 81.58           N  
ANISOU    1  N   MSE A   1     8232  15719   7045   2179    407   2562       N  
HETATM    2  CA  MSE A   1      24.135  38.100 -14.589  1.00 79.86           C  
ANISOU    2  CA  MSE A   1     7789  15613   6943   2219    465   2515       C  
HETATM    3  C   MSE A   1      23.103  37.326 -13.770  1.00 72.78           C  
ANISOU    3  C   MSE A   1     6871  14605   6175   2373    516   2364       C  
HETATM    4  O   MSE A   1      23.453  36.670 -12.783  1.00 72.03           O  
ANISOU    4  O   MSE A   1     6648  14551   6169   2403    556   2321       O  
HETATM    5  CB  MSE A   1      25.083  38.871 -13.661  1.00 83.58           C  
ANISOU    5  CB  MSE A   1     8284  16090   7385   2007    410   2613       C  
HETATM    6  CG  MSE A   1      26.551  38.662 -14.006  1.00 88.10           C  
ANISOU    6  CG  MSE A   1     8635  16945   7893   1923    421   2719       C  
HETATM    7 SE   MSE A   1      26.899  39.097 -15.882  0.57138.99          SE  
ANISOU    7 SE   MSE A   1    15137  23512  14161   1868    401   2827      SE  
HETATM    8  CE  MSE A   1      28.503  38.025 -16.178  1.00 92.19           C  
ANISOU    8  CE  MSE A   1     8784  18025   8217   1933    467   2881       C  
ATOM      9  N   ILE A   2      21.840  37.410 -14.181  1.00 68.63           N  
ANISOU    9  N   ILE A   2     6475  13957   5644   2464    511   2288       N  
ATOM     10  CA  ILE A   2      20.774  36.606 -13.587  1.00 64.40           C  
ANISOU   10  CA  ILE A   2     5911  13353   5204   2601    559   2143       C  
ATOM     11  C   ILE A   2      19.744  36.162 -14.622  1.00 62.42           C  
ANISOU   11  C   ILE A   2     5679  13119   4918   2730    574   2069       C  
ATOM     12  O   ILE A   2      19.400  36.909 -15.537  1.00 70.34           O  
ANISOU   12  O   ILE A   2     6802  14100   5824   2715    528   2119       O  
ATOM     13  CB  ILE A   2      20.047  37.339 -12.438  1.00 67.08           C  
ANISOU   13  CB  ILE A   2     6400  13509   5576   2552    521   2108       C  
ATOM     14  CG1 ILE A   2      19.323  38.581 -12.949  1.00 70.48           C  
ANISOU   14  CG1 ILE A   2     7065  13809   5906   2526    441   2153       C  
ATOM     15  CG2 ILE A   2      21.016  37.721 -11.343  1.00 69.86           C  
ANISOU   15  CG2 ILE A   2     6744  13843   5957   2412    496   2174       C  
ATOM     16  CD1 ILE A   2      18.628  39.354 -11.839  1.00 70.48           C  
ANISOU   16  CD1 ILE A   2     7234  13627   5918   2506    393   2123       C  
ATOM     17  N   TRP A   3      19.265  34.933 -14.479  1.00 54.47           N  
ANISOU   17  N   TRP A   3     4572  12150   3974   2848    627   1955       N  
ATOM     18  CA  TRP A   3      18.185  34.426 -15.319  1.00 54.34           C  
ANISOU   18  CA  TRP A   3     4573  12155   3918   2948    628   1872       C  
ATOM     19  C   TRP A   3      16.970  34.099 -14.448  1.00 51.80           C  
ANISOU   19  C   TRP A   3     4317  11710   3654   2959    617   1748       C  
ATOM     20  O   TRP A   3      17.070  33.328 -13.489  1.00 50.57           O  
ANISOU   20  O   TRP A   3     4213  11416   3585   2889    602   1676       O  
ATOM     21  CB  TRP A   3      18.658  33.194 -16.097  1.00 57.38           C  
ANISOU   21  CB  TRP A   3     4910  12602   4289   2992    636   1839       C  
ATOM     22  CG  TRP A   3      17.632  32.595 -17.014  1.00 56.83           C  
ANISOU   22  CG  TRP A   3     4863  12569   4160   3070    620   1761       C  
ATOM     23  CD1 TRP A   3      17.027  33.200 -18.084  1.00 60.90           C  
ANISOU   23  CD1 TRP A   3     5392  13174   4573   3110    604   1791       C  
ATOM     24  CD2 TRP A   3      17.106  31.260 -16.958  1.00 57.40           C  
ANISOU   24  CD2 TRP A   3     4992  12567   4250   3081    594   1645       C  
ATOM     25  NE1 TRP A   3      16.146  32.328 -18.683  1.00 59.77           N  
ANISOU   25  NE1 TRP A   3     5243  13080   4386   3172    587   1699       N  
ATOM     26  CE2 TRP A   3      16.180  31.134 -18.019  1.00 60.16           C  
ANISOU   26  CE2 TRP A   3     5315  13040   4505   3154    580   1614       C  
ATOM     27  CE3 TRP A   3      17.323  30.166 -16.112  1.00 55.52           C  
ANISOU   27  CE3 TRP A   3     4817  12197   4080   3052    582   1576       C  
ATOM     28  CZ2 TRP A   3      15.472  29.950 -18.249  1.00 60.13           C  
ANISOU   28  CZ2 TRP A   3     5331  13048   4468   3182    549   1517       C  
ATOM     29  CZ3 TRP A   3      16.617  28.995 -16.345  1.00 55.13           C  
ANISOU   29  CZ3 TRP A   3     4802  12151   3994   3099    557   1489       C  
ATOM     30  CH2 TRP A   3      15.704  28.896 -17.402  1.00 57.14           C  
ANISOU   30  CH2 TRP A   3     5015  12546   4150   3156    538   1460       C  
ATOM     31  N   THR A   4      15.829  34.702 -14.763  1.00 52.29           N  
ANISOU   31  N   THR A   4     4421  11790   3656   3018    603   1723       N  
ATOM     32  CA  THR A   4      14.623  34.505 -13.959  1.00 57.39           C  
ANISOU   32  CA  THR A   4     5111  12359   4338   3025    588   1612       C  
ATOM     33  C   THR A   4      13.708  33.458 -14.584  1.00 58.31           C  
ANISOU   33  C   THR A   4     5221  12509   4424   3037    557   1510       C  
ATOM     34  O   THR A   4      13.402  33.516 -15.770  1.00 52.74           O  
ANISOU   34  O   THR A   4     4467  11947   3624   3117    558   1528       O  
ATOM     35  CB  THR A   4      13.848  35.823 -13.759  1.00 58.70           C  
ANISOU   35  CB  THR A   4     5366  12497   4441   3073    567   1635       C  
ATOM     36  OG1 THR A   4      14.688  36.776 -13.094  1.00 59.50           O  
ANISOU   36  OG1 THR A   4     5570  12475   4562   2988    543   1726       O  
ATOM     37  CG2 THR A   4      12.593  35.587 -12.914  1.00 56.24           C  
ANISOU   37  CG2 THR A   4     5039  12180   4151   3117    572   1520       C  
ATOM     38  N   THR A   5      13.270  32.497 -13.781  1.00 50.37           N  
ANISOU   38  N   THR A   5     4253  11401   3486   2963    528   1414       N  
ATOM     39  CA  THR A   5      12.481  31.393 -14.309  1.00 50.65           C  
ANISOU   39  CA  THR A   5     4261  11507   3477   2968    494   1332       C  
ATOM     40  C   THR A   5      11.457  30.847 -13.318  1.00 49.88           C  
ANISOU   40  C   THR A   5     4178  11362   3411   2905    458   1236       C  
ATOM     41  O   THR A   5      11.326  31.334 -12.186  1.00 50.41           O  
ANISOU   41  O   THR A   5     4287  11322   3544   2862    461   1226       O  
ATOM     42  CB  THR A   5      13.393  30.241 -14.847  1.00 51.45           C  
ANISOU   42  CB  THR A   5     4359  11616   3574   2977    496   1343       C  
ATOM     43  OG1 THR A   5      12.611  29.330 -15.628  1.00 52.15           O  
ANISOU   43  OG1 THR A   5     4403  11840   3572   3015    465   1283       O  
ATOM     44  CG2 THR A   5      14.072  29.481 -13.703  1.00 52.35           C  
ANISOU   44  CG2 THR A   5     4534  11576   3778   2920    497   1327       C  
ATOM     45  N   GLY A   6      10.732  29.827 -13.754  1.00 58.39           N  
ANISOU   45  N   GLY A   6     5206  12553   4427   2903    423   1171       N  
ATOM     46  CA  GLY A   6       9.630  29.278 -12.989  1.00 55.63           C  
ANISOU   46  CA  GLY A   6     4828  12240   4070   2841    384   1086       C  
ATOM     47  C   GLY A   6       8.957  28.176 -13.779  1.00 56.57           C  
ANISOU   47  C   GLY A   6     4854  12567   4071   2847    346   1032       C  
ATOM     48  O   GLY A   6       9.280  27.962 -14.958  1.00 53.07           O  
ANISOU   48  O   GLY A   6     4379  12231   3554   2914    352   1057       O  
ATOM     49  N   LYS A   7       8.034  27.472 -13.130  1.00 56.72           N  
ANISOU   49  N   LYS A   7     4815  12681   4055   2775    307    958       N  
ATOM     50  CA  LYS A   7       7.306  26.382 -13.765  1.00 62.11           C  
ANISOU   50  CA  LYS A   7     5500  13505   4593   2675    243    890       C  
ATOM     51  C   LYS A   7       6.601  26.871 -15.019  1.00 64.79           C  
ANISOU   51  C   LYS A   7     5736  14055   4825   2715    229    875       C  
ATOM     52  O   LYS A   7       6.851  26.376 -16.126  1.00 64.84           O  
ANISOU   52  O   LYS A   7     5819  14081   4737   2692    203    877       O  
ATOM     53  CB  LYS A   7       6.285  25.793 -12.797  1.00 66.19           C  
ANISOU   53  CB  LYS A   7     6012  14070   5068   2515    195    807       C  
ATOM     54  CG  LYS A   7       5.680  24.466 -13.219  1.00 71.01           C  
ANISOU   54  CG  LYS A   7     6764  14716   5499   2297    132    721       C  
ATOM     55  CD  LYS A   7       4.703  23.957 -12.156  1.00 76.48           C  
ANISOU   55  CD  LYS A   7     7462  15461   6137   2105    101    639       C  
ATOM     56  CE  LYS A   7       4.125  22.596 -12.520  1.00 80.49           C  
ANISOU   56  CE  LYS A   7     8181  15976   6427   1832     70    538       C  
ATOM     57  NZ  LYS A   7       3.457  22.603 -13.860  1.00 83.31           N  
ANISOU   57  NZ  LYS A   7     8447  16562   6645   1794     37    491       N  
ATOM     58  N   THR A   8       5.731  27.859 -14.863  1.00 66.47           N  
ANISOU   58  N   THR A   8     5794  14429   5034   2788    250    859       N  
ATOM     59  CA  THR A   8       4.991  28.336 -16.023  1.00 73.44           C  
ANISOU   59  CA  THR A   8     6586  15530   5790   2843    236    845       C  
ATOM     60  C   THR A   8       5.866  29.208 -16.920  1.00 74.86           C  
ANISOU   60  C   THR A   8     6820  15641   5981   2988    285    939       C  
ATOM     61  O   THR A   8       5.721  29.192 -18.141  1.00 78.15           O  
ANISOU   61  O   THR A   8     7240  16166   6287   3002    255    947       O  
ATOM     62  CB  THR A   8       3.664  29.050 -15.641  1.00 72.43           C  
ANISOU   62  CB  THR A   8     6345  15569   5608   2860    228    786       C  
ATOM     63  OG1 THR A   8       3.904  30.438 -15.364  1.00 69.38           O  
ANISOU   63  OG1 THR A   8     6066  15014   5281   2981    270    844       O  
ATOM     64  CG2 THR A   8       3.030  28.368 -14.436  1.00 71.48           C  
ANISOU   64  CG2 THR A   8     6175  15474   5511   2714    197    710       C  
ATOM     65  N   LEU A   9       6.790  29.954 -16.328  1.00 71.21           N  
ANISOU   65  N   LEU A   9     6483  14930   5642   3022    330   1009       N  
ATOM     66  CA  LEU A   9       7.644  30.817 -17.137  1.00 73.72           C  
ANISOU   66  CA  LEU A   9     6849  15210   5952   3130    372   1106       C  
ATOM     67  C   LEU A   9       8.580  29.997 -18.041  1.00 74.63           C  
ANISOU   67  C   LEU A   9     6982  15328   6045   3123    370   1141       C  
ATOM     68  O   LEU A   9       9.033  30.474 -19.086  1.00 78.91           O  
ANISOU   68  O   LEU A   9     7561  15894   6527   3174    374   1206       O  
ATOM     69  CB  LEU A   9       8.423  31.792 -16.252  1.00 70.63           C  
ANISOU   69  CB  LEU A   9     6572  14593   5672   3138    414   1171       C  
ATOM     70  CG  LEU A   9       9.305  32.822 -16.958  1.00 67.16           C  
ANISOU   70  CG  LEU A   9     6162  14151   5203   3243    460   1284       C  
ATOM     71  CD1 LEU A   9       8.562  33.476 -18.108  1.00 65.19           C  
ANISOU   71  CD1 LEU A   9     5888  14078   4802   3352    438   1302       C  
ATOM     72  CD2 LEU A   9       9.793  33.866 -15.965  1.00 67.68           C  
ANISOU   72  CD2 LEU A   9     6312  14061   5342   3253    492   1338       C  
ATOM     73  N   CYS A  10       8.843  28.754 -17.648  1.00 70.04           N  
ANISOU   73  N   CYS A  10     6443  14675   5492   3032    341   1097       N  
ATOM     74  CA  CYS A  10       9.721  27.876 -18.417  1.00 64.16           C  
ANISOU   74  CA  CYS A  10     5798  13874   4707   3013    326   1117       C  
ATOM     75  C   CYS A  10       9.055  27.414 -19.721  1.00 74.47           C  
ANISOU   75  C   CYS A  10     7126  15327   5843   2965    263   1075       C  
ATOM     76  O   CYS A  10       9.733  27.014 -20.671  1.00 73.70           O  
ANISOU   76  O   CYS A  10     7110  15215   5677   2978    259   1103       O  
ATOM     77  CB  CYS A  10      10.148  26.670 -17.569  1.00 56.60           C  
ANISOU   77  CB  CYS A  10     4946  12771   3790   2942    312   1081       C  
ATOM     78  SG  CYS A  10      11.665  25.870 -18.111  1.00 94.45           S  
ANISOU   78  SG  CYS A  10     9874  17446   8566   3003    339   1133       S  
ATOM     79  N   LYS A  11       7.727  27.489 -19.770  1.00 81.95           N  
ANISOU   79  N   LYS A  11     7990  16436   6709   2909    217   1006       N  
ATOM     80  CA  LYS A  11       6.970  26.976 -20.916  1.00 89.43           C  
ANISOU   80  CA  LYS A  11     8949  17552   7477   2830    149    950       C  
ATOM     81  C   LYS A  11       7.069  27.845 -22.177  1.00 90.16           C  
ANISOU   81  C   LYS A  11     9012  17753   7493   2939    152   1015       C  
ATOM     82  O   LYS A  11       6.898  27.348 -23.293  1.00 92.68           O  
ANISOU   82  O   LYS A  11     9384  18166   7665   2884    103    993       O  
ATOM     83  CB  LYS A  11       5.498  26.779 -20.541  1.00 96.10           C  
ANISOU   83  CB  LYS A  11     9681  18588   8243   2725     98    852       C  
ATOM     84  CG  LYS A  11       4.701  28.076 -20.451  1.00101.09           C  
ANISOU   84  CG  LYS A  11    10137  19390   8881   2862    123    869       C  
ATOM     85  CD  LYS A  11       3.252  27.833 -20.051  1.00104.69           C  
ANISOU   85  CD  LYS A  11    10441  20087   9248   2770     80    764       C  
ATOM     86  CE  LYS A  11       2.456  27.198 -21.183  1.00109.03           C  
ANISOU   86  CE  LYS A  11    10963  20868   9596   2645      0    696       C  
ATOM     87  NZ  LYS A  11       1.024  26.993 -20.812  1.00110.79           N  
ANISOU   87  NZ  LYS A  11    10998  21382   9714   2539    -38    589       N  
ATOM     88  N   THR A  12       7.334  29.137 -21.998  1.00 86.95           N  
ANISOU   88  N   THR A  12     8557  17320   7160   3075    206   1096       N  
ATOM     89  CA  THR A  12       7.358  30.090 -23.112  1.00 84.14           C  
ANISOU   89  CA  THR A  12     8213  17046   6710   3171    200   1168       C  
ATOM     90  C   THR A  12       8.766  30.599 -23.336  1.00 74.91           C  
ANISOU   90  C   THR A  12     7133  15721   5609   3223    253   1281       C  
ATOM     91  O   THR A  12       9.133  31.039 -24.429  1.00 72.77           O  
ANISOU   91  O   THR A  12     6915  15486   5248   3259    238   1351       O  
ATOM     92  CB  THR A  12       6.502  31.321 -22.794  1.00 88.63           C  
ANISOU   92  CB  THR A  12     8718  17698   7257   3283    209   1181       C  
ATOM     93  OG1 THR A  12       6.902  31.856 -21.523  1.00 85.07           O  
ANISOU   93  OG1 THR A  12     8282  17089   6952   3317    274   1204       O  
ATOM     94  CG2 THR A  12       5.024  30.954 -22.746  1.00 92.85           C  
ANISOU   94  CG2 THR A  12     9122  18469   7689   3250    157   1074       C  
ATOM     95  N   GLN A  13       9.544  30.542 -22.267  1.00 67.01           N  
ANISOU   95  N   GLN A  13     6141  14561   4757   3216    309   1299       N  
ATOM     96  CA  GLN A  13      10.900  31.056 -22.236  1.00 62.87           C  
ANISOU   96  CA  GLN A  13     5669  13914   4305   3245    363   1403       C  
ATOM     97  C   GLN A  13      11.783  30.411 -23.282  1.00 62.11           C  
ANISOU   97  C   GLN A  13     5620  13837   4143   3235    357   1437       C  
ATOM     98  O   GLN A  13      11.698  29.202 -23.506  1.00 60.91           O  
ANISOU   98  O   GLN A  13     5494  13702   3947   3194    330   1366       O  
ATOM     99  CB  GLN A  13      11.494  30.763 -20.864  1.00 60.43           C  
ANISOU   99  CB  GLN A  13     5342  13467   4152   3223    412   1391       C  
ATOM    100  CG  GLN A  13      12.463  31.791 -20.370  1.00 61.40           C  
ANISOU  100  CG  GLN A  13     5489  13487   4354   3239    463   1491       C  
ATOM    101  CD  GLN A  13      12.626  31.710 -18.864  1.00 58.58           C  
ANISOU  101  CD  GLN A  13     5106  13019   4132   3216    500   1463       C  
ATOM    102  OE1 GLN A  13      12.263  30.703 -18.237  1.00 55.23           O  
ANISOU  102  OE1 GLN A  13     4661  12571   3752   3184    487   1379       O  
ATOM    103  NE2 GLN A  13      13.153  32.775 -18.274  1.00 58.92           N  
ANISOU  103  NE2 GLN A  13     5184  12976   4225   3207    529   1537       N  
ATOM    104  N   LYS A  14      12.649  31.216 -23.894  1.00 62.18           N  
ANISOU  104  N   LYS A  14     5664  13836   4125   3261    377   1547       N  
ATOM    105  CA  LYS A  14      13.655  30.700 -24.820  1.00 66.97           C  
ANISOU  105  CA  LYS A  14     6302  14475   4669   3263    387   1592       C  
ATOM    106  C   LYS A  14      14.820  30.096 -24.035  1.00 68.57           C  
ANISOU  106  C   LYS A  14     6475  14595   4984   3275    443   1604       C  
ATOM    107  O   LYS A  14      15.015  30.408 -22.859  1.00 68.67           O  
ANISOU  107  O   LYS A  14     6447  14520   5125   3268    475   1610       O  
ATOM    108  CB  LYS A  14      14.163  31.811 -25.744  1.00 68.07           C  
ANISOU  108  CB  LYS A  14     6490  14652   4722   3267    381   1716       C  
ATOM    109  N   ARG A  15      15.588  29.224 -24.681  1.00 64.05           N  
ANISOU  109  N   ARG A  15     5929  14057   4349   3304    452   1606       N  
ATOM    110  CA  ARG A  15      16.756  28.645 -24.037  1.00 62.85           C  
ANISOU  110  CA  ARG A  15     5746  13856   4277   3355    502   1626       C  
ATOM    111  C   ARG A  15      17.870  29.684 -23.951  1.00 63.73           C  
ANISOU  111  C   ARG A  15     5779  14003   4432   3349    546   1755       C  
ATOM    112  O   ARG A  15      18.273  30.257 -24.961  1.00 63.53           O  
ANISOU  112  O   ARG A  15     5763  14067   4307   3331    542   1836       O  
ATOM    113  CB  ARG A  15      17.216  27.399 -24.791  1.00 65.11           C  
ANISOU  113  CB  ARG A  15     6114  14173   4451   3414    499   1589       C  
ATOM    114  CG  ARG A  15      18.317  26.589 -24.116  1.00 61.72           C  
ANISOU  114  CG  ARG A  15     5678  13697   4077   3511    544   1598       C  
ATOM    115  CD  ARG A  15      18.463  25.260 -24.832  1.00 63.12           C  
ANISOU  115  CD  ARG A  15     6013  13864   4106   3573    537   1536       C  
ATOM    116  NE  ARG A  15      19.536  24.411 -24.320  1.00 63.22           N  
ANISOU  116  NE  ARG A  15     6052  13836   4131   3712    582   1548       N  
ATOM    117  CZ  ARG A  15      20.830  24.597 -24.574  1.00 65.19           C  
ANISOU  117  CZ  ARG A  15     6191  14206   4372   3827    631   1640       C  
ATOM    118  NH1 ARG A  15      21.221  25.625 -25.315  1.00 71.32           N  
ANISOU  118  NH1 ARG A  15     6841  15132   5124   3784    641   1731       N  
ATOM    119  NH2 ARG A  15      21.736  23.764 -24.077  1.00 64.43           N  
ANISOU  119  NH2 ARG A  15     6116  14090   4272   3985    669   1649       N  
ATOM    120  N   PRO A  16      18.363  29.947 -22.734  1.00 63.16           N  
ANISOU  120  N   PRO A  16     5642  13866   4491   3341    581   1778       N  
ATOM    121  CA  PRO A  16      19.425  30.938 -22.539  1.00 65.34           C  
ANISOU  121  CA  PRO A  16     5852  14181   4793   3292    609   1902       C  
ATOM    122  C   PRO A  16      20.578  30.739 -23.514  1.00 70.95           C  
ANISOU  122  C   PRO A  16     6514  15038   5404   3327    626   1982       C  
ATOM    123  O   PRO A  16      20.828  29.608 -23.946  1.00 71.69           O  
ANISOU  123  O   PRO A  16     6612  15179   5447   3433    635   1933       O  
ATOM    124  CB  PRO A  16      19.897  30.653 -21.115  1.00 59.83           C  
ANISOU  124  CB  PRO A  16     5084  13417   4231   3306    644   1885       C  
ATOM    125  CG  PRO A  16      18.669  30.168 -20.434  1.00 60.79           C  
ANISOU  125  CG  PRO A  16     5265  13421   4410   3313    625   1766       C  
ATOM    126  CD  PRO A  16      17.916  29.363 -21.455  1.00 64.58           C  
ANISOU  126  CD  PRO A  16     5820  13934   4785   3351    585   1693       C  
ATOM    127  N   ARG A  17      21.261  31.827 -23.860  1.00 74.24           N  
ANISOU  127  N   ARG A  17     6913  15522   5773   3232    624   2108       N  
ATOM    128  CA  ARG A  17      22.468  31.736 -24.674  1.00 79.49           C  
ANISOU  128  CA  ARG A  17     7505  16360   6336   3245    643   2199       C  
ATOM    129  C   ARG A  17      23.674  31.502 -23.774  1.00 74.62           C  
ANISOU  129  C   ARG A  17     6732  15827   5795   3273    681   2246       C  
ATOM    130  O   ARG A  17      24.654  30.879 -24.182  1.00 73.16           O  
ANISOU  130  O   ARG A  17     6445  15806   5547   3368    706   2279       O  
ATOM    131  CB  ARG A  17      22.649  32.987 -25.534  1.00 88.29           C  
ANISOU  131  CB  ARG A  17     8695  17521   7331   3103    611   2322       C  
ATOM    132  CG  ARG A  17      21.618  33.107 -26.652  1.00 97.97           C  
ANISOU  132  CG  ARG A  17    10064  18716   8443   3108    571   2290       C  
ATOM    133  CD  ARG A  17      21.853  34.340 -27.513  1.00105.72           C  
ANISOU  133  CD  ARG A  17    11160  19725   9283   2974    532   2426       C  
ATOM    134  NE  ARG A  17      20.704  35.243 -27.496  1.00109.99           N  
ANISOU  134  NE  ARG A  17    11870  20114   9808   2931    469   2426       N  
ATOM    135  CZ  ARG A  17      20.667  36.415 -28.123  1.00114.34           C  
ANISOU  135  CZ  ARG A  17    12595  20621  10228   2826    411   2543       C  
ATOM    136  NH1 ARG A  17      21.718  36.829 -28.820  1.00116.90           N  
ANISOU  136  NH1 ARG A  17    12944  21048  10426   2717    415   2668       N  
ATOM    137  NH2 ARG A  17      19.579  37.174 -28.055  1.00114.34           N  
ANISOU  137  NH2 ARG A  17    12758  20481  10207   2833    343   2539       N  
ATOM    138  N   ASN A  18      23.590  31.991 -22.539  1.00 72.86           N  
ANISOU  138  N   ASN A  18     6489  15502   5691   3202    681   2248       N  
ATOM    139  CA  ASN A  18      24.598  31.677 -21.533  1.00 71.30           C  
ANISOU  139  CA  ASN A  18     6141  15380   5571   3236    711   2277       C  
ATOM    140  C   ASN A  18      24.560  30.178 -21.250  1.00 66.19           C  
ANISOU  140  C   ASN A  18     5583  14609   4958   3366    718   2150       C  
ATOM    141  O   ASN A  18      23.507  29.636 -20.896  1.00 64.32           O  
ANISOU  141  O   ASN A  18     5477  14185   4776   3389    704   2034       O  
ATOM    142  CB  ASN A  18      24.356  32.474 -20.251  1.00 73.99           C  
ANISOU  142  CB  ASN A  18     6505  15588   6020   3107    701   2285       C  
ATOM    143  CG  ASN A  18      25.495  32.346 -19.260  1.00 77.28           C  
ANISOU  143  CG  ASN A  18     6848  16029   6488   3049    704   2320       C  
ATOM    144  OD1 ASN A  18      25.993  31.249 -19.000  1.00 76.41           O  
ANISOU  144  OD1 ASN A  18     6784  15855   6395   3120    709   2251       O  
ATOM    145  ND2 ASN A  18      25.918  33.473 -18.702  1.00 78.85           N  
ANISOU  145  ND2 ASN A  18     6955  16312   6691   2910    693   2432       N  
ATOM    146  N   PRO A  19      25.705  29.498 -21.423  1.00 50.82           N  
ANISOU  146  N   PRO A  19     4739  10428   4143   2349    855   2703       N  
ATOM    147  CA  PRO A  19      25.760  28.039 -21.266  1.00 54.85           C  
ANISOU  147  CA  PRO A  19     5344  11004   4494   2180    735   2386       C  
ATOM    148  C   PRO A  19      25.433  27.608 -19.840  1.00 55.09           C  
ANISOU  148  C   PRO A  19     5469  10828   4633   1962    653   2209       C  
ATOM    149  O   PRO A  19      24.779  26.586 -19.632  1.00 58.36           O  
ANISOU  149  O   PRO A  19     5903  11372   4897   1833    530   1917       O  
ATOM    150  CB  PRO A  19      27.220  27.709 -21.587  1.00 56.98           C  
ANISOU  150  CB  PRO A  19     5698  11122   4831   2168    817   2440       C  
ATOM    151  CG  PRO A  19      27.960  28.981 -21.310  1.00 57.56           C  
ANISOU  151  CG  PRO A  19     5757  10915   5199   2254    966   2750       C  
ATOM    152  CD  PRO A  19      27.026  30.068 -21.740  1.00 55.53           C  
ANISOU  152  CD  PRO A  19     5350  10824   4924   2429   1003   2929       C  
ATOM    153  N   TYR A  20      25.888  28.379 -18.864  1.00 52.75           N  
ANISOU  153  N   TYR A  20     5221  10203   4618   1921    726   2373       N  
ATOM    154  CA  TYR A  20      25.644  28.018 -17.472  1.00 51.06           C  
ANISOU  154  CA  TYR A  20     5095   9785   4520   1725    657   2225       C  
ATOM    155  C   TYR A  20      24.132  27.923 -17.211  1.00 51.19           C  
ANISOU  155  C   TYR A  20     5042  10010   4399   1703    532   2078       C  
ATOM    156  O   TYR A  20      23.640  26.908 -16.712  1.00 52.49           O  
ANISOU  156  O   TYR A  20     5249  10235   4459   1544    418   1793       O  
ATOM    157  CB  TYR A  20      26.321  29.009 -16.524  1.00 48.19           C  
ANISOU  157  CB  TYR A  20     4768   9027   4514   1709    758   2440       C  
ATOM    158  CG  TYR A  20      26.002  28.730 -15.069  1.00 51.42           C  
ANISOU  158  CG  TYR A  20     5253   9232   5051   1527    688   2310       C  
ATOM    159  CD1 TYR A  20      26.660  27.727 -14.373  1.00 46.43           C  
ANISOU  159  CD1 TYR A  20     4746   8449   4445   1338    678   2126       C  
ATOM    160  CD2 TYR A  20      25.031  29.465 -14.401  1.00 50.36           C  
ANISOU  160  CD2 TYR A  20     5058   9061   5014   1543    638   2364       C  
ATOM    161  CE1 TYR A  20      26.365  27.472 -13.054  1.00 47.31           C  
ANISOU  161  CE1 TYR A  20     4909   8333   4735   1159    611   1948       C  
ATOM    162  CE2 TYR A  20      24.721  29.214 -13.082  1.00 47.84           C  
ANISOU  162  CE2 TYR A  20     4796   8554   4827   1388    559   2237       C  
ATOM    163  CZ  TYR A  20      25.390  28.217 -12.412  1.00 44.93           C  
ANISOU  163  CZ  TYR A  20     4540   7982   4549   1180    545   1984       C  
ATOM    164  OH  TYR A  20      25.086  27.959 -11.104  1.00 34.94           O  
ANISOU  164  OH  TYR A  20     3317   6472   3487   1002    468   1772       O  
ATOM    165  N   PHE A  21      23.402  28.964 -17.603  1.00 45.32           N  
ANISOU  165  N   PHE A  21     4184   9373   3663   1859    561   2257       N  
ATOM    166  CA  PHE A  21      21.958  29.025 -17.411  1.00 45.22           C  
ANISOU  166  CA  PHE A  21     4098   9540   3542   1853    456   2141       C  
ATOM    167  C   PHE A  21      21.197  27.994 -18.239  1.00 50.22           C  
ANISOU  167  C   PHE A  21     4680  10518   3883   1846    350   1874       C  
ATOM    168  O   PHE A  21      20.094  27.575 -17.872  1.00 52.43           O  
ANISOU  168  O   PHE A  21     4932  10902   4085   1763    237   1663       O  
ATOM    169  CB  PHE A  21      21.443  30.424 -17.736  1.00 45.47           C  
ANISOU  169  CB  PHE A  21     4025   9594   3657   2021    541   2405       C  
ATOM    170  CG  PHE A  21      21.856  31.462 -16.744  1.00 48.84           C  
ANISOU  170  CG  PHE A  21     4486   9656   4416   1992    623   2602       C  
ATOM    171  CD1 PHE A  21      21.983  31.142 -15.400  1.00 47.90           C  
ANISOU  171  CD1 PHE A  21     4459   9274   4466   1819    555   2492       C  
ATOM    172  CD2 PHE A  21      22.111  32.762 -17.148  1.00 56.35           C  
ANISOU  172  CD2 PHE A  21     5368  10516   5527   2128    770   2881       C  
ATOM    173  CE1 PHE A  21      22.363  32.099 -14.478  1.00 49.41           C  
ANISOU  173  CE1 PHE A  21     4674   9103   4996   1786    624   2642       C  
ATOM    174  CE2 PHE A  21      22.493  33.724 -16.234  1.00 58.28           C  
ANISOU  174  CE2 PHE A  21     5640  10397   6108   2075    847   3018       C  
ATOM    175  CZ  PHE A  21      22.618  33.392 -14.893  1.00 50.59           C  
ANISOU  175  CZ  PHE A  21     4759   9147   5314   1902    770   2888       C  
ATOM    176  N   ALA A  22      21.788  27.587 -19.354  1.00 49.13           N  
ANISOU  176  N   ALA A  22     4523  10536   3607   1931    387   1874       N  
ATOM    177  CA  ALA A  22      21.163  26.607 -20.227  1.00 55.15           C  
ANISOU  177  CA  ALA A  22     5226  11605   4124   1933    295   1621       C  
ATOM    178  C   ALA A  22      21.178  25.225 -19.577  1.00 49.15           C  
ANISOU  178  C   ALA A  22     4553  10771   3352   1699    191   1274       C  
ATOM    179  O   ALA A  22      20.323  24.385 -19.874  1.00 48.14           O  
ANISOU  179  O   ALA A  22     4370  10827   3094   1642     92   1007       O  
ATOM    180  CB  ALA A  22      21.855  26.580 -21.592  1.00 57.59           C  
ANISOU  180  CB  ALA A  22     5486  12091   4303   2096    365   1728       C  
ATOM    181  N   GLN A  23      22.146  24.994 -18.690  1.00 48.61           N  
ANISOU  181  N   GLN A  23     4612  10418   3439   1562    225   1277       N  
ATOM    182  CA  GLN A  23      22.154  23.780 -17.884  1.00 47.72           C  
ANISOU  182  CA  GLN A  23     4582  10193   3356   1327    144    961       C  
ATOM    183  C   GLN A  23      20.849  23.707 -17.100  1.00 46.84           C  
ANISOU  183  C   GLN A  23     4428  10101   3268   1236     40    796       C  
ATOM    184  O   GLN A  23      20.201  22.664 -17.038  1.00 49.14           O  
ANISOU  184  O   GLN A  23     4699  10459   3513   1109    -50    491       O  
ATOM    185  CB  GLN A  23      23.312  23.787 -16.887  1.00 48.94           C  
ANISOU  185  CB  GLN A  23     4876  10020   3697   1207    215   1031       C  
ATOM    186  CG  GLN A  23      24.700  23.828 -17.482  1.00 57.47           C  
ANISOU  186  CG  GLN A  23     6020  11010   4807   1266    330   1185       C  
ATOM    187  CD  GLN A  23      25.758  23.713 -16.403  1.00 60.52           C  
ANISOU  187  CD  GLN A  23     6543  11055   5399   1120    404   1209       C  
ATOM    188  OE1 GLN A  23      26.131  24.706 -15.776  1.00 61.75           O  
ANISOU  188  OE1 GLN A  23     6721  10990   5753   1162    487   1455       O  
ATOM    189  NE2 GLN A  23      26.221  22.491 -16.156  1.00 57.99           N  
ANISOU  189  NE2 GLN A  23     6305  10667   5063    941    380    944       N  
ATOM    190  N   ALA A  24      20.477  24.826 -16.494  1.00 42.84           N  
ANISOU  190  N   ALA A  24     3902   9509   2866   1301     62   1006       N  
ATOM    191  CA  ALA A  24      19.265  24.891 -15.689  1.00 44.95           C  
ANISOU  191  CA  ALA A  24     4133   9770   3176   1222    -31    879       C  
ATOM    192  C   ALA A  24      18.033  24.644 -16.568  1.00 46.99           C  
ANISOU  192  C   ALA A  24     4273  10316   3267   1292    -93    739       C  
ATOM    193  O   ALA A  24      17.174  23.803 -16.272  1.00 43.20           O  
ANISOU  193  O   ALA A  24     3774   9867   2774   1163   -182    457       O  
ATOM    194  CB  ALA A  24      19.176  26.247 -15.007  1.00 42.86           C  
ANISOU  194  CB  ALA A  24     3863   9352   3071   1305     12   1167       C  
ATOM    195  N   TYR A  25      17.966  25.374 -17.669  1.00 52.11           N  
ANISOU  195  N   TYR A  25     4837  11160   3801   1499    -34    942       N  
ATOM    196  CA  TYR A  25      16.835  25.259 -18.574  1.00 50.88           C  
ANISOU  196  CA  TYR A  25     4561  11294   3475   1592    -80    842       C  
ATOM    197  C   TYR A  25      16.668  23.811 -19.050  1.00 50.06           C  
ANISOU  197  C   TYR A  25     4442  11308   3270   1487   -152    509       C  
ATOM    198  O   TYR A  25      15.559  23.269 -19.028  1.00 47.71           O  
ANISOU  198  O   TYR A  25     4087  11105   2936   1426   -229    287       O  
ATOM    199  CB  TYR A  25      17.004  26.220 -19.743  1.00 55.60           C  
ANISOU  199  CB  TYR A  25     5074  12085   3968   1839     13   1122       C  
ATOM    200  CG  TYR A  25      15.903  26.128 -20.772  1.00 57.85           C  
ANISOU  200  CG  TYR A  25     5227  12695   4058   1957    -26   1032       C  
ATOM    201  CD1 TYR A  25      14.719  26.857 -20.633  1.00 57.33           C  
ANISOU  201  CD1 TYR A  25     5092  12709   3981   2016    -43   1084       C  
ATOM    202  CD2 TYR A  25      16.041  25.305 -21.879  1.00 58.71           C  
ANISOU  202  CD2 TYR A  25     5280  13030   3997   2009    -46    890       C  
ATOM    203  CE1 TYR A  25      13.712  26.768 -21.583  1.00 60.08           C  
ANISOU  203  CE1 TYR A  25     5320  13360   4148   2128    -75   1001       C  
ATOM    204  CE2 TYR A  25      15.044  25.212 -22.833  1.00 61.12           C  
ANISOU  204  CE2 TYR A  25     5456  13642   4125   2126    -82    805       C  
ATOM    205  CZ  TYR A  25      13.887  25.944 -22.683  1.00 62.58           C  
ANISOU  205  CZ  TYR A  25     5575  13906   4296   2187    -94    862       C  
ATOM    206  OH  TYR A  25      12.907  25.834 -23.641  1.00 63.18           O  
ANISOU  206  OH  TYR A  25     5523  14291   4192   2306   -127    773       O  
ATOM    207  N   ASP A  26      17.772  23.182 -19.445  1.00 47.11           N  
ANISOU  207  N   ASP A  26     4122  10901   2875   1461   -121    478       N  
ATOM    208  CA  ASP A  26      17.752  21.790 -19.902  1.00 55.69           C  
ANISOU  208  CA  ASP A  26     5197  12065   3897   1358   -178    175       C  
ATOM    209  C   ASP A  26      17.229  20.821 -18.848  1.00 52.72           C  
ANISOU  209  C   ASP A  26     4867  11507   3659   1123   -250   -115       C  
ATOM    210  O   ASP A  26      16.389  19.955 -19.128  1.00 46.40           O  
ANISOU  210  O   ASP A  26     3998  10806   2825   1066   -310   -360       O  
ATOM    211  CB  ASP A  26      19.143  21.347 -20.374  1.00 50.93           C  
ANISOU  211  CB  ASP A  26     4664  11410   3276   1356   -123    211       C  
ATOM    212  CG  ASP A  26      19.556  22.016 -21.675  1.00 55.57           C  
ANISOU  212  CG  ASP A  26     5183  12222   3710   1595    -55    442       C  
ATOM    213  OD1 ASP A  26      18.695  22.680 -22.290  1.00 53.06           O  
ANISOU  213  OD1 ASP A  26     4750  12127   3285   1757    -57    537       O  
ATOM    214  OD2 ASP A  26      20.733  21.871 -22.082  1.00 54.85           O  
ANISOU  214  OD2 ASP A  26     5150  12080   3610   1622      7    528       O  
ATOM    215  N   PHE A  27      17.733  20.960 -17.627  1.00 42.89           N  
ANISOU  215  N   PHE A  27     3730   9984   2583    991   -235    -81       N  
ATOM    216  CA  PHE A  27      17.231  20.138 -16.554  1.00 41.99           C  
ANISOU  216  CA  PHE A  27     3656   9678   2622    780   -289   -327       C  
ATOM    217  C   PHE A  27      15.737  20.361 -16.370  1.00 44.66           C  
ANISOU  217  C   PHE A  27     3910  10103   2955    795   -345   -399       C  
ATOM    218  O   PHE A  27      14.967  19.404 -16.290  1.00 45.39           O  
ANISOU  218  O   PHE A  27     3968  10190   3086    691   -389   -644       O  
ATOM    219  CB  PHE A  27      17.954  20.418 -15.231  1.00 41.02           C  
ANISOU  219  CB  PHE A  27     3652   9260   2673    659   -263   -256       C  
ATOM    220  CG  PHE A  27      17.346  19.697 -14.075  1.00 40.01           C  
ANISOU  220  CG  PHE A  27     3556   8927   2718    460   -309   -482       C  
ATOM    221  CD1 PHE A  27      17.704  18.392 -13.794  1.00 45.87           C  
ANISOU  221  CD1 PHE A  27     4348   9514   3566    291   -305   -710       C  
ATOM    222  CD2 PHE A  27      16.390  20.311 -13.285  1.00 39.40           C  
ANISOU  222  CD2 PHE A  27     3458   8799   2714    452   -346   -453       C  
ATOM    223  CE1 PHE A  27      17.134  17.716 -12.729  1.00 48.50           C  
ANISOU  223  CE1 PHE A  27     4712   9632   4084    125   -322   -884       C  
ATOM    224  CE2 PHE A  27      15.808  19.645 -12.238  1.00 39.40           C  
ANISOU  224  CE2 PHE A  27     3492   8597   2884    283   -373   -643       C  
ATOM    225  CZ  PHE A  27      16.182  18.346 -11.953  1.00 47.10           C  
ANISOU  225  CZ  PHE A  27     4518   9406   3971    125   -354   -849       C  
HETATM  226  N   MSE A  28      15.322  21.622 -16.303  1.00 42.16           N  
ANISOU  226  N   MSE A  28     3561   9852   2605    927   -334   -174       N  
HETATM  227  CA  MSE A  28      13.906  21.918 -16.091  1.00 50.86           C  
ANISOU  227  CA  MSE A  28     4594  11024   3705    941   -383   -228       C  
HETATM  228  C   MSE A  28      13.015  21.353 -17.195  1.00 56.42           C  
ANISOU  228  C   MSE A  28     5184  11993   4258   1011   -417   -383       C  
HETATM  229  O   MSE A  28      11.969  20.748 -16.919  1.00 45.35           O  
ANISOU  229  O   MSE A  28     3748  10582   2899    924   -466   -587       O  
HETATM  230  CB  MSE A  28      13.689  23.417 -15.930  1.00 50.75           C  
ANISOU  230  CB  MSE A  28     4563  11034   3687   1085   -355     63       C  
HETATM  231  CG  MSE A  28      14.319  23.945 -14.663  1.00 48.13           C  
ANISOU  231  CG  MSE A  28     4328  10421   3537   1002   -339    186       C  
HETATM  232 SE   MSE A  28      14.317  25.871 -14.600  0.57 48.67          SE  
ANISOU  232 SE   MSE A  28     4368  10477   3645   1204   -276    606      SE  
HETATM  233  CE  MSE A  28      12.467  26.140 -14.039  1.00 45.91           C  
ANISOU  233  CE  MSE A  28     3963  10154   3326   1165   -360    482       C  
ATOM    234  N   GLU A  29      13.436  21.546 -18.444  1.00 54.86           N  
ANISOU  234  N   GLU A  29     4925  12029   3890   1176   -385   -281       N  
ATOM    235  CA  GLU A  29      12.691  20.996 -19.562  1.00 56.64           C  
ANISOU  235  CA  GLU A  29     5032  12527   3961   1257   -418   -430       C  
ATOM    236  C   GLU A  29      12.531  19.494 -19.356  1.00 56.95           C  
ANISOU  236  C   GLU A  29     5081  12474   4083   1077   -462   -750       C  
ATOM    237  O   GLU A  29      11.441  18.954 -19.528  1.00 50.48           O  
ANISOU  237  O   GLU A  29     4185  11746   3249   1053   -508   -936       O  
ATOM    238  CB  GLU A  29      13.400  21.305 -20.877  1.00 63.43           C  
ANISOU  238  CB  GLU A  29     5837  13622   4642   1449   -371   -278       C  
ATOM    239  CG  GLU A  29      13.236  22.756 -21.321  1.00 72.64           C  
ANISOU  239  CG  GLU A  29     6952  14933   5717   1664   -316     35       C  
ATOM    240  CD  GLU A  29      11.882  23.031 -21.981  1.00 82.20           C  
ANISOU  240  CD  GLU A  29     8032  16408   6793   1785   -350     -7       C  
ATOM    241  OE1 GLU A  29      11.729  22.701 -23.184  1.00 88.27           O  
ANISOU  241  OE1 GLU A  29     8698  17451   7389   1911   -355    -67       O  
ATOM    242  OE2 GLU A  29      10.978  23.578 -21.302  1.00 79.88           O  
ANISOU  242  OE2 GLU A  29     7737  16049   6564   1757   -371     18       O  
ATOM    243  N   LYS A  30      13.607  18.821 -18.953  1.00 55.96           N  
ANISOU  243  N   LYS A  30     5050  12151   4062    949   -440   -806       N  
ATOM    244  CA  LYS A  30      13.535  17.378 -18.734  1.00 54.95           C  
ANISOU  244  CA  LYS A  30     4933  11906   4042    778   -463  -1087       C  
ATOM    245  C   LYS A  30      12.604  17.013 -17.567  1.00 51.53           C  
ANISOU  245  C   LYS A  30     4527  11264   3788    623   -488  -1223       C  
ATOM    246  O   LYS A  30      11.810  16.068 -17.667  1.00 51.80           O  
ANISOU  246  O   LYS A  30     4505  11316   3862    559   -515  -1436       O  
ATOM    247  CB  LYS A  30      14.929  16.761 -18.537  1.00 53.02           C  
ANISOU  247  CB  LYS A  30     4789  11480   3877    676   -424  -1103       C  
ATOM    248  CG  LYS A  30      14.891  15.236 -18.505  1.00 54.52           C  
ANISOU  248  CG  LYS A  30     4973  11571   4170    526   -435  -1373       C  
ATOM    249  CD  LYS A  30      16.252  14.589 -18.271  1.00 58.78           C  
ANISOU  249  CD  LYS A  30     5616  11915   4803    417   -392  -1392       C  
ATOM    250  CE  LYS A  30      16.088  13.067 -18.192  1.00 62.15           C  
ANISOU  250  CE  LYS A  30     6025  12233   5354    275   -394  -1646       C  
ATOM    251  NZ  LYS A  30      17.332  12.337 -17.816  1.00 60.89           N  
ANISOU  251  NZ  LYS A  30     5971  11845   5319    149   -347  -1675       N  
ATOM    252  N   TRP A  31      12.694  17.758 -16.467  1.00 45.95           N  
ANISOU  252  N   TRP A  31     3904  10360   3196    573   -476  -1094       N  
ATOM    253  CA  TRP A  31      11.806  17.513 -15.336  1.00 46.87           C  
ANISOU  253  CA  TRP A  31     4050  10277   3479    443   -495  -1197       C  
ATOM    254  C   TRP A  31      10.337  17.591 -15.762  1.00 49.45           C  
ANISOU  254  C   TRP A  31     4271  10792   3727    514   -539  -1275       C  
ATOM    255  O   TRP A  31       9.559  16.659 -15.530  1.00 49.70           O  
ANISOU  255  O   TRP A  31     4277  10763   3845    422   -555  -1470       O  
ATOM    256  CB  TRP A  31      12.069  18.498 -14.195  1.00 44.69           C  
ANISOU  256  CB  TRP A  31     3864   9807   3311    413   -483  -1026       C  
ATOM    257  CG  TRP A  31      11.187  18.247 -13.006  1.00 44.03           C  
ANISOU  257  CG  TRP A  31     3817   9510   3402    288   -499  -1124       C  
ATOM    258  CD1 TRP A  31       9.986  18.830 -12.737  1.00 44.79           C  
ANISOU  258  CD1 TRP A  31     3873   9653   3492    329   -534  -1101       C  
ATOM    259  CD2 TRP A  31      11.439  17.334 -11.936  1.00 43.07           C  
ANISOU  259  CD2 TRP A  31     3785   9090   3490    112   -473  -1246       C  
ATOM    260  NE1 TRP A  31       9.472  18.338 -11.565  1.00 41.76           N  
ANISOU  260  NE1 TRP A  31     3549   9020   3297    191   -534  -1202       N  
ATOM    261  CE2 TRP A  31      10.344  17.418 -11.053  1.00 45.10           C  
ANISOU  261  CE2 TRP A  31     4051   9228   3855     63   -493  -1283       C  
ATOM    262  CE3 TRP A  31      12.484  16.453 -11.639  1.00 43.55           C  
ANISOU  262  CE3 TRP A  31     3920   8968   3659      0   -428  -1313       C  
ATOM    263  CZ2 TRP A  31      10.268  16.655  -9.884  1.00 43.62           C  
ANISOU  263  CZ2 TRP A  31     3947   8751   3877    -80   -464  -1370       C  
ATOM    264  CZ3 TRP A  31      12.406  15.696 -10.481  1.00 43.16           C  
ANISOU  264  CZ3 TRP A  31     3950   8628   3821   -143   -397  -1399       C  
ATOM    265  CH2 TRP A  31      11.310  15.806  -9.614  1.00 39.49           C  
ANISOU  265  CH2 TRP A  31     3494   8055   3455   -175   -413  -1419       C  
ATOM    266  N   LEU A  32       9.969  18.709 -16.384  1.00 48.61           N  
ANISOU  266  N   LEU A  32     4100  10908   3461    686   -550  -1108       N  
ATOM    267  CA  LEU A  32       8.598  18.939 -16.837  1.00 52.20           C  
ANISOU  267  CA  LEU A  32     4452  11559   3822    772   -590  -1157       C  
ATOM    268  C   LEU A  32       8.121  17.877 -17.829  1.00 54.73           C  
ANISOU  268  C   LEU A  32     4668  12072   4054    792   -614  -1375       C  
ATOM    269  O   LEU A  32       6.937  17.530 -17.857  1.00 57.96           O  
ANISOU  269  O   LEU A  32     5010  12543   4468    780   -649  -1515       O  
ATOM    270  CB  LEU A  32       8.463  20.341 -17.446  1.00 51.95           C  
ANISOU  270  CB  LEU A  32     4370  11741   3630    972   -581   -909       C  
ATOM    271  CG  LEU A  32       8.839  21.491 -16.499  1.00 55.63           C  
ANISOU  271  CG  LEU A  32     4921  12027   4189    972   -556   -677       C  
ATOM    272  CD1 LEU A  32       8.773  22.833 -17.213  1.00 59.89           C  
ANISOU  272  CD1 LEU A  32     5402  12773   4581   1185   -527   -409       C  
ATOM    273  CD2 LEU A  32       7.948  21.497 -15.256  1.00 55.57           C  
ANISOU  273  CD2 LEU A  32     4960  11805   4347    843   -590   -754       C  
ATOM    274  N   GLY A  33       9.044  17.360 -18.636  1.00 51.77           N  
ANISOU  274  N   GLY A  33     4277  11790   3603    824   -596  -1405       N  
ATOM    275  CA  GLY A  33       8.722  16.355 -19.634  1.00 53.70           C  
ANISOU  275  CA  GLY A  33     4414  12227   3761    852   -620  -1611       C  
ATOM    276  C   GLY A  33       8.263  15.025 -19.057  1.00 56.27           C  
ANISOU  276  C   GLY A  33     4748  12370   4263    677   -630  -1862       C  
ATOM    277  O   GLY A  33       7.617  14.239 -19.747  1.00 57.66           O  
ANISOU  277  O   GLY A  33     4818  12702   4389    699   -658  -2050       O  
ATOM    278  N   GLY A  34       8.616  14.752 -17.802  1.00 53.12           N  
ANISOU  278  N   GLY A  34     4469  11642   4072    512   -602  -1859       N  
ATOM    279  CA  GLY A  34       8.115  13.570 -17.116  1.00 55.19           C  
ANISOU  279  CA  GLY A  34     4745  11704   4521    357   -595  -2055       C  
ATOM    280  C   GLY A  34       9.129  12.471 -16.835  1.00 57.60           C  
ANISOU  280  C   GLY A  34     5117  11806   4963    227   -551  -2141       C  
ATOM    281  O   GLY A  34       8.767  11.417 -16.300  1.00 56.30           O  
ANISOU  281  O   GLY A  34     4960  11474   4958    109   -534  -2288       O  
ATOM    282  N   ALA A  35      10.393  12.714 -17.181  1.00 56.56           N  
ANISOU  282  N   ALA A  35     5034  11684   4773    254   -529  -2038       N  
ATOM    283  CA  ALA A  35      11.456  11.728 -16.983  1.00 51.20           C  
ANISOU  283  CA  ALA A  35     4421  10820   4212    139   -485  -2105       C  
ATOM    284  C   ALA A  35      11.342  11.046 -15.631  1.00 49.83           C  
ANISOU  284  C   ALA A  35     4339  10306   4287    -29   -444  -2155       C  
ATOM    285  O   ALA A  35      11.072  11.701 -14.619  1.00 49.45           O  
ANISOU  285  O   ALA A  35     4363  10100   4325    -65   -438  -2051       O  
ATOM    286  CB  ALA A  35      12.805  12.383 -17.112  1.00 49.56           C  
ANISOU  286  CB  ALA A  35     4293  10593   3944    173   -460  -1934       C  
ATOM    287  N   ARG A  36      11.553   9.734 -15.604  1.00 49.60           N  
ANISOU  287  N   ARG A  36     4305  10167   4373   -122   -413  -2303       N  
ATOM    288  CA  ARG A  36      11.459   9.000 -14.343  1.00 55.34           C  
ANISOU  288  CA  ARG A  36     5105  10593   5329   -261   -359  -2339       C  
ATOM    289  C   ARG A  36      12.796   8.950 -13.598  1.00 49.97           C  
ANISOU  289  C   ARG A  36     4558   9662   4765   -345   -300  -2230       C  
ATOM    290  O   ARG A  36      12.845   8.584 -12.426  1.00 48.66           O  
ANISOU  290  O   ARG A  36     4446   9273   4771   -440   -241  -2227       O  
ATOM    291  CB  ARG A  36      10.902   7.590 -14.564  1.00 63.18           C  
ANISOU  291  CB  ARG A  36     5972  11644   6391   -309   -332  -2576       C  
ATOM    292  CG  ARG A  36       9.378   7.537 -14.680  1.00 72.14           C  
ANISOU  292  CG  ARG A  36     6993  12921   7498   -267   -370  -2694       C  
ATOM    293  CD  ARG A  36       8.887   6.101 -14.884  1.00 80.79           C  
ANISOU  293  CD  ARG A  36     7961  14060   8677   -315   -339  -2938       C  
ATOM    294  NE  ARG A  36       9.376   5.217 -13.827  1.00 84.12           N  
ANISOU  294  NE  ARG A  36     8437  14222   9304   -439   -248  -2963       N  
ATOM    295  CZ  ARG A  36       8.690   4.905 -12.731  1.00 86.75           C  
ANISOU  295  CZ  ARG A  36     8782  14396   9783   -501   -204  -2988       C  
ATOM    296  NH1 ARG A  36       7.466   5.390 -12.544  1.00 86.94           N  
ANISOU  296  NH1 ARG A  36     8768  14488   9779   -462   -247  -3001       N  
ATOM    297  NH2 ARG A  36       9.228   4.101 -11.822  1.00 85.98           N  
ANISOU  297  NH2 ARG A  36     8735  14079   9856   -596   -114  -2996       N  
ATOM    298  N   GLU A  37      13.883   9.296 -14.281  1.00 47.97           N  
ANISOU  298  N   GLU A  37     4337   9482   4409   -302   -305  -2156       N  
ATOM    299  CA  GLU A  37      15.178   9.365 -13.603  1.00 48.25           C  
ANISOU  299  CA  GLU A  37     4501   9287   4546   -375   -253  -2046       C  
ATOM    300  C   GLU A  37      16.139  10.368 -14.240  1.00 42.98           C  
ANISOU  300  C   GLU A  37     3855   8754   3720   -292   -269  -1915       C  
ATOM    301  O   GLU A  37      15.916  10.836 -15.355  1.00 44.30           O  
ANISOU  301  O   GLU A  37     3934   9209   3689   -167   -314  -1910       O  
ATOM    302  CB  GLU A  37      15.815   7.977 -13.426  1.00 48.31           C  
ANISOU  302  CB  GLU A  37     4513   9153   4689   -477   -187  -2159       C  
ATOM    303  CG  GLU A  37      16.325   7.286 -14.678  1.00 52.26           C  
ANISOU  303  CG  GLU A  37     4942   9827   5087   -444   -198  -2265       C  
ATOM    304  CD  GLU A  37      17.181   6.065 -14.343  1.00 54.18           C  
ANISOU  304  CD  GLU A  37     5193   9917   5476   -552   -118  -2349       C  
ATOM    305  OE1 GLU A  37      16.650   5.124 -13.713  1.00 57.99           O  
ANISOU  305  OE1 GLU A  37     5618  10316   6099   -625    -63  -2468       O  
ATOM    306  OE2 GLU A  37      18.385   6.048 -14.689  1.00 51.96           O  
ANISOU  306  OE2 GLU A  37     4979   9596   5170   -560   -103  -2290       O  
ATOM    307  N   PHE A  38      17.187  10.709 -13.499  1.00 42.81           N  
ANISOU  307  N   PHE A  38     3952   8526   3786   -349   -227  -1799       N  
ATOM    308  CA  PHE A  38      18.085  11.794 -13.860  1.00 40.96           C  
ANISOU  308  CA  PHE A  38     3757   8384   3423   -272   -234  -1644       C  
ATOM    309  C   PHE A  38      19.514  11.441 -13.503  1.00 45.15           C  
ANISOU  309  C   PHE A  38     4398   8707   4050   -356   -177  -1605       C  
ATOM    310  O   PHE A  38      19.785  10.894 -12.435  1.00 48.08           O  
ANISOU  310  O   PHE A  38     4849   8798   4621   -473   -129  -1621       O  
ATOM    311  CB  PHE A  38      17.691  13.094 -13.146  1.00 35.52           C  
ANISOU  311  CB  PHE A  38     3094   7676   2727   -230   -253  -1499       C  
ATOM    312  CG  PHE A  38      16.268  13.499 -13.387  1.00 40.56           C  
ANISOU  312  CG  PHE A  38     3633   8494   3284   -150   -305  -1523       C  
ATOM    313  CD1 PHE A  38      15.952  14.421 -14.371  1.00 40.72           C  
ANISOU  313  CD1 PHE A  38     3571   8811   3089     14   -346  -1428       C  
ATOM    314  CD2 PHE A  38      15.240  12.940 -12.642  1.00 41.50           C  
ANISOU  314  CD2 PHE A  38     3742   8484   3540   -227   -306  -1627       C  
ATOM    315  CE1 PHE A  38      14.635  14.781 -14.610  1.00 42.22           C  
ANISOU  315  CE1 PHE A  38     3668   9166   3206     90   -391  -1450       C  
ATOM    316  CE2 PHE A  38      13.921  13.293 -12.881  1.00 42.16           C  
ANISOU  316  CE2 PHE A  38     3738   8732   3550   -156   -354  -1656       C  
ATOM    317  CZ  PHE A  38      13.619  14.214 -13.867  1.00 41.00           C  
ANISOU  317  CZ  PHE A  38     3506   8880   3191     -2   -398  -1575       C  
ATOM    318  N   VAL A  39      20.418  11.762 -14.418  1.00 45.80           N  
ANISOU  318  N   VAL A  39     4487   8932   3983   -280   -177  -1539       N  
ATOM    319  CA  VAL A  39      21.847  11.664 -14.176  1.00 49.34           C  
ANISOU  319  CA  VAL A  39     5047   9210   4490   -338   -123  -1475       C  
ATOM    320  C   VAL A  39      22.371  13.056 -13.845  1.00 48.21           C  
ANISOU  320  C   VAL A  39     4969   9067   4282   -273   -113  -1276       C  
ATOM    321  O   VAL A  39      22.501  13.896 -14.738  1.00 56.52           O  
ANISOU  321  O   VAL A  39     5989  10351   5136   -121   -124  -1147       O  
ATOM    322  CB  VAL A  39      22.598  11.122 -15.424  1.00 45.81           C  
ANISOU  322  CB  VAL A  39     4578   8913   3913   -285   -117  -1515       C  
ATOM    323  CG1 VAL A  39      24.080  11.022 -15.134  1.00 46.36           C  
ANISOU  323  CG1 VAL A  39     4775   8789   4053   -348    -55  -1446       C  
ATOM    324  CG2 VAL A  39      22.040   9.763 -15.833  1.00 46.03           C  
ANISOU  324  CG2 VAL A  39     4524   8972   3994   -336   -130  -1714       C  
ATOM    325  N   LEU A  40      22.644  13.304 -12.564  1.00 37.94           N  
ANISOU  325  N   LEU A  40     3753   7510   3151   -372    -83  -1236       N  
ATOM    326  CA  LEU A  40      23.226  14.568 -12.136  1.00 43.78           C  
ANISOU  326  CA  LEU A  40     4557   8225   3851   -323    -63  -1053       C  
ATOM    327  C   LEU A  40      24.705  14.360 -11.742  1.00 48.05           C  
ANISOU  327  C   LEU A  40     5223   8547   4485   -407     13  -1018       C  
ATOM    328  O   LEU A  40      25.262  13.278 -11.945  1.00 50.25           O  
ANISOU  328  O   LEU A  40     5529   8727   4839   -484     39  -1124       O  
ATOM    329  CB  LEU A  40      22.427  15.162 -10.980  1.00 47.82           C  
ANISOU  329  CB  LEU A  40     5065   8630   4474   -362    -88  -1032       C  
ATOM    330  CG  LEU A  40      20.906  15.043 -11.126  1.00 53.92           C  
ANISOU  330  CG  LEU A  40     5732   9533   5223   -324   -147  -1111       C  
ATOM    331  CD1 LEU A  40      20.189  15.896 -10.083  1.00 50.99           C  
ANISOU  331  CD1 LEU A  40     5363   9082   4929   -329   -173  -1046       C  
ATOM    332  CD2 LEU A  40      20.449  15.411 -12.539  1.00 61.28           C  
ANISOU  332  CD2 LEU A  40     6562  10806   5917   -160   -187  -1065       C  
ATOM    333  N   HIS A  41      25.342  15.389 -11.193  1.00 46.39           N  
ANISOU  333  N   HIS A  41     5086   8265   4275   -384     58   -860       N  
ATOM    334  CA  HIS A  41      26.775  15.316 -10.879  1.00 47.01           C  
ANISOU  334  CA  HIS A  41     5287   8142   4433   -448    153   -809       C  
ATOM    335  C   HIS A  41      27.088  15.698  -9.442  1.00 45.22           C  
ANISOU  335  C   HIS A  41     5137   7650   4394   -562    195   -799       C  
ATOM    336  O   HIS A  41      26.405  16.526  -8.845  1.00 48.15           O  
ANISOU  336  O   HIS A  41     5476   8026   4792   -530    166   -728       O  
ATOM    337  CB  HIS A  41      27.585  16.234 -11.799  1.00 46.72           C  
ANISOU  337  CB  HIS A  41     5275   8250   4226   -278    239   -565       C  
ATOM    338  CG  HIS A  41      27.656  15.768 -13.218  1.00 50.29           C  
ANISOU  338  CG  HIS A  41     5680   8915   4514   -176    216   -580       C  
ATOM    339  ND1 HIS A  41      26.859  16.292 -14.213  1.00 54.46           N  
ANISOU  339  ND1 HIS A  41     6101   9737   4856     -4    167   -491       N  
ATOM    340  CD2 HIS A  41      28.435  14.835 -13.812  1.00 50.35           C  
ANISOU  340  CD2 HIS A  41     5725   8885   4519   -217    237   -673       C  
ATOM    341  CE1 HIS A  41      27.143  15.700 -15.357  1.00 61.31           C  
ANISOU  341  CE1 HIS A  41     6941  10745   5608     53    161   -540       C  
ATOM    342  NE2 HIS A  41      28.097  14.810 -15.142  1.00 59.28           N  
ANISOU  342  NE2 HIS A  41     6772  10295   5458    -75    202   -650       N  
ATOM    343  N   THR A  42      28.140  15.100  -8.894  1.00 43.53           N  
ANISOU  343  N   THR A  42     5021   7170   4349   -685    260   -853       N  
ATOM    344  CA  THR A  42      28.634  15.462  -7.568  1.00 41.39           C  
ANISOU  344  CA  THR A  42     4832   6593   4300   -783    314   -829       C  
ATOM    345  C   THR A  42      30.169  15.367  -7.604  1.00 42.89           C  
ANISOU  345  C   THR A  42     5129   6566   4600   -807    426   -742       C  
ATOM    346  O   THR A  42      30.736  14.960  -8.613  1.00 44.36           O  
ANISOU  346  O   THR A  42     5327   6896   4631   -772    468   -746       O  
ATOM    347  CB  THR A  42      28.028  14.551  -6.456  1.00 46.39           C  
ANISOU  347  CB  THR A  42     5447   7004   5174   -882    272   -945       C  
ATOM    348  OG1 THR A  42      28.389  15.045  -5.160  1.00 46.58           O  
ANISOU  348  OG1 THR A  42     5550   6745   5405   -907    313   -878       O  
ATOM    349  CG2 THR A  42      28.507  13.119  -6.595  1.00 44.98           C  
ANISOU  349  CG2 THR A  42     5286   6713   5091   -902    316   -982       C  
ATOM    350  N   SER A  43      30.841  15.765  -6.530  1.00 41.12           N  
ANISOU  350  N   SER A  43     4978   6008   4637   -856    475   -664       N  
ATOM    351  CA  SER A  43      32.298  15.626  -6.463  1.00 43.65           C  
ANISOU  351  CA  SER A  43     5400   6104   5083   -891    579   -601       C  
ATOM    352  C   SER A  43      32.674  14.235  -5.942  1.00 42.41           C  
ANISOU  352  C   SER A  43     5294   5830   4990  -1006    589   -784       C  
ATOM    353  O   SER A  43      32.097  13.776  -4.967  1.00 40.80           O  
ANISOU  353  O   SER A  43     5081   5538   4882   -892    539   -745       O  
ATOM    354  CB  SER A  43      32.897  16.695  -5.545  1.00 47.81           C  
ANISOU  354  CB  SER A  43     5968   6319   5879   -851    626   -413       C  
ATOM    355  OG  SER A  43      32.891  17.971  -6.163  1.00 55.90           O  
ANISOU  355  OG  SER A  43     6947   7408   6885   -669    654   -147       O  
ATOM    356  N   GLY A  44      33.623  13.561  -6.589  1.00 36.11           N  
ANISOU  356  N   GLY A  44     4523   5016   4181  -1034    622   -783       N  
ATOM    357  CA  GLY A  44      34.089  12.271  -6.099  1.00 35.37           C  
ANISOU  357  CA  GLY A  44     4448   4812   4178   -918    612   -732       C  
ATOM    358  C   GLY A  44      35.184  12.404  -5.042  1.00 33.34           C  
ANISOU  358  C   GLY A  44     4294   4341   4033   -760    609   -617       C  
ATOM    359  O   GLY A  44      35.523  13.504  -4.631  1.00 29.45           O  
ANISOU  359  O   GLY A  44     3857   3743   3588   -715    626   -578       O  
ATOM    360  N   SER A  45      35.764  11.284  -4.632  1.00 39.46           N  
ANISOU  360  N   SER A  45     5065   5093   4835   -729    627   -610       N  
ATOM    361  CA  SER A  45      36.813  11.294  -3.610  1.00 42.36           C  
ANISOU  361  CA  SER A  45     5475   5352   5269   -635    639   -551       C  
ATOM    362  C   SER A  45      38.075  12.055  -4.042  1.00 37.53           C  
ANISOU  362  C   SER A  45     4927   4655   4676   -598    659   -510       C  
ATOM    363  O   SER A  45      38.882  12.456  -3.200  1.00 35.31           O  
ANISOU  363  O   SER A  45     4655   4301   4459   -523    671   -470       O  
ATOM    364  CB  SER A  45      37.169   9.863  -3.202  1.00 43.07           C  
ANISOU  364  CB  SER A  45     5537   5461   5366   -624    645   -557       C  
ATOM    365  OG  SER A  45      37.687   9.147  -4.313  1.00 48.86           O  
ANISOU  365  OG  SER A  45     6273   6231   6062   -675    660   -579       O  
ATOM    366  N   THR A  46      38.259  12.269  -5.345  1.00 26.91           N  
ANISOU  366  N   THR A  46     3616   3326   3281   -656    666   -526       N  
ATOM    367  CA  THR A  46      39.405  13.060  -5.788  1.00 25.72           C  
ANISOU  367  CA  THR A  46     3542   3063   3168   -627    716   -495       C  
ATOM    368  C   THR A  46      39.047  14.506  -6.089  1.00 29.60           C  
ANISOU  368  C   THR A  46     4022   3475   3750   -626    702   -379       C  
ATOM    369  O   THR A  46      39.859  15.235  -6.652  1.00 33.03           O  
ANISOU  369  O   THR A  46     4454   3840   4254   -586    737   -227       O  
ATOM    370  CB  THR A  46      40.044  12.478  -7.045  1.00 27.96           C  
ANISOU  370  CB  THR A  46     3859   3371   3392   -690    724   -520       C  
ATOM    371  OG1 THR A  46      39.106  12.567  -8.126  1.00 33.99           O  
ANISOU  371  OG1 THR A  46     4627   4244   4044   -912    777   -635       O  
ATOM    372  CG2 THR A  46      40.391  11.019  -6.820  1.00 30.05           C  
ANISOU  372  CG2 THR A  46     4065   3712   3641   -661    687   -515       C  
ATOM    373  N   GLY A  47      37.838  14.919  -5.718  1.00 25.58           N  
ANISOU  373  N   GLY A  47     3470   3009   3242   -665    679   -389       N  
ATOM    374  CA  GLY A  47      37.399  16.282  -5.977  1.00 24.85           C  
ANISOU  374  CA  GLY A  47     3318   2899   3226   -656    716   -203       C  
ATOM    375  C   GLY A  47      37.015  16.558  -7.430  1.00 26.87           C  
ANISOU  375  C   GLY A  47     3518   3405   3286   -690    860    -84       C  
ATOM    376  O   GLY A  47      36.835  17.716  -7.828  1.00 31.99           O  
ANISOU  376  O   GLY A  47     4113   4111   3932   -582    936    147       O  
HETATM  377  N   MSE A  48      36.894  15.508  -8.237  1.00 24.14           N  
ANISOU  377  N   MSE A  48     3173   3274   2726   -760    870   -237       N  
HETATM  378  CA  MSE A  48      36.491  15.668  -9.648  1.00 24.55           C  
ANISOU  378  CA  MSE A  48     3156   3693   2477   -656    920   -158       C  
HETATM  379  C   MSE A  48      35.017  15.239  -9.817  1.00 28.67           C  
ANISOU  379  C   MSE A  48     3588   4508   2797   -681    812   -340       C  
HETATM  380  O   MSE A  48      34.500  14.493  -8.998  1.00 29.08           O  
ANISOU  380  O   MSE A  48     3643   4469   2938   -816    725   -552       O  
HETATM  381  CB  MSE A  48      37.401  14.819 -10.546  1.00 25.00           C  
ANISOU  381  CB  MSE A  48     3254   3803   2440   -639    932   -206       C  
HETATM  382  CG  MSE A  48      38.892  15.096 -10.315  1.00 34.43           C  
ANISOU  382  CG  MSE A  48     4527   4706   3850   -614    994    -62       C  
HETATM  383 SE   MSE A  48      39.383  16.942 -10.789  0.60 40.98          SE  
ANISOU  383 SE   MSE A  48     5309   5512   4749   -411   1102    352      SE  
HETATM  384  CE  MSE A  48      39.290  16.705 -12.647  1.00 31.24           C  
ANISOU  384  CE  MSE A  48     4029   4725   3117   -288   1179    421       C  
ATOM    385  N   PRO A  49      34.334  15.720 -10.872  1.00 27.02           N  
ANISOU  385  N   PRO A  49     3291   4623   2354   -520    782   -236       N  
ATOM    386  CA  PRO A  49      32.904  15.432 -11.034  1.00 28.34           C  
ANISOU  386  CA  PRO A  49     3362   5053   2354   -516    658   -392       C  
ATOM    387  C   PRO A  49      32.645  13.951 -11.242  1.00 32.06           C  
ANISOU  387  C   PRO A  49     3822   5538   2820   -620    545   -663       C  
ATOM    388  O   PRO A  49      33.454  13.245 -11.854  1.00 30.06           O  
ANISOU  388  O   PRO A  49     3607   5263   2554   -625    565   -697       O  
ATOM    389  CB  PRO A  49      32.536  16.166 -12.333  1.00 34.94           C  
ANISOU  389  CB  PRO A  49     4117   6205   2954   -295    656   -200       C  
ATOM    390  CG  PRO A  49      33.594  17.168 -12.528  1.00 34.05           C  
ANISOU  390  CG  PRO A  49     4046   5954   2939   -178    787    110       C  
ATOM    391  CD  PRO A  49      34.846  16.563 -11.959  1.00 29.10           C  
ANISOU  391  CD  PRO A  49     3533   5019   2504   -322    862     39       C  
ATOM    392  N   LYS A  50      31.514  13.482 -10.745  1.00 35.88           N  
ANISOU  392  N   LYS A  50     4234   6047   3351   -693    437   -821       N  
ATOM    393  CA  LYS A  50      31.096  12.130 -11.052  1.00 43.66           C  
ANISOU  393  CA  LYS A  50     5153   7056   4381   -756    359   -995       C  
ATOM    394  C   LYS A  50      29.585  12.063 -11.160  1.00 36.88           C  
ANISOU  394  C   LYS A  50     4174   6374   3464   -722    269  -1069       C  
ATOM    395  O   LYS A  50      28.873  12.719 -10.394  1.00 36.15           O  
ANISOU  395  O   LYS A  50     4064   6257   3415   -730    248  -1043       O  
ATOM    396  CB  LYS A  50      31.626  11.142 -10.010  1.00 47.71           C  
ANISOU  396  CB  LYS A  50     5699   7260   5167   -902    391  -1054       C  
ATOM    397  CG  LYS A  50      30.833  11.031  -8.735  1.00 49.29           C  
ANISOU  397  CG  LYS A  50     5871   7309   5547   -947    388  -1054       C  
ATOM    398  CD  LYS A  50      31.551  10.071  -7.808  1.00 51.39           C  
ANISOU  398  CD  LYS A  50     6187   7321   6018   -975    467  -1001       C  
ATOM    399  CE  LYS A  50      30.699   9.615  -6.649  1.00 52.33           C  
ANISOU  399  CE  LYS A  50     6274   7375   6233   -961    504  -1000       C  
ATOM    400  NZ  LYS A  50      30.866   8.138  -6.478  1.00 52.81           N  
ANISOU  400  NZ  LYS A  50     6279   7448   6337  -1010    603  -1072       N  
ATOM    401  N   PRO A  51      29.096  11.286 -12.128  1.00 36.55           N  
ANISOU  401  N   PRO A  51     4049   6511   3328   -683    223  -1164       N  
ATOM    402  CA  PRO A  51      27.650  11.164 -12.331  1.00 36.75           C  
ANISOU  402  CA  PRO A  51     3956   6707   3302   -645    150  -1241       C  
ATOM    403  C   PRO A  51      26.996  10.312 -11.252  1.00 38.77           C  
ANISOU  403  C   PRO A  51     4192   6755   3784   -750    157  -1323       C  
ATOM    404  O   PRO A  51      27.593   9.351 -10.775  1.00 44.15           O  
ANISOU  404  O   PRO A  51     4917   7232   4626   -826    211  -1345       O  
ATOM    405  CB  PRO A  51      27.533  10.494 -13.705  1.00 40.87           C  
ANISOU  405  CB  PRO A  51     4404   7456   3671   -575    120  -1323       C  
ATOM    406  CG  PRO A  51      28.847   9.844 -13.946  1.00 44.88           C  
ANISOU  406  CG  PRO A  51     4990   7839   4224   -623    175  -1328       C  
ATOM    407  CD  PRO A  51      29.877  10.642 -13.198  1.00 39.99           C  
ANISOU  407  CD  PRO A  51     4495   7027   3671   -650    241  -1192       C  
ATOM    408  N   ILE A  52      25.789  10.687 -10.851  1.00 36.61           N  
ANISOU  408  N   ILE A  52     3861   6538   3513   -727    117  -1335       N  
ATOM    409  CA  ILE A  52      24.974   9.832  -9.997  1.00 35.42           C  
ANISOU  409  CA  ILE A  52     3692   6234   3531   -779    133  -1393       C  
ATOM    410  C   ILE A  52      23.557   9.856 -10.543  1.00 37.51           C  
ANISOU  410  C   ILE A  52     3844   6718   3690   -721     68  -1474       C  
ATOM    411  O   ILE A  52      23.078  10.891 -11.007  1.00 41.48           O  
ANISOU  411  O   ILE A  52     4300   7424   4039   -641     13  -1435       O  
ATOM    412  CB  ILE A  52      24.962  10.297  -8.535  1.00 40.44           C  
ANISOU  412  CB  ILE A  52     4407   6631   4328   -810    168  -1300       C  
ATOM    413  CG1 ILE A  52      24.490  11.741  -8.452  1.00 44.24           C  
ANISOU  413  CG1 ILE A  52     4868   7230   4710   -764    117  -1242       C  
ATOM    414  CG2 ILE A  52      26.351  10.143  -7.879  1.00 41.77           C  
ANISOU  414  CG2 ILE A  52     4685   6562   4625   -855    243  -1217       C  
ATOM    415  CD1 ILE A  52      24.377  12.252  -7.031  1.00 42.61           C  
ANISOU  415  CD1 ILE A  52     4732   6800   4659   -785    142  -1165       C  
ATOM    416  N   THR A  53      22.876   8.723 -10.518  1.00 33.54           N  
ANISOU  416  N   THR A  53     3289   6198   3259   -749     79  -1579       N  
ATOM    417  CA  THR A  53      21.514   8.737 -11.019  1.00 35.07           C  
ANISOU  417  CA  THR A  53     3375   6589   3361   -696     21  -1665       C  
ATOM    418  C   THR A  53      20.526   8.762  -9.865  1.00 34.42           C  
ANISOU  418  C   THR A  53     3274   6409   3395   -728     43  -1674       C  
ATOM    419  O   THR A  53      20.710   8.079  -8.850  1.00 39.98           O  
ANISOU  419  O   THR A  53     3996   6942   4253   -801    129  -1690       O  
ATOM    420  CB  THR A  53      21.217   7.595 -12.038  1.00 59.53           C  
ANISOU  420  CB  THR A  53     6350   9869   6400   -697     19  -1835       C  
ATOM    421  OG1 THR A  53      20.717   6.434 -11.361  1.00 63.48           O  
ANISOU  421  OG1 THR A  53     6779  10294   7047   -777     89  -1958       O  
ATOM    422  CG2 THR A  53      22.468   7.244 -12.826  1.00 50.71           C  
ANISOU  422  CG2 THR A  53     5268   8770   5230   -699     32  -1833       C  
ATOM    423  N   VAL A  54      19.502   9.593 -10.004  1.00 31.35           N  
ANISOU  423  N   VAL A  54     2855   6134   2920   -660    -27  -1648       N  
ATOM    424  CA  VAL A  54      18.485   9.713  -8.965  1.00 34.50           C  
ANISOU  424  CA  VAL A  54     3240   6456   3413   -679    -16  -1654       C  
ATOM    425  C   VAL A  54      17.123   9.655  -9.615  1.00 37.11           C  
ANISOU  425  C   VAL A  54     3455   7001   3645   -626    -74  -1753       C  
ATOM    426  O   VAL A  54      16.953  10.113 -10.748  1.00 40.03           O  
ANISOU  426  O   VAL A  54     3773   7589   3848   -546   -139  -1756       O  
ATOM    427  CB  VAL A  54      18.617  11.030  -8.202  1.00 35.32           C  
ANISOU  427  CB  VAL A  54     3441   6442   3537   -651    -44  -1496       C  
ATOM    428  CG1 VAL A  54      19.942  11.063  -7.453  1.00 35.39           C  
ANISOU  428  CG1 VAL A  54     3560   6227   3659   -701     18  -1409       C  
ATOM    429  CG2 VAL A  54      18.504  12.198  -9.174  1.00 35.71           C  
ANISOU  429  CG2 VAL A  54     3417   6769   3381   -563   -109  -1459       C  
ATOM    430  N   THR A  55      16.152   9.074  -8.919  1.00 37.71           N  
ANISOU  430  N   THR A  55     3478   7039   3813   -663    -41  -1840       N  
ATOM    431  CA  THR A  55      14.838   8.904  -9.525  1.00 42.48           C  
ANISOU  431  CA  THR A  55     3963   7842   4337   -618    -91  -1955       C  
ATOM    432  C   THR A  55      14.043  10.191  -9.380  1.00 44.08           C  
ANISOU  432  C   THR A  55     4183   8099   4467   -548   -163  -1853       C  
ATOM    433  O   THR A  55      14.369  11.049  -8.542  1.00 38.19           O  
ANISOU  433  O   THR A  55     3535   7202   3775   -552   -162  -1715       O  
ATOM    434  CB  THR A  55      14.049   7.730  -8.904  1.00 46.98           C  
ANISOU  434  CB  THR A  55     4463   8359   5029   -678    -29  -2100       C  
ATOM    435  OG1 THR A  55      13.631   8.060  -7.572  1.00 49.62           O  
ANISOU  435  OG1 THR A  55     4859   8523   5472   -702      2  -2029       O  
ATOM    436  CG2 THR A  55      14.899   6.469  -8.870  1.00 48.70           C  
ANISOU  436  CG2 THR A  55     4671   8493   5339   -747     56  -2180       C  
ATOM    437  N   ARG A  56      13.013  10.328 -10.205  1.00 40.34           N  
ANISOU  437  N   ARG A  56     3608   7846   3872   -480   -224  -1924       N  
ATOM    438  CA  ARG A  56      12.077  11.439 -10.078  1.00 39.73           C  
ANISOU  438  CA  ARG A  56     3527   7839   3730   -412   -286  -1842       C  
ATOM    439  C   ARG A  56      11.424  11.433  -8.691  1.00 43.92           C  
ANISOU  439  C   ARG A  56     4092   8188   4410   -469   -253  -1834       C  
ATOM    440  O   ARG A  56      11.297  12.477  -8.032  1.00 37.36           O  
ANISOU  440  O   ARG A  56     3327   7272   3597   -447   -279  -1704       O  
ATOM    441  CB  ARG A  56      10.994  11.349 -11.160  1.00 37.73           C  
ANISOU  441  CB  ARG A  56     3139   7865   3332   -332   -342  -1951       C  
ATOM    442  CG  ARG A  56      10.092  12.551 -11.174  1.00 37.76           C  
ANISOU  442  CG  ARG A  56     3102   8009   3236   -246   -397  -1874       C  
ATOM    443  CD  ARG A  56       8.848  12.359 -12.029  1.00 43.52           C  
ANISOU  443  CD  ARG A  56     3701   8982   3853   -174   -445  -1993       C  
ATOM    444  NE  ARG A  56       8.198  13.652 -12.223  1.00 45.32           N  
ANISOU  444  NE  ARG A  56     3890   9376   3953    -68   -495  -1886       N  
ATOM    445  CZ  ARG A  56       8.560  14.533 -13.152  1.00 45.72           C  
ANISOU  445  CZ  ARG A  56     3893   9663   3817     57   -521  -1787       C  
ATOM    446  NH1 ARG A  56       9.543  14.244 -14.002  1.00 44.32           N  
ANISOU  446  NH1 ARG A  56     3699   9589   3551     90   -507  -1794       N  
ATOM    447  NH2 ARG A  56       7.929  15.696 -13.243  1.00 45.69           N  
ANISOU  447  NH2 ARG A  56     3856   9792   3712    159   -558  -1670       N  
ATOM    448  N   ALA A  57      11.026  10.247  -8.244  1.00 47.19           N  
ANISOU  448  N   ALA A  57     4458   8542   4931   -536   -194  -1973       N  
ATOM    449  CA  ALA A  57      10.340  10.102  -6.968  1.00 46.52           C  
ANISOU  449  CA  ALA A  57     4396   8304   4976   -578   -155  -1976       C  
ATOM    450  C   ALA A  57      11.190  10.620  -5.804  1.00 42.44           C  
ANISOU  450  C   ALA A  57     4010   7553   4563   -610   -115  -1831       C  
ATOM    451  O   ALA A  57      10.670  11.253  -4.860  1.00 35.61           O  
ANISOU  451  O   ALA A  57     3186   6592   3750   -603   -124  -1760       O  
ATOM    452  CB  ALA A  57       9.938   8.638  -6.748  1.00 46.04           C  
ANISOU  452  CB  ALA A  57     4262   8218   5011   -636    -87  -2144       C  
ATOM    453  N   GLN A  58      12.491  10.341  -5.879  1.00 43.49           N  
ANISOU  453  N   GLN A  58     4200   7598   4724   -642    -71  -1793       N  
ATOM    454  CA  GLN A  58      13.467  10.789  -4.880  1.00 42.74           C  
ANISOU  454  CA  GLN A  58     4225   7290   4722   -666    -31  -1663       C  
ATOM    455  C   GLN A  58      13.501  12.303  -4.784  1.00 37.58           C  
ANISOU  455  C   GLN A  58     3631   6629   4018   -611   -105  -1518       C  
ATOM    456  O   GLN A  58      13.421  12.877  -3.702  1.00 40.17           O  
ANISOU  456  O   GLN A  58     4022   6812   4428   -612    -99  -1438       O  
ATOM    457  CB  GLN A  58      14.873  10.329  -5.283  1.00 46.24           C  
ANISOU  457  CB  GLN A  58     4710   7684   5174   -697     14  -1649       C  
ATOM    458  CG  GLN A  58      15.215   8.924  -4.891  1.00 47.39           C  
ANISOU  458  CG  GLN A  58     4838   7746   5422   -760    114  -1742       C  
ATOM    459  CD  GLN A  58      16.662   8.585  -5.177  1.00 42.06           C  
ANISOU  459  CD  GLN A  58     4214   7004   4763   -791    160  -1708       C  
ATOM    460  OE1 GLN A  58      17.020   8.271  -6.304  1.00 44.59           O  
ANISOU  460  OE1 GLN A  58     4488   7450   5004   -789    137  -1764       O  
ATOM    461  NE2 GLN A  58      17.501   8.646  -4.152  1.00 39.66           N  
ANISOU  461  NE2 GLN A  58     4005   6507   4556   -811    224  -1616       N  
ATOM    462  N   LEU A  59      13.692  12.938  -5.933  1.00 35.89           N  
ANISOU  462  N   LEU A  59     3396   6575   3667   -554   -174  -1480       N  
ATOM    463  CA  LEU A  59      13.771  14.387  -6.011  1.00 37.56           C  
ANISOU  463  CA  LEU A  59     3623   6846   3802   -492   -235  -1356       C  
ATOM    464  C   LEU A  59      12.480  15.042  -5.525  1.00 38.45           C  
ANISOU  464  C   LEU A  59     3705   6984   3918   -455   -282  -1333       C  
ATOM    465  O   LEU A  59      12.517  16.036  -4.797  1.00 31.42           O  
ANISOU  465  O   LEU A  59     2854   6014   3069   -438   -302  -1231       O  
ATOM    466  CB  LEU A  59      14.085  14.817  -7.452  1.00 38.73           C  
ANISOU  466  CB  LEU A  59     3681   7288   3747   -418   -271  -1358       C  
ATOM    467  CG  LEU A  59      15.450  14.324  -7.963  1.00 39.27           C  
ANISOU  467  CG  LEU A  59     3782   7339   3800   -448   -229  -1365       C  
ATOM    468  CD1 LEU A  59      15.637  14.578  -9.451  1.00 36.09           C  
ANISOU  468  CD1 LEU A  59     3287   7245   3181   -354   -264  -1368       C  
ATOM    469  CD2 LEU A  59      16.592  14.943  -7.161  1.00 37.82           C  
ANISOU  469  CD2 LEU A  59     3697   6971   3701   -483   -200  -1252       C  
ATOM    470  N   ALA A  60      11.341  14.489  -5.938  1.00 38.62           N  
ANISOU  470  N   ALA A  60     3653   7120   3901   -443   -302  -1433       N  
ATOM    471  CA  ALA A  60      10.047  15.043  -5.559  1.00 37.59           C  
ANISOU  471  CA  ALA A  60     3485   7031   3765   -409   -345  -1424       C  
ATOM    472  C   ALA A  60       9.813  14.942  -4.044  1.00 37.13           C  
ANISOU  472  C   ALA A  60     3484   6758   3866   -463   -300  -1412       C  
ATOM    473  O   ALA A  60       9.267  15.854  -3.430  1.00 38.59           O  
ANISOU  473  O   ALA A  60     3688   6900   4075   -434   -339  -1331       O  
ATOM    474  CB  ALA A  60       8.909  14.351  -6.331  1.00 38.63           C  
ANISOU  474  CB  ALA A  60     3498   7364   3817   -390   -361  -1571       C  
ATOM    475  N   ALA A  61      10.207  13.817  -3.461  1.00 35.06           N  
ANISOU  475  N   ALA A  61     3241   6375   3707   -531   -216  -1490       N  
ATOM    476  CA  ALA A  61      10.053  13.598  -2.032  1.00 37.95           C  
ANISOU  476  CA  ALA A  61     3659   6552   4209   -566   -162  -1477       C  
ATOM    477  C   ALA A  61      10.901  14.599  -1.262  1.00 32.64           C  
ANISOU  477  C   ALA A  61     3088   5718   3595   -554   -170  -1332       C  
ATOM    478  O   ALA A  61      10.447  15.191  -0.290  1.00 30.45           O  
ANISOU  478  O   ALA A  61     2841   5348   3380   -539   -183  -1277       O  
ATOM    479  CB  ALA A  61      10.449  12.180  -1.665  1.00 40.15           C  
ANISOU  479  CB  ALA A  61     3934   6749   4571   -625    -65  -1573       C  
ATOM    480  N   SER A  62      12.126  14.805  -1.732  1.00 34.47           N  
ANISOU  480  N   SER A  62     3366   5922   3807   -556   -168  -1275       N  
ATOM    481  CA  SER A  62      13.073  15.712  -1.095  1.00 33.10           C  
ANISOU  481  CA  SER A  62     3285   5593   3700   -545   -177  -1147       C  
ATOM    482  C   SER A  62      12.580  17.164  -1.108  1.00 31.75           C  
ANISOU  482  C   SER A  62     3107   5459   3499   -486   -272  -1040       C  
ATOM    483  O   SER A  62      12.580  17.842  -0.078  1.00 30.73           O  
ANISOU  483  O   SER A  62     3020   5190   3465   -477   -281   -969       O  
ATOM    484  CB  SER A  62      14.436  15.581  -1.778  1.00 34.89           C  
ANISOU  484  CB  SER A  62     3550   5806   3899   -560   -160  -1119       C  
ATOM    485  OG  SER A  62      15.388  16.422  -1.189  1.00 35.84           O  
ANISOU  485  OG  SER A  62     3752   5773   4095   -551   -169  -1006       O  
ATOM    486  N   ALA A  63      12.171  17.631  -2.284  1.00 27.62           N  
ANISOU  486  N   ALA A  63     2499   5167   2830   -439   -329  -1044       N  
ATOM    487  CA  ALA A  63      11.533  18.935  -2.438  1.00 28.18           C  
ANISOU  487  CA  ALA A  63     2502   5375   2831   -367   -399   -967       C  
ATOM    488  C   ALA A  63      10.331  19.110  -1.520  1.00 27.91           C  
ANISOU  488  C   ALA A  63     2481   5242   2882   -365   -422   -962       C  
ATOM    489  O   ALA A  63      10.209  20.138  -0.862  1.00 29.45           O  
ANISOU  489  O   ALA A  63     2683   5369   3137   -335   -457   -869       O  
ATOM    490  CB  ALA A  63      11.090  19.143  -3.898  1.00 27.41           C  
ANISOU  490  CB  ALA A  63     2289   5600   2526   -293   -437   -987       C  
ATOM    491  N   ALA A  64       9.416  18.141  -1.511  1.00 27.15           N  
ANISOU  491  N   ALA A  64     2361   5171   2782   -393   -399  -1070       N  
ATOM    492  CA  ALA A  64       8.255  18.230  -0.618  1.00 31.14           C  
ANISOU  492  CA  ALA A  64     2848   5639   3344   -393   -402  -1095       C  
ATOM    493  C   ALA A  64       8.612  18.413   0.871  1.00 32.24           C  
ANISOU  493  C   ALA A  64     3066   5554   3629   -418   -365  -1048       C  
ATOM    494  O   ALA A  64       7.929  19.154   1.582  1.00 30.30           O  
ANISOU  494  O   ALA A  64     2819   5265   3427   -392   -399   -998       O  
ATOM    495  CB  ALA A  64       7.301  17.037  -0.809  1.00 32.89           C  
ANISOU  495  CB  ALA A  64     3003   5955   3540   -424   -365  -1248       C  
HETATM  496  N   MSE A  65       9.679  17.762   1.333  1.00 34.16           N  
ANISOU  496  N   MSE A  65     3373   5663   3943   -458   -295  -1061       N  
HETATM  497  CA  MSE A  65      10.089  17.857   2.738  1.00 32.11           C  
ANISOU  497  CA  MSE A  65     3186   5207   3809   -465   -252  -1020       C  
HETATM  498  C   MSE A  65      10.521  19.265   3.071  1.00 30.83           C  
ANISOU  498  C   MSE A  65     3057   4962   3695   -427   -314   -891       C  
HETATM  499  O   MSE A  65      10.176  19.812   4.119  1.00 26.75           O  
ANISOU  499  O   MSE A  65     2560   4347   3256   -407   -323   -851       O  
HETATM  500  CB  MSE A  65      11.270  16.935   3.026  1.00 32.01           C  
ANISOU  500  CB  MSE A  65     3229   5085   3846   -500   -164  -1046       C  
HETATM  501  CG  MSE A  65      10.945  15.460   2.986  1.00 38.07           C  
ANISOU  501  CG  MSE A  65     3961   5895   4610   -538    -87  -1166       C  
HETATM  502 SE   MSE A  65      12.484  14.470   3.630  0.45 40.13          SE  
ANISOU  502 SE   MSE A  65     4296   6000   4954   -564     27  -1164      SE  
HETATM  503  CE  MSE A  65      13.865  15.310   2.553  1.00 50.61           C  
ANISOU  503  CE  MSE A  65     5668   7330   6233   -563    -20  -1079       C  
ATOM    504  N   THR A  66      11.298  19.838   2.163  1.00 29.93           N  
ANISOU  504  N   THR A  66     2939   4890   3541   -413   -357   -823       N  
ATOM    505  CA  THR A  66      11.863  21.160   2.346  1.00 33.15           C  
ANISOU  505  CA  THR A  66     3356   5220   4021   -376   -417   -688       C  
ATOM    506  C   THR A  66      10.741  22.173   2.436  1.00 33.15           C  
ANISOU  506  C   THR A  66     3291   5286   4018   -323   -487   -630       C  
ATOM    507  O   THR A  66      10.739  23.026   3.328  1.00 32.35           O  
ANISOU  507  O   THR A  66     3199   5064   4030   -301   -508   -552       O  
ATOM    508  CB  THR A  66      12.816  21.520   1.174  1.00 35.59           C  
ANISOU  508  CB  THR A  66     3608   5669   4244   -361   -431   -663       C  
ATOM    509  OG1 THR A  66      13.839  20.523   1.083  1.00 36.36           O  
ANISOU  509  OG1 THR A  66     3780   5681   4354   -416   -365   -714       O  
ATOM    510  CG2 THR A  66      13.468  22.887   1.393  1.00 34.43           C  
ANISOU  510  CG2 THR A  66     3410   5484   4186   -313   -469   -536       C  
ATOM    511  N   GLY A  67       9.787  22.060   1.514  1.00 30.24           N  
ANISOU  511  N   GLY A  67     2846   5132   3513   -298   -515   -678       N  
ATOM    512  CA  GLY A  67       8.652  22.963   1.446  1.00 33.80           C  
ANISOU  512  CA  GLY A  67     3225   5686   3933   -237   -575   -631       C  
ATOM    513  C   GLY A  67       7.823  22.956   2.719  1.00 33.45           C  
ANISOU  513  C   GLY A  67     3219   5501   3991   -257   -568   -646       C  
ATOM    514  O   GLY A  67       7.395  24.006   3.197  1.00 31.73           O  
ANISOU  514  O   GLY A  67     2976   5241   3837   -214   -612   -560       O  
ATOM    515  N   LYS A  68       7.584  21.767   3.256  1.00 31.08           N  
ANISOU  515  N   LYS A  68     2951   5166   3693   -311   -499   -766       N  
ATOM    516  CA  LYS A  68       6.820  21.621   4.492  1.00 34.52           C  
ANISOU  516  CA  LYS A  68     3402   5515   4198   -318   -473   -802       C  
ATOM    517  C   LYS A  68       7.606  22.138   5.699  1.00 32.45           C  
ANISOU  517  C   LYS A  68     3206   5060   4061   -312   -454   -736       C  
ATOM    518  O   LYS A  68       7.108  22.963   6.460  1.00 30.62           O  
ANISOU  518  O   LYS A  68     2969   4777   3889   -282   -483   -684       O  
ATOM    519  CB  LYS A  68       6.450  20.154   4.716  1.00 41.27           C  
ANISOU  519  CB  LYS A  68     4259   6386   5035   -364   -397   -935       C  
ATOM    520  CG  LYS A  68       5.461  19.926   5.866  1.00 49.42           C  
ANISOU  520  CG  LYS A  68     5288   7367   6122   -362   -373   -975       C  
ATOM    521  CD  LYS A  68       4.028  20.243   5.437  1.00 57.08           C  
ANISOU  521  CD  LYS A  68     6181   8478   7028   -342   -429   -999       C  
ATOM    522  CE  LYS A  68       2.987  19.727   6.438  1.00 59.81           C  
ANISOU  522  CE  LYS A  68     6513   8794   7418   -350   -397  -1063       C  
ATOM    523  NZ  LYS A  68       2.879  20.545   7.691  1.00 58.63           N  
ANISOU  523  NZ  LYS A  68     6403   8522   7352   -320   -407   -992       N  
ATOM    524  N   ALA A  69       8.824  21.633   5.873  1.00 27.02           N  
ANISOU  524  N   ALA A  69     2580   4274   3412   -337   -400   -743       N  
ATOM    525  CA  ALA A  69       9.637  21.966   7.036  1.00 28.01           C  
ANISOU  525  CA  ALA A  69     2770   4226   3646   -324   -367   -700       C  
ATOM    526  C   ALA A  69       9.923  23.469   7.131  1.00 33.36           C  
ANISOU  526  C   ALA A  69     3428   4853   4392   -288   -434   -575       C  
ATOM    527  O   ALA A  69       9.984  24.019   8.227  1.00 28.64           O  
ANISOU  527  O   ALA A  69     2858   4151   3875   -261   -421   -550       O  
ATOM    528  CB  ALA A  69      10.934  21.180   7.019  1.00 26.29           C  
ANISOU  528  CB  ALA A  69     2612   3930   3445   -349   -298   -725       C  
ATOM    529  N   LEU A  70      10.088  24.146   5.996  1.00 26.99           N  
ANISOU  529  N   LEU A  70     3136   4327   2792    -46   -388   -367       N  
ATOM    530  CA  LEU A  70      10.424  25.573   6.069  1.00 26.91           C  
ANISOU  530  CA  LEU A  70     3000   4339   2886     10   -314   -343       C  
ATOM    531  C   LEU A  70       9.255  26.483   5.659  1.00 24.36           C  
ANISOU  531  C   LEU A  70     2556   4069   2632     27   -273   -378       C  
ATOM    532  O   LEU A  70       9.419  27.696   5.561  1.00 29.73           O  
ANISOU  532  O   LEU A  70     3125   4722   3449     92   -204   -345       O  
ATOM    533  CB  LEU A  70      11.691  25.884   5.247  1.00 26.96           C  
ANISOU  533  CB  LEU A  70     2999   4320   2924    168   -295   -245       C  
ATOM    534  CG  LEU A  70      12.952  25.132   5.700  1.00 28.58           C  
ANISOU  534  CG  LEU A  70     3284   4485   3089    179   -330   -207       C  
ATOM    535  CD1 LEU A  70      14.113  25.355   4.739  1.00 29.61           C  
ANISOU  535  CD1 LEU A  70     3390   4626   3236    340   -305   -126       C  
ATOM    536  CD2 LEU A  70      13.342  25.517   7.125  1.00 28.59           C  
ANISOU  536  CD2 LEU A  70     3241   4503   3117     53   -316   -229       C  
ATOM    537  N   SER A  71       8.082  25.891   5.440  1.00 23.40           N  
ANISOU  537  N   SER A  71     2444   4010   2437    -31   -314   -440       N  
ATOM    538  CA  SER A  71       6.881  26.641   5.060  1.00 28.27           C  
ANISOU  538  CA  SER A  71     2925   4709   3108     -4   -290   -468       C  
ATOM    539  C   SER A  71       7.120  27.554   3.863  1.00 30.44           C  
ANISOU  539  C   SER A  71     3110   5004   3452    189   -266   -337       C  
ATOM    540  O   SER A  71       6.825  28.752   3.900  1.00 30.00           O  
ANISOU  540  O   SER A  71     2922   4918   3558    251   -202   -295       O  
ATOM    541  CB  SER A  71       6.334  27.461   6.230  1.00 32.85           C  
ANISOU  541  CB  SER A  71     3399   5286   3798   -104   -220   -563       C  
ATOM    542  OG  SER A  71       5.996  26.604   7.297  1.00 39.15           O  
ANISOU  542  OG  SER A  71     4259   6124   4491   -295   -241   -655       O  
ATOM    543  N   LEU A  72       7.632  26.968   2.790  1.00 28.09           N  
ANISOU  543  N   LEU A  72     2875   4760   3037    283   -312   -270       N  
ATOM    544  CA  LEU A  72       7.917  27.717   1.579  1.00 26.80           C  
ANISOU  544  CA  LEU A  72     2624   4672   2886    457   -292   -110       C  
ATOM    545  C   LEU A  72       6.894  27.356   0.504  1.00 30.29           C  
ANISOU  545  C   LEU A  72     3005   5323   3179    506   -358   -113       C  
ATOM    546  O   LEU A  72       7.129  26.467  -0.321  1.00 30.80           O  
ANISOU  546  O   LEU A  72     3130   5502   3068    530   -411   -154       O  
ATOM    547  CB  LEU A  72       9.348  27.415   1.111  1.00 24.13           C  
ANISOU  547  CB  LEU A  72     2365   4310   2493    531   -281    -38       C  
ATOM    548  CG  LEU A  72      10.415  27.653   2.187  1.00 27.60           C  
ANISOU  548  CG  LEU A  72     2850   4586   3051    472   -232    -49       C  
ATOM    549  CD1 LEU A  72      11.751  27.030   1.776  1.00 25.38           C  
ANISOU  549  CD1 LEU A  72     2647   4307   2688    538   -241    -14       C  
ATOM    550  CD2 LEU A  72      10.566  29.138   2.483  1.00 26.43           C  
ANISOU  550  CD2 LEU A  72     2577   4347   3120    497   -141     39       C  
ATOM    551  N   GLY A  73       5.756  28.048   0.516  1.00 30.51           N  
ANISOU  551  N   GLY A  73     2893   5419   3281    522   -355    -90       N  
ATOM    552  CA  GLY A  73       4.675  27.723  -0.400  1.00 35.04           C  
ANISOU  552  CA  GLY A  73     3374   6236   3702    553   -431   -104       C  
ATOM    553  C   GLY A  73       4.773  28.445  -1.730  1.00 30.93           C  
ANISOU  553  C   GLY A  73     2751   5867   3133    732   -424    120       C  
ATOM    554  O   GLY A  73       5.820  29.016  -2.056  1.00 31.48           O  
ANISOU  554  O   GLY A  73     2841   5859   3261    824   -365    285       O  
ATOM    555  N   PRO A  74       3.678  28.437  -2.506  1.00 33.28           N  
ANISOU  555  N   PRO A  74     2970   6342   3332    747   -454    134       N  
ATOM    556  CA  PRO A  74       3.676  29.099  -3.814  1.00 34.75           C  
ANISOU  556  CA  PRO A  74     3088   6665   3450    877   -427    358       C  
ATOM    557  C   PRO A  74       3.969  30.597  -3.712  1.00 33.16           C  
ANISOU  557  C   PRO A  74     2814   6286   3499    994   -353    620       C  
ATOM    558  O   PRO A  74       3.454  31.283  -2.826  1.00 29.22           O  
ANISOU  558  O   PRO A  74     2244   5619   3238    998   -331    610       O  
ATOM    559  CB  PRO A  74       2.239  28.871  -4.325  1.00 39.77           C  
ANISOU  559  CB  PRO A  74     3621   7517   3973    853   -481    297       C  
ATOM    560  CG  PRO A  74       1.774  27.653  -3.609  1.00 41.53           C  
ANISOU  560  CG  PRO A  74     3911   7736   4133    681   -530      0       C  
ATOM    561  CD  PRO A  74       2.395  27.770  -2.226  1.00 37.44           C  
ANISOU  561  CD  PRO A  74     3461   6973   3793    625   -509    -58       C  
ATOM    562  N   GLY A  75       4.779  31.105  -4.633  1.00 31.97           N  
ANISOU  562  N   GLY A  75     2669   6166   3311   1079   -300    837       N  
ATOM    563  CA  GLY A  75       5.099  32.520  -4.661  1.00 31.55           C  
ANISOU  563  CA  GLY A  75     2553   5921   3512   1170   -220   1099       C  
ATOM    564  C   GLY A  75       6.430  32.803  -3.974  1.00 28.30           C  
ANISOU  564  C   GLY A  75     2216   5269   3270   1147   -146   1110       C  
ATOM    565  O   GLY A  75       6.960  33.911  -4.066  1.00 35.33           O  
ANISOU  565  O   GLY A  75     3065   5986   4373   1200    -62   1319       O  
ATOM    566  N   THR A  76       6.961  31.808  -3.273  1.00 28.21           N  
ANISOU  566  N   THR A  76     2300   5243   3174   1063   -175    888       N  
ATOM    567  CA  THR A  76       8.276  31.947  -2.630  1.00 30.68           C  
ANISOU  567  CA  THR A  76     2672   5373   3612   1037   -113    883       C  
ATOM    568  C   THR A  76       9.309  32.494  -3.622  1.00 31.86           C  
ANISOU  568  C   THR A  76     2819   5555   3731   1099    -40   1122       C  
ATOM    569  O   THR A  76       9.520  31.913  -4.693  1.00 33.80           O  
ANISOU  569  O   THR A  76     3083   6045   3713   1127    -55   1156       O  
ATOM    570  CB  THR A  76       8.790  30.599  -2.086  1.00 28.12           C  
ANISOU  570  CB  THR A  76     2457   5107   3118    960   -172    647       C  
ATOM    571  OG1 THR A  76       7.978  30.187  -0.980  1.00 26.57           O  
ANISOU  571  OG1 THR A  76     2276   4841   2976    853   -211    431       O  
ATOM    572  CG2 THR A  76      10.219  30.717  -1.592  1.00 30.00           C  
ANISOU  572  CG2 THR A  76     2744   5203   3451    947   -110    663       C  
ATOM    573  N   ARG A  77       9.946  33.607  -3.272  1.00 27.11           N  
ANISOU  573  N   ARG A  77     2172   4724   3406   1111     54   1270       N  
ATOM    574  CA  ARG A  77      10.997  34.173  -4.114  1.00 31.06           C  
ANISOU  574  CA  ARG A  77     2647   5253   3901   1149    139   1516       C  
ATOM    575  C   ARG A  77      12.339  33.597  -3.694  1.00 30.77           C  
ANISOU  575  C   ARG A  77     2676   5197   3817   1103    161   1410       C  
ATOM    576  O   ARG A  77      12.863  33.950  -2.643  1.00 30.94           O  
ANISOU  576  O   ARG A  77     2690   4994   4073   1048    203   1331       O  
ATOM    577  CB  ARG A  77      11.013  35.695  -3.990  1.00 31.95           C  
ANISOU  577  CB  ARG A  77     2661   5108   4369   1175    239   1744       C  
ATOM    578  CG  ARG A  77       9.762  36.372  -4.536  1.00 41.14           C  
ANISOU  578  CG  ARG A  77     3742   6295   5595   1248    225   1898       C  
ATOM    579  CD  ARG A  77       9.684  37.815  -4.063  1.00 46.62           C  
ANISOU  579  CD  ARG A  77     4347   6641   6725   1266    325   2041       C  
ATOM    580  NE  ARG A  77       9.681  37.870  -2.601  1.00 49.01           N  
ANISOU  580  NE  ARG A  77     4665   6679   7276   1195    341   1753       N  
ATOM    581  CZ  ARG A  77       9.778  38.989  -1.889  1.00 51.48           C  
ANISOU  581  CZ  ARG A  77     4909   6648   8003   1174    445   1750       C  
ATOM    582  NH1 ARG A  77       9.895  40.158  -2.502  1.00 51.76           N  
ANISOU  582  NH1 ARG A  77     4861   6522   8284   1224    538   2052       N  
ATOM    583  NH2 ARG A  77       9.770  38.936  -0.562  1.00 52.87           N  
ANISOU  583  NH2 ARG A  77     5086   6649   8355   1089    470   1434       N  
ATOM    584  N   ALA A  78      12.881  32.694  -4.506  1.00 25.48           N  
ANISOU  584  N   ALA A  78     2053   4779   2850   1126    138   1382       N  
ATOM    585  CA  ALA A  78      14.063  31.953  -4.120  1.00 27.54           C  
ANISOU  585  CA  ALA A  78     2377   5047   3042   1101    140   1248       C  
ATOM    586  C   ALA A  78      15.253  32.378  -4.970  1.00 31.33           C  
ANISOU  586  C   ALA A  78     2792   5639   3473   1142    236   1458       C  
ATOM    587  O   ALA A  78      15.135  32.523  -6.195  1.00 35.25           O  
ANISOU  587  O   ALA A  78     3225   6369   3799   1197    271   1621       O  
ATOM    588  CB  ALA A  78      13.810  30.464  -4.263  1.00 28.44           C  
ANISOU  588  CB  ALA A  78     2585   5333   2888   1103     44    999       C  
ATOM    589  N   LEU A  79      16.394  32.587  -4.321  1.00 30.72           N  
ANISOU  589  N   LEU A  79     2702   5429   3542   1108    287   1451       N  
ATOM    590  CA  LEU A  79      17.633  32.890  -5.036  1.00 31.83           C  
ANISOU  590  CA  LEU A  79     2763   5699   3632   1139    379   1635       C  
ATOM    591  C   LEU A  79      18.454  31.606  -5.195  1.00 32.34           C  
ANISOU  591  C   LEU A  79     2886   5954   3447   1175    340   1431       C  
ATOM    592  O   LEU A  79      18.738  30.916  -4.217  1.00 28.05           O  
ANISOU  592  O   LEU A  79     2419   5291   2950   1138    285   1202       O  
ATOM    593  CB  LEU A  79      18.451  33.944  -4.278  1.00 30.06           C  
ANISOU  593  CB  LEU A  79     2450   5223   3750   1069    474   1741       C  
ATOM    594  CG  LEU A  79      19.874  34.228  -4.791  1.00 34.50           C  
ANISOU  594  CG  LEU A  79     2911   5900   4299   1070    576   1903       C  
ATOM    595  CD1 LEU A  79      19.835  35.024  -6.090  1.00 37.10           C  
ANISOU  595  CD1 LEU A  79     3122   6394   4580   1135    660   2292       C  
ATOM    596  CD2 LEU A  79      20.647  34.996  -3.748  1.00 39.27           C  
ANISOU  596  CD2 LEU A  79     3446   6232   5243    945    657   1864       C  
ATOM    597  N   VAL A  80      18.812  31.278  -6.431  1.00 30.51           N  
ANISOU  597  N   VAL A  80     2601   6035   2956   1254    376   1512       N  
ATOM    598  CA  VAL A  80      19.600  30.083  -6.707  1.00 31.84           C  
ANISOU  598  CA  VAL A  80     2798   6397   2903   1319    353   1306       C  
ATOM    599  C   VAL A  80      21.054  30.478  -6.972  1.00 35.92           C  
ANISOU  599  C   VAL A  80     3213   7004   3430   1334    447   1448       C  
ATOM    600  O   VAL A  80      21.376  30.933  -8.069  1.00 39.06           O  
ANISOU  600  O   VAL A  80     3497   7656   3690   1383    506   1676       O  
ATOM    601  CB  VAL A  80      19.049  29.344  -7.955  1.00 34.18           C  
ANISOU  601  CB  VAL A  80     3054   7018   2916   1398    337   1211       C  
ATOM    602  CG1 VAL A  80      19.837  28.054  -8.216  1.00 35.15           C  
ANISOU  602  CG1 VAL A  80     3185   7299   2873   1487    297    948       C  
ATOM    603  CG2 VAL A  80      17.562  29.056  -7.782  1.00 36.90           C  
ANISOU  603  CG2 VAL A  80     3480   7275   3265   1354    244   1087       C  
ATOM    604  N   CYS A  81      21.917  30.311  -5.971  1.00 34.53           N  
ANISOU  604  N   CYS A  81     3074   6625   3421   1275    445   1313       N  
ATOM    605  CA  CYS A  81      23.318  30.737  -6.059  1.00 35.61           C  
ANISOU  605  CA  CYS A  81     3122   6791   3616   1243    529   1406       C  
ATOM    606  C   CYS A  81      24.270  29.576  -5.825  1.00 36.29           C  
ANISOU  606  C   CYS A  81     3256   6932   3602   1290    488   1153       C  
ATOM    607  O   CYS A  81      25.465  29.777  -5.622  1.00 35.54           O  
ANISOU  607  O   CYS A  81     3096   6829   3579   1253    535   1167       O  
ATOM    608  CB  CYS A  81      23.618  31.846  -5.047  1.00 36.23           C  
ANISOU  608  CB  CYS A  81     3150   6584   4033   1106    584   1499       C  
ATOM    609  SG  CYS A  81      23.221  31.399  -3.306  1.00 35.38           S  
ANISOU  609  SG  CYS A  81     3146   6189   4108   1027    487   1216       S  
ATOM    610  N   LEU A  82      23.726  28.364  -5.841  1.00 32.69           N  
ANISOU  610  N   LEU A  82     2900   6516   3003   1374    402    923       N  
ATOM    611  CA  LEU A  82      24.528  27.157  -5.819  1.00 33.08           C  
ANISOU  611  CA  LEU A  82     2987   6613   2968   1458    365    694       C  
ATOM    612  C   LEU A  82      24.698  26.669  -7.252  1.00 35.51           C  
ANISOU  612  C   LEU A  82     3239   7233   3020   1563    377    654       C  
ATOM    613  O   LEU A  82      23.816  26.858  -8.091  1.00 35.82           O  
ANISOU  613  O   LEU A  82     3250   7441   2919   1584    361    722       O  
ATOM    614  CB  LEU A  82      23.835  26.103  -4.972  1.00 34.61           C  
ANISOU  614  CB  LEU A  82     3313   6628   3210   1486    262    467       C  
ATOM    615  CG  LEU A  82      23.747  26.525  -3.506  1.00 36.80           C  
ANISOU  615  CG  LEU A  82     3630   6633   3720   1370    223    492       C  
ATOM    616  CD1 LEU A  82      22.789  25.643  -2.748  1.00 27.16           C  
ANISOU  616  CD1 LEU A  82     2535   5258   2529   1379    111    332       C  
ATOM    617  CD2 LEU A  82      25.143  26.489  -2.915  1.00 38.54           C  
ANISOU  617  CD2 LEU A  82     3796   6816   4031   1355    242    480       C  
ATOM    618  N   ASN A  83      25.839  26.053  -7.523  1.00 39.98           N  
ANISOU  618  N   ASN A  83     3767   7883   3541   1625    393    535       N  
ATOM    619  CA  ASN A  83      26.211  25.647  -8.870  1.00 44.38           C  
ANISOU  619  CA  ASN A  83     4237   8739   3885   1706    409    472       C  
ATOM    620  C   ASN A  83      25.195  24.660  -9.431  1.00 41.78           C  
ANISOU  620  C   ASN A  83     3967   8485   3423   1770    332    242       C  
ATOM    621  O   ASN A  83      25.055  23.554  -8.909  1.00 43.39           O  
ANISOU  621  O   ASN A  83     4277   8520   3690   1821    281    -15       O  
ATOM    622  CB  ASN A  83      27.617  25.034  -8.853  1.00 44.17           C  
ANISOU  622  CB  ASN A  83     4164   8740   3878   1767    441    336       C  
ATOM    623  CG  ASN A  83      28.252  24.991 -10.226  1.00 49.41           C  
ANISOU  623  CG  ASN A  83     4691   9739   4343   1815    490    332       C  
ATOM    624  OD1 ASN A  83      27.622  24.577 -11.195  1.00 45.85           O  
ANISOU  624  OD1 ASN A  83     4217   9483   3719   1855    460    231       O  
ATOM    625  ND2 ASN A  83      29.508  25.433 -10.319  1.00 52.91           N  
ANISOU  625  ND2 ASN A  83     5024  10269   4811   1797    566    431       N  
ATOM    626  N   VAL A  84      24.465  25.066 -10.472  1.00 41.45           N  
ANISOU  626  N   VAL A  84     3842   8678   3228   1757    322    340       N  
ATOM    627  CA  VAL A  84      23.438  24.200 -11.048  1.00 42.66           C  
ANISOU  627  CA  VAL A  84     4025   8910   3273   1778    252    109       C  
ATOM    628  C   VAL A  84      24.066  23.141 -11.943  1.00 50.64           C  
ANISOU  628  C   VAL A  84     4987  10099   4153   1847    257   -169       C  
ATOM    629  O   VAL A  84      23.371  22.301 -12.506  1.00 55.75           O  
ANISOU  629  O   VAL A  84     5649  10818   4717   1851    211   -412       O  
ATOM    630  CB  VAL A  84      22.378  24.985 -11.853  1.00 45.37           C  
ANISOU  630  CB  VAL A  84     4266   9451   3520   1732    240    301       C  
ATOM    631  CG1 VAL A  84      21.486  25.792 -10.922  1.00 33.18           C  
ANISOU  631  CG1 VAL A  84     2785   7684   2137   1671    232    492       C  
ATOM    632  CG2 VAL A  84      23.047  25.866 -12.913  1.00 47.36           C  
ANISOU  632  CG2 VAL A  84     4333  10008   3654   1738    306    556       C  
ATOM    633  N   GLY A  85      25.384  23.192 -12.091  1.00 52.26           N  
ANISOU  633  N   GLY A  85     5124  10381   4351   1891    322   -145       N  
ATOM    634  CA  GLY A  85      26.085  22.110 -12.754  1.00 54.10           C  
ANISOU  634  CA  GLY A  85     5317  10732   4507   1971    341   -442       C  
ATOM    635  C   GLY A  85      26.113  20.905 -11.823  1.00 56.80           C  
ANISOU  635  C   GLY A  85     5810  10734   5036   2032    305   -726       C  
ATOM    636  O   GLY A  85      26.455  19.800 -12.244  1.00 61.70           O  
ANISOU  636  O   GLY A  85     6427  11358   5656   2106    315  -1026       O  
ATOM    637  N   TYR A  86      25.755  21.122 -10.556  1.00 52.14           N  
ANISOU  637  N   TYR A  86     5344   9845   4624   2002    270   -625       N  
ATOM    638  CA  TYR A  86      25.804  20.059  -9.544  1.00 56.60           C  
ANISOU  638  CA  TYR A  86     6044  10067   5394   2064    231   -830       C  
ATOM    639  C   TYR A  86      24.487  19.900  -8.789  1.00 57.80           C  
ANISOU  639  C   TYR A  86     6339   9997   5625   2002    156   -856       C  
ATOM    640  O   TYR A  86      23.618  20.769  -8.845  1.00 54.54           O  
ANISOU  640  O   TYR A  86     5919   9672   5134   1912    140   -681       O  
ATOM    641  CB  TYR A  86      26.975  20.273  -8.568  1.00 56.09           C  
ANISOU  641  CB  TYR A  86     5967   9846   5499   2102    258   -704       C  
ATOM    642  CG  TYR A  86      28.316  20.174  -9.261  1.00 61.79           C  
ANISOU  642  CG  TYR A  86     6552  10760   6166   2172    331   -741       C  
ATOM    643  CD1 TYR A  86      29.120  19.049  -9.112  1.00 67.32           C  
ANISOU  643  CD1 TYR A  86     7252  11331   6996   2299    338   -959       C  
ATOM    644  CD2 TYR A  86      28.763  21.191 -10.098  1.00 62.23           C  
ANISOU  644  CD2 TYR A  86     6468  11126   6051   2117    396   -550       C  
ATOM    645  CE1 TYR A  86      30.341  18.950  -9.766  1.00 71.56           C  
ANISOU  645  CE1 TYR A  86     7648  12061   7481   2369    412  -1009       C  
ATOM    646  CE2 TYR A  86      29.978  21.099 -10.757  1.00 68.15           C  
ANISOU  646  CE2 TYR A  86     7082  12077   6736   2174    468   -591       C  
ATOM    647  CZ  TYR A  86      30.762  19.979 -10.588  1.00 73.38           C  
ANISOU  647  CZ  TYR A  86     7741  12625   7514   2300    477   -833       C  
ATOM    648  OH  TYR A  86      31.972  19.894 -11.239  1.00 80.19           O  
ANISOU  648  OH  TYR A  86     8454  13700   8314   2362    554   -884       O  
ATOM    649  N   ILE A  87      24.359  18.787  -8.073  1.00 64.82           N  
ANISOU  649  N   ILE A  87     7351  10589   6689   2056    113  -1063       N  
ATOM    650  CA  ILE A  87      23.110  18.423  -7.403  1.00 65.22           C  
ANISOU  650  CA  ILE A  87     7545  10419   6815   1995     41  -1138       C  
ATOM    651  C   ILE A  87      22.583  19.475  -6.432  1.00 64.17           C  
ANISOU  651  C   ILE A  87     7444  10224   6715   1914     22   -878       C  
ATOM    652  O   ILE A  87      21.373  19.680  -6.332  1.00 67.41           O  
ANISOU  652  O   ILE A  87     7917  10623   7072   1819    -18   -876       O  
ATOM    653  CB  ILE A  87      23.237  17.066  -6.672  1.00 68.87           C  
ANISOU  653  CB  ILE A  87     8133  10521   7514   2077      1  -1354       C  
ATOM    654  CG1 ILE A  87      21.916  16.691  -5.994  1.00 71.26           C  
ANISOU  654  CG1 ILE A  87     8592  10594   7889   1990    -74  -1430       C  
ATOM    655  CG2 ILE A  87      24.363  17.108  -5.666  1.00 66.16           C  
ANISOU  655  CG2 ILE A  87     7773  10013   7353   2171      1  -1198       C  
ATOM    656  CD1 ILE A  87      21.411  15.308  -6.366  1.00 74.71           C  
ANISOU  656  CD1 ILE A  87     9123  10835   8430   1980   -100  -1757       C  
ATOM    657  N   ALA A  88      23.473  20.140  -5.707  1.00 61.18           N  
ANISOU  657  N   ALA A  88     7010   9802   6435   1928     49   -670       N  
ATOM    658  CA  ALA A  88      23.031  21.140  -4.733  1.00 53.44           C  
ANISOU  658  CA  ALA A  88     6045   8719   5540   1811     25   -437       C  
ATOM    659  C   ALA A  88      22.194  22.235  -5.401  1.00 46.22           C  
ANISOU  659  C   ALA A  88     5074   8008   4479   1718     58   -286       C  
ATOM    660  O   ALA A  88      21.132  22.620  -4.909  1.00 41.74           O  
ANISOU  660  O   ALA A  88     4580   7319   3960   1595      2   -217       O  
ATOM    661  CB  ALA A  88      24.224  21.742  -4.016  1.00 58.35           C  
ANISOU  661  CB  ALA A  88     6585   9304   6280   1805     53   -262       C  
ATOM    662  N   GLY A  89      22.686  22.730  -6.531  1.00 45.54           N  
ANISOU  662  N   GLY A  89     4864   8205   4234   1751    128   -207       N  
ATOM    663  CA  GLY A  89      21.984  23.741  -7.294  1.00 42.59           C  
ANISOU  663  CA  GLY A  89     4412   8038   3732   1689    150    -14       C  
ATOM    664  C   GLY A  89      20.747  23.192  -7.969  1.00 40.67           C  
ANISOU  664  C   GLY A  89     4204   7875   3372   1663     81   -167       C  
ATOM    665  O   GLY A  89      19.698  23.827  -7.954  1.00 42.34           O  
ANISOU  665  O   GLY A  89     4410   8095   3581   1589     59    -43       O  
ATOM    666  N   LEU A  90      20.865  22.021  -8.589  1.00 38.86           N  
ANISOU  666  N   LEU A  90     3996   7691   3079   1709     53   -444       N  
ATOM    667  CA  LEU A  90      19.709  21.408  -9.237  1.00 39.90           C  
ANISOU  667  CA  LEU A  90     4146   7886   3129   1650     -8   -627       C  
ATOM    668  C   LEU A  90      18.539  21.195  -8.258  1.00 38.09           C  
ANISOU  668  C   LEU A  90     4060   7407   3004   1557    -79   -678       C  
ATOM    669  O   LEU A  90      17.385  21.323  -8.644  1.00 37.25           O  
ANISOU  669  O   LEU A  90     3933   7373   2848   1469   -120   -680       O  
ATOM    670  CB  LEU A  90      20.104  20.108  -9.941  1.00 42.38           C  
ANISOU  670  CB  LEU A  90     4463   8239   3400   1701    -11   -956       C  
ATOM    671  CG  LEU A  90      21.112  20.347 -11.075  1.00 40.28           C  
ANISOU  671  CG  LEU A  90     4033   8283   2987   1770     53   -919       C  
ATOM    672  CD1 LEU A  90      21.452  19.052 -11.789  1.00 51.27           C  
ANISOU  672  CD1 LEU A  90     5418   9714   4348   1815     61  -1278       C  
ATOM    673  CD2 LEU A  90      20.534  21.359 -12.051  1.00 44.49           C  
ANISOU  673  CD2 LEU A  90     4413   9142   3350   1719     60   -695       C  
HETATM  674  N   MSE A  91      18.821  20.900  -6.990  1.00 37.47           N  
ANISOU  674  N   MSE A  91     4112   7054   3069   1571    -94   -709       N  
HETATM  675  CA  MSE A  91      17.720  20.738  -6.034  1.00 35.55           C  
ANISOU  675  CA  MSE A  91     4000   6586   2923   1454   -174   -736       C  
HETATM  676  C   MSE A  91      16.904  22.027  -5.850  1.00 31.48           C  
ANISOU  676  C   MSE A  91     3427   6138   2394   1364   -183   -478       C  
HETATM  677  O   MSE A  91      15.704  21.981  -5.574  1.00 29.14           O  
ANISOU  677  O   MSE A  91     3173   5766   2131   1252   -244   -508       O  
HETATM  678  CB  MSE A  91      18.189  20.171  -4.686  1.00 37.02           C  
ANISOU  678  CB  MSE A  91     4310   6394   3361   1429   -211   -741       C  
HETATM  679  CG  MSE A  91      18.316  18.645  -4.678  1.00 46.05           C  
ANISOU  679  CG  MSE A  91     5558   7349   4591   1474   -241  -1022       C  
HETATM  680 SE   MSE A  91      16.607  17.671  -4.860  0.52 55.94          SE  
ANISOU  680 SE   MSE A  91     6921   8505   5828   1313   -322  -1289      SE  
HETATM  681  CE  MSE A  91      15.403  18.971  -4.082  1.00 43.51           C  
ANISOU  681  CE  MSE A  91     5332   6959   4240   1136   -367  -1012       C  
HETATM  682  N   MSE A  92      17.538  23.181  -6.016  1.00 31.07           N  
ANISOU  682  N   MSE A  92     3265   6202   2341   1406   -111   -221       N  
HETATM  683  CA  MSE A  92      16.789  24.432  -5.910  1.00 31.14           C  
ANISOU  683  CA  MSE A  92     3205   6215   2410   1333    -99     23       C  
HETATM  684  C   MSE A  92      15.764  24.534  -7.042  1.00 35.81           C  
ANISOU  684  C   MSE A  92     3708   7006   2891   1309   -100     19       C  
HETATM  685  O   MSE A  92      14.660  25.082  -6.850  1.00 29.97           O  
ANISOU  685  O   MSE A  92     2957   6226   2203   1237   -124    104       O  
HETATM  686  CB  MSE A  92      17.735  25.636  -5.927  1.00 29.58           C  
ANISOU  686  CB  MSE A  92     2899   6059   2280   1370     -5    299       C  
HETATM  687  CG  MSE A  92      18.558  25.788  -4.659  1.00 28.12           C  
ANISOU  687  CG  MSE A  92     2763   5602   2320   1325      5    317       C  
HETATM  688 SE   MSE A  92      17.421  26.140  -3.123  0.47 27.96          SE  
ANISOU  688 SE   MSE A  92     2837   5261   2525   1163    -65    303      SE  
HETATM  689  CE  MSE A  92      16.728  27.877  -3.643  1.00 31.53           C  
ANISOU  689  CE  MSE A  92     3141   5786   3051   1156      2    600       C  
ATOM    690  N   LEU A  93      16.121  23.998  -8.216  1.00 33.16           N  
ANISOU  690  N   LEU A  93     3294   6903   2405   1370    -82    -86       N  
ATOM    691  CA  LEU A  93      15.215  24.011  -9.374  1.00 33.81           C  
ANISOU  691  CA  LEU A  93     3264   7229   2354   1348    -97   -103       C  
ATOM    692  C   LEU A  93      14.027  23.083  -9.166  1.00 35.45           C  
ANISOU  692  C   LEU A  93     3556   7347   2565   1251   -186   -347       C  
ATOM    693  O   LEU A  93      12.890  23.434  -9.478  1.00 36.26           O  
ANISOU  693  O   LEU A  93     3598   7546   2635   1195   -211   -293       O  
ATOM    694  CB  LEU A  93      15.955  23.598 -10.648  1.00 40.73           C  
ANISOU  694  CB  LEU A  93     4022   8394   3060   1420    -67   -184       C  
ATOM    695  CG  LEU A  93      17.216  24.400 -10.980  1.00 38.05           C  
ANISOU  695  CG  LEU A  93     3576   8181   2699   1504     21     45       C  
ATOM    696  CD1 LEU A  93      17.799  23.913 -12.296  1.00 42.50           C  
ANISOU  696  CD1 LEU A  93     4012   9065   3070   1557     33    -66       C  
ATOM    697  CD2 LEU A  93      16.890  25.883 -11.044  1.00 34.32           C  
ANISOU  697  CD2 LEU A  93     3006   7751   2283   1490     85    413       C  
ATOM    698  N   VAL A  94      14.307  21.888  -8.651  1.00 36.08           N  
ANISOU  698  N   VAL A  94     3771   7242   2696   1231   -228   -612       N  
ATOM    699  CA  VAL A  94      13.273  20.907  -8.343  1.00 35.95           C  
ANISOU  699  CA  VAL A  94     3850   7089   2720   1114   -302   -850       C  
ATOM    700  C   VAL A  94      12.274  21.457  -7.340  1.00 33.13           C  
ANISOU  700  C   VAL A  94     3545   6571   2473   1015   -342   -730       C  
ATOM    701  O   VAL A  94      11.059  21.384  -7.562  1.00 34.54           O  
ANISOU  701  O   VAL A  94     3685   6812   2627    922   -381   -777       O  
ATOM    702  CB  VAL A  94      13.881  19.596  -7.789  1.00 37.62           C  
ANISOU  702  CB  VAL A  94     4214   7057   3022   1119   -321  -1116       C  
ATOM    703  CG1 VAL A  94      12.778  18.676  -7.261  1.00 32.45           C  
ANISOU  703  CG1 VAL A  94     3672   6202   2456    969   -389  -1317       C  
ATOM    704  CG2 VAL A  94      14.700  18.897  -8.876  1.00 41.40           C  
ANISOU  704  CG2 VAL A  94     4629   7695   3407   1207   -280  -1304       C  
ATOM    705  N   ARG A  95      12.780  22.009  -6.234  1.00 34.26           N  
ANISOU  705  N   ARG A  95     3757   6527   2733   1031   -332   -585       N  
ATOM    706  CA  ARG A  95      11.910  22.655  -5.243  1.00 31.55           C  
ANISOU  706  CA  ARG A  95     3438   6051   2500    939   -364   -470       C  
ATOM    707  C   ARG A  95      11.082  23.743  -5.916  1.00 31.08           C  
ANISOU  707  C   ARG A  95     3229   6183   2396    951   -338   -284       C  
ATOM    708  O   ARG A  95       9.867  23.812  -5.747  1.00 35.23           O  
ANISOU  708  O   ARG A  95     3732   6716   2939    869   -379   -309       O  
ATOM    709  CB  ARG A  95      12.734  23.259  -4.101  1.00 29.44           C  
ANISOU  709  CB  ARG A  95     3221   5610   2354    964   -348   -326       C  
ATOM    710  CG  ARG A  95      13.400  22.226  -3.206  1.00 30.19           C  
ANISOU  710  CG  ARG A  95     3462   5465   2545    936   -375   -469       C  
ATOM    711  CD  ARG A  95      14.542  22.850  -2.400  1.00 34.13           C  
ANISOU  711  CD  ARG A  95     3959   5823   3187    969   -323   -306       C  
ATOM    712  NE  ARG A  95      15.296  21.842  -1.660  1.00 34.31           N  
ANISOU  712  NE  ARG A  95     4092   5637   3305    968   -346   -400       N  
ATOM    713  CZ  ARG A  95      16.558  21.987  -1.270  1.00 35.67           C  
ANISOU  713  CZ  ARG A  95     4249   5753   3551   1038   -311   -318       C  
ATOM    714  NH1 ARG A  95      17.220  23.102  -1.546  1.00 43.94           N  
ANISOU  714  NH1 ARG A  95     5179   6921   4594   1090   -242   -159       N  
ATOM    715  NH2 ARG A  95      17.159  21.019  -0.605  1.00 34.39           N  
ANISOU  715  NH2 ARG A  95     4174   5414   3478   1055   -345   -381       N  
ATOM    716  N   GLY A  96      11.751  24.584  -6.694  1.00 34.40           N  
ANISOU  716  N   GLY A  96     3543   6767   2760   1056   -264    -87       N  
ATOM    717  CA  GLY A  96      11.078  25.634  -7.439  1.00 37.31           C  
ANISOU  717  CA  GLY A  96     3770   7319   3086   1086   -227    127       C  
ATOM    718  C   GLY A  96       9.925  25.150  -8.301  1.00 39.57           C  
ANISOU  718  C   GLY A  96     3978   7818   3237   1048   -275      7       C  
ATOM    719  O   GLY A  96       8.871  25.787  -8.349  1.00 39.34           O  
ANISOU  719  O   GLY A  96     3877   7850   3222   1031   -288    119       O  
HETATM  720  N   MSE A  97      10.113  24.032  -8.998  1.00 37.70           N  
ANISOU  720  N   MSE A  97     3745   7701   2879   1035   -300   -228       N  
HETATM  721  CA  MSE A  97       9.070  23.544  -9.892  1.00 39.27           C  
ANISOU  721  CA  MSE A  97     3848   8130   2943    986   -343   -361       C  
HETATM  722  C   MSE A  97       7.990  22.768  -9.148  1.00 40.83           C  
ANISOU  722  C   MSE A  97     4134   8160   3219    847   -417   -568       C  
HETATM  723  O   MSE A  97       6.817  22.805  -9.519  1.00 40.31           O  
ANISOU  723  O   MSE A  97     3975   8247   3093    794   -450   -592       O  
HETATM  724  CB  MSE A  97       9.662  22.684 -11.003  1.00 39.50           C  
ANISOU  724  CB  MSE A  97     3822   8372   2816   1013   -335   -551       C  
HETATM  725  CG  MSE A  97      10.391  23.470 -12.066  1.00 43.53           C  
ANISOU  725  CG  MSE A  97     4174   9175   3190   1130   -265   -339       C  
HETATM  726 SE   MSE A  97      11.102  22.232 -13.359  0.44 46.60          SE  
ANISOU  726 SE   MSE A  97     4487   9840   3380   1147   -268   -651      SE  
HETATM  727  CE  MSE A  97      12.376  21.282 -12.236  1.00 42.76           C  
ANISOU  727  CE  MSE A  97     4230   8945   3073   1161   -264   -859       C  
ATOM    728  N   GLU A  98       8.388  22.053  -8.104  1.00 37.41           N  
ANISOU  728  N   GLU A  98     3870   7428   2917    783   -441   -708       N  
ATOM    729  CA  GLU A  98       7.422  21.298  -7.322  1.00 39.68           C  
ANISOU  729  CA  GLU A  98     4245   7536   3294    629   -499   -880       C  
ATOM    730  C   GLU A  98       6.561  22.196  -6.441  1.00 36.04           C  
ANISOU  730  C   GLU A  98     3759   7007   2929    589   -512   -720       C  
ATOM    731  O   GLU A  98       5.394  21.900  -6.208  1.00 42.05           O  
ANISOU  731  O   GLU A  98     4497   7771   3707    475   -551   -810       O  
ATOM    732  CB  GLU A  98       8.128  20.241  -6.480  1.00 40.10           C  
ANISOU  732  CB  GLU A  98     4484   7294   3457    573   -514  -1054       C  
ATOM    733  CG  GLU A  98       8.623  19.076  -7.303  1.00 43.99           C  
ANISOU  733  CG  GLU A  98     5004   7823   3887    581   -509  -1304       C  
ATOM    734  CD  GLU A  98       7.471  18.306  -7.920  1.00 50.85           C  
ANISOU  734  CD  GLU A  98     5823   8793   4704    453   -543  -1511       C  
ATOM    735  OE1 GLU A  98       6.850  17.498  -7.193  1.00 54.69           O  
ANISOU  735  OE1 GLU A  98     6417   9056   5305    304   -577  -1653       O  
ATOM    736  OE2 GLU A  98       7.178  18.523  -9.118  1.00 52.58           O  
ANISOU  736  OE2 GLU A  98     5884   9329   4766    493   -534  -1523       O  
ATOM    737  N   LEU A  99       7.135  23.305  -5.985  1.00 32.40           N  
ANISOU  737  N   LEU A  99     3283   6496   2532    682   -474   -492       N  
ATOM    738  CA  LEU A  99       6.512  24.142  -4.955  1.00 36.59           C  
ANISOU  738  CA  LEU A  99     3798   6919   3188    650   -482   -372       C  
ATOM    739  C   LEU A  99       6.024  25.480  -5.519  1.00 38.83           C  
ANISOU  739  C   LEU A  99     3922   7376   3455    756   -451   -126       C  
ATOM    740  O   LEU A  99       5.508  26.316  -4.784  1.00 37.40           O  
ANISOU  740  O   LEU A  99     3696   7113   3399    759   -453    -16       O  
ATOM    741  CB  LEU A  99       7.503  24.368  -3.800  1.00 28.71           C  
ANISOU  741  CB  LEU A  99     2904   5685   2317    656   -467   -320       C  
ATOM    742  CG  LEU A  99       8.011  23.080  -3.124  1.00 29.91           C  
ANISOU  742  CG  LEU A  99     3225   5640   2501    560   -497   -521       C  
ATOM    743  CD1 LEU A  99       9.097  23.334  -2.063  1.00 23.52           C  
ANISOU  743  CD1 LEU A  99     2498   4652   1787    585   -483   -449       C  
ATOM    744  CD2 LEU A  99       6.861  22.301  -2.508  1.00 37.88           C  
ANISOU  744  CD2 LEU A  99     4281   6559   3553    383   -543   -681       C  
ATOM    745  N   ASP A 100       6.193  25.669  -6.828  1.00 39.40           N  
ANISOU  745  N   ASP A 100     3902   7686   3385    842   -419    -39       N  
ATOM    746  CA  ASP A 100       5.763  26.894  -7.518  1.00 43.08           C  
ANISOU  746  CA  ASP A 100     4224   8318   3827    942   -382    234       C  
ATOM    747  C   ASP A 100       6.487  28.129  -6.977  1.00 37.30           C  
ANISOU  747  C   ASP A 100     3503   7392   3276   1018   -319    498       C  
ATOM    748  O   ASP A 100       5.856  29.096  -6.533  1.00 31.48           O  
ANISOU  748  O   ASP A 100     2709   6556   2695   1044   -317    652       O  
ATOM    749  CB  ASP A 100       4.247  27.109  -7.401  1.00 47.38           C  
ANISOU  749  CB  ASP A 100     4677   8945   4379    905   -434    223       C  
ATOM    750  CG  ASP A 100       3.438  26.008  -8.056  1.00 56.54           C  
ANISOU  750  CG  ASP A 100     5793  10315   5374    818   -486    -17       C  
ATOM    751  OD1 ASP A 100       3.945  25.343  -8.985  1.00 56.66           O  
ANISOU  751  OD1 ASP A 100     5796  10489   5245    824   -476   -116       O  
ATOM    752  OD2 ASP A 100       2.272  25.825  -7.640  1.00 63.70           O  
ANISOU  752  OD2 ASP A 100     6661  11234   6308    738   -534   -115       O  
ATOM    753  N   TRP A 101       7.811  28.101  -6.996  1.00 32.08           N  
ANISOU  753  N   TRP A 101     2904   6659   2626   1051   -265    537       N  
ATOM    754  CA  TRP A 101       8.554  29.274  -6.569  1.00 35.48           C  
ANISOU  754  CA  TRP A 101     3330   6901   3249   1102   -193    782       C  
ATOM    755  C   TRP A 101       8.891  30.122  -7.778  1.00 35.94           C  
ANISOU  755  C   TRP A 101     3277   7137   3243   1187   -113   1059       C  
ATOM    756  O   TRP A 101       8.923  29.622  -8.895  1.00 39.00           O  
ANISOU  756  O   TRP A 101     3600   7813   3406   1213   -108   1025       O  
ATOM    757  CB  TRP A 101       9.865  28.875  -5.908  1.00 31.14           C  
ANISOU  757  CB  TRP A 101     2884   6192   2755   1085   -169    701       C  
ATOM    758  CG  TRP A 101       9.755  28.133  -4.613  1.00 32.95           C  
ANISOU  758  CG  TRP A 101     3218   6236   3066   1001   -237    477       C  
ATOM    759  CD1 TRP A 101       8.625  27.880  -3.882  1.00 35.80           C  
ANISOU  759  CD1 TRP A 101     3581   6546   3474    924   -307    348       C  
ATOM    760  CD2 TRP A 101      10.841  27.527  -3.905  1.00 29.90           C  
ANISOU  760  CD2 TRP A 101     2933   5719   2708    980   -241    368       C  
ATOM    761  NE1 TRP A 101       8.955  27.159  -2.747  1.00 34.85           N  
ANISOU  761  NE1 TRP A 101     3564   6275   3403    842   -351    173       N  
ATOM    762  CE2 TRP A 101      10.308  26.929  -2.743  1.00 32.46           C  
ANISOU  762  CE2 TRP A 101     3328   5913   3091    882   -317    190       C  
ATOM    763  CE3 TRP A 101      12.218  27.442  -4.141  1.00 27.58           C  
ANISOU  763  CE3 TRP A 101     2664   5423   2391   1035   -187    412       C  
ATOM    764  CZ2 TRP A 101      11.106  26.252  -1.814  1.00 30.52           C  
ANISOU  764  CZ2 TRP A 101     3215   5466   2914    808   -311     64       C  
ATOM    765  CZ3 TRP A 101      13.020  26.765  -3.209  1.00 25.89           C  
ANISOU  765  CZ3 TRP A 101     2549   5061   2227   1007   -216    283       C  
ATOM    766  CH2 TRP A 101      12.452  26.175  -2.068  1.00 30.37           C  
ANISOU  766  CH2 TRP A 101     3218   5438   2881    881   -266    114       C  
ATOM    767  N   GLU A 102       9.162  31.401  -7.548  1.00 34.97           N  
ANISOU  767  N   GLU A 102     3114   6838   3337   1224    -47   1327       N  
ATOM    768  CA  GLU A 102       9.860  32.207  -8.534  1.00 37.12           C  
ANISOU  768  CA  GLU A 102     3289   7228   3585   1287     50   1617       C  
ATOM    769  C   GLU A 102      11.357  31.986  -8.315  1.00 37.24           C  
ANISOU  769  C   GLU A 102     3361   7176   3612   1274    112   1592       C  
ATOM    770  O   GLU A 102      11.867  32.242  -7.226  1.00 37.80           O  
ANISOU  770  O   GLU A 102     3503   6960   3898   1236    123   1560       O  
ATOM    771  CB  GLU A 102       9.528  33.680  -8.333  1.00 47.14           C  
ANISOU  771  CB  GLU A 102     4484   8286   5139   1324    102   1914       C  
ATOM    772  CG  GLU A 102      10.214  34.609  -9.319  1.00 57.54           C  
ANISOU  772  CG  GLU A 102     5681   9706   6474   1378    212   2262       C  
ATOM    773  CD  GLU A 102      10.033  36.074  -8.962  1.00 69.90           C  
ANISOU  773  CD  GLU A 102     7180  10971   8407   1406    277   2543       C  
ATOM    774  OE1 GLU A 102      10.573  36.932  -9.694  1.00 78.32           O  
ANISOU  774  OE1 GLU A 102     8133  12080   9546   1441    376   2862       O  
ATOM    775  OE2 GLU A 102       9.351  36.372  -7.957  1.00 72.42           O  
ANISOU  775  OE2 GLU A 102     7540  11011   8964   1395    237   2437       O  
ATOM    776  N   LEU A 103      12.062  31.505  -9.335  1.00 36.70           N  
ANISOU  776  N   LEU A 103     3235   7389   3318   1309    151   1589       N  
ATOM    777  CA  LEU A 103      13.492  31.242  -9.199  1.00 36.30           C  
ANISOU  777  CA  LEU A 103     3214   7317   3261   1313    207   1558       C  
ATOM    778  C   LEU A 103      14.324  32.351  -9.826  1.00 38.22           C  
ANISOU  778  C   LEU A 103     3325   7617   3578   1348    327   1903       C  
ATOM    779  O   LEU A 103      14.138  32.698 -11.002  1.00 45.49           O  
ANISOU  779  O   LEU A 103     4098   8812   4374   1395    362   2084       O  
ATOM    780  CB  LEU A 103      13.872  29.892  -9.823  1.00 37.82           C  
ANISOU  780  CB  LEU A 103     3410   7764   3197   1340    169   1286       C  
ATOM    781  CG  LEU A 103      13.158  28.658  -9.278  1.00 43.02           C  
ANISOU  781  CG  LEU A 103     4187   8357   3800   1295     56    938       C  
ATOM    782  CD1 LEU A 103      13.436  27.445 -10.137  1.00 44.57           C  
ANISOU  782  CD1 LEU A 103     4352   8798   3783   1325     21    690       C  
ATOM    783  CD2 LEU A 103      13.596  28.406  -7.845  1.00 42.56           C  
ANISOU  783  CD2 LEU A 103     4278   7979   3914   1248     27    823       C  
ATOM    784  N   THR A 104      15.238  32.909  -9.040  1.00 35.93           N  
ANISOU  784  N   THR A 104     3069   7080   3504   1317    386   1998       N  
ATOM    785  CA  THR A 104      16.238  33.828  -9.564  1.00 40.87           C  
ANISOU  785  CA  THR A 104     3557   7753   4217   1334    506   2306       C  
ATOM    786  C   THR A 104      17.589  33.127  -9.590  1.00 42.74           C  
ANISOU  786  C   THR A 104     3793   8119   4329   1349    534   2185       C  
ATOM    787  O   THR A 104      18.199  32.885  -8.553  1.00 36.87           O  
ANISOU  787  O   THR A 104     3152   7166   3690   1311    523   2061       O  
ATOM    788  CB  THR A 104      16.349  35.098  -8.713  1.00 40.52           C  
ANISOU  788  CB  THR A 104     3505   7326   4564   1286    569   2525       C  
ATOM    789  OG1 THR A 104      15.113  35.810  -8.758  1.00 42.31           O  
ANISOU  789  OG1 THR A 104     3706   7435   4933   1297    548   2644       O  
ATOM    790  CG2 THR A 104      17.477  35.997  -9.225  1.00 36.71           C  
ANISOU  790  CG2 THR A 104     2863   6876   4209   1288    699   2846       C  
ATOM    791  N   VAL A 105      18.052  32.784 -10.782  1.00 39.62           N  
ANISOU  791  N   VAL A 105     3263   8079   3712   1415    550   2207       N  
ATOM    792  CA  VAL A 105      19.258  32.001 -10.898  1.00 41.80           C  
ANISOU  792  CA  VAL A 105     3523   8500   3859   1456    542   2048       C  
ATOM    793  C   VAL A 105      20.431  32.918 -11.184  1.00 42.90           C  
ANISOU  793  C   VAL A 105     3525   8663   4113   1459    617   2343       C  
ATOM    794  O   VAL A 105      20.398  33.690 -12.143  1.00 42.35           O  
ANISOU  794  O   VAL A 105     3305   8750   4035   1472    658   2617       O  
ATOM    795  CB  VAL A 105      19.144  30.955 -12.021  1.00 47.49           C  
ANISOU  795  CB  VAL A 105     4188   9577   4277   1522    469   1836       C  
ATOM    796  CG1 VAL A 105      20.376  30.057 -12.032  1.00 46.54           C  
ANISOU  796  CG1 VAL A 105     4091   9547   4046   1566    436   1627       C  
ATOM    797  CG2 VAL A 105      17.870  30.133 -11.848  1.00 46.90           C  
ANISOU  797  CG2 VAL A 105     4226   9473   4119   1505    382   1571       C  
ATOM    798  N   THR A 106      21.464  32.833 -10.353  1.00 43.36           N  
ANISOU  798  N   THR A 106     3657   8550   4268   1431    620   2292       N  
ATOM    799  CA  THR A 106      22.666  33.634 -10.553  1.00 49.50           C  
ANISOU  799  CA  THR A 106     4351   9312   5143   1395    687   2535       C  
ATOM    800  C   THR A 106      23.884  32.727 -10.711  1.00 47.32           C  
ANISOU  800  C   THR A 106     4116   9195   4670   1405    673   2312       C  
ATOM    801  O   THR A 106      23.840  31.559 -10.326  1.00 43.78           O  
ANISOU  801  O   THR A 106     3781   8760   4092   1443    605   1987       O  
ATOM    802  CB  THR A 106      22.905  34.595  -9.380  1.00 48.74           C  
ANISOU  802  CB  THR A 106     4308   8808   5403   1281    764   2671       C  
ATOM    803  OG1 THR A 106      23.956  35.506  -9.721  1.00 57.63           O  
ANISOU  803  OG1 THR A 106     5327   9899   6670   1210    861   2900       O  
ATOM    804  CG2 THR A 106      23.320  33.825  -8.159  1.00 42.46           C  
ANISOU  804  CG2 THR A 106     3659   7831   4643   1215    747   2337       C  
ATOM    805  N   GLU A 107      24.960  33.260 -11.284  1.00 49.72           N  
ANISOU  805  N   GLU A 107     4312   9607   4973   1370    746   2481       N  
ATOM    806  CA  GLU A 107      26.188  32.492 -11.430  1.00 54.14           C  
ANISOU  806  CA  GLU A 107     4875  10316   5380   1377    758   2275       C  
ATOM    807  C   GLU A 107      26.780  32.285 -10.053  1.00 54.47           C  
ANISOU  807  C   GLU A 107     5024  10057   5615   1300    780   2089       C  
ATOM    808  O   GLU A 107      26.828  33.213  -9.244  1.00 57.59           O  
ANISOU  808  O   GLU A 107     5416  10169   6296   1188    840   2222       O  
ATOM    809  CB  GLU A 107      27.187  33.192 -12.366  1.00 59.84           C  
ANISOU  809  CB  GLU A 107     5434  11242   6059   1342    843   2513       C  
ATOM    810  CG  GLU A 107      26.568  33.597 -13.693  1.00 67.16           C  
ANISOU  810  CG  GLU A 107     6219  12464   6835   1398    829   2745       C  
ATOM    811  CD  GLU A 107      27.586  33.893 -14.795  1.00 74.11           C  
ANISOU  811  CD  GLU A 107     6937  13661   7560   1383    896   2902       C  
ATOM    812  OE1 GLU A 107      28.768  34.174 -14.488  1.00 74.68           O  
ANISOU  812  OE1 GLU A 107     6991  13660   7722   1304    978   2927       O  
ATOM    813  OE2 GLU A 107      27.189  33.844 -15.980  1.00 73.98           O  
ANISOU  813  OE2 GLU A 107     6795  13988   7325   1441    870   2992       O  
ATOM    814  N   PRO A 108      27.217  31.055  -9.767  1.00 53.23           N  
ANISOU  814  N   PRO A 108     4942   9951   5335   1358    729   1762       N  
ATOM    815  CA  PRO A 108      27.661  30.782  -8.405  1.00 46.06           C  
ANISOU  815  CA  PRO A 108     4111   8768   4620   1298    723   1575       C  
ATOM    816  C   PRO A 108      28.969  31.523  -8.150  1.00 46.66           C  
ANISOU  816  C   PRO A 108     4073   8800   4856   1194    814   1676       C  
ATOM    817  O   PRO A 108      29.922  31.377  -8.922  1.00 51.24           O  
ANISOU  817  O   PRO A 108     4557   9610   5302   1223    856   1690       O  
ATOM    818  CB  PRO A 108      27.873  29.269  -8.413  1.00 49.54           C  
ANISOU  818  CB  PRO A 108     4629   9303   4892   1415    646   1245       C  
ATOM    819  CG  PRO A 108      28.269  28.960  -9.823  1.00 55.39           C  
ANISOU  819  CG  PRO A 108     5273  10391   5383   1498    662   1253       C  
ATOM    820  CD  PRO A 108      27.561  29.968 -10.701  1.00 56.92           C  
ANISOU  820  CD  PRO A 108     5382  10720   5524   1471    687   1559       C  
ATOM    821  N   THR A 109      28.987  32.338  -7.103  1.00 37.10           N  
ANISOU  821  N   THR A 109     2855   7308   3933   1062    847   1728       N  
ATOM    822  CA  THR A 109      30.167  33.085  -6.694  1.00 44.01           C  
ANISOU  822  CA  THR A 109     3612   8111   4998    931    929   1780       C  
ATOM    823  C   THR A 109      30.169  33.130  -5.172  1.00 40.78           C  
ANISOU  823  C   THR A 109     3237   7434   4823    833    888   1597       C  
ATOM    824  O   THR A 109      29.227  32.652  -4.534  1.00 40.06           O  
ANISOU  824  O   THR A 109     3261   7219   4742    870    805   1471       O  
ATOM    825  CB  THR A 109      30.145  34.534  -7.195  1.00 48.26           C  
ANISOU  825  CB  THR A 109     4048   8579   5710    819   1039   2110       C  
ATOM    826  OG1 THR A 109      28.986  35.192  -6.667  1.00 48.82           O  
ANISOU  826  OG1 THR A 109     4174   8382   5993    773   1035   2200       O  
ATOM    827  CG2 THR A 109      30.100  34.580  -8.691  1.00 51.59           C  
ANISOU  827  CG2 THR A 109     4412   9296   5893    910   1064   2328       C  
ATOM    828  N   ALA A 110      31.217  33.716  -4.596  1.00 39.09           N  
ANISOU  828  N   ALA A 110     2908   7158   4787    700    943   1574       N  
ATOM    829  CA  ALA A 110      31.375  33.765  -3.142  1.00 39.50           C  
ANISOU  829  CA  ALA A 110     2953   7026   5030    594    895   1376       C  
ATOM    830  C   ALA A 110      30.345  34.687  -2.505  1.00 41.42           C  
ANISOU  830  C   ALA A 110     3222   6995   5522    478    916   1423       C  
ATOM    831  O   ALA A 110      29.933  34.488  -1.357  1.00 43.21           O  
ANISOU  831  O   ALA A 110     3488   7092   5837    432    845   1237       O  
ATOM    832  CB  ALA A 110      32.779  34.220  -2.775  1.00 34.43           C  
ANISOU  832  CB  ALA A 110     2151   6429   4502    467    953   1329       C  
ATOM    833  N   ASN A 111      29.938  35.705  -3.253  1.00 38.37           N  
ANISOU  833  N   ASN A 111     2803   6524   5254    435   1015   1680       N  
ATOM    834  CA  ASN A 111      28.962  36.660  -2.748  1.00 39.43           C  
ANISOU  834  CA  ASN A 111     2949   6360   5672    341   1051   1742       C  
ATOM    835  C   ASN A 111      27.772  36.783  -3.684  1.00 37.31           C  
ANISOU  835  C   ASN A 111     2748   6092   5335    466   1054   1983       C  
ATOM    836  O   ASN A 111      27.809  37.559  -4.640  1.00 36.18           O  
ANISOU  836  O   ASN A 111     2544   5960   5243    469   1138   2282       O  
ATOM    837  CB  ASN A 111      29.601  38.032  -2.524  1.00 43.92           C  
ANISOU  837  CB  ASN A 111     3390   6724   6573    140   1175   1827       C  
ATOM    838  CG  ASN A 111      28.697  38.973  -1.734  1.00 44.09           C  
ANISOU  838  CG  ASN A 111     3422   6384   6946     29   1207   1789       C  
ATOM    839  OD1 ASN A 111      27.464  38.932  -1.863  1.00 37.51           O  
ANISOU  839  OD1 ASN A 111     2670   5451   6131    127   1178   1866       O  
ATOM    840  ND2 ASN A 111      29.310  39.819  -0.903  1.00 42.99           N  
ANISOU  840  ND2 ASN A 111     3191   6057   7086   -178   1268   1641       N  
ATOM    841  N   PRO A 112      26.716  36.010  -3.407  1.00 37.60           N  
ANISOU  841  N   PRO A 112     2900   6138   5249    569    955   1860       N  
ATOM    842  CA  PRO A 112      25.505  35.968  -4.233  1.00 40.32           C  
ANISOU  842  CA  PRO A 112     3299   6537   5485    697    936   2044       C  
ATOM    843  C   PRO A 112      24.743  37.296  -4.308  1.00 44.53           C  
ANISOU  843  C   PRO A 112     3771   6805   6342    645   1022   2295       C  
ATOM    844  O   PRO A 112      23.944  37.464  -5.227  1.00 50.39           O  
ANISOU  844  O   PRO A 112     4508   7641   6999    757   1023   2546       O  
ATOM    845  CB  PRO A 112      24.644  34.905  -3.543  1.00 40.07           C  
ANISOU  845  CB  PRO A 112     3396   6505   5323    764    808   1776       C  
ATOM    846  CG  PRO A 112      25.234  34.737  -2.192  1.00 41.24           C  
ANISOU  846  CG  PRO A 112     3541   6523   5604    650    776   1510       C  
ATOM    847  CD  PRO A 112      26.679  35.021  -2.318  1.00 33.85           C  
ANISOU  847  CD  PRO A 112     2502   5664   4695    576    843   1537       C  
ATOM    848  N   LEU A 113      24.969  38.207  -3.366  1.00 39.40           N  
ANISOU  848  N   LEU A 113     3066   5838   6064    485   1087   2218       N  
ATOM    849  CA  LEU A 113      24.265  39.487  -3.370  1.00 40.82           C  
ANISOU  849  CA  LEU A 113     3189   5694   6626    441   1177   2424       C  
ATOM    850  C   LEU A 113      25.068  40.577  -4.059  1.00 45.10           C  
ANISOU  850  C   LEU A 113     3630   6144   7363    372   1294   2712       C  
ATOM    851  O   LEU A 113      24.545  41.651  -4.363  1.00 46.04           O  
ANISOU  851  O   LEU A 113     3697   6007   7790    379   1366   2964       O  
ATOM    852  CB  LEU A 113      23.938  39.933  -1.943  1.00 39.92           C  
ANISOU  852  CB  LEU A 113     3075   5250   6845    302   1185   2124       C  
ATOM    853  CG  LEU A 113      22.816  39.200  -1.209  1.00 39.71           C  
ANISOU  853  CG  LEU A 113     3134   5227   6728    365   1079   1879       C  
ATOM    854  CD1 LEU A 113      22.480  39.956   0.074  1.00 38.89           C  
ANISOU  854  CD1 LEU A 113     3006   4780   6991    212   1112   1611       C  
ATOM    855  CD2 LEU A 113      21.581  39.061  -2.089  1.00 38.81           C  
ANISOU  855  CD2 LEU A 113     3079   5181   6487    546   1027   2098       C  
ATOM    856  N   ALA A 114      26.339  40.295  -4.310  1.00 47.48           N  
ANISOU  856  N   ALA A 114     3895   6649   7497    316   1308   2673       N  
ATOM    857  CA  ALA A 114      27.260  41.325  -4.783  1.00 54.69           C  
ANISOU  857  CA  ALA A 114     4701   7469   8608    209   1420   2881       C  
ATOM    858  C   ALA A 114      26.826  41.945  -6.100  1.00 61.81           C  
ANISOU  858  C   ALA A 114     5554   8422   9509    328   1457   3325       C  
ATOM    859  O   ALA A 114      26.943  43.157  -6.288  1.00 69.71           O  
ANISOU  859  O   ALA A 114     6475   9158  10852    257   1552   3539       O  
ATOM    860  CB  ALA A 114      28.681  40.776  -4.896  1.00 54.73           C  
ANISOU  860  CB  ALA A 114     4658   7752   8383    144   1423   2755       C  
ATOM    861  N   GLY A 115      26.324  41.118  -7.010  1.00 62.67           N  
ANISOU  861  N   GLY A 115     5697   8885   9231    510   1375   3443       N  
ATOM    862  CA  GLY A 115      26.007  41.586  -8.350  1.00 71.22           C  
ANISOU  862  CA  GLY A 115     6695  10136  10227    629   1383   3836       C  
ATOM    863  C   GLY A 115      24.629  42.194  -8.548  1.00 74.47           C  
ANISOU  863  C   GLY A 115     7083  10377  10836    740   1368   4049       C  
ATOM    864  O   GLY A 115      24.380  42.877  -9.538  1.00 77.60           O  
ANISOU  864  O   GLY A 115     7365  10851  11270    812   1392   4384       O  
ATOM    865  N   LEU A 116      23.709  41.931  -7.631  1.00 72.65           N  
ANISOU  865  N   LEU A 116     6937   9935  10731    750   1332   3850       N  
ATOM    866  CA  LEU A 116      22.340  42.379  -7.838  1.00 79.13           C  
ANISOU  866  CA  LEU A 116     7722  10653  11693    871   1310   4011       C  
ATOM    867  C   LEU A 116      21.788  43.213  -6.695  1.00 84.30           C  
ANISOU  867  C   LEU A 116     8385  10782  12862    789   1375   3903       C  
ATOM    868  O   LEU A 116      21.620  42.718  -5.582  1.00 84.36           O  
ANISOU  868  O   LEU A 116     8487  10640  12926    707   1360   3578       O  
ATOM    869  CB  LEU A 116      21.424  41.180  -8.094  1.00 78.27           C  
ANISOU  869  CB  LEU A 116     7686  10884  11169    999   1189   3872       C  
ATOM    870  CG  LEU A 116      21.282  40.175  -6.951  1.00 73.91           C  
ANISOU  870  CG  LEU A 116     7280  10411  10390    946   1134   3505       C  
ATOM    871  CD1 LEU A 116      21.522  38.759  -7.449  1.00 74.44           C  
ANISOU  871  CD1 LEU A 116     7392  10958   9935   1074   1021   3405       C  
ATOM    872  CD2 LEU A 116      22.232  40.514  -5.816  1.00 71.68           C  
ANISOU  872  CD2 LEU A 116     7059   9820  10356    886   1137   3270       C  
ATOM    873  N   ASP A 117      21.488  44.477  -6.974  1.00 88.60           N  
ANISOU  873  N   ASP A 117     8817  11062  13787    804   1452   4141       N  
ATOM    874  CA  ASP A 117      20.782  45.287  -5.993  1.00 93.55           C  
ANISOU  874  CA  ASP A 117     9434  11204  14908    759   1510   4002       C  
ATOM    875  C   ASP A 117      19.272  45.179  -6.192  1.00 88.68           C  
ANISOU  875  C   ASP A 117     8811  10649  14236    894   1452   4051       C  
ATOM    876  O   ASP A 117      18.796  44.661  -7.207  1.00 87.07           O  
ANISOU  876  O   ASP A 117     8595  10850  13637   1005   1380   4223       O  
ATOM    877  CB  ASP A 117      21.235  46.747  -6.008  1.00104.10           C  
ANISOU  877  CB  ASP A 117    10657  12155  16741    680   1637   4146       C  
ATOM    878  CG  ASP A 117      20.786  47.501  -4.766  1.00108.42           C  
ANISOU  878  CG  ASP A 117    11201  12188  17805    594   1707   3851       C  
ATOM    879  OD1 ASP A 117      19.697  48.119  -4.802  1.00111.43           O  
ANISOU  879  OD1 ASP A 117    11515  12391  18431    685   1727   3929       O  
ATOM    880  OD2 ASP A 117      21.515  47.455  -3.749  1.00107.20           O  
ANISOU  880  OD2 ASP A 117    11103  11849  17780    421   1740   3501       O  
ATOM    881  N   HIS A 118      18.530  45.667  -5.206  1.00 83.97           N  
ANISOU  881  N   HIS A 118     8228   9664  14012    859   1483   3841       N  
ATOM    882  CA  HIS A 118      17.098  45.441  -5.151  1.00 79.71           C  
ANISOU  882  CA  HIS A 118     7741   9171  13376    947   1407   3776       C  
ATOM    883  C   HIS A 118      16.806  43.974  -4.871  1.00 63.25           C  
ANISOU  883  C   HIS A 118     5822   7395  10816    973   1266   3531       C  
ATOM    884  O   HIS A 118      15.705  43.492  -5.126  1.00 57.23           O  
ANISOU  884  O   HIS A 118     5133   6823   9788   1056   1158   3477       O  
ATOM    885  CB  HIS A 118      16.422  45.907  -6.438  1.00 88.58           C  
ANISOU  885  CB  HIS A 118     8771  10502  14381   1067   1396   4147       C  
ATOM    886  CG  HIS A 118      16.085  47.359  -6.439  1.00 97.85           C  
ANISOU  886  CG  HIS A 118     9812  11289  16078   1076   1503   4320       C  
ATOM    887  ND1 HIS A 118      16.076  48.119  -5.281  1.00100.55           N  
ANISOU  887  ND1 HIS A 118    10136  11133  16936    988   1590   4065       N  
ATOM    888  CD2 HIS A 118      15.743  48.204  -7.437  1.00103.58           C  
ANISOU  888  CD2 HIS A 118    10406  12045  16904   1162   1542   4706       C  
ATOM    889  CE1 HIS A 118      15.742  49.357  -5.573  1.00105.56           C  
ANISOU  889  CE1 HIS A 118    10641  11499  17970   1025   1678   4280       C  
ATOM    890  NE2 HIS A 118      15.533  49.440  -6.879  1.00107.57           N  
ANISOU  890  NE2 HIS A 118    10826  12057  17989   1135   1649   4698       N  
ATOM    891  N   ALA A 119      17.816  43.275  -4.358  1.00 52.44           N  
ANISOU  891  N   ALA A 119     4506   6076   9344    905   1260   3375       N  
ATOM    892  CA  ALA A 119      17.659  41.912  -3.878  1.00 47.66           C  
ANISOU  892  CA  ALA A 119     4033   5722   8352    936   1116   3057       C  
ATOM    893  C   ALA A 119      16.520  41.877  -2.875  1.00 44.96           C  
ANISOU  893  C   ALA A 119     3762   5187   8135    926   1051   2710       C  
ATOM    894  O   ALA A 119      16.474  42.709  -1.973  1.00 49.73           O  
ANISOU  894  O   ALA A 119     4301   5400   9194    851   1140   2556       O  
ATOM    895  CB  ALA A 119      18.946  41.448  -3.212  1.00 44.59           C  
ANISOU  895  CB  ALA A 119     3678   5375   7889    770   1141   2777       C  
ATOM    896  N   ASP A 120      15.602  40.926  -3.030  1.00 39.33           N  
ANISOU  896  N   ASP A 120     3167   4749   7028    990    906   2565       N  
ATOM    897  CA  ASP A 120      14.529  40.756  -2.060  1.00 39.26           C  
ANISOU  897  CA  ASP A 120     3214   4617   7087    977    838   2233       C  
ATOM    898  C   ASP A 120      13.939  39.351  -2.161  1.00 38.05           C  
ANISOU  898  C   ASP A 120     3186   4817   6455   1015    678   2042       C  
ATOM    899  O   ASP A 120      13.079  39.086  -2.993  1.00 41.98           O  
ANISOU  899  O   ASP A 120     3709   5522   6719   1099    605   2161       O  
ATOM    900  CB  ASP A 120      13.460  41.837  -2.257  1.00 46.50           C  
ANISOU  900  CB  ASP A 120     4065   5311   8293   1032    883   2379       C  
ATOM    901  CG  ASP A 120      12.593  42.035  -1.022  1.00 56.87           C  
ANISOU  901  CG  ASP A 120     5381   6393   9833    994    873   2017       C  
ATOM    902  OD1 ASP A 120      11.509  42.651  -1.154  1.00 63.27           O  
ANISOU  902  OD1 ASP A 120     6150   7100  10789   1063    873   2076       O  
ATOM    903  OD2 ASP A 120      12.990  41.571   0.075  1.00 52.95           O  
ANISOU  903  OD2 ASP A 120     4912   5855   9350    891    869   1666       O  
ATOM    904  N   PHE A 121      14.409  38.445  -1.310  1.00 30.85           N  
ANISOU  904  N   PHE A 121     2335   3977   5410    939    630   1736       N  
ATOM    905  CA  PHE A 121      14.029  37.043  -1.418  1.00 28.27           C  
ANISOU  905  CA  PHE A 121     2122   3952   4666    963    493   1571       C  
ATOM    906  C   PHE A 121      13.329  36.520  -0.181  1.00 34.38           C  
ANISOU  906  C   PHE A 121     2929   4672   5463    896    438   1231       C  
ATOM    907  O   PHE A 121      13.346  37.165   0.871  1.00 34.99           O  
ANISOU  907  O   PHE A 121     2960   4508   5827    800    507   1056       O  
ATOM    908  CB  PHE A 121      15.269  36.204  -1.738  1.00 28.73           C  
ANISOU  908  CB  PHE A 121     2225   4217   4473    948    479   1567       C  
ATOM    909  CG  PHE A 121      15.990  36.682  -2.949  1.00 33.13           C  
ANISOU  909  CG  PHE A 121     2722   4883   4982   1004    550   1900       C  
ATOM    910  CD1 PHE A 121      15.484  36.415  -4.208  1.00 39.09           C  
ANISOU  910  CD1 PHE A 121     3494   5902   5456   1090    511   2080       C  
ATOM    911  CD2 PHE A 121      17.139  37.447  -2.837  1.00 37.06           C  
ANISOU  911  CD2 PHE A 121     3115   5241   5723    952    672   2031       C  
ATOM    912  CE1 PHE A 121      16.130  36.885  -5.350  1.00 41.33           C  
ANISOU  912  CE1 PHE A 121     3690   6342   5673   1131    596   2404       C  
ATOM    913  CE2 PHE A 121      17.796  37.913  -3.972  1.00 40.20           C  
ANISOU  913  CE2 PHE A 121     3427   5764   6082   1001    751   2384       C  
ATOM    914  CZ  PHE A 121      17.286  37.635  -5.225  1.00 44.19           C  
ANISOU  914  CZ  PHE A 121     3952   6561   6277   1093    713   2580       C  
ATOM    915  N   ASP A 122      12.702  35.356  -0.330  1.00 33.43           N  
ANISOU  915  N   ASP A 122     2892   4784   5025    922    319   1119       N  
ATOM    916  CA  ASP A 122      12.025  34.683   0.767  1.00 30.04           C  
ANISOU  916  CA  ASP A 122     2530   4346   4537    822    258    810       C  
ATOM    917  C   ASP A 122      12.826  33.486   1.219  1.00 29.05           C  
ANISOU  917  C   ASP A 122     2540   4328   4170    732    197    635       C  
ATOM    918  O   ASP A 122      12.582  32.937   2.286  1.00 25.08           O  
ANISOU  918  O   ASP A 122     2101   3805   3624    616    158    402       O  
ATOM    919  CB  ASP A 122      10.634  34.217   0.337  1.00 28.37           C  
ANISOU  919  CB  ASP A 122     2308   4295   4176    894    170    807       C  
ATOM    920  CG  ASP A 122       9.735  35.377  -0.083  1.00 31.92           C  
ANISOU  920  CG  ASP A 122     2644   4634   4850    983    212    970       C  
ATOM    921  OD1 ASP A 122       9.694  36.397   0.632  1.00 34.81           O  
ANISOU  921  OD1 ASP A 122     2934   4739   5552    956    305    923       O  
ATOM    922  OD2 ASP A 122       9.094  35.279  -1.147  1.00 28.66           O  
ANISOU  922  OD2 ASP A 122     2233   4388   4270   1064    153   1124       O  
ATOM    923  N   PHE A 123      13.765  33.064   0.379  1.00 21.73           N  
ANISOU  923  N   PHE A 123     1643   3533   3081    793    189    763       N  
ATOM    924  CA  PHE A 123      14.519  31.870   0.657  1.00 21.70           C  
ANISOU  924  CA  PHE A 123     1754   3627   2865    750    128    622       C  
ATOM    925  C   PHE A 123      15.785  31.792  -0.187  1.00 22.29           C  
ANISOU  925  C   PHE A 123     1808   3808   2853    822    165    765       C  
ATOM    926  O   PHE A 123      15.784  32.118  -1.377  1.00 25.94           O  
ANISOU  926  O   PHE A 123     2205   4399   3251    929    195    975       O  
ATOM    927  CB  PHE A 123      13.677  30.622   0.421  1.00 20.11           C  
ANISOU  927  CB  PHE A 123     1652   3570   2418    767     18    506       C  
ATOM    928  CG  PHE A 123      14.421  29.354   0.704  1.00 23.01           C  
ANISOU  928  CG  PHE A 123     2140   3984   2620    739    -41    372       C  
ATOM    929  CD1 PHE A 123      14.864  29.077   1.978  1.00 25.03           C  
ANISOU  929  CD1 PHE A 123     2445   4131   2932    627    -54    242       C  
ATOM    930  CD2 PHE A 123      14.694  28.450  -0.312  1.00 29.24           C  
ANISOU  930  CD2 PHE A 123     2974   4935   3202    834    -81    378       C  
ATOM    931  CE1 PHE A 123      15.566  27.909   2.255  1.00 26.48           C  
ANISOU  931  CE1 PHE A 123     2728   4342   2993    625   -114    163       C  
ATOM    932  CE2 PHE A 123      15.389  27.280  -0.046  1.00 28.93           C  
ANISOU  932  CE2 PHE A 123     3037   4892   3063    832   -128    251       C  
ATOM    933  CZ  PHE A 123      15.823  27.012   1.236  1.00 27.49           C  
ANISOU  933  CZ  PHE A 123     2908   4574   2964    736   -147    168       C  
ATOM    934  N   VAL A 124      16.865  31.360   0.435  1.00 22.81           N  
ANISOU  934  N   VAL A 124     1911   3855   2901    765    165    662       N  
ATOM    935  CA  VAL A 124      18.084  31.077  -0.314  1.00 27.22           C  
ANISOU  935  CA  VAL A 124     2445   4550   3349    838    194    755       C  
ATOM    936  C   VAL A 124      18.825  29.924   0.330  1.00 29.53           C  
ANISOU  936  C   VAL A 124     2823   4873   3524    820    127    581       C  
ATOM    937  O   VAL A 124      18.888  29.841   1.567  1.00 28.10           O  
ANISOU  937  O   VAL A 124     2670   4584   3422    712     97    450       O  
ATOM    938  CB  VAL A 124      19.008  32.296  -0.383  1.00 28.85           C  
ANISOU  938  CB  VAL A 124     2518   4677   3764    801    314    912       C  
ATOM    939  CG1 VAL A 124      19.382  32.754   1.018  1.00 31.32           C  
ANISOU  939  CG1 VAL A 124     2809   4810   4283    648    334    753       C  
ATOM    940  CG2 VAL A 124      20.268  31.967  -1.212  1.00 26.40           C  
ANISOU  940  CG2 VAL A 124     2161   4557   3314    874    353   1011       C  
ATOM    941  N   ALA A 125      19.385  29.032  -0.492  1.00 26.13           N  
ANISOU  941  N   ALA A 125     2420   4604   2905    932    106    579       N  
ATOM    942  CA  ALA A 125      20.269  27.996   0.051  1.00 26.93           C  
ANISOU  942  CA  ALA A 125     2577   4712   2943    950     54    451       C  
ATOM    943  C   ALA A 125      21.684  28.342  -0.364  1.00 28.26           C  
ANISOU  943  C   ALA A 125     2626   4986   3124   1001    131    542       C  
ATOM    944  O   ALA A 125      21.915  28.746  -1.499  1.00 28.56           O  
ANISOU  944  O   ALA A 125     2585   5169   3098   1073    205    674       O  
ATOM    945  CB  ALA A 125      19.878  26.614  -0.452  1.00 25.58           C  
ANISOU  945  CB  ALA A 125     2520   4603   2597   1041    -23    327       C  
HETATM  946  N   MSE A 126      22.636  28.211   0.549  1.00 29.75           N  
ANISOU  946  N   MSE A 126     2782   5140   3381    958    117    486       N  
HETATM  947  CA  MSE A 126      23.999  28.571   0.218  1.00 31.40           C  
ANISOU  947  CA  MSE A 126     2851   5467   3612    990    193    563       C  
HETATM  948  C   MSE A 126      24.978  27.844   1.116  1.00 28.35           C  
ANISOU  948  C   MSE A 126     2455   5096   3222    999    128    463       C  
HETATM  949  O   MSE A 126      24.568  27.125   2.026  1.00 27.27           O  
ANISOU  949  O   MSE A 126     2415   4875   3072    978     27    368       O  
HETATM  950  CB  MSE A 126      24.183  30.093   0.290  1.00 31.95           C  
ANISOU  950  CB  MSE A 126     2792   5475   3872    864    301    692       C  
HETATM  951  CG  MSE A 126      24.056  30.704   1.671  1.00 32.58           C  
ANISOU  951  CG  MSE A 126     2852   5394   4132    693    284    594       C  
HETATM  952 SE   MSE A 126      24.224  32.679   1.616  0.67 46.99          SE  
ANISOU  952 SE   MSE A 126     4508   7066   6280    532    447    725      SE  
HETATM  953  CE  MSE A 126      22.835  33.079   0.337  1.00 64.71           C  
ANISOU  953  CE  MSE A 126     6813   9260   8516    639    485    932       C  
ATOM    954  N   VAL A 127      26.271  27.978   0.824  1.00 23.00           N  
ANISOU  954  N   VAL A 127     1682   4515   2543   1015    181    496       N  
ATOM    955  CA  VAL A 127      27.282  27.399   1.696  1.00 23.02           C  
ANISOU  955  CA  VAL A 127     1644   4550   2552   1025    118    427       C  
ATOM    956  C   VAL A 127      27.700  28.471   2.686  1.00 28.77           C  
ANISOU  956  C   VAL A 127     2231   5277   3423    852    142    433       C  
ATOM    957  O   VAL A 127      27.491  29.658   2.436  1.00 27.94           O  
ANISOU  957  O   VAL A 127     2050   5127   3439    742    239    497       O  
ATOM    958  CB  VAL A 127      28.514  26.822   0.943  1.00 32.59           C  
ANISOU  958  CB  VAL A 127     2811   5886   3685   1143    149    423       C  
ATOM    959  CG1 VAL A 127      28.086  25.663   0.037  1.00 34.84           C  
ANISOU  959  CG1 VAL A 127     3218   6179   3842   1308    127    353       C  
ATOM    960  CG2 VAL A 127      29.247  27.909   0.157  1.00 35.53           C  
ANISOU  960  CG2 VAL A 127     3047   6365   4089   1080    273    531       C  
ATOM    961  N   PRO A 128      28.252  28.054   3.832  1.00 24.33           N  
ANISOU  961  N   PRO A 128     1676   4080   3488    277    438     51       N  
ATOM    962  CA  PRO A 128      28.579  28.981   4.920  1.00 24.90           C  
ANISOU  962  CA  PRO A 128     1650   4078   3731    224    326     29       C  
ATOM    963  C   PRO A 128      29.504  30.108   4.477  1.00 29.20           C  
ANISOU  963  C   PRO A 128     2057   4575   4461    166    416     60       C  
ATOM    964  O   PRO A 128      29.317  31.250   4.903  1.00 27.87           O  
ANISOU  964  O   PRO A 128     1852   4372   4366    108    380     79       O  
ATOM    965  CB  PRO A 128      29.304  28.081   5.935  1.00 30.90           C  
ANISOU  965  CB  PRO A 128     2357   4823   4562    257    189    -33       C  
ATOM    966  CG  PRO A 128      28.657  26.735   5.732  1.00 30.89           C  
ANISOU  966  CG  PRO A 128     2488   4889   4360    323    209    -64       C  
ATOM    967  CD  PRO A 128      28.425  26.646   4.230  1.00 27.94           C  
ANISOU  967  CD  PRO A 128     2165   4557   3893    334    390    -17       C  
HETATM  968  N   MSE A 129      30.491  29.796   3.636  1.00 24.58           N  
ANISOU  968  N   MSE A 129     1409   4003   3926    181    549     80       N  
HETATM  969  CA  MSE A 129      31.389  30.821   3.149  1.00 29.73           C  
ANISOU  969  CA  MSE A 129     1956   4609   4730    121    662    157       C  
HETATM  970  C   MSE A 129      30.656  31.911   2.367  1.00 30.10           C  
ANISOU  970  C   MSE A 129     2086   4622   4728     94    793    282       C  
HETATM  971  O   MSE A 129      31.069  33.075   2.362  1.00 31.18           O  
ANISOU  971  O   MSE A 129     2151   4661   5033     23    846    346       O  
HETATM  972  CB  MSE A 129      32.473  30.209   2.267  1.00 30.22           C  
ANISOU  972  CB  MSE A 129     1958   4679   4844    157    830    180       C  
HETATM  973  CG  MSE A 129      33.701  31.043   2.228  1.00 36.30           C  
ANISOU  973  CG  MSE A 129     2562   5363   5869     88    893    231       C  
HETATM  974 SE   MSE A 129      35.189  30.063   1.491  0.48 36.48          SE  
ANISOU  974 SE   MSE A 129     2458   5382   6020    155   1072    238      SE  
HETATM  975  CE  MSE A 129      35.845  29.155   3.087  1.00 45.89           C  
ANISOU  975  CE  MSE A 129     3489   6598   7348    199    755    133       C  
ATOM    976  N   GLN A 130      29.583  31.539   1.686  1.00 23.63           N  
ANISOU  976  N   GLN A 130     1416   3877   3685    157    840    338       N  
ATOM    977  CA  GLN A 130      28.811  32.550   0.964  1.00 28.69           C  
ANISOU  977  CA  GLN A 130     2130   4517   4254    165    934    498       C  
ATOM    978  C   GLN A 130      28.132  33.528   1.912  1.00 29.22           C  
ANISOU  978  C   GLN A 130     2162   4512   4427    128    812    493       C  
ATOM    979  O   GLN A 130      28.058  34.728   1.631  1.00 28.33           O  
ANISOU  979  O   GLN A 130     2033   4306   4424    103    905    616       O  
ATOM    980  CB  GLN A 130      27.793  31.919   0.017  1.00 26.63           C  
ANISOU  980  CB  GLN A 130     2018   4408   3692    253    968    574       C  
ATOM    981  CG  GLN A 130      28.433  31.371  -1.264  1.00 30.27           C  
ANISOU  981  CG  GLN A 130     2571   4914   4015    291   1179    628       C  
ATOM    982  CD  GLN A 130      27.438  30.602  -2.104  1.00 33.58           C  
ANISOU  982  CD  GLN A 130     3180   5500   4081    363   1156    649       C  
ATOM    983  OE1 GLN A 130      26.704  29.758  -1.592  1.00 27.73           O  
ANISOU  983  OE1 GLN A 130     2465   4819   3249    369    971    524       O  
ATOM    984  NE2 GLN A 130      27.398  30.894  -3.397  1.00 32.13           N  
ANISOU  984  NE2 GLN A 130     3178   5346   3683    397   1306    782       N  
ATOM    985  N   LEU A 131      27.632  33.026   3.041  1.00 23.54           N  
ANISOU  985  N   LEU A 131     1447   3814   3682    129    632    360       N  
ATOM    986  CA  LEU A 131      26.983  33.922   3.988  1.00 26.63           C  
ANISOU  986  CA  LEU A 131     1819   4127   4172    102    553    342       C  
ATOM    987  C   LEU A 131      28.028  34.795   4.670  1.00 26.40           C  
ANISOU  987  C   LEU A 131     1668   3952   4412     -1    541    294       C  
ATOM    988  O   LEU A 131      27.807  35.973   4.933  1.00 30.39           O  
ANISOU  988  O   LEU A 131     2179   4316   5051    -49    569    318       O  
ATOM    989  CB  LEU A 131      26.195  33.139   5.038  1.00 29.03           C  
ANISOU  989  CB  LEU A 131     2193   4480   4357    127    401    213       C  
ATOM    990  CG  LEU A 131      25.498  33.970   6.112  1.00 31.47           C  
ANISOU  990  CG  LEU A 131     2565   4670   4721    102    341    145       C  
ATOM    991  CD1 LEU A 131      24.542  34.961   5.457  1.00 30.50           C  
ANISOU  991  CD1 LEU A 131     2474   4495   4620    145    435    273       C  
ATOM    992  CD2 LEU A 131      24.757  33.040   7.080  1.00 28.62           C  
ANISOU  992  CD2 LEU A 131     2306   4357   4212    130    245     27       C  
ATOM    993  N   GLN A 132      29.180  34.220   4.967  1.00 26.06           N  
ANISOU  993  N   GLN A 132     1542   3922   4438    -39    478    210       N  
ATOM    994  CA AGLN A 132      30.238  34.983   5.618  0.59 28.54           C  
ANISOU  994  CA AGLN A 132     1724   4106   5015   -151    416    154       C  
ATOM    995  CA BGLN A 132      30.213  35.000   5.627  0.41 28.47           C  
ANISOU  995  CA BGLN A 132     1717   4095   5005   -152    416    154       C  
ATOM    996  C   GLN A 132      30.719  36.101   4.698  1.00 30.14           C  
ANISOU  996  C   GLN A 132     1880   4189   5384   -211    614    281       C  
ATOM    997  O   GLN A 132      31.068  37.184   5.161  1.00 30.24           O  
ANISOU  997  O   GLN A 132     1819   4037   5635   -320    603    256       O  
ATOM    998  CB AGLN A 132      31.404  34.073   6.012  0.59 29.90           C  
ANISOU  998  CB AGLN A 132     1800   4332   5228   -153    296     78       C  
ATOM    999  CB BGLN A 132      31.362  34.115   6.105  0.41 30.53           C  
ANISOU  999  CB BGLN A 132     1881   4406   5312   -158    283     71       C  
ATOM   1000  CG AGLN A 132      32.304  34.647   7.121  0.59 34.31           C  
ANISOU 1000  CG AGLN A 132     2234   4776   6026   -269    102    -28       C  
ATOM   1001  CG BGLN A 132      32.112  34.695   7.308  0.41 34.51           C  
ANISOU 1001  CG BGLN A 132     2278   4795   6039   -273     74    -46       C  
ATOM   1002  CD AGLN A 132      33.435  35.507   6.592  0.59 39.33           C  
ANISOU 1002  CD AGLN A 132     2721   5297   6923   -366    212     24       C  
ATOM   1003  CD BGLN A 132      33.242  33.804   7.771  0.41 38.28           C  
ANISOU 1003  CD BGLN A 132     2655   5327   6563   -255    -83    -95       C  
ATOM   1004  OE1AGLN A 132      33.712  35.525   5.394  0.59 36.30           O  
ANISOU 1004  OE1AGLN A 132     2327   4928   6539   -333    445    144       O  
ATOM   1005  OE1BGLN A 132      33.972  33.248   6.954  0.41 40.62           O  
ANISOU 1005  OE1BGLN A 132     2877   5678   6881   -203     47    -23       O  
ATOM   1006  NE2AGLN A 132      34.113  36.215   7.495  0.59 46.34           N  
ANISOU 1006  NE2AGLN A 132     3506   6063   8040   -493     39    -78       N  
ATOM   1007  NE2BGLN A 132      33.397  33.661   9.088  0.41 42.86           N  
ANISOU 1007  NE2BGLN A 132     3243   5884   7158   -291   -367   -222       N  
ATOM   1008  N   SER A 133      30.744  35.824   3.389  1.00 33.84           N  
ANISOU 1008  N   SER A 133     2404   4721   5731   -145    804    409       N  
ATOM   1009  CA  SER A 133      31.210  36.801   2.396  1.00 36.88           C  
ANISOU 1009  CA  SER A 133     2776   4991   6247   -186   1030    562       C  
ATOM   1010  C   SER A 133      30.259  37.983   2.334  1.00 37.14           C  
ANISOU 1010  C   SER A 133     2879   4907   6325   -190   1097    674       C  
ATOM   1011  O   SER A 133      30.683  39.130   2.291  1.00 40.29           O  
ANISOU 1011  O   SER A 133     3231   5120   6958   -276   1200    733       O  
ATOM   1012  CB  SER A 133      31.300  36.181   0.996  1.00 44.04           C  
ANISOU 1012  CB  SER A 133     3776   5996   6963   -101   1227    681       C  
ATOM   1013  OG  SER A 133      32.473  35.407   0.839  1.00 51.61           O  
ANISOU 1013  OG  SER A 133     4639   6988   7981   -108   1261    612       O  
ATOM   1014  N   ILE A 134      28.968  37.685   2.295  1.00 34.80           N  
ANISOU 1014  N   ILE A 134     2690   4709   5822    -88   1047    713       N  
ATOM   1015  CA  ILE A 134      27.948  38.720   2.322  1.00 32.36           C  
ANISOU 1015  CA  ILE A 134     2462   4293   5542    -55   1077    813       C  
ATOM   1016  C   ILE A 134      28.107  39.602   3.560  1.00 31.22           C  
ANISOU 1016  C   ILE A 134     2272   3950   5639   -163    989    669       C  
ATOM   1017  O   ILE A 134      28.022  40.820   3.473  1.00 34.76           O  
ANISOU 1017  O   ILE A 134     2750   4197   6259   -200   1093    748       O  
ATOM   1018  CB  ILE A 134      26.542  38.112   2.328  1.00 32.03           C  
ANISOU 1018  CB  ILE A 134     2552   4391   5225     72    946    807       C  
ATOM   1019  CG1 ILE A 134      26.219  37.511   0.959  1.00 32.29           C  
ANISOU 1019  CG1 ILE A 134     2682   4586   5002    170   1015    963       C  
ATOM   1020  CG2 ILE A 134      25.512  39.163   2.741  1.00 34.79           C  
ANISOU 1020  CG2 ILE A 134     2974   4596   5650    113    924    842       C  
ATOM   1021  CD1 ILE A 134      24.951  36.674   0.951  1.00 34.77           C  
ANISOU 1021  CD1 ILE A 134     3078   5060   5074    264    848    924       C  
ATOM   1022  N   LEU A 135      28.346  38.974   4.705  1.00 29.85           N  
ANISOU 1022  N   LEU A 135     2057   3822   5464   -211    795    457       N  
ATOM   1023  CA  LEU A 135      28.494  39.692   5.972  1.00 34.59           C  
ANISOU 1023  CA  LEU A 135     2670   4248   6226   -318    674    281       C  
ATOM   1024  C   LEU A 135      29.774  40.526   6.082  1.00 40.85           C  
ANISOU 1024  C   LEU A 135     3303   4861   7359   -491    709    249       C  
ATOM   1025  O   LEU A 135      29.816  41.504   6.831  1.00 45.64           O  
ANISOU 1025  O   LEU A 135     3952   5258   8130   -595    664    139       O  
ATOM   1026  CB  LEU A 135      28.424  38.707   7.141  1.00 34.77           C  
ANISOU 1026  CB  LEU A 135     2736   4380   6096   -313    443     80       C  
ATOM   1027  CG  LEU A 135      27.051  38.071   7.336  1.00 33.91           C  
ANISOU 1027  CG  LEU A 135     2789   4384   5712   -179    420     74       C  
ATOM   1028  CD1 LEU A 135      27.152  36.825   8.212  1.00 29.66           C  
ANISOU 1028  CD1 LEU A 135     2290   3977   5003   -164    241    -69       C  
ATOM   1029  CD2 LEU A 135      26.094  39.105   7.934  1.00 35.59           C  
ANISOU 1029  CD2 LEU A 135     3143   4420   5958   -166    467     32       C  
ATOM   1030  N   GLU A 136      30.815  40.141   5.346  1.00 39.77           N  
ANISOU 1030  N   GLU A 136     3000   4788   7322   -522    794    330       N  
ATOM   1031  CA  GLU A 136      32.103  40.832   5.436  1.00 49.45           C  
ANISOU 1031  CA  GLU A 136     4098   5858   8831   -670    801    289       C  
ATOM   1032  C   GLU A 136      32.214  42.004   4.472  1.00 49.41           C  
ANISOU 1032  C   GLU A 136     4121   5667   8985   -702   1074    472       C  
ATOM   1033  O   GLU A 136      32.944  42.978   4.719  1.00 49.87           O  
ANISOU 1033  O   GLU A 136     4104   5516   9330   -845   1098    427       O  
ATOM   1034  CB  GLU A 136      33.248  39.854   5.180  1.00 57.66           C  
ANISOU 1034  CB  GLU A 136     5023   7044   9841   -650    748    269       C  
ATOM   1035  CG  GLU A 136      33.536  38.954   6.359  1.00 68.90           C  
ANISOU 1035  CG  GLU A 136     6393   8576  11211   -657    443     82       C  
ATOM   1036  CD  GLU A 136      34.269  39.678   7.475  1.00 77.90           C  
ANISOU 1036  CD  GLU A 136     7431   9558  12608   -826    227    -87       C  
ATOM   1037  OE1 GLU A 136      35.379  40.201   7.210  1.00 79.84           O  
ANISOU 1037  OE1 GLU A 136     7530   9706  13100   -919    277    -66       O  
ATOM   1038  OE2 GLU A 136      33.730  39.724   8.608  1.00 79.28           O  
ANISOU 1038  OE2 GLU A 136     7688   9703  12731   -870      3   -252       O  
ATOM   1039  N   ASN A 137      31.496  41.890   3.363  1.00 44.86           N  
ANISOU 1039  N   ASN A 137     3669   5167   8209   -565   1265    680       N  
ATOM   1040  CA  ASN A 137      31.561  42.872   2.296  1.00 47.34           C  
ANISOU 1040  CA  ASN A 137     4053   5325   8607   -558   1534    900       C  
ATOM   1041  C   ASN A 137      30.561  43.997   2.575  1.00 50.74           C  
ANISOU 1041  C   ASN A 137     4586   5548   9144   -558   1595    970       C  
ATOM   1042  O   ASN A 137      29.346  43.826   2.412  1.00 41.63           O  
ANISOU 1042  O   ASN A 137     3559   4475   7782   -415   1583   1062       O  
ATOM   1043  CB  ASN A 137      31.277  42.182   0.963  1.00 46.26           C  
ANISOU 1043  CB  ASN A 137     4035   5369   8173   -408   1687   1094       C  
ATOM   1044  CG  ASN A 137      31.487  43.095  -0.222  1.00 50.29           C  
ANISOU 1044  CG  ASN A 137     4648   5732   8727   -390   1970   1335       C  
ATOM   1045  OD1 ASN A 137      31.390  44.318  -0.100  1.00 53.94           O  
ANISOU 1045  OD1 ASN A 137     5137   5955   9404   -447   2059   1404       O  
ATOM   1046  ND2 ASN A 137      31.777  42.505  -1.382  1.00 46.84           N  
ANISOU 1046  ND2 ASN A 137     4297   5422   8077   -309   2122   1458       N  
ATOM   1047  N   SER A 138      31.080  45.143   3.011  1.00 58.23           N  
ANISOU 1047  N   SER A 138     5499   6221  10404   -703   1637    910       N  
ATOM   1048  CA  SER A 138      30.234  46.228   3.509  1.00 64.17           C  
ANISOU 1048  CA  SER A 138     6361   6717  11304   -722   1681    916       C  
ATOM   1049  C   SER A 138      29.353  46.872   2.447  1.00 61.51           C  
ANISOU 1049  C   SER A 138     6194   6293  10882   -564   1907   1229       C  
ATOM   1050  O   SER A 138      28.632  47.829   2.725  1.00 63.69           O  
ANISOU 1050  O   SER A 138     6605   6347  11248   -520   1943   1254       O  
ATOM   1051  CB  SER A 138      31.072  47.290   4.225  1.00 76.05           C  
ANISOU 1051  CB  SER A 138     7814   7936  13146   -923   1656    744       C  
ATOM   1052  OG  SER A 138      31.254  46.939   5.589  1.00 80.36           O  
ANISOU 1052  OG  SER A 138     8298   8494  13742  -1048   1382    435       O  
ATOM   1053  N   ALA A 139      29.416  46.345   1.232  1.00 58.89           N  
ANISOU 1053  N   ALA A 139     5909   6148  10319   -445   2015   1440       N  
ATOM   1054  CA  ALA A 139      28.508  46.760   0.176  1.00 54.86           C  
ANISOU 1054  CA  ALA A 139     5585   5614   9644   -267   2165   1757       C  
ATOM   1055  C   ALA A 139      27.276  45.863   0.193  1.00 49.25           C  
ANISOU 1055  C   ALA A 139     4963   5172   8577    -73   1948   1742       C  
ATOM   1056  O   ALA A 139      26.234  46.219  -0.352  1.00 47.45           O  
ANISOU 1056  O   ALA A 139     4883   4937   8211    102   1942   1936       O  
ATOM   1057  CB  ALA A 139      29.193  46.685  -1.163  1.00 56.66           C  
ANISOU 1057  CB  ALA A 139     5889   5911   9730   -226   2345   1944       C  
ATOM   1058  N   THR A 140      27.406  44.700   0.831  1.00 44.41           N  
ANISOU 1058  N   THR A 140     4250   4789   7837   -104   1755   1510       N  
ATOM   1059  CA  THR A 140      26.322  43.725   0.877  1.00 40.01           C  
ANISOU 1059  CA  THR A 140     3753   4485   6963     50   1555   1468       C  
ATOM   1060  C   THR A 140      25.890  43.396   2.301  1.00 40.02           C  
ANISOU 1060  C   THR A 140     3711   4500   6997     21   1354   1188       C  
ATOM   1061  O   THR A 140      24.793  42.886   2.513  1.00 38.47           O  
ANISOU 1061  O   THR A 140     3562   4432   6622    143   1224   1156       O  
ATOM   1062  CB  THR A 140      26.691  42.409   0.142  1.00 40.95           C  
ANISOU 1062  CB  THR A 140     3857   4888   6813     78   1536   1484       C  
ATOM   1063  OG1 THR A 140      27.823  41.787   0.774  1.00 38.57           O  
ANISOU 1063  OG1 THR A 140     3390   4627   6639    -64   1513   1282       O  
ATOM   1064  CG2 THR A 140      27.010  42.680  -1.330  1.00 45.05           C  
ANISOU 1064  CG2 THR A 140     4492   5406   7219    128   1760   1767       C  
ATOM   1065  N   SER A 141      26.736  43.686   3.283  1.00 40.42           N  
ANISOU 1065  N   SER A 141     3676   4411   7271   -147   1327    984       N  
ATOM   1066  CA  SER A 141      26.410  43.302   4.654  1.00 38.02           C  
ANISOU 1066  CA  SER A 141     3386   4128   6933   -177   1137    714       C  
ATOM   1067  C   SER A 141      25.081  43.900   5.110  1.00 37.46           C  
ANISOU 1067  C   SER A 141     3445   3940   6848    -56   1143    710       C  
ATOM   1068  O   SER A 141      24.315  43.253   5.829  1.00 36.75           O  
ANISOU 1068  O   SER A 141     3399   3960   6605      9   1030    578       O  
ATOM   1069  CB  SER A 141      27.520  43.699   5.626  1.00 40.53           C  
ANISOU 1069  CB  SER A 141     3627   4284   7487   -382   1072    499       C  
ATOM   1070  OG  SER A 141      27.765  45.092   5.570  1.00 45.70           O  
ANISOU 1070  OG  SER A 141     4306   4630   8428   -470   1221    547       O  
ATOM   1071  N   GLY A 142      24.808  45.128   4.689  1.00 38.82           N  
ANISOU 1071  N   GLY A 142     3674   3875   7202    -19   1301    865       N  
ATOM   1072  CA  GLY A 142      23.604  45.819   5.124  1.00 41.60           C  
ANISOU 1072  CA  GLY A 142     4125   4068   7612    110   1342    869       C  
ATOM   1073  C   GLY A 142      22.333  45.224   4.545  1.00 44.95           C  
ANISOU 1073  C   GLY A 142     4543   4695   7842    322   1285   1023       C  
ATOM   1074  O   GLY A 142      21.228  45.539   4.995  1.00 44.61           O  
ANISOU 1074  O   GLY A 142     4530   4570   7851    448   1302   1007       O  
ATOM   1075  N   GLN A 143      22.490  44.362   3.542  1.00 44.84           N  
ANISOU 1075  N   GLN A 143     4483   4935   7619    357   1221   1162       N  
ATOM   1076  CA  GLN A 143      21.347  43.748   2.873  1.00 41.98           C  
ANISOU 1076  CA  GLN A 143     4107   4777   7066    531   1119   1303       C  
ATOM   1077  C   GLN A 143      21.219  42.260   3.171  1.00 38.73           C  
ANISOU 1077  C   GLN A 143     3645   4646   6425    506    963   1142       C  
ATOM   1078  O   GLN A 143      20.427  41.578   2.530  1.00 34.40           O  
ANISOU 1078  O   GLN A 143     3074   4289   5707    609    855   1235       O  
ATOM   1079  CB  GLN A 143      21.442  43.932   1.351  1.00 45.89           C  
ANISOU 1079  CB  GLN A 143     4653   5336   7449    611   1154   1606       C  
ATOM   1080  CG  GLN A 143      21.240  45.354   0.865  1.00 54.74           C  
ANISOU 1080  CG  GLN A 143     5847   6188   8765    697   1297   1843       C  
ATOM   1081  CD  GLN A 143      22.403  46.258   1.211  1.00 62.00           C  
ANISOU 1081  CD  GLN A 143     6790   6836   9932    531   1492   1793       C  
ATOM   1082  OE1 GLN A 143      23.490  46.139   0.635  1.00 63.60           O  
ANISOU 1082  OE1 GLN A 143     6997   7063  10105    416   1590   1849       O  
ATOM   1083  NE2 GLN A 143      22.185  47.169   2.155  1.00 63.26           N  
ANISOU 1083  NE2 GLN A 143     6963   6719  10356    510   1565   1675       N  
ATOM   1084  N   VAL A 144      21.988  41.747   4.131  1.00 37.27           N  
ANISOU 1084  N   VAL A 144     3447   4475   6238    367    933    906       N  
ATOM   1085  CA  VAL A 144      21.944  40.311   4.424  1.00 33.83           C  
ANISOU 1085  CA  VAL A 144     2983   4277   5595    347    801    770       C  
ATOM   1086  C   VAL A 144      20.522  39.808   4.742  1.00 33.39           C  
ANISOU 1086  C   VAL A 144     2913   4307   5467    459    733    743       C  
ATOM   1087  O   VAL A 144      20.172  38.664   4.430  1.00 30.58           O  
ANISOU 1087  O   VAL A 144     2526   4159   4933    480    632    730       O  
ATOM   1088  CB  VAL A 144      22.914  39.924   5.556  1.00 33.77           C  
ANISOU 1088  CB  VAL A 144     2979   4242   5608    205    752    532       C  
ATOM   1089  CG1 VAL A 144      22.486  40.557   6.870  1.00 35.55           C  
ANISOU 1089  CG1 VAL A 144     3287   4280   5940    185    771    365       C  
ATOM   1090  CG2 VAL A 144      23.004  38.409   5.687  1.00 34.08           C  
ANISOU 1090  CG2 VAL A 144     2999   4511   5437    199    633    438       C  
ATOM   1091  N   ASP A 145      19.699  40.659   5.345  1.00 30.26           N  
ANISOU 1091  N   ASP A 145     2528   3733   5237    528    810    732       N  
ATOM   1092  CA  ASP A 145      18.342  40.244   5.689  1.00 34.58           C  
ANISOU 1092  CA  ASP A 145     3018   4337   5785    632    788    711       C  
ATOM   1093  C   ASP A 145      17.409  40.117   4.462  1.00 37.38           C  
ANISOU 1093  C   ASP A 145     3266   4823   6114    766    692    937       C  
ATOM   1094  O   ASP A 145      16.391  39.430   4.522  1.00 32.49           O  
ANISOU 1094  O   ASP A 145     2547   4319   5478    823    619    921       O  
ATOM   1095  CB  ASP A 145      17.761  41.121   6.804  1.00 35.94           C  
ANISOU 1095  CB  ASP A 145     3237   4266   6152    672    940    606       C  
ATOM   1096  CG  ASP A 145      18.372  40.796   8.168  1.00 42.78           C  
ANISOU 1096  CG  ASP A 145     4240   5074   6939    543    968    338       C  
ATOM   1097  OD1 ASP A 145      19.036  39.744   8.293  1.00 46.57           O  
ANISOU 1097  OD1 ASP A 145     4739   5725   7232    450    852    251       O  
ATOM   1098  OD2 ASP A 145      18.190  41.571   9.121  1.00 45.67           O  
ANISOU 1098  OD2 ASP A 145     4716   5219   7416    543   1101    214       O  
ATOM   1099  N   ARG A 146      17.787  40.733   3.344  1.00 34.91           N  
ANISOU 1099  N   ARG A 146     2982   4493   5789    806    681   1146       N  
ATOM   1100  CA AARG A 146      17.031  40.589   2.105  0.52 34.60           C  
ANISOU 1100  CA AARG A 146     2893   4594   5658    928    539   1367       C  
ATOM   1101  CA BARG A 146      17.027  40.587   2.103  0.48 34.66           C  
ANISOU 1101  CA BARG A 146     2900   4603   5666    928    539   1367       C  
ATOM   1102  C   ARG A 146      17.032  39.140   1.604  1.00 32.77           C  
ANISOU 1102  C   ARG A 146     2653   4640   5159    871    375   1303       C  
ATOM   1103  O   ARG A 146      16.318  38.793   0.660  1.00 35.44           O  
ANISOU 1103  O   ARG A 146     2959   5125   5384    947    204   1433       O  
ATOM   1104  CB AARG A 146      17.573  41.530   1.031  0.52 37.22           C  
ANISOU 1104  CB AARG A 146     3327   4838   5977    975    589   1613       C  
ATOM   1105  CB BARG A 146      17.560  41.510   1.005  0.48 37.27           C  
ANISOU 1105  CB BARG A 146     3333   4851   5978    977    584   1616       C  
ATOM   1106  CG AARG A 146      16.895  42.904   0.973  0.52 41.82           C  
ANISOU 1106  CG AARG A 146     3890   5183   6817   1127    664   1800       C  
ATOM   1107  CG BARG A 146      17.485  43.009   1.297  0.48 40.80           C  
ANISOU 1107  CG BARG A 146     3802   4991   6707   1048    747   1722       C  
ATOM   1108  CD AARG A 146      17.109  43.723   2.236  0.52 43.77           C  
ANISOU 1108  CD AARG A 146     4145   5152   7332   1079    865   1637       C  
ATOM   1109  CD BARG A 146      16.098  43.474   1.734  0.48 43.57           C  
ANISOU 1109  CD BARG A 146     4026   5242   7287   1213    729   1761       C  
ATOM   1110  NE AARG A 146      17.047  45.161   1.966  0.52 46.27           N  
ANISOU 1110  NE AARG A 146     4518   5186   7878   1179   1002   1830       N  
ATOM   1111  NE BARG A 146      16.129  43.844   3.143  0.48 45.01           N  
ANISOU 1111  NE BARG A 146     4208   5222   7671   1157    905   1530       N  
ATOM   1112  CZ AARG A 146      17.821  46.063   2.562  0.52 43.92           C  
ANISOU 1112  CZ AARG A 146     4312   4615   7759   1083   1195   1746       C  
ATOM   1113  CZ BARG A 146      15.435  43.237   4.097  0.48 44.31           C  
ANISOU 1113  CZ BARG A 146     4034   5179   7623   1155    913   1339       C  
ATOM   1114  NH1AARG A 146      17.711  47.347   2.258  0.52 50.28           N  
ANISOU 1114  NH1AARG A 146     5178   5140   8786   1178   1329   1934       N  
ATOM   1115  NH1BARG A 146      14.468  42.385   3.784  0.48 45.60           N  
ANISOU 1115  NH1BARG A 146     4089   5572   7664   1177    743   1338       N  
ATOM   1116  NH2AARG A 146      18.708  45.679   3.465  0.52 44.93           N  
ANISOU 1116  NH2AARG A 146     4475   4740   7855    890   1235   1474       N  
ATOM   1117  NH2BARG A 146      15.699  43.500   5.366  0.48 45.11           N  
ANISOU 1117  NH2BARG A 146     4206   5080   7853   1102   1091   1131       N  
ATOM   1118  N   LEU A 147      17.848  38.293   2.224  1.00 27.59           N  
ANISOU 1118  N   LEU A 147     2037   4044   4403    737    410   1101       N  
ATOM   1119  CA  LEU A 147      17.825  36.860   1.912  1.00 27.70           C  
ANISOU 1119  CA  LEU A 147     2052   4279   4196    683    284   1010       C  
ATOM   1120  C   LEU A 147      16.535  36.184   2.404  1.00 31.67           C  
ANISOU 1120  C   LEU A 147     2429   4848   4757    711    191    927       C  
ATOM   1121  O   LEU A 147      16.172  35.110   1.909  1.00 27.78           O  
ANISOU 1121  O   LEU A 147     1917   4525   4115    683     53    892       O  
ATOM   1122  CB  LEU A 147      19.041  36.148   2.496  1.00 27.41           C  
ANISOU 1122  CB  LEU A 147     2077   4262   4077    558    349    834       C  
ATOM   1123  CG  LEU A 147      20.414  36.571   1.954  1.00 28.33           C  
ANISOU 1123  CG  LEU A 147     2265   4334   4165    507    450    899       C  
ATOM   1124  CD1 LEU A 147      21.537  35.910   2.754  1.00 29.15           C  
ANISOU 1124  CD1 LEU A 147     2366   4439   4270    397    485    715       C  
ATOM   1125  CD2 LEU A 147      20.549  36.240   0.475  1.00 29.70           C  
ANISOU 1125  CD2 LEU A 147     2518   4645   4120    544    418   1049       C  
ATOM   1126  N   GLY A 148      15.844  36.812   3.363  1.00 27.88           N  
ANISOU 1126  N   GLY A 148     1894   4206   4494    748    285    876       N  
ATOM   1127  CA  GLY A 148      14.604  36.257   3.912  1.00 29.28           C  
ANISOU 1127  CA  GLY A 148     2011   4380   4733    737    249    759       C  
ATOM   1128  C   GLY A 148      14.822  35.144   4.934  1.00 31.39           C  
ANISOU 1128  C   GLY A 148     2341   4673   4912    624    303    539       C  
ATOM   1129  O   GLY A 148      14.607  35.314   6.146  1.00 26.86           O  
ANISOU 1129  O   GLY A 148     1798   3981   4425    613    450    426       O  
ATOM   1130  N   LYS A 149      15.233  33.980   4.450  1.00 26.59           N  
ANISOU 1130  N   LYS A 149     1766   4215   4122    551    198    494       N  
ATOM   1131  CA  LYS A 149      15.539  32.867   5.346  1.00 25.24           C  
ANISOU 1131  CA  LYS A 149     1666   4056   3869    458    248    320       C  
ATOM   1132  C   LYS A 149      16.583  31.983   4.675  1.00 25.29           C  
ANISOU 1132  C   LYS A 149     1749   4190   3669    403    169    310       C  
ATOM   1133  O   LYS A 149      16.495  31.726   3.473  1.00 23.38           O  
ANISOU 1133  O   LYS A 149     1478   4080   3325    420     51    399       O  
ATOM   1134  CB  LYS A 149      14.251  32.134   5.769  1.00 32.20           C  
ANISOU 1134  CB  LYS A 149     2465   4930   4838    434    252    241       C  
ATOM   1135  CG  LYS A 149      14.089  30.704   5.370  1.00 35.66           C  
ANISOU 1135  CG  LYS A 149     2896   5470   5183    355    154    187       C  
ATOM   1136  CD  LYS A 149      12.963  29.984   6.178  1.00 22.18           C  
ANISOU 1136  CD  LYS A 149     1102   3714   3613    309    238     86       C  
ATOM   1137  CE  LYS A 149      11.810  30.880   6.559  1.00 26.12           C  
ANISOU 1137  CE  LYS A 149     1482   4162   4281    378    313    112       C  
ATOM   1138  NZ  LYS A 149      10.637  30.046   7.018  1.00 31.32           N  
ANISOU 1138  NZ  LYS A 149     2029   4843   5030    326    373     63       N  
ATOM   1139  N   VAL A 150      17.603  31.585   5.429  1.00 24.44           N  
ANISOU 1139  N   VAL A 150     1736   4057   3493    353    231    211       N  
ATOM   1140  CA  VAL A 150      18.783  30.961   4.833  1.00 24.18           C  
ANISOU 1140  CA  VAL A 150     1767   4114   3308    321    193    204       C  
ATOM   1141  C   VAL A 150      18.952  29.505   5.257  1.00 29.74           C  
ANISOU 1141  C   VAL A 150     2539   4854   3907    268    175     85       C  
ATOM   1142  O   VAL A 150      18.921  29.179   6.460  1.00 26.57           O  
ANISOU 1142  O   VAL A 150     2177   4390   3529    250    226     -2       O  
ATOM   1143  CB  VAL A 150      20.058  31.722   5.239  1.00 26.43           C  
ANISOU 1143  CB  VAL A 150     2071   4331   3641    312    257    203       C  
ATOM   1144  CG1 VAL A 150      21.292  31.034   4.669  1.00 23.71           C  
ANISOU 1144  CG1 VAL A 150     1762   4054   3194    284    247    190       C  
ATOM   1145  CG2 VAL A 150      19.990  33.168   4.781  1.00 23.91           C  
ANISOU 1145  CG2 VAL A 150     1692   3949   3444    360    306    339       C  
ATOM   1146  N   LEU A 151      19.102  28.626   4.275  1.00 26.21           N  
ANISOU 1146  N   LEU A 151     2097   4533   3328    258    117     86       N  
ATOM   1147  CA  LEU A 151      19.496  27.253   4.552  1.00 21.73           C  
ANISOU 1147  CA  LEU A 151     1590   3999   2670    223    121    -21       C  
ATOM   1148  C   LEU A 151      20.960  27.056   4.153  1.00 26.04           C  
ANISOU 1148  C   LEU A 151     2175   4571   3147    243    157    -22       C  
ATOM   1149  O   LEU A 151      21.331  27.251   2.985  1.00 23.58           O  
ANISOU 1149  O   LEU A 151     1874   4328   2758    262    169     41       O  
ATOM   1150  CB  LEU A 151      18.597  26.277   3.800  1.00 22.72           C  
ANISOU 1150  CB  LEU A 151     1696   4219   2719    185     47    -59       C  
ATOM   1151  CG  LEU A 151      18.993  24.814   3.980  1.00 26.41           C  
ANISOU 1151  CG  LEU A 151     2263   4670   3102    145     70   -173       C  
ATOM   1152  CD1 LEU A 151      18.805  24.386   5.412  1.00 20.73           C  
ANISOU 1152  CD1 LEU A 151     1570   3846   2461    128    141   -229       C  
ATOM   1153  CD2 LEU A 151      18.201  23.926   3.053  1.00 32.16           C  
ANISOU 1153  CD2 LEU A 151     3008   5462   3752     83    -19   -229       C  
ATOM   1154  N   LEU A 152      21.796  26.703   5.131  1.00 22.08           N  
ANISOU 1154  N   LEU A 152     1717   3989   2683    242    178    -82       N  
ATOM   1155  CA  LEU A 152      23.202  26.459   4.870  1.00 22.40           C  
ANISOU 1155  CA  LEU A 152     1755   4026   2730    266    208    -83       C  
ATOM   1156  C   LEU A 152      23.487  24.980   4.649  1.00 27.08           C  
ANISOU 1156  C   LEU A 152     2396   4657   3236    287    228   -155       C  
ATOM   1157  O   LEU A 152      22.958  24.141   5.365  1.00 22.07           O  
ANISOU 1157  O   LEU A 152     1827   3983   2575    273    201   -218       O  
ATOM   1158  CB  LEU A 152      24.055  26.981   6.041  1.00 22.97           C  
ANISOU 1158  CB  LEU A 152     1798   4011   2920    265    174   -102       C  
ATOM   1159  CG  LEU A 152      24.012  28.497   6.289  1.00 23.33           C  
ANISOU 1159  CG  LEU A 152     1790   3998   3076    239    177    -56       C  
ATOM   1160  CD1 LEU A 152      24.842  28.888   7.506  1.00 21.53           C  
ANISOU 1160  CD1 LEU A 152     1531   3710   2940    222    104   -119       C  
ATOM   1161  CD2 LEU A 152      24.503  29.250   5.044  1.00 24.24           C  
ANISOU 1161  CD2 LEU A 152     1852   4117   3240    238    252     44       C  
ATOM   1162  N   GLY A 153      24.319  24.673   3.648  1.00 29.17           N  
ANISOU 1162  N   GLY A 153     2661   4956   3465    320    305   -142       N  
ATOM   1163  CA  GLY A 153      24.848  23.330   3.444  1.00 31.83           C  
ANISOU 1163  CA  GLY A 153     3064   5272   3758    357    357   -213       C  
ATOM   1164  C   GLY A 153      26.292  23.235   3.945  1.00 31.56           C  
ANISOU 1164  C   GLY A 153     2932   5181   3879    424    389   -200       C  
ATOM   1165  O   GLY A 153      26.647  23.929   4.903  1.00 36.00           O  
ANISOU 1165  O   GLY A 153     3416   5701   4562    414    300   -174       O  
ATOM   1166  N   GLY A 154      27.112  22.372   3.340  1.00 30.79           N  
ANISOU 1166  N   GLY A 154     2843   5063   3792    490    504   -227       N  
ATOM   1167  CA  GLY A 154      28.537  22.274   3.690  1.00 33.63           C  
ANISOU 1167  CA  GLY A 154     3066   5352   4361    561    533   -199       C  
ATOM   1168  C   GLY A 154      28.832  21.912   5.155  1.00 33.17           C  
ANISOU 1168  C   GLY A 154     2957   5243   4404    604    362   -212       C  
ATOM   1169  O   GLY A 154      27.941  21.446   5.870  1.00 31.96           O  
ANISOU 1169  O   GLY A 154     2945   5065   4134    579    271   -247       O  
ATOM   1170  N   ALA A 155      30.075  22.120   5.603  1.00 36.15           N  
ANISOU 1170  N   ALA A 155     3169   5564   5001    649    306   -171       N  
ATOM   1171  CA  ALA A 155      30.495  21.699   6.947  1.00 37.15           C  
ANISOU 1171  CA  ALA A 155     3261   5652   5203    715    100   -174       C  
ATOM   1172  C   ALA A 155      29.816  22.562   8.016  1.00 40.30           C  
ANISOU 1172  C   ALA A 155     3745   6059   5510    624    -80   -185       C  
ATOM   1173  O   ALA A 155      29.446  23.704   7.734  1.00 38.39           O  
ANISOU 1173  O   ALA A 155     3468   5854   5263    532    -49   -181       O  
ATOM   1174  CB  ALA A 155      32.041  21.746   7.093  1.00 34.05           C  
ANISOU 1174  CB  ALA A 155     2645   5187   5105    772     51   -118       C  
ATOM   1175  N   PRO A 156      29.613  22.006   9.233  1.00 41.05           N  
ANISOU 1175  N   PRO A 156     3984   6100   5515    657   -242   -195       N  
ATOM   1176  CA  PRO A 156      29.044  22.824  10.313  1.00 40.52           C  
ANISOU 1176  CA  PRO A 156     4035   6021   5338    580   -383   -219       C  
ATOM   1177  C   PRO A 156      29.826  24.127  10.445  1.00 37.94           C  
ANISOU 1177  C   PRO A 156     3527   5707   5180    517   -493   -225       C  
ATOM   1178  O   PRO A 156      31.057  24.151  10.349  1.00 35.75           O  
ANISOU 1178  O   PRO A 156     3036   5426   5122    556   -577   -202       O  
ATOM   1179  CB  PRO A 156      29.213  21.945  11.555  1.00 42.17           C  
ANISOU 1179  CB  PRO A 156     4413   6161   5450    658   -551   -206       C  
ATOM   1180  CG  PRO A 156      29.167  20.545  11.022  1.00 42.69           C  
ANISOU 1180  CG  PRO A 156     4523   6187   5508    750   -423   -180       C  
ATOM   1181  CD  PRO A 156      29.859  20.617   9.670  1.00 45.31           C  
ANISOU 1181  CD  PRO A 156     4620   6566   6028    773   -278   -178       C  
ATOM   1182  N   VAL A 157      29.076  25.204  10.610  1.00 34.63           N  
ANISOU 1182  N   VAL A 157     3176   5288   4693    419   -469   -257       N  
ATOM   1183  CA  VAL A 157      29.590  26.563  10.660  1.00 35.28           C  
ANISOU 1183  CA  VAL A 157     3122   5351   4931    331   -531   -274       C  
ATOM   1184  C   VAL A 157      30.657  26.755  11.742  1.00 32.73           C  
ANISOU 1184  C   VAL A 157     2743   4982   4709    323   -814   -316       C  
ATOM   1185  O   VAL A 157      30.544  26.200  12.840  1.00 31.29           O  
ANISOU 1185  O   VAL A 157     2755   4774   4359    364   -987   -344       O  
ATOM   1186  CB  VAL A 157      28.396  27.497  10.896  1.00 38.19           C  
ANISOU 1186  CB  VAL A 157     3646   5692   5175    255   -457   -309       C  
ATOM   1187  CG1 VAL A 157      28.834  28.875  11.355  1.00 45.91           C  
ANISOU 1187  CG1 VAL A 157     4567   6597   6278    158   -554   -358       C  
ATOM   1188  CG2 VAL A 157      27.538  27.559   9.631  1.00 34.43           C  
ANISOU 1188  CG2 VAL A 157     3140   5270   4671    256   -232   -250       C  
ATOM   1189  N   ASN A 158      31.703  27.517  11.441  1.00 28.40           N  
ANISOU 1189  N   ASN A 158     1954   4413   4425    261   -861   -305       N  
ATOM   1190  CA  ASN A 158      32.719  27.779  12.465  1.00 33.44           C  
ANISOU 1190  CA  ASN A 158     2557   4997   5150    218  -1143   -336       C  
ATOM   1191  C   ASN A 158      32.247  28.791  13.522  1.00 34.51           C  
ANISOU 1191  C   ASN A 158     2853   5078   5183    117  -1342   -476       C  
ATOM   1192  O   ASN A 158      31.215  29.452  13.351  1.00 32.05           O  
ANISOU 1192  O   ASN A 158     2687   4739   4751     66  -1164   -504       O  
ATOM   1193  CB  ASN A 158      34.085  28.170  11.867  1.00 40.80           C  
ANISOU 1193  CB  ASN A 158     3228   5912   6361    168  -1086   -267       C  
ATOM   1194  CG  ASN A 158      34.041  29.477  11.071  1.00 45.64           C  
ANISOU 1194  CG  ASN A 158     3742   6487   7113     48   -899   -266       C  
ATOM   1195  OD1 ASN A 158      33.452  30.468  11.500  1.00 45.44           O  
ANISOU 1195  OD1 ASN A 158     3796   6404   7067    -48   -959   -350       O  
ATOM   1196  ND2 ASN A 158      34.672  29.473   9.898  1.00 48.17           N  
ANISOU 1196  ND2 ASN A 158     3906   6826   7569     62   -663   -177       N  
ATOM   1197  N   HIS A 159      33.007  28.895  14.608  1.00 30.93           N  
ANISOU 1197  N   HIS A 159     2460   4579   4711     80  -1633   -522       N  
ATOM   1198  CA  HIS A 159      32.588  29.680  15.769  1.00 40.88           C  
ANISOU 1198  CA  HIS A 159     3975   5769   5788     -8  -1843   -673       C  
ATOM   1199  C   HIS A 159      32.294  31.149  15.453  1.00 38.51           C  
ANISOU 1199  C   HIS A 159     3626   5384   5623   -158  -1728   -761       C  
ATOM   1200  O   HIS A 159      31.252  31.673  15.856  1.00 33.88           O  
ANISOU 1200  O   HIS A 159     3322   4733   4816   -188  -1602   -827       O  
ATOM   1201  CB  HIS A 159      33.613  29.571  16.896  1.00 48.04           C  
ANISOU 1201  CB  HIS A 159     4952   6649   6655    -33  -2163   -692       C  
ATOM   1202  CG  HIS A 159      33.116  30.089  18.213  1.00 56.94           C  
ANISOU 1202  CG  HIS A 159     6460   7704   7471    -97  -2357   -838       C  
ATOM   1203  ND1 HIS A 159      33.724  31.134  18.879  1.00 63.22           N  
ANISOU 1203  ND1 HIS A 159     7279   8419   8321   -244  -2548   -957       N  
ATOM   1204  CD2 HIS A 159      32.071  29.708  18.982  1.00 58.75           C  
ANISOU 1204  CD2 HIS A 159     7095   7916   7310    -36  -2346   -886       C  
ATOM   1205  CE1 HIS A 159      33.077  31.367  20.007  1.00 65.28           C  
ANISOU 1205  CE1 HIS A 159     7960   8619   8223   -268  -2643  -1076       C  
ATOM   1206  NE2 HIS A 159      32.071  30.517  20.096  1.00 63.67           N  
ANISOU 1206  NE2 HIS A 159     8003   8449   7741   -141  -2501  -1026       N  
ATOM   1207  N   ALA A 160      33.197  31.810  14.735  1.00 38.72           N  
ANISOU 1207  N   ALA A 160     3350   5379   5983   -244  -1668   -717       N  
ATOM   1208  CA  ALA A 160      32.979  33.209  14.349  1.00 37.46           C  
ANISOU 1208  CA  ALA A 160     3117   5108   6007   -386  -1549   -785       C  
ATOM   1209  C   ALA A 160      31.731  33.431  13.480  1.00 35.47           C  
ANISOU 1209  C   ALA A 160     2965   4863   5650   -335  -1178   -703       C  
ATOM   1210  O   ALA A 160      31.001  34.407  13.666  1.00 34.44           O  
ANISOU 1210  O   ALA A 160     2999   4623   5465   -398  -1070   -762       O  
ATOM   1211  CB  ALA A 160      34.233  33.789  13.670  1.00 42.03           C  
ANISOU 1211  CB  ALA A 160     3404   5643   6922   -472  -1474   -703       C  
ATOM   1212  N   LEU A 161      31.463  32.534  12.536  1.00 30.55           N  
ANISOU 1212  N   LEU A 161     2259   4356   4993   -216   -984   -567       N  
ATOM   1213  CA  LEU A 161      30.278  32.698  11.717  1.00 30.45           C  
ANISOU 1213  CA  LEU A 161     2343   4362   4864   -168   -688   -485       C  
ATOM   1214  C   LEU A 161      29.032  32.354  12.553  1.00 28.33           C  
ANISOU 1214  C   LEU A 161     2393   4092   4279   -113   -680   -544       C  
ATOM   1215  O   LEU A 161      27.992  32.994  12.430  1.00 29.92           O  
ANISOU 1215  O   LEU A 161     2710   4239   4419   -116   -511   -540       O  
ATOM   1216  CB  LEU A 161      30.365  31.860  10.424  1.00 27.09           C  
ANISOU 1216  CB  LEU A 161     1764   4055   4474    -75   -501   -346       C  
ATOM   1217  CG  LEU A 161      29.101  31.828   9.572  1.00 24.10           C  
ANISOU 1217  CG  LEU A 161     1497   3722   3937    -17   -266   -263       C  
ATOM   1218  CD1 LEU A 161      28.742  33.216   9.073  1.00 22.53           C  
ANISOU 1218  CD1 LEU A 161     1281   3428   3852    -82   -127   -217       C  
ATOM   1219  CD2 LEU A 161      29.191  30.838   8.378  1.00 25.99           C  
ANISOU 1219  CD2 LEU A 161     1654   4080   4143     70   -120   -162       C  
ATOM   1220  N   ALA A 162      29.149  31.365  13.428  1.00 29.11           N  
ANISOU 1220  N   ALA A 162     2629   4234   4198    -58   -850   -587       N  
ATOM   1221  CA  ALA A 162      28.032  31.030  14.308  1.00 27.49           C  
ANISOU 1221  CA  ALA A 162     2742   4004   3699    -15   -807   -638       C  
ATOM   1222  C   ALA A 162      27.638  32.233  15.193  1.00 29.11           C  
ANISOU 1222  C   ALA A 162     3150   4067   3843   -101   -819   -768       C  
ATOM   1223  O   ALA A 162      26.452  32.536  15.364  1.00 24.65           O  
ANISOU 1223  O   ALA A 162     2755   3448   3164    -79   -615   -784       O  
ATOM   1224  CB  ALA A 162      28.369  29.816  15.163  1.00 25.73           C  
ANISOU 1224  CB  ALA A 162     2664   3824   3288     57   -995   -645       C  
HETATM 1225  N   MSE A 163      28.628  32.931  15.730  1.00 28.70           N  
ANISOU 1225  N   MSE A 163     3069   3940   3896   -201  -1050   -871       N  
HETATM 1226  CA  MSE A 163      28.362  34.130  16.535  1.00 34.59           C  
ANISOU 1226  CA  MSE A 163     4025   4522   4596   -300  -1066  -1025       C  
HETATM 1227  C   MSE A 163      27.668  35.245  15.746  1.00 31.69           C  
ANISOU 1227  C   MSE A 163     3575   4056   4408   -328   -782   -990       C  
HETATM 1228  O   MSE A 163      26.780  35.921  16.274  1.00 37.43           O  
ANISOU 1228  O   MSE A 163     4532   4656   5034   -330   -635  -1073       O  
HETATM 1229  CB  MSE A 163      29.649  34.665  17.176  1.00 39.91           C  
ANISOU 1229  CB  MSE A 163     4651   5128   5386   -431  -1412  -1157       C  
HETATM 1230  CG  MSE A 163      30.216  33.778  18.278  1.00 48.76           C  
ANISOU 1230  CG  MSE A 163     5950   6308   6268   -399  -1754  -1216       C  
HETATM 1231 SE   MSE A 163      29.162  33.825  19.910  0.53 98.06          SE  
ANISOU 1231 SE   MSE A 163    12827  12445  11985   -377  -1744  -1378      SE  
HETATM 1232  CE  MSE A 163      29.329  31.963  20.459  1.00 78.06           C  
ANISOU 1232  CE  MSE A 163    10440  10069   9151   -210  -1924  -1247       C  
ATOM   1233  N   GLN A 164      28.080  35.446  14.497  1.00 28.80           N  
ANISOU 1233  N   GLN A 164     2900   3735   4308   -337   -690   -860       N  
ATOM   1234  CA  GLN A 164      27.430  36.405  13.592  1.00 29.89           C  
ANISOU 1234  CA  GLN A 164     2958   3791   4607   -334   -428   -773       C  
ATOM   1235  C   GLN A 164      25.980  36.043  13.256  1.00 27.97           C  
ANISOU 1235  C   GLN A 164     2810   3602   4216   -205   -197   -683       C  
ATOM   1236  O   GLN A 164      25.103  36.913  13.200  1.00 28.52           O  
ANISOU 1236  O   GLN A 164     2951   3551   4333   -184    -19   -678       O  
ATOM   1237  CB  GLN A 164      28.207  36.518  12.276  1.00 33.29           C  
ANISOU 1237  CB  GLN A 164     3076   4276   5298   -356   -365   -624       C  
ATOM   1238  CG  GLN A 164      29.415  37.446  12.333  1.00 44.02           C  
ANISOU 1238  CG  GLN A 164     4277   5503   6946   -512   -475   -686       C  
ATOM   1239  CD  GLN A 164      30.175  37.488  11.014  1.00 48.02           C  
ANISOU 1239  CD  GLN A 164     4482   6054   7708   -527   -346   -520       C  
ATOM   1240  OE1 GLN A 164      30.763  36.493  10.591  1.00 47.15           O  
ANISOU 1240  OE1 GLN A 164     4215   6092   7606   -474   -384   -453       O  
ATOM   1241  NE2 GLN A 164      30.163  38.641  10.362  1.00 50.12           N  
ANISOU 1241  NE2 GLN A 164     4687   6173   8183   -591   -163   -447       N  
ATOM   1242  N   ILE A 165      25.742  34.761  13.006  1.00 23.52           N  
ANISOU 1242  N   ILE A 165     2222   3204   3510   -121   -204   -612       N  
ATOM   1243  CA  ILE A 165      24.408  34.281  12.683  1.00 23.78           C  
ANISOU 1243  CA  ILE A 165     2305   3297   3435    -22    -21   -537       C  
ATOM   1244  C   ILE A 165      23.467  34.458  13.870  1.00 27.66           C  
ANISOU 1244  C   ILE A 165     3057   3681   3772     -3     63   -649       C  
ATOM   1245  O   ILE A 165      22.306  34.819  13.684  1.00 26.24           O  
ANISOU 1245  O   ILE A 165     2886   3454   3630     55    263   -608       O  
ATOM   1246  CB  ILE A 165      24.433  32.824  12.223  1.00 24.04           C  
ANISOU 1246  CB  ILE A 165     2274   3500   3359     39    -55   -464       C  
ATOM   1247  CG1 ILE A 165      25.048  32.738  10.822  1.00 28.37           C  
ANISOU 1247  CG1 ILE A 165     2589   4142   4049     45    -35   -340       C  
ATOM   1248  CG2 ILE A 165      23.021  32.242  12.221  1.00 23.48           C  
ANISOU 1248  CG2 ILE A 165     2280   3465   3176    109     98   -431       C  
ATOM   1249  CD1 ILE A 165      25.445  31.342  10.404  1.00 24.11           C  
ANISOU 1249  CD1 ILE A 165     1994   3738   3429     93    -84   -302       C  
ATOM   1250  N   SER A 166      23.979  34.238  15.084  1.00 27.07           N  
ANISOU 1250  N   SER A 166     3197   3560   3530    -46    -87   -785       N  
ATOM   1251  CA  SER A 166      23.190  34.397  16.304  1.00 33.02           C  
ANISOU 1251  CA  SER A 166     4266   4196   4085    -32     17   -905       C  
ATOM   1252  C   SER A 166      22.609  35.790  16.435  1.00 34.24           C  
ANISOU 1252  C   SER A 166     4482   4162   4364    -48    197   -971       C  
ATOM   1253  O   SER A 166      21.589  35.982  17.088  1.00 31.75           O  
ANISOU 1253  O   SER A 166     4361   3744   3956      2    413  -1028       O  
ATOM   1254  CB  SER A 166      24.034  34.126  17.554  1.00 39.70           C  
ANISOU 1254  CB  SER A 166     5372   5009   4702    -87   -228  -1045       C  
ATOM   1255  OG  SER A 166      24.327  32.749  17.669  1.00 50.38           O  
ANISOU 1255  OG  SER A 166     6739   6499   5904    -35   -350   -976       O  
ATOM   1256  N   ASP A 167      23.274  36.770  15.840  1.00 32.15           N  
ANISOU 1256  N   ASP A 167     4059   3829   4328   -115    136   -963       N  
ATOM   1257  CA  ASP A 167      22.807  38.142  15.953  1.00 35.39           C  
ANISOU 1257  CA  ASP A 167     4539   4024   4885   -128    307  -1024       C  
ATOM   1258  C   ASP A 167      21.941  38.650  14.799  1.00 32.90           C  
ANISOU 1258  C   ASP A 167     4005   3696   4802    -33    528   -845       C  
ATOM   1259  O   ASP A 167      21.539  39.819  14.798  1.00 30.74           O  
ANISOU 1259  O   ASP A 167     3767   3223   4691    -20    683   -865       O  
ATOM   1260  CB  ASP A 167      23.974  39.092  16.205  1.00 43.21           C  
ANISOU 1260  CB  ASP A 167     5547   4874   5997   -276    126  -1149       C  
ATOM   1261  CG  ASP A 167      23.908  39.701  17.579  1.00 62.81           C  
ANISOU 1261  CG  ASP A 167     8394   7158   8313   -340    111  -1392       C  
ATOM   1262  OD1 ASP A 167      23.304  40.790  17.723  1.00 66.71           O  
ANISOU 1262  OD1 ASP A 167     8997   7433   8918   -331    327  -1457       O  
ATOM   1263  OD2 ASP A 167      24.428  39.068  18.525  1.00 72.61           O  
ANISOU 1263  OD2 ASP A 167     9840   8455   9295   -388   -110  -1515       O  
ATOM   1264  N   LEU A 168      21.651  37.780  13.832  1.00 29.52           N  
ANISOU 1264  N   LEU A 168     3368   3464   4382     37    528   -673       N  
ATOM   1265  CA  LEU A 168      20.814  38.151  12.695  1.00 29.10           C  
ANISOU 1265  CA  LEU A 168     3119   3429   4508    134    675   -490       C  
ATOM   1266  C   LEU A 168      19.336  37.971  13.023  1.00 28.26           C  
ANISOU 1266  C   LEU A 168     3048   3297   4391    247    874   -476       C  
ATOM   1267  O   LEU A 168      18.931  36.921  13.487  1.00 29.84           O  
ANISOU 1267  O   LEU A 168     3308   3598   4431    261    884   -512       O  
ATOM   1268  CB  LEU A 168      21.166  37.315  11.461  1.00 30.66           C  
ANISOU 1268  CB  LEU A 168     3106   3845   4699    149    570   -329       C  
ATOM   1269  CG  LEU A 168      22.572  37.456  10.881  1.00 31.53           C  
ANISOU 1269  CG  LEU A 168     3113   3988   4878     59    437   -297       C  
ATOM   1270  CD1 LEU A 168      22.770  36.481   9.703  1.00 28.93           C  
ANISOU 1270  CD1 LEU A 168     2627   3870   4495     96    392   -155       C  
ATOM   1271  CD2 LEU A 168      22.806  38.888  10.444  1.00 36.19           C  
ANISOU 1271  CD2 LEU A 168     3660   4395   5694     30    524   -239       C  
ATOM   1272  N   ALA A 169      18.542  39.005  12.766  1.00 29.99           N  
ANISOU 1272  N   ALA A 169     3213   3365   4815    330   1047   -413       N  
ATOM   1273  CA  ALA A 169      17.094  38.929  12.887  1.00 32.89           C  
ANISOU 1273  CA  ALA A 169     3522   3703   5270    455   1250   -366       C  
ATOM   1274  C   ALA A 169      16.481  38.254  11.664  1.00 34.38           C  
ANISOU 1274  C   ALA A 169     3439   4095   5527    526   1175   -168       C  
ATOM   1275  O   ALA A 169      15.640  38.844  10.967  1.00 38.66           O  
ANISOU 1275  O   ALA A 169     3809   4598   6282    639   1242    -22       O  
ATOM   1276  CB  ALA A 169      16.510  40.339  13.076  1.00 35.76           C  
ANISOU 1276  CB  ALA A 169     3916   3803   5868    540   1461   -368       C  
HETATM 1277  N   MSE A 170      16.908  37.019  11.415  1.00 29.30           N  
ANISOU 1277  N   MSE A 170     2771   3657   4703    463   1021   -167       N  
HETATM 1278  CA  MSE A 170      16.509  36.262  10.231  1.00 27.49           C  
ANISOU 1278  CA  MSE A 170     2334   3627   4484    496    909    -18       C  
HETATM 1279  C   MSE A 170      16.740  34.778  10.474  1.00 24.68           C  
ANISOU 1279  C   MSE A 170     2025   3426   3926    427    825    -88       C  
HETATM 1280  O   MSE A 170      17.819  34.397  10.915  1.00 28.37           O  
ANISOU 1280  O   MSE A 170     2629   3911   4238    351    737   -176       O  
HETATM 1281  CB  MSE A 170      17.355  36.691   9.027  1.00 24.19           C  
ANISOU 1281  CB  MSE A 170     1840   3270   4080    484    772    112       C  
HETATM 1282  CG  MSE A 170      17.239  35.733   7.867  1.00 25.57           C  
ANISOU 1282  CG  MSE A 170     1891   3662   4161    490    630    221       C  
HETATM 1283 SE   MSE A 170      18.110  36.344   6.237  0.56 33.14          SE  
ANISOU 1283 SE   MSE A 170     2801   4683   5107    503    532    418      SE  
HETATM 1284  CE  MSE A 170      19.946  36.311   6.897  1.00 27.32           C  
ANISOU 1284  CE  MSE A 170     2184   3891   4305    365    527    276       C  
ATOM   1285  N   PRO A 171      15.748  33.930  10.153  1.00 27.13           N  
ANISOU 1285  N   PRO A 171     2207   3837   4265    452    837    -43       N  
ATOM   1286  CA  PRO A 171      15.888  32.488  10.385  1.00 27.35           C  
ANISOU 1286  CA  PRO A 171     2291   3975   4126    384    785   -106       C  
ATOM   1287  C   PRO A 171      17.010  31.875   9.558  1.00 27.57           C  
ANISOU 1287  C   PRO A 171     2323   4141   4011    336    595    -81       C  
ATOM   1288  O   PRO A 171      16.975  31.988   8.337  1.00 26.49           O  
ANISOU 1288  O   PRO A 171     2057   4100   3908    358    498     26       O  
ATOM   1289  CB  PRO A 171      14.534  31.909   9.928  1.00 28.60           C  
ANISOU 1289  CB  PRO A 171     2291   4197   4379    395    788    -53       C  
ATOM   1290  CG  PRO A 171      13.626  33.049   9.790  1.00 29.77           C  
ANISOU 1290  CG  PRO A 171     2358   4249   4705    468    838     12       C  
ATOM   1291  CD  PRO A 171      14.443  34.276   9.561  1.00 26.70           C  
ANISOU 1291  CD  PRO A 171     1999   3781   4366    516    836     57       C  
ATOM   1292  N   VAL A 172      17.976  31.231  10.220  1.00 21.79           N  
ANISOU 1292  N   VAL A 172     1747   3413   3121    285    548   -171       N  
ATOM   1293  CA  VAL A 172      19.060  30.533   9.544  1.00 22.44           C  
ANISOU 1293  CA  VAL A 172     1819   3605   3101    255    407   -157       C  
ATOM   1294  C   VAL A 172      19.141  29.085  10.053  1.00 26.64           C  
ANISOU 1294  C   VAL A 172     2451   4176   3497    228    390   -221       C  
ATOM   1295  O   VAL A 172      19.099  28.836  11.273  1.00 22.70           O  
ANISOU 1295  O   VAL A 172     2114   3592   2919    220    445   -295       O  
ATOM   1296  CB  VAL A 172      20.411  31.240   9.796  1.00 20.94           C  
ANISOU 1296  CB  VAL A 172     1680   3362   2914    230    338   -185       C  
ATOM   1297  CG1 VAL A 172      21.519  30.525   9.085  1.00 22.07           C  
ANISOU 1297  CG1 VAL A 172     1773   3608   3005    215    236   -161       C  
ATOM   1298  CG2 VAL A 172      20.351  32.706   9.326  1.00 19.74           C  
ANISOU 1298  CG2 VAL A 172     1452   3131   2917    247    383   -115       C  
ATOM   1299  N   TYR A 173      19.240  28.141   9.118  1.00 22.00           N  
ANISOU 1299  N   TYR A 173     1798   3696   2866    219    327   -192       N  
ATOM   1300  CA  TYR A 173      19.254  26.720   9.431  1.00 24.48           C  
ANISOU 1300  CA  TYR A 173     2199   4022   3081    197    326   -242       C  
ATOM   1301  C   TYR A 173      20.456  26.104   8.766  1.00 22.28           C  
ANISOU 1301  C   TYR A 173     1920   3809   2738    209    232   -238       C  
ATOM   1302  O   TYR A 173      21.008  26.698   7.840  1.00 24.26           O  
ANISOU 1302  O   TYR A 173     2080   4116   3022    222    195   -189       O  
ATOM   1303  CB  TYR A 173      17.998  26.034   8.884  1.00 21.04           C  
ANISOU 1303  CB  TYR A 173     1676   3624   2694    162    366   -235       C  
ATOM   1304  CG  TYR A 173      16.724  26.597   9.435  1.00 24.20           C  
ANISOU 1304  CG  TYR A 173     2012   3957   3225    160    489   -227       C  
ATOM   1305  CD1 TYR A 173      16.160  26.087  10.604  1.00 24.48           C  
ANISOU 1305  CD1 TYR A 173     2157   3888   3254    138    643   -274       C  
ATOM   1306  CD2 TYR A 173      16.076  27.642   8.790  1.00 24.37           C  
ANISOU 1306  CD2 TYR A 173     1868   4004   3389    194    474   -157       C  
ATOM   1307  CE1 TYR A 173      14.981  26.610  11.112  1.00 30.09           C  
ANISOU 1307  CE1 TYR A 173     2794   4522   4117    145    812   -266       C  
ATOM   1308  CE2 TYR A 173      14.909  28.165   9.286  1.00 29.84           C  
ANISOU 1308  CE2 TYR A 173     2481   4606   4250    212    603   -138       C  
ATOM   1309  CZ  TYR A 173      14.361  27.649  10.439  1.00 32.27           C  
ANISOU 1309  CZ  TYR A 173     2865   4825   4572    187    791   -205       C  
ATOM   1310  OH  TYR A 173      13.194  28.187  10.920  1.00 35.56           O  
ANISOU 1310  OH  TYR A 173     3228   5149   5136    213    924   -172       O  
ATOM   1311  N   GLN A 174      20.870  24.930   9.240  1.00 18.38           N  
ANISOU 1311  N   GLN A 174     1532   3289   2164    214    220   -279       N  
ATOM   1312  CA  GLN A 174      21.915  24.167   8.567  1.00 16.55           C  
ANISOU 1312  CA  GLN A 174     1286   3099   1902    244    167   -279       C  
ATOM   1313  C   GLN A 174      21.440  22.735   8.341  1.00 23.58           C  
ANISOU 1313  C   GLN A 174     2247   3975   2739    227    209   -317       C  
ATOM   1314  O   GLN A 174      20.825  22.140   9.223  1.00 21.94           O  
ANISOU 1314  O   GLN A 174     2145   3687   2504    206    260   -338       O  
ATOM   1315  CB  GLN A 174      23.253  24.192   9.338  1.00 18.61           C  
ANISOU 1315  CB  GLN A 174     1584   3317   2169    293     81   -283       C  
ATOM   1316  CG  GLN A 174      24.399  23.524   8.538  1.00 21.78           C  
ANISOU 1316  CG  GLN A 174     1912   3755   2610    345     63   -270       C  
ATOM   1317  CD  GLN A 174      25.786  23.973   8.970  1.00 34.17           C  
ANISOU 1317  CD  GLN A 174     3397   5306   4282    385    -41   -255       C  
ATOM   1318  OE1 GLN A 174      26.004  24.313  10.125  1.00 33.56           O  
ANISOU 1318  OE1 GLN A 174     3386   5176   4191    382   -154   -272       O  
ATOM   1319  NE2 GLN A 174      26.724  23.999   8.024  1.00 38.47           N  
ANISOU 1319  NE2 GLN A 174     3795   5888   4933    415      0   -226       N  
ATOM   1320  N   SER A 175      21.710  22.204   7.151  1.00 21.65           N  
ANISOU 1320  N   SER A 175     1965   3787   2472    229    209   -329       N  
ATOM   1321  CA  SER A 175      21.275  20.859   6.762  1.00 23.61           C  
ANISOU 1321  CA  SER A 175     2290   4003   2678    196    246   -391       C  
ATOM   1322  C   SER A 175      22.184  19.769   7.312  1.00 22.76           C  
ANISOU 1322  C   SER A 175     2291   3799   2556    263    267   -407       C  
ATOM   1323  O   SER A 175      23.394  19.971   7.473  1.00 22.72           O  
ANISOU 1323  O   SER A 175     2256   3795   2582    349    232   -373       O  
ATOM   1324  CB  SER A 175      21.319  20.721   5.235  1.00 27.67           C  
ANISOU 1324  CB  SER A 175     2776   4603   3133    179    238   -418       C  
ATOM   1325  OG  SER A 175      20.421  21.624   4.625  1.00 36.93           O  
ANISOU 1325  OG  SER A 175     3860   5865   4307    131    183   -384       O  
ATOM   1326  N   TYR A 176      21.601  18.611   7.580  1.00 22.10           N  
ANISOU 1326  N   TYR A 176     2319   3620   2458    225    323   -450       N  
ATOM   1327  CA  TYR A 176      22.373  17.377   7.689  1.00 22.74           C  
ANISOU 1327  CA  TYR A 176     2511   3594   2535    296    360   -467       C  
ATOM   1328  C   TYR A 176      21.867  16.460   6.584  1.00 24.18           C  
ANISOU 1328  C   TYR A 176     2736   3753   2700    225    420   -567       C  
ATOM   1329  O   TYR A 176      20.665  16.243   6.469  1.00 22.39           O  
ANISOU 1329  O   TYR A 176     2512   3513   2483    101    433   -616       O  
ATOM   1330  CB  TYR A 176      22.160  16.710   9.050  1.00 21.44           C  
ANISOU 1330  CB  TYR A 176     2500   3288   2358    315    391   -425       C  
ATOM   1331  CG  TYR A 176      22.782  15.323   9.162  1.00 21.31           C  
ANISOU 1331  CG  TYR A 176     2618   3125   2355    395    438   -425       C  
ATOM   1332  CD1 TYR A 176      24.091  15.160   9.591  1.00 24.56           C  
ANISOU 1332  CD1 TYR A 176     3037   3503   2791    550    363   -357       C  
ATOM   1333  CD2 TYR A 176      22.039  14.176   8.867  1.00 20.16           C  
ANISOU 1333  CD2 TYR A 176     2577   2855   2228    315    551   -490       C  
ATOM   1334  CE1 TYR A 176      24.659  13.883   9.714  1.00 25.40           C  
ANISOU 1334  CE1 TYR A 176     3259   3453   2939    653    409   -337       C  
ATOM   1335  CE2 TYR A 176      22.591  12.908   8.985  1.00 24.90           C  
ANISOU 1335  CE2 TYR A 176     3319   3285   2858    397    615   -486       C  
ATOM   1336  CZ  TYR A 176      23.897  12.766   9.412  1.00 28.10           C  
ANISOU 1336  CZ  TYR A 176     3736   3656   3286    580    550   -400       C  
ATOM   1337  OH  TYR A 176      24.441  11.505   9.533  1.00 26.45           O  
ANISOU 1337  OH  TYR A 176     3658   3258   3134    688    618   -377       O  
ATOM   1338  N   GLY A 177      22.770  15.951   5.755  1.00 25.92           N  
ANISOU 1338  N   GLY A 177     2982   3963   2905    296    460   -606       N  
ATOM   1339  CA  GLY A 177      22.373  15.080   4.665  1.00 28.51           C  
ANISOU 1339  CA  GLY A 177     3400   4254   3178    226    517   -730       C  
ATOM   1340  C   GLY A 177      23.583  14.482   3.983  1.00 30.19           C  
ANISOU 1340  C   GLY A 177     3671   4415   3386    347    618   -767       C  
ATOM   1341  O   GLY A 177      24.717  14.641   4.447  1.00 28.34           O  
ANISOU 1341  O   GLY A 177     3369   4162   3238    489    638   -682       O  
HETATM 1342  N   MSE A 178      23.337  13.761   2.893  1.00 30.69           N  
ANISOU 1342  N   MSE A 178     3691   4693   3276   -488    307  -1118       N  
HETATM 1343  CA  MSE A 178      24.401  13.159   2.113  1.00 33.07           C  
ANISOU 1343  CA  MSE A 178     3939   5022   3604   -490    311  -1280       C  
HETATM 1344  C   MSE A 178      23.837  12.877   0.712  1.00 34.70           C  
ANISOU 1344  C   MSE A 178     4026   5443   3714   -595    338  -1399       C  
HETATM 1345  O   MSE A 178      22.622  12.919   0.513  1.00 33.40           O  
ANISOU 1345  O   MSE A 178     3817   5377   3496   -640    335  -1396       O  
HETATM 1346  CB  MSE A 178      24.831  11.864   2.782  1.00 35.63           C  
ANISOU 1346  CB  MSE A 178     4369   5110   4060   -429    306  -1379       C  
HETATM 1347  CG  MSE A 178      23.712  10.828   2.837  1.00 37.72           C  
ANISOU 1347  CG  MSE A 178     4690   5269   4374   -532    393  -1428       C  
HETATM 1348 SE   MSE A 178      23.582   9.872   4.548  0.56 38.76          SE  
ANISOU 1348 SE   MSE A 178     5165   4972   4592   -431    459  -1332      SE  
HETATM 1349  CE  MSE A 178      23.299  11.380   5.748  1.00 46.44           C  
ANISOU 1349  CE  MSE A 178     6190   5982   5473   -345    399  -1081       C  
ATOM   1350  N   THR A 179      24.701  12.579  -0.252  1.00 36.75           N  
ANISOU 1350  N   THR A 179     4215   5798   3950   -621    359  -1545       N  
ATOM   1351  CA  THR A 179      24.221  12.311  -1.604  1.00 39.93           C  
ANISOU 1351  CA  THR A 179     4515   6431   4223   -694    375  -1675       C  
ATOM   1352  C   THR A 179      23.248  11.127  -1.613  1.00 36.97           C  
ANISOU 1352  C   THR A 179     4074   6026   3947   -761    381  -1834       C  
ATOM   1353  O   THR A 179      22.259  11.146  -2.353  1.00 35.78           O  
ANISOU 1353  O   THR A 179     3815   6078   3699   -791    358  -1912       O  
ATOM   1354  CB  THR A 179      25.374  12.079  -2.621  1.00 50.11           C  
ANISOU 1354  CB  THR A 179     5741   7808   5490   -726    423  -1815       C  
ATOM   1355  OG1 THR A 179      25.814  10.720  -2.550  1.00 58.25           O  
ANISOU 1355  OG1 THR A 179     6712   8703   6719   -735    419  -1989       O  
ATOM   1356  CG2 THR A 179      26.541  12.992  -2.334  1.00 46.65           C  
ANISOU 1356  CG2 THR A 179     5350   7325   5052   -706    480  -1761       C  
ATOM   1357  N   GLU A 180      23.524  10.100  -0.798  1.00 33.73           N  
ANISOU 1357  N   GLU A 180     3738   5346   3733   -768    420  -1894       N  
ATOM   1358  CA  GLU A 180      22.636   8.928  -0.711  1.00 37.92           C  
ANISOU 1358  CA  GLU A 180     4249   5766   4392   -874    504  -2057       C  
ATOM   1359  C   GLU A 180      21.215   9.257  -0.232  1.00 34.22           C  
ANISOU 1359  C   GLU A 180     3757   5326   3918   -943    545  -2016       C  
ATOM   1360  O   GLU A 180      20.301   8.447  -0.360  1.00 35.96           O  
ANISOU 1360  O   GLU A 180     3896   5527   4243  -1077    649  -2220       O  
ATOM   1361  CB  GLU A 180      23.244   7.830   0.169  1.00 47.07           C  
ANISOU 1361  CB  GLU A 180     5599   6556   5730   -833    566  -2080       C  
ATOM   1362  CG  GLU A 180      24.144   6.850  -0.571  1.00 59.89           C  
ANISOU 1362  CG  GLU A 180     7167   8150   7437   -820    562  -2291       C  
ATOM   1363  CD  GLU A 180      24.268   5.510   0.150  1.00 72.68           C  
ANISOU 1363  CD  GLU A 180     9005   9376   9235   -794    656  -2369       C  
ATOM   1364  OE1 GLU A 180      23.671   4.513  -0.321  1.00 78.66           O  
ANISOU 1364  OE1 GLU A 180     9707  10072  10108   -919    774  -2502       O  
ATOM   1365  OE2 GLU A 180      24.962   5.451   1.187  1.00 76.26           O  
ANISOU 1365  OE2 GLU A 180     9693   9575   9706   -607    602  -2232       O  
ATOM   1366  N   THR A 181      21.028  10.441   0.332  1.00 33.46           N  
ANISOU 1366  N   THR A 181     3712   5275   3726   -863    480  -1794       N  
ATOM   1367  CA  THR A 181      19.690  10.861   0.741  1.00 38.25           C  
ANISOU 1367  CA  THR A 181     4259   5948   4328   -913    500  -1790       C  
ATOM   1368  C   THR A 181      19.198  11.987  -0.162  1.00 38.68           C  
ANISOU 1368  C   THR A 181     4172   6349   4176   -823    360  -1777       C  
ATOM   1369  O   THR A 181      18.230  12.682   0.162  1.00 37.88           O  
ANISOU 1369  O   THR A 181     4015   6341   4035   -791    317  -1748       O  
ATOM   1370  CB  THR A 181      19.616  11.255   2.259  1.00 31.60           C  
ANISOU 1370  CB  THR A 181     3606   4857   3543   -881    547  -1570       C  
ATOM   1371  OG1 THR A 181      20.507  12.341   2.545  1.00 32.42           O  
ANISOU 1371  OG1 THR A 181     3790   4977   3553   -733    437  -1344       O  
ATOM   1372  CG2 THR A 181      19.971  10.049   3.153  1.00 31.95           C  
ANISOU 1372  CG2 THR A 181     3873   4533   3735   -925    693  -1580       C  
ATOM   1373  N   VAL A 182      19.868  12.109  -1.311  1.00 38.77           N  
ANISOU 1373  N   VAL A 182     4147   6538   4045   -769    298  -1814       N  
ATOM   1374  CA  VAL A 182      19.681  13.191  -2.277  1.00 41.68           C  
ANISOU 1374  CA  VAL A 182     4498   7188   4150   -635    182  -1747       C  
ATOM   1375  C   VAL A 182      20.149  14.524  -1.707  1.00 47.56           C  
ANISOU 1375  C   VAL A 182     5414   7844   4811   -535    162  -1442       C  
ATOM   1376  O   VAL A 182      21.135  15.103  -2.180  1.00 51.42           O  
ANISOU 1376  O   VAL A 182     6015   8337   5186   -499    194  -1325       O  
ATOM   1377  CB  VAL A 182      18.223  13.311  -2.761  1.00 42.60           C  
ANISOU 1377  CB  VAL A 182     4440   7523   4225   -562     84  -1879       C  
ATOM   1378  CG1 VAL A 182      18.138  14.302  -3.916  1.00 40.41           C  
ANISOU 1378  CG1 VAL A 182     4218   7466   3671   -349    -49  -1766       C  
ATOM   1379  CG2 VAL A 182      17.701  11.958  -3.184  1.00 42.65           C  
ANISOU 1379  CG2 VAL A 182     4236   7555   4414   -679    153  -2172       C  
ATOM   1380  N   SER A 183      19.435  14.990  -0.687  1.00 43.14           N  
ANISOU 1380  N   SER A 183     4866   7196   4330   -513    142  -1345       N  
ATOM   1381  CA  SER A 183      19.746  16.234   0.002  1.00 41.91           C  
ANISOU 1381  CA  SER A 183     4846   6939   4138   -427    129  -1085       C  
ATOM   1382  C   SER A 183      19.605  16.019   1.519  1.00 36.84           C  
ANISOU 1382  C   SER A 183     4234   6064   3700   -485    181  -1024       C  
ATOM   1383  O   SER A 183      19.986  14.976   2.060  1.00 34.08           O  
ANISOU 1383  O   SER A 183     3911   5538   3498   -571    259  -1096       O  
ATOM   1384  CB  SER A 183      18.786  17.336  -0.469  1.00 46.05           C  
ANISOU 1384  CB  SER A 183     5372   7659   4464   -268      9  -1024       C  
ATOM   1385  OG  SER A 183      19.326  18.631  -0.272  1.00 49.42           O  
ANISOU 1385  OG  SER A 183     5977   7995   4803   -176     25   -772       O  
ATOM   1386  N   HIS A 184      19.025  16.990   2.206  1.00 35.23           N  
ANISOU 1386  N   HIS A 184     4052   5850   3483   -418    140   -896       N  
ATOM   1387  CA  HIS A 184      18.965  16.931   3.660  1.00 35.38           C  
ANISOU 1387  CA  HIS A 184     4131   5661   3649   -456    196   -820       C  
ATOM   1388  C   HIS A 184      17.928  15.916   4.190  1.00 36.41           C  
ANISOU 1388  C   HIS A 184     4196   5739   3899   -586    284   -991       C  
ATOM   1389  O   HIS A 184      16.930  15.619   3.516  1.00 33.96           O  
ANISOU 1389  O   HIS A 184     3718   5609   3575   -633    270  -1197       O  
ATOM   1390  CB  HIS A 184      18.742  18.347   4.231  1.00 41.48           C  
ANISOU 1390  CB  HIS A 184     4940   6439   4380   -352    141   -645       C  
ATOM   1391  CG  HIS A 184      17.518  19.043   3.702  1.00 50.76           C  
ANISOU 1391  CG  HIS A 184     6014   7821   5451   -266     39   -694       C  
ATOM   1392  ND1 HIS A 184      17.265  20.378   3.925  1.00 51.97           N  
ANISOU 1392  ND1 HIS A 184     6214   7992   5541   -134    -31   -550       N  
ATOM   1393  CD2 HIS A 184      16.470  18.579   2.978  1.00 50.61           C  
ANISOU 1393  CD2 HIS A 184     5837   8007   5386   -265    -22   -912       C  
ATOM   1394  CE1 HIS A 184      16.110  20.708   3.371  1.00 42.73           C  
ANISOU 1394  CE1 HIS A 184     4937   7026   4274    -22   -154   -662       C  
ATOM   1395  NE2 HIS A 184      15.614  19.637   2.783  1.00 51.29           N  
ANISOU 1395  NE2 HIS A 184     5876   8246   5364    -96   -158   -902       N  
ATOM   1396  N   VAL A 185      18.182  15.364   5.381  1.00 29.57           N  
ANISOU 1396  N   VAL A 185     3476   4620   3140   -640    393   -933       N  
ATOM   1397  CA  VAL A 185      17.197  14.547   6.092  1.00 29.06           C  
ANISOU 1397  CA  VAL A 185     3426   4433   3180   -792    557  -1061       C  
ATOM   1398  C   VAL A 185      16.890  15.151   7.461  1.00 27.03           C  
ANISOU 1398  C   VAL A 185     3282   4053   2935   -773    604   -920       C  
ATOM   1399  O   VAL A 185      16.003  14.669   8.183  1.00 26.13           O  
ANISOU 1399  O   VAL A 185     3204   3832   2892   -917    780  -1014       O  
ATOM   1400  CB  VAL A 185      17.669  13.092   6.283  1.00 31.02           C  
ANISOU 1400  CB  VAL A 185     3845   4427   3514   -882    709  -1128       C  
ATOM   1401  CG1 VAL A 185      17.933  12.448   4.935  1.00 25.81           C  
ANISOU 1401  CG1 VAL A 185     3046   3900   2860   -916    672  -1305       C  
ATOM   1402  CG2 VAL A 185      18.919  13.029   7.186  1.00 30.49           C  
ANISOU 1402  CG2 VAL A 185     4046   4123   3418   -730    677   -922       C  
ATOM   1403  N   ALA A 186      17.622  16.208   7.813  1.00 23.83           N  
ANISOU 1403  N   ALA A 186     2927   3661   2465   -616    476   -724       N  
ATOM   1404  CA  ALA A 186      17.420  16.876   9.103  1.00 22.99           C  
ANISOU 1404  CA  ALA A 186     2910   3465   2360   -575    498   -603       C  
ATOM   1405  C   ALA A 186      17.938  18.311   9.072  1.00 23.23           C  
ANISOU 1405  C   ALA A 186     2882   3601   2344   -425    347   -465       C  
ATOM   1406  O   ALA A 186      18.761  18.642   8.232  1.00 27.40           O  
ANISOU 1406  O   ALA A 186     3381   4195   2836   -356    266   -432       O  
ATOM   1407  CB  ALA A 186      18.085  16.086  10.241  1.00 20.99           C  
ANISOU 1407  CB  ALA A 186     2939   2935   2100   -542    595   -517       C  
ATOM   1408  N   LEU A 187      17.446  19.152   9.989  1.00 23.44           N  
ANISOU 1408  N   LEU A 187     2898   3626   2380   -395    343   -404       N  
ATOM   1409  CA  LEU A 187      17.810  20.570  10.013  1.00 22.53           C  
ANISOU 1409  CA  LEU A 187     2732   3580   2250   -270    233   -294       C  
ATOM   1410  C   LEU A 187      18.143  21.068  11.422  1.00 21.16           C  
ANISOU 1410  C   LEU A 187     2644   3296   2100   -208    246   -214       C  
ATOM   1411  O   LEU A 187      17.409  20.788  12.372  1.00 21.80           O  
ANISOU 1411  O   LEU A 187     2774   3324   2186   -265    330   -238       O  
ATOM   1412  CB  LEU A 187      16.673  21.440   9.460  1.00 27.51           C  
ANISOU 1412  CB  LEU A 187     3204   4386   2861   -245    163   -339       C  
ATOM   1413  CG  LEU A 187      16.198  21.283   8.028  1.00 31.25           C  
ANISOU 1413  CG  LEU A 187     3576   5036   3261   -227     92   -438       C  
ATOM   1414  CD1 LEU A 187      14.926  22.117   7.809  1.00 30.31           C  
ANISOU 1414  CD1 LEU A 187     3308   5092   3116   -135    -14   -528       C  
ATOM   1415  CD2 LEU A 187      17.300  21.714   7.058  1.00 28.92           C  
ANISOU 1415  CD2 LEU A 187     3368   4742   2877   -142     48   -321       C  
ATOM   1416  N   LYS A 188      19.239  21.813  11.536  1.00 17.87           N  
ANISOU 1416  N   LYS A 188     2236   2855   1697   -102    184   -152       N  
ATOM   1417  CA  LYS A 188      19.630  22.469  12.789  1.00 23.89           C  
ANISOU 1417  CA  LYS A 188     3032   3560   2486    -13    166   -122       C  
ATOM   1418  C   LYS A 188      19.231  23.945  12.770  1.00 24.18           C  
ANISOU 1418  C   LYS A 188     2950   3664   2574     15    135    -85       C  
ATOM   1419  O   LYS A 188      19.463  24.638  11.783  1.00 21.39           O  
ANISOU 1419  O   LYS A 188     2551   3346   2232     25    121    -54       O  
ATOM   1420  CB  LYS A 188      21.148  22.389  12.949  1.00 22.25           C  
ANISOU 1420  CB  LYS A 188     2857   3299   2298     93    119   -168       C  
ATOM   1421  CG  LYS A 188      21.684  23.113  14.211  1.00 27.97           C  
ANISOU 1421  CG  LYS A 188     3573   4005   3049    218     73   -203       C  
ATOM   1422  CD  LYS A 188      23.206  23.052  14.281  1.00 32.07           C  
ANISOU 1422  CD  LYS A 188     4054   4518   3612    339      8   -346       C  
ATOM   1423  CE  LYS A 188      23.704  21.678  14.674  1.00 42.12           C  
ANISOU 1423  CE  LYS A 188     5498   5718   4787    466    -54   -392       C  
ATOM   1424  NZ  LYS A 188      25.204  21.620  14.686  1.00 49.05           N  
ANISOU 1424  NZ  LYS A 188     6287   6631   5721    621   -155   -605       N  
ATOM   1425  N   ALA A 189      18.647  24.449  13.849  1.00 18.22           N  
ANISOU 1425  N   ALA A 189     2176   2907   1839     34    141    -85       N  
ATOM   1426  CA  ALA A 189      18.369  25.886  13.916  1.00 18.64           C  
ANISOU 1426  CA  ALA A 189     2126   2994   1963     83    108    -62       C  
ATOM   1427  C   ALA A 189      19.592  26.613  14.448  1.00 23.15           C  
ANISOU 1427  C   ALA A 189     2684   3504   2608    157    105    -87       C  
ATOM   1428  O   ALA A 189      20.076  26.288  15.531  1.00 23.11           O  
ANISOU 1428  O   ALA A 189     2714   3480   2589    214     90   -146       O  
ATOM   1429  CB  ALA A 189      17.127  26.163  14.828  1.00 26.47           C  
ANISOU 1429  CB  ALA A 189     3057   4034   2967     62    121   -103       C  
ATOM   1430  N   LEU A 190      20.104  27.593  13.706  1.00 20.93           N  
ANISOU 1430  N   LEU A 190     2367   3189   2397    164    134    -68       N  
ATOM   1431  CA  LEU A 190      21.342  28.258  14.137  1.00 22.26           C  
ANISOU 1431  CA  LEU A 190     2480   3299   2680    190    177   -171       C  
ATOM   1432  C   LEU A 190      21.114  29.584  14.867  1.00 21.50           C  
ANISOU 1432  C   LEU A 190     2303   3167   2700    224    200   -200       C  
ATOM   1433  O   LEU A 190      22.056  30.197  15.364  1.00 22.49           O  
ANISOU 1433  O   LEU A 190     2340   3256   2949    236    248   -343       O  
ATOM   1434  CB  LEU A 190      22.297  28.483  12.954  1.00 20.75           C  
ANISOU 1434  CB  LEU A 190     2309   3049   2526    126    280   -191       C  
ATOM   1435  CG  LEU A 190      22.816  27.240  12.226  1.00 21.71           C  
ANISOU 1435  CG  LEU A 190     2475   3209   2566     93    267   -219       C  
ATOM   1436  CD1 LEU A 190      23.622  27.663  10.969  1.00 22.09           C  
ANISOU 1436  CD1 LEU A 190     2553   3202   2640      1    414   -238       C  
ATOM   1437  CD2 LEU A 190      23.664  26.354  13.143  1.00 23.63           C  
ANISOU 1437  CD2 LEU A 190     2675   3480   2822    172    187   -380       C  
ATOM   1438  N   ASN A 191      19.876  30.055  14.915  1.00 23.24           N  
ANISOU 1438  N   ASN A 191     2525   3405   2900    242    167   -112       N  
ATOM   1439  CA  ASN A 191      19.581  31.253  15.713  1.00 22.29           C  
ANISOU 1439  CA  ASN A 191     2321   3251   2898    286    177   -158       C  
ATOM   1440  C   ASN A 191      18.117  31.259  16.130  1.00 25.02           C  
ANISOU 1440  C   ASN A 191     2629   3680   3196    315    102   -130       C  
ATOM   1441  O   ASN A 191      17.390  30.308  15.858  1.00 23.72           O  
ANISOU 1441  O   ASN A 191     2492   3599   2921    282     64   -104       O  
ATOM   1442  CB  ASN A 191      19.962  32.556  14.971  1.00 19.50           C  
ANISOU 1442  CB  ASN A 191     2009   2742   2660    282    290   -122       C  
ATOM   1443  CG  ASN A 191      19.239  32.707  13.631  1.00 24.08           C  
ANISOU 1443  CG  ASN A 191     2743   3281   3124    323    280     51       C  
ATOM   1444  OD1 ASN A 191      18.279  31.991  13.344  1.00 23.15           O  
ANISOU 1444  OD1 ASN A 191     2626   3290   2880    361    161     95       O  
ATOM   1445  ND2 ASN A 191      19.697  33.650  12.811  1.00 22.36           N  
ANISOU 1445  ND2 ASN A 191     2671   2884   2941    324    419    125       N  
ATOM   1446  N   GLY A 192      17.692  32.311  16.822  1.00 25.91           N  
ANISOU 1446  N   GLY A 192     2655   3775   3413    362     97   -181       N  
ATOM   1447  CA  GLY A 192      16.343  32.363  17.361  1.00 25.27           C  
ANISOU 1447  CA  GLY A 192     2493   3795   3315    382     37   -223       C  
ATOM   1448  C   GLY A 192      16.301  31.610  18.683  1.00 22.22           C  
ANISOU 1448  C   GLY A 192     2082   3496   2866    331     58   -314       C  
ATOM   1449  O   GLY A 192      17.282  30.957  19.072  1.00 19.40           O  
ANISOU 1449  O   GLY A 192     1798   3125   2448    330     77   -324       O  
ATOM   1450  N   PRO A 193      15.151  31.654  19.372  1.00 26.87           N  
ANISOU 1450  N   PRO A 193     2587   4174   3447    306     60   -395       N  
ATOM   1451  CA  PRO A 193      15.138  31.054  20.706  1.00 25.47           C  
ANISOU 1451  CA  PRO A 193     2453   4051   3174    263    124   -466       C  
ATOM   1452  C   PRO A 193      15.238  29.527  20.658  1.00 28.35           C  
ANISOU 1452  C   PRO A 193     3004   4402   3368    184    194   -408       C  
ATOM   1453  O   PRO A 193      15.540  28.933  21.678  1.00 25.36           O  
ANISOU 1453  O   PRO A 193     2767   4014   2856    196    251   -418       O  
ATOM   1454  CB  PRO A 193      13.796  31.517  21.292  1.00 27.79           C  
ANISOU 1454  CB  PRO A 193     2605   4438   3516    220    152   -592       C  
ATOM   1455  CG  PRO A 193      12.922  31.751  20.105  1.00 25.89           C  
ANISOU 1455  CG  PRO A 193     2265   4227   3345    231     83   -602       C  
ATOM   1456  CD  PRO A 193      13.850  32.244  19.005  1.00 28.32           C  
ANISOU 1456  CD  PRO A 193     2646   4420   3694    333      8   -458       C  
ATOM   1457  N   GLU A 194      15.018  28.901  19.502  1.00 24.99           N  
ANISOU 1457  N   GLU A 194     2603   3962   2928    126    191   -352       N  
ATOM   1458  CA  GLU A 194      15.160  27.450  19.410  1.00 23.55           C  
ANISOU 1458  CA  GLU A 194     2603   3733   2612     45    275   -311       C  
ATOM   1459  C   GLU A 194      16.535  26.973  18.921  1.00 26.19           C  
ANISOU 1459  C   GLU A 194     3058   3989   2903    127    216   -224       C  
ATOM   1460  O   GLU A 194      16.709  25.788  18.643  1.00 25.54           O  
ANISOU 1460  O   GLU A 194     3127   3849   2728     82    267   -188       O  
ATOM   1461  CB  GLU A 194      14.066  26.852  18.516  1.00 36.76           C  
ANISOU 1461  CB  GLU A 194     4208   5459   4301    -86    326   -371       C  
ATOM   1462  CG  GLU A 194      12.697  26.902  19.141  1.00 49.32           C  
ANISOU 1462  CG  GLU A 194     5684   7133   5922   -208    436   -537       C  
ATOM   1463  CD  GLU A 194      11.779  25.821  18.607  1.00 60.55           C  
ANISOU 1463  CD  GLU A 194     7080   8585   7340   -389    569   -669       C  
ATOM   1464  OE1 GLU A 194      11.617  25.746  17.366  1.00 63.68           O  
ANISOU 1464  OE1 GLU A 194     7364   9052   7778   -360    464   -702       O  
ATOM   1465  OE2 GLU A 194      11.237  25.045  19.429  1.00 61.00           O  
ANISOU 1465  OE2 GLU A 194     7245   8589   7344   -564    800   -756       O  
ATOM   1466  N   ALA A 195      17.503  27.880  18.823  1.00 24.98           N  
ANISOU 1466  N   ALA A 195     2826   3826   2838    233    132   -229       N  
ATOM   1467  CA  ALA A 195      18.846  27.526  18.383  1.00 26.29           C  
ANISOU 1467  CA  ALA A 195     3048   3944   2998    299     89   -225       C  
ATOM   1468  C   ALA A 195      19.427  26.415  19.250  1.00 29.33           C  
ANISOU 1468  C   ALA A 195     3622   4297   3224    389     78   -244       C  
ATOM   1469  O   ALA A 195      19.320  26.457  20.470  1.00 28.19           O  
ANISOU 1469  O   ALA A 195     3550   4171   2991    467     79   -281       O  
ATOM   1470  CB  ALA A 195      19.754  28.748  18.440  1.00 29.82           C  
ANISOU 1470  CB  ALA A 195     3356   4383   3591    368     58   -309       C  
ATOM   1471  N   SER A 196      20.045  25.423  18.627  1.00 26.23           N  
ANISOU 1471  N   SER A 196     3338   3851   2776    403     64   -220       N  
ATOM   1472  CA  SER A 196      20.654  24.347  19.396  1.00 31.60           C  
ANISOU 1472  CA  SER A 196     4252   4469   3287    549     31   -232       C  
ATOM   1473  C   SER A 196      21.527  23.433  18.566  1.00 30.70           C  
ANISOU 1473  C   SER A 196     4203   4300   3162    593    -15   -248       C  
ATOM   1474  O   SER A 196      21.694  23.626  17.356  1.00 26.14           O  
ANISOU 1474  O   SER A 196     3482   3747   2704    485     -4   -253       O  
ATOM   1475  CB  SER A 196      19.591  23.527  20.126  1.00 34.49           C  
ANISOU 1475  CB  SER A 196     4860   4753   3490    479    168   -142       C  
ATOM   1476  OG  SER A 196      19.185  22.430  19.340  1.00 31.63           O  
ANISOU 1476  OG  SER A 196     4618   4294   3107    347    270    -81       O  
ATOM   1477  N   GLU A 197      22.116  22.447  19.233  1.00 32.42           N  
ANISOU 1477  N   GLU A 197     4662   4440   3215    781    -72   -263       N  
ATOM   1478  CA  GLU A 197      22.983  21.504  18.544  1.00 37.12           C  
ANISOU 1478  CA  GLU A 197     5328   4977   3799    860   -134   -309       C  
ATOM   1479  C   GLU A 197      22.199  20.383  17.868  1.00 33.25           C  
ANISOU 1479  C   GLU A 197     5010   4356   3269    689      9   -183       C  
ATOM   1480  O   GLU A 197      22.774  19.607  17.110  1.00 38.26           O  
ANISOU 1480  O   GLU A 197     5675   4940   3923    710    -22   -221       O  
ATOM   1481  CB  GLU A 197      24.025  20.909  19.499  1.00 52.61           C  
ANISOU 1481  CB  GLU A 197     7486   6907   5595   1205   -298   -412       C  
ATOM   1482  CG  GLU A 197      25.208  21.824  19.791  1.00 64.73           C  
ANISOU 1482  CG  GLU A 197     8750   8614   7231   1391   -475   -671       C  
ATOM   1483  CD  GLU A 197      25.106  22.485  21.153  1.00 73.49           C  
ANISOU 1483  CD  GLU A 197     9888   9804   8232   1560   -542   -723       C  
ATOM   1484  OE1 GLU A 197      24.067  22.300  21.823  1.00 76.80           O  
ANISOU 1484  OE1 GLU A 197    10541  10143   8496   1503   -429   -534       O  
ATOM   1485  OE2 GLU A 197      26.062  23.184  21.555  1.00 76.02           O  
ANISOU 1485  OE2 GLU A 197     9980  10276   8628   1737   -690   -991       O  
ATOM   1486  N   LEU A 198      20.892  20.307  18.123  1.00 24.35           N  
ANISOU 1486  N   LEU A 198     3962   3182   2109    506    177    -83       N  
ATOM   1487  CA  LEU A 198      20.087  19.200  17.604  1.00 26.56           C  
ANISOU 1487  CA  LEU A 198     4390   3333   2371    321    353    -32       C  
ATOM   1488  C   LEU A 198      19.775  19.381  16.126  1.00 25.64           C  
ANISOU 1488  C   LEU A 198     4000   3328   2413    137    355    -80       C  
ATOM   1489  O   LEU A 198      19.443  20.475  15.678  1.00 27.33           O  
ANISOU 1489  O   LEU A 198     3961   3696   2726     75    308    -98       O  
ATOM   1490  CB  LEU A 198      18.771  19.026  18.372  1.00 31.18           C  
ANISOU 1490  CB  LEU A 198     5118   3841   2890    154    575     12       C  
ATOM   1491  CG  LEU A 198      18.770  18.522  19.818  1.00 34.17           C  
ANISOU 1491  CG  LEU A 198     5897   4047   3039    285    676     93       C  
ATOM   1492  CD1 LEU A 198      17.326  18.457  20.311  1.00 40.09           C  
ANISOU 1492  CD1 LEU A 198     6709   4746   3779     16    966     86       C  
ATOM   1493  CD2 LEU A 198      19.440  17.154  20.001  1.00 35.66           C  
ANISOU 1493  CD2 LEU A 198     6506   3983   3061    449    707    162       C  
ATOM   1494  N   TYR A 199      19.894  18.301  15.371  1.00 26.63           N  
ANISOU 1494  N   TYR A 199     2712   3358   4050    120    325   -774       N  
ATOM   1495  CA  TYR A 199      19.333  18.258  14.027  1.00 24.91           C  
ANISOU 1495  CA  TYR A 199     2454   3151   3861     44    342   -663       C  
ATOM   1496  C   TYR A 199      17.950  17.625  14.151  1.00 24.36           C  
ANISOU 1496  C   TYR A 199     2348   3292   3614    -66    431   -714       C  
ATOM   1497  O   TYR A 199      17.830  16.502  14.623  1.00 27.28           O  
ANISOU 1497  O   TYR A 199     2837   3728   3800   -181    533   -701       O  
ATOM   1498  CB  TYR A 199      20.210  17.407  13.114  1.00 18.15           C  
ANISOU 1498  CB  TYR A 199     1739   2203   2954    -32    399   -508       C  
ATOM   1499  CG  TYR A 199      21.576  18.008  12.787  1.00 22.77           C  
ANISOU 1499  CG  TYR A 199     2309   2627   3715     54    330   -411       C  
ATOM   1500  CD1 TYR A 199      21.736  18.918  11.740  1.00 21.28           C  
ANISOU 1500  CD1 TYR A 199     2008   2388   3690     77    258   -286       C  
ATOM   1501  CD2 TYR A 199      22.699  17.632  13.499  1.00 24.81           C  
ANISOU 1501  CD2 TYR A 199     2649   2804   3975    100    334   -410       C  
ATOM   1502  CE1 TYR A 199      22.995  19.441  11.425  1.00 21.27           C  
ANISOU 1502  CE1 TYR A 199     1963   2262   3855    120    207   -157       C  
ATOM   1503  CE2 TYR A 199      23.961  18.145  13.194  1.00 25.32           C  
ANISOU 1503  CE2 TYR A 199     2661   2750   4210    159    273   -307       C  
ATOM   1504  CZ  TYR A 199      24.100  19.043  12.161  1.00 25.46           C  
ANISOU 1504  CZ  TYR A 199     2556   2725   4394    158    219   -178       C  
ATOM   1505  OH  TYR A 199      25.347  19.543  11.886  1.00 29.17           O  
ANISOU 1505  OH  TYR A 199     2945   3099   5039    186    167    -45       O  
ATOM   1506  N   VAL A 200      16.913  18.332  13.717  1.00 26.20           N  
ANISOU 1506  N   VAL A 200     2408   3627   3922    -37    384   -749       N  
ATOM   1507  CA  VAL A 200      15.553  17.813  13.779  1.00 23.49           C  
ANISOU 1507  CA  VAL A 200     1973   3518   3434   -150    459   -788       C  
ATOM   1508  C   VAL A 200      15.185  17.127  12.462  1.00 23.53           C  
ANISOU 1508  C   VAL A 200     2019   3550   3372   -316    467   -664       C  
ATOM   1509  O   VAL A 200      15.250  17.735  11.394  1.00 25.00           O  
ANISOU 1509  O   VAL A 200     2148   3690   3662   -273    376   -581       O  
ATOM   1510  CB  VAL A 200      14.551  18.930  14.097  1.00 24.38           C  
ANISOU 1510  CB  VAL A 200     1838   3765   3662     -1    399   -918       C  
ATOM   1511  CG1 VAL A 200      13.118  18.391  14.171  1.00 29.79           C  
ANISOU 1511  CG1 VAL A 200     2374   4745   4200   -123    486   -945       C  
ATOM   1512  CG2 VAL A 200      14.933  19.632  15.420  1.00 27.91           C  
ANISOU 1512  CG2 VAL A 200     2258   4191   4155    183    380  -1106       C  
ATOM   1513  N   PHE A 201      14.816  15.853  12.544  1.00 27.38           N  
ANISOU 1513  N   PHE A 201     2613   4110   3682   -515    562   -647       N  
ATOM   1514  CA  PHE A 201      14.474  15.059  11.360  1.00 27.52           C  
ANISOU 1514  CA  PHE A 201     2699   4144   3616   -693    556   -583       C  
ATOM   1515  C   PHE A 201      13.329  15.658  10.543  1.00 30.36           C  
ANISOU 1515  C   PHE A 201     2836   4692   4006   -712    469   -576       C  
ATOM   1516  O   PHE A 201      12.286  16.018  11.083  1.00 29.80           O  
ANISOU 1516  O   PHE A 201     2557   4813   3952   -703    473   -634       O  
ATOM   1517  CB  PHE A 201      14.112  13.623  11.769  1.00 29.51           C  
ANISOU 1517  CB  PHE A 201     3085   4411   3718   -922    649   -583       C  
ATOM   1518  CG  PHE A 201      15.297  12.803  12.220  1.00 30.89           C  
ANISOU 1518  CG  PHE A 201     3515   4361   3862   -915    708   -549       C  
ATOM   1519  CD1 PHE A 201      16.290  12.424  11.307  1.00 25.40           C  
ANISOU 1519  CD1 PHE A 201     2995   3476   3179   -878    692   -525       C  
ATOM   1520  CD2 PHE A 201      15.436  12.438  13.558  1.00 28.80           C  
ANISOU 1520  CD2 PHE A 201     3297   4102   3543   -921    779   -533       C  
ATOM   1521  CE1 PHE A 201      17.392  11.680  11.719  1.00 25.12           C  
ANISOU 1521  CE1 PHE A 201     3168   3236   3139   -835    740   -496       C  
ATOM   1522  CE2 PHE A 201      16.538  11.694  13.991  1.00 26.88           C  
ANISOU 1522  CE2 PHE A 201     3277   3653   3284   -893    810   -476       C  
ATOM   1523  CZ  PHE A 201      17.513  11.303  13.077  1.00 28.88           C  
ANISOU 1523  CZ  PHE A 201     3694   3692   3587   -843    787   -461       C  
ATOM   1524  N   LEU A 202      13.535  15.759   9.233  1.00 30.79           N  
ANISOU 1524  N   LEU A 202     2923   4723   4053   -726    391   -500       N  
ATOM   1525  CA  LEU A 202      12.485  16.180   8.315  1.00 30.32           C  
ANISOU 1525  CA  LEU A 202     2673   4860   3989   -763    284   -463       C  
ATOM   1526  C   LEU A 202      11.353  15.150   8.293  1.00 35.46           C  
ANISOU 1526  C   LEU A 202     3281   5691   4501  -1014    307   -525       C  
ATOM   1527  O   LEU A 202      11.575  13.969   8.548  1.00 32.70           O  
ANISOU 1527  O   LEU A 202     3122   5254   4049  -1188    388   -566       O  
ATOM   1528  CB  LEU A 202      13.063  16.347   6.907  1.00 30.57           C  
ANISOU 1528  CB  LEU A 202     2781   4863   3971   -747    206   -351       C  
ATOM   1529  CG  LEU A 202      14.024  17.518   6.728  1.00 35.96           C  
ANISOU 1529  CG  LEU A 202     3439   5403   4820   -536    156   -225       C  
ATOM   1530  CD1 LEU A 202      14.780  17.401   5.407  1.00 39.22           C  
ANISOU 1530  CD1 LEU A 202     3960   5827   5115   -554    136    -94       C  
ATOM   1531  CD2 LEU A 202      13.272  18.825   6.805  1.00 35.81           C  
ANISOU 1531  CD2 LEU A 202     3165   5443   4999   -387     30   -171       C  
ATOM   1532  N   PRO A 203      10.130  15.593   7.973  1.00 44.71           N  
ANISOU 1532  N   PRO A 203     4190   7103   5694  -1039    220   -518       N  
ATOM   1533  CA  PRO A 203       9.002  14.654   7.983  1.00 46.51           C  
ANISOU 1533  CA  PRO A 203     4330   7525   5815  -1307    229   -564       C  
ATOM   1534  C   PRO A 203       9.177  13.596   6.889  1.00 38.58           C  
ANISOU 1534  C   PRO A 203     3533   6467   4660  -1530    174   -581       C  
ATOM   1535  O   PRO A 203       9.680  13.908   5.809  1.00 40.50           O  
ANISOU 1535  O   PRO A 203     3853   6685   4851  -1452     87   -541       O  
ATOM   1536  CB  PRO A 203       7.801  15.551   7.666  1.00 49.75           C  
ANISOU 1536  CB  PRO A 203     4440   8163   6301  -1197    112   -524       C  
ATOM   1537  CG  PRO A 203       8.389  16.674   6.825  1.00 46.32           C  
ANISOU 1537  CG  PRO A 203     3948   7688   5961   -991     -9   -438       C  
ATOM   1538  CD  PRO A 203       9.785  16.892   7.358  1.00 44.76           C  
ANISOU 1538  CD  PRO A 203     3980   7197   5828   -844     81   -437       C  
ATOM   1539  N   GLY A 204       8.783  12.364   7.172  1.00 33.00           N  
ANISOU 1539  N   GLY A 204     2922   5737   3879  -1800    220   -639       N  
ATOM   1540  CA  GLY A 204       8.874  11.298   6.192  1.00 39.33           C  
ANISOU 1540  CA  GLY A 204     3926   6460   4556  -2022    150   -715       C  
ATOM   1541  C   GLY A 204      10.158  10.505   6.295  1.00 40.05           C  
ANISOU 1541  C   GLY A 204     4376   6222   4620  -1996    240   -762       C  
ATOM   1542  O   GLY A 204      10.316   9.481   5.635  1.00 42.70           O  
ANISOU 1542  O   GLY A 204     4922   6432   4870  -2159    198   -868       O  
ATOM   1543  N   ILE A 205      11.078  10.977   7.126  1.00 36.56           N  
ANISOU 1543  N   ILE A 205     3995   5636   4260  -1779    349   -703       N  
ATOM   1544  CA  ILE A 205      12.306  10.251   7.394  1.00 35.62           C  
ANISOU 1544  CA  ILE A 205     4177   5218   4140  -1727    437   -726       C  
ATOM   1545  C   ILE A 205      12.098   9.270   8.548  1.00 35.48           C  
ANISOU 1545  C   ILE A 205     4251   5070   4160  -1902    521   -706       C  
ATOM   1546  O   ILE A 205      11.634   9.656   9.618  1.00 34.14           O  
ANISOU 1546  O   ILE A 205     3916   5027   4030  -1895    583   -633       O  
ATOM   1547  CB  ILE A 205      13.451  11.216   7.770  1.00 32.94           C  
ANISOU 1547  CB  ILE A 205     3844   4795   3878  -1426    493   -655       C  
ATOM   1548  CG1 ILE A 205      13.727  12.202   6.635  1.00 36.56           C  
ANISOU 1548  CG1 ILE A 205     4211   5365   4317  -1271    412   -611       C  
ATOM   1549  CG2 ILE A 205      14.713  10.450   8.112  1.00 33.07           C  
ANISOU 1549  CG2 ILE A 205     4131   4531   3903  -1360    578   -668       C  
ATOM   1550  CD1 ILE A 205      14.142  11.531   5.304  1.00 38.54           C  
ANISOU 1550  CD1 ILE A 205     4637   5599   4407  -1324    380   -682       C  
ATOM   1551  N   GLN A 206      12.430   8.001   8.331  1.00 34.93           N  
ANISOU 1551  N   GLN A 206     4444   4754   4074  -2054    521   -767       N  
ATOM   1552  CA  GLN A 206      12.465   7.028   9.424  1.00 37.58           C  
ANISOU 1552  CA  GLN A 206     4912   4898   4466  -2201    593   -691       C  
ATOM   1553  C   GLN A 206      13.919   6.933   9.877  1.00 37.90           C  
ANISOU 1553  C   GLN A 206     5168   4688   4546  -1959    666   -658       C  
ATOM   1554  O   GLN A 206      14.836   6.989   9.045  1.00 35.83           O  
ANISOU 1554  O   GLN A 206     5036   4310   4268  -1787    651   -746       O  
ATOM   1555  CB  GLN A 206      11.949   5.658   8.964  1.00 43.97           C  
ANISOU 1555  CB  GLN A 206     5887   5532   5289  -2443    510   -744       C  
ATOM   1556  CG  GLN A 206      10.488   5.657   8.525  1.00 56.33           C  
ANISOU 1556  CG  GLN A 206     7228   7350   6824  -2624    409   -748       C  
ATOM   1557  CD  GLN A 206      10.325   5.413   7.028  1.00 69.33           C  
ANISOU 1557  CD  GLN A 206     8941   9002   8400  -2685    272   -932       C  
ATOM   1558  OE1 GLN A 206       9.748   6.235   6.309  1.00 74.07           O  
ANISOU 1558  OE1 GLN A 206     9332   9891   8920  -2667    199   -968       O  
ATOM   1559  NE2 GLN A 206      10.835   4.276   6.551  1.00 71.49           N  
ANISOU 1559  NE2 GLN A 206     9501   8963   8700  -2732    225  -1050       N  
ATOM   1560  N   TYR A 207      14.132   6.795  11.183  1.00 33.27           N  
ANISOU 1560  N   TYR A 207     4596   4055   3990  -1944    746   -524       N  
ATOM   1561  CA  TYR A 207      15.479   6.906  11.761  1.00 28.87           C  
ANISOU 1561  CA  TYR A 207     4177   3326   3466  -1692    797   -472       C  
ATOM   1562  C   TYR A 207      15.667   5.960  12.940  1.00 32.63           C  
ANISOU 1562  C   TYR A 207     4803   3633   3964  -1789    844   -321       C  
ATOM   1563  O   TYR A 207      14.697   5.496  13.542  1.00 32.41           O  
ANISOU 1563  O   TYR A 207     4710   3694   3909  -2039    866   -219       O  
ATOM   1564  CB  TYR A 207      15.769   8.351  12.193  1.00 25.72           C  
ANISOU 1564  CB  TYR A 207     3570   3141   3060  -1452    817   -456       C  
ATOM   1565  CG  TYR A 207      14.653   8.958  13.022  1.00 28.83           C  
ANISOU 1565  CG  TYR A 207     3713   3832   3409  -1531    847   -416       C  
ATOM   1566  CD1 TYR A 207      14.589   8.741  14.395  1.00 33.21           C  
ANISOU 1566  CD1 TYR A 207     4259   4452   3909  -1560    920   -311       C  
ATOM   1567  CD2 TYR A 207      13.656   9.732  12.432  1.00 27.75           C  
ANISOU 1567  CD2 TYR A 207     3335   3939   3270  -1562    803   -480       C  
ATOM   1568  CE1 TYR A 207      13.564   9.279  15.162  1.00 35.85           C  
ANISOU 1568  CE1 TYR A 207     4344   5109   4167  -1611    974   -298       C  
ATOM   1569  CE2 TYR A 207      12.622  10.279  13.196  1.00 29.98           C  
ANISOU 1569  CE2 TYR A 207     3358   4514   3517  -1599    844   -466       C  
ATOM   1570  CZ  TYR A 207      12.593  10.050  14.557  1.00 35.62           C  
ANISOU 1570  CZ  TYR A 207     4065   5309   4160  -1618    941   -389       C  
ATOM   1571  OH  TYR A 207      11.581  10.579  15.320  1.00 41.50           O  
ANISOU 1571  OH  TYR A 207     4540   6390   4839  -1629   1003   -396       O  
ATOM   1572  N   GLY A 208      16.923   5.667  13.253  1.00 32.54           N  
ANISOU 1572  N   GLY A 208     4972   3392   3998  -1595    856   -281       N  
ATOM   1573  CA  GLY A 208      17.253   4.770  14.353  1.00 38.90           C  
ANISOU 1573  CA  GLY A 208     5936   4019   4826  -1649    879   -100       C  
ATOM   1574  C   GLY A 208      18.763   4.634  14.400  1.00 34.68           C  
ANISOU 1574  C   GLY A 208     5562   3256   4358  -1366    868    -96       C  
ATOM   1575  O   GLY A 208      19.452   5.281  13.617  1.00 28.87           O  
ANISOU 1575  O   GLY A 208     4784   2543   3644  -1159    861   -228       O  
ATOM   1576  N   VAL A 209      19.279   3.802  15.298  1.00 33.85           N  
ANISOU 1576  N   VAL A 209     5621   2950   4290  -1358    863     78       N  
ATOM   1577  CA  VAL A 209      20.718   3.546  15.355  1.00 34.86           C  
ANISOU 1577  CA  VAL A 209     5888   2852   4504  -1081    839     95       C  
ATOM   1578  C   VAL A 209      20.991   2.045  15.272  1.00 34.48           C  
ANISOU 1578  C   VAL A 209     6125   2377   4597  -1141    795    161       C  
ATOM   1579  O   VAL A 209      20.154   1.247  15.656  1.00 37.89           O  
ANISOU 1579  O   VAL A 209     6600   2748   5048  -1382    759    285       O  
ATOM   1580  CB  VAL A 209      21.356   4.120  16.651  1.00 33.35           C  
ANISOU 1580  CB  VAL A 209     5610   2827   4236   -924    836    254       C  
ATOM   1581  CG1 VAL A 209      21.285   5.643  16.654  1.00 28.95           C  
ANISOU 1581  CG1 VAL A 209     4795   2609   3596   -815    851    138       C  
ATOM   1582  CG2 VAL A 209      20.662   3.550  17.877  1.00 40.60           C  
ANISOU 1582  CG2 VAL A 209     6561   3809   5055  -1132    848    495       C  
ATOM   1583  N   ASP A 210      22.155   1.668  14.752  1.00 33.24           N  
ANISOU 1583  N   ASP A 210     6084   1991   4553   -878    768     72       N  
ATOM   1584  CA  ASP A 210      22.564   0.275  14.751  1.00 42.71           C  
ANISOU 1584  CA  ASP A 210     7446   2867   5914   -821    670    118       C  
ATOM   1585  C   ASP A 210      23.170  -0.053  16.113  1.00 44.71           C  
ANISOU 1585  C   ASP A 210     7750   3043   6193   -740    634    412       C  
ATOM   1586  O   ASP A 210      23.084   0.752  17.048  1.00 40.20           O  
ANISOU 1586  O   ASP A 210     7103   2696   5475   -773    688    568       O  
ATOM   1587  CB  ASP A 210      23.573   0.002  13.628  1.00 45.68           C  
ANISOU 1587  CB  ASP A 210     7864   3109   6383   -541    655   -114       C  
ATOM   1588  CG  ASP A 210      24.852   0.795  13.790  1.00 46.53           C  
ANISOU 1588  CG  ASP A 210     7874   3332   6473   -229    704    -99       C  
ATOM   1589  OD1 ASP A 210      25.049   1.405  14.865  1.00 44.10           O  
ANISOU 1589  OD1 ASP A 210     7509   3136   6110   -211    721     93       O  
ATOM   1590  OD2 ASP A 210      25.669   0.812  12.846  1.00 49.11           O  
ANISOU 1590  OD2 ASP A 210     8166   3661   6834     -4    724   -278       O  
ATOM   1591  N   GLU A 211      23.797  -1.219  16.216  1.00 48.12           N  
ANISOU 1591  N   GLU A 211     8305   3169   6808   -625    536    483       N  
ATOM   1592  CA  GLU A 211      24.338  -1.694  17.490  1.00 51.09           C  
ANISOU 1592  CA  GLU A 211     8732   3456   7224   -559    472    798       C  
ATOM   1593  C   GLU A 211      25.512  -0.857  18.002  1.00 47.77           C  
ANISOU 1593  C   GLU A 211     8238   3188   6723   -269    488    850       C  
ATOM   1594  O   GLU A 211      25.886  -0.954  19.174  1.00 45.10           O  
ANISOU 1594  O   GLU A 211     7918   2884   6333   -226    437   1126       O  
ATOM   1595  CB  GLU A 211      24.742  -3.171  17.382  1.00 58.54           C  
ANISOU 1595  CB  GLU A 211     9804   3996   8442   -491    351    852       C  
ATOM   1596  CG  GLU A 211      23.576  -4.095  17.069  1.00 69.49           C  
ANISOU 1596  CG  GLU A 211    11259   5191   9952   -796    315    850       C  
ATOM   1597  CD  GLU A 211      23.975  -5.566  17.028  1.00 79.95           C  
ANISOU 1597  CD  GLU A 211    12712   6061  11606   -728    204    911       C  
ATOM   1598  OE1 GLU A 211      24.989  -5.899  16.371  1.00 82.59           O  
ANISOU 1598  OE1 GLU A 211    13082   6206  12091   -436    161    712       O  
ATOM   1599  OE2 GLU A 211      23.273  -6.391  17.656  1.00 82.63           O  
ANISOU 1599  OE2 GLU A 211    13095   6238  12062   -961    180   1162       O  
ATOM   1600  N   ARG A 212      26.085  -0.031  17.130  1.00 45.52           N  
ANISOU 1600  N   ARG A 212     7851   3020   6422    -78    550    604       N  
ATOM   1601  CA  ARG A 212      27.215   0.818  17.511  1.00 44.01           C  
ANISOU 1601  CA  ARG A 212     7541   2984   6195    192    555    638       C  
ATOM   1602  C   ARG A 212      26.732   2.149  18.073  1.00 43.85           C  
ANISOU 1602  C   ARG A 212     7354   3333   5973     91    604    660       C  
ATOM   1603  O   ARG A 212      27.502   2.901  18.680  1.00 41.72           O  
ANISOU 1603  O   ARG A 212     6930   3271   5652    255    557    708       O  
ATOM   1604  CB  ARG A 212      28.126   1.079  16.309  1.00 43.45           C  
ANISOU 1604  CB  ARG A 212     7355   2938   6216    437    586    385       C  
ATOM   1605  CG  ARG A 212      28.696  -0.176  15.646  1.00 48.75           C  
ANISOU 1605  CG  ARG A 212     8108   3342   7071    574    521    284       C  
ATOM   1606  CD  ARG A 212      29.384   0.184  14.332  1.00 49.50           C  
ANISOU 1606  CD  ARG A 212     8080   3547   7179    768    594     19       C  
ATOM   1607  NE  ARG A 212      28.468   0.853  13.409  1.00 45.21           N  
ANISOU 1607  NE  ARG A 212     7514   3160   6502    599    692   -158       N  
ATOM   1608  CZ  ARG A 212      28.854   1.593  12.375  1.00 43.09           C  
ANISOU 1608  CZ  ARG A 212     7107   3098   6168    709    781   -326       C  
ATOM   1609  NH1 ARG A 212      27.953   2.160  11.583  1.00 38.42           N  
ANISOU 1609  NH1 ARG A 212     6504   2642   5454    543    851   -456       N  
ATOM   1610  NH2 ARG A 212      30.143   1.771  12.134  1.00 45.81           N  
ANISOU 1610  NH2 ARG A 212     7307   3532   6567    976    797   -342       N  
ATOM   1611  N   GLY A 213      25.453   2.435  17.859  1.00 40.02           N  
ANISOU 1611  N   GLY A 213     6832   2988   5384   -180    662    592       N  
ATOM   1612  CA  GLY A 213      24.896   3.732  18.179  1.00 35.07           C  
ANISOU 1612  CA  GLY A 213     5975   2757   4591   -255    692    529       C  
ATOM   1613  C   GLY A 213      25.006   4.722  17.026  1.00 32.99           C  
ANISOU 1613  C   GLY A 213     5554   2616   4364   -173    735    286       C  
ATOM   1614  O   GLY A 213      24.889   5.927  17.235  1.00 32.00           O  
ANISOU 1614  O   GLY A 213     5228   2763   4166   -152    731    225       O  
ATOM   1615  N   CYS A 214      25.237   4.218  15.812  1.00 29.89           N  
ANISOU 1615  N   CYS A 214     5255   2020   4080   -121    769    149       N  
ATOM   1616  CA  CYS A 214      25.377   5.071  14.627  1.00 29.69           C  
ANISOU 1616  CA  CYS A 214     5088   2131   4061    -48    816    -40       C  
ATOM   1617  C   CYS A 214      24.057   5.237  13.863  1.00 29.90           C  
ANISOU 1617  C   CYS A 214     5092   2256   4011   -282    850   -161       C  
ATOM   1618  O   CYS A 214      23.312   4.277  13.653  1.00 30.87           O  
ANISOU 1618  O   CYS A 214     5376   2213   4139   -464    848   -182       O  
ATOM   1619  CB  CYS A 214      26.424   4.498  13.669  1.00 31.01           C  
ANISOU 1619  CB  CYS A 214     5338   2107   4336    171    849   -141       C  
ATOM   1620  SG  CYS A 214      28.141   4.587  14.233  1.00 44.10           S  
ANISOU 1620  SG  CYS A 214     6916   3734   6107    501    814    -29       S  
ATOM   1621  N   LEU A 215      23.814   6.451  13.394  1.00 27.64           N  
ANISOU 1621  N   LEU A 215     4602   2222   3678   -275    862   -234       N  
ATOM   1622  CA  LEU A 215      22.548   6.797  12.757  1.00 28.76           C  
ANISOU 1622  CA  LEU A 215     4671   2514   3744   -475    871   -323       C  
ATOM   1623  C   LEU A 215      22.319   6.043  11.455  1.00 30.30           C  
ANISOU 1623  C   LEU A 215     4998   2588   3927   -536    888   -472       C  
ATOM   1624  O   LEU A 215      23.207   5.962  10.587  1.00 29.20           O  
ANISOU 1624  O   LEU A 215     4894   2397   3805   -359    920   -559       O  
ATOM   1625  CB  LEU A 215      22.511   8.296  12.471  1.00 24.42           C  
ANISOU 1625  CB  LEU A 215     3877   2217   3184   -404    858   -349       C  
ATOM   1626  CG  LEU A 215      21.240   8.886  11.843  1.00 25.50           C  
ANISOU 1626  CG  LEU A 215     3885   2547   3257   -563    846   -416       C  
ATOM   1627  CD1 LEU A 215      20.037   8.705  12.773  1.00 25.65           C  
ANISOU 1627  CD1 LEU A 215     3866   2661   3218   -758    843   -378       C  
ATOM   1628  CD2 LEU A 215      21.454  10.370  11.541  1.00 22.65           C  
ANISOU 1628  CD2 LEU A 215     3303   2360   2943   -443    813   -408       C  
ATOM   1629  N   HIS A 216      21.128   5.482  11.315  1.00 27.32           N  
ANISOU 1629  N   HIS A 216     4682   2191   3509   -790    865   -512       N  
ATOM   1630  CA  HIS A 216      20.673   5.088   9.982  1.00 30.70           C  
ANISOU 1630  CA  HIS A 216     5178   2601   3886   -881    850   -697       C  
ATOM   1631  C   HIS A 216      19.350   5.774   9.635  1.00 35.16           C  
ANISOU 1631  C   HIS A 216     5558   3441   4362  -1086    813   -720       C  
ATOM   1632  O   HIS A 216      18.535   6.067  10.515  1.00 32.09           O  
ANISOU 1632  O   HIS A 216     5049   3175   3971  -1227    807   -611       O  
ATOM   1633  CB  HIS A 216      20.565   3.574   9.844  1.00 31.60           C  
ANISOU 1633  CB  HIS A 216     5564   2371   4070   -996    818   -778       C  
ATOM   1634  CG  HIS A 216      19.590   2.954  10.788  1.00 37.53           C  
ANISOU 1634  CG  HIS A 216     6360   3029   4869  -1279    779   -640       C  
ATOM   1635  ND1 HIS A 216      18.227   3.118  10.664  1.00 36.87           N  
ANISOU 1635  ND1 HIS A 216     6153   3131   4725  -1566    745   -648       N  
ATOM   1636  CD2 HIS A 216      19.778   2.176  11.883  1.00 40.18           C  
ANISOU 1636  CD2 HIS A 216     6796   3173   5296  -1301    758   -448       C  
ATOM   1637  CE1 HIS A 216      17.618   2.464  11.637  1.00 39.79           C  
ANISOU 1637  CE1 HIS A 216     6529   3445   5143  -1746    719   -465       C  
ATOM   1638  NE2 HIS A 216      18.537   1.877  12.386  1.00 40.14           N  
ANISOU 1638  NE2 HIS A 216     6723   3254   5275  -1600    725   -336       N  
ATOM   1639  N   ILE A 217      19.146   6.048   8.351  1.00 33.50           N  
ANISOU 1639  N   ILE A 217     5307   3361   4059  -1085    790   -858       N  
ATOM   1640  CA  ILE A 217      17.921   6.697   7.916  1.00 31.14           C  
ANISOU 1640  CA  ILE A 217     4819   3332   3680  -1255    732   -872       C  
ATOM   1641  C   ILE A 217      17.359   6.035   6.665  1.00 32.52           C  
ANISOU 1641  C   ILE A 217     5090   3515   3751  -1403    663  -1063       C  
ATOM   1642  O   ILE A 217      18.089   5.380   5.903  1.00 34.09           O  
ANISOU 1642  O   ILE A 217     5477   3570   3906  -1301    677  -1215       O  
ATOM   1643  CB  ILE A 217      18.101   8.234   7.674  1.00 30.06           C  
ANISOU 1643  CB  ILE A 217     4437   3463   3522  -1088    733   -787       C  
ATOM   1644  CG1 ILE A 217      19.113   8.505   6.568  1.00 34.11           C  
ANISOU 1644  CG1 ILE A 217     4981   4011   3967   -894    762   -832       C  
ATOM   1645  CG2 ILE A 217      18.507   8.970   8.982  1.00 26.37           C  
ANISOU 1645  CG2 ILE A 217     3861   2998   3163   -966    768   -646       C  
ATOM   1646  CD1 ILE A 217      20.571   8.409   7.013  1.00 35.12           C  
ANISOU 1646  CD1 ILE A 217     5188   3975   4183   -667    844   -781       C  
ATOM   1647  N   SER A 218      16.054   6.198   6.467  1.00 33.39           N  
ANISOU 1647  N   SER A 218     5059   3813   3815  -1635    582  -1073       N  
ATOM   1648  CA  SER A 218      15.383   5.684   5.287  1.00 42.77           C  
ANISOU 1648  CA  SER A 218     6300   5066   4885  -1804    478  -1260       C  
ATOM   1649  C   SER A 218      14.125   6.509   5.037  1.00 42.69           C  
ANISOU 1649  C   SER A 218     6006   5401   4814  -1949    390  -1200       C  
ATOM   1650  O   SER A 218      13.591   7.126   5.959  1.00 38.60           O  
ANISOU 1650  O   SER A 218     5287   4999   4379  -1976    417  -1044       O  
ATOM   1651  CB  SER A 218      15.040   4.194   5.439  1.00 53.47           C  
ANISOU 1651  CB  SER A 218     7884   6110   6323  -2032    423  -1377       C  
ATOM   1652  OG  SER A 218      13.986   3.999   6.367  1.00 59.73           O  
ANISOU 1652  OG  SER A 218     8541   6936   7216  -2252    395  -1212       O  
ATOM   1653  N   GLY A 219      13.666   6.516   3.786  1.00 43.44           N  
ANISOU 1653  N   GLY A 219     6076   5678   4750  -2022    281  -1336       N  
ATOM   1654  CA  GLY A 219      12.493   7.275   3.376  1.00 43.69           C  
ANISOU 1654  CA  GLY A 219     5829   6055   4715  -2138    168  -1279       C  
ATOM   1655  C   GLY A 219      12.296   7.203   1.866  1.00 42.26           C  
ANISOU 1655  C   GLY A 219     5677   6074   4306  -2172     40  -1437       C  
ATOM   1656  O   GLY A 219      13.066   6.540   1.171  1.00 41.14           O  
ANISOU 1656  O   GLY A 219     5777   5807   4047  -2102     59  -1619       O  
ATOM   1657  N   ALA A 220      11.269   7.875   1.354  1.00 36.90           N  
ANISOU 1657  N   ALA A 220     4744   5728   3548  -2261    -92  -1377       N  
ATOM   1658  CA  ALA A 220      11.119   7.995  -0.085  1.00 44.29           C  
ANISOU 1658  CA  ALA A 220     5679   6927   4222  -2261   -224  -1481       C  
ATOM   1659  C   ALA A 220      12.402   8.568  -0.694  1.00 44.79           C  
ANISOU 1659  C   ALA A 220     5834   7037   4150  -1956   -119  -1422       C  
ATOM   1660  O   ALA A 220      12.780   8.178  -1.797  1.00 40.89           O  
ANISOU 1660  O   ALA A 220     5484   6650   3403  -1925   -152  -1589       O  
ATOM   1661  CB  ALA A 220       9.913   8.844  -0.449  1.00 42.91           C  
ANISOU 1661  CB  ALA A 220     5174   7123   4006  -2344   -385  -1351       C  
ATOM   1662  N   VAL A 221      13.094   9.459   0.016  1.00 40.25           N  
ANISOU 1662  N   VAL A 221     5170   6391   3731  -1738      8  -1200       N  
ATOM   1663  CA  VAL A 221      14.329  10.013  -0.559  1.00 43.16           C  
ANISOU 1663  CA  VAL A 221     5590   6816   3993  -1482    108  -1109       C  
ATOM   1664  C   VAL A 221      15.435   8.977  -0.758  1.00 44.26           C  
ANISOU 1664  C   VAL A 221     6019   6744   4053  -1398    232  -1319       C  
ATOM   1665  O   VAL A 221      16.359   9.202  -1.537  1.00 51.40           O  
ANISOU 1665  O   VAL A 221     6967   7777   4785  -1218    311  -1305       O  
ATOM   1666  CB  VAL A 221      14.893  11.242   0.206  1.00 40.83           C  
ANISOU 1666  CB  VAL A 221     5130   6471   3912  -1281    190   -829       C  
ATOM   1667  CG1 VAL A 221      13.968  12.444   0.055  1.00 44.21           C  
ANISOU 1667  CG1 VAL A 221     5269   7137   4392  -1282     56   -622       C  
ATOM   1668  CG2 VAL A 221      15.183  10.916   1.671  1.00 36.75           C  
ANISOU 1668  CG2 VAL A 221     4676   5638   3650  -1272    293   -840       C  
ATOM   1669  N   THR A 222      15.340   7.845  -0.068  1.00 40.70           N  
ANISOU 1669  N   THR A 222     5754   5978   3732  -1521    251  -1499       N  
ATOM   1670  CA  THR A 222      16.295   6.750  -0.263  1.00 42.66           C  
ANISOU 1670  CA  THR A 222     6290   5980   3941  -1429    341  -1730       C  
ATOM   1671  C   THR A 222      15.729   5.545  -1.020  1.00 44.16           C  
ANISOU 1671  C   THR A 222     6672   6105   4001  -1609    218  -2057       C  
ATOM   1672  O   THR A 222      16.328   4.465  -1.015  1.00 47.25           O  
ANISOU 1672  O   THR A 222     7282   6192   4478  -1509    251  -2219       O  
ATOM   1673  CB  THR A 222      16.880   6.250   1.080  1.00 39.28           C  
ANISOU 1673  CB  THR A 222     5975   5157   3793  -1380    448  -1677       C  
ATOM   1674  OG1 THR A 222      15.841   5.659   1.880  1.00 37.19           O  
ANISOU 1674  OG1 THR A 222     5723   4722   3687  -1654    362  -1688       O  
ATOM   1675  CG2 THR A 222      17.541   7.391   1.845  1.00 38.08           C  
ANISOU 1675  CG2 THR A 222     5644   5048   3776  -1186    549  -1390       C  
ATOM   1676  N   ASN A 223      14.585   5.724  -1.674  1.00 42.52           N  
ANISOU 1676  N   ASN A 223     6328   6155   3670  -1792     47  -2072       N  
ATOM   1677  CA  ASN A 223      13.903   4.614  -2.328  1.00 55.19           C  
ANISOU 1677  CA  ASN A 223     8049   7667   5253  -1924   -111  -2292       C  
ATOM   1678  C   ASN A 223      13.570   3.514  -1.322  1.00 53.94           C  
ANISOU 1678  C   ASN A 223     8014   7073   5408  -2080   -136  -2326       C  
ATOM   1679  O   ASN A 223      13.573   2.323  -1.646  1.00 53.72           O  
ANISOU 1679  O   ASN A 223     8181   6792   5438  -2100   -221  -2540       O  
ATOM   1680  CB  ASN A 223      14.747   4.073  -3.490  1.00 64.50           C  
ANISOU 1680  CB  ASN A 223     9419   8881   6208  -1701    -93  -2527       C  
ATOM   1681  CG  ASN A 223      15.335   5.188  -4.346  1.00 66.30           C  
ANISOU 1681  CG  ASN A 223     9522   9541   6129  -1507    -11  -2409       C  
ATOM   1682  OD1 ASN A 223      14.615   6.080  -4.801  1.00 64.16           O  
ANISOU 1682  OD1 ASN A 223     9039   9632   5704  -1601   -108  -2256       O  
ATOM   1683  ND2 ASN A 223      16.652   5.156  -4.545  1.00 68.33           N  
ANISOU 1683  ND2 ASN A 223     9882   9769   6313  -1227    165  -2439       N  
ATOM   1684  N   GLY A 224      13.294   3.940  -0.092  1.00 50.73           N  
ANISOU 1684  N   GLY A 224     7482   6594   5199  -2179    -69  -2102       N  
ATOM   1685  CA  GLY A 224      12.875   3.045   0.972  1.00 53.79           C  
ANISOU 1685  CA  GLY A 224     7933   6645   5862  -2344    -81  -2039       C  
ATOM   1686  C   GLY A 224      13.974   2.154   1.522  1.00 53.05           C  
ANISOU 1686  C   GLY A 224     8096   6134   5926  -2185     14  -2087       C  
ATOM   1687  O   GLY A 224      13.727   1.338   2.406  1.00 54.99           O  
ANISOU 1687  O   GLY A 224     8411   6087   6396  -2307     -5  -2006       O  
ATOM   1688  N   GLN A 225      15.186   2.303   1.000  1.00 48.85           N  
ANISOU 1688  N   GLN A 225     7684   5598   5278  -1900    111  -2194       N  
ATOM   1689  CA  GLN A 225      16.314   1.521   1.482  1.00 52.82           C  
ANISOU 1689  CA  GLN A 225     8395   5737   5938  -1694    197  -2231       C  
ATOM   1690  C   GLN A 225      16.987   2.262   2.629  1.00 50.57           C  
ANISOU 1690  C   GLN A 225     8042   5417   5754  -1585    359  -1984       C  
ATOM   1691  O   GLN A 225      17.160   3.482   2.576  1.00 49.59           O  
ANISOU 1691  O   GLN A 225     7762   5573   5507  -1521    443  -1887       O  
ATOM   1692  CB  GLN A 225      17.316   1.262   0.362  1.00 59.73           C  
ANISOU 1692  CB  GLN A 225     9397   6655   6643  -1405    228  -2472       C  
ATOM   1693  CG  GLN A 225      16.941   0.120  -0.564  1.00 69.42           C  
ANISOU 1693  CG  GLN A 225    10779   7759   7839  -1445     54  -2778       C  
ATOM   1694  CD  GLN A 225      18.162  -0.473  -1.232  1.00 80.53           C  
ANISOU 1694  CD  GLN A 225    12353   9067   9177  -1100    104  -3018       C  
ATOM   1695  OE1 GLN A 225      19.235   0.135  -1.234  1.00 82.22           O  
ANISOU 1695  OE1 GLN A 225    12522   9416   9303   -837    279  -2941       O  
ATOM   1696  NE2 GLN A 225      18.012  -1.667  -1.796  1.00 88.83           N  
ANISOU 1696  NE2 GLN A 225    13582   9889  10281  -1090    -58  -3317       N  
ATOM   1697  N   THR A 226      17.360   1.542   3.676  1.00 49.28           N  
ANISOU 1697  N   THR A 226     7991   4914   5818  -1563    385  -1877       N  
ATOM   1698  CA  THR A 226      17.953   2.224   4.817  1.00 51.32           C  
ANISOU 1698  CA  THR A 226     8184   5153   6162  -1463    515  -1644       C  
ATOM   1699  C   THR A 226      19.434   2.482   4.555  1.00 46.34           C  
ANISOU 1699  C   THR A 226     7609   4501   5496  -1111    637  -1686       C  
ATOM   1700  O   THR A 226      20.144   1.631   4.018  1.00 45.88           O  
ANISOU 1700  O   THR A 226     7693   4280   5460   -930    622  -1846       O  
ATOM   1701  CB  THR A 226      17.738   1.472   6.147  1.00 56.23           C  
ANISOU 1701  CB  THR A 226     8868   5496   7002  -1581    494  -1452       C  
ATOM   1702  OG1 THR A 226      18.764   0.493   6.315  1.00 67.02           O  
ANISOU 1702  OG1 THR A 226    10426   6531   8508  -1374    493  -1489       O  
ATOM   1703  CG2 THR A 226      16.375   0.793   6.165  1.00 51.54           C  
ANISOU 1703  CG2 THR A 226     8244   4875   6464  -1908    360  -1448       C  
ATOM   1704  N   VAL A 227      19.872   3.683   4.909  1.00 38.30           N  
ANISOU 1704  N   VAL A 227     6446   3670   4434  -1008    747  -1547       N  
ATOM   1705  CA  VAL A 227      21.248   4.097   4.734  1.00 36.39           C  
ANISOU 1705  CA  VAL A 227     6171   3478   4179   -679    862  -1513       C  
ATOM   1706  C   VAL A 227      21.894   4.135   6.110  1.00 34.32           C  
ANISOU 1706  C   VAL A 227     5898   3031   4112   -578    903  -1300       C  
ATOM   1707  O   VAL A 227      21.397   4.806   7.015  1.00 32.02           O  
ANISOU 1707  O   VAL A 227     5459   2834   3872   -684    880  -1106       O  
ATOM   1708  CB  VAL A 227      21.314   5.495   4.086  1.00 39.12           C  
ANISOU 1708  CB  VAL A 227     6258   4232   4374   -601    894  -1403       C  
ATOM   1709  CG1 VAL A 227      22.741   6.032   4.099  1.00 42.86           C  
ANISOU 1709  CG1 VAL A 227     6644   4765   4877   -303   1013  -1297       C  
ATOM   1710  CG2 VAL A 227      20.767   5.443   2.670  1.00 38.49           C  
ANISOU 1710  CG2 VAL A 227     6190   4382   4052   -676    848  -1595       C  
ATOM   1711  N   GLN A 228      22.990   3.402   6.269  1.00 35.94           N  
ANISOU 1711  N   GLN A 228     6227   3012   4417   -355    941  -1330       N  
ATOM   1712  CA  GLN A 228      23.688   3.324   7.548  1.00 37.90           C  
ANISOU 1712  CA  GLN A 228     6474   3092   4833   -243    953  -1127       C  
ATOM   1713  C   GLN A 228      24.869   4.283   7.535  1.00 39.06           C  
ANISOU 1713  C   GLN A 228     6452   3412   4975     20   1051  -1039       C  
ATOM   1714  O   GLN A 228      25.769   4.130   6.710  1.00 41.41           O  
ANISOU 1714  O   GLN A 228     6730   3772   5232    238   1110  -1140       O  
ATOM   1715  CB  GLN A 228      24.188   1.893   7.784  1.00 43.75           C  
ANISOU 1715  CB  GLN A 228     7384   3519   5721   -144    878  -1160       C  
ATOM   1716  CG  GLN A 228      24.906   1.718   9.124  1.00 43.07           C  
ANISOU 1716  CG  GLN A 228     7299   3279   5787    -33    864   -930       C  
ATOM   1717  CD  GLN A 228      24.001   2.024  10.305  1.00 39.06           C  
ANISOU 1717  CD  GLN A 228     6780   2774   5288   -280    839   -727       C  
ATOM   1718  OE1 GLN A 228      23.061   1.283  10.579  1.00 40.14           O  
ANISOU 1718  OE1 GLN A 228     7014   2778   5460   -518    767   -698       O  
ATOM   1719  NE2 GLN A 228      24.270   3.127  10.996  1.00 30.64           N  
ANISOU 1719  NE2 GLN A 228     5574   1876   4192   -229    895   -590       N  
ATOM   1720  N   THR A 229      24.865   5.282   8.421  1.00 35.64           N  
ANISOU 1720  N   THR A 229     5831   3126   4584     -3   1032   -829       N  
ATOM   1721  CA  THR A 229      25.999   6.205   8.504  1.00 35.61           C  
ANISOU 1721  CA  THR A 229     5630   3279   4621    212   1078   -714       C  
ATOM   1722  C   THR A 229      27.038   5.627   9.445  1.00 36.74           C  
ANISOU 1722  C   THR A 229     5836   3213   4909    394   1073   -626       C  
ATOM   1723  O   THR A 229      26.812   4.583  10.061  1.00 36.84           O  
ANISOU 1723  O   THR A 229     6049   2962   4987    347   1029   -624       O  
ATOM   1724  CB  THR A 229      25.602   7.588   9.039  1.00 33.40           C  
ANISOU 1724  CB  THR A 229     5123   3217   4352    123   1028   -562       C  
ATOM   1725  OG1 THR A 229      25.257   7.492  10.435  1.00 29.95           O  
ANISOU 1725  OG1 THR A 229     4714   2684   3980     41    964   -461       O  
ATOM   1726  CG2 THR A 229      24.426   8.152   8.254  1.00 33.67           C  
ANISOU 1726  CG2 THR A 229     5084   3443   4266    -59   1005   -615       C  
ATOM   1727  N   ASN A 230      28.181   6.298   9.551  1.00 30.21           N  
ANISOU 1727  N   ASN A 230     4827   2506   4145    591   1102   -529       N  
ATOM   1728  CA  ASN A 230      29.141   5.969  10.598  1.00 32.22           C  
ANISOU 1728  CA  ASN A 230     5083   2621   4536    755   1061   -408       C  
ATOM   1729  C   ASN A 230      29.180   7.122  11.606  1.00 33.22           C  
ANISOU 1729  C   ASN A 230     5018   2904   4699    694    976   -245       C  
ATOM   1730  O   ASN A 230      30.177   7.312  12.308  1.00 39.08           O  
ANISOU 1730  O   ASN A 230     5659   3649   5539    842    929   -137       O  
ATOM   1731  CB  ASN A 230      30.534   5.686  10.016  1.00 32.88           C  
ANISOU 1731  CB  ASN A 230     5056   2768   4668   1010   1096   -428       C  
ATOM   1732  CG  ASN A 230      30.560   4.460   9.102  1.00 38.30           C  
ANISOU 1732  CG  ASN A 230     5903   3336   5313   1080   1122   -624       C  
ATOM   1733  OD1 ASN A 230      30.061   3.395   9.462  1.00 39.85           O  
ANISOU 1733  OD1 ASN A 230     6305   3281   5553   1010   1044   -670       O  
ATOM   1734  ND2 ASN A 230      31.157   4.609   7.913  1.00 36.39           N  
ANISOU 1734  ND2 ASN A 230     5553   3283   4992   1219   1226   -738       N  
ATOM   1735  N   ASP A 231      28.092   7.893  11.666  1.00 27.19           N  
ANISOU 1735  N   ASP A 231     4268   3297   2764   1108    493   -333       N  
ATOM   1736  CA  ASP A 231      27.957   8.947  12.672  1.00 29.10           C  
ANISOU 1736  CA  ASP A 231     4286   3549   3221    782    502   -192       C  
ATOM   1737  C   ASP A 231      27.356   8.436  13.980  1.00 30.40           C  
ANISOU 1737  C   ASP A 231     4676   3396   3480    594    436   -253       C  
ATOM   1738  O   ASP A 231      26.179   8.082  14.033  1.00 28.07           O  
ANISOU 1738  O   ASP A 231     4570   2880   3217    397    387   -343       O  
ATOM   1739  CB  ASP A 231      27.090  10.105  12.156  1.00 29.48           C  
ANISOU 1739  CB  ASP A 231     4149   3657   3396    500    506   -159       C  
ATOM   1740  CG  ASP A 231      27.746  10.877  11.019  1.00 31.78           C  
ANISOU 1740  CG  ASP A 231     4131   4321   3623    593    544     -5       C  
ATOM   1741  OD1 ASP A 231      28.990  10.973  10.986  1.00 34.26           O  
ANISOU 1741  OD1 ASP A 231     4235   4933   3851    786    571    170       O  
ATOM   1742  OD2 ASP A 231      27.011  11.384  10.158  1.00 30.38           O  
ANISOU 1742  OD2 ASP A 231     3896   4175   3473    458    538    -24       O  
ATOM   1743  N   LEU A 232      28.168   8.416  15.033  1.00 32.14           N  
ANISOU 1743  N   LEU A 232     4844   3636   3730    636    425   -162       N  
ATOM   1744  CA  LEU A 232      27.680   8.192  16.393  1.00 31.07           C  
ANISOU 1744  CA  LEU A 232     4835   3299   3669    431    374   -169       C  
ATOM   1745  C   LEU A 232      26.756   9.345  16.820  1.00 28.04           C  
ANISOU 1745  C   LEU A 232     4293   2953   3408    145    383   -165       C  
ATOM   1746  O   LEU A 232      27.150  10.518  16.790  1.00 25.67           O  
ANISOU 1746  O   LEU A 232     3755   2807   3191    114    370    -92       O  
ATOM   1747  CB  LEU A 232      28.878   8.136  17.339  1.00 32.58           C  
ANISOU 1747  CB  LEU A 232     4959   3556   3863    552    356    -56       C  
ATOM   1748  CG  LEU A 232      28.853   7.291  18.596  1.00 42.60           C  
ANISOU 1748  CG  LEU A 232     6439   4625   5122    495    287    -54       C  
ATOM   1749  CD1 LEU A 232      28.756   5.811  18.240  1.00 46.62           C  
ANISOU 1749  CD1 LEU A 232     7286   4897   5532    650    193   -141       C  
ATOM   1750  CD2 LEU A 232      30.116   7.575  19.408  1.00 43.32           C  
ANISOU 1750  CD2 LEU A 232     6387   4838   5235    599    273     82       C  
ATOM   1751  N   VAL A 233      25.539   9.016  17.248  1.00 22.55           N  
ANISOU 1751  N   VAL A 233     3727   2130   2711    -54    369   -224       N  
ATOM   1752  CA  VAL A 233      24.558  10.037  17.595  1.00 23.60           C  
ANISOU 1752  CA  VAL A 233     3709   2348   2911   -243    384   -253       C  
ATOM   1753  C   VAL A 233      23.800   9.673  18.868  1.00 29.24           C  
ANISOU 1753  C   VAL A 233     4487   3058   3565   -389    379   -237       C  
ATOM   1754  O   VAL A 233      23.797   8.535  19.297  1.00 29.32           O  
ANISOU 1754  O   VAL A 233     4678   2956   3505   -430    341   -177       O  
ATOM   1755  CB  VAL A 233      23.522  10.267  16.451  1.00 30.23           C  
ANISOU 1755  CB  VAL A 233     4521   3189   3774   -342    403   -310       C  
ATOM   1756  CG1 VAL A 233      24.246  10.609  15.119  1.00 23.05           C  
ANISOU 1756  CG1 VAL A 233     3525   2352   2881   -198    413   -300       C  
ATOM   1757  CG2 VAL A 233      22.621   9.045  16.260  1.00 27.00           C  
ANISOU 1757  CG2 VAL A 233     4339   2627   3292   -464    366   -309       C  
ATOM   1758  N   GLU A 234      23.140  10.651  19.458  1.00 25.31           N  
ANISOU 1758  N   GLU A 234     3836   2706   3075   -451    392   -281       N  
ATOM   1759  CA  GLU A 234      22.145  10.357  20.468  1.00 31.62           C  
ANISOU 1759  CA  GLU A 234     4627   3631   3757   -577    419   -250       C  
ATOM   1760  C   GLU A 234      20.831  10.907  19.974  1.00 30.12           C  
ANISOU 1760  C   GLU A 234     4301   3578   3564   -667    457   -296       C  
ATOM   1761  O   GLU A 234      20.715  12.105  19.720  1.00 27.86           O  
ANISOU 1761  O   GLU A 234     3882   3356   3347   -572    439   -411       O  
ATOM   1762  CB  GLU A 234      22.523  11.003  21.797  1.00 35.83           C  
ANISOU 1762  CB  GLU A 234     5093   4296   4225   -480    400   -286       C  
ATOM   1763  CG  GLU A 234      23.544  10.214  22.582  1.00 50.25           C  
ANISOU 1763  CG  GLU A 234     7049   6030   6012   -452    366   -192       C  
ATOM   1764  CD  GLU A 234      22.922   9.056  23.354  1.00 63.14           C  
ANISOU 1764  CD  GLU A 234     8766   7724   7502   -619    378    -51       C  
ATOM   1765  OE1 GLU A 234      21.676   8.910  23.327  1.00 65.65           O  
ANISOU 1765  OE1 GLU A 234     9003   8207   7734   -771    418      4       O  
ATOM   1766  OE2 GLU A 234      23.682   8.292  23.990  1.00 69.27           O  
ANISOU 1766  OE2 GLU A 234     9670   8400   8250   -618    325     43       O  
ATOM   1767  N   ILE A 235      19.845  10.032  19.812  1.00 27.16           N  
ANISOU 1767  N   ILE A 235     3965   3232   3120   -862    467   -183       N  
ATOM   1768  CA  ILE A 235      18.513  10.468  19.402  1.00 25.74           C  
ANISOU 1768  CA  ILE A 235     3623   3234   2923   -967    505   -180       C  
ATOM   1769  C   ILE A 235      17.703  11.011  20.593  1.00 28.61           C  
ANISOU 1769  C   ILE A 235     3770   3981   3119   -927    573   -171       C  
ATOM   1770  O   ILE A 235      17.760  10.463  21.687  1.00 29.62           O  
ANISOU 1770  O   ILE A 235     3900   4254   3098   -967    588    -57       O  
ATOM   1771  CB  ILE A 235      17.765   9.347  18.628  1.00 43.06           C  
ANISOU 1771  CB  ILE A 235     5938   5307   5116  -1221    437    -22       C  
ATOM   1772  CG1 ILE A 235      18.459   9.117  17.273  1.00 45.19           C  
ANISOU 1772  CG1 ILE A 235     6401   5263   5507  -1147    375   -116       C  
ATOM   1773  CG2 ILE A 235      16.297   9.702  18.410  1.00 39.40           C  
ANISOU 1773  CG2 ILE A 235     5258   5103   4608  -1372    472     54       C  
ATOM   1774  CD1 ILE A 235      17.931   7.962  16.479  1.00 50.65           C  
ANISOU 1774  CD1 ILE A 235     7317   5738   6190  -1338    232    -12       C  
ATOM   1775  N   HIS A 236      16.975  12.100  20.369  1.00 28.51           N  
ANISOU 1775  N   HIS A 236     3571   4153   3109   -812    602   -297       N  
ATOM   1776  CA  HIS A 236      16.096  12.683  21.390  1.00 32.00           C  
ANISOU 1776  CA  HIS A 236     3790   5029   3341   -675    668   -330       C  
ATOM   1777  C   HIS A 236      14.754  13.021  20.744  1.00 31.82           C  
ANISOU 1777  C   HIS A 236     3557   5235   3300   -729    709   -299       C  
ATOM   1778  O   HIS A 236      14.613  14.059  20.076  1.00 32.74           O  
ANISOU 1778  O   HIS A 236     3629   5272   3539   -575    659   -487       O  
ATOM   1779  CB  HIS A 236      16.699  13.979  21.936  1.00 28.36           C  
ANISOU 1779  CB  HIS A 236     3337   4554   2885   -335    592   -601       C  
ATOM   1780  CG  HIS A 236      18.014  13.801  22.619  1.00 33.49           C  
ANISOU 1780  CG  HIS A 236     4164   5008   3553   -275    529   -621       C  
ATOM   1781  ND1 HIS A 236      19.221  14.064  22.001  1.00 38.12           N  
ANISOU 1781  ND1 HIS A 236     4898   5227   4359   -264    417   -668       N  
ATOM   1782  CD2 HIS A 236      18.318  13.395  23.871  1.00 33.22           C  
ANISOU 1782  CD2 HIS A 236     4155   5134   3331   -229    555   -570       C  
ATOM   1783  CE1 HIS A 236      20.207  13.823  22.844  1.00 30.20           C  
ANISOU 1783  CE1 HIS A 236     4004   4153   3318   -213    375   -645       C  
ATOM   1784  NE2 HIS A 236      19.685  13.407  23.985  1.00 33.95           N  
ANISOU 1784  NE2 HIS A 236     4428   4918   3554   -194    454   -599       N  
ATOM   1785  N   GLY A 237      13.772  12.149  20.902  1.00 28.11           N  
ANISOU 1785  N   GLY A 237     2951   5042   2690   -976    765    -25       N  
ATOM   1786  CA  GLY A 237      12.525  12.337  20.182  1.00 30.60           C  
ANISOU 1786  CA  GLY A 237     3058   5562   3006  -1081    788     65       C  
ATOM   1787  C   GLY A 237      12.837  12.407  18.690  1.00 28.20           C  
ANISOU 1787  C   GLY A 237     2940   4797   2978  -1187    697    -20       C  
ATOM   1788  O   GLY A 237      13.686  11.665  18.197  1.00 32.83           O  
ANISOU 1788  O   GLY A 237     3795   4994   3685  -1319    624      9       O  
ATOM   1789  N   ASN A 238      12.187  13.312  17.966  1.00 30.20           N  
ANISOU 1789  N   ASN A 238     3052   5111   3310  -1094    693   -136       N  
ATOM   1790  CA  ASN A 238      12.387  13.400  16.520  1.00 32.82           C  
ANISOU 1790  CA  ASN A 238     3527   5074   3871  -1208    610   -188       C  
ATOM   1791  C   ASN A 238      13.588  14.243  16.068  1.00 31.68           C  
ANISOU 1791  C   ASN A 238     3530   4606   3900  -1007    540   -426       C  
ATOM   1792  O   ASN A 238      13.497  14.998  15.100  1.00 28.64           O  
ANISOU 1792  O   ASN A 238     3118   4100   3663   -979    473   -518       O  
ATOM   1793  CB  ASN A 238      11.118  13.922  15.849  1.00 38.71           C  
ANISOU 1793  CB  ASN A 238     4058   6011   4640  -1241    603   -151       C  
ATOM   1794  CG  ASN A 238      10.944  15.414  16.030  1.00 41.75           C  
ANISOU 1794  CG  ASN A 238     4275   6546   5044   -902    595   -410       C  
ATOM   1795  OD1 ASN A 238      11.379  15.989  17.036  1.00 35.95           O  
ANISOU 1795  OD1 ASN A 238     3530   5918   4211   -612    596   -576       O  
ATOM   1796  ND2 ASN A 238      10.316  16.056  15.047  1.00 44.49           N  
ANISOU 1796  ND2 ASN A 238     4531   6855   5520   -913    535   -456       N  
ATOM   1797  N   ALA A 239      14.710  14.100  16.763  1.00 30.19           N  
ANISOU 1797  N   ALA A 239     3478   4301   3692   -898    533   -478       N  
ATOM   1798  CA  ALA A 239      15.901  14.898  16.501  1.00 28.35           C  
ANISOU 1798  CA  ALA A 239     3339   3829   3604   -738    436   -626       C  
ATOM   1799  C   ALA A 239      17.115  14.142  17.012  1.00 28.00           C  
ANISOU 1799  C   ALA A 239     3468   3640   3531   -734    448   -573       C  
ATOM   1800  O   ALA A 239      16.982  13.182  17.767  1.00 28.82           O  
ANISOU 1800  O   ALA A 239     3622   3828   3500   -814    512   -464       O  
ATOM   1801  CB  ALA A 239      15.802  16.283  17.205  1.00 27.40           C  
ANISOU 1801  CB  ALA A 239     3113   3820   3477   -465    334   -821       C  
ATOM   1802  N   PHE A 240      18.307  14.563  16.616  1.00 24.32           N  
ANISOU 1802  N   PHE A 240     3072   2983   3186   -653    366   -611       N  
ATOM   1803  CA  PHE A 240      19.491  13.901  17.139  1.00 23.21           C  
ANISOU 1803  CA  PHE A 240     3063   2742   3012   -613    375   -554       C  
ATOM   1804  C   PHE A 240      20.616  14.862  17.390  1.00 28.29           C  
ANISOU 1804  C   PHE A 240     3682   3316   3749   -478    244   -592       C  
ATOM   1805  O   PHE A 240      20.674  15.952  16.824  1.00 28.07           O  
ANISOU 1805  O   PHE A 240     3569   3249   3849   -454    110   -629       O  
ATOM   1806  CB  PHE A 240      19.969  12.768  16.213  1.00 21.97           C  
ANISOU 1806  CB  PHE A 240     3056   2434   2857   -690    414   -461       C  
ATOM   1807  CG  PHE A 240      20.667  13.254  14.948  1.00 25.24           C  
ANISOU 1807  CG  PHE A 240     3432   2786   3374   -640    371   -456       C  
ATOM   1808  CD1 PHE A 240      22.041  13.419  14.912  1.00 23.58           C  
ANISOU 1808  CD1 PHE A 240     3206   2565   3190   -518    334   -398       C  
ATOM   1809  CD2 PHE A 240      19.936  13.509  13.794  1.00 22.80           C  
ANISOU 1809  CD2 PHE A 240     3072   2478   3112   -727    364   -468       C  
ATOM   1810  CE1 PHE A 240      22.683  13.845  13.735  1.00 24.47           C  
ANISOU 1810  CE1 PHE A 240     3219   2729   3350   -482    301   -327       C  
ATOM   1811  CE2 PHE A 240      20.566  13.928  12.611  1.00 22.94           C  
ANISOU 1811  CE2 PHE A 240     3027   2503   3184   -691    328   -428       C  
ATOM   1812  CZ  PHE A 240      21.929  14.099  12.580  1.00 20.90           C  
ANISOU 1812  CZ  PHE A 240     2720   2293   2928   -569    301   -345       C  
ATOM   1813  N   GLN A 241      21.516  14.438  18.263  1.00 23.11           N  
ANISOU 1813  N   GLN A 241     3108   2633   3038   -418    243   -550       N  
ATOM   1814  CA  GLN A 241      22.728  15.168  18.502  1.00 21.67           C  
ANISOU 1814  CA  GLN A 241     2911   2377   2945   -334     90   -518       C  
ATOM   1815  C   GLN A 241      23.874  14.328  17.967  1.00 24.19           C  
ANISOU 1815  C   GLN A 241     3268   2651   3271   -333    149   -368       C  
ATOM   1816  O   GLN A 241      23.964  13.119  18.243  1.00 24.12           O  
ANISOU 1816  O   GLN A 241     3383   2622   3161   -327    263   -339       O  
ATOM   1817  CB  GLN A 241      22.935  15.376  20.000  1.00 28.30           C  
ANISOU 1817  CB  GLN A 241     3809   3250   3694   -232     23   -583       C  
ATOM   1818  CG  GLN A 241      24.276  15.981  20.304  1.00 35.87           C  
ANISOU 1818  CG  GLN A 241     4777   4103   4748   -187   -176   -503       C  
ATOM   1819  CD  GLN A 241      24.491  16.212  21.793  1.00 44.95           C  
ANISOU 1819  CD  GLN A 241     6021   5264   5795    -77   -277   -585       C  
ATOM   1820  OE1 GLN A 241      23.776  15.656  22.638  1.00 47.44           O  
ANISOU 1820  OE1 GLN A 241     6378   5718   5928    -30   -139   -667       O  
ATOM   1821  NE2 GLN A 241      25.485  17.029  22.119  1.00 46.43           N  
ANISOU 1821  NE2 GLN A 241     6233   5327   6081    -51   -544   -531       N  
ATOM   1822  N   TRP A 242      24.755  14.956  17.207  1.00 23.74           N  
ANISOU 1822  N   TRP A 242     3098   2604   3318   -326     45   -254       N  
ATOM   1823  CA  TRP A 242      25.927  14.249  16.708  1.00 25.18           C  
ANISOU 1823  CA  TRP A 242     3259   2848   3460   -250    106   -100       C  
ATOM   1824  C   TRP A 242      26.967  14.185  17.828  1.00 24.48           C  
ANISOU 1824  C   TRP A 242     3190   2750   3362   -187     33    -16       C  
ATOM   1825  O   TRP A 242      27.281  15.200  18.435  1.00 22.50           O  
ANISOU 1825  O   TRP A 242     2883   2466   3199   -229   -165     20       O  
ATOM   1826  CB  TRP A 242      26.502  14.985  15.500  1.00 27.51           C  
ANISOU 1826  CB  TRP A 242     3350   3274   3830   -277     25     63       C  
ATOM   1827  CG  TRP A 242      27.728  14.337  14.873  1.00 26.09           C  
ANISOU 1827  CG  TRP A 242     3076   3289   3550   -133    107    242       C  
ATOM   1828  CD1 TRP A 242      27.737  13.384  13.890  1.00 28.22           C  
ANISOU 1828  CD1 TRP A 242     3396   3655   3673     16    267    208       C  
ATOM   1829  CD2 TRP A 242      29.108  14.607  15.178  1.00 26.85           C  
ANISOU 1829  CD2 TRP A 242     3003   3544   3657    -85     11    484       C  
ATOM   1830  NE1 TRP A 242      29.031  13.053  13.564  1.00 28.26           N  
ANISOU 1830  NE1 TRP A 242     3260   3910   3568    210    303    388       N  
ATOM   1831  CE2 TRP A 242      29.889  13.781  14.341  1.00 26.79           C  
ANISOU 1831  CE2 TRP A 242     2910   3787   3483    129    160    588       C  
ATOM   1832  CE3 TRP A 242      29.755  15.471  16.066  1.00 24.94           C  
ANISOU 1832  CE3 TRP A 242     2679   3263   3533   -191   -214    630       C  
ATOM   1833  CZ2 TRP A 242      31.280  13.797  14.368  1.00 29.26           C  
ANISOU 1833  CZ2 TRP A 242     2998   4381   3739    241    130    862       C  
ATOM   1834  CZ3 TRP A 242      31.146  15.488  16.086  1.00 29.81           C  
ANISOU 1834  CZ3 TRP A 242     3094   4106   4127   -144   -279    929       C  
ATOM   1835  CH2 TRP A 242      31.891  14.661  15.240  1.00 30.77           C  
ANISOU 1835  CH2 TRP A 242     3073   4543   4076     71    -88   1058       C  
ATOM   1836  N   ILE A 243      27.497  12.992  18.074  1.00 22.96           N  
ANISOU 1836  N   ILE A 243     3103   2556   3064    -81    150     13       N  
ATOM   1837  CA  ILE A 243      28.447  12.753  19.162  1.00 28.54           C  
ANISOU 1837  CA  ILE A 243     3843   3251   3752    -21     96     97       C  
ATOM   1838  C   ILE A 243      29.870  12.596  18.630  1.00 31.14           C  
ANISOU 1838  C   ILE A 243     4019   3742   4072    109     85    313       C  
ATOM   1839  O   ILE A 243      30.807  13.129  19.216  1.00 31.06           O  
ANISOU 1839  O   ILE A 243     3898   3785   4117     90    -54    478       O  
ATOM   1840  CB  ILE A 243      28.105  11.467  19.922  1.00 23.47           C  
ANISOU 1840  CB  ILE A 243     3420   2502   2994     11    198     15       C  
ATOM   1841  CG1 ILE A 243      26.718  11.570  20.576  1.00 30.60           C  
ANISOU 1841  CG1 ILE A 243     4405   3365   3857   -124    220   -125       C  
ATOM   1842  CG2 ILE A 243      29.182  11.139  20.953  1.00 29.16           C  
ANISOU 1842  CG2 ILE A 243     4171   3214   3693     83    141    120       C  
ATOM   1843  CD1 ILE A 243      26.514  12.847  21.377  1.00 32.58           C  
ANISOU 1843  CD1 ILE A 243     4576   3657   4146   -149     95   -188       C  
ATOM   1844  N   GLY A 244      30.030  11.848  17.532  1.00 26.88           N  
ANISOU 1844  N   GLY A 244     3471   3308   3436    262    214    319       N  
ATOM   1845  CA  GLY A 244      31.354  11.563  16.995  1.00 25.26           C  
ANISOU 1845  CA  GLY A 244     3089   3362   3148    474    242    517       C  
ATOM   1846  C   GLY A 244      31.420  10.361  16.046  1.00 29.79           C  
ANISOU 1846  C   GLY A 244     3782   4002   3537    766    384    414       C  
ATOM   1847  O   GLY A 244      30.455  10.067  15.341  1.00 30.10           O  
ANISOU 1847  O   GLY A 244     3968   3929   3538    747    433    243       O  
ATOM   1848  N   ARG A 245      32.568   9.686  16.020  1.00 28.32           N  
ANISOU 1848  N   ARG A 245     3539   3999   3223   1061    419    514       N  
ATOM   1849  CA  ARG A 245      32.747   8.446  15.256  1.00 35.06           C  
ANISOU 1849  CA  ARG A 245     4572   4884   3865   1446    497    367       C  
ATOM   1850  C   ARG A 245      32.880   7.247  16.186  1.00 40.16           C  
ANISOU 1850  C   ARG A 245     5544   5231   4483   1582    439    242       C  
ATOM   1851  O   ARG A 245      33.624   7.290  17.176  1.00 45.66           O  
ANISOU 1851  O   ARG A 245     6166   5946   5238   1565    398    378       O  
ATOM   1852  CB  ARG A 245      33.983   8.551  14.363  1.00 42.11           C  
ANISOU 1852  CB  ARG A 245     5128   6301   4571   1783    574    572       C  
ATOM   1853  CG  ARG A 245      33.909   9.695  13.413  1.00 41.62           C  
ANISOU 1853  CG  ARG A 245     4721   6570   4522   1618    597    761       C  
ATOM   1854  CD  ARG A 245      33.022   9.363  12.214  1.00 47.88           C  
ANISOU 1854  CD  ARG A 245     5676   7330   5187   1721    666    537       C  
ATOM   1855  NE  ARG A 245      33.569   8.261  11.434  1.00 51.46           N  
ANISOU 1855  NE  ARG A 245     6231   7993   5328   2260    746    407       N  
ATOM   1856  CZ  ARG A 245      33.335   8.076  10.140  1.00 51.63           C  
ANISOU 1856  CZ  ARG A 245     6277   8186   5153   2420    766    316       C  
ATOM   1857  NH1 ARG A 245      32.565   8.931   9.477  1.00 43.72           N  
ANISOU 1857  NH1 ARG A 245     5143   7248   4222   2162    801    356       N  
ATOM   1858  NH2 ARG A 245      33.876   7.042   9.509  1.00 56.53           N  
ANISOU 1858  NH2 ARG A 245     7065   8896   5516   2804    704    196       N  
ATOM   1859  N   ALA A 246      32.156   6.175  15.872  1.00 47.28           N  
ANISOU 1859  N   ALA A 246     6822   5836   5305   1691    390      5       N  
ATOM   1860  CA  ALA A 246      31.919   5.085  16.833  1.00 53.04           C  
ANISOU 1860  CA  ALA A 246     7916   6177   6060   1672    256    -92       C  
ATOM   1861  C   ALA A 246      33.161   4.569  17.578  1.00 50.60           C  
ANISOU 1861  C   ALA A 246     7587   5928   5710   1927    216      6       C  
ATOM   1862  O   ALA A 246      33.146   4.391  18.811  1.00 48.80           O  
ANISOU 1862  O   ALA A 246     7450   5506   5586   1726    140     68       O  
ATOM   1863  CB  ALA A 246      31.195   3.933  16.152  1.00 59.47           C  
ANISOU 1863  CB  ALA A 246     9149   6675   6770   1812    121   -317       C  
ATOM   1864  N   ASP A 247      34.229   4.332  16.826  1.00 40.29           N  
ANISOU 1864  N   ASP A 247     6140   4941   4230   2386    270     32       N  
ATOM   1865  CA  ASP A 247      35.424   3.712  17.373  1.00 43.79           C  
ANISOU 1865  CA  ASP A 247     6565   5474   4600   2718    225    110       C  
ATOM   1866  C   ASP A 247      36.318   4.721  18.070  1.00 35.54           C  
ANISOU 1866  C   ASP A 247     5090   4757   3658   2549    299    427       C  
ATOM   1867  O   ASP A 247      37.376   4.367  18.583  1.00 35.98           O  
ANISOU 1867  O   ASP A 247     5054   4946   3672   2778    270    554       O  
ATOM   1868  CB  ASP A 247      36.211   3.011  16.264  1.00 56.05           C  
ANISOU 1868  CB  ASP A 247     8095   7332   5871   3162    230     14       C  
ATOM   1869  CG  ASP A 247      35.445   1.857  15.647  1.00 70.86           C  
ANISOU 1869  CG  ASP A 247    10431   8853   7640   3237     42   -281       C  
ATOM   1870  OD1 ASP A 247      35.634   0.707  16.102  1.00 77.32           O  
ANISOU 1870  OD1 ASP A 247    11562   9393   8424   3348   -160   -396       O  
ATOM   1871  OD2 ASP A 247      34.653   2.099  14.710  1.00 76.69           O  
ANISOU 1871  OD2 ASP A 247    11208   9590   8339   3161     61   -375       O  
ATOM   1872  N   ASN A 248      35.900   5.980  18.091  1.00 30.61           N  
ANISOU 1872  N   ASN A 248     4218   4240   3172   2152    348    560       N  
ATOM   1873  CA  ASN A 248      36.723   7.014  18.712  1.00 31.83           C  
ANISOU 1873  CA  ASN A 248     4005   4652   3437   1956    327    876       C  
ATOM   1874  C   ASN A 248      36.158   7.529  20.050  1.00 33.51           C  
ANISOU 1874  C   ASN A 248     4342   4537   3851   1522    218    875       C  
ATOM   1875  O   ASN A 248      36.759   8.400  20.696  1.00 30.08           O  
ANISOU 1875  O   ASN A 248     3686   4221   3522   1334    129   1106       O  
ATOM   1876  CB  ASN A 248      36.925   8.179  17.729  1.00 32.83           C  
ANISOU 1876  CB  ASN A 248     3725   5195   3555   1865    378   1090       C  
ATOM   1877  CG  ASN A 248      37.952   9.183  18.221  1.00 36.92           C  
ANISOU 1877  CG  ASN A 248     3849   6007   4172   1680    275   1490       C  
ATOM   1878  OD1 ASN A 248      38.912   8.825  18.910  1.00 36.54           O  
ANISOU 1878  OD1 ASN A 248     3727   6052   4106   1811    232   1646       O  
ATOM   1879  ND2 ASN A 248      37.746  10.451  17.884  1.00 36.70           N  
ANISOU 1879  ND2 ASN A 248     3585   6098   4263   1355    186   1675       N  
ATOM   1880  N   VAL A 249      35.002   6.999  20.453  1.00 32.81           N  
ANISOU 1880  N   VAL A 249     4604   4069   3794   1372    200    635       N  
ATOM   1881  CA  VAL A 249      34.333   7.452  21.672  1.00 29.55           C  
ANISOU 1881  CA  VAL A 249     4294   3436   3500   1018    125    613       C  
ATOM   1882  C   VAL A 249      33.997   6.240  22.533  1.00 31.62           C  
ANISOU 1882  C   VAL A 249     4889   3402   3724   1017     68    511       C  
ATOM   1883  O   VAL A 249      33.478   5.234  22.035  1.00 31.65           O  
ANISOU 1883  O   VAL A 249     5144   3223   3659   1127     54    369       O  
ATOM   1884  CB  VAL A 249      33.046   8.248  21.377  1.00 27.13           C  
ANISOU 1884  CB  VAL A 249     3994   3060   3254    754    151    488       C  
ATOM   1885  CG1 VAL A 249      32.490   8.833  22.663  1.00 28.01           C  
ANISOU 1885  CG1 VAL A 249     4162   3052   3428    487     74    464       C  
ATOM   1886  CG2 VAL A 249      33.313   9.390  20.378  1.00 30.29           C  
ANISOU 1886  CG2 VAL A 249     4090   3717   3701    737    162    602       C  
ATOM   1887  N   ILE A 250      34.329   6.307  23.816  1.00 24.57           N  
ANISOU 1887  N   ILE A 250     4015   2450   2869    887    -10    606       N  
ATOM   1888  CA  ILE A 250      33.970   5.220  24.712  1.00 25.35           C  
ANISOU 1888  CA  ILE A 250     4405   2296   2931    821    -92    564       C  
ATOM   1889  C   ILE A 250      33.033   5.744  25.792  1.00 30.91           C  
ANISOU 1889  C   ILE A 250     5140   2963   3640    483   -106    549       C  
ATOM   1890  O   ILE A 250      32.924   6.956  25.996  1.00 27.18           O  
ANISOU 1890  O   ILE A 250     4492   2630   3206    371    -88    552       O  
ATOM   1891  CB  ILE A 250      35.200   4.573  25.382  1.00 28.69           C  
ANISOU 1891  CB  ILE A 250     4851   2704   3344   1007   -182    698       C  
ATOM   1892  CG1 ILE A 250      35.893   5.580  26.304  1.00 27.96           C  
ANISOU 1892  CG1 ILE A 250     4540   2772   3313    870   -217    866       C  
ATOM   1893  CG2 ILE A 250      36.174   4.028  24.328  1.00 29.10           C  
ANISOU 1893  CG2 ILE A 250     4842   2881   3335   1441   -159    704       C  
ATOM   1894  CD1 ILE A 250      36.972   4.960  27.142  1.00 28.16           C  
ANISOU 1894  CD1 ILE A 250     4595   2770   3336    987   -318   1015       C  
ATOM   1895  N   ASN A 251      32.366   4.824  26.478  1.00 26.64           N  
ANISOU 1895  N   ASN A 251     4824   2255   3041    340   -171    546       N  
ATOM   1896  CA  ASN A 251      31.487   5.199  27.575  1.00 31.26           C  
ANISOU 1896  CA  ASN A 251     5404   2912   3559     65   -167    561       C  
ATOM   1897  C   ASN A 251      31.954   4.511  28.839  1.00 30.75           C  
ANISOU 1897  C   ASN A 251     5454   2787   3443      0   -279    698       C  
ATOM   1898  O   ASN A 251      31.799   3.300  28.993  1.00 27.52           O  
ANISOU 1898  O   ASN A 251     5253   2193   3011    -50   -391    771       O  
ATOM   1899  CB  ASN A 251      30.032   4.846  27.266  1.00 33.89           C  
ANISOU 1899  CB  ASN A 251     5821   3221   3833   -131   -139    512       C  
ATOM   1900  CG  ASN A 251      29.078   5.346  28.335  1.00 37.87           C  
ANISOU 1900  CG  ASN A 251     6239   3941   4211   -356    -97    538       C  
ATOM   1901  OD1 ASN A 251      29.511   5.825  29.373  1.00 36.88           O  
ANISOU 1901  OD1 ASN A 251     6053   3934   4024   -350   -114    567       O  
ATOM   1902  ND2 ASN A 251      27.781   5.225  28.091  1.00 41.87           N  
ANISOU 1902  ND2 ASN A 251     6730   4531   4647   -532    -54    536       N  
ATOM   1903  N   SER A 252      32.552   5.294  29.728  1.00 25.62           N  
ANISOU 1903  N   SER A 252     4689   2266   2781     -7   -295    742       N  
ATOM   1904  CA  SER A 252      33.102   4.792  30.985  1.00 28.63           C  
ANISOU 1904  CA  SER A 252     5154   2620   3106    -67   -404    879       C  
ATOM   1905  C   SER A 252      32.276   5.352  32.138  1.00 29.40           C  
ANISOU 1905  C   SER A 252     5219   2918   3036   -260   -387    865       C  
ATOM   1906  O   SER A 252      32.304   6.562  32.382  1.00 28.53           O  
ANISOU 1906  O   SER A 252     4995   2944   2900   -221   -378    766       O  
ATOM   1907  CB  SER A 252      34.562   5.241  31.138  1.00 27.03           C  
ANISOU 1907  CB  SER A 252     4844   2432   2995    101   -471    965       C  
ATOM   1908  OG  SER A 252      35.107   4.855  32.400  1.00 29.67           O  
ANISOU 1908  OG  SER A 252     5254   2743   3276     34   -586   1098       O  
ATOM   1909  N   GLY A 253      31.533   4.486  32.818  1.00 30.27           N  
ANISOU 1909  N   GLY A 253     5428   3063   3012   -454   -415    972       N  
ATOM   1910  CA  GLY A 253      30.665   4.909  33.905  1.00 37.02           C  
ANISOU 1910  CA  GLY A 253     6210   4224   3632   -601   -372    984       C  
ATOM   1911  C   GLY A 253      29.697   6.023  33.516  1.00 35.34           C  
ANISOU 1911  C   GLY A 253     5849   4236   3342   -553   -240    789       C  
ATOM   1912  O   GLY A 253      29.447   6.930  34.315  1.00 33.39           O  
ANISOU 1912  O   GLY A 253     5530   4234   2922   -487   -227    686       O  
ATOM   1913  N   GLY A 254      29.142   5.949  32.304  1.00 30.33           N  
ANISOU 1913  N   GLY A 254     5192   3512   2819   -556   -169    724       N  
ATOM   1914  CA  GLY A 254      28.247   6.976  31.793  1.00 26.52           C  
ANISOU 1914  CA  GLY A 254     4571   3207   2297   -500    -60    544       C  
ATOM   1915  C   GLY A 254      28.926   8.272  31.350  1.00 32.05           C  
ANISOU 1915  C   GLY A 254     5214   3831   3130   -300    -98    364       C  
ATOM   1916  O   GLY A 254      28.266   9.216  30.908  1.00 30.71           O  
ANISOU 1916  O   GLY A 254     4953   3760   2953   -234    -60    202       O  
ATOM   1917  N   VAL A 255      30.246   8.343  31.471  1.00 31.44           N  
ANISOU 1917  N   VAL A 255     4628   2408   4909    117   1031   -192       N  
ATOM   1918  CA  VAL A 255      30.968   9.512  30.972  1.00 22.52           C  
ANISOU 1918  CA  VAL A 255     3396   1247   3912    252    922    -81       C  
ATOM   1919  C   VAL A 255      31.580   9.214  29.578  1.00 26.25           C  
ANISOU 1919  C   VAL A 255     3881   1787   4308    370    752    134       C  
ATOM   1920  O   VAL A 255      32.372   8.287  29.415  1.00 27.84           O  
ANISOU 1920  O   VAL A 255     4238   2054   4286    358    703    202       O  
ATOM   1921  CB  VAL A 255      32.082   9.957  31.937  1.00 27.38           C  
ANISOU 1921  CB  VAL A 255     4106   1874   4425    205    933   -106       C  
ATOM   1922  CG1 VAL A 255      32.932  11.060  31.288  1.00 29.01           C  
ANISOU 1922  CG1 VAL A 255     4202   2084   4737    306    798     20       C  
ATOM   1923  CG2 VAL A 255      31.478  10.471  33.256  1.00 26.92           C  
ANISOU 1923  CG2 VAL A 255     4014   1769   4447     86   1118   -354       C  
ATOM   1924  N   LYS A 256      31.189   9.989  28.573  1.00 27.72           N  
ANISOU 1924  N   LYS A 256     3885   1969   4678    487    666    242       N  
ATOM   1925  CA  LYS A 256      31.709   9.774  27.228  1.00 28.07           C  
ANISOU 1925  CA  LYS A 256     3932   2110   4624    587    528    447       C  
ATOM   1926  C   LYS A 256      33.088  10.414  27.095  1.00 27.63           C  
ANISOU 1926  C   LYS A 256     3902   2130   4464    593    437    547       C  
ATOM   1927  O   LYS A 256      33.278  11.584  27.433  1.00 29.92           O  
ANISOU 1927  O   LYS A 256     4104   2371   4893    589    435    542       O  
ATOM   1928  CB  LYS A 256      30.748  10.352  26.184  1.00 30.36           C  
ANISOU 1928  CB  LYS A 256     3995   2457   5084    688    432    556       C  
ATOM   1929  CG  LYS A 256      29.784   9.336  25.584  1.00 42.00           C  
ANISOU 1929  CG  LYS A 256     5422   4105   6433    637    383    471       C  
ATOM   1930  CD  LYS A 256      28.622   9.007  26.491  1.00 47.53           C  
ANISOU 1930  CD  LYS A 256     6058   4759   7240    525    504    234       C  
ATOM   1931  CE  LYS A 256      27.691   7.971  25.830  1.00 50.52           C  
ANISOU 1931  CE  LYS A 256     6372   5315   7509    445    453    136       C  
ATOM   1932  NZ  LYS A 256      26.782   8.554  24.786  1.00 50.78           N  
ANISOU 1932  NZ  LYS A 256     6121   5506   7667    546    297    228       N  
ATOM   1933  N   ILE A 257      34.040   9.637  26.592  1.00 23.09           N  
ANISOU 1933  N   ILE A 257     3438   1661   3675    597    382    615       N  
ATOM   1934  CA  ILE A 257      35.420  10.085  26.431  1.00 26.65           C  
ANISOU 1934  CA  ILE A 257     3892   2185   4046    590    317    684       C  
ATOM   1935  C   ILE A 257      35.892   9.873  24.992  1.00 25.22           C  
ANISOU 1935  C   ILE A 257     3689   2140   3753    657    243    839       C  
ATOM   1936  O   ILE A 257      35.796   8.762  24.453  1.00 25.54           O  
ANISOU 1936  O   ILE A 257     3808   2242   3654    694    255    844       O  
ATOM   1937  CB  ILE A 257      36.361   9.290  27.371  1.00 21.04           C  
ANISOU 1937  CB  ILE A 257     3306   1493   3197    531    345    600       C  
ATOM   1938  CG1 ILE A 257      36.044   9.629  28.832  1.00 22.70           C  
ANISOU 1938  CG1 ILE A 257     3550   1595   3481    460    434    473       C  
ATOM   1939  CG2 ILE A 257      37.830   9.606  27.079  1.00 21.11           C  
ANISOU 1939  CG2 ILE A 257     3294   1578   3149    541    288    677       C  
ATOM   1940  CD1 ILE A 257      36.698   8.608  29.811  1.00 27.97           C  
ANISOU 1940  CD1 ILE A 257     4370   2283   3974    414    471    428       C  
ATOM   1941  N   VAL A 258      36.408  10.932  24.384  1.00 25.89           N  
ANISOU 1941  N   VAL A 258     3685   2264   3889    672    195    961       N  
ATOM   1942  CA  VAL A 258      36.896  10.875  23.002  1.00 27.59           C  
ANISOU 1942  CA  VAL A 258     3869   2636   3978    721    146   1127       C  
ATOM   1943  C   VAL A 258      38.376  10.485  23.040  1.00 30.75           C  
ANISOU 1943  C   VAL A 258     4327   3100   4257    695    170   1108       C  
ATOM   1944  O   VAL A 258      39.190  11.186  23.653  1.00 26.36           O  
ANISOU 1944  O   VAL A 258     3753   2482   3780    648    185   1087       O  
ATOM   1945  CB  VAL A 258      36.705  12.225  22.279  1.00 29.07           C  
ANISOU 1945  CB  VAL A 258     3928   2831   4285    741    103   1296       C  
ATOM   1946  CG1 VAL A 258      37.125  12.120  20.796  1.00 33.62           C  
ANISOU 1946  CG1 VAL A 258     4471   3618   4686    779     59   1493       C  
ATOM   1947  CG2 VAL A 258      35.252  12.715  22.388  1.00 27.19           C  
ANISOU 1947  CG2 VAL A 258     3591   2510   4230    788     79   1313       C  
ATOM   1948  N   LEU A 259      38.729   9.359  22.415  1.00 24.42           N  
ANISOU 1948  N   LEU A 259     3589   2416   3275    745    191   1116       N  
ATOM   1949  CA  LEU A 259      40.084   8.827  22.587  1.00 28.15           C  
ANISOU 1949  CA  LEU A 259     4105   2929   3661    754    232   1077       C  
ATOM   1950  C   LEU A 259      41.189   9.782  22.126  1.00 28.80           C  
ANISOU 1950  C   LEU A 259     4098   3075   3770    739    239   1204       C  
ATOM   1951  O   LEU A 259      42.173   9.978  22.837  1.00 31.49           O  
ANISOU 1951  O   LEU A 259     4434   3369   4163    714    258   1168       O  
ATOM   1952  CB  LEU A 259      40.238   7.466  21.913  1.00 28.62           C  
ANISOU 1952  CB  LEU A 259     4265   3081   3528    855    283   1053       C  
ATOM   1953  CG  LEU A 259      39.414   6.361  22.594  1.00 27.50           C  
ANISOU 1953  CG  LEU A 259     4260   2811   3376    861    310    900       C  
ATOM   1954  CD1 LEU A 259      39.389   5.109  21.708  1.00 28.72           C  
ANISOU 1954  CD1 LEU A 259     4546   3025   3342    971    360    848       C  
ATOM   1955  CD2 LEU A 259      39.940   6.043  24.006  1.00 28.26           C  
ANISOU 1955  CD2 LEU A 259     4389   2801   3549    789    314    780       C  
ATOM   1956  N   ASP A 260      41.026  10.384  20.956  1.00 29.18           N  
ANISOU 1956  N   ASP A 260     4072   3237   3777    755    226   1372       N  
ATOM   1957  CA  ASP A 260      42.080  11.250  20.437  1.00 37.18           C  
ANISOU 1957  CA  ASP A 260     5001   4314   4813    732    260   1520       C  
ATOM   1958  C   ASP A 260      42.210  12.526  21.271  1.00 37.42           C  
ANISOU 1958  C   ASP A 260     4982   4160   5077    659    256   1517       C  
ATOM   1959  O   ASP A 260      43.285  13.115  21.344  1.00 38.82           O  
ANISOU 1959  O   ASP A 260     5103   4325   5321    628    306   1591       O  
ATOM   1960  CB  ASP A 260      41.920  11.541  18.930  1.00 41.83           C  
ANISOU 1960  CB  ASP A 260     5523   5110   5262    752    253   1727       C  
ATOM   1961  CG  ASP A 260      40.837  12.569  18.623  1.00 52.09           C  
ANISOU 1961  CG  ASP A 260     6760   6350   6683    729    178   1840       C  
ATOM   1962  OD1 ASP A 260      41.159  13.613  18.011  1.00 53.42           O  
ANISOU 1962  OD1 ASP A 260     6846   6541   6911    699    185   2028       O  
ATOM   1963  OD2 ASP A 260      39.657  12.328  18.961  1.00 56.81           O  
ANISOU 1963  OD2 ASP A 260     7380   6878   7325    753    119   1762       O  
ATOM   1964  N   GLN A 261      41.126  12.935  21.923  1.00 32.43           N  
ANISOU 1964  N   GLN A 261     4361   3387   4576    640    216   1436       N  
ATOM   1965  CA  GLN A 261      41.195  14.112  22.796  1.00 36.39           C  
ANISOU 1965  CA  GLN A 261     4818   3706   5303    587    239   1408       C  
ATOM   1966  C   GLN A 261      41.961  13.800  24.067  1.00 33.73           C  
ANISOU 1966  C   GLN A 261     4534   3298   4986    550    268   1261       C  
ATOM   1967  O   GLN A 261      42.786  14.593  24.518  1.00 31.84           O  
ANISOU 1967  O   GLN A 261     4243   2971   4884    504    312   1289       O  
ATOM   1968  CB  GLN A 261      39.804  14.646  23.135  1.00 37.58           C  
ANISOU 1968  CB  GLN A 261     4943   3735   5600    598    215   1363       C  
ATOM   1969  CG  GLN A 261      39.107  15.285  21.955  1.00 45.82           C  
ANISOU 1969  CG  GLN A 261     5900   4823   6687    643    176   1561       C  
ATOM   1970  CD  GLN A 261      37.763  15.881  22.324  1.00 57.24           C  
ANISOU 1970  CD  GLN A 261     7283   6135   8329    677    159   1532       C  
ATOM   1971  OE1 GLN A 261      37.343  15.842  23.487  1.00 57.35           O  
ANISOU 1971  OE1 GLN A 261     7319   6022   8448    657    198   1347       O  
ATOM   1972  NE2 GLN A 261      37.075  16.440  21.328  1.00 61.77           N  
ANISOU 1972  NE2 GLN A 261     7766   6747   8958    734    105   1729       N  
ATOM   1973  N   ILE A 262      41.682  12.651  24.662  1.00 33.52           N  
ANISOU 1973  N   ILE A 262     4601   3297   4836    568    246   1123       N  
ATOM   1974  CA  ILE A 262      42.430  12.277  25.854  1.00 27.97           C  
ANISOU 1974  CA  ILE A 262     3952   2549   4126    547    261   1023       C  
ATOM   1975  C   ILE A 262      43.899  12.046  25.478  1.00 30.68           C  
ANISOU 1975  C   ILE A 262     4261   2987   4408    578    283   1117       C  
ATOM   1976  O   ILE A 262      44.805  12.393  26.243  1.00 30.24           O  
ANISOU 1976  O   ILE A 262     4183   2873   4433    558    307   1125       O  
ATOM   1977  CB  ILE A 262      41.790  11.080  26.625  1.00 31.67           C  
ANISOU 1977  CB  ILE A 262     4525   3020   4488    555    242    889       C  
ATOM   1978  CG1 ILE A 262      42.439  10.943  27.996  1.00 34.30           C  
ANISOU 1978  CG1 ILE A 262     4917   3288   4826    533    260    824       C  
ATOM   1979  CG2 ILE A 262      41.883   9.780  25.852  1.00 29.13           C  
ANISOU 1979  CG2 ILE A 262     4244   2822   4002    614    230    898       C  
ATOM   1980  CD1 ILE A 262      42.069  12.090  28.923  1.00 39.14           C  
ANISOU 1980  CD1 ILE A 262     5512   3734   5624    468    315    759       C  
ATOM   1981  N   ASP A 263      44.133  11.512  24.274  1.00 31.62           N  
ANISOU 1981  N   ASP A 263     4360   3251   4403    634    293   1205       N  
ATOM   1982  CA  ASP A 263      45.497  11.302  23.786  1.00 32.85           C  
ANISOU 1982  CA  ASP A 263     4458   3520   4506    686    346   1312       C  
ATOM   1983  C   ASP A 263      46.267  12.625  23.730  1.00 37.56           C  
ANISOU 1983  C   ASP A 263     4931   4063   5276    619    395   1457       C  
ATOM   1984  O   ASP A 263      47.432  12.683  24.133  1.00 36.24           O  
ANISOU 1984  O   ASP A 263     4700   3904   5164    627    432   1514       O  
ATOM   1985  CB  ASP A 263      45.495  10.653  22.401  1.00 36.15           C  
ANISOU 1985  CB  ASP A 263     4865   4112   4757    762    385   1398       C  
ATOM   1986  CG  ASP A 263      45.531   9.138  22.460  1.00 39.85           C  
ANISOU 1986  CG  ASP A 263     5431   4633   5078    869    394   1284       C  
ATOM   1987  OD1 ASP A 263      45.692   8.584  23.568  1.00 40.69           O  
ANISOU 1987  OD1 ASP A 263     5598   4648   5213    875    358   1161       O  
ATOM   1988  OD2 ASP A 263      45.418   8.494  21.392  1.00 42.39           O  
ANISOU 1988  OD2 ASP A 263     5772   5090   5245    957    444   1330       O  
ATOM   1989  N   GLN A 264      45.617  13.683  23.236  1.00 35.46           N  
ANISOU 1989  N   GLN A 264     4617   3733   5123    557    396   1535       N  
ATOM   1990  CA  GLN A 264      46.269  14.992  23.119  1.00 38.11           C  
ANISOU 1990  CA  GLN A 264     4833   3979   5669    475    452   1681       C  
ATOM   1991  C   GLN A 264      46.650  15.518  24.495  1.00 35.35           C  
ANISOU 1991  C   GLN A 264     4467   3434   5529    404    466   1579       C  
ATOM   1992  O   GLN A 264      47.715  16.095  24.671  1.00 37.40           O  
ANISOU 1992  O   GLN A 264     4622   3638   5951    333    523   1672       O  
ATOM   1993  CB  GLN A 264      45.379  16.026  22.402  1.00 40.37           C  
ANISOU 1993  CB  GLN A 264     5079   4199   6059    444    439   1784       C  
ATOM   1994  CG  GLN A 264      44.960  15.642  20.978  1.00 49.67           C  
ANISOU 1994  CG  GLN A 264     6258   5575   7037    499    418   1923       C  
ATOM   1995  CD  GLN A 264      44.082  16.702  20.308  1.00 60.02           C  
ANISOU 1995  CD  GLN A 264     7521   6819   8463    486    388   2069       C  
ATOM   1996  OE1 GLN A 264      43.709  17.703  20.927  1.00 60.75           O  
ANISOU 1996  OE1 GLN A 264     7580   6698   8805    451    391   2045       O  
ATOM   1997  NE2 GLN A 264      43.753  16.482  19.034  1.00 63.41           N  
ANISOU 1997  NE2 GLN A 264     7938   7438   8715    523    362   2229       N  
ATOM   1998  N   ARG A 265      45.768  15.320  25.466  1.00 37.07           N  
ANISOU 1998  N   ARG A 265     4778   3549   5757    406    423   1392       N  
ATOM   1999  CA  ARG A 265      46.040  15.712  26.852  1.00 40.20           C  
ANISOU 1999  CA  ARG A 265     5175   3765   6334    333    444   1268       C  
ATOM   2000  C   ARG A 265      47.211  14.957  27.484  1.00 44.87           C  
ANISOU 2000  C   ARG A 265     5767   4412   6870    358    438   1288       C  
ATOM   2001  O   ARG A 265      48.037  15.544  28.184  1.00 49.03           O  
ANISOU 2001  O   ARG A 265     6196   4911   7521    236    439   1194       O  
ATOM   2002  CB  ARG A 265      44.780  15.561  27.709  1.00 40.75           C  
ANISOU 2002  CB  ARG A 265     5344   3746   6393    335    422   1074       C  
ATOM   2003  CG  ARG A 265      43.791  16.679  27.471  1.00 50.89           C  
ANISOU 2003  CG  ARG A 265     6569   4904   7864    302    445   1053       C  
ATOM   2004  CD  ARG A 265      42.432  16.428  28.105  1.00 58.43           C  
ANISOU 2004  CD  ARG A 265     7591   5814   8794    324    437    889       C  
ATOM   2005  NE  ARG A 265      41.446  17.382  27.599  1.00 60.00           N  
ANISOU 2005  NE  ARG A 265     7706   5929   9162    340    448    925       N  
ATOM   2006  CZ  ARG A 265      41.330  18.633  28.031  1.00 62.72           C  
ANISOU 2006  CZ  ARG A 265     7957   6076   9799    284    513    863       C  
ATOM   2007  NH1 ARG A 265      42.135  19.083  28.986  1.00 64.84           N  
ANISOU 2007  NH1 ARG A 265     8205   6214  10217    179    574    723       N  
ATOM   2008  NH2 ARG A 265      40.410  19.436  27.506  1.00 61.96           N  
ANISOU 2008  NH2 ARG A 265     7776   5900   9866    328    517    930       N  
ATOM   2009  N   ILE A 266      47.281  13.653  27.240  1.00 39.42           N  
ANISOU 2009  N   ILE A 266     5159   3909   5908    485    390   1290       N  
ATOM   2010  CA  ILE A 266      48.416  12.868  27.705  1.00 39.12           C  
ANISOU 2010  CA  ILE A 266     5090   4037   5735    534    338   1255       C  
ATOM   2011  C   ILE A 266      49.712  13.215  26.956  1.00 39.56           C  
ANISOU 2011  C   ILE A 266     4960   4229   5840    511    375   1374       C  
ATOM   2012  O   ILE A 266      50.799  13.188  27.534  1.00 41.74           O  
ANISOU 2012  O   ILE A 266     5119   4627   6115    472    328   1300       O  
ATOM   2013  CB  ILE A 266      48.119  11.374  27.582  1.00 39.74           C  
ANISOU 2013  CB  ILE A 266     5307   4213   5581    698    298   1246       C  
ATOM   2014  CG1 ILE A 266      47.150  10.972  28.693  1.00 44.52           C  
ANISOU 2014  CG1 ILE A 266     6072   4721   6124    677    259   1108       C  
ATOM   2015  CG2 ILE A 266      49.399  10.564  27.661  1.00 38.54           C  
ANISOU 2015  CG2 ILE A 266     5076   4247   5318    791    249   1249       C  
ATOM   2016  CD1 ILE A 266      46.467   9.662  28.458  1.00 49.51           C  
ANISOU 2016  CD1 ILE A 266     6817   5426   6570    729    217   1019       C  
ATOM   2017  N   ALA A 267      49.589  13.549  25.674  1.00 37.38           N  
ANISOU 2017  N   ALA A 267     4645   3964   5594    527    459   1566       N  
ATOM   2018  CA  ALA A 267      50.753  13.934  24.880  1.00 39.62           C  
ANISOU 2018  CA  ALA A 267     4748   4392   5913    480    531   1698       C  
ATOM   2019  C   ALA A 267      51.483  15.121  25.499  1.00 44.58           C  
ANISOU 2019  C   ALA A 267     5222   4923   6794    284    548   1657       C  
ATOM   2020  O   ALA A 267      52.711  15.139  25.546  1.00 51.91           O  
ANISOU 2020  O   ALA A 267     5977   6012   7734    234    557   1636       O  
ATOM   2021  CB  ALA A 267      50.348  14.249  23.443  1.00 40.24           C  
ANISOU 2021  CB  ALA A 267     4825   4505   5959    494    623   1941       C  
ATOM   2022  N   ALA A 268      50.733  16.119  25.962  1.00 44.92           N  
ANISOU 2022  N   ALA A 268     5306   4699   7063    170    561   1624       N  
ATOM   2023  CA  ALA A 268      51.346  17.277  26.616  1.00 47.43           C  
ANISOU 2023  CA  ALA A 268     5484   4880   7658    -41    589   1526       C  
ATOM   2024  C   ALA A 268      52.136  16.846  27.857  1.00 47.60           C  
ANISOU 2024  C   ALA A 268     5441   5062   7581    -86    481   1261       C  
ATOM   2025  O   ALA A 268      53.155  17.447  28.193  1.00 48.04           O  
ANISOU 2025  O   ALA A 268     5313   5169   7771   -248    486   1180       O  
ATOM   2026  CB  ALA A 268      50.298  18.325  26.978  1.00 46.76           C  
ANISOU 2026  CB  ALA A 268     5463   4447   7857   -129    630   1480       C  
ATOM   2027  N   VAL A 269      51.666  15.797  28.529  1.00 46.70           N  
ANISOU 2027  N   VAL A 269     5471   5043   7228     47    379   1143       N  
ATOM   2028  CA  VAL A 269      52.383  15.262  29.678  1.00 44.92           C  
ANISOU 2028  CA  VAL A 269     5198   5015   6857     33    249    954       C  
ATOM   2029  C   VAL A 269      53.687  14.589  29.246  1.00 45.72           C  
ANISOU 2029  C   VAL A 269     5131   5388   6852    124    210   1040       C  
ATOM   2030  O   VAL A 269      54.741  14.867  29.808  1.00 47.51           O  
ANISOU 2030  O   VAL A 269     5164   5767   7121     19    145    938       O  
ATOM   2031  CB  VAL A 269      51.526  14.271  30.476  1.00 44.63           C  
ANISOU 2031  CB  VAL A 269     5369   5000   6588    151    161    865       C  
ATOM   2032  CG1 VAL A 269      52.388  13.505  31.481  1.00 42.23           C  
ANISOU 2032  CG1 VAL A 269     5013   4953   6080    186      5    771       C  
ATOM   2033  CG2 VAL A 269      50.385  15.006  31.169  1.00 46.32           C  
ANISOU 2033  CG2 VAL A 269     5694   4992   6911     30    206    705       C  
ATOM   2034  N   PHE A 270      53.616  13.706  28.251  1.00 42.87           N  
ANISOU 2034  N   PHE A 270     4824   5103   6364    316    252   1200       N  
ATOM   2035  CA  PHE A 270      54.824  13.077  27.707  1.00 46.84           C  
ANISOU 2035  CA  PHE A 270     5146   5851   6800    422    254   1263       C  
ATOM   2036  C   PHE A 270      55.864  14.115  27.285  1.00 50.41           C  
ANISOU 2036  C   PHE A 270     5336   6371   7447    238    341   1302       C  
ATOM   2037  O   PHE A 270      57.025  14.039  27.684  1.00 52.16           O  
ANISOU 2037  O   PHE A 270     5334   6794   7689    209    279   1227       O  
ATOM   2038  CB  PHE A 270      54.484  12.191  26.508  1.00 45.78           C  
ANISOU 2038  CB  PHE A 270     5104   5759   6531    614    342   1393       C  
ATOM   2039  CG  PHE A 270      54.062  10.800  26.879  1.00 42.61           C  
ANISOU 2039  CG  PHE A 270     4869   5372   5950    827    253   1338       C  
ATOM   2040  CD1 PHE A 270      52.914  10.582  27.618  1.00 40.42           C  
ANISOU 2040  CD1 PHE A 270     4818   4927   5613    827    189   1280       C  
ATOM   2041  CD2 PHE A 270      54.801   9.709  26.460  1.00 43.19           C  
ANISOU 2041  CD2 PHE A 270     4865   5605   5940   1025    255   1343       C  
ATOM   2042  CE1 PHE A 270      52.526   9.297  27.949  1.00 43.36           C  
ANISOU 2042  CE1 PHE A 270     5349   5285   5841    999    125   1255       C  
ATOM   2043  CE2 PHE A 270      54.422   8.426  26.789  1.00 43.23           C  
ANISOU 2043  CE2 PHE A 270     5027   5564   5833   1219    186   1307       C  
ATOM   2044  CZ  PHE A 270      53.283   8.217  27.532  1.00 44.35           C  
ANISOU 2044  CZ  PHE A 270     5409   5531   5912   1196    120   1278       C  
ATOM   2045  N   HIS A 271      55.445  15.078  26.468  1.00 54.31           N  
ANISOU 2045  N   HIS A 271     5844   6699   8093    111    484   1439       N  
ATOM   2046  CA  HIS A 271      56.357  16.123  25.996  1.00 61.10           C  
ANISOU 2046  CA  HIS A 271     6471   7578   9166    -95    598   1517       C  
ATOM   2047  C   HIS A 271      57.020  16.815  27.181  1.00 62.01           C  
ANISOU 2047  C   HIS A 271     6427   7684   9452   -298    512   1299       C  
ATOM   2048  O   HIS A 271      58.238  17.017  27.199  1.00 62.65           O  
ANISOU 2048  O   HIS A 271     6243   7953   9608   -402    521   1258       O  
ATOM   2049  CB  HIS A 271      55.610  17.149  25.133  1.00 64.52           C  
ANISOU 2049  CB  HIS A 271     6984   7762   9770   -208    741   1732       C  
ATOM   2050  CG  HIS A 271      56.350  18.439  24.945  1.00 69.08           C  
ANISOU 2050  CG  HIS A 271     7361   8239  10648   -475    857   1803       C  
ATOM   2051  ND1 HIS A 271      56.212  19.510  25.804  1.00 70.76           N  
ANISOU 2051  ND1 HIS A 271     7548   8180  11158   -686    845   1655       N  
ATOM   2052  CD2 HIS A 271      57.232  18.830  23.996  1.00 70.81           C  
ANISOU 2052  CD2 HIS A 271     7392   8584  10929   -584   1006   1995       C  
ATOM   2053  CE1 HIS A 271      56.979  20.504  25.392  1.00 73.00           C  
ANISOU 2053  CE1 HIS A 271     7639   8393  11702   -916    976   1758       C  
ATOM   2054  NE2 HIS A 271      57.608  20.119  24.297  1.00 73.00           N  
ANISOU 2054  NE2 HIS A 271     7538   8640  11558   -864   1077   1984       N  
ATOM   2055  N   HIS A 272      56.206  17.162  28.174  1.00 63.02           N  
ANISOU 2055  N   HIS A 272     6700   7616   9628   -364    434   1132       N  
ATOM   2056  CA  HIS A 272      56.681  17.860  29.364  1.00 66.93           C  
ANISOU 2056  CA  HIS A 272     7068   8108  10256   -583    353    867       C  
ATOM   2057  C   HIS A 272      57.703  17.046  30.156  1.00 61.78           C  
ANISOU 2057  C   HIS A 272     6254   7815   9403   -521    174    728       C  
ATOM   2058  O   HIS A 272      58.564  17.614  30.830  1.00 61.36           O  
ANISOU 2058  O   HIS A 272     5980   7881   9452   -722    111    545       O  
ATOM   2059  CB  HIS A 272      55.504  18.241  30.267  1.00 71.62           C  
ANISOU 2059  CB  HIS A 272     7867   8461  10886   -639    321    686       C  
ATOM   2060  CG  HIS A 272      55.913  18.926  31.535  1.00 79.85           C  
ANISOU 2060  CG  HIS A 272     8791   9529  12020   -877    244    357       C  
ATOM   2061  ND1 HIS A 272      55.846  18.314  32.768  1.00 80.67           N  
ANISOU 2061  ND1 HIS A 272     8950   9842  11860   -850     73    141       N  
ATOM   2062  CD2 HIS A 272      56.399  20.171  31.758  1.00 84.66           C  
ANISOU 2062  CD2 HIS A 272     9226   9993  12946  -1164    318    197       C  
ATOM   2063  CE1 HIS A 272      56.272  19.151  33.696  1.00 83.97           C  
ANISOU 2063  CE1 HIS A 272     9228  10285  12391  -1112     35   -160       C  
ATOM   2064  NE2 HIS A 272      56.613  20.285  33.110  1.00 86.08           N  
ANISOU 2064  NE2 HIS A 272     9353  10321  13033  -1310    187   -153       N  
ATOM   2065  N   LEU A 273      57.597  15.721  30.078  1.00 57.51           N  
ANISOU 2065  N   LEU A 273     5815   7440   8596   -245     85    815       N  
ATOM   2066  CA  LEU A 273      58.534  14.833  30.766  1.00 61.64           C  
ANISOU 2066  CA  LEU A 273     6187   8289   8944   -128   -100    747       C  
ATOM   2067  C   LEU A 273      59.608  14.276  29.832  1.00 62.46           C  
ANISOU 2067  C   LEU A 273     6063   8609   9060     14    -48    884       C  
ATOM   2068  O   LEU A 273      60.434  13.458  30.244  1.00 63.45           O  
ANISOU 2068  O   LEU A 273     6031   8995   9080    164   -194    862       O  
ATOM   2069  CB  LEU A 273      57.793  13.682  31.457  1.00 63.05           C  
ANISOU 2069  CB  LEU A 273     6611   8490   8855     89   -239    752       C  
ATOM   2070  CG  LEU A 273      57.307  13.918  32.890  1.00 66.83           C  
ANISOU 2070  CG  LEU A 273     7196   8979   9216    -41   -378    556       C  
ATOM   2071  CD1 LEU A 273      56.438  15.164  32.979  1.00 68.99           C  
ANISOU 2071  CD1 LEU A 273     7570   8965   9677   -281   -244    418       C  
ATOM   2072  CD2 LEU A 273      56.554  12.700  33.406  1.00 65.09           C  
ANISOU 2072  CD2 LEU A 273     7231   8772   8730    174   -479    630       C  
ATOM   2073  N   ASN A 274      59.593  14.718  28.578  1.00 61.91           N  
ANISOU 2073  N   ASN A 274     5966   8443   9117    -30    163   1031       N  
ATOM   2074  CA  ASN A 274      60.556  14.247  27.586  1.00 66.35           C  
ANISOU 2074  CA  ASN A 274     6308   9224   9676     82    264   1140       C  
ATOM   2075  C   ASN A 274      60.561  12.719  27.429  1.00 62.71           C  
ANISOU 2075  C   ASN A 274     5920   8893   9013    430    195   1175       C  
ATOM   2076  O   ASN A 274      61.615  12.082  27.413  1.00 64.33           O  
ANISOU 2076  O   ASN A 274     5880   9347   9215    568    148   1150       O  
ATOM   2077  CB  ASN A 274      61.961  14.770  27.908  1.00 77.86           C  
ANISOU 2077  CB  ASN A 274     7378  10919  11288    -88    231   1039       C  
ATOM   2078  CG  ASN A 274      62.991  14.356  26.871  1.00 89.35           C  
ANISOU 2078  CG  ASN A 274     8565  12620  12763     10    369   1130       C  
ATOM   2079  OD1 ASN A 274      63.879  13.547  27.151  1.00 95.72           O  
ANISOU 2079  OD1 ASN A 274     9151  13693  13526    187    259   1066       O  
ATOM   2080  ND2 ASN A 274      62.869  14.900  25.663  1.00 91.30           N  
ANISOU 2080  ND2 ASN A 274     8823  12794  13075    -96    615   1290       N  
ATOM   2081  N   ILE A 275      59.370  12.140  27.319  1.00 54.50           N  
ANISOU 2081  N   ILE A 275     5203   7667   7837    569    195   1224       N  
ATOM   2082  CA  ILE A 275      59.230  10.719  27.056  1.00 48.67           C  
ANISOU 2082  CA  ILE A 275     4568   6975   6949    875    167   1252       C  
ATOM   2083  C   ILE A 275      59.016  10.520  25.565  1.00 49.79           C  
ANISOU 2083  C   ILE A 275     4746   7120   7053    941    384   1345       C  
ATOM   2084  O   ILE A 275      58.025  10.993  25.005  1.00 46.70           O  
ANISOU 2084  O   ILE A 275     4549   6565   6631    849    480   1424       O  
ATOM   2085  CB  ILE A 275      58.037  10.138  27.819  1.00 49.92           C  
ANISOU 2085  CB  ILE A 275     5052   6939   6976    962     50   1233       C  
ATOM   2086  CG1 ILE A 275      58.186  10.419  29.316  1.00 53.94           C  
ANISOU 2086  CG1 ILE A 275     5539   7492   7465    860   -155   1137       C  
ATOM   2087  CG2 ILE A 275      57.917   8.647  27.569  1.00 47.10           C  
ANISOU 2087  CG2 ILE A 275     4802   6581   6512   1264     31   1259       C  
ATOM   2088  CD1 ILE A 275      57.066   9.851  30.163  1.00 51.69           C  
ANISOU 2088  CD1 ILE A 275     5559   7056   7026    921   -256   1125       C  
ATOM   2089  N   GLY A 276      59.953   9.833  24.922  1.00 52.78           N  
ANISOU 2089  N   GLY A 276     4918   7708   7427   1100    461   1329       N  
ATOM   2090  CA  GLY A 276      59.910   9.643  23.485  1.00 54.20           C  
ANISOU 2090  CA  GLY A 276     5091   7971   7531   1142    685   1382       C  
ATOM   2091  C   GLY A 276      59.136   8.405  23.075  1.00 52.90           C  
ANISOU 2091  C   GLY A 276     5159   7720   7220   1380    702   1333       C  
ATOM   2092  O   GLY A 276      58.847   8.217  21.895  1.00 52.79           O  
ANISOU 2092  O   GLY A 276     5194   7774   7090   1398    875   1347       O  
ATOM   2093  N   ASN A 277      58.809   7.558  24.048  1.00 46.70           N  
ANISOU 2093  N   ASN A 277     4514   6797   6431   1544    526   1274       N  
ATOM   2094  CA  ASN A 277      58.050   6.344  23.779  1.00 42.32           C  
ANISOU 2094  CA  ASN A 277     4188   6106   5784   1751    540   1216       C  
ATOM   2095  C   ASN A 277      56.727   6.659  23.104  1.00 41.64           C  
ANISOU 2095  C   ASN A 277     4359   5894   5569   1633    625   1254       C  
ATOM   2096  O   ASN A 277      56.015   7.591  23.502  1.00 45.67           O  
ANISOU 2096  O   ASN A 277     4980   6287   6084   1446    572   1335       O  
ATOM   2097  CB  ASN A 277      57.760   5.590  25.075  1.00 41.05           C  
ANISOU 2097  CB  ASN A 277     4172   5779   5645   1884    330   1210       C  
ATOM   2098  CG  ASN A 277      58.998   5.354  25.903  1.00 49.22           C  
ANISOU 2098  CG  ASN A 277     4950   6959   6793   1998    185   1214       C  
ATOM   2099  OD1 ASN A 277      59.630   6.298  26.380  1.00 54.45           O  
ANISOU 2099  OD1 ASN A 277     5418   7765   7506   1832    117   1233       O  
ATOM   2100  ND2 ASN A 277      59.342   4.088  26.099  1.00 45.66           N  
ANISOU 2100  ND2 ASN A 277     4486   6462   6401   2282    129   1194       N  
ATOM   2101  N   ALA A 278      56.382   5.884  22.086  1.00 37.33           N  
ANISOU 2101  N   ALA A 278     3891   5378   4916   1744    755   1179       N  
ATOM   2102  CA  ALA A 278      55.080   6.057  21.459  1.00 41.48           C  
ANISOU 2102  CA  ALA A 278     4644   5817   5298   1649    803   1207       C  
ATOM   2103  C   ALA A 278      54.027   5.558  22.445  1.00 38.55           C  
ANISOU 2103  C   ALA A 278     4529   5175   4943   1687    656   1181       C  
ATOM   2104  O   ALA A 278      54.340   4.784  23.352  1.00 35.79           O  
ANISOU 2104  O   ALA A 278     4200   4725   4674   1827    551   1135       O  
ATOM   2105  CB  ALA A 278      55.010   5.292  20.144  1.00 46.53           C  
ANISOU 2105  CB  ALA A 278     5287   6604   5788   1740    971   1087       C  
ATOM   2106  N   PHE A 279      52.787   6.004  22.281  1.00 31.54           N  
ANISOU 2106  N   PHE A 279     3822   4181   3981   1563    647   1230       N  
ATOM   2107  CA  PHE A 279      51.722   5.558  23.161  1.00 33.48           C  
ANISOU 2107  CA  PHE A 279     4295   4192   4235   1573    539   1195       C  
ATOM   2108  C   PHE A 279      50.383   5.777  22.470  1.00 32.44           C  
ANISOU 2108  C   PHE A 279     4312   4015   4001   1480    578   1204       C  
ATOM   2109  O   PHE A 279      50.281   6.532  21.502  1.00 28.95           O  
ANISOU 2109  O   PHE A 279     3797   3713   3490   1388    651   1294       O  
ATOM   2110  CB  PHE A 279      51.737   6.369  24.460  1.00 32.87           C  
ANISOU 2110  CB  PHE A 279     4217   4019   4253   1460    414   1263       C  
ATOM   2111  CG  PHE A 279      51.221   7.775  24.280  1.00 36.87           C  
ANISOU 2111  CG  PHE A 279     4703   4503   4801   1261    437   1357       C  
ATOM   2112  CD1 PHE A 279      49.886   8.077  24.516  1.00 37.88           C  
ANISOU 2112  CD1 PHE A 279     4995   4475   4924   1163    409   1340       C  
ATOM   2113  CD2 PHE A 279      52.061   8.783  23.817  1.00 43.71           C  
ANISOU 2113  CD2 PHE A 279     5370   5498   5740   1158    499   1449       C  
ATOM   2114  CE1 PHE A 279      49.396   9.371  24.322  1.00 36.12           C  
ANISOU 2114  CE1 PHE A 279     4736   4196   4790   1006    429   1423       C  
ATOM   2115  CE2 PHE A 279      51.576  10.079  23.614  1.00 45.69           C  
ANISOU 2115  CE2 PHE A 279     5608   5672   6081    984    530   1564       C  
ATOM   2116  CZ  PHE A 279      50.240  10.368  23.874  1.00 39.43           C  
ANISOU 2116  CZ  PHE A 279     4982   4691   5308    936    493   1570       C  
ATOM   2117  N   PHE A 280      49.351   5.119  22.979  1.00 30.19           N  
ANISOU 2117  N   PHE A 280     4220   3547   3704   1495    523   1130       N  
ATOM   2118  CA  PHE A 280      47.991   5.458  22.585  1.00 32.49           C  
ANISOU 2118  CA  PHE A 280     4612   3799   3934   1363    520   1117       C  
ATOM   2119  C   PHE A 280      47.036   5.054  23.692  1.00 33.30           C  
ANISOU 2119  C   PHE A 280     4833   3732   4088   1236    423    978       C  
ATOM   2120  O   PHE A 280      47.222   4.026  24.361  1.00 31.25           O  
ANISOU 2120  O   PHE A 280     4639   3388   3848   1284    392    892       O  
ATOM   2121  CB  PHE A 280      47.595   4.819  21.233  1.00 31.08           C  
ANISOU 2121  CB  PHE A 280     4463   3748   3597   1428    610   1051       C  
ATOM   2122  CG  PHE A 280      47.656   3.308  21.220  1.00 33.04           C  
ANISOU 2122  CG  PHE A 280     4803   3912   3839   1559    647    849       C  
ATOM   2123  CD1 PHE A 280      46.538   2.548  21.560  1.00 29.40           C  
ANISOU 2123  CD1 PHE A 280     4518   3265   3389   1540    618    741       C  
ATOM   2124  CD2 PHE A 280      48.826   2.652  20.871  1.00 31.26           C  
ANISOU 2124  CD2 PHE A 280     4474   3774   3631   1700    723    761       C  
ATOM   2125  CE1 PHE A 280      46.585   1.169  21.547  1.00 27.84           C  
ANISOU 2125  CE1 PHE A 280     4409   2934   3234   1647    666    562       C  
ATOM   2126  CE2 PHE A 280      48.888   1.258  20.864  1.00 33.33           C  
ANISOU 2126  CE2 PHE A 280     4815   3900   3950   1838    769    570       C  
ATOM   2127  CZ  PHE A 280      47.763   0.514  21.191  1.00 28.25           C  
ANISOU 2127  CZ  PHE A 280     4367   3036   3330   1806    741    475       C  
ATOM   2128  N   CYS A 281      46.035   5.892  23.913  1.00 32.25           N  
ANISOU 2128  N   CYS A 281     4704   3560   3991   1077    380    978       N  
ATOM   2129  CA  CYS A 281      44.949   5.523  24.798  1.00 33.05           C  
ANISOU 2129  CA  CYS A 281     4897   3543   4119    978    325    868       C  
ATOM   2130  C   CYS A 281      44.080   4.492  24.105  1.00 29.95           C  
ANISOU 2130  C   CYS A 281     4615   3118   3648   1037    376    799       C  
ATOM   2131  O   CYS A 281      43.929   4.507  22.884  1.00 23.92           O  
ANISOU 2131  O   CYS A 281     3860   2433   2795   1124    434    849       O  
ATOM   2132  CB  CYS A 281      44.126   6.752  25.174  1.00 35.81           C  
ANISOU 2132  CB  CYS A 281     5199   3856   4550    840    284    882       C  
ATOM   2133  SG  CYS A 281      44.965   7.756  26.396  1.00 42.91           S  
ANISOU 2133  SG  CYS A 281     6046   4710   5546    783    238    917       S  
ATOM   2134  N   TRP A 282      43.517   3.593  24.899  1.00 26.45           N  
ANISOU 2134  N   TRP A 282     4268   2561   3221    999    359    706       N  
ATOM   2135  CA  TRP A 282      42.632   2.574  24.373  1.00 29.52           C  
ANISOU 2135  CA  TRP A 282     4788   2864   3564   1039    415    622       C  
ATOM   2136  C   TRP A 282      41.633   2.218  25.468  1.00 28.98           C  
ANISOU 2136  C   TRP A 282     4777   2690   3545    908    391    563       C  
ATOM   2137  O   TRP A 282      41.448   2.983  26.417  1.00 26.98           O  
ANISOU 2137  O   TRP A 282     4463   2457   3332    808    343    591       O  
ATOM   2138  CB  TRP A 282      43.439   1.348  23.946  1.00 28.73           C  
ANISOU 2138  CB  TRP A 282     4759   2705   3452   1195    473    565       C  
ATOM   2139  CG  TRP A 282      42.752   0.473  22.941  1.00 36.35           C  
ANISOU 2139  CG  TRP A 282     5862   3579   4369   1285    564    434       C  
ATOM   2140  CD1 TRP A 282      42.430  -0.853  23.085  1.00 37.36           C  
ANISOU 2140  CD1 TRP A 282     6094   3534   4567   1275    605    284       C  
ATOM   2141  CD2 TRP A 282      42.313   0.852  21.631  1.00 32.68           C  
ANISOU 2141  CD2 TRP A 282     5333   3316   3768   1269    589    375       C  
ATOM   2142  NE1 TRP A 282      41.815  -1.313  21.948  1.00 37.23           N  
ANISOU 2142  NE1 TRP A 282     6123   3543   4481   1285    681     87       N  
ATOM   2143  CE2 TRP A 282      41.734  -0.289  21.038  1.00 36.66           C  
ANISOU 2143  CE2 TRP A 282     5907   3775   4248   1243    648    136       C  
ATOM   2144  CE3 TRP A 282      42.371   2.037  20.895  1.00 33.07           C  
ANISOU 2144  CE3 TRP A 282     5242   3615   3709   1233    557    505       C  
ATOM   2145  CZ2 TRP A 282      41.206  -0.276  19.740  1.00 41.10           C  
ANISOU 2145  CZ2 TRP A 282     6392   4587   4636   1175    659     -2       C  
ATOM   2146  CZ3 TRP A 282      41.840   2.051  19.605  1.00 36.79           C  
ANISOU 2146  CZ3 TRP A 282     5646   4328   4005   1181    564    424       C  
ATOM   2147  CH2 TRP A 282      41.266   0.902  19.043  1.00 38.28           C  
ANISOU 2147  CH2 TRP A 282     5896   4519   4128   1150    608    160       C  
ATOM   2148  N   TRP A 283      40.966   1.079  25.331  1.00 26.36           N  
ANISOU 2148  N   TRP A 283     4572   2232   3210    913    441    477       N  
ATOM   2149  CA  TRP A 283      39.952   0.718  26.317  1.00 25.78           C  
ANISOU 2149  CA  TRP A 283     4555   2066   3175    784    444    442       C  
ATOM   2150  C   TRP A 283      39.796  -0.780  26.403  1.00 30.13           C  
ANISOU 2150  C   TRP A 283     5225   2455   3767    791    493    375       C  
ATOM   2151  O   TRP A 283      40.241  -1.525  25.522  1.00 30.29           O  
ANISOU 2151  O   TRP A 283     5292   2412   3804    893    535    304       O  
ATOM   2152  CB  TRP A 283      38.608   1.341  25.962  1.00 26.21           C  
ANISOU 2152  CB  TRP A 283     4612   2115   3231    713    469    405       C  
ATOM   2153  CG  TRP A 283      38.091   0.832  24.670  1.00 25.97           C  
ANISOU 2153  CG  TRP A 283     4682   2021   3166    780    525    318       C  
ATOM   2154  CD1 TRP A 283      38.387   1.319  23.417  1.00 30.17           C  
ANISOU 2154  CD1 TRP A 283     5159   2694   3612    880    510    338       C  
ATOM   2155  CD2 TRP A 283      37.203  -0.276  24.472  1.00 33.27           C  
ANISOU 2155  CD2 TRP A 283     5735   2785   4122    717    596    156       C  
ATOM   2156  NE1 TRP A 283      37.731   0.581  22.461  1.00 34.71           N  
ANISOU 2156  NE1 TRP A 283     5723   3344   4122    826    528    151       N  
ATOM   2157  CE2 TRP A 283      37.000  -0.403  23.077  1.00 34.91           C  
ANISOU 2157  CE2 TRP A 283     5870   3156   4240    731    586     21       C  
ATOM   2158  CE3 TRP A 283      36.565  -1.178  25.334  1.00 35.59           C  
ANISOU 2158  CE3 TRP A 283     6079   2953   4492    579    636     97       C  
ATOM   2159  CZ2 TRP A 283      36.185  -1.395  22.526  1.00 36.45           C  
ANISOU 2159  CZ2 TRP A 283     6091   3320   4438    625    629   -213       C  
ATOM   2160  CZ3 TRP A 283      35.756  -2.160  24.788  1.00 37.27           C  
ANISOU 2160  CZ3 TRP A 283     6379   3031   4750    499    710    -98       C  
ATOM   2161  CH2 TRP A 283      35.572  -2.263  23.390  1.00 37.77           C  
ANISOU 2161  CH2 TRP A 283     6391   3223   4738    517    705   -282       C  
ATOM   2162  N   GLU A 284      39.160  -1.233  27.470  1.00 32.69           N  
ANISOU 2162  N   GLU A 284     5601   2697   4122    684    502    389       N  
ATOM   2163  CA  GLU A 284      38.828  -2.647  27.553  1.00 36.01           C  
ANISOU 2163  CA  GLU A 284     6132   2932   4620    660    557    338       C  
ATOM   2164  C   GLU A 284      37.489  -2.816  28.247  1.00 33.31           C  
ANISOU 2164  C   GLU A 284     5853   2515   4287    499    614    315       C  
ATOM   2165  O   GLU A 284      37.031  -1.917  28.958  1.00 29.36           O  
ANISOU 2165  O   GLU A 284     5320   2105   3731    428    607    357       O  
ATOM   2166  CB  GLU A 284      39.934  -3.444  28.248  1.00 39.06           C  
ANISOU 2166  CB  GLU A 284     6527   3249   5064    743    511    445       C  
ATOM   2167  CG  GLU A 284      40.162  -3.075  29.693  1.00 44.94           C  
ANISOU 2167  CG  GLU A 284     7267   4053   5757    698    451    593       C  
ATOM   2168  CD  GLU A 284      41.241  -3.932  30.327  1.00 55.82           C  
ANISOU 2168  CD  GLU A 284     8661   5347   7202    795    387    727       C  
ATOM   2169  OE1 GLU A 284      42.377  -3.439  30.486  1.00 53.56           O  
ANISOU 2169  OE1 GLU A 284     8288   5169   6893    887    305    800       O  
ATOM   2170  OE2 GLU A 284      40.954  -5.105  30.657  1.00 64.68           O  
ANISOU 2170  OE2 GLU A 284     9877   6277   8420    779    415    771       O  
ATOM   2171  N   PRO A 285      36.827  -3.944  27.990  1.00 35.56           N  
ANISOU 2171  N   PRO A 285     6225   2625   4661    432    686    221       N  
ATOM   2172  CA  PRO A 285      35.543  -4.179  28.640  1.00 36.41           C  
ANISOU 2172  CA  PRO A 285     6390   2656   4789    258    763    194       C  
ATOM   2173  C   PRO A 285      35.745  -4.177  30.150  1.00 37.15           C  
ANISOU 2173  C   PRO A 285     6526   2758   4831    224    753    366       C  
ATOM   2174  O   PRO A 285      36.770  -4.651  30.636  1.00 38.95           O  
ANISOU 2174  O   PRO A 285     6774   2955   5071    318    692    493       O  
ATOM   2175  CB  PRO A 285      35.159  -5.579  28.159  1.00 43.00           C  
ANISOU 2175  CB  PRO A 285     7300   3277   5760    201    833     75       C  
ATOM   2176  CG  PRO A 285      35.908  -5.764  26.864  1.00 46.95           C  
ANISOU 2176  CG  PRO A 285     7772   3778   6288    335    808    -50       C  
ATOM   2177  CD  PRO A 285      37.194  -5.011  27.043  1.00 42.26           C  
ANISOU 2177  CD  PRO A 285     7113   3333   5611    500    718    101       C  
ATOM   2178  N   ASP A 286      34.788  -3.619  30.879  1.00 37.27           N  
ANISOU 2178  N   ASP A 286     6556   2815   4789     91    817    363       N  
ATOM   2179  CA  ASP A 286      34.833  -3.609  32.333  1.00 33.29           C  
ANISOU 2179  CA  ASP A 286     6129   2320   4199     31    839    504       C  
ATOM   2180  C   ASP A 286      33.411  -3.741  32.866  1.00 35.00           C  
ANISOU 2180  C   ASP A 286     6407   2477   4415   -173    988    444       C  
ATOM   2181  O   ASP A 286      32.540  -2.952  32.492  1.00 34.18           O  
ANISOU 2181  O   ASP A 286     6231   2432   4325   -247   1046    310       O  
ATOM   2182  CB  ASP A 286      35.456  -2.298  32.850  1.00 31.17           C  
ANISOU 2182  CB  ASP A 286     5802   2227   3815     90    773    552       C  
ATOM   2183  CG  ASP A 286      35.610  -2.295  34.380  1.00 34.71           C  
ANISOU 2183  CG  ASP A 286     6358   2696   4133     22    794    694       C  
ATOM   2184  OD1 ASP A 286      34.949  -1.485  35.074  1.00 31.41           O  
ANISOU 2184  OD1 ASP A 286     5976   2337   3622    -93    882    653       O  
ATOM   2185  OD2 ASP A 286      36.380  -3.138  34.876  1.00 38.80           O  
ANISOU 2185  OD2 ASP A 286     6928   3167   4645     76    729    854       O  
ATOM   2186  N   ALA A 287      33.183  -4.704  33.761  1.00 35.90           N  
ANISOU 2186  N   ALA A 287     6639   2477   4526   -271   1053    556       N  
ATOM   2187  CA  ALA A 287      31.845  -4.952  34.285  1.00 34.49           C  
ANISOU 2187  CA  ALA A 287     6510   2243   4350   -493   1218    502       C  
ATOM   2188  C   ALA A 287      31.262  -3.707  34.936  1.00 35.11           C  
ANISOU 2188  C   ALA A 287     6559   2473   4308   -589   1302    440       C  
ATOM   2189  O   ALA A 287      30.078  -3.414  34.774  1.00 37.88           O  
ANISOU 2189  O   ALA A 287     6846   2832   4714   -743   1433    283       O  
ATOM   2190  CB  ALA A 287      31.837  -6.137  35.272  1.00 35.28           C  
ANISOU 2190  CB  ALA A 287     6746   2208   4450   -581   1268    692       C  
ATOM   2191  N   LYS A 288      32.092  -2.977  35.669  1.00 32.38           N  
ANISOU 2191  N   LYS A 288     6243   2244   3817   -512   1236    544       N  
ATOM   2192  CA  LYS A 288      31.609  -1.824  36.428  1.00 34.01           C  
ANISOU 2192  CA  LYS A 288     6445   2569   3907   -625   1343    473       C  
ATOM   2193  C   LYS A 288      31.383  -0.593  35.555  1.00 30.47           C  
ANISOU 2193  C   LYS A 288     5848   2165   3563   -563   1333    303       C  
ATOM   2194  O   LYS A 288      30.340   0.058  35.639  1.00 31.61           O  
ANISOU 2194  O   LYS A 288     5917   2323   3770   -699   1480    150       O  
ATOM   2195  CB  LYS A 288      32.590  -1.468  37.547  1.00 37.61           C  
ANISOU 2195  CB  LYS A 288     6993   3142   4157   -592   1277    630       C  
ATOM   2196  CG  LYS A 288      32.205  -0.214  38.317  1.00 45.31           C  
ANISOU 2196  CG  LYS A 288     7971   4249   4995   -726   1407    519       C  
ATOM   2197  CD  LYS A 288      32.964  -0.110  39.636  1.00 55.51           C  
ANISOU 2197  CD  LYS A 288     9371   5709   6013   -769   1367    669       C  
ATOM   2198  CE  LYS A 288      32.749   1.255  40.283  1.00 61.97           C  
ANISOU 2198  CE  LYS A 288    10169   6694   6682   -901   1501    495       C  
ATOM   2199  NZ  LYS A 288      31.311   1.512  40.586  1.00 64.21           N  
ANISOU 2199  NZ  LYS A 288    10387   7013   6997  -1123   1759    282       N  
ATOM   2200  N   LEU A 289      32.366  -0.285  34.724  1.00 27.06           N  
ANISOU 2200  N   LEU A 289     5344   1761   3175   -361   1162    335       N  
ATOM   2201  CA  LEU A 289      32.365   0.960  33.955  1.00 25.70           C  
ANISOU 2201  CA  LEU A 289     5022   1642   3099   -274   1116    236       C  
ATOM   2202  C   LEU A 289      31.798   0.817  32.537  1.00 28.78           C  
ANISOU 2202  C   LEU A 289     5284   2007   3645   -232   1075    140       C  
ATOM   2203  O   LEU A 289      31.469   1.814  31.899  1.00 29.06           O  
ANISOU 2203  O   LEU A 289     5180   2073   3787   -184   1052     65       O  
ATOM   2204  CB  LEU A 289      33.787   1.495  33.872  1.00 25.62           C  
ANISOU 2204  CB  LEU A 289     4987   1714   3034   -104    961    333       C  
ATOM   2205  CG  LEU A 289      34.340   1.942  35.226  1.00 33.62           C  
ANISOU 2205  CG  LEU A 289     6125   2767   3884   -159    994    405       C  
ATOM   2206  CD1 LEU A 289      35.838   2.208  35.116  1.00 30.41           C  
ANISOU 2206  CD1 LEU A 289     5682   2440   3433      0    825    508       C  
ATOM   2207  CD2 LEU A 289      33.590   3.179  35.720  1.00 35.55           C  
ANISOU 2207  CD2 LEU A 289     6353   2992   4162   -286   1151    264       C  
ATOM   2208  N   GLY A 290      31.683  -0.416  32.058  1.00 28.68           N  
ANISOU 2208  N   GLY A 290     5323   1921   3654   -254   1068    141       N  
ATOM   2209  CA  GLY A 290      31.293  -0.678  30.681  1.00 29.83           C  
ANISOU 2209  CA  GLY A 290     5391   2034   3907   -229   1030     35       C  
ATOM   2210  C   GLY A 290      32.554  -0.769  29.841  1.00 30.27           C  
ANISOU 2210  C   GLY A 290     5439   2133   3930    -42    889    104       C  
ATOM   2211  O   GLY A 290      32.985  -1.855  29.438  1.00 32.66           O  
ANISOU 2211  O   GLY A 290     5806   2358   4244    -12    873    102       O  
ATOM   2212  N   GLN A 291      33.159   0.391  29.604  1.00 25.88           N  
ANISOU 2212  N   GLN A 291     4792   1689   3353     75    806    155       N  
ATOM   2213  CA  GLN A 291      34.449   0.477  28.935  1.00 30.75           C  
ANISOU 2213  CA  GLN A 291     5375   2380   3929    232    694    227       C  
ATOM   2214  C   GLN A 291      35.432   1.217  29.850  1.00 31.00           C  
ANISOU 2214  C   GLN A 291     5368   2509   3901    282    636    330       C  
ATOM   2215  O   GLN A 291      35.117   2.275  30.386  1.00 31.19           O  
ANISOU 2215  O   GLN A 291     5343   2566   3941    247    656    325       O  
ATOM   2216  CB  GLN A 291      34.286   1.181  27.593  1.00 29.17           C  
ANISOU 2216  CB  GLN A 291     5099   2221   3763    313    654    194       C  
ATOM   2217  CG  GLN A 291      33.299   0.466  26.674  1.00 30.29           C  
ANISOU 2217  CG  GLN A 291     5307   2252   3949    253    717     42       C  
ATOM   2218  CD  GLN A 291      33.096   1.205  25.361  1.00 34.74           C  
ANISOU 2218  CD  GLN A 291     5681   3039   4481    320    612     21       C  
ATOM   2219  OE1 GLN A 291      32.433   2.237  25.321  1.00 29.54           O  
ANISOU 2219  OE1 GLN A 291     4859   2484   3879    313    569     56       O  
ATOM   2220  NE2 GLN A 291      33.673   0.675  24.280  1.00 36.11           N  
ANISOU 2220  NE2 GLN A 291     5863   3296   4560    389    573    -30       N  
ATOM   2221  N   LYS A 292      36.607   0.631  30.044  1.00 29.98           N  
ANISOU 2221  N   LYS A 292     5265   2399   3728    357    577    404       N  
ATOM   2222  CA  LYS A 292      37.615   1.180  30.937  1.00 31.37           C  
ANISOU 2222  CA  LYS A 292     5421   2649   3848    393    519    491       C  
ATOM   2223  C   LYS A 292      38.762   1.745  30.104  1.00 30.25           C  
ANISOU 2223  C   LYS A 292     5157   2609   3729    504    432    518       C  
ATOM   2224  O   LYS A 292      39.407   1.018  29.338  1.00 28.19           O  
ANISOU 2224  O   LYS A 292     4891   2338   3483    587    411    523       O  
ATOM   2225  CB  LYS A 292      38.159   0.085  31.856  1.00 31.87           C  
ANISOU 2225  CB  LYS A 292     5594   2651   3865    398    508    587       C  
ATOM   2226  CG  LYS A 292      39.148   0.591  32.907  1.00 45.58           C  
ANISOU 2226  CG  LYS A 292     7340   4461   5516    426    442    693       C  
ATOM   2227  CD  LYS A 292      40.117  -0.500  33.407  1.00 51.71           C  
ANISOU 2227  CD  LYS A 292     8161   5202   6284    497    371    836       C  
ATOM   2228  CE  LYS A 292      39.402  -1.746  33.879  1.00 58.70           C  
ANISOU 2228  CE  LYS A 292     9174   5946   7182    430    433    892       C  
ATOM   2229  NZ  LYS A 292      40.359  -2.754  34.442  1.00 63.90           N  
ANISOU 2229  NZ  LYS A 292     9866   6548   7863    510    348   1077       N  
ATOM   2230  N   LEU A 293      39.025   3.033  30.276  1.00 25.58           N  
ANISOU 2230  N   LEU A 293     4479   2089   3150    500    404    531       N  
ATOM   2231  CA  LEU A 293      40.090   3.704  29.545  1.00 24.88           C  
ANISOU 2231  CA  LEU A 293     4272   2089   3091    575    338    570       C  
ATOM   2232  C   LEU A 293      41.413   3.143  30.048  1.00 25.74           C  
ANISOU 2232  C   LEU A 293     4399   2220   3160    642    284    641       C  
ATOM   2233  O   LEU A 293      41.606   2.997  31.259  1.00 25.52           O  
ANISOU 2233  O   LEU A 293     4449   2171   3075    618    270    691       O  
ATOM   2234  CB  LEU A 293      40.038   5.215  29.815  1.00 20.81           C  
ANISOU 2234  CB  LEU A 293     3678   1594   2637    538    331    577       C  
ATOM   2235  CG  LEU A 293      41.103   6.062  29.105  1.00 29.11           C  
ANISOU 2235  CG  LEU A 293     4608   2714   3738    588    277    637       C  
ATOM   2236  CD1 LEU A 293      40.821   6.151  27.621  1.00 27.72           C  
ANISOU 2236  CD1 LEU A 293     4362   2586   3585    626    277    653       C  
ATOM   2237  CD2 LEU A 293      41.133   7.462  29.712  1.00 30.76           C  
ANISOU 2237  CD2 LEU A 293     4777   2875   4037    543    286    643       C  
ATOM   2238  N   VAL A 294      42.318   2.828  29.119  1.00 24.32           N  
ANISOU 2238  N   VAL A 294     4161   2079   2998    737    260    659       N  
ATOM   2239  CA  VAL A 294      43.657   2.390  29.487  1.00 25.76           C  
ANISOU 2239  CA  VAL A 294     4329   2281   3176    826    203    733       C  
ATOM   2240  C   VAL A 294      44.711   3.108  28.661  1.00 26.55           C  
ANISOU 2240  C   VAL A 294     4313   2473   3300    901    187    762       C  
ATOM   2241  O   VAL A 294      44.381   3.782  27.689  1.00 25.09           O  
ANISOU 2241  O   VAL A 294     4076   2331   3126    887    226    739       O  
ATOM   2242  CB  VAL A 294      43.810   0.884  29.312  1.00 26.24           C  
ANISOU 2242  CB  VAL A 294     4464   2248   3260    903    218    733       C  
ATOM   2243  CG1 VAL A 294      42.808   0.163  30.215  1.00 26.10           C  
ANISOU 2243  CG1 VAL A 294     4567   2124   3225    817    243    740       C  
ATOM   2244  CG2 VAL A 294      43.611   0.491  27.828  1.00 29.03           C  
ANISOU 2244  CG2 VAL A 294     4821   2579   3631    971    291    649       C  
ATOM   2245  N   LEU A 295      45.968   2.969  29.055  1.00 27.90           N  
ANISOU 2245  N   LEU A 295     4443   2680   3477    989    129    835       N  
ATOM   2246  CA  LEU A 295      47.066   3.575  28.319  1.00 31.01           C  
ANISOU 2246  CA  LEU A 295     4720   3166   3896   1078    131    876       C  
ATOM   2247  C   LEU A 295      48.068   2.507  27.875  1.00 31.85           C  
ANISOU 2247  C   LEU A 295     4799   3274   4030   1250    137    891       C  
ATOM   2248  O   LEU A 295      48.477   1.646  28.663  1.00 31.65           O  
ANISOU 2248  O   LEU A 295     4803   3194   4028   1306     70    932       O  
ATOM   2249  CB  LEU A 295      47.751   4.638  29.187  1.00 30.22           C  
ANISOU 2249  CB  LEU A 295     4561   3122   3799   1055     64    955       C  
ATOM   2250  CG  LEU A 295      48.975   5.350  28.623  1.00 30.07           C  
ANISOU 2250  CG  LEU A 295     4393   3207   3823   1146     71   1030       C  
ATOM   2251  CD1 LEU A 295      48.625   6.109  27.344  1.00 31.92           C  
ANISOU 2251  CD1 LEU A 295     4570   3468   4090   1106    173   1031       C  
ATOM   2252  CD2 LEU A 295      49.540   6.285  29.679  1.00 30.42           C  
ANISOU 2252  CD2 LEU A 295     4394   3293   3873   1133     -1   1115       C  
ATOM   2253  N   VAL A 296      48.458   2.559  26.606  1.00 24.33           N  
ANISOU 2253  N   VAL A 296     3785   2382   3078   1351    226    874       N  
ATOM   2254  CA  VAL A 296      49.421   1.606  26.050  1.00 27.22           C  
ANISOU 2254  CA  VAL A 296     4102   2750   3491   1551    266    860       C  
ATOM   2255  C   VAL A 296      50.681   2.352  25.601  1.00 34.13           C  
ANISOU 2255  C   VAL A 296     4790   3794   4385   1663    292    935       C  
ATOM   2256  O   VAL A 296      50.603   3.329  24.843  1.00 31.74           O  
ANISOU 2256  O   VAL A 296     4424   3598   4037   1634    367    985       O  
ATOM   2257  CB  VAL A 296      48.848   0.870  24.834  1.00 28.70           C  
ANISOU 2257  CB  VAL A 296     4369   2886   3650   1631    393    752       C  
ATOM   2258  CG1 VAL A 296      49.801  -0.220  24.399  1.00 31.20           C  
ANISOU 2258  CG1 VAL A 296     4630   3165   4061   1840    445    684       C  
ATOM   2259  CG2 VAL A 296      47.466   0.311  25.137  1.00 29.57           C  
ANISOU 2259  CG2 VAL A 296     4640   2850   3745   1501    386    682       C  
ATOM   2260  N   ILE A 297      51.834   1.885  26.060  1.00 37.48           N  
ANISOU 2260  N   ILE A 297     5102   4249   4890   1797    230    966       N  
ATOM   2261  CA  ILE A 297      53.108   2.538  25.788  1.00 40.55           C  
ANISOU 2261  CA  ILE A 297     5256   4827   5323   1907    246   1036       C  
ATOM   2262  C   ILE A 297      54.058   1.541  25.131  1.00 39.79           C  
ANISOU 2262  C   ILE A 297     5030   4768   5321   2130    317    960       C  
ATOM   2263  O   ILE A 297      54.073   0.368  25.497  1.00 41.95           O  
ANISOU 2263  O   ILE A 297     5378   4884   5675   2202    265    905       O  
ATOM   2264  CB  ILE A 297      53.737   3.049  27.101  1.00 42.76           C  
ANISOU 2264  CB  ILE A 297     5451   5165   5630   1867     79   1134       C  
ATOM   2265  CG1 ILE A 297      52.804   4.059  27.777  1.00 41.35           C  
ANISOU 2265  CG1 ILE A 297     5391   4941   5377   1659     34   1169       C  
ATOM   2266  CG2 ILE A 297      55.106   3.666  26.857  1.00 40.03           C  
ANISOU 2266  CG2 ILE A 297     4802   5048   5361   1977     87   1201       C  
ATOM   2267  CD1 ILE A 297      53.372   4.637  29.057  1.00 40.76           C  
ANISOU 2267  CD1 ILE A 297     5236   4957   5294   1640   -120   1260       C  
ATOM   2268  N   GLU A 298      54.848   2.005  24.166  1.00 35.26           N  
ANISOU 2268  N   GLU A 298     4238   4402   4758   2232    450    955       N  
ATOM   2269  CA  GLU A 298      55.814   1.147  23.474  1.00 34.88           C  
ANISOU 2269  CA  GLU A 298     4018   4427   4809   2433    551    829       C  
ATOM   2270  C   GLU A 298      57.175   1.139  24.173  1.00 39.93           C  
ANISOU 2270  C   GLU A 298     4407   5175   5591   2525    436    881       C  
ATOM   2271  O   GLU A 298      57.741   2.195  24.449  1.00 41.39           O  
ANISOU 2271  O   GLU A 298     4401   5554   5771   2461    399    990       O  
ATOM   2272  CB  GLU A 298      55.989   1.595  22.025  1.00 35.46           C  
ANISOU 2272  CB  GLU A 298     3949   4738   4786   2444    782    753       C  
ATOM   2273  CG  GLU A 298      56.842   0.653  21.172  1.00 39.31           C  
ANISOU 2273  CG  GLU A 298     4267   5316   5354   2640    941    548       C  
ATOM   2274  CD  GLU A 298      56.908   1.093  19.713  1.00 50.48           C  
ANISOU 2274  CD  GLU A 298     5575   7022   6584   2540   1172    442       C  
ATOM   2275  OE1 GLU A 298      57.199   2.285  19.459  1.00 49.85           O  
ANISOU 2275  OE1 GLU A 298     5368   7164   6408   2348   1198    583       O  
ATOM   2276  OE2 GLU A 298      56.662   0.248  18.823  1.00 54.03           O  
ANISOU 2276  OE2 GLU A 298     6075   7478   6977   2623   1325    214       O  
ATOM   2277  N   ASN A 299      57.695  -0.057  24.441  1.00 47.89           N  
ANISOU 2277  N   ASN A 299     5393   6052   6751   2676    377    804       N  
ATOM   2278  CA  ASN A 299      58.949  -0.220  25.183  1.00 57.69           C  
ANISOU 2278  CA  ASN A 299     6399   7377   8143   2790    231    862       C  
ATOM   2279  C   ASN A 299      58.797   0.107  26.665  1.00 58.66           C  
ANISOU 2279  C   ASN A 299     6607   7463   8216   2692    -15   1037       C  
ATOM   2280  O   ASN A 299      58.097   1.052  27.032  1.00 51.38           O  
ANISOU 2280  O   ASN A 299     5797   6578   7146   2512    -45   1113       O  
ATOM   2281  CB  ASN A 299      60.070   0.632  24.578  1.00 66.50           C  
ANISOU 2281  CB  ASN A 299     7158   8823   9287   2815    334    843       C  
ATOM   2282  CG  ASN A 299      60.364   0.272  23.139  1.00 75.56           C  
ANISOU 2282  CG  ASN A 299     8184  10069  10457   2904    596    650       C  
ATOM   2283  OD1 ASN A 299      60.409  -0.906  22.777  1.00 80.33           O  
ANISOU 2283  OD1 ASN A 299     8835  10505  11181   3048    651    491       O  
ATOM   2284  ND2 ASN A 299      60.562   1.288  22.302  1.00 77.56           N  
ANISOU 2284  ND2 ASN A 299     8269  10603  10598   2800    774    656       N  
ATOM   2285  N   ALA A 300      59.462  -0.671  27.516  1.00 66.55           N  
ANISOU 2285  N   ALA A 300     7544   8399   9344   2816   -191   1098       N  
ATOM   2286  CA  ALA A 300      59.374  -0.466  28.959  1.00 68.92           C  
ANISOU 2286  CA  ALA A 300     7918   8709   9561   2737   -430   1265       C  
ATOM   2287  C   ALA A 300      60.012   0.853  29.373  1.00 67.37           C  
ANISOU 2287  C   ALA A 300     7491   8825   9282   2651   -513   1326       C  
ATOM   2288  O   ALA A 300      60.870   1.389  28.670  1.00 67.37           O  
ANISOU 2288  O   ALA A 300     7200   9038   9359   2693   -420   1264       O  
ATOM   2289  CB  ALA A 300      60.023  -1.629  29.710  1.00 75.42           C  
ANISOU 2289  CB  ALA A 300     8700   9417  10540   2914   -609   1350       C  
HETATM 2290  N   MSE A 301      59.575   1.377  30.513  1.00 65.46           N  
ANISOU 2290  N   MSE A 301     7360   8628   8886   2513   -676   1436       N  
HETATM 2291  CA  MSE A 301      60.174   2.572  31.093  1.00 62.32           C  
ANISOU 2291  CA  MSE A 301     6723   8539   8416   2419   -794   1483       C  
HETATM 2292  C   MSE A 301      60.595   2.246  32.518  1.00 61.99           C  
ANISOU 2292  C   MSE A 301     6661   8598   8293   2443  -1076   1605       C  
HETATM 2293  O   MSE A 301      60.047   1.327  33.131  1.00 56.78           O  
ANISOU 2293  O   MSE A 301     6256   7734   7585   2473  -1152   1687       O  
HETATM 2294  CB  MSE A 301      59.176   3.733  31.112  1.00 54.90           C  
ANISOU 2294  CB  MSE A 301     5911   7610   7340   2207   -723   1484       C  
HETATM 2295  CG  MSE A 301      58.380   3.916  29.835  1.00 55.36           C  
ANISOU 2295  CG  MSE A 301     6104   7503   7428   2163   -466   1407       C  
HETATM 2296 SE   MSE A 301      57.357   5.592  29.860  0.46 63.53          SE  
ANISOU 2296 SE   MSE A 301     7261   8509   8369   1784   -382   1346      SE  
HETATM 2297  CE  MSE A 301      56.908   5.656  31.738  1.00 38.36           C  
ANISOU 2297  CE  MSE A 301     4230   5344   5001   1674   -631   1388       C  
ATOM   2298  N   PRO A 302      61.563   3.004  33.055  1.00 68.02           N  
ANISOU 2298  N   PRO A 302     7105   9703   9037   2405  -1234   1620       N  
ATOM   2299  CA  PRO A 302      62.008   2.803  34.441  1.00 73.35           C  
ANISOU 2299  CA  PRO A 302     7736  10552   9581   2403  -1527   1732       C  
ATOM   2300  C   PRO A 302      60.888   3.142  35.425  1.00 71.75           C  
ANISOU 2300  C   PRO A 302     7823  10336   9101   2221  -1605   1793       C  
ATOM   2301  O   PRO A 302      60.124   4.087  35.187  1.00 67.19           O  
ANISOU 2301  O   PRO A 302     7312   9775   8443   2055  -1492   1724       O  
ATOM   2302  CB  PRO A 302      63.172   3.788  34.586  1.00 75.12           C  
ANISOU 2302  CB  PRO A 302     7519  11186   9839   2324  -1640   1661       C  
ATOM   2303  CG  PRO A 302      62.903   4.841  33.563  1.00 74.23           C  
ANISOU 2303  CG  PRO A 302     7293  11108   9802   2186  -1409   1546       C  
ATOM   2304  CD  PRO A 302      62.240   4.143  32.410  1.00 68.93           C  
ANISOU 2304  CD  PRO A 302     6867  10084   9238   2314  -1147   1528       C  
ATOM   2305  N   GLU A 303      60.789   2.369  36.503  1.00 71.44           N  
ANISOU 2305  N   GLU A 303     7948  10268   8928   2254  -1789   1931       N  
ATOM   2306  CA  GLU A 303      59.720   2.542  37.483  1.00 72.50           C  
ANISOU 2306  CA  GLU A 303     8372  10400   8776   2079  -1843   1991       C  
ATOM   2307  C   GLU A 303      59.572   4.005  37.914  1.00 67.90           C  
ANISOU 2307  C   GLU A 303     7652  10162   7984   1841  -1898   1878       C  
ATOM   2308  O   GLU A 303      58.455   4.506  38.074  1.00 63.42           O  
ANISOU 2308  O   GLU A 303     7307   9522   7268   1669  -1796   1822       O  
ATOM   2309  CB  GLU A 303      59.960   1.642  38.704  1.00 81.17           C  
ANISOU 2309  CB  GLU A 303     9572  11540   9729   2135  -2076   2176       C  
ATOM   2310  CG  GLU A 303      58.802   1.600  39.700  1.00 87.52           C  
ANISOU 2310  CG  GLU A 303    10709  12317  10229   1958  -2095   2250       C  
ATOM   2311  CD  GLU A 303      59.103   0.763  40.947  1.00100.22           C  
ANISOU 2311  CD  GLU A 303    12409  14010  11659   2007  -2331   2460       C  
ATOM   2312  OE1 GLU A 303      60.121   0.031  40.963  1.00106.46           O  
ANISOU 2312  OE1 GLU A 303    13041  14797  12612   2217  -2477   2572       O  
ATOM   2313  OE2 GLU A 303      58.317   0.842  41.920  1.00102.20           O  
ANISOU 2313  OE2 GLU A 303    12889  14342  11600   1841  -2366   2515       O  
ATOM   2314  N   ALA A 304      60.705   4.680  38.092  1.00 66.97           N  
ANISOU 2314  N   ALA A 304     7152  10407   7886   1795  -2050   1804       N  
ATOM   2315  CA  ALA A 304      60.726   6.069  38.545  1.00 62.15           C  
ANISOU 2315  CA  ALA A 304     6411  10045   7158   1444  -2076   1558       C  
ATOM   2316  C   ALA A 304      59.976   6.989  37.591  1.00 60.24           C  
ANISOU 2316  C   ALA A 304     6286   9510   7093   1238  -1764   1338       C  
ATOM   2317  O   ALA A 304      59.149   7.802  38.017  1.00 56.12           O  
ANISOU 2317  O   ALA A 304     5930   8930   6462    963  -1686   1162       O  
ATOM   2318  CB  ALA A 304      62.162   6.545  38.716  1.00 63.88           C  
ANISOU 2318  CB  ALA A 304     6174  10649   7450   1411  -2258   1476       C  
ATOM   2319  N   LEU A 305      60.275   6.857  36.300  1.00 60.12           N  
ANISOU 2319  N   LEU A 305     6170   9323   7349   1379  -1584   1352       N  
ATOM   2320  CA  LEU A 305      59.651   7.688  35.276  1.00 58.34           C  
ANISOU 2320  CA  LEU A 305     6030   8847   7290   1212  -1304   1206       C  
ATOM   2321  C   LEU A 305      58.180   7.322  35.114  1.00 55.40           C  
ANISOU 2321  C   LEU A 305     6057   8152   6840   1226  -1161   1249       C  
ATOM   2322  O   LEU A 305      57.343   8.190  34.890  1.00 54.27           O  
ANISOU 2322  O   LEU A 305     6043   7845   6731   1012  -1007   1115       O  
ATOM   2323  CB  LEU A 305      60.394   7.563  33.945  1.00 59.41           C  
ANISOU 2323  CB  LEU A 305     5947   8952   7674   1357  -1152   1230       C  
ATOM   2324  CG  LEU A 305      60.036   8.582  32.861  1.00 59.80           C  
ANISOU 2324  CG  LEU A 305     6004   8833   7886   1158   -889   1118       C  
ATOM   2325  CD1 LEU A 305      60.018   9.988  33.427  1.00 60.39           C  
ANISOU 2325  CD1 LEU A 305     6000   8964   7982    802   -898    937       C  
ATOM   2326  CD2 LEU A 305      61.010   8.494  31.702  1.00 61.12           C  
ANISOU 2326  CD2 LEU A 305     5892   9087   8243   1269   -759   1141       C  
ATOM   2327  N   THR A 306      57.865   6.039  35.250  1.00 55.96           N  
ANISOU 2327  N   THR A 306     6306   8122   6833   1476  -1215   1437       N  
ATOM   2328  CA  THR A 306      56.480   5.595  35.187  1.00 56.58           C  
ANISOU 2328  CA  THR A 306     6746   7915   6836   1475  -1092   1474       C  
ATOM   2329  C   THR A 306      55.648   6.237  36.303  1.00 57.41           C  
ANISOU 2329  C   THR A 306     7018   8069   6725   1213  -1133   1374       C  
ATOM   2330  O   THR A 306      54.504   6.640  36.081  1.00 56.30           O  
ANISOU 2330  O   THR A 306     7079   7722   6593   1078   -968   1276       O  
ATOM   2331  CB  THR A 306      56.376   4.062  35.258  1.00 54.98           C  
ANISOU 2331  CB  THR A 306     6693   7582   6614   1771  -1150   1699       C  
ATOM   2332  OG1 THR A 306      57.131   3.490  34.182  1.00 56.44           O  
ANISOU 2332  OG1 THR A 306     6729   7675   7041   1940  -1062   1668       O  
ATOM   2333  CG2 THR A 306      54.928   3.622  35.134  1.00 49.64           C  
ANISOU 2333  CG2 THR A 306     6371   6589   5899   1687   -993   1673       C  
ATOM   2334  N   GLU A 307      56.237   6.336  37.491  1.00 57.55           N  
ANISOU 2334  N   GLU A 307     6932   8389   6546   1144  -1352   1385       N  
ATOM   2335  CA  GLU A 307      55.605   6.998  38.632  1.00 57.76           C  
ANISOU 2335  CA  GLU A 307     7074   8541   6330    873  -1392   1239       C  
ATOM   2336  C   GLU A 307      55.388   8.495  38.400  1.00 55.49           C  
ANISOU 2336  C   GLU A 307     6696   8210   6180    582  -1249    928       C  
ATOM   2337  O   GLU A 307      54.308   9.021  38.694  1.00 53.59           O  
ANISOU 2337  O   GLU A 307     6638   7834   5889    402  -1120    776       O  
ATOM   2338  CB  GLU A 307      56.422   6.778  39.906  1.00 61.86           C  
ANISOU 2338  CB  GLU A 307     7464   9467   6573    857  -1682   1313       C  
ATOM   2339  CG  GLU A 307      56.058   5.509  40.657  1.00 66.85           C  
ANISOU 2339  CG  GLU A 307     8318  10124   6957   1025  -1807   1615       C  
ATOM   2340  CD  GLU A 307      56.989   5.223  41.835  1.00 75.01           C  
ANISOU 2340  CD  GLU A 307     9192  11602   7706   1051  -2133   1761       C  
ATOM   2341  OE1 GLU A 307      57.800   6.105  42.206  1.00 76.23           O  
ANISOU 2341  OE1 GLU A 307     9072  12082   7812    882  -2261   1560       O  
ATOM   2342  OE2 GLU A 307      56.910   4.105  42.387  1.00 78.99           O  
ANISOU 2342  OE2 GLU A 307     9877  12024   8112   1192  -2214   2006       O  
ATOM   2343  N   ARG A 308      56.408   9.183  37.887  1.00 52.79           N  
ANISOU 2343  N   ARG A 308     6059   7965   6035    535  -1260    836       N  
ATOM   2344  CA  ARG A 308      56.255  10.585  37.507  1.00 51.34           C  
ANISOU 2344  CA  ARG A 308     5784   7663   6060    275  -1101    585       C  
ATOM   2345  C   ARG A 308      55.118  10.721  36.499  1.00 48.21           C  
ANISOU 2345  C   ARG A 308     5597   6884   5838    305   -854    611       C  
ATOM   2346  O   ARG A 308      54.272  11.608  36.607  1.00 42.83           O  
ANISOU 2346  O   ARG A 308     5010   6031   5232    113   -723    436       O  
ATOM   2347  CB  ARG A 308      57.540  11.149  36.892  1.00 55.28           C  
ANISOU 2347  CB  ARG A 308     5935   8285   6782    241  -1116    544       C  
ATOM   2348  CG  ARG A 308      58.586  11.611  37.895  1.00 66.68           C  
ANISOU 2348  CG  ARG A 308     7106  10108   8121     73  -1330    388       C  
ATOM   2349  CD  ARG A 308      59.541  12.626  37.268  1.00 73.01           C  
ANISOU 2349  CD  ARG A 308     7583  10942   9217    -96  -1258    250       C  
ATOM   2350  NE  ARG A 308      58.896  13.925  37.075  1.00 77.19           N  
ANISOU 2350  NE  ARG A 308     8175  11202   9951   -382  -1054     25       N  
ATOM   2351  CZ  ARG A 308      59.512  15.017  36.629  1.00 81.85           C  
ANISOU 2351  CZ  ARG A 308     8531  11741  10829   -603   -951   -117       C  
ATOM   2352  NH1 ARG A 308      60.802  14.975  36.318  1.00 84.57           N  
ANISOU 2352  NH1 ARG A 308     8544  12322  11268   -588  -1027    -77       N  
ATOM   2353  NH2 ARG A 308      58.837  16.154  36.491  1.00 82.90           N  
ANISOU 2353  NH2 ARG A 308     8746  11569  11183   -838   -764   -294       N  
ATOM   2354  N   LEU A 309      55.110   9.835  35.511  1.00 48.36           N  
ANISOU 2354  N   LEU A 309     5668   6777   5927    553   -794    817       N  
ATOM   2355  CA  LEU A 309      54.135   9.916  34.437  1.00 46.78           C  
ANISOU 2355  CA  LEU A 309     5629   6276   5871    589   -586    852       C  
ATOM   2356  C   LEU A 309      52.734   9.777  35.003  1.00 44.95           C  
ANISOU 2356  C   LEU A 309     5676   5889   5515    528   -532    803       C  
ATOM   2357  O   LEU A 309      51.854  10.606  34.746  1.00 42.77           O  
ANISOU 2357  O   LEU A 309     5469   5421   5360    392   -391    691       O  
ATOM   2358  CB  LEU A 309      54.383   8.819  33.411  1.00 43.57           C  
ANISOU 2358  CB  LEU A 309     5235   5815   5504    862   -547   1039       C  
ATOM   2359  CG  LEU A 309      53.246   8.718  32.403  1.00 44.22           C  
ANISOU 2359  CG  LEU A 309     5508   5637   5657    898   -365   1071       C  
ATOM   2360  CD1 LEU A 309      53.191   9.981  31.540  1.00 42.58           C  
ANISOU 2360  CD1 LEU A 309     5190   5344   5645    742   -221   1018       C  
ATOM   2361  CD2 LEU A 309      53.411   7.465  31.563  1.00 48.55           C  
ANISOU 2361  CD2 LEU A 309     6098   6147   6203   1157   -333   1199       C  
ATOM   2362  N   THR A 310      52.540   8.711  35.766  1.00 46.09           N  
ANISOU 2362  N   THR A 310     5967   6112   5434    636   -642    907       N  
ATOM   2363  CA  THR A 310      51.255   8.420  36.379  1.00 47.28           C  
ANISOU 2363  CA  THR A 310     6376   6152   5438    574   -584    880       C  
ATOM   2364  C   THR A 310      50.733   9.615  37.175  1.00 49.55           C  
ANISOU 2364  C   THR A 310     6657   6469   5700    299   -533    620       C  
ATOM   2365  O   THR A 310      49.572  10.014  37.024  1.00 44.52           O  
ANISOU 2365  O   THR A 310     6145   5631   5141    216   -378    517       O  
ATOM   2366  CB  THR A 310      51.354   7.185  37.289  1.00 51.42           C  
ANISOU 2366  CB  THR A 310     7028   6808   5702    691   -732   1059       C  
ATOM   2367  OG1 THR A 310      51.596   6.022  36.485  1.00 55.26           O  
ANISOU 2367  OG1 THR A 310     7554   7166   6276    957   -732   1270       O  
ATOM   2368  CG2 THR A 310      50.070   6.993  38.092  1.00 48.36           C  
ANISOU 2368  CG2 THR A 310     6889   6358   5128    566   -658   1017       C  
ATOM   2369  N   ALA A 311      51.595  10.188  38.012  1.00 49.53           N  
ANISOU 2369  N   ALA A 311     6490   6723   5607    159   -662    492       N  
ATOM   2370  CA  ALA A 311      51.205  11.310  38.863  1.00 52.54           C  
ANISOU 2370  CA  ALA A 311     6848   7154   5960   -118   -612    185       C  
ATOM   2371  C   ALA A 311      50.865  12.570  38.064  1.00 51.79           C  
ANISOU 2371  C   ALA A 311     6667   6780   6230   -235   -428     14       C  
ATOM   2372  O   ALA A 311      49.866  13.240  38.340  1.00 54.18           O  
ANISOU 2372  O   ALA A 311     7054   6921   6610   -371   -287   -185       O  
ATOM   2373  CB  ALA A 311      52.294  11.605  39.907  1.00 54.12           C  
ANISOU 2373  CB  ALA A 311     6866   7731   5967   -256   -810     61       C  
ATOM   2374  N   GLU A 312      51.696  12.897  37.081  1.00 49.20           N  
ANISOU 2374  N   GLU A 312     6162   6394   6137   -180   -421    103       N  
ATOM   2375  CA  GLU A 312      51.463  14.082  36.255  1.00 52.53           C  
ANISOU 2375  CA  GLU A 312     6500   6543   6918   -284   -253     17       C  
ATOM   2376  C   GLU A 312      50.139  13.984  35.494  1.00 50.48           C  
ANISOU 2376  C   GLU A 312     6422   5986   6774   -185    -95    111       C  
ATOM   2377  O   GLU A 312      49.409  14.972  35.378  1.00 47.10           O  
ANISOU 2377  O   GLU A 312     5996   5321   6580   -299     39    -24       O  
ATOM   2378  CB  GLU A 312      52.632  14.317  35.289  1.00 59.95           C  
ANISOU 2378  CB  GLU A 312     7220   7513   8045   -244   -264    150       C  
ATOM   2379  CG  GLU A 312      52.332  15.277  34.140  1.00 69.01           C  
ANISOU 2379  CG  GLU A 312     8320   8361   9541   -292    -82    205       C  
ATOM   2380  CD  GLU A 312      52.375  16.743  34.540  1.00 80.32           C  
ANISOU 2380  CD  GLU A 312     9633   9638  11246   -563      0    -44       C  
ATOM   2381  OE1 GLU A 312      52.416  17.033  35.758  1.00 84.41           O  
ANISOU 2381  OE1 GLU A 312    10133  10277  11661   -727    -65   -324       O  
ATOM   2382  OE2 GLU A 312      52.373  17.605  33.627  1.00 83.32           O  
ANISOU 2382  OE2 GLU A 312     9937   9776  11946   -618    134     41       O  
ATOM   2383  N   ILE A 313      49.830  12.789  34.991  1.00 48.13           N  
ANISOU 2383  N   ILE A 313     6258   5695   6333     28   -117    331       N  
ATOM   2384  CA  ILE A 313      48.581  12.561  34.268  1.00 43.07           C  
ANISOU 2384  CA  ILE A 313     5772   4825   5766    119      6    413       C  
ATOM   2385  C   ILE A 313      47.395  12.784  35.197  1.00 46.03           C  
ANISOU 2385  C   ILE A 313     6278   5126   6084      4     73    221       C  
ATOM   2386  O   ILE A 313      46.448  13.498  34.857  1.00 44.79           O  
ANISOU 2386  O   ILE A 313     6134   4747   6138    -39    201    146       O  
ATOM   2387  CB  ILE A 313      48.516  11.135  33.668  1.00 39.98           C  
ANISOU 2387  CB  ILE A 313     5498   4471   5220    342    -31    630       C  
ATOM   2388  CG1 ILE A 313      49.458  11.029  32.466  1.00 36.92           C  
ANISOU 2388  CG1 ILE A 313     4971   4119   4936    461    -31    788       C  
ATOM   2389  CG2 ILE A 313      47.105  10.814  33.206  1.00 42.41           C  
ANISOU 2389  CG2 ILE A 313     5971   4591   5552    391     75    656       C  
ATOM   2390  CD1 ILE A 313      49.394   9.694  31.740  1.00 37.69           C  
ANISOU 2390  CD1 ILE A 313     5166   4224   4929    677    -36    944       C  
ATOM   2391  N   ARG A 314      47.476  12.192  36.384  1.00 43.37           N  
ANISOU 2391  N   ARG A 314     6023   4996   5462    -44    -13    151       N  
ATOM   2392  CA  ARG A 314      46.405  12.278  37.361  1.00 49.13           C  
ANISOU 2392  CA  ARG A 314     6876   5721   6070   -167     65    -36       C  
ATOM   2393  C   ARG A 314      46.135  13.719  37.821  1.00 50.01           C  
ANISOU 2393  C   ARG A 314     6878   5736   6388   -375    171   -357       C  
ATOM   2394  O   ARG A 314      45.039  14.029  38.287  1.00 45.56           O  
ANISOU 2394  O   ARG A 314     6382   5078   5852   -457    302   -543       O  
ATOM   2395  CB  ARG A 314      46.722  11.367  38.551  1.00 53.80           C  
ANISOU 2395  CB  ARG A 314     7567   6607   6270   -193    -62     -3       C  
ATOM   2396  CG  ARG A 314      45.598  11.222  39.562  1.00 61.11           C  
ANISOU 2396  CG  ARG A 314     8644   7580   6995   -322     35   -152       C  
ATOM   2397  CD  ARG A 314      45.821   9.987  40.427  1.00 69.39           C  
ANISOU 2397  CD  ARG A 314     9837   8881   7647   -288    -90     36       C  
ATOM   2398  NE  ARG A 314      45.063  10.043  41.673  1.00 77.58           N  
ANISOU 2398  NE  ARG A 314    10979  10087   8409   -482    -13   -141       N  
ATOM   2399  CZ  ARG A 314      45.076   9.087  42.597  1.00 84.09           C  
ANISOU 2399  CZ  ARG A 314    11947  11151   8850   -504    -95     23       C  
ATOM   2400  NH1 ARG A 314      45.806   7.993  42.409  1.00 84.78           N  
ANISOU 2400  NH1 ARG A 314    12088  11290   8836   -317   -265    373       N  
ATOM   2401  NH2 ARG A 314      44.360   9.224  43.710  1.00 86.42           N  
ANISOU 2401  NH2 ARG A 314    12330  11633   8873   -710      4   -156       N  
ATOM   2402  N   SER A 315      47.130  14.595  37.681  1.00 52.24           N  
ANISOU 2402  N   SER A 315     6334   6668   6845    594  -1272      7       N  
ATOM   2403  CA  SER A 315      46.991  15.992  38.093  1.00 52.34           C  
ANISOU 2403  CA  SER A 315     6349   6560   6976    370  -1405   -197       C  
ATOM   2404  C   SER A 315      46.381  16.871  37.006  1.00 46.57           C  
ANISOU 2404  C   SER A 315     5672   5512   6509    148  -1335   -153       C  
ATOM   2405  O   SER A 315      45.989  18.016  37.262  1.00 43.13           O  
ANISOU 2405  O   SER A 315     5310   4881   6197     -9  -1380   -292       O  
ATOM   2406  CB  SER A 315      48.352  16.568  38.493  1.00 58.45           C  
ANISOU 2406  CB  SER A 315     6872   7611   7724    225  -1592   -342       C  
ATOM   2407  OG  SER A 315      48.837  15.960  39.678  1.00 63.17           O  
ANISOU 2407  OG  SER A 315     7415   8547   8040    452  -1683   -417       O  
ATOM   2408  N   ARG A 316      46.321  16.335  35.791  1.00 42.69           N  
ANISOU 2408  N   ARG A 316     5150   4981   6090    159  -1214     42       N  
ATOM   2409  CA  ARG A 316      45.877  17.095  34.626  1.00 42.28           C  
ANISOU 2409  CA  ARG A 316     5109   4702   6252     -6  -1138    124       C  
ATOM   2410  C   ARG A 316      44.444  16.756  34.194  1.00 36.06           C  
ANISOU 2410  C   ARG A 316     4505   3727   5470     97  -1000    205       C  
ATOM   2411  O   ARG A 316      43.827  17.500  33.420  1.00 34.15           O  
ANISOU 2411  O   ARG A 316     4298   3309   5370      6   -937    260       O  
ATOM   2412  CB  ARG A 316      46.845  16.862  33.463  1.00 53.38           C  
ANISOU 2412  CB  ARG A 316     6321   6239   7723    -68  -1106    280       C  
ATOM   2413  CG  ARG A 316      46.628  17.789  32.278  1.00 68.07           C  
ANISOU 2413  CG  ARG A 316     8153   7912   9798   -229  -1028    382       C  
ATOM   2414  CD  ARG A 316      47.433  17.350  31.059  1.00 74.93           C  
ANISOU 2414  CD  ARG A 316     8852   8930  10690   -222   -966    571       C  
ATOM   2415  NE  ARG A 316      46.990  18.028  29.843  1.00 77.90           N  
ANISOU 2415  NE  ARG A 316     9232   9148  11219   -289   -853    709       N  
ATOM   2416  CZ  ARG A 316      47.531  19.148  29.373  1.00 83.51           C  
ANISOU 2416  CZ  ARG A 316     9832   9769  12130   -472   -829    764       C  
ATOM   2417  NH1 ARG A 316      48.548  19.719  30.017  1.00 85.84           N  
ANISOU 2417  NH1 ARG A 316     9988  10113  12513   -656   -928    655       N  
ATOM   2418  NH2 ARG A 316      47.059  19.693  28.256  1.00 84.43           N  
ANISOU 2418  NH2 ARG A 316     9966   9758  12356   -471   -696    927       N  
ATOM   2419  N   VAL A 317      43.920  15.627  34.676  1.00 29.96           N  
ANISOU 2419  N   VAL A 317     3835   3008   4542    292   -939    221       N  
ATOM   2420  CA  VAL A 317      42.587  15.175  34.272  1.00 27.88           C  
ANISOU 2420  CA  VAL A 317     3706   2604   4284    365   -806    281       C  
ATOM   2421  C   VAL A 317      41.814  14.652  35.476  1.00 30.44           C  
ANISOU 2421  C   VAL A 317     4183   2899   4485    524   -770    217       C  
ATOM   2422  O   VAL A 317      42.401  14.265  36.475  1.00 28.64           O  
ANISOU 2422  O   VAL A 317     3957   2801   4125    639   -820    166       O  
ATOM   2423  CB  VAL A 317      42.645  14.054  33.205  1.00 31.27           C  
ANISOU 2423  CB  VAL A 317     4095   3101   4686    419   -693    403       C  
ATOM   2424  CG1 VAL A 317      43.561  14.444  32.035  1.00 33.58           C  
ANISOU 2424  CG1 VAL A 317     4224   3472   5064    310   -718    493       C  
ATOM   2425  CG2 VAL A 317      43.087  12.741  33.834  1.00 32.15           C  
ANISOU 2425  CG2 VAL A 317     4244   3329   4642    597   -637    419       C  
ATOM   2426  N   SER A 318      40.490  14.662  35.373  1.00 28.81           N  
ANISOU 2426  N   SER A 318     4086   2549   4310    545   -677    232       N  
ATOM   2427  CA  SER A 318      39.640  14.054  36.380  1.00 29.65           C  
ANISOU 2427  CA  SER A 318     4328   2620   4317    701   -599    209       C  
ATOM   2428  C   SER A 318      39.942  12.563  36.542  1.00 30.31           C  
ANISOU 2428  C   SER A 318     4431   2788   4298    843   -485    275       C  
ATOM   2429  O   SER A 318      40.328  11.876  35.590  1.00 26.50           O  
ANISOU 2429  O   SER A 318     3887   2340   3842    809   -423    341       O  
ATOM   2430  CB  SER A 318      38.163  14.235  36.004  1.00 29.76           C  
ANISOU 2430  CB  SER A 318     4406   2502   4398    679   -499    239       C  
ATOM   2431  OG  SER A 318      37.361  13.396  36.817  1.00 38.55           O  
ANISOU 2431  OG  SER A 318     5624   3590   5433    818   -382    250       O  
ATOM   2432  N   THR A 319      39.744  12.055  37.750  1.00 29.85           N  
ANISOU 2432  N   THR A 319     4474   2752   4116   1025   -433    267       N  
ATOM   2433  CA  THR A 319      39.873  10.623  37.974  1.00 29.22           C  
ANISOU 2433  CA  THR A 319     4451   2699   3951   1192   -264    357       C  
ATOM   2434  C   THR A 319      38.995   9.845  36.988  1.00 25.81           C  
ANISOU 2434  C   THR A 319     4052   2121   3632   1102    -89    404       C  
ATOM   2435  O   THR A 319      39.347   8.739  36.578  1.00 26.52           O  
ANISOU 2435  O   THR A 319     4165   2203   3709   1152     48    462       O  
ATOM   2436  CB  THR A 319      39.546  10.237  39.449  1.00 36.24           C  
ANISOU 2436  CB  THR A 319     5463   3612   4695   1433   -189    372       C  
ATOM   2437  OG1 THR A 319      39.694   8.826  39.621  1.00 37.15           O  
ANISOU 2437  OG1 THR A 319     5651   3719   4744   1613     25    492       O  
ATOM   2438  CG2 THR A 319      38.117  10.643  39.822  1.00 30.52           C  
ANISOU 2438  CG2 THR A 319     4834   2735   4028   1413   -128    348       C  
ATOM   2439  N   TYR A 320      37.861  10.418  36.594  1.00 24.61           N  
ANISOU 2439  N   TYR A 320     3899   1870   3582    972    -88    367       N  
ATOM   2440  CA  TYR A 320      36.966   9.711  35.684  1.00 32.67           C  
ANISOU 2440  CA  TYR A 320     4915   2806   4692    867     56    372       C  
ATOM   2441  C   TYR A 320      37.535   9.589  34.257  1.00 33.24           C  
ANISOU 2441  C   TYR A 320     4882   2937   4811    739     21    368       C  
ATOM   2442  O   TYR A 320      37.099   8.715  33.496  1.00 29.36           O  
ANISOU 2442  O   TYR A 320     4392   2403   4358    670    149    344       O  
ATOM   2443  CB  TYR A 320      35.584  10.371  35.640  1.00 29.81           C  
ANISOU 2443  CB  TYR A 320     4541   2392   4394    787     60    345       C  
ATOM   2444  CG  TYR A 320      34.865  10.352  36.963  1.00 32.11           C  
ANISOU 2444  CG  TYR A 320     4939   2624   4638    927    135    363       C  
ATOM   2445  CD1 TYR A 320      34.276   9.186  37.437  1.00 34.47           C  
ANISOU 2445  CD1 TYR A 320     5315   2839   4944    994    350    404       C  
ATOM   2446  CD2 TYR A 320      34.796  11.494  37.756  1.00 30.11           C  
ANISOU 2446  CD2 TYR A 320     4721   2385   4335   1000     12    341       C  
ATOM   2447  CE1 TYR A 320      33.624   9.165  38.659  1.00 36.17           C  
ANISOU 2447  CE1 TYR A 320     5612   3026   5105   1137    432    445       C  
ATOM   2448  CE2 TYR A 320      34.142  11.482  38.975  1.00 25.26           C  
ANISOU 2448  CE2 TYR A 320     4211   1736   3652   1160     84    360       C  
ATOM   2449  CZ  TYR A 320      33.557  10.321  39.420  1.00 32.19           C  
ANISOU 2449  CZ  TYR A 320     5130   2577   4525   1225    289    423       C  
ATOM   2450  OH  TYR A 320      32.906  10.297  40.642  1.00 32.78           O  
ANISOU 2450  OH  TYR A 320     5249   2690   4515   1347    361    450       O  
ATOM   2451  N   GLU A 321      38.476  10.470  33.895  1.00 28.45           N  
ANISOU 2451  N   GLU A 321     4182   2426   4202    700   -141    379       N  
ATOM   2452  CA  GLU A 321      39.088  10.451  32.552  1.00 30.23           C  
ANISOU 2452  CA  GLU A 321     4298   2729   4460    610   -171    404       C  
ATOM   2453  C   GLU A 321      40.572  10.052  32.548  1.00 28.62           C  
ANISOU 2453  C   GLU A 321     4053   2632   4190    690   -199    458       C  
ATOM   2454  O   GLU A 321      41.278  10.212  31.545  1.00 32.11           O  
ANISOU 2454  O   GLU A 321     4389   3163   4649    637   -241    500       O  
ATOM   2455  CB  GLU A 321      38.863  11.799  31.845  1.00 26.75           C  
ANISOU 2455  CB  GLU A 321     3755   2314   4094    493   -288    413       C  
ATOM   2456  CG  GLU A 321      37.374  12.096  31.717  1.00 30.06           C  
ANISOU 2456  CG  GLU A 321     4192   2681   4549    450   -241    384       C  
ATOM   2457  CD  GLU A 321      37.061  13.394  31.024  1.00 35.38           C  
ANISOU 2457  CD  GLU A 321     4784   3379   5280    391   -314    428       C  
ATOM   2458  OE1 GLU A 321      37.929  13.933  30.298  1.00 37.56           O  
ANISOU 2458  OE1 GLU A 321     4976   3706   5589    351   -372    486       O  
ATOM   2459  OE2 GLU A 321      35.921  13.862  31.208  1.00 37.77           O  
ANISOU 2459  OE2 GLU A 321     5106   3653   5594    401   -288    423       O  
ATOM   2460  N   ASN A 322      41.016   9.524  33.682  1.00 28.18           N  
ANISOU 2460  N   ASN A 322     4071   2596   4041    846   -165    475       N  
ATOM   2461  CA  ASN A 322      42.375   9.053  33.903  1.00 27.66           C  
ANISOU 2461  CA  ASN A 322     3958   2679   3872    979   -177    541       C  
ATOM   2462  C   ASN A 322      42.470   7.573  33.486  1.00 30.98           C  
ANISOU 2462  C   ASN A 322     4476   3046   4249   1095     38    598       C  
ATOM   2463  O   ASN A 322      41.653   6.759  33.920  1.00 33.63           O  
ANISOU 2463  O   ASN A 322     4961   3229   4590   1157    213    587       O  
ATOM   2464  CB  ASN A 322      42.665   9.205  35.406  1.00 33.85           C  
ANISOU 2464  CB  ASN A 322     4777   3545   4541   1134   -233    529       C  
ATOM   2465  CG  ASN A 322      44.110   8.969  35.759  1.00 44.72           C  
ANISOU 2465  CG  ASN A 322     6048   5161   5781   1277   -294    589       C  
ATOM   2466  OD1 ASN A 322      44.977   8.944  34.890  1.00 49.14           O  
ANISOU 2466  OD1 ASN A 322     6486   5828   6356   1230   -326    642       O  
ATOM   2467  ND2 ASN A 322      44.382   8.788  37.050  1.00 51.95           N  
ANISOU 2467  ND2 ASN A 322     6996   6201   6542   1476   -307    591       N  
ATOM   2468  N   PRO A 323      43.452   7.215  32.636  1.00 30.29           N  
ANISOU 2468  N   PRO A 323     4315   3065   4129   1123     50    661       N  
ATOM   2469  CA  PRO A 323      43.644   5.798  32.280  1.00 29.76           C  
ANISOU 2469  CA  PRO A 323     4372   2925   4009   1260    276    710       C  
ATOM   2470  C   PRO A 323      43.759   4.934  33.540  1.00 34.25           C  
ANISOU 2470  C   PRO A 323     5083   3458   4474   1507    434    783       C  
ATOM   2471  O   PRO A 323      44.509   5.299  34.444  1.00 31.10           O  
ANISOU 2471  O   PRO A 323     4607   3249   3959   1650    329    843       O  
ATOM   2472  CB  PRO A 323      44.983   5.802  31.538  1.00 29.49           C  
ANISOU 2472  CB  PRO A 323     4207   3090   3910   1321    222    801       C  
ATOM   2473  CG  PRO A 323      45.079   7.207  30.949  1.00 30.36           C  
ANISOU 2473  CG  PRO A 323     4126   3301   4110   1113     -2    771       C  
ATOM   2474  CD  PRO A 323      44.392   8.111  31.931  1.00 32.31           C  
ANISOU 2474  CD  PRO A 323     4377   3492   4405   1030   -120    695       C  
ATOM   2475  N   LYS A 324      43.044   3.812  33.592  1.00 38.26           N  
ANISOU 2475  N   LYS A 324     5783   3736   5017   1560    693    775       N  
ATOM   2476  CA  LYS A 324      42.965   3.006  34.821  1.00 37.98           C  
ANISOU 2476  CA  LYS A 324     5887   3650   4895   1777    882    857       C  
ATOM   2477  C   LYS A 324      44.050   1.944  34.887  1.00 40.77           C  
ANISOU 2477  C   LYS A 324     6281   4113   5097   1985   1048    972       C  
ATOM   2478  O   LYS A 324      44.174   1.214  35.873  1.00 45.07           O  
ANISOU 2478  O   LYS A 324     6902   4704   5519   2141   1207   1048       O  
ATOM   2479  CB  LYS A 324      41.596   2.339  34.941  1.00 41.71           C  
ANISOU 2479  CB  LYS A 324     6485   3883   5481   1619   1074    764       C  
ATOM   2480  CG  LYS A 324      40.431   3.302  34.872  1.00 46.21           C  
ANISOU 2480  CG  LYS A 324     7009   4366   6185   1422    942    658       C  
ATOM   2481  CD  LYS A 324      40.341   4.159  36.116  1.00 48.97           C  
ANISOU 2481  CD  LYS A 324     7314   4835   6458   1518    799    692       C  
ATOM   2482  CE  LYS A 324      39.246   5.202  35.981  1.00 48.63           C  
ANISOU 2482  CE  LYS A 324     7224   4721   6531   1336    666    598       C  
ATOM   2483  NZ  LYS A 324      39.155   6.019  37.216  1.00 52.36           N  
ANISOU 2483  NZ  LYS A 324     7688   5287   6918   1452    542    616       N  
ATOM   2484  N   HIS A 325      44.820   1.837  33.816  1.00 35.32           N  
ANISOU 2484  N   HIS A 325     5545   3472   4401   2004   1032   1002       N  
ATOM   2485  CA  HIS A 325      45.918   0.895  33.767  1.00 35.30           C  
ANISOU 2485  CA  HIS A 325     5573   3597   4242   2214   1187   1122       C  
ATOM   2486  C   HIS A 325      46.873   1.336  32.674  1.00 34.61           C  
ANISOU 2486  C   HIS A 325     5343   3668   4140   2237   1052   1171       C  
ATOM   2487  O   HIS A 325      46.458   1.927  31.675  1.00 34.79           O  
ANISOU 2487  O   HIS A 325     5308   3618   4291   2030    936   1077       O  
ATOM   2488  CB  HIS A 325      45.402  -0.508  33.471  1.00 42.29           C  
ANISOU 2488  CB  HIS A 325     6681   4225   5161   2184   1512   1090       C  
ATOM   2489  CG  HIS A 325      46.421  -1.579  33.698  1.00 51.46           C  
ANISOU 2489  CG  HIS A 325     7923   5494   6135   2432   1727   1243       C  
ATOM   2490  ND1 HIS A 325      47.151  -2.142  32.673  1.00 56.46           N  
ANISOU 2490  ND1 HIS A 325     8598   6130   6724   2500   1826   1278       N  
ATOM   2491  CD2 HIS A 325      46.847  -2.175  34.838  1.00 56.06           C  
ANISOU 2491  CD2 HIS A 325     8557   6203   6539   2652   1876   1384       C  
ATOM   2492  CE1 HIS A 325      47.975  -3.050  33.169  1.00 59.57           C  
ANISOU 2492  CE1 HIS A 325     9072   6637   6926   2743   2030   1439       C  
ATOM   2493  NE2 HIS A 325      47.812  -3.086  34.481  1.00 61.28           N  
ANISOU 2493  NE2 HIS A 325     9293   6937   7055   2842   2067   1509       N  
ATOM   2494  N   ILE A 326      48.154   1.075  32.873  1.00 36.57           N  
ANISOU 2494  N   ILE A 326     5494   4191   4209   2447   1059   1308       N  
ATOM   2495  CA  ILE A 326      49.141   1.356  31.847  1.00 40.01           C  
ANISOU 2495  CA  ILE A 326     5774   4816   4613   2475    964   1379       C  
ATOM   2496  C   ILE A 326      49.757   0.039  31.409  1.00 42.92           C  
ANISOU 2496  C   ILE A 326     6286   5163   4860   2651   1244   1454       C  
ATOM   2497  O   ILE A 326      50.332  -0.687  32.219  1.00 43.41           O  
ANISOU 2497  O   ILE A 326     6397   5348   4750   2856   1397   1555       O  
ATOM   2498  CB  ILE A 326      50.228   2.323  32.350  1.00 42.22           C  
ANISOU 2498  CB  ILE A 326     5755   5498   4788   2531    703   1466       C  
ATOM   2499  CG1 ILE A 326      49.595   3.664  32.739  1.00 44.25           C  
ANISOU 2499  CG1 ILE A 326     5888   5755   5171   2292    431   1347       C  
ATOM   2500  CG2 ILE A 326      51.318   2.512  31.289  1.00 38.94           C  
ANISOU 2500  CG2 ILE A 326     5152   5307   4337   2541    638   1558       C  
ATOM   2501  CD1 ILE A 326      50.581   4.695  33.233  1.00 49.96           C  
ANISOU 2501  CD1 ILE A 326     6310   6848   5824   2258    163   1365       C  
ATOM   2502  N   TYR A 327      49.592  -0.283  30.132  1.00 38.47           N  
ANISOU 2502  N   TYR A 327     5808   4438   4371   2588   1326   1405       N  
ATOM   2503  CA  TYR A 327      50.169  -1.491  29.560  1.00 41.47           C  
ANISOU 2503  CA  TYR A 327     6346   4774   4636   2750   1591   1465       C  
ATOM   2504  C   TYR A 327      51.423  -1.121  28.794  1.00 43.35           C  
ANISOU 2504  C   TYR A 327     6373   5329   4767   2861   1484   1589       C  
ATOM   2505  O   TYR A 327      51.456  -0.096  28.116  1.00 39.04           O  
ANISOU 2505  O   TYR A 327     5632   4890   4312   2729   1255   1575       O  
ATOM   2506  CB  TYR A 327      49.196  -2.146  28.585  1.00 42.24           C  
ANISOU 2506  CB  TYR A 327     6681   4499   4869   2606   1760   1295       C  
ATOM   2507  CG  TYR A 327      47.970  -2.751  29.219  1.00 41.58           C  
ANISOU 2507  CG  TYR A 327     6800   4099   4898   2452   1918   1165       C  
ATOM   2508  CD1 TYR A 327      47.999  -4.036  29.739  1.00 45.15           C  
ANISOU 2508  CD1 TYR A 327     7465   4416   5274   2546   2211   1226       C  
ATOM   2509  CD2 TYR A 327      46.774  -2.049  29.270  1.00 38.78           C  
ANISOU 2509  CD2 TYR A 327     6414   3593   4726   2208   1787   1002       C  
ATOM   2510  CE1 TYR A 327      46.876  -4.600  30.312  1.00 44.02           C  
ANISOU 2510  CE1 TYR A 327     7471   4005   5248   2386   2364   1131       C  
ATOM   2511  CE2 TYR A 327      45.647  -2.604  29.835  1.00 39.06           C  
ANISOU 2511  CE2 TYR A 327     6593   3381   4867   2048   1931    891       C  
ATOM   2512  CZ  TYR A 327      45.707  -3.883  30.359  1.00 43.37           C  
ANISOU 2512  CZ  TYR A 327     7324   3806   5348   2133   2218    958       C  
ATOM   2513  OH  TYR A 327      44.584  -4.438  30.932  1.00 48.59           O  
ANISOU 2513  OH  TYR A 327     8096   4239   6126   1971   2371    874       O  
ATOM   2514  N   PHE A 328      52.449  -1.956  28.888  1.00 40.83           N  
ANISOU 2514  N   PHE A 328     6088   5173   4251   3095   1664   1727       N  
ATOM   2515  CA  PHE A 328      53.667  -1.739  28.115  1.00 44.61           C  
ANISOU 2515  CA  PHE A 328     6368   5962   4620   3201   1606   1848       C  
ATOM   2516  C   PHE A 328      53.804  -2.843  27.085  1.00 48.76           C  
ANISOU 2516  C   PHE A 328     7139   6316   5072   3327   1873   1861       C  
ATOM   2517  O   PHE A 328      53.723  -4.019  27.428  1.00 51.17           O  
ANISOU 2517  O   PHE A 328     7716   6443   5283   3457   2150   1894       O  
ATOM   2518  CB  PHE A 328      54.900  -1.739  29.025  1.00 51.11           C  
ANISOU 2518  CB  PHE A 328     6993   7184   5244   3391   1594   2003       C  
ATOM   2519  CG  PHE A 328      54.983  -0.543  29.932  1.00 53.71           C  
ANISOU 2519  CG  PHE A 328     7044   7742   5622   3263   1292   1980       C  
ATOM   2520  CD1 PHE A 328      55.644   0.608  29.521  1.00 52.70           C  
ANISOU 2520  CD1 PHE A 328     6586   7890   5548   3116   1022   2006       C  
ATOM   2521  CD2 PHE A 328      54.401  -0.569  31.193  1.00 54.81           C  
ANISOU 2521  CD2 PHE A 328     7260   7816   5748   3280   1290   1934       C  
ATOM   2522  CE1 PHE A 328      55.718   1.715  30.347  1.00 54.61           C  
ANISOU 2522  CE1 PHE A 328     6591   8323   5836   2975    747   1968       C  
ATOM   2523  CE2 PHE A 328      54.468   0.535  32.029  1.00 57.74           C  
ANISOU 2523  CE2 PHE A 328     7396   8397   6144   3174   1008   1894       C  
ATOM   2524  CZ  PHE A 328      55.129   1.680  31.605  1.00 56.42           C  
ANISOU 2524  CZ  PHE A 328     6911   8491   6036   3014    731   1902       C  
ATOM   2525  N   ALA A 329      54.016  -2.467  25.829  1.00 48.72           N  
ANISOU 2525  N   ALA A 329     7046   6366   5101   3286   1794   1848       N  
ATOM   2526  CA  ALA A 329      54.238  -3.438  24.761  1.00 53.54           C  
ANISOU 2526  CA  ALA A 329     7879   6846   5616   3424   2023   1855       C  
ATOM   2527  C   ALA A 329      55.664  -3.344  24.238  1.00 57.72           C  
ANISOU 2527  C   ALA A 329     8200   7766   5963   3605   2020   2041       C  
ATOM   2528  O   ALA A 329      56.200  -2.248  24.056  1.00 59.36           O  
ANISOU 2528  O   ALA A 329     8061   8280   6215   3508   1782   2096       O  
ATOM   2529  CB  ALA A 329      53.241  -3.211  23.623  1.00 50.54           C  
ANISOU 2529  CB  ALA A 329     7597   6211   5396   3265   1978   1653       C  
ATOM   2530  N   LYS A 330      56.272  -4.494  23.971  1.00 62.13           N  
ANISOU 2530  N   LYS A 330     8977   8299   6328   3839   2289   2147       N  
ATOM   2531  CA  LYS A 330      57.628  -4.523  23.435  1.00 63.45           C  
ANISOU 2531  CA  LYS A 330     8967   8836   6305   4034   2334   2324       C  
ATOM   2532  C   LYS A 330      57.700  -3.802  22.093  1.00 63.62           C  
ANISOU 2532  C   LYS A 330     8826   8956   6391   3945   2189   2289       C  
ATOM   2533  O   LYS A 330      58.611  -3.006  21.854  1.00 65.22           O  
ANISOU 2533  O   LYS A 330     8673   9528   6580   3922   2052   2391       O  
ATOM   2534  CB  LYS A 330      58.129  -5.964  23.307  1.00 69.16           C  
ANISOU 2534  CB  LYS A 330     9997   9412   6870   4269   2599   2423       C  
ATOM   2535  N   ALA A 331      56.730  -4.075  21.223  1.00 59.31           N  
ANISOU 2535  N   ALA A 331     8530   8078   5928   3881   2221   2135       N  
ATOM   2536  CA  ALA A 331      56.638  -3.399  19.934  1.00 54.01           C  
ANISOU 2536  CA  ALA A 331     7721   7501   5298   3822   2092   2089       C  
ATOM   2537  C   ALA A 331      55.182  -3.270  19.496  1.00 50.23           C  
ANISOU 2537  C   ALA A 331     7403   6678   5002   3654   2043   1816       C  
ATOM   2538  O   ALA A 331      54.395  -4.217  19.625  1.00 49.60           O  
ANISOU 2538  O   ALA A 331     7661   6221   4966   3619   2221   1616       O  
ATOM   2539  CB  ALA A 331      57.459  -4.134  18.867  1.00 59.52           C  
ANISOU 2539  CB  ALA A 331     8545   8293   5777   4065   2265   2200       C  
ATOM   2540  N   PHE A 332      54.818  -2.085  19.011  1.00 45.20           N  
ANISOU 2540  N   PHE A 332     6507   6184   4485   3503   1808   1791       N  
ATOM   2541  CA  PHE A 332      53.471  -1.870  18.499  1.00 44.99           C  
ANISOU 2541  CA  PHE A 332     6576   5946   4574   3198   1725   1476       C  
ATOM   2542  C   PHE A 332      53.328  -2.582  17.164  1.00 47.60           C  
ANISOU 2542  C   PHE A 332     7098   6219   4770   3293   1873   1306       C  
ATOM   2543  O   PHE A 332      54.232  -2.540  16.344  1.00 46.69           O  
ANISOU 2543  O   PHE A 332     6886   6351   4504   3515   1904   1474       O  
ATOM   2544  CB  PHE A 332      53.179  -0.383  18.307  1.00 40.59           C  
ANISOU 2544  CB  PHE A 332     5689   5601   4134   2925   1418   1507       C  
ATOM   2545  CG  PHE A 332      52.916   0.359  19.588  1.00 43.23           C  
ANISOU 2545  CG  PHE A 332     5888   5912   4627   2741   1255   1550       C  
ATOM   2546  CD1 PHE A 332      52.819  -0.319  20.802  1.00 43.22           C  
ANISOU 2546  CD1 PHE A 332     6054   5722   4645   2817   1371   1542       C  
ATOM   2547  CD2 PHE A 332      52.746   1.740  19.575  1.00 42.21           C  
ANISOU 2547  CD2 PHE A 332     5478   5938   4622   2509   1005   1599       C  
ATOM   2548  CE1 PHE A 332      52.572   0.373  21.987  1.00 40.14           C  
ANISOU 2548  CE1 PHE A 332     5542   5337   4371   2670   1214   1569       C  
ATOM   2549  CE2 PHE A 332      52.497   2.439  20.750  1.00 41.77           C  
ANISOU 2549  CE2 PHE A 332     5318   5850   4702   2342    858   1610       C  
ATOM   2550  CZ  PHE A 332      52.412   1.753  21.960  1.00 40.25           C  
ANISOU 2550  CZ  PHE A 332     5284   5506   4505   2424    950   1586       C  
ATOM   2551  N   ALA A 333      52.188  -3.231  16.958  1.00 54.35           N  
ANISOU 2551  N   ALA A 333     8214   6761   5676   3118   1964    961       N  
ATOM   2552  CA  ALA A 333      51.860  -3.822  15.668  1.00 56.51           C  
ANISOU 2552  CA  ALA A 333     8657   6992   5823   3139   2063    710       C  
ATOM   2553  C   ALA A 333      51.607  -2.720  14.660  1.00 54.71           C  
ANISOU 2553  C   ALA A 333     8144   7088   5554   3005   1807    694       C  
ATOM   2554  O   ALA A 333      51.019  -1.687  14.987  1.00 51.21           O  
ANISOU 2554  O   ALA A 333     7481   6728   5246   2759   1580    705       O  
ATOM   2555  CB  ALA A 333      50.638  -4.714  15.784  1.00 59.39           C  
ANISOU 2555  CB  ALA A 333     9327   6956   6282   2919   2205    312       C  
ATOM   2556  N   LYS A 334      52.051  -2.935  13.427  1.00 57.12           N  
ANISOU 2556  N   LYS A 334     8465   7579   5660   3197   1863    682       N  
ATOM   2557  CA  LYS A 334      51.888  -1.916  12.406  1.00 58.83           C  
ANISOU 2557  CA  LYS A 334     8414   8132   5805   3139   1657    712       C  
ATOM   2558  C   LYS A 334      51.195  -2.444  11.158  1.00 58.45           C  
ANISOU 2558  C   LYS A 334     8513   8114   5582   3126   1695    359       C  
ATOM   2559  O   LYS A 334      51.387  -3.598  10.769  1.00 62.34           O  
ANISOU 2559  O   LYS A 334     9295   8448   5943   3286   1914    181       O  
ATOM   2560  CB  LYS A 334      53.233  -1.278  12.066  1.00 62.66           C  
ANISOU 2560  CB  LYS A 334     8648   8957   6203   3402   1634   1130       C  
ATOM   2561  CG  LYS A 334      53.381   0.110  12.646  1.00 64.20           C  
ANISOU 2561  CG  LYS A 334     8497   9317   6578   3234   1415   1389       C  
ATOM   2562  CD  LYS A 334      54.738   0.303  13.278  1.00 68.52           C  
ANISOU 2562  CD  LYS A 334     8880  10007   7147   3419   1453   1762       C  
ATOM   2563  CE  LYS A 334      54.755   1.571  14.114  1.00 70.94           C  
ANISOU 2563  CE  LYS A 334     8893  10388   7673   3180   1243   1928       C  
ATOM   2564  NZ  LYS A 334      56.007   1.683  14.911  1.00 74.72           N  
ANISOU 2564  NZ  LYS A 334     9207  11002   8180   3228   1268   2172       N  
ATOM   2565  N   THR A 335      50.374  -1.594  10.555  1.00 54.97           N  
ANISOU 2565  N   THR A 335     7872   7884   5132   2945   1488    248       N  
ATOM   2566  CA  THR A 335      49.669  -1.934   9.326  1.00 62.49           C  
ANISOU 2566  CA  THR A 335     8892   8971   5882   2931   1474    -95       C  
ATOM   2567  C   THR A 335      50.647  -1.975   8.155  1.00 67.34           C  
ANISOU 2567  C   THR A 335     9467   9891   6229   3293   1545     72       C  
ATOM   2568  O   THR A 335      51.862  -1.888   8.348  1.00 61.73           O  
ANISOU 2568  O   THR A 335     8703   9245   5508   3542   1635    440       O  
ATOM   2569  CB  THR A 335      48.588  -0.900   9.009  1.00 60.79           C  
ANISOU 2569  CB  THR A 335     8425   8979   5695   2700   1230   -191       C  
ATOM   2570  OG1 THR A 335      49.213   0.325   8.611  1.00 61.61           O  
ANISOU 2570  OG1 THR A 335     8224   9417   5766   2850   1115    204       O  
ATOM   2571  CG2 THR A 335      47.706  -0.654  10.234  1.00 59.48           C  
ANISOU 2571  CG2 THR A 335     8248   8551   5799   2371   1148   -273       C  
ATOM   2572  N   GLN A 336      50.121  -2.106   6.942  1.00 74.17           N  
ANISOU 2572  N   GLN A 336    10339  10980   6861   3334   1504   -196       N  
ATOM   2573  CA  GLN A 336      50.974  -2.112   5.758  1.00 82.00           C  
ANISOU 2573  CA  GLN A 336    11289  12299   7569   3702   1571    -43       C  
ATOM   2574  C   GLN A 336      51.360  -0.692   5.362  1.00 79.61           C  
ANISOU 2574  C   GLN A 336    10605  12386   7258   3805   1421    376       C  
ATOM   2575  O   GLN A 336      52.294  -0.475   4.587  1.00 83.62           O  
ANISOU 2575  O   GLN A 336    11012  13169   7589   4129   1490    655       O  
ATOM   2576  CB  GLN A 336      50.279  -2.810   4.593  1.00 90.91           C  
ANISOU 2576  CB  GLN A 336    12573  13553   8417   3730   1586   -511       C  
ATOM   2577  CG  GLN A 336      50.637  -4.270   4.448  1.00 97.71           C  
ANISOU 2577  CG  GLN A 336    13805  14088   9232   3793   1796   -756       C  
ATOM   2578  CD  GLN A 336      50.336  -4.793   3.059  1.00103.20           C  
ANISOU 2578  CD  GLN A 336    14569  14974   9669   3842   1763  -1093       C  
ATOM   2579  OE1 GLN A 336      51.218  -5.317   2.376  1.00107.35           O  
ANISOU 2579  OE1 GLN A 336    15194  15525  10069   4089   1858   -981       O  
ATOM   2580  NE2 GLN A 336      49.086  -4.648   2.630  1.00102.32           N  
ANISOU 2580  NE2 GLN A 336    14387  15022   9467   3611   1616  -1508       N  
ATOM   2581  N   THR A 337      50.625   0.271   5.901  1.00 72.28           N  
ANISOU 2581  N   THR A 337     9473  11460   6528   3535   1240    424       N  
ATOM   2582  CA  THR A 337      50.892   1.678   5.659  1.00 69.05           C  
ANISOU 2582  CA  THR A 337     8727  11339   6172   3589   1125    817       C  
ATOM   2583  C   THR A 337      51.768   2.285   6.769  1.00 64.00           C  
ANISOU 2583  C   THR A 337     7956  10549   5812   3531   1132   1211       C  
ATOM   2584  O   THR A 337      51.985   3.498   6.806  1.00 59.98           O  
ANISOU 2584  O   THR A 337     7178  10185   5427   3501   1051   1528       O  
ATOM   2585  CB  THR A 337      49.576   2.451   5.556  1.00 73.43           C  
ANISOU 2585  CB  THR A 337     9134  12001   6764   3357    940    655       C  
ATOM   2586  OG1 THR A 337      48.763   2.147   6.696  1.00 78.35           O  
ANISOU 2586  OG1 THR A 337     9878  12278   7615   3021    885    411       O  
ATOM   2587  CG2 THR A 337      48.824   2.046   4.293  1.00 76.95           C  
ANISOU 2587  CG2 THR A 337     9616  12742   6880   3460    907    312       C  
ATOM   2588  N   ASP A 338      52.269   1.422   7.654  1.00 60.04           N  
ANISOU 2588  N   ASP A 338     7648   9764   5400   3525   1243   1180       N  
ATOM   2589  CA  ASP A 338      53.127   1.796   8.783  1.00 58.70           C  
ANISOU 2589  CA  ASP A 338     7368   9483   5454   3486   1250   1497       C  
ATOM   2590  C   ASP A 338      52.400   2.589   9.868  1.00 54.20           C  
ANISOU 2590  C   ASP A 338     6696   8740   5160   3145   1087   1475       C  
ATOM   2591  O   ASP A 338      52.993   3.421  10.563  1.00 51.36           O  
ANISOU 2591  O   ASP A 338     6132   8400   4982   3077   1026   1760       O  
ATOM   2592  CB  ASP A 338      54.385   2.545   8.342  1.00 61.66           C  
ANISOU 2592  CB  ASP A 338     7470  10153   5804   3706   1282   1948       C  
ATOM   2593  CG  ASP A 338      55.505   2.438   9.371  1.00 62.64           C  
ANISOU 2593  CG  ASP A 338     7536  10200   6063   3711   1346   2188       C  
ATOM   2594  OD1 ASP A 338      55.543   1.411  10.083  1.00 59.34           O  
ANISOU 2594  OD1 ASP A 338     7351   9561   5633   3779   1437   2061       O  
ATOM   2595  OD2 ASP A 338      56.342   3.362   9.471  1.00 63.66           O  
ANISOU 2595  OD2 ASP A 338     7406  10453   6329   3518   1341   2396       O  
ATOM   2596  N   LYS A 339      51.110   2.323  10.007  1.00 50.65           N  
ANISOU 2596  N   LYS A 339     6381   8129   4733   2928   1021   1120       N  
ATOM   2597  CA  LYS A 339      50.331   2.932  11.064  1.00 48.53           C  
ANISOU 2597  CA  LYS A 339     6057   7678   4704   2628    889   1070       C  
ATOM   2598  C   LYS A 339      50.179   1.926  12.201  1.00 45.81           C  
ANISOU 2598  C   LYS A 339     5961   6984   4461   2533    979    893       C  
ATOM   2599  O   LYS A 339      50.142   0.711  11.970  1.00 48.82           O  
ANISOU 2599  O   LYS A 339     6599   7226   4725   2624   1135    675       O  
ATOM   2600  CB  LYS A 339      48.971   3.367  10.515  1.00 48.25           C  
ANISOU 2600  CB  LYS A 339     5970   7733   4630   2463    764    833       C  
ATOM   2601  CG  LYS A 339      49.097   4.231   9.264  1.00 50.74           C  
ANISOU 2601  CG  LYS A 339     6068   8421   4791   2631    718   1012       C  
ATOM   2602  CD  LYS A 339      47.750   4.566   8.666  1.00 50.02           C  
ANISOU 2602  CD  LYS A 339     5917   8486   4602   2524    605    774       C  
ATOM   2603  CE  LYS A 339      47.917   5.380   7.378  1.00 51.25           C  
ANISOU 2603  CE  LYS A 339     5863   9045   4564   2761    590    985       C  
ATOM   2604  NZ  LYS A 339      46.584   5.752   6.801  1.00 51.84           N  
ANISOU 2604  NZ  LYS A 339     5848   9341   4509   2696    475    774       N  
ATOM   2605  N   ILE A 340      50.123   2.425  13.428  1.00 45.43           N  
ANISOU 2605  N   ILE A 340     5849   6787   4627   2368    902    994       N  
ATOM   2606  CA  ILE A 340      49.882   1.559  14.571  1.00 42.54           C  
ANISOU 2606  CA  ILE A 340     5704   6102   4356   2293    994    854       C  
ATOM   2607  C   ILE A 340      48.565   0.824  14.364  1.00 40.90           C  
ANISOU 2607  C   ILE A 340     5702   5704   4135   2119   1034    453       C  
ATOM   2608  O   ILE A 340      47.521   1.448  14.189  1.00 41.63           O  
ANISOU 2608  O   ILE A 340     5689   5852   4277   1914    891    314       O  
ATOM   2609  CB  ILE A 340      49.808   2.368  15.887  1.00 44.99           C  
ANISOU 2609  CB  ILE A 340     5890   6324   4879   2124    869    987       C  
ATOM   2610  CG1 ILE A 340      51.135   3.082  16.144  1.00 49.26           C  
ANISOU 2610  CG1 ILE A 340     6203   7066   5448   2250    824   1343       C  
ATOM   2611  CG2 ILE A 340      49.464   1.458  17.079  1.00 40.79           C  
ANISOU 2611  CG2 ILE A 340     5592   5477   4428   2075    980    852       C  
ATOM   2612  CD1 ILE A 340      51.043   4.176  17.185  1.00 47.23           C  
ANISOU 2612  CD1 ILE A 340     5771   6787   5389   2052    659   1448       C  
ATOM   2613  N   ASP A 341      48.612  -0.501  14.356  1.00 44.47           N  
ANISOU 2613  N   ASP A 341     6440   5936   4520   2203   1242    265       N  
ATOM   2614  CA  ASP A 341      47.383  -1.267  14.452  1.00 48.82           C  
ANISOU 2614  CA  ASP A 341     7192   6233   5124   1979   1309   -125       C  
ATOM   2615  C   ASP A 341      47.073  -1.368  15.937  1.00 47.49           C  
ANISOU 2615  C   ASP A 341     7100   5777   5167   1849   1346    -82       C  
ATOM   2616  O   ASP A 341      47.610  -2.238  16.628  1.00 51.43           O  
ANISOU 2616  O   ASP A 341     7810   6040   5691   1989   1554    -17       O  
ATOM   2617  CB  ASP A 341      47.560  -2.659  13.860  1.00 53.91           C  
ANISOU 2617  CB  ASP A 341     8142   6702   5637   2106   1556   -358       C  
ATOM   2618  CG  ASP A 341      46.238  -3.400  13.697  1.00 57.24           C  
ANISOU 2618  CG  ASP A 341     8734   6902   6111   1823   1616   -821       C  
ATOM   2619  OD1 ASP A 341      45.304  -3.164  14.495  1.00 54.61           O  
ANISOU 2619  OD1 ASP A 341     8359   6427   5962   1561   1550   -913       O  
ATOM   2620  OD2 ASP A 341      46.137  -4.229  12.772  1.00 57.39           O  
ANISOU 2620  OD2 ASP A 341     8925   6895   5986   1859   1736  -1105       O  
ATOM   2621  N   LYS A 342      46.226  -0.471  16.433  1.00 47.03           N  
ANISOU 2621  N   LYS A 342     6874   5753   5243   1618   1162    -97       N  
ATOM   2622  CA  LYS A 342      45.940  -0.417  17.865  1.00 45.89           C  
ANISOU 2622  CA  LYS A 342     6775   5381   5282   1517   1176    -32       C  
ATOM   2623  C   LYS A 342      45.207  -1.656  18.348  1.00 46.42           C  
ANISOU 2623  C   LYS A 342     7128   5078   5430   1410   1399   -292       C  
ATOM   2624  O   LYS A 342      45.580  -2.247  19.362  1.00 42.56           O  
ANISOU 2624  O   LYS A 342     6804   4357   5010   1516   1568   -181       O  
ATOM   2625  CB  LYS A 342      45.163   0.847  18.214  1.00 42.79           C  
ANISOU 2625  CB  LYS A 342     6151   5107   4999   1312    941      3       C  
ATOM   2626  CG  LYS A 342      45.955   2.110  17.916  1.00 44.18           C  
ANISOU 2626  CG  LYS A 342     6066   5574   5145   1406    765    291       C  
ATOM   2627  CD  LYS A 342      45.154   3.361  18.208  1.00 42.60           C  
ANISOU 2627  CD  LYS A 342     5677   5453   5058   1221    570    320       C  
ATOM   2628  CE  LYS A 342      45.900   4.600  17.712  1.00 41.62           C  
ANISOU 2628  CE  LYS A 342     5310   5584   4919   1300    441    589       C  
ATOM   2629  NZ  LYS A 342      45.072   5.822  17.844  1.00 37.03           N  
ANISOU 2629  NZ  LYS A 342     4574   5059   4436   1145    289    614       N  
ATOM   2630  N   ARG A 343      44.173  -2.048  17.613  1.00 50.22           N  
ANISOU 2630  N   ARG A 343     7657   5523   5900   1205   1410   -636       N  
ATOM   2631  CA  ARG A 343      43.412  -3.253  17.920  1.00 54.13           C  
ANISOU 2631  CA  ARG A 343     8418   5651   6499   1048   1644   -930       C  
ATOM   2632  C   ARG A 343      44.299  -4.506  17.997  1.00 50.03           C  
ANISOU 2632  C   ARG A 343     8217   4856   5936   1285   1963   -899       C  
ATOM   2633  O   ARG A 343      44.203  -5.283  18.949  1.00 47.86           O  
ANISOU 2633  O   ARG A 343     8166   4227   5793   1296   2201   -885       O  
ATOM   2634  CB  ARG A 343      42.290  -3.432  16.895  1.00 62.72           C  
ANISOU 2634  CB  ARG A 343     9455   6832   7542    787   1579  -1336       C  
ATOM   2635  CG  ARG A 343      41.464  -4.693  17.059  1.00 71.55           C  
ANISOU 2635  CG  ARG A 343    10828   7570   8786    563   1829  -1700       C  
ATOM   2636  CD  ARG A 343      40.055  -4.465  16.539  1.00 77.42           C  
ANISOU 2636  CD  ARG A 343    11393   8473   9553    213   1677  -2057       C  
ATOM   2637  NE  ARG A 343      39.377  -3.442  17.333  1.00 80.11           N  
ANISOU 2637  NE  ARG A 343    11500   8929  10009     92   1488  -1896       N  
ATOM   2638  CZ  ARG A 343      38.603  -3.705  18.384  1.00 81.71           C  
ANISOU 2638  CZ  ARG A 343    11761   8859  10426    -98   1594  -1935       C  
ATOM   2639  NH1 ARG A 343      38.032  -2.716  19.062  1.00 74.77           N  
ANISOU 2639  NH1 ARG A 343    10673   8112   9624   -170   1417  -1777       N  
ATOM   2640  NH2 ARG A 343      38.395  -4.963  18.755  1.00 87.52           N  
ANISOU 2640  NH2 ARG A 343    12776   9174  11303   -205   1902  -2125       N  
ATOM   2641  N   ALA A 344      45.166  -4.699  17.008  1.00 49.01           N  
ANISOU 2641  N   ALA A 344     8116   4892   5615   1506   1991   -864       N  
ATOM   2642  CA  ALA A 344      46.046  -5.871  16.993  1.00 52.63           C  
ANISOU 2642  CA  ALA A 344     8885   5109   6004   1776   2309   -819       C  
ATOM   2643  C   ALA A 344      47.056  -5.795  18.133  1.00 55.94           C  
ANISOU 2643  C   ALA A 344     9315   5492   6446   2056   2393   -405       C  
ATOM   2644  O   ALA A 344      47.316  -6.790  18.820  1.00 54.45           O  
ANISOU 2644  O   ALA A 344     9350   5024   6313   2142   2630   -326       O  
ATOM   2645  CB  ALA A 344      46.763  -5.998  15.656  1.00 56.06           C  
ANISOU 2645  CB  ALA A 344     9321   5778   6201   1980   2305   -852       C  
ATOM   2646  N   THR A 345      47.609  -4.601  18.336  1.00 54.90           N  
ANISOU 2646  N   THR A 345     8870   5711   6278   2125   2128   -115       N  
ATOM   2647  CA  THR A 345      48.526  -4.350  19.444  1.00 51.61           C  
ANISOU 2647  CA  THR A 345     8386   5352   5870   2349   2141    249       C  
ATOM   2648  C   THR A 345      47.895  -4.749  20.771  1.00 49.97           C  
ANISOU 2648  C   THR A 345     8326   4833   5827   2265   2270    232       C  
ATOM   2649  O   THR A 345      48.550  -5.365  21.618  1.00 50.83           O  
ANISOU 2649  O   THR A 345     8548   4858   5907   2467   2433    446       O  
ATOM   2650  CB  THR A 345      48.967  -2.865  19.505  1.00 41.05           C  
ANISOU 2650  CB  THR A 345     6664   4409   4523   2319   1808    484       C  
ATOM   2651  OG1 THR A 345      49.748  -2.548  18.345  1.00 44.35           O  
ANISOU 2651  OG1 THR A 345     6947   5120   4785   2463   1740    579       O  
ATOM   2652  CG2 THR A 345      49.806  -2.595  20.747  1.00 41.97           C  
ANISOU 2652  CG2 THR A 345     6688   4606   4651   2497   1795    794       C  
ATOM   2653  N   PHE A 346      46.625  -4.404  20.959  1.00 44.85           N  
ANISOU 2653  N   PHE A 346     7630   4081   5332   1928   2159     10       N  
ATOM   2654  CA  PHE A 346      45.987  -4.664  22.244  1.00 44.66           C  
ANISOU 2654  CA  PHE A 346     7712   3791   5466   1849   2270     20       C  
ATOM   2655  C   PHE A 346      45.768  -6.156  22.491  1.00 52.22           C  
ANISOU 2655  C   PHE A 346     8948   4422   6470   1806   2566    -60       C  
ATOM   2656  O   PHE A 346      46.066  -6.652  23.573  1.00 56.34           O  
ANISOU 2656  O   PHE A 346     9532   4878   6997   1901   2681    157       O  
ATOM   2657  CB  PHE A 346      44.684  -3.876  22.410  1.00 41.53           C  
ANISOU 2657  CB  PHE A 346     7147   3419   5212   1490   2054   -158       C  
ATOM   2658  CG  PHE A 346      44.242  -3.763  23.832  1.00 42.41           C  
ANISOU 2658  CG  PHE A 346     7282   3381   5453   1465   2092    -50       C  
ATOM   2659  CD1 PHE A 346      44.917  -2.933  24.710  1.00 43.40           C  
ANISOU 2659  CD1 PHE A 346     7240   3718   5533   1624   1930    232       C  
ATOM   2660  CD2 PHE A 346      43.175  -4.506  24.302  1.00 46.00           C  
ANISOU 2660  CD2 PHE A 346     7897   3519   6061   1268   2280   -226       C  
ATOM   2661  CE1 PHE A 346      44.534  -2.834  26.025  1.00 46.04           C  
ANISOU 2661  CE1 PHE A 346     7600   3943   5950   1635   1962    324       C  
ATOM   2662  CE2 PHE A 346      42.778  -4.414  25.629  1.00 50.03           C  
ANISOU 2662  CE2 PHE A 346     8373   3985   6651   1236   2279    -85       C  
ATOM   2663  CZ  PHE A 346      43.458  -3.578  26.493  1.00 51.45           C  
ANISOU 2663  CZ  PHE A 346     8424   4362   6761   1440   2131    179       C  
ATOM   2664  N   GLN A 347      45.258  -6.864  21.487  1.00 59.73           N  
ANISOU 2664  N   GLN A 347    10031   5226   7438   1640   2665   -363       N  
ATOM   2665  CA  GLN A 347      45.048  -8.306  21.580  1.00 68.96           C  
ANISOU 2665  CA  GLN A 347    11435   6100   8668   1557   2928   -444       C  
ATOM   2666  C   GLN A 347      46.333  -9.036  21.946  1.00 70.00           C  
ANISOU 2666  C   GLN A 347    11700   6238   8659   1892   3107   -116       C  
ATOM   2667  O   GLN A 347      46.320  -9.996  22.717  1.00 70.54           O  
ANISOU 2667  O   GLN A 347    11931   6100   8770   1911   3338      1       O  
ATOM   2668  CB  GLN A 347      44.535  -8.860  20.252  1.00 79.67           C  
ANISOU 2668  CB  GLN A 347    12883   7366  10020   1369   2968   -833       C  
ATOM   2669  CG  GLN A 347      43.060  -8.627  19.977  1.00 86.63           C  
ANISOU 2669  CG  GLN A 347    13677   8190  11050    968   2870  -1210       C  
ATOM   2670  CD  GLN A 347      42.647  -9.158  18.612  1.00 96.89           C  
ANISOU 2670  CD  GLN A 347    15036   9484  12293    797   2877  -1616       C  
ATOM   2671  OE1 GLN A 347      42.801  -8.476  17.594  1.00 97.86           O  
ANISOU 2671  OE1 GLN A 347    15056   9878  12248    846   2715  -1760       O  
ATOM   2672  NE2 GLN A 347      42.133 -10.385  18.583  1.00101.80           N  
ANISOU 2672  NE2 GLN A 347    15824   9821  13035    610   3077  -1801       N  
ATOM   2673  N   LYS A 348      47.441  -8.588  21.370  1.00 70.75           N  
ANISOU 2673  N   LYS A 348    11717   6594   8569   2165   3015     46       N  
ATOM   2674  CA  LYS A 348      48.726  -9.222  21.607  1.00 75.47           C  
ANISOU 2674  CA  LYS A 348    12415   7260   8999   2495   3167    366       C  
ATOM   2675  C   LYS A 348      49.092  -9.149  23.085  1.00 76.52           C  
ANISOU 2675  C   LYS A 348    12500   7464   9109   2627   3200    684       C  
ATOM   2676  O   LYS A 348      49.652 -10.090  23.640  1.00 81.13           O  
ANISOU 2676  O   LYS A 348    13253   7967   9605   2802   3432    891       O  
ATOM   2677  CB  LYS A 348      49.811  -8.563  20.757  1.00 77.68           C  
ANISOU 2677  CB  LYS A 348    12547   7882   9088   2751   3023    505       C  
ATOM   2678  CG  LYS A 348      50.980  -9.480  20.436  1.00 85.11           C  
ANISOU 2678  CG  LYS A 348    13646   8846   9845   3046   3211    717       C  
ATOM   2679  CD  LYS A 348      52.082  -8.753  19.668  1.00 87.81           C  
ANISOU 2679  CD  LYS A 348    13789   9579   9995   3303   3057    901       C  
ATOM   2680  CE  LYS A 348      51.599  -8.234  18.320  1.00 88.25           C  
ANISOU 2680  CE  LYS A 348    13768   9717  10047   3185   2927    608       C  
ATOM   2681  NZ  LYS A 348      52.718  -7.652  17.518  1.00 87.93           N  
ANISOU 2681  NZ  LYS A 348    13537  10066   9808   3454   2818    825       N  
ATOM   2682  N   LEU A 349      48.760  -8.034  23.726  1.00 70.64           N  
ANISOU 2682  N   LEU A 349    11531   6884   8426   2554   2979    716       N  
ATOM   2683  CA  LEU A 349      49.065  -7.857  25.144  1.00 73.06           C  
ANISOU 2683  CA  LEU A 349    11763   7313   8685   2673   2976    973       C  
ATOM   2684  C   LEU A 349      48.621  -9.041  25.999  1.00 82.48           C  
ANISOU 2684  C   LEU A 349    13185   8231   9925   2636   3269   1013       C  
ATOM   2685  O   LEU A 349      49.067  -9.192  27.137  1.00 85.27           O  
ANISOU 2685  O   LEU A 349    13530   8701  10169   2813   3346   1257       O  
ATOM   2686  CB  LEU A 349      48.466  -6.552  25.674  1.00 66.61           C  
ANISOU 2686  CB  LEU A 349    10705   6629   7974   2530   2705    920       C  
ATOM   2687  CG  LEU A 349      49.185  -5.305  25.159  1.00 63.24           C  
ANISOU 2687  CG  LEU A 349    10011   6543   7475   2644   2436   1001       C  
ATOM   2688  CD1 LEU A 349      48.551  -4.056  25.703  1.00 63.70           C  
ANISOU 2688  CD1 LEU A 349     9860   6684   7658   2496   2184    957       C  
ATOM   2689  CD2 LEU A 349      50.649  -5.365  25.548  1.00 67.46           C  
ANISOU 2689  CD2 LEU A 349    10445   7399   7786   2955   2446   1310       C  
ATOM   2690  N   SER A 350      47.750  -9.882  25.449  1.00 88.58           N  
ANISOU 2690  N   SER A 350    14147   8661  10847   2410   3442    766       N  
ATOM   2691  CA  SER A 350      47.327 -11.104  26.133  1.00 93.64           C  
ANISOU 2691  CA  SER A 350    15014   9014  11550   2370   3772    805       C  
ATOM   2692  C   SER A 350      48.291 -12.263  25.867  1.00 96.08           C  
ANISOU 2692  C   SER A 350    15565   9237  11706   2625   4060    981       C  
ATOM   2693  O   SER A 350      48.754 -12.929  26.796  1.00 96.56           O  
ANISOU 2693  O   SER A 350    15746   9289  11655   2835   4295   1252       O  
ATOM   2694  CB  SER A 350      45.909 -11.495  25.713  1.00 96.31           C  
ANISOU 2694  CB  SER A 350    15421   9037  12136   1984   3840    449       C  
ATOM   2695  OG  SER A 350      45.619 -12.828  26.093  1.00101.42           O  
ANISOU 2695  OG  SER A 350    16311   9377  12846   1954   4210    471       O  
TER    2696      SER A 350                                                      
HETATM 2697  I   IOD A 401      36.693  30.406  13.918  0.44 54.46           I  
HETATM 2698  I   IOD A 402      34.941   7.996  -6.025  0.78 91.53           I  
HETATM 2699  I   IOD A 403      33.475  30.710   6.561  0.70 33.91           I  
HETATM 2700  I   IOD A 404      22.590  18.246   2.443  0.43 39.97           I  
HETATM 2701  I   IOD A 405      29.645   5.836  23.166  0.45 44.34           I  
HETATM 2702  I   IOD A 406      45.533   2.744   5.617  0.57114.30           I  
HETATM 2703  I   IOD A 407      31.472  13.304 -15.221  0.48 35.19           I  
HETATM 2704  I   IOD A 408      31.909  11.640 -17.025  0.46 38.86           I  
HETATM 2705  I   IOD A 409      17.616  40.660  -8.063  0.52 60.18           I  
HETATM 2706  I   IOD A 410      58.206  -3.759  27.286  0.46 57.07           I  
HETATM 2707  I   IOD A 411      34.361  39.434   1.239  0.31 46.85           I  
HETATM 2708  I   IOD A 412       6.894  31.895 -13.122  0.59 40.17           I  
HETATM 2709  C1  EDO A 413      28.288  24.521  -5.201  1.00 47.04           C  
HETATM 2710  O1  EDO A 413      27.291  23.580  -4.775  1.00 48.87           O  
HETATM 2711  C2  EDO A 413      27.716  25.933  -5.266  1.00 40.25           C  
HETATM 2712  O2  EDO A 413      28.751  26.908  -5.052  1.00 40.36           O  
HETATM 2713  C1  EDO A 414      21.481  22.172   1.937  1.00 39.32           C  
HETATM 2714  O1  EDO A 414      20.529  21.148   1.583  1.00 40.42           O  
HETATM 2715  C2  EDO A 414      21.700  23.086   0.736  1.00 50.39           C  
HETATM 2716  O2  EDO A 414      22.335  24.296   1.177  1.00 55.11           O  
HETATM 2717  C1  EDO A 415      52.254   8.509  18.650  1.00 52.27           C  
HETATM 2718  O1  EDO A 415      52.555   8.309  20.043  1.00 56.57           O  
HETATM 2719  C2  EDO A 415      53.084   7.574  17.782  1.00 42.01           C  
HETATM 2720  O2  EDO A 415      54.444   7.969  17.925  1.00 45.09           O  
HETATM 2721  C1  EDO A 416      40.559   6.661  -3.426  1.00 68.78           C  
HETATM 2722  O1  EDO A 416      40.727   7.470  -2.256  1.00 69.92           O  
HETATM 2723  C2  EDO A 416      40.606   7.565  -4.649  1.00 68.31           C  
HETATM 2724  O2  EDO A 416      39.432   7.336  -5.436  1.00 69.81           O  
HETATM 2725  C1  EDO A 417      52.859  -7.610  23.964  1.00 59.30           C  
HETATM 2726  O1  EDO A 417      52.200  -8.109  22.797  1.00 62.18           O  
HETATM 2727  C2  EDO A 417      54.184  -7.005  23.537  1.00 58.58           C  
HETATM 2728  O2  EDO A 417      54.966  -6.742  24.707  1.00 62.21           O  
HETATM 2729  C1  EDO A 418       8.012  19.028  10.000  1.00 59.34           C  
HETATM 2730  O1  EDO A 418       6.952  19.737   9.346  1.00 57.41           O  
HETATM 2731  C2  EDO A 418       9.251  19.912  10.126  1.00 61.14           C  
HETATM 2732  O2  EDO A 418      10.346  19.165  10.686  1.00 60.90           O  
HETATM 2733  C1  EDO A 419       4.622  24.998   2.533  1.00 62.37           C  
HETATM 2734  O1  EDO A 419       3.863  26.025   3.192  1.00 63.13           O  
HETATM 2735  C2  EDO A 419       3.721  24.116   1.669  1.00 63.17           C  
HETATM 2736  O2  EDO A 419       4.411  22.909   1.306  1.00 60.72           O  
HETATM 2737  C1  EDO A 420      19.333  14.782 -16.229  1.00 45.82           C  
HETATM 2738  O1  EDO A 420      19.696  13.464 -16.685  1.00 46.41           O  
HETATM 2739  C2  EDO A 420      20.220  15.814 -16.910  1.00 39.05           C  
HETATM 2740  O2  EDO A 420      19.535  17.052 -17.045  1.00 25.56           O  
HETATM 2741  C1  EDO A 421      28.792  26.887 -18.063  1.00 53.19           C  
HETATM 2742  O1  EDO A 421      28.873  25.478 -17.810  1.00 55.58           O  
HETATM 2743  C2  EDO A 421      29.985  27.603 -17.441  1.00 54.16           C  
HETATM 2744  O2  EDO A 421      29.992  28.980 -17.853  1.00 55.71           O  
HETATM 2745  C1  EDO A 422      33.064  26.190   4.694  1.00 57.57           C  
HETATM 2746  O1  EDO A 422      33.399  27.480   5.220  1.00 62.43           O  
HETATM 2747  C2  EDO A 422      31.674  26.199   4.056  1.00 47.90           C  
HETATM 2748  O2  EDO A 422      31.613  27.038   2.894  1.00 32.52           O  
HETATM 2749  C1  EDO A 423       6.179  15.870   3.730  1.00 54.42           C  
HETATM 2750  O1  EDO A 423       5.864  17.103   3.080  1.00 57.32           O  
HETATM 2751  C2  EDO A 423       7.473  15.336   3.135  1.00 53.13           C  
HETATM 2752  O2  EDO A 423       7.830  14.087   3.746  1.00 53.82           O  
HETATM 2753  C1  EDO A 424      33.262  15.711  30.564  1.00 41.05           C  
HETATM 2754  O1  EDO A 424      31.947  15.212  30.310  1.00 39.13           O  
HETATM 2755  C2  EDO A 424      34.209  15.298  29.454  1.00 40.50           C  
HETATM 2756  O2  EDO A 424      35.407  16.069  29.565  1.00 43.34           O  
HETATM 2757  O   HOH A 501      31.618  25.654   7.825  1.00 32.43           O  
HETATM 2758  O   HOH A 502       8.571  26.709   9.095  1.00 37.57           O  
HETATM 2759  O   HOH A 503      17.323  -1.437   3.406  1.00 50.27           O  
HETATM 2760  O   HOH A 504      11.617   6.644  12.723  1.00 37.16           O  
HETATM 2761  O   HOH A 505      26.973  18.217  -4.770  1.00 49.60           O  
HETATM 2762  O   HOH A 506      13.264  19.759  10.393  1.00 32.55           O  
HETATM 2763  O   HOH A 507      24.738  17.846  16.779  1.00 23.89           O  
HETATM 2764  O   HOH A 508      29.743  14.073  30.887  1.00 48.60           O  
HETATM 2765  O   HOH A 509      36.918  13.499  25.845  1.00 29.53           O  
HETATM 2766  O   HOH A 510      20.188   7.272  20.632  1.00 31.39           O  
HETATM 2767  O   HOH A 511      27.579  19.142   7.532  1.00 34.36           O  
HETATM 2768  O   HOH A 512      36.032  26.734   8.704  1.00 45.60           O  
HETATM 2769  O   HOH A 513      25.803  23.274  16.882  1.00 42.31           O  
HETATM 2770  O   HOH A 514      24.703  30.227  15.026  1.00 27.82           O  
HETATM 2771  O   HOH A 515      25.905  39.701  12.718  1.00 47.07           O  
HETATM 2772  O   HOH A 516      10.812  12.184  10.382  1.00 34.74           O  
HETATM 2773  O   HOH A 517      29.146   8.520   8.016  1.00 49.96           O  
HETATM 2774  O   HOH A 518      33.590   2.266  21.853  1.00 35.74           O  
HETATM 2775  O   HOH A 519      19.475  41.310  11.368  1.00 41.00           O  
HETATM 2776  O   HOH A 520      22.476  30.815  18.276  1.00 36.54           O  
HETATM 2777  O   HOH A 521      25.514  17.168   6.288  1.00 27.63           O  
HETATM 2778  O   HOH A 522      16.929  29.423  13.046  1.00 26.51           O  
HETATM 2779  O   HOH A 523      48.691   8.827  20.693  1.00 43.43           O  
HETATM 2780  O   HOH A 524      17.275   2.705  17.216  1.00 43.17           O  
HETATM 2781  O   HOH A 525      36.312   5.972  36.876  1.00 34.79           O  
HETATM 2782  O   HOH A 526      35.712  -6.488  34.486  1.00 42.96           O  
HETATM 2783  O   HOH A 527      31.691  23.430   4.126  1.00 37.05           O  
HETATM 2784  O   HOH A 528      30.293   2.727  23.695  1.00 36.90           O  
HETATM 2785  O   HOH A 529      20.574  28.783  -3.825  1.00 25.32           O  
HETATM 2786  O   HOH A 530      22.097  19.032  21.087  1.00 27.81           O  
HETATM 2787  O   HOH A 531      22.805  26.514  17.013  1.00 29.01           O  
HETATM 2788  O   HOH A 532      20.165   7.475  -4.619  1.00 38.20           O  
HETATM 2789  O   HOH A 533      12.455   8.863  18.450  1.00 51.10           O  
HETATM 2790  O   HOH A 534      27.113   4.216  24.990  1.00 52.26           O  
HETATM 2791  O   HOH A 535      30.879   7.995  36.350  1.00 27.33           O  
HETATM 2792  O   HOH A 536      40.214  -3.855  21.301  1.00 37.67           O  
HETATM 2793  O   HOH A 537      11.736  10.935   2.352  1.00 34.53           O  
HETATM 2794  O   HOH A 538       7.426  12.152  -9.293  1.00 44.22           O  
HETATM 2795  O   HOH A 539      18.711  11.387  26.279  1.00 55.76           O  
HETATM 2796  O   HOH A 540      39.575  -3.612  23.859  1.00 40.23           O  
HETATM 2797  O   HOH A 541      32.780   0.987  13.293  1.00 47.27           O  
HETATM 2798  O   HOH A 542      34.021  24.565   8.722  1.00 48.25           O  
HETATM 2799  O   HOH A 543      12.831  39.851   1.713  1.00 42.24           O  
HETATM 2800  O   HOH A 544      34.255   4.824  14.685  1.00 47.22           O  
HETATM 2801  O   HOH A 545       7.516  27.689 -10.315  1.00 35.66           O  
HETATM 2802  O   HOH A 546      25.203   5.653  29.705  1.00 50.05           O  
HETATM 2803  O   HOH A 547      19.728  34.005  17.996  1.00 43.71           O  
HETATM 2804  O   HOH A 548      44.132   6.327  20.939  1.00 39.55           O  
HETATM 2805  O   HOH A 549       7.304  17.356  -4.510  1.00 39.34           O  
HETATM 2806  O   HOH A 550      39.657  -6.265  24.599  1.00 44.98           O  
HETATM 2807  O   HOH A 551      26.385  23.823  12.724  1.00 37.35           O  
HETATM 2808  O   HOH A 552      40.972   9.147  42.475  1.00 59.37           O  
HETATM 2809  O   HOH A 553       9.544   9.593   3.027  1.00 45.20           O  
HETATM 2810  O   HOH A 554      17.885  35.863  15.705  1.00 56.87           O  
HETATM 2811  O   HOH A 555      39.783  13.734  39.990  1.00 28.99           O  
HETATM 2812  O   HOH A 556      12.596  29.954  15.349  1.00 42.71           O  
HETATM 2813  O   HOH A 557      31.665  11.304  10.014  1.00 39.26           O  
HETATM 2814  O   HOH A 558      25.074  27.785  16.209  1.00 36.28           O  
HETATM 2815  O   HOH A 559       5.462  20.131   0.896  1.00 39.63           O  
HETATM 2816  O   HOH A 560      43.466  19.892  37.835  1.00 50.92           O  
HETATM 2817  O   HOH A 561      25.964   9.272   0.297  1.00 43.12           O  
HETATM 2818  O   HOH A 562      34.689  -3.988  36.850  1.00 38.09           O  
HETATM 2819  O   HOH A 563      11.088  28.120   8.971  1.00 32.71           O  
HETATM 2820  O   HOH A 564      30.174  15.877  19.825  1.00 41.93           O  
HETATM 2821  O   HOH A 565      14.897  29.644  16.736  1.00 28.42           O  
HETATM 2822  O   HOH A 566      44.600  -8.518  25.426  1.00 54.63           O  
HETATM 2823  O   HOH A 567       6.362  13.806  -3.410  1.00 53.27           O  
HETATM 2824  O   HOH A 568      29.950   1.431  28.338  1.00 33.99           O  
HETATM 2825  O   HOH A 569      31.913  24.484 -12.439  1.00 42.80           O  
HETATM 2826  O   HOH A 570      15.144  19.065  -0.936  1.00 36.20           O  
HETATM 2827  O   HOH A 571      35.533   6.675  34.430  1.00 27.52           O  
HETATM 2828  O   HOH A 572      37.432   1.502  19.727  1.00 43.09           O  
HETATM 2829  O   HOH A 573      18.282  22.880  15.983  1.00 32.48           O  
HETATM 2830  O   HOH A 574      12.499  38.919  -5.980  1.00 48.51           O  
HETATM 2831  O   HOH A 575       8.120  10.858  -4.394  1.00 39.95           O  
HETATM 2832  O   HOH A 576      34.017  18.310  -8.568  1.00 40.10           O  
HETATM 2833  O   HOH A 577      23.234  29.220  -9.793  1.00 34.91           O  
HETATM 2834  O   HOH A 578      25.018  42.967   8.619  1.00 49.57           O  
HETATM 2835  O   HOH A 579      37.853   4.382  32.503  1.00 27.16           O  
HETATM 2836  O   HOH A 580      25.657  46.994   2.679  1.00 58.72           O  
HETATM 2837  O   HOH A 581      18.568   9.970  24.222  1.00 47.79           O  
HETATM 2838  O   HOH A 582      13.236  35.168  -7.021  1.00 36.19           O  
HETATM 2839  O   HOH A 583      44.319   1.230  14.865  1.00 50.34           O  
HETATM 2840  O   HOH A 584      49.040   0.464  35.592  1.00 46.75           O  
HETATM 2841  O   HOH A 585      23.137  44.524  -1.859  1.00 51.49           O  
HETATM 2842  O   HOH A 586      34.571   0.999  19.889  1.00 46.32           O  
HETATM 2843  O   HOH A 587      39.001  14.335  27.463  1.00 44.27           O  
HETATM 2844  O   HOH A 588       7.117  10.816   9.338  1.00 57.01           O  
HETATM 2845  O   HOH A 589      11.586  22.018  14.505  1.00 48.01           O  
HETATM 2846  O   HOH A 590      40.639  -7.097  27.870  1.00 51.41           O  
HETATM 2847  O   HOH A 591       6.073  13.550  -0.243  1.00 58.67           O  
HETATM 2848  O   HOH A 592      31.889  28.188   8.591  1.00 29.04           O  
HETATM 2849  O   HOH A 593      10.774   7.395  -9.727  1.00 48.76           O  
HETATM 2850  O   HOH A 594      20.078  22.882  -2.126  1.00 50.70           O  
HETATM 2851  O   HOH A 595      25.575  19.722   9.163  1.00 33.83           O  
HETATM 2852  O   HOH A 596      13.660   5.330 -13.290  1.00 54.89           O  
HETATM 2853  O   HOH A 597      47.455   8.396  35.897  1.00 47.59           O  
HETATM 2854  O   HOH A 598      33.630  13.147  19.241  1.00 39.37           O  
HETATM 2855  O   HOH A 599      35.057  37.467   4.627  1.00 48.08           O  
HETATM 2856  O   HOH A 600      28.523  24.703 -13.973  1.00 37.69           O  
HETATM 2857  O   HOH A 601      16.500  15.026   0.840  1.00 33.96           O  
HETATM 2858  O   HOH A 602      15.528  22.804  12.896  1.00 32.14           O  
HETATM 2859  O   HOH A 603       8.496  13.307   1.310  1.00 51.27           O  
HETATM 2860  O   HOH A 604      39.014   6.610  33.089  1.00 45.19           O  
HETATM 2861  O   HOH A 605      24.118   1.949   3.924  1.00 42.30           O  
HETATM 2862  O   HOH A 606      13.248  21.889  11.768  1.00 47.58           O  
HETATM 2863  O   HOH A 607      15.870  23.570  16.977  1.00 42.07           O  
HETATM 2864  O   HOH A 608       4.612  24.023   6.415  1.00 47.80           O  
HETATM 2865  O   HOH A 609      16.196   3.918   9.048  1.00 43.80           O  
HETATM 2866  O   HOH A 610       6.518  35.390  -6.317  1.00 43.80           O  
HETATM 2867  O   HOH A 611      24.866   5.819  25.546  1.00 58.64           O  
HETATM 2868  O   HOH A 612      36.287  -0.593  37.415  1.00 41.94           O  
HETATM 2869  O   HOH A 613      11.945  23.494  10.791  1.00 51.69           O  
HETATM 2870  O   HOH A 614      36.449  12.219  -7.772  1.00 38.32           O  
HETATM 2871  O   HOH A 615      25.830   7.320  20.919  1.00 50.58           O  
HETATM 2872  O   HOH A 616      26.405  18.387  18.846  1.00 52.23           O  
HETATM 2873  O   HOH A 617       7.868   8.822 -10.477  1.00 49.98           O  
HETATM 2874  O   HOH A 618      31.142  26.976 -14.442  1.00 51.46           O  
HETATM 2875  O   HOH A 619      36.078   2.052  38.856  1.00 49.23           O  
HETATM 2876  O   HOH A 620      34.885  16.367  24.087  1.00 41.45           O  
HETATM 2877  O   HOH A 621      59.736   1.521  44.135  1.00 67.62           O  
HETATM 2878  O   HOH A 622       9.737  14.479  19.145  1.00 46.26           O  
HETATM 2879  O   HOH A 623      47.098   3.922  14.073  1.00 38.11           O  
HETATM 2880  O   HOH A 624      43.009  -0.763  15.134  1.00 55.07           O  
HETATM 2881  O   HOH A 625      19.056  31.380  21.166  1.00 41.92           O  
HETATM 2882  O   HOH A 626      11.031   4.193   4.054  1.00 55.65           O  
HETATM 2883  O   HOH A 627      21.410  20.277 -16.851  1.00 46.14           O  
HETATM 2884  O   HOH A 628      25.365   7.389 -12.572  1.00 47.77           O  
HETATM 2885  O   HOH A 629      22.226   1.921   1.282  1.00 52.15           O  
HETATM 2886  O   HOH A 630      28.404  24.622  14.060  1.00 43.22           O  
HETATM 2887  O   HOH A 631      42.557  -3.330  13.520  1.00 62.14           O  
HETATM 2888  O   HOH A 632      12.657  16.110  18.982  1.00 42.05           O  
HETATM 2889  O   HOH A 633       9.361   8.617  11.313  1.00 52.19           O  
HETATM 2890  O   HOH A 634      24.786  23.094  -0.456  1.00 29.15           O  
HETATM 2891  O   HOH A 635      14.453  46.164   2.040  1.00 58.39           O  
HETATM 2892  O   HOH A 636      30.198  35.208 -12.058  1.00 46.21           O  
HETATM 2893  O   HOH A 637      11.246   7.107  -3.452  1.00 45.70           O  
HETATM 2894  O   HOH A 638      12.071   2.670  -4.404  1.00 43.17           O  
HETATM 2895  O   HOH A 639      58.618   3.449  20.989  1.00 52.29           O  
HETATM 2896  O   HOH A 640      22.322   6.101  20.109  1.00 51.89           O  
HETATM 2897  O   HOH A 641      56.598   5.747   8.092  1.00 45.52           O  
HETATM 2898  O   HOH A 642      28.110  19.781 -14.454  1.00 50.46           O  
HETATM 2899  O   HOH A 643      35.101  13.648  27.485  1.00 43.76           O  
HETATM 2900  O   HOH A 644       6.478  19.920 -11.233  1.00 46.31           O  
HETATM 2901  O   HOH A 645      46.095   0.747   7.908  1.00 66.34           O  
HETATM 2902  O   HOH A 646      42.176   7.005  38.500  1.00 46.13           O  
HETATM 2903  O   HOH A 647      15.559  36.321 -17.059  1.00 50.80           O  
HETATM 2904  O   HOH A 648      28.047  42.002   9.443  1.00 59.71           O  
HETATM 2905  O   HOH A 649      51.309  -5.791  22.002  1.00 49.26           O  
HETATM 2906  O   HOH A 650       7.393  33.975 -12.714  1.00 35.63           O  
HETATM 2907  O   HOH A 651      18.173  46.056  -1.010  1.00 59.75           O  
HETATM 2908  O   HOH A 652      32.977   7.876  34.643  1.00 32.59           O  
HETATM 2909  O   HOH A 653      25.281  21.003   5.417  1.00 40.81           O  
HETATM 2910  O   HOH A 654      31.203  43.816  -4.340  1.00 54.58           O  
HETATM 2911  O   HOH A 655      62.567   8.801  25.455  1.00 60.05           O  
CONECT    1    2                                                                
CONECT    2    1    3    5                                                      
CONECT    3    2    4    9                                                      
CONECT    4    3                                                                
CONECT    5    2    6                                                           
CONECT    6    5    7                                                           
CONECT    7    6    8                                                           
CONECT    8    7                                                                
CONECT    9    3                                                                
CONECT  217  226                                                                
CONECT  226  217  227                                                           
CONECT  227  226  228  230                                                      
CONECT  228  227  229  234                                                      
CONECT  229  228                                                                
CONECT  230  227  231                                                           
CONECT  231  230  232                                                           
CONECT  232  231  233                                                           
CONECT  233  232                                                                
CONECT  234  228                                                                
CONECT  375  377                                                                
CONECT  377  375  378                                                           
CONECT  378  377  379  381                                                      
CONECT  379  378  380  385                                                      
CONECT  380  379                                                                
CONECT  381  378  382                                                           
CONECT  382  381  383                                                           
CONECT  383  382  384                                                           
CONECT  384  383                                                                
CONECT  385  379                                                                
CONECT  493  496                                                                
CONECT  496  493  497                                                           
CONECT  497  496  498  500                                                      
CONECT  498  497  499  504                                                      
CONECT  499  498                                                                
CONECT  500  497  501                                                           
CONECT  501  500  502                                                           
CONECT  502  501  503                                                           
CONECT  503  502                                                                
CONECT  504  498                                                                
CONECT  668  674                                                                
CONECT  674  668  675                                                           
CONECT  675  674  676  678                                                      
CONECT  676  675  677  682                                                      
CONECT  677  676                                                                
CONECT  678  675  679                                                           
CONECT  679  678  680                                                           
CONECT  680  679  681                                                           
CONECT  681  680                                                                
CONECT  682  676  683                                                           
CONECT  683  682  684  686                                                      
CONECT  684  683  685  690                                                      
CONECT  685  684                                                                
CONECT  686  683  687                                                           
CONECT  687  686  688                                                           
CONECT  688  687  689                                                           
CONECT  689  688                                                                
CONECT  690  684                                                                
CONECT  718  720                                                                
CONECT  720  718  721                                                           
CONECT  721  720  722  724                                                      
CONECT  722  721  723  728                                                      
CONECT  723  722                                                                
CONECT  724  721  725                                                           
CONECT  725  724  726                                                           
CONECT  726  725  727                                                           
CONECT  727  726                                                                
CONECT  728  722                                                                
CONECT  943  946                                                                
CONECT  946  943  947                                                           
CONECT  947  946  948  950                                                      
CONECT  948  947  949  954                                                      
CONECT  949  948                                                                
CONECT  950  947  951                                                           
CONECT  951  950  952                                                           
CONECT  952  951  953                                                           
CONECT  953  952                                                                
CONECT  954  948                                                                
CONECT  963  968                                                                
CONECT  968  963  969                                                           
CONECT  969  968  970  972                                                      
CONECT  970  969  971  976                                                      
CONECT  971  970                                                                
CONECT  972  969  973                                                           
CONECT  973  972  974                                                           
CONECT  974  973  975                                                           
CONECT  975  974                                                                
CONECT  976  970                                                                
CONECT 1222 1225                                                                
CONECT 1225 1222 1226                                                           
CONECT 1226 1225 1227 1229                                                      
CONECT 1227 1226 1228 1233                                                      
CONECT 1228 1227                                                                
CONECT 1229 1226 1230                                                           
CONECT 1230 1229 1231                                                           
CONECT 1231 1230 1232                                                           
CONECT 1232 1231                                                                
CONECT 1233 1227                                                                
CONECT 1274 1277                                                                
CONECT 1277 1274 1278                                                           
CONECT 1278 1277 1279 1281                                                      
CONECT 1279 1278 1280 1285                                                      
CONECT 1280 1279                                                                
CONECT 1281 1278 1282                                                           
CONECT 1282 1281 1283                                                           
CONECT 1283 1282 1284                                                           
CONECT 1284 1283                                                                
CONECT 1285 1279                                                                
CONECT 1340 1342                                                                
CONECT 1342 1340 1343                                                           
CONECT 1343 1342 1344 1346                                                      
CONECT 1344 1343 1345 1350                                                      
CONECT 1345 1344                                                                
CONECT 1346 1343 1347                                                           
CONECT 1347 1346 1348                                                           
CONECT 1348 1347 1349                                                           
CONECT 1349 1348                                                                
CONECT 1350 1344                                                                
CONECT 2287 2290                                                                
CONECT 2290 2287 2291                                                           
CONECT 2291 2290 2292 2294                                                      
CONECT 2292 2291 2293 2298                                                      
CONECT 2293 2292                                                                
CONECT 2294 2291 2295                                                           
CONECT 2295 2294 2296                                                           
CONECT 2296 2295 2297                                                           
CONECT 2297 2296                                                                
CONECT 2298 2292                                                                
CONECT 2709 2710 2711                                                           
CONECT 2710 2709                                                                
CONECT 2711 2709 2712                                                           
CONECT 2712 2711                                                                
CONECT 2713 2714 2715                                                           
CONECT 2714 2713                                                                
CONECT 2715 2713 2716                                                           
CONECT 2716 2715                                                                
CONECT 2717 2718 2719                                                           
CONECT 2718 2717                                                                
CONECT 2719 2717 2720                                                           
CONECT 2720 2719                                                                
CONECT 2721 2722 2723                                                           
CONECT 2722 2721                                                                
CONECT 2723 2721 2724                                                           
CONECT 2724 2723                                                                
CONECT 2725 2726 2727                                                           
CONECT 2726 2725                                                                
CONECT 2727 2725 2728                                                           
CONECT 2728 2727                                                                
CONECT 2729 2730 2731                                                           
CONECT 2730 2729                                                                
CONECT 2731 2729 2732                                                           
CONECT 2732 2731                                                                
CONECT 2733 2734 2735                                                           
CONECT 2734 2733                                                                
CONECT 2735 2733 2736                                                           
CONECT 2736 2735                                                                
CONECT 2737 2738 2739                                                           
CONECT 2738 2737                                                                
CONECT 2739 2737 2740                                                           
CONECT 2740 2739                                                                
CONECT 2741 2742 2743                                                           
CONECT 2742 2741                                                                
CONECT 2743 2741 2744                                                           
CONECT 2744 2743                                                                
CONECT 2745 2746 2747                                                           
CONECT 2746 2745                                                                
CONECT 2747 2745 2748                                                           
CONECT 2748 2747                                                                
CONECT 2749 2750 2751                                                           
CONECT 2750 2749                                                                
CONECT 2751 2749 2752                                                           
CONECT 2752 2751                                                                
CONECT 2753 2754 2755                                                           
CONECT 2754 2753                                                                
CONECT 2755 2753 2756                                                           
CONECT 2756 2755                                                                
MASTER      497    0   37   13   19    0   27    6 2896    1  175   28          
END